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SLiMSuite SLiMFinder Server

# Output for SLiMFinder V5.2.3: Tue Dec  8 23:27:22 2015
# 201 warnings; 20 errors: see log output (below) for details.
# JobID: 15120800036

Your SLiMFinder job has finished running and outputs have been parsed. Click on tabs to see server output. (Mouseover for description.)

The outfmt tab contains more information on the outputs. Click here for SLiMFinder help/documentation.

Content for individual tabs can be returned using &rest=X, where X is the tab name (e.g. &rest=log). Full output can be returned as text using &rest=full and parsed using SLiMParser.

JobID 15120800036 (slimfinder) Finished.
IP:129.94.133.155
No queue.
slimfinder&uniprotid=LIG_CtBP_PxDLS_1&dismask=T&runid=CtBP-NoEFilter&efilter=F
Run Started: 2015-12-08 23:27:22; PID=39031
Run finished: 2015-12-09 00:02:11

SLiMs and SLiMFinder

Short linear motifs (SLiMs) in proteins are functional microdomains of fundamental importance in many biological
systems. SLiMs typically consist of a 3 to 10 amino acid stretch of the primary protein sequence, of which as few
as two sites may be important for activity. SLiMFinder is a SLiM discovery program building on the principles of
the SLiMDisc software for accounting for evolutionary relationships between input proteins. This stops results
being dominated by motifs shared for reasons of history, rather than function. SLiMFinder runs in two phases:
(1) SLiMBuild constructs the motif search space based on number of defined positions, maximum length of "wildcard
spacers" and allowed amino acid ambiguities; (2) SLiMChance assesses the over-representation of all motifs,
correcting for the size of the SLiMBuild search space. This gives SLiMFinder high specificity.

Protein sequences can be masked prior to SLiMBuild. Disorder masking (using IUPred predictions) is highly
recommended. Other masking options are described in the manual and/or literature.

Running SLiMFinder

The standared REST server call for SLiMFinder is in the form:
slimfinder&uniprotid=LIST&dismask=T/F&consmask=T/F

Run with &rest=docs for program documentation and options. A plain text version is accessed with &rest=help.
&rest=OUTFMT can be used to retrieve individual parts of the output, matching the tabs in the default
(&rest=format) output. Individual OUTFMT elements can also be parsed from the full (&rest=full) server output,
which is formatted as follows:
###~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~###
# OUTFMT:
... contents for OUTFMT section ...


More options are available through the SLiMFinder server: http://www.slimsuite.unsw.edu.au/servers/slimfinder.php

After running, click on the main tab to see overall SLiM predictions. If any SLiMS have been predicted, the
occ tab will have details of which proteins (and where) they occur.

If no SLiMs are returned: [1] Try altering the masking settings. (Disorder masking is recommended. Conservation
masking can sometimes help but it depend on the dataset.) [2] Try relaxing the probability cutoff. Set
[probcut=1.0]{cmd:probcut} to see the best motifs, regardless of significance. (You may also want to reduce the [topranks=X]{cmd:topranks}
setting.)

Available REST Outputs

main = Main results table of predicted SLiM patterns (if any) [[extras=-1]{cmd:extras}]
occ = Occurrence table showing individual SLiM occurrences in input proteins [[extras=0]{cmd:extras}]
upc = List of Unrelated Protein Clusters (UPC) used for evolutionary corrections [[extras=0]{cmd:extras}]
cloud = Predicted SLiM "cloud" output, which groups overlapping motifs [[extras=1]{cmd:extras}]
seqin = Input sequence data [[extras=-1]{cmd:extras}]
slimdb = Parsed input sequences in fasta format, used for UPC generation etc. [[extras=0]{cmd:extras}]
masked = Masked input sequences (masked residues marked with X) [[extras=1]{cmd:extras}]
mapping = Fasta format with positions of SLiM occurrences aligned [[extras=1]{cmd:extras}]
motifaln = Fasta format of individual SLiM alignments (unmasked sequences) [[extras=1]{cmd:extras}]
maskaln = Fasta format of individual SLiM alignments (masked sequences) [[extras=1]{cmd:extras}]

Additional REST Outputs [extras>1]

To get additional REST outputs, set &extras=2 or &extras=3. This may increase run times noticeably,
depending on the number of SLiMs returned.

motifs = SLiM predictions reformatted in plain motif format for CompariMotif [[extras=2]{cmd:extras}]
compare = Results of all-by-all CompariMotif search of predicted SLiMs [[extras=2]{cmd:extras}]
xgmml = SLiMs, occurrences and motif relationships in a Cytoscape-compatible network [[extras=2]{cmd:extras}]
dismatrix = Input sequence distance matrix [[extras=3]{cmd:extras}]
rank = Main table in SLiMDisc output format [[extras=3]{cmd:extras}]
dat.rank = Occurrence table in SLiMDisc output format [[extras=3]{cmd:extras}]
teiresias = Motif prediction output in TEIRESIAS format [[extras=3]{cmd:extras} [teiresias=T]{cmd:teiresias}]
teiresias.fasta = TEIRESIAS masked fasta output [[extras=3]{cmd:extras} [teiresias=T]{cmd:teiresias}]
Dataset,RunID,Masking,Build,Chance,RunTime,SeqNum,UPNum,AANum,MotNum,Rank,Sig,Pattern,IC,Occ,Support,UP,ExpUP,Prob,Cloud,CloudSeq,CloudUP
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,1,0.00e+00,P..C..C.[KR].[FY],4.54,14,9,9,0.002,5.29e-32,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,2,0.00e+00,P..C..C..[AS][FY],4.54,10,9,9,0.003,2.66e-30,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,3,0.00e+00,P..C..C.[KR].F,4.77,12,7,7,8.43e-04,2.74e-26,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,4,0.00e+00,[ST]..KP..C..C,4.77,11,8,8,0.003,8.78e-26,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,5,0.00e+00,C..C.[KR][AS][FY],4.31,9,8,8,0.003,1.48e-25,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,6,3.33e-16,[KR]P..C..C.[KR],4.54,15,8,8,0.004,1.24e-24,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,7,1.89e-15,C..C.[KR].[FY],3.54,18,9,9,0.020,4.31e-22,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,8,3.00e-15,H..E..[FY].C..C,4.77,9,6,6,4.94e-04,1.17e-23,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,9,3.44e-15,"KP..C..C.{1,2}R",5.00,10,7,7,0.002,1.31e-23,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,10,3.55e-15,[ST]..[KR]P..C..C,4.54,15,8,8,0.006,1.36e-23,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,11,8.22e-15,P..C..C.[KR][AS],4.54,9,8,8,0.007,3.18e-23,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,12,5.31e-14,PY.C..C.[KR],4.77,9,6,6,7.97e-04,2.05e-22,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,13,6.45e-14,C..C..[AS][FY],3.54,12,9,9,0.030,1.49e-20,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,14,1.82e-13,H..E.P..C..C,5.00,8,6,6,9.79e-04,7.04e-22,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,15,6.08e-13,E.P[FY].C..C,4.77,8,6,6,0.001,2.34e-21,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,16,6.37e-13,C..CG[KR].[FY],4.54,6,6,6,0.001,2.46e-21,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,17,8.07e-13,P..C..C.[KR],3.77,17,9,9,0.040,1.87e-19,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,18,8.12e-13,C..C..S[FY],3.77,8,8,8,0.020,1.88e-19,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,19,1.07e-12,H[ST]..[KR]P..C,4.54,14,8,8,0.012,4.13e-21,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,20,1.13e-12,P..C..C..[AS]F,4.77,7,6,6,0.001,4.38e-21,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,21,1.18e-12,R.H..E..[FY].C,4.77,8,6,6,0.001,4.56e-21,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,22,1.50e-12,KP..C..C,4.00,11,8,8,0.021,3.48e-19,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,23,2.13e-12,RP[FHY].C..C,4.63,6,6,6,0.001,8.21e-21,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,24,3.11e-12,P..C..C..S[FY],4.77,6,6,6,0.002,1.20e-20,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,25,4.64e-12,[HY].C..C..[AS][FY],4.31,6,6,6,0.002,1.79e-20,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,26,4.72e-12,[KR]P[FY].C..C,4.54,9,6,6,0.002,1.82e-20,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,27,6.20e-12,C..C.[KR].F,3.77,16,7,7,0.011,1.44e-18,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,28,6.66e-12,C..C.[KR][AS]F,4.54,7,6,6,0.002,2.57e-20,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,29,8.08e-12,C..C..[AS][FY]K,4.54,6,6,6,0.002,3.12e-20,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,30,1.21e-11,[KR]P..C..C..[AS],4.54,7,7,7,0.007,4.66e-20,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,31,1.97e-11,R..[ST]..[KR]P..C,4.54,12,8,8,0.018,7.59e-20,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,32,2.05e-11,H.R.H..E.P,5.00,9,7,7,0.007,7.91e-20,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,33,2.26e-11,P[HY].C..C.[KR],4.54,11,6,6,0.002,8.71e-20,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,34,2.83e-11,H..E.P[FY].C,4.77,8,6,6,0.002,1.09e-19,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,35,3.24e-11,P..C..C.[KR]..K,4.77,6,6,6,0.002,1.25e-19,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,36,3.69e-11,P..C..C..[AS],3.77,10,9,9,0.062,8.55e-18,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,37,3.98e-11,"P..C..C.{1,2}R.{0,1}S",5.00,9,7,7,0.008,1.54e-19,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,38,8.96e-11,P[FY].C..C,3.77,12,7,7,0.016,2.07e-17,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,39,9.85e-11,R.H..E.P..C,5.00,8,6,6,0.003,3.80e-19,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,40,1.46e-10,[KR].Y.C..C.K,4.77,8,5,5,6.27e-04,5.63e-19,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,41,1.46e-10,R.[FHY].C..C,3.63,10,7,7,0.017,3.38e-17,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,42,1.70e-10,"P..C..C.{1,2}R",4.00,11,8,8,0.038,3.94e-17,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,43,2.24e-10,H.R.H[ST]..K,4.77,12,7,7,0.010,8.63e-19,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,44,2.54e-10,R.[HY].C..C.K,4.77,6,5,5,7.01e-04,9.81e-19,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,45,2.78e-10,[KR]P..C..C,3.77,18,8,8,0.041,6.45e-17,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,46,2.91e-10,P..C..C..[AS].K,4.77,6,6,6,0.003,1.12e-18,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,47,3.45e-10,"C..C.{1,2}R.{0,1}F",4.00,9,7,7,0.019,7.99e-17,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,48,3.58e-10,"K.{0,1}P..C..C",4.00,13,8,8,0.042,8.30e-17,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,49,5.81e-10,PY.C..C,4.00,9,6,6,0.007,1.34e-16,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,50,5.81e-10,[KR].[FY].C..C,3.54,13,7,7,0.020,1.35e-16,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,51,8.21e-10,C..C.[KR].F.[HR],4.54,10,5,5,8.87e-04,3.17e-18,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,52,8.94e-10,D.P[IL]DL,4.77,8,8,8,0.028,3.45e-18,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,53,1.03e-09,P..C..CG..[FY],4.77,5,5,5,9.28e-04,3.99e-18,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,54,1.13e-09,R.H[ST].E.P,4.77,10,8,8,0.029,4.36e-18,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,55,1.13e-09,H.R.H[ST].E,4.77,9,7,7,0.013,4.37e-18,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,56,1.31e-09,[ST].E.P..C..C,4.77,8,6,6,0.004,5.03e-18,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,57,1.36e-09,C..C.RS[FY],4.77,5,5,5,9.81e-04,5.25e-18,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,58,1.41e-09,Y.C..C.K.F,5.00,8,4,4,1.13e-04,5.43e-18,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,59,2.79e-09,L..H.R.H[ST],4.77,9,7,7,0.014,1.08e-17,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,60,2.82e-09,C..C.[KR].F..S,4.77,7,5,5,0.001,1.09e-17,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,61,2.92e-09,H.R.H.GE,5.00,8,6,6,0.005,1.13e-17,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,62,3.01e-09,Y.C..C.[KR],3.77,12,6,6,0.010,6.97e-16,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,63,4.68e-09,KP..C..CG,5.00,5,5,5,0.001,1.81e-17,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,64,5.16e-09,P[IL]DLS,4.77,9,9,9,0.068,1.99e-17,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,65,5.51e-09,R.[HR]..E.P[FHY],4.40,10,8,8,0.036,2.13e-17,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,66,5.70e-09,C..CG..[FY],3.77,6,6,6,0.011,1.32e-15,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,67,6.33e-09,C..C.[KR].[FY]K,4.54,5,5,5,0.001,2.44e-17,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,68,6.48e-09,P[FHY].C..C,3.63,14,7,7,0.029,1.50e-15,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,69,6.63e-09,L..H.R.H.G,5.00,8,6,6,0.006,2.56e-17,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,70,6.70e-09,C..C..[AS]F.[HR],4.54,5,5,5,0.001,2.59e-17,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,71,1.02e-08,H.R.H.G..P,5.00,8,6,6,0.006,3.92e-17,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,72,1.04e-08,"C..C.{1,2}R.{0,1}F.{0,2}S",5.00,8,6,6,0.006,4.00e-17,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,73,1.57e-08,"P..C..C.{1,2}R.{0,1}F",5.00,7,5,5,0.002,6.05e-17,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,74,1.86e-08,L..H.R.H..E,5.00,8,6,6,0.007,7.17e-17,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,75,2.25e-08,P.DLS,4.00,13,13,13,0.59,5.21e-15,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,76,2.72e-08,C.[KR].F.[HR]..H,4.54,5,5,5,0.002,1.05e-16,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,77,3.02e-08,E..[FY].C..C,3.77,10,6,6,0.014,7.00e-15,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,78,3.24e-08,R.H[ST]..[KR]P,4.54,14,8,8,0.044,1.25e-16,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,79,3.29e-08,R.H..E.P[FY],4.77,8,6,6,0.007,1.27e-16,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,80,3.42e-08,Q..P[LMV]DL,4.63,8,8,8,0.045,1.32e-16,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,81,4.43e-08,P..C..C.RS,5.00,5,5,5,0.002,1.71e-16,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,82,4.70e-08,Y.CD.C.K,5.00,5,4,4,2.71e-04,1.81e-16,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,83,4.92e-08,R.H..E[KR]P,4.77,9,7,7,0.022,1.90e-16,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,84,5.10e-08,T.H.R.H[ST],4.77,6,6,6,0.008,1.97e-16,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,85,5.87e-08,C..C..[AS]F,3.77,9,6,6,0.016,1.36e-14,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,86,6.37e-08,H[FLM]R.H[ST],4.40,8,7,7,0.022,2.46e-16,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,87,6.51e-08,C..C..[AS]..[HR]..H,4.54,5,5,5,0.002,2.51e-16,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,88,6.60e-08,[KR]P.QC..C,4.77,7,5,5,0.002,2.55e-16,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,89,6.68e-08,C..C.[KR][AS],3.54,10,8,8,0.081,1.55e-14,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,90,6.81e-08,H.R..[ST]..KP,4.77,12,7,7,0.023,2.63e-16,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,91,7.20e-08,H[ST].E.P..C,4.77,8,6,6,0.008,2.78e-16,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,92,7.39e-08,S..KP..C..C,5.00,8,5,5,0.002,2.85e-16,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,93,8.61e-08,[HY].C..C.K.F,4.77,11,4,4,3.15e-04,3.32e-16,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,94,9.11e-08,C..CGK.F,5.00,4,4,4,3.20e-04,3.51e-16,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,95,1.18e-07,Y.C..C.K,4.00,10,5,5,0.005,2.72e-14,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,96,1.53e-07,P..C..CG[KR],4.77,5,5,5,0.003,5.89e-16,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,96,1.53e-07,[KR]P..C..CG,4.77,8,5,5,0.003,5.89e-16,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,98,1.67e-07,H[FLM]..H[ST]..K,4.40,8,7,7,0.026,6.42e-16,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,99,1.86e-07,C..C.K.F,4.00,13,5,5,0.006,4.30e-14,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,100,1.95e-07,RP..C..C,4.00,7,6,6,0.020,4.51e-14,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,101,1.98e-07,Y.C..C..S[FY],4.77,4,4,4,3.88e-04,7.63e-16,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,102,2.01e-07,"C..C.{1,2}R.{0,1}S",4.00,10,8,8,0.093,4.66e-14,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,103,2.39e-07,H.R.H[ST]G,4.77,8,6,6,0.010,9.21e-16,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,104,2.51e-07,[FY].C..C.[KR],3.54,14,6,6,0.020,5.80e-14,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,105,2.53e-07,P[ILMV][DE]L,3.31,22,19,19,2.52,5.86e-14,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,106,2.54e-07,C..[AS]F.[HR]..H,4.54,5,5,5,0.003,9.78e-16,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,107,2.82e-07,PY.C..C.K,5.00,7,4,4,4.24e-04,1.09e-15,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,108,3.31e-07,"H.{0,1}R.{1,2}H..E.P",5.00,9,7,7,0.028,1.28e-15,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,109,3.38e-07,P..C..C.K.F,5.00,9,4,4,4.44e-04,1.30e-15,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,110,3.45e-07,H.R..[ST].E.P,4.77,9,7,7,0.028,1.33e-15,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,111,3.63e-07,"Y.C..C.{0,1}K.{1,2}F",5.00,8,4,4,4.52e-04,1.40e-15,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,112,3.70e-07,H.R.H[ST],3.77,15,9,9,0.17,8.57e-14,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,113,4.40e-07,G..PY.C..C,5.00,6,4,4,4.74e-04,1.70e-15,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,114,5.00e-07,H.R.H..E..[FY],4.77,7,5,5,0.003,1.93e-15,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,115,5.17e-07,E[KR]P..C..C,4.77,7,5,5,0.003,1.99e-15,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,116,6.14e-07,R..[ST].E.P..C,4.77,8,6,6,0.012,2.37e-15,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,117,6.18e-07,P[HY].C..C..[AS],4.54,5,5,5,0.003,2.38e-15,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,118,6.71e-07,C..CD[KR].F,4.77,4,4,4,5.27e-04,2.59e-15,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,119,6.90e-07,"L..H.{1,2}R.H",4.00,12,9,9,0.19,1.60e-13,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,120,7.30e-07,R.H.GE.P,5.00,8,6,6,0.012,2.82e-15,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,121,7.32e-07,F.[HR]..HL..H,4.77,5,5,5,0.003,2.82e-15,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,122,8.63e-07,T..R.[FH].C..C,4.77,4,4,4,5.61e-04,3.33e-15,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,123,8.92e-07,L..[HR].R[IL][HK],4.31,10,8,8,0.067,3.44e-15,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,124,9.89e-07,R.H..E.P,4.00,11,9,9,0.19,2.29e-13,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,125,9.92e-07,"EH.{1,2}RI.S",5.00,6,6,6,0.013,3.83e-15,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,126,1.05e-06,H.R.H.G.K,5.00,7,5,5,0.004,4.05e-15,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,127,1.06e-06,HL..H.R.H,5.00,8,5,5,0.004,4.07e-15,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,128,1.16e-06,"P.DLS.{1,2}K",5.00,8,8,8,0.069,4.46e-15,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,129,1.22e-06,[HY].C..C.[KR],3.54,15,6,6,0.027,2.82e-13,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,130,1.37e-06,"G.{0,1}K.Y.C..C",5.00,6,4,4,6.30e-04,5.30e-15,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,131,1.41e-06,"L.EH.{1,2}R.H",5.00,8,6,6,0.014,5.44e-15,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,132,1.41e-06,H..E..[FY].C,3.77,9,6,6,0.027,3.27e-13,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,133,1.46e-06,"T.{1,2}K.{0,1}P..C..C",5.00,5,5,5,0.004,5.64e-15,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,134,1.67e-06,LK.[HR].R.[HK],4.54,7,7,7,0.036,6.46e-15,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,135,1.73e-06,"KP..C.{0,1}D.{0,1}C",5.00,5,5,5,0.004,6.68e-15,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,136,2.02e-06,R.[HY].C..C..A,4.77,4,4,4,6.94e-04,7.77e-15,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,137,2.34e-06,[HY].C..C.[KR][AS],4.31,7,5,5,0.004,9.03e-15,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,138,2.36e-06,E.P..C..C,4.00,8,6,6,0.030,5.47e-13,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,139,2.41e-06,C..CG[KR],3.77,7,6,6,0.030,5.58e-13,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,140,2.62e-06,"PY.C..C.{1,2}R",5.00,6,4,4,7.41e-04,1.01e-14,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,141,2.75e-06,HS..KP..C,5.00,8,5,5,0.004,1.06e-14,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,142,2.78e-06,R.H[ST].E[KR],4.54,9,7,7,0.038,1.07e-14,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,143,2.98e-06,E..[FY]QC..C,4.77,4,4,4,7.65e-04,1.15e-14,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,144,3.08e-06,C..C..SF,4.00,5,5,5,0.010,7.13e-13,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,145,3.10e-06,H.G..P..C..C,5.00,9,4,4,7.73e-04,1.20e-14,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,146,3.12e-06,C..C.[KR]..K,3.77,6,6,6,0.031,7.23e-13,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,147,3.49e-06,P[FY]QC..C,4.77,5,4,4,7.96e-04,1.35e-14,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,148,3.50e-06,R.[HR]..E.P,3.77,13,11,11,0.49,8.10e-13,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,149,3.61e-06,[HR].[KR].[HK].[AG]E,4.07,11,9,9,0.14,1.39e-14,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,150,3.86e-06,"Y.C..C.{0,1}K",4.00,10,5,5,0.011,8.93e-13,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,151,3.97e-06,H.R.H..EK,5.00,7,5,5,0.005,1.53e-14,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,152,4.09e-06,E..[FY].C..CG,4.77,4,4,4,8.28e-04,1.58e-14,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,153,4.38e-06,T..RP..C..C,5.00,4,4,4,8.42e-04,1.69e-14,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,154,4.47e-06,[LV]..[HR].[KR].[HK]..E,4.07,12,9,9,0.14,1.73e-14,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,155,4.63e-06,"PY.C..C.{0,1}K",5.00,7,4,4,8.54e-04,1.79e-14,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,156,4.80e-06,C..C.[KR][AS].K,4.54,5,5,5,0.005,1.85e-14,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,157,4.86e-06,[HY].C..C..[AS]F,4.54,4,4,4,8.65e-04,1.88e-14,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,158,5.00e-06,QPL.[LV][ST],4.54,9,9,9,0.15,1.93e-14,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,159,5.32e-06,P..C..C..[AS]..[HR],4.54,5,5,5,0.005,2.05e-14,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,160,5.96e-06,H.G..PY.C,5.00,6,4,4,9.10e-04,2.30e-14,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,161,6.51e-06,P..C..C,3.00,20,9,9,0.38,9.04e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,162,6.52e-06,"C.{0,1}D.{0,1}CD..F",5.00,4,4,4,9.31e-04,2.52e-14,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,163,6.54e-06,H[FLM]R.H,3.63,10,8,8,0.14,1.51e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,164,6.78e-06,Q..P.DL.[LMV],4.63,7,7,7,0.044,2.62e-14,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,165,7.07e-06,C..C.K.F[ST],4.77,6,4,4,9.49e-04,2.73e-14,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,166,7.65e-06,C..C.K.F[AS],4.77,6,4,4,9.68e-04,2.95e-14,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,167,7.72e-06,[HY].C..C.K..K,4.77,4,4,4,9.71e-04,2.98e-14,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,168,7.75e-06,P[FY].C..CG,4.77,5,4,4,9.71e-04,2.99e-14,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,169,8.23e-06,P.DL,3.00,26,21,21,5.05,1.14e-10,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,170,8.54e-06,H.R.H..E,4.00,9,7,7,0.081,1.98e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,171,9.56e-06,KP..C..C.R,5.00,4,4,4,0.001,3.69e-14,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,171,9.56e-06,RP..C..C.K,5.00,5,4,4,0.001,3.69e-14,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,173,9.90e-06,Q..P.DL[ST],4.77,7,7,7,0.046,3.82e-14,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,174,1.06e-05,"P.DL..K.{0,2}R",5.00,7,7,7,0.046,4.11e-14,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,175,1.08e-05,P..C..C..S,4.00,6,6,6,0.038,2.49e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,176,1.10e-05,G.Y.Q.M..R,5.00,4,4,4,0.001,4.24e-14,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,177,1.18e-05,"H.{0,1}R.{1,2}H.GE",5.00,8,6,6,0.020,4.57e-14,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,178,1.23e-05,[HY].C..C..[AS],3.54,9,6,6,0.039,2.85e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,179,1.28e-05,H..E[KR]P..C,4.77,7,5,5,0.006,4.94e-14,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,180,1.36e-05,H.R..[ST]GE,4.77,8,6,6,0.020,5.23e-14,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,181,1.44e-05,R..S..KP..C,5.00,8,5,5,0.006,5.55e-14,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,182,1.48e-05,H[KR]..[HY].[AG].[KR],4.07,7,7,7,0.049,5.73e-14,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,183,1.54e-05,K.[HR].R[IL][HK],4.31,7,7,7,0.049,5.93e-14,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,184,1.55e-05,KP.QC..C,5.00,4,4,4,0.001,5.99e-14,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,185,1.57e-05,R.H[ST]GE,4.77,8,6,6,0.021,6.06e-14,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,186,1.64e-05,HT..R.[FH].C,4.77,4,4,4,0.001,6.33e-14,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,187,1.74e-05,[KR].[FY].C..CG,4.54,6,4,4,0.001,6.71e-14,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,188,1.82e-05,H..RI..IW,5.00,3,3,3,7.77e-05,7.02e-14,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,189,1.83e-05,D.PLDL,5.00,6,6,6,0.021,7.07e-14,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,190,1.91e-05,S.L..H[KR]..H,4.77,6,6,6,0.021,7.36e-14,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,191,1.96e-05,P.DL[ST].K,4.77,7,7,7,0.051,7.55e-14,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,192,2.01e-05,C..C.[KR][AS]..[HR],4.31,5,5,5,0.007,7.76e-14,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,193,2.10e-05,PLDLS,5.00,7,7,7,0.051,8.11e-14,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,194,2.10e-05,L..H.R..[ST]..K,4.77,8,6,6,0.022,8.11e-14,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,195,2.19e-05,"H.{1,2}Y.{0,1}YC",4.00,5,5,5,0.015,5.08e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,196,2.20e-05,C..C..[AS].K,3.77,6,6,6,0.043,5.10e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,197,2.27e-05,G..P[HY].C..C,4.77,8,4,4,0.001,8.74e-14,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,198,2.30e-05,L..H.R.H,4.00,10,7,7,0.094,5.32e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,199,2.39e-05,H.R.HS..K,5.00,8,5,5,0.007,9.22e-14,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,200,2.52e-05,Y.C..CD..F,5.00,4,3,3,8.66e-05,9.73e-14,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,201,2.59e-05,Y.C..C,3.00,14,6,6,0.088,3.59e-10,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,202,2.66e-05,P..C..C.K..K,5.00,4,4,4,0.001,1.03e-13,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,203,2.68e-05,H.G.I..IW,5.00,3,3,3,8.83e-05,1.03e-13,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,204,2.68e-05,"L..H.{0,1}R.{1,2}H.G",5.00,8,6,6,0.023,1.03e-13,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,205,2.76e-05,M.H.Y.YC,5.00,3,3,3,8.92e-05,1.06e-13,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,206,2.89e-05,"C.{1,2}C.{1,2}R",3.00,15,11,11,0.88,4.01e-10,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,207,2.94e-05,L..H.R..[ST]G,4.77,8,6,6,0.023,1.13e-13,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,208,3.06e-05,"P..C.{0,1}D.{0,1}C.{1,2}R",5.00,5,5,5,0.007,1.18e-13,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,209,3.15e-05,HA..I..IW,5.00,3,3,3,9.33e-05,1.22e-13,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,210,3.26e-05,"H.{0,1}L..H.R.H",5.00,13,5,5,0.007,1.26e-13,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,211,3.29e-05,C.[DE]C.[KR].F,4.54,4,4,4,0.001,1.27e-13,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,212,3.86e-05,H..E..[FY]QC,4.77,4,4,4,0.001,1.49e-13,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,213,4.09e-05,"H.{0,1}R.{1,2}H.G..P",5.00,8,6,6,0.024,1.58e-13,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,214,4.10e-05,MN..Y.YC,5.00,3,3,3,1.02e-04,1.58e-13,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,215,4.26e-05,[FY].C..C,2.77,18,7,7,0.18,5.92e-10,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,216,4.30e-05,H.R..[ST]G..P,4.77,8,6,6,0.024,1.66e-13,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,217,4.44e-05,"R.{1,2}H.GE.P",5.00,10,6,6,0.025,1.71e-13,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,218,4.54e-05,R.H.GEK,5.00,7,5,5,0.008,1.75e-13,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,219,4.74e-05,E.P.QC..C,5.00,4,4,4,0.002,1.83e-13,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,220,4.79e-05,"H.{1,2}Y.{0,1}YC.{1,2}R",5.00,4,4,4,0.002,1.85e-13,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,221,4.84e-05,Y.C..CD,4.00,5,4,4,0.004,1.12e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,222,5.05e-05,R.H[ST]G..P,4.77,8,6,6,0.025,1.95e-13,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,223,5.06e-05,Y.CD.C,4.00,5,4,4,0.004,1.17e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,224,5.50e-05,[ST]..KP..C,3.77,11,8,8,0.19,1.27e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,225,5.68e-05,"E.{0,1}PN.K.R",5.00,6,6,6,0.026,2.19e-13,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,226,5.71e-05,IK.E,3.00,19,15,15,2.30,7.94e-10,2,19,19
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,227,5.86e-05,R.R..Q.[MV]..R,4.77,5,5,5,0.008,2.26e-13,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,228,5.95e-05,S.[IL]..K[MV].E,4.54,7,7,7,0.060,2.30e-13,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,229,5.97e-05,T.H.R.H,4.00,7,6,6,0.051,1.38e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,230,6.04e-05,R.T..E.N.K,5.00,5,5,5,0.008,2.33e-13,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,231,6.10e-05,C..C.[KR],2.77,23,9,9,0.49,8.47e-10,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,232,6.14e-05,[HR]H[FILM]..H,3.31,13,9,9,0.31,1.42e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,233,6.33e-05,E[KR].[FY].C..C,4.54,6,4,4,0.002,2.44e-13,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,234,6.41e-05,M..RY.YC,5.00,3,3,3,1.18e-04,2.47e-13,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,235,6.51e-05,C.[KR][AS][FY],3.31,9,8,8,0.19,1.51e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,236,6.66e-05,P..C..C.R,4.00,5,5,5,0.019,1.54e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,237,6.66e-05,C..CD..F,4.00,6,4,4,0.005,1.54e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,238,6.72e-05,C.[KR][AS]F.[HR],4.31,5,5,5,0.009,2.59e-13,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,239,6.83e-05,[FLM][KR].[HR][ST]..K,3.94,10,9,9,0.20,2.64e-13,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,240,7.22e-05,HT..RP..C,5.00,4,4,4,0.002,2.79e-13,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,241,7.30e-05,P.QC..C,4.00,7,5,5,0.020,1.69e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,242,7.43e-05,C..C..RF,4.00,6,4,4,0.005,1.72e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,243,7.50e-05,"L..H.{0,1}R.{1,2}H..E",5.00,8,6,6,0.027,2.89e-13,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,244,7.61e-05,H[KR]..YC,3.77,5,5,5,0.020,1.76e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,245,8.09e-05,P[IL]D.[ST],3.54,13,13,13,1.13,1.87e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,246,8.22e-05,R.HT.E.P,5.00,5,5,5,0.009,3.17e-13,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,247,8.26e-05,L..H.R..[ST].E,4.77,8,6,6,0.027,3.19e-13,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,248,8.44e-05,[FHY].C..C,2.63,22,8,8,0.34,1.17e-09,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,249,8.45e-05,[HK]..HL..H.R,4.77,5,5,5,0.009,3.26e-13,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,250,8.56e-05,[ILM]DL[GS],3.40,16,14,14,1.43,1.98e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,251,8.69e-05,"P..C..C.{0,1}K.{1,2}F",5.00,9,4,4,0.002,3.35e-13,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,252,9.10e-05,GE.P..C..C,5.00,6,4,4,0.002,3.51e-13,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,252,9.10e-05,E.P..C..CG,5.00,4,4,4,0.002,3.51e-13,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,254,9.11e-05,RI..IW.R,5.00,3,3,3,1.33e-04,3.52e-13,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,255,9.21e-05,"Y.C..C.{1,2}R.{0,1}S",5.00,6,4,4,0.002,3.55e-13,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,256,9.67e-05,R.H.G.KP,5.00,7,5,5,0.009,3.73e-13,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,257,9.69e-05,H..E.P..C,4.00,8,6,6,0.055,2.24e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,258,9.83e-05,PLDL,4.00,10,10,10,0.48,2.28e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,259,1.02e-04,K.H.RIH,5.00,4,4,4,0.002,3.92e-13,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,260,1.09e-04,H[ST].E[KR]P,4.54,9,7,7,0.065,4.19e-13,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,261,1.10e-04,Y..H..H.Y..C,5.00,3,3,3,1.41e-04,4.23e-13,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,262,1.21e-04,P..C..CD[KR],4.77,4,4,4,0.002,4.68e-13,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,263,1.22e-04,H..H.Y.YC,5.00,3,3,3,1.47e-04,4.72e-13,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,264,1.23e-04,P.[DE]L[ST],3.54,19,16,16,2.19,2.86e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,265,1.25e-04,C..CG..F,4.00,4,4,4,0.005,2.88e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,266,1.26e-04,K.Y.C..C,4.00,6,4,4,0.005,2.91e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,267,1.26e-04,[HK].GRI..[IV],4.54,5,5,5,0.010,4.86e-13,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,268,1.27e-04,[KR].F.[HR]..HL,4.54,5,5,5,0.010,4.89e-13,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,269,1.28e-04,G.I..IW.R,5.00,3,3,3,1.49e-04,4.94e-13,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,270,1.35e-04,Y..H.N..Y..C,5.00,3,3,3,1.52e-04,5.23e-13,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,271,1.37e-04,[HR]H[FIL][KR].H,4.17,6,6,6,0.030,5.30e-13,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,272,1.38e-04,HM.H.Y..C,5.00,3,3,3,1.52e-04,5.31e-13,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,273,1.38e-04,[HY].Q[FH][LM].[HK],4.07,6,6,6,0.030,5.32e-13,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,274,1.38e-04,GRI..IW,5.00,3,3,3,1.53e-04,5.33e-13,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,275,1.47e-04,C..[AS]..[HR]..HL,4.54,5,5,5,0.010,5.67e-13,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,276,1.47e-04,P[IL]DL..[KR],4.54,7,7,7,0.068,5.67e-13,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,277,1.47e-04,A..I..IW.R,5.00,3,3,3,1.56e-04,5.68e-13,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,278,1.48e-04,H.N..Y.YC,5.00,3,3,3,1.56e-04,5.72e-13,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,279,1.52e-04,K.H.R.H[ST],4.77,5,5,5,0.010,5.86e-13,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,280,1.57e-04,"RP..C..C.{0,1}K",5.00,5,4,4,0.002,6.05e-13,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,281,1.58e-04,A.RI..IW,5.00,3,3,3,1.60e-04,6.09e-13,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,282,1.58e-04,NH.Y.YC,5.00,3,3,3,1.60e-04,6.09e-13,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,283,1.59e-04,"K.{1,2}QC.{1,2}C",4.00,6,6,6,0.060,3.68e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,284,1.70e-04,I..IW.R.Q,5.00,3,3,3,1.64e-04,6.57e-13,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,285,1.71e-04,H..R.Q.IW,5.00,3,3,3,1.64e-04,6.58e-13,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,286,1.72e-04,H..RIQ..W,5.00,3,3,3,1.64e-04,6.63e-13,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,287,1.75e-04,HMN..Y..C,5.00,3,3,3,1.65e-04,6.75e-13,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,288,1.77e-04,[HR]H.[KR].H,3.54,9,8,8,0.22,4.09e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,289,1.79e-04,P[ILMV].[LV][ST],3.07,30,21,21,4.79,4.15e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,290,1.80e-04,MNH.Y..C,5.00,3,3,3,1.67e-04,6.93e-13,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,291,1.81e-04,IQ.IW.R,5.00,3,3,3,1.67e-04,7.00e-13,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,292,1.83e-04,C..C.RS,4.00,5,5,5,0.024,4.24e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,293,1.86e-04,"K..H.{0,1}L..H.R",5.00,5,5,5,0.010,7.18e-13,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,294,1.89e-04,RIQ.IW,5.00,3,3,3,1.69e-04,7.28e-13,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,295,1.89e-04,"C..C.{0,1}K.{1,2}F",4.00,13,5,5,0.024,4.37e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,296,1.93e-04,[DE].P.DL..[KR],4.54,7,7,7,0.070,7.45e-13,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,297,1.94e-04,P..C..CG,4.00,8,5,5,0.024,4.50e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,298,1.97e-04,"K.{1,2}HL..H.R",5.00,5,5,5,0.011,7.58e-13,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,299,1.97e-04,KP..C..C..S,5.00,4,4,4,0.002,7.58e-13,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,300,1.98e-04,[ST].E..[FY].C..C,4.54,6,4,4,0.002,7.65e-13,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,301,2.04e-04,GRI..[IV].S,4.77,5,5,5,0.011,7.85e-13,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,302,2.11e-04,"Y.C..C.{0,1}K.{0,2}K",5.00,4,4,4,0.002,8.13e-13,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,303,2.12e-04,Q[HK][MV]..R.S,4.54,6,6,6,0.032,8.19e-13,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,304,2.14e-04,KA[FH].[HR].H,4.54,5,5,5,0.011,8.25e-13,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,305,2.17e-04,C..CD[KR],3.77,5,5,5,0.025,5.03e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,306,2.25e-04,L..H.R[IL]H,4.77,7,5,5,0.011,8.69e-13,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,307,2.31e-04,D.PL.L[ST],4.77,8,7,7,0.072,8.92e-13,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,308,2.35e-04,EH.RIH,5.00,4,4,4,0.002,9.06e-13,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,309,2.39e-04,I..IW.R..E,5.00,3,3,3,1.83e-04,9.22e-13,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,310,2.39e-04,AG.I..IW,5.00,3,3,3,1.83e-04,9.23e-13,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,311,2.48e-04,[HY].C..C..[AS].K,4.54,4,4,4,0.002,9.57e-13,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,312,2.53e-04,C.IC.K.F,5.00,3,3,3,1.87e-04,9.75e-13,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,313,2.53e-04,R.H..EKP,5.00,7,5,5,0.011,9.76e-13,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,314,2.55e-04,H.G.IQ..W,5.00,3,3,3,1.87e-04,9.83e-13,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,314,2.55e-04,H.G..Q.IW,5.00,3,3,3,1.87e-04,9.83e-13,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,316,2.56e-04,G.IQ.IW,5.00,3,3,3,1.88e-04,9.88e-13,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,317,2.68e-04,R.H.G..P..C,5.00,6,4,4,0.002,1.03e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,318,2.70e-04,E.P[FY].C,3.77,8,6,6,0.066,6.25e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,319,2.79e-04,GRI..[IV]..[KR],4.54,5,5,5,0.011,1.08e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,320,2.81e-04,HM..RY..C,5.00,3,3,3,1.93e-04,1.08e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,320,2.81e-04,HM..R..YC,5.00,3,3,3,1.93e-04,1.08e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,322,2.87e-04,Q.M.H.Y..C,5.00,3,3,3,1.95e-04,1.11e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,323,2.89e-04,M.HRY..C,5.00,3,3,3,1.95e-04,1.12e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,323,2.89e-04,M.HR..YC,5.00,3,3,3,1.95e-04,1.12e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,325,2.99e-04,C..C..AF.H,5.00,3,3,3,1.97e-04,1.15e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,326,3.00e-04,HRY.YC,5.00,3,3,3,1.98e-04,1.16e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,327,3.03e-04,H.R.H.G,4.00,8,6,6,0.067,7.02e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,328,3.04e-04,[HR].[KR].[HK]..E[KR],4.07,10,8,8,0.14,1.17e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,329,3.07e-04,H[FLM]R..[ST]..K,4.40,7,6,6,0.034,1.18e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,330,3.10e-04,HA..IQ..W,5.00,3,3,3,2.00e-04,1.20e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,331,3.17e-04,[KR]..QC..C,3.77,7,5,5,0.026,7.34e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,332,3.17e-04,"L..H.{1,2}R.{0,1}H",4.00,13,9,9,0.37,7.35e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,333,3.23e-04,H.C..C.K.F,5.00,3,3,3,2.03e-04,1.25e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,333,3.23e-04,C..C.K.F.H,5.00,8,3,3,2.03e-04,1.25e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,335,3.24e-04,L..H[KR]..H.G,4.77,6,5,5,0.012,1.25e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,336,3.24e-04,[FLM]R.H[ST]..K,4.40,7,6,6,0.034,1.25e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,337,3.28e-04,L..H.RIH,5.00,4,4,4,0.002,1.26e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,338,3.30e-04,A..IQ.IW,5.00,3,3,3,2.04e-04,1.27e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,339,3.32e-04,CG[KR].[FY],3.54,6,6,6,0.068,7.69e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,340,3.33e-04,Y..H..H.Y.Y,5.00,3,3,3,2.05e-04,1.28e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,341,3.41e-04,H.K.H.R.H,5.00,4,4,4,0.003,1.31e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,342,3.41e-04,F..R.T..E.N,5.00,4,4,4,0.003,1.32e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,343,3.45e-04,"P..C..CG.{0,1}R",5.00,4,4,4,0.003,1.33e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,344,3.56e-04,[IV]K.[DE]P,3.54,12,11,11,0.75,8.25e-11,2,19,19
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,345,3.69e-04,N.RY.YC,5.00,3,3,3,2.12e-04,1.42e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,346,3.74e-04,H..H..R.Q..W,5.00,3,3,3,2.13e-04,1.44e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,347,3.81e-04,H.G..P[HY].C,4.77,8,4,4,0.003,1.47e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,348,3.81e-04,"QC.{1,2}CG",4.00,5,5,5,0.027,8.81e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,349,3.90e-04,Y..H.N..Y.Y,5.00,3,3,3,2.16e-04,1.50e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,350,3.90e-04,RI..IW..L,5.00,3,3,3,2.16e-04,1.50e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,351,3.91e-04,H[ST]GE.P,4.77,8,6,6,0.035,1.51e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,352,3.95e-04,L..H..[ILM]H,3.63,12,8,8,0.24,9.14e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,353,3.96e-04,Y..HM.H.Y,5.00,3,3,3,2.17e-04,1.53e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,354,4.01e-04,I..IW.RL,5.00,3,3,3,2.18e-04,1.55e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,355,4.08e-04,HM.H.Y.Y,5.00,3,3,3,2.19e-04,1.58e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,356,4.09e-04,"R.{1,2}H..E.P",4.00,14,9,9,0.38,9.47e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,357,4.12e-04,A..S..V[HK]..L,4.77,6,6,6,0.036,1.59e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,358,4.13e-04,QPL.L..K,5.00,6,6,6,0.036,1.60e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,359,4.14e-04,Y.Q..N..Y..C,5.00,3,3,3,2.20e-04,1.60e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,360,4.15e-04,MN.R..YC,5.00,3,3,3,2.20e-04,1.60e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,360,4.15e-04,MN.RY..C,5.00,3,3,3,2.20e-04,1.60e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,362,4.37e-04,H[KR]..H.G..P,4.77,6,5,5,0.012,1.69e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,363,4.39e-04,Q..N..Y.YC,5.00,3,3,3,2.25e-04,1.70e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,364,4.40e-04,TRH.R.H,5.00,4,4,4,0.003,1.70e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,365,4.42e-04,C.[KR][AS][FY]K,4.31,5,5,5,0.012,1.71e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,366,4.63e-04,P[IL].L[ST].[KR],4.31,9,9,9,0.24,1.79e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,367,4.66e-04,[HR][HK][FILM]..H,3.07,15,11,11,0.77,1.08e-10,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,368,4.70e-04,Y..HMN..Y,5.00,3,3,3,2.30e-04,1.81e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,369,4.82e-04,HMN..Y.Y,5.00,3,3,3,2.32e-04,1.86e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,370,4.86e-04,D.P.DL,4.00,8,8,8,0.25,1.13e-10,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,371,4.95e-04,MNH.Y.Y,5.00,3,3,3,2.34e-04,1.91e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,372,5.13e-04,T..RP[FH].C,4.77,4,4,4,0.003,1.98e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,373,5.18e-04,H..E..Y.C..C,5.00,6,3,3,2.37e-04,2.00e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,374,5.28e-04,LK.[HR]..[IL][HK],4.31,7,7,7,0.081,2.04e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,375,5.31e-04,Q.MN..Y..C,5.00,3,3,3,2.39e-04,2.05e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,376,5.54e-04,H[LM]R.HS,4.77,6,5,5,0.013,2.14e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,377,5.60e-04,H..H.G..Q..W,5.00,3,3,3,2.43e-04,2.16e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,378,5.60e-04,G.I..IW..L,5.00,3,3,3,2.43e-04,2.16e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,379,5.62e-04,H.Y.YCK,5.00,3,3,3,2.44e-04,2.17e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,380,5.67e-04,P[IL]D.S,3.77,11,11,11,0.79,1.31e-10,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,381,5.67e-04,M.H.Y..CK,5.00,3,3,3,2.44e-04,2.19e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,382,6.34e-04,Y.C.NC.K,5.00,3,3,3,2.54e-04,2.45e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,382,6.34e-04,K.Y.C.NC,5.00,3,3,3,2.54e-04,2.45e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,384,6.42e-04,H..E.P.QC,5.00,4,4,4,0.003,2.48e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,385,6.45e-04,H.RIH,4.00,5,5,5,0.030,1.49e-10,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,386,6.61e-04,H..E..F.C..C,5.00,3,3,3,2.57e-04,2.55e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,387,6.62e-04,A..I..IW..L,5.00,3,3,3,2.57e-04,2.55e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,388,6.81e-04,R.Y.C..C.K,5.00,3,3,3,2.60e-04,2.63e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,389,6.86e-04,S.L.R[HR]K,4.77,6,6,6,0.039,2.65e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,390,6.92e-04,H.GEKP,5.00,7,5,5,0.014,2.67e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,391,7.15e-04,[DE].P[ILMV].L,3.31,18,16,16,2.46,1.66e-10,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,392,7.29e-04,P..A..I..IW,5.00,3,3,3,2.66e-04,2.81e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,393,7.33e-04,C.[KR][AS]..[HR]..H,4.31,5,5,5,0.014,2.83e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,394,7.35e-04,H.NH.Y..C,5.00,3,3,3,2.67e-04,2.84e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,395,7.35e-04,LK.H..IH,5.00,4,4,4,0.003,2.84e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,396,7.41e-04,Q.M..RY..C,5.00,3,3,3,2.67e-04,2.86e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,396,7.41e-04,Q.M..R..YC,5.00,3,3,3,2.67e-04,2.86e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,398,7.49e-04,KA[FH][KR]..H,4.54,5,5,5,0.014,2.89e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,399,7.59e-04,Y..HM..R..Y,5.00,3,3,3,2.69e-04,2.93e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,400,7.77e-04,Y.C..CDK,5.00,3,3,3,2.72e-04,3.00e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,401,7.78e-04,P.DL..[KR],3.77,10,10,10,0.59,1.80e-10,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,402,7.98e-04,I..IW..LQ,5.00,3,3,3,2.74e-04,3.08e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,403,8.03e-04,R.F.C..CG,5.00,3,3,3,2.75e-04,3.10e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,404,8.09e-04,[DE].P.[DE]L,3.54,16,14,14,1.70,1.87e-10,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,405,8.09e-04,Y..HM..RY,5.00,3,3,3,2.75e-04,3.12e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,406,8.14e-04,"Y.C..C.{1,2}R",4.00,6,4,4,0.009,1.88e-10,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,407,8.18e-04,[ST]..[KR].[FY].C..C,4.31,6,4,4,0.003,3.16e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,408,8.19e-04,IQ.IW..L,5.00,3,3,3,2.76e-04,3.16e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,409,8.28e-04,HL..H.R..[ST],4.77,7,5,5,0.014,3.20e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,410,8.29e-04,H..E[KR].[FY].C,4.54,6,4,4,0.003,3.20e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,411,8.32e-04,I.SIW.R,5.00,3,3,3,2.78e-04,3.21e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,412,8.33e-04,C.NC.K.F,5.00,3,3,3,2.78e-04,3.21e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,413,8.33e-04,HM..RY.Y,5.00,3,3,3,2.78e-04,3.22e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,414,8.33e-04,Y.Q.M.H.Y,5.00,3,3,3,2.78e-04,3.22e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,414,8.33e-04,Q.M.H.Y.Y,5.00,3,3,3,2.78e-04,3.22e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,416,8.40e-04,I..IWSR,5.00,3,3,3,2.79e-04,3.24e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,416,8.40e-04,RI..IWS,5.00,3,3,3,2.79e-04,3.24e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,418,8.58e-04,M.HRY.Y,5.00,3,3,3,2.81e-04,3.31e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,419,8.63e-04,RI.SIW,5.00,3,3,3,2.81e-04,3.33e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,420,8.78e-04,R.Q.IW.R,5.00,3,3,3,2.83e-04,3.39e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,421,8.84e-04,RIQ..W.R,5.00,3,3,3,2.84e-04,3.41e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,422,9.02e-04,Y.C.N..K.F,5.00,3,3,3,2.85e-04,3.48e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,423,9.30e-04,H..RI.S.W,5.00,3,3,3,2.88e-04,3.59e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,424,9.35e-04,YQC..C.K,5.00,3,3,3,2.89e-04,3.61e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,425,9.37e-04,H..R..SIW,5.00,3,3,3,2.89e-04,3.62e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,426,9.80e-04,"K.{1,2}QC.{1,2}CG",5.00,4,4,4,0.003,3.78e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,427,9.81e-04,S.L..[HK]..E[HR],4.54,7,7,7,0.089,3.79e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,428,9.85e-04,Y.C..C..S,4.00,4,4,4,0.009,2.28e-10,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,429,0.001,CD.C.K.F,5.00,4,3,3,2.96e-04,3.90e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,430,0.001,C..C..S,3.00,8,8,8,0.47,1.41e-08,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,431,0.001,H.RIHS,5.00,4,4,4,0.003,3.95e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,432,0.001,H[LM]..HS..K,4.77,6,5,5,0.015,4.00e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,433,0.001,[ST]G..P..C..C,4.77,9,4,4,0.003,4.01e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,434,0.001,"L..L.{1,2}N..K.K",5.00,6,6,6,0.042,4.07e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,435,0.001,RI..[IV]..[KR]..E,4.54,5,5,5,0.015,4.11e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,436,0.001,"H.{0,1}R.{1,2}H.G.K",5.00,7,5,5,0.015,4.11e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,437,0.001,A..S..V..[KR]L,4.77,6,6,6,0.042,4.14e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,438,0.001,"HL..H.{0,1}R.{1,2}H",5.00,9,5,5,0.015,4.14e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,438,0.001,"HL..H.{1,2}R.{0,1}H",5.00,9,5,5,0.015,4.14e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,440,0.001,C.NC..R..H,5.00,3,3,3,3.04e-04,4.19e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,441,0.001,Y..D.C.K.F,5.00,4,3,3,3.04e-04,4.21e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,442,0.001,R.T..E.N..[LV],4.77,5,5,5,0.015,4.21e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,443,0.001,I..IW..L.E,5.00,3,3,3,3.05e-04,4.23e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,444,0.001,N..Y.YCK,5.00,3,3,3,3.05e-04,4.24e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,445,0.001,H.GE.P..C,5.00,6,4,4,0.003,4.49e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,446,0.001,MN..Y..CK,5.00,3,3,3,3.11e-04,4.50e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,447,0.001,Y.Q..N..Y.Y,5.00,3,3,3,3.11e-04,4.51e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,448,0.001,YEC.NC,5.00,3,3,3,3.12e-04,4.54e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,449,0.001,MN.RY.Y,5.00,3,3,3,3.13e-04,4.61e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,450,0.001,R.H..E..[FY],3.77,8,6,6,0.085,2.77e-10,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,451,0.001,RP[FHY].C,3.63,6,6,6,0.085,2.80e-10,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,452,0.001,QP[LV].[LV],3.54,13,13,13,1.41,2.81e-10,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,453,0.001,C..C..AF..K,5.00,3,3,3,3.15e-04,4.70e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,454,0.001,K.Y.C..CG,5.00,3,3,3,3.17e-04,4.78e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,455,0.001,C..C..A..H..H,5.00,3,3,3,3.18e-04,4.80e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,456,0.001,H[HK]L..H..L,4.77,5,5,5,0.015,4.83e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,457,0.001,G.I..IWS,5.00,3,3,3,3.18e-04,4.83e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,458,0.001,E.P[FY]QC,4.77,4,4,4,0.003,4.84e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,459,0.001,[AS]F.[HR]..HL,4.54,5,5,5,0.015,4.88e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,460,0.001,G.IQ..W.R,5.00,3,3,3,3.20e-04,4.90e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,460,0.001,G..Q.IW.R,5.00,3,3,3,3.20e-04,4.90e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,460,0.001,IW.R.Q..G,5.00,3,3,3,3.20e-04,4.90e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,463,0.001,P.DL[ST]..[KR],4.54,7,7,7,0.092,4.92e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,464,0.001,S..R..Y.H.G,5.00,4,4,4,0.003,4.96e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,465,0.001,G.I.SIW,5.00,3,3,3,3.21e-04,4.97e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,466,0.001,C..C..A..H.H,5.00,3,3,3,3.21e-04,4.98e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,467,0.001,C..C..AFK,5.00,3,3,3,3.22e-04,5.02e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,468,0.001,H..[IL][HY],2.54,22,16,16,3.39,1.83e-08,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,469,0.001,[FY].C.QC,3.77,5,4,4,0.010,3.08e-10,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,470,0.001,C..C.KAF,5.00,4,3,3,3.25e-04,5.16e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,471,0.001,[FY]QC..C,3.77,5,4,4,0.010,3.11e-10,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,472,0.001,R..[ST].E[KR]P,4.54,9,7,7,0.093,5.25e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,473,0.001,GR.Q.IW,5.00,3,3,3,3.28e-04,5.27e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,474,0.001,GRIQ..W,5.00,3,3,3,3.28e-04,5.29e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,475,0.001,QH..H.Y..C,5.00,3,3,3,3.28e-04,5.31e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,476,0.001,M..RY..CK,5.00,3,3,3,3.29e-04,5.32e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,476,0.001,M..R..YCK,5.00,3,3,3,3.29e-04,5.32e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,478,0.001,QC..C.K.F,5.00,4,3,3,3.29e-04,5.36e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,479,0.001,A..I..IWS,5.00,3,3,3,3.30e-04,5.36e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,480,0.001,H.R..[ST]G.K,4.77,7,5,5,0.016,5.42e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,481,0.001,"R.{1,2}H.GEK",5.00,9,5,5,0.016,5.42e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,482,0.001,H.R..S..KP,5.00,8,5,5,0.016,5.45e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,483,0.001,A..I.SIW,5.00,3,3,3,3.33e-04,5.51e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,484,0.001,H..HR..YC,5.00,3,3,3,3.33e-04,5.51e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,484,0.001,H..HRY..C,5.00,3,3,3,3.33e-04,5.51e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,486,0.001,H..R.Q..W.R,5.00,3,3,3,3.33e-04,5.52e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,487,0.001,H[KR]..H.G.[KR],4.54,5,5,5,0.016,5.52e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,488,0.001,RY.YCK,5.00,3,3,3,3.34e-04,5.60e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,489,0.001,H.G.I.S.W,5.00,3,3,3,3.36e-04,5.66e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,490,0.001,"YC.{1,2}R",3.00,9,8,8,0.49,2.04e-08,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,491,0.001,Y.Q.MN..Y,5.00,3,3,3,3.36e-04,5.69e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,491,0.001,Q.MN..Y.Y,5.00,3,3,3,3.36e-04,5.69e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,493,0.001,A..IQ..W.R,5.00,3,3,3,3.37e-04,5.72e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,494,0.002,F..R.T.S..N,5.00,4,4,4,0.004,5.84e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,495,0.002,E..Y.CD.C,5.00,3,3,3,3.41e-04,5.93e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,496,0.002,I..IWS..Q,5.00,3,3,3,3.43e-04,6.04e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,497,0.002,R.H[ST]G.K,4.77,7,5,5,0.016,6.05e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,498,0.002,"C.{0,1}D.{0,1}C.{1,2}R.{0,1}F",5.00,4,4,4,0.004,6.06e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,499,0.002,R.HS..KP,5.00,8,5,5,0.016,6.07e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,500,0.002,A.R.Q.IW,5.00,3,3,3,3.44e-04,6.10e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,501,0.002,A.RIQ..W,5.00,3,3,3,3.45e-04,6.15e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,502,0.002,H.N.RY..C,5.00,3,3,3,3.46e-04,6.19e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,502,0.002,H.N.R..YC,5.00,3,3,3,3.46e-04,6.19e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,504,0.002,C..C..[AS],2.77,13,9,9,0.72,2.26e-08,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,505,0.002,"Q.{0,2}P.DLS",5.00,8,7,7,0.096,6.32e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,506,0.002,K.H.R.H.G,5.00,4,4,4,0.004,6.33e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,507,0.002,PY.C..CD,5.00,3,3,3,3.49e-04,6.38e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,508,0.002,IQ..W.R.Q,5.00,3,3,3,3.51e-04,6.47e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,509,0.002,HA..I.S.W,5.00,3,3,3,3.52e-04,6.53e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,510,0.002,IQ.IWS,5.00,3,3,3,3.53e-04,6.59e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,511,0.002,NHRY..C,5.00,3,3,3,3.54e-04,6.62e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,511,0.002,NHR..YC,5.00,3,3,3,3.54e-04,6.62e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,513,0.002,PY.CD.C,5.00,3,3,3,3.54e-04,6.62e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,514,0.002,Q.IW.R.Q,5.00,3,3,3,3.54e-04,6.67e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,515,0.002,"H.{1,2}RI.S",4.00,7,7,7,0.17,4.01e-10,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,516,0.002,I.S..KP..C,5.00,4,4,4,0.004,6.73e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,517,0.002,IQSIW,5.00,3,3,3,3.57e-04,6.84e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,518,0.002,H.R.HT.E,5.00,4,4,4,0.004,6.92e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,519,0.002,Q..P.DL,4.00,8,8,8,0.30,4.19e-10,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,520,0.002,[FL]..R.R..Q.[MV],4.54,5,5,5,0.016,6.98e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,521,0.002,M.H.Y.Y.K,5.00,3,3,3,3.60e-04,7.01e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,522,0.002,Y..H.NH.Y,5.00,3,3,3,3.62e-04,7.09e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,523,0.002,[AG][GS]..Q.[IM]..R,4.31,7,6,6,0.046,7.12e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,524,0.002,K.H..IH,4.00,5,5,5,0.038,4.29e-10,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,525,0.002,CD.C..R..H,5.00,3,3,3,3.64e-04,7.20e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,526,0.002,H.NH.Y.Y,5.00,3,3,3,3.65e-04,7.30e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,527,0.002,K.Y.C..C.K,5.00,5,3,3,3.68e-04,7.44e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,528,0.002,PYQC..C,5.00,3,3,3,3.68e-04,7.47e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,529,0.002,G.I..[IV]..[KR]..E,4.54,5,5,5,0.017,7.56e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,529,0.002,I..[IV]..[KR]..E.G,4.54,5,5,5,0.017,7.56e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,531,0.002,K.[HR].R.[HKR],3.40,11,10,10,0.65,4.55e-10,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,532,0.002,"G.{1,2}Y.C..C",4.00,4,4,4,0.011,4.61e-10,3,4,4
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,533,0.002,P..C.YC.R,5.00,3,3,3,3.73e-04,7.75e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,534,0.002,P..C..CD..F,5.00,3,3,3,3.74e-04,7.82e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,535,0.002,IW.R..E.G,5.00,3,3,3,3.74e-04,7.86e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,536,0.002,R.R..Q..[AG].R,4.77,5,5,5,0.017,7.87e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,537,0.002,QH.N..Y..C,5.00,3,3,3,3.75e-04,7.88e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,537,0.002,Q..NH.Y..C,5.00,3,3,3,3.75e-04,7.88e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,539,0.002,IQ..W.R..E,5.00,3,3,3,3.78e-04,8.07e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,540,0.002,F..RKT..E,5.00,4,4,4,0.004,8.12e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,541,0.002,[FY].C..CG,3.77,6,4,4,0.011,4.93e-10,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,542,0.002,Q.IW.R..E,5.00,3,3,3,3.81e-04,8.31e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,543,0.002,QC..C..R..H,5.00,3,3,3,3.84e-04,8.46e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,544,0.002,H.G..Q..W.R,5.00,3,3,3,3.84e-04,8.47e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,545,0.002,H..H..R..S.W,5.00,3,3,3,3.86e-04,8.61e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,546,0.002,Y.Q.M..R..Y,5.00,3,3,3,3.87e-04,8.66e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,547,0.002,"GRI.{1,2}I.{1,2}S",5.00,5,5,5,0.017,8.81e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,548,0.002,IW.R.QE,5.00,3,3,3,3.90e-04,8.88e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,549,0.002,[ST]..[KR]..QC..C,4.54,5,4,4,0.004,9.09e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,550,0.002,H..IHS..K,5.00,4,4,4,0.004,9.11e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,551,0.002,H.GR.Q..W,5.00,3,3,3,3.94e-04,9.17e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,552,0.002,Q.M..RY.Y,5.00,3,3,3,3.95e-04,9.20e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,552,0.002,Y.Q.M..RY,5.00,3,3,3,3.95e-04,9.20e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,554,0.002,Y..HMNH,5.00,3,3,3,3.96e-04,9.27e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,555,0.002,H..H.Y..CK,5.00,3,3,3,3.97e-04,9.36e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,556,0.002,AG.IQ..W,5.00,3,3,3,3.99e-04,9.49e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,556,0.002,AG..Q.IW,5.00,3,3,3,3.99e-04,9.49e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,558,0.002,HMNH.Y,5.00,3,3,3,3.99e-04,9.51e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,559,0.002,P..C..C.R.F,5.00,3,3,3,3.99e-04,9.53e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,560,0.002,K.H.R..[ST]..K,4.77,5,5,5,0.018,9.62e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,561,0.003,"R.{1,2}HT.E.P",5.00,7,5,5,0.018,9.77e-12,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,562,0.003,[KR]P[FY].C,3.54,9,6,6,0.097,6.06e-10,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,563,0.003,C..C.K.F..K,5.00,3,3,3,4.08e-04,1.02e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,564,0.003,FP.RKT,5.00,4,4,4,0.004,1.03e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,565,0.003,R..Q.[MV]..R[KR],4.54,5,5,5,0.018,1.05e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,566,0.003,HA.R.Q..W,5.00,3,3,3,4.13e-04,1.06e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,567,0.003,C..C.K.FK,5.00,3,3,3,4.15e-04,1.07e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,568,0.003,GE..Y.C..C,5.00,5,3,3,4.16e-04,1.07e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,569,0.003,S..M.H.Y..C,5.00,3,3,3,4.18e-04,1.09e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,570,0.003,[HK]..RI..[IV].S,4.54,5,5,5,0.018,1.10e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,571,0.003,H.YSYC,5.00,3,3,3,4.19e-04,1.10e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,572,0.003,F.LRKT,5.00,4,4,4,0.004,1.12e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,573,0.003,"H..E.P..C.{0,1}N",5.00,4,4,4,0.004,1.13e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,574,0.003,"V..R.{1,2}SP",4.00,10,10,10,0.68,6.84e-10,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,575,0.003,C.K.F.H..H,5.00,3,3,3,4.24e-04,1.14e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,576,0.003,H[ST].E..[FY].C,4.54,6,4,4,0.004,1.14e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,577,0.003,"R.{1,2}H.G.KP",5.00,9,5,5,0.018,1.15e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,578,0.003,F.L..T..E.N,5.00,4,4,4,0.004,1.16e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,579,0.003,C.K.F.H.H,5.00,3,3,3,4.28e-04,1.17e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,580,0.003,[IL]DLS.K,4.77,6,6,6,0.050,1.19e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,581,0.003,KPY.C..C,5.00,5,3,3,4.30e-04,1.19e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,582,0.003,E..Y.C..C.K,5.00,5,3,3,4.30e-04,1.19e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,583,0.003,M.H.YS.C,5.00,3,3,3,4.31e-04,1.20e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,584,0.003,C..AF.H..H,5.00,3,3,3,4.31e-04,1.20e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,585,0.003,M.H..SYC,5.00,3,3,3,4.33e-04,1.21e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,586,0.003,P.DL..K,4.00,8,8,8,0.32,7.32e-10,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,587,0.003,C..AF.H.H,5.00,3,3,3,4.37e-04,1.25e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,588,0.003,R.H.C..C.K,5.00,3,3,3,4.41e-04,1.29e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,589,0.003,"C.{1,2}CG",3.00,12,8,8,0.54,4.65e-08,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,590,0.003,C..C.KR..H,5.00,6,3,3,4.42e-04,1.30e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,590,0.003,C.KC..R..H,5.00,3,3,3,4.42e-04,1.30e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,592,0.003,Y..H..HR..Y,5.00,3,3,3,4.45e-04,1.32e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,593,0.003,MN..Y.Y.K,5.00,3,3,3,4.45e-04,1.32e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,594,0.003,K.YEC..C,5.00,3,3,3,4.45e-04,1.32e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,594,0.003,YEC..C.K,5.00,3,3,3,4.45e-04,1.32e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,596,0.003,Y.[HK].G.[KR]P,4.54,5,5,5,0.019,1.32e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,597,0.003,"K.{0,1}R.{0,1}R",3.00,28,23,23,8.62,4.82e-08,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,598,0.004,Y.QH..H.Y,5.00,3,3,3,4.51e-04,1.37e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,598,0.004,QH..H.Y.Y,5.00,3,3,3,4.51e-04,1.37e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,600,0.004,C.[KR][AS]F,3.54,7,6,6,0.10,8.31e-10,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,601,0.004,Y..H..HRY,5.00,3,3,3,4.55e-04,1.41e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,602,0.004,C..C..R..H.G,5.00,6,3,3,4.56e-04,1.42e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,603,0.004,Y..H.N.R..Y,5.00,3,3,3,4.56e-04,1.42e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,604,0.004,CP.C.K.F,5.00,3,3,3,4.58e-04,1.44e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,605,0.004,H..HRY.Y,5.00,3,3,3,4.60e-04,1.46e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,606,0.004,P..C..CG..F,5.00,3,3,3,4.61e-04,1.47e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,607,0.004,I..IWS.L,5.00,3,3,3,4.63e-04,1.48e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,607,0.004,I.SIW..L,5.00,3,3,3,4.63e-04,1.48e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,609,0.004,R.H..E..[FY]Q,4.77,4,4,4,0.005,1.50e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,610,0.004,Y..H.N.RY,5.00,3,3,3,4.65e-04,1.51e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,611,0.004,"R.K.{1,2}K.A..R",5.00,5,5,5,0.019,1.51e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,612,0.004,H[ILM][KR].H,3.40,15,8,8,0.33,9.15e-10,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,613,0.004,R.Q.IW..L,5.00,3,3,3,4.67e-04,1.53e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,614,0.004,C.YC.RS,5.00,3,3,3,4.68e-04,1.53e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,615,0.004,G.R.H.C..C,5.00,3,3,3,4.68e-04,1.53e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,616,0.004,C.NC.K,4.00,4,4,4,0.013,9.21e-10,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,617,0.004,RIQ..W..L,5.00,3,3,3,4.68e-04,1.54e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,618,0.004,H.N.RY.Y,5.00,3,3,3,4.70e-04,1.55e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,619,0.004,"H.{0,1}R.{1,2}H..EK",5.00,7,5,5,0.019,1.55e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,620,0.004,C..S[FY],2.77,10,10,10,1.09,5.65e-08,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,621,0.004,IQ..W.RL,5.00,3,3,3,4.73e-04,1.59e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,622,0.004,Q.IW.RL,5.00,3,3,3,4.79e-04,1.64e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,623,0.004,NHRY.Y,5.00,3,3,3,4.80e-04,1.66e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,624,0.004,L..H.[KR].H,3.77,14,7,7,0.20,9.96e-10,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,625,0.004,H.N..Y..CK,5.00,3,3,3,4.81e-04,1.67e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,626,0.004,R.R..Q.[MV][AG],4.54,5,5,5,0.020,1.68e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,626,0.004,R..Q.[MV][AG].R,4.54,5,5,5,0.020,1.68e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,628,0.004,"H.{1,2}EH.G.{0,1}R",5.00,5,5,5,0.020,1.68e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,629,0.004,[HK]..RI..[IV]..[KR],4.31,5,5,5,0.020,1.69e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,630,0.004,RI.S.W.R,5.00,3,3,3,4.83e-04,1.69e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,631,0.004,R..SIW.R,5.00,3,3,3,4.84e-04,1.70e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,632,0.004,HM.HR..Y,5.00,3,3,3,4.85e-04,1.70e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,632,0.004,Y..HM.HR,5.00,3,3,3,4.85e-04,1.70e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,634,0.004,IW.RLQ,5.00,3,3,3,4.85e-04,1.71e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,635,0.004,[KR].[HK].[AG]E[KR],4.07,10,8,8,0.20,1.71e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,636,0.004,C..C..A.K..H,5.00,3,3,3,4.86e-04,1.72e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,637,0.004,N..YSYC,5.00,3,3,3,4.87e-04,1.73e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,638,0.004,P..C..C..AF,5.00,4,3,3,4.87e-04,1.73e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,639,0.004,"E.P..C.{0,1}N.{0,1}C",5.00,4,4,4,0.005,1.73e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,640,0.004,HAG..Q..W,5.00,3,3,3,4.88e-04,1.74e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,641,0.004,C..CD..F..S,5.00,3,3,3,4.88e-04,1.74e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,642,0.005,K.H.R.H..E,5.00,4,4,4,0.005,1.76e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,643,0.005,PY.C..CG,5.00,3,3,3,4.89e-04,1.76e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,644,0.005,EC..C.K.F,5.00,4,3,3,4.90e-04,1.76e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,645,0.005,D..[IL]DL,3.77,9,8,8,0.33,1.06e-09,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,646,0.005,NH.Y..CK,5.00,3,3,3,4.90e-04,1.77e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,647,0.005,C..[AS][FY]K,3.54,6,6,6,0.11,1.07e-09,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,648,0.005,C..C..A..HK,5.00,3,3,3,4.93e-04,1.79e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,649,0.005,F..RK..S..N,5.00,4,4,4,0.005,1.79e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,650,0.005,"Y.{0,1}YC",3.00,6,6,6,0.21,6.48e-08,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,651,0.005,R..[ST]GE.P,4.77,8,6,6,0.053,1.80e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,652,0.005,M..RY.Y.K,5.00,3,3,3,4.94e-04,1.81e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,653,0.005,HM.HRY,5.00,3,3,3,4.96e-04,1.82e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,654,0.005,S..MN..Y..C,5.00,3,3,3,4.97e-04,1.84e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,655,0.005,C..C.KA..H,5.00,3,3,3,4.98e-04,1.85e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,655,0.005,C..C..A.KH,5.00,3,3,3,4.98e-04,1.85e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,657,0.005,Y.QH.N..Y,5.00,3,3,3,4.98e-04,1.85e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,657,0.005,QH.N..Y.Y,5.00,3,3,3,4.98e-04,1.85e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,657,0.005,Q..NH.Y.Y,5.00,3,3,3,4.98e-04,1.85e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,657,0.005,Y.Q..NH.Y,5.00,3,3,3,4.98e-04,1.85e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,661,0.005,Y..HMN.R,5.00,3,3,3,5.00e-04,1.87e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,661,0.005,HMN.R..Y,5.00,3,3,3,5.00e-04,1.87e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,663,0.005,C..C.R.F..S,5.00,3,3,3,5.00e-04,1.87e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,664,0.005,CD.C.K,4.00,6,4,4,0.014,1.14e-09,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,665,0.005,KT.S.PN,5.00,5,5,5,0.020,1.90e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,666,0.005,F..R.T..E..L,5.00,4,4,4,0.005,1.90e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,667,0.005,A[IV].S..VK,4.77,5,5,5,0.020,1.92e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,668,0.005,[KR][AS]F.[HR]..H,4.31,5,5,5,0.020,1.92e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,669,0.005,EH..IHS,5.00,4,4,4,0.005,1.93e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,670,0.005,H[HK]L..H..[IL],4.54,7,5,5,0.020,1.93e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,671,0.005,[LM][KR].[HR]S..K,4.31,8,7,7,0.11,1.93e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,672,0.005,MNHR..Y,5.00,3,3,3,5.06e-04,1.94e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,673,0.005,Y.QHM.H,5.00,3,3,3,5.08e-04,1.96e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,673,0.005,QHM.H.Y,5.00,3,3,3,5.08e-04,1.96e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,675,0.005,HMN.RY,5.00,3,3,3,5.10e-04,1.99e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,676,0.005,"Y.C.NC.{0,1}K",5.00,3,3,3,5.10e-04,1.99e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,677,0.005,MN..YS.C,5.00,3,3,3,5.11e-04,1.99e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,678,0.005,[FM]..RK.[AG]..P,4.54,5,5,5,0.020,2.00e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,679,0.005,R.H[ST].E,3.77,10,8,8,0.34,1.20e-09,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,680,0.005,[IV]K.E..[DE],3.54,12,10,10,0.72,1.21e-09,2,19,19
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,681,0.005,C..C..RFS,5.00,5,3,3,5.13e-04,2.03e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,682,0.005,H.R..[ST].EK,4.77,7,5,5,0.020,2.03e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,683,0.005,"G..S.H..H.{0,2}R",5.00,5,5,5,0.020,2.03e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,684,0.005,C.[KR].F..S..L,4.77,5,4,4,0.005,2.05e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,685,0.005,MNHRY,5.00,3,3,3,5.16e-04,2.05e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,686,0.005,"H.{1,2}K.H.R.H",5.00,6,4,4,0.005,2.06e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,687,0.005,C..CD,3.00,8,6,6,0.22,7.51e-08,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,688,0.005,C..C.RSF,5.00,3,3,3,5.18e-04,2.09e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,689,0.005,Q..N.RY..C,5.00,3,3,3,5.19e-04,2.09e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,689,0.005,Q..N.R..YC,5.00,3,3,3,5.19e-04,2.09e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,691,0.005,F..R.T..EP,5.00,4,4,4,0.005,2.10e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,692,0.005,L.E..RIH,5.00,4,4,4,0.005,2.10e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,693,0.005,C.[KR].[FY],2.54,21,10,10,1.12,7.65e-08,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,694,0.006,IW.R..E..L,5.00,3,3,3,5.23e-04,2.15e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,695,0.006,"L.{0,1}E.{0,1}H.{1,2}R.H",5.00,8,6,6,0.055,2.15e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,696,0.006,[HK].G.I..[IV].S,4.54,5,5,5,0.021,2.15e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,697,0.006,F.LR.T..E,5.00,4,4,4,0.005,2.16e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,698,0.006,G.Y..H..H.Y,5.00,3,3,3,5.26e-04,2.18e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,699,0.006,C..R..H.G.Y,5.00,5,3,3,5.26e-04,2.18e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,700,0.006,FP.R.T..E,5.00,4,4,4,0.005,2.19e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,701,0.006,Y.C..C..[AS],3.77,7,4,4,0.014,1.33e-09,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,702,0.006,G.IQ..W..L,5.00,3,3,3,5.32e-04,2.25e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,702,0.006,G..Q.IW..L,5.00,3,3,3,5.32e-04,2.25e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,704,0.006,K.[FH][KR][HR].H,4.31,5,5,5,0.021,2.25e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,705,0.006,A[FH][KR][HR].H,4.31,5,5,5,0.021,2.27e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,706,0.006,H.G.Y..HM,5.00,3,3,3,5.35e-04,2.30e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,706,0.006,G.Y..HM.H,5.00,3,3,3,5.35e-04,2.30e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,708,0.006,HR..YCK,5.00,3,3,3,5.38e-04,2.33e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,708,0.006,HRY..CK,5.00,3,3,3,5.38e-04,2.33e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,710,0.006,KA.[KR][HR].H,4.54,5,5,5,0.021,2.33e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,711,0.006,IW..LQ..G,5.00,3,3,3,5.38e-04,2.34e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,712,0.006,G.Y..H.N..Y,5.00,3,3,3,5.41e-04,2.37e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,713,0.006,IW.RL.E,5.00,3,3,3,5.41e-04,2.38e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,714,0.006,RP..C.IC,5.00,3,3,3,5.43e-04,2.39e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,715,0.006,R..Y.H[ST]G,4.77,4,4,4,0.005,2.44e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,716,0.006,L.E..R[IL]H,4.77,7,5,5,0.021,2.46e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,717,0.006,"K.{1,2}HL..H.{0,1}R",5.00,5,5,5,0.021,2.47e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,718,0.006,Q.MNH.Y,5.00,3,3,3,5.50e-04,2.49e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,718,0.006,Y.Q.MNH,5.00,3,3,3,5.50e-04,2.49e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,720,0.006,QHMN..Y,5.00,3,3,3,5.51e-04,2.51e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,721,0.007,[ILM]D[LV][ST],3.17,18,14,14,1.99,1.53e-09,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,722,0.007,C..CG..F..S,5.00,3,3,3,5.55e-04,2.56e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,723,0.007,L..H..IH,4.00,5,5,5,0.049,1.54e-09,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,724,0.007,S..M..RY..C,5.00,3,3,3,5.55e-04,2.57e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,724,0.007,S..M..R..YC,5.00,3,3,3,5.55e-04,2.57e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,726,0.007,Y.QHMN,5.00,3,3,3,5.56e-04,2.57e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,727,0.007,I.S.W.R.Q,5.00,3,3,3,5.57e-04,2.59e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,728,0.007,G.I.S.W.R,5.00,3,3,3,5.59e-04,2.61e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,729,0.007,RI..[IV].S[KR],4.54,5,5,5,0.021,2.62e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,730,0.007,A..IQ..W..L,5.00,3,3,3,5.60e-04,2.63e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,731,0.007,H..R.Q..W..L,5.00,3,3,3,5.63e-04,2.67e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,732,0.007,E.PY.C..C,5.00,5,3,3,5.65e-04,2.71e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,733,0.007,Y..D.C.K,4.00,5,4,4,0.015,1.62e-09,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,734,0.007,G.Y..HMN,5.00,3,3,3,5.68e-04,2.75e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,735,0.007,[FLM]..H[ST]..KP,4.40,7,6,6,0.057,2.75e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,736,0.007,RYSYC,5.00,3,3,3,5.69e-04,2.76e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,737,0.007,H..H.Y.Y.K,5.00,3,3,3,5.70e-04,2.77e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,738,0.007,LK.H.R.H,5.00,4,4,4,0.005,2.78e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,739,0.007,A..I.S.W.R,5.00,3,3,3,5.70e-04,2.78e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,740,0.007,K..QC..C,4.00,4,4,4,0.015,1.67e-09,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,741,0.007,[ST]..[KR]P..C,3.54,15,8,8,0.35,1.67e-09,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,742,0.007,C..C.KA,4.00,5,4,4,0.015,1.67e-09,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,743,0.007,R.Q.IWS,5.00,3,3,3,5.71e-04,2.79e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,743,0.007,SIW.R.Q,5.00,3,3,3,5.71e-04,2.79e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,743,0.007,IQS.W.R,5.00,3,3,3,5.71e-04,2.79e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,746,0.007,RIQ..WS,5.00,3,3,3,5.73e-04,2.81e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,746,0.007,IQ..WSR,5.00,3,3,3,5.73e-04,2.81e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,748,0.007,M..R.SYC,5.00,3,3,3,5.73e-04,2.82e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,748,0.007,M..RYS.C,5.00,3,3,3,5.73e-04,2.82e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,750,0.007,GRI.S.W,5.00,3,3,3,5.73e-04,2.82e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,751,0.007,GR..SIW,5.00,3,3,3,5.74e-04,2.83e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,752,0.007,H.RI.S..K,5.00,4,4,4,0.005,2.84e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,753,0.007,P..A..IQ..W,5.00,3,3,3,5.76e-04,2.86e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,754,0.007,C..C..SYK,5.00,3,3,3,5.77e-04,2.87e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,755,0.007,H..R..S.W.R,5.00,3,3,3,5.77e-04,2.88e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,756,0.007,IWSR.Q,5.00,3,3,3,5.79e-04,2.90e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,756,0.007,Q.IWSR,5.00,3,3,3,5.79e-04,2.90e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,756,0.007,RIQS.W,5.00,3,3,3,5.79e-04,2.90e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,756,0.007,QSIW.R,5.00,3,3,3,5.79e-04,2.90e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,756,0.007,R.QSIW,5.00,3,3,3,5.79e-04,2.90e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,761,0.008,HLK.H.R,5.00,4,4,4,0.005,2.91e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,762,0.008,P.H..R.Q..W,5.00,3,3,3,5.80e-04,2.92e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,763,0.008,C.[KR].F.[HR],3.54,10,5,5,0.050,1.77e-09,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,764,0.008,A.RI.S.W,5.00,3,3,3,5.84e-04,2.99e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,765,0.008,A.R..SIW,5.00,3,3,3,5.86e-04,3.01e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,766,0.008,"R.{1,2}H..EKP",5.00,9,5,5,0.022,3.01e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,767,0.008,C.[KR].F.[HR]S,4.54,4,4,4,0.005,3.02e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,768,0.008,T.H[FL]R.H,4.77,4,4,4,0.005,3.05e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,769,0.008,RIHS..K,5.00,4,4,4,0.006,3.10e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,770,0.008,T..E.N.K[LV],4.77,5,5,5,0.022,3.12e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,771,0.008,P[FY].C,2.77,14,9,9,0.87,1.13e-07,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,772,0.008,C.NC.KR,5.00,3,3,3,5.96e-04,3.17e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,773,0.008,[HK].G.I..[IV]..[KR],4.31,5,5,5,0.022,3.18e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,774,0.008,IQ..W..LQ,5.00,3,3,3,5.99e-04,3.22e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,775,0.008,C..C.K..K..H,5.00,3,3,3,6.01e-04,3.25e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,776,0.008,S..M.H.Y.Y,5.00,3,3,3,6.04e-04,3.29e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,777,0.009,Q.IW..LQ,5.00,3,3,3,6.05e-04,3.32e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,778,0.009,F..RKT.S,5.00,4,4,4,0.006,3.32e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,779,0.009,C..CGK,4.00,5,4,4,0.016,2.04e-09,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,780,0.009,YS..M.H.Y,5.00,3,3,3,6.11e-04,3.41e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,781,0.009,"C..CG.{0,1}R.{0,1}S",5.00,4,4,4,0.006,3.44e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,782,0.009,C..C.K..KH,5.00,3,3,3,6.13e-04,3.44e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,783,0.009,[HR].[KR].[HK].[AG].[KR],3.84,10,8,8,0.22,3.45e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,784,0.009,H..E..Y..D.C,5.00,3,3,3,6.20e-04,3.57e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,785,0.009,P..C.IC.K,5.00,3,3,3,6.22e-04,3.61e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,786,0.009,IW..L.E.G,5.00,3,3,3,6.23e-04,3.62e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,787,0.009,M.H.YSY,5.00,3,3,3,6.24e-04,3.64e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,788,0.010,I.SIWS,5.00,3,3,3,6.27e-04,3.70e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,789,0.010,R..[ST].E..[FY].C,4.54,6,4,4,0.006,3.72e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,790,0.010,E.PF.C..C,5.00,3,3,3,6.31e-04,3.77e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,791,0.010,"L..H.{0,2}R.{1,2}H",4.00,13,9,9,0.55,2.28e-09,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,792,0.010,H..E..Y.CD,5.00,3,3,3,6.34e-04,3.82e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,793,0.010,P..C..C..R..H,5.00,6,3,3,6.35e-04,3.83e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,794,0.010,C..C.K.F..S,5.00,4,3,3,6.35e-04,3.83e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,795,0.010,C..AF..K.H,5.00,3,3,3,6.36e-04,3.86e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,796,0.010,H..R.Q..WS,5.00,3,3,3,6.39e-04,3.90e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,797,0.010,IQ..W..L.E,5.00,3,3,3,6.39e-04,3.91e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,798,0.010,H.R.HS,4.00,9,6,6,0.12,2.36e-09,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,799,0.010,R.H..E..Y.C,5.00,5,3,3,6.44e-04,4.00e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,800,0.010,C..AF..KH,5.00,3,3,3,6.44e-04,4.00e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,800,0.010,C..AFK..H,5.00,3,3,3,6.44e-04,4.00e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,802,0.010,I.S.W.R..E,5.00,3,3,3,6.45e-04,4.02e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,803,0.010,Q.IW..L.E,5.00,3,3,3,6.45e-04,4.03e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,804,0.010,H..R.QS.W,5.00,3,3,3,6.46e-04,4.03e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,805,0.011,CD.C.KR,5.00,3,3,3,6.49e-04,4.10e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,806,0.011,C..AF.HK,5.00,3,3,3,6.50e-04,4.12e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,807,0.011,IWS..Q..G,5.00,3,3,3,6.52e-04,4.14e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,808,0.011,H.G..Q..W..L,5.00,3,3,3,6.52e-04,4.15e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,809,0.011,C.K.F[ST],3.77,7,5,5,0.054,2.50e-09,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,810,0.011,Q.M.HR..Y,5.00,3,3,3,6.54e-04,4.18e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,811,0.011,PY.C,3.00,10,7,7,0.42,1.51e-07,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,812,0.011,QHM..R..Y,5.00,3,3,3,6.55e-04,4.21e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,813,0.011,C.KAF.H,5.00,3,3,3,6.56e-04,4.23e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,814,0.011,G.IQ..WS,5.00,3,3,3,6.58e-04,4.27e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,814,0.011,G..Q.IWS,5.00,3,3,3,6.58e-04,4.27e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,816,0.011,C..AFKH,5.00,3,3,3,6.58e-04,4.27e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,817,0.011,Y.Q.M.HR,5.00,3,3,3,6.60e-04,4.30e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,818,0.011,H.[HY].L..[HK].[HR],4.31,5,5,5,0.024,4.30e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,819,0.011,Q.M.[HY]R,3.77,5,5,5,0.054,2.59e-09,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,820,0.011,SIW.R..E,5.00,3,3,3,6.61e-04,4.32e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,821,0.011,Y.QHM..R,5.00,3,3,3,6.61e-04,4.33e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,822,0.011,IW..LQE,5.00,3,3,3,6.61e-04,4.33e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,823,0.011,HR.L.[HR]..S,4.77,8,5,5,0.024,4.33e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,824,0.011,H.N..Y.Y.K,5.00,3,3,3,6.63e-04,4.36e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,825,0.011,R.Q..W.R.Q,5.00,3,3,3,6.63e-04,4.36e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,826,0.011,N.R..YCK,5.00,3,3,3,6.63e-04,4.37e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,826,0.011,N.RY..CK,5.00,3,3,3,6.63e-04,4.37e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,828,0.011,GS..Q.M..R,5.00,4,4,4,0.006,4.39e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,829,0.011,G.IQS.W,5.00,3,3,3,6.65e-04,4.41e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,830,0.011,I..IW.R,4.00,3,3,3,0.003,2.66e-09,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,831,0.011,"EH.{1,2}RI",4.00,6,6,6,0.12,2.66e-09,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,832,0.011,G..QSIW,5.00,3,3,3,6.66e-04,4.43e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,833,0.011,Q.M.HRY,5.00,3,3,3,6.68e-04,4.46e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,834,0.012,IWSR..E,5.00,3,3,3,6.69e-04,4.48e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,835,0.012,QHM..RY,5.00,3,3,3,6.69e-04,4.49e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,836,0.012,RI..IW,4.00,3,3,3,0.003,2.76e-09,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,837,0.012,NH.Y.Y.K,5.00,3,3,3,6.75e-04,4.61e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,838,0.012,P[ILMV].[LV][AS],3.07,29,20,20,5.27,2.78e-09,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,839,0.012,FPLR.T,5.00,4,4,4,0.006,4.68e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,840,0.012,P.H.G..Q..W,5.00,3,3,3,6.84e-04,4.78e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,841,0.012,Y.Q..N.R..Y,5.00,3,3,3,6.85e-04,4.81e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,842,0.012,A..IQ..WS,5.00,3,3,3,6.85e-04,4.82e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,843,0.012,G.I..[IV].S[KR],4.54,5,5,5,0.024,4.83e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,844,0.012,GR.Q..W.R,5.00,3,3,3,6.87e-04,4.85e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,845,0.013,C.K.F[AS],3.77,7,5,5,0.055,2.93e-09,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,846,0.013,K.K.K.[GS].[IV],4.54,6,6,6,0.063,4.95e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,847,0.013,A..IQS.W,5.00,3,3,3,6.92e-04,4.97e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,848,0.013,K..QC..C..R,5.00,3,3,3,6.92e-04,4.97e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,849,0.013,C.RS[FY],3.77,5,5,5,0.056,2.99e-09,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,850,0.013,R.H..E..F.C,5.00,3,3,3,6.94e-04,4.99e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,851,0.013,H..[ILM][HY],2.40,24,16,16,3.98,1.80e-07,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,852,0.013,Y..H..H..S.C,5.00,3,3,3,6.95e-04,5.03e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,853,0.013,H.GR..S.W,5.00,3,3,3,6.95e-04,5.04e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,854,0.013,P..C.NC..R,5.00,3,3,3,6.95e-04,5.04e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,855,0.013,HR.L.RT,5.00,5,4,4,0.006,5.07e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,856,0.013,G.Y..HM..R,5.00,3,3,3,6.97e-04,5.08e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,857,0.013,Y.Q..N.RY,5.00,3,3,3,6.99e-04,5.11e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,857,0.013,Q..N.RY.Y,5.00,3,3,3,6.99e-04,5.11e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,859,0.013,AG.I.S.W,5.00,3,3,3,7.00e-04,5.13e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,860,0.013,H[ST]..[KR].[FY].C,4.31,6,4,4,0.006,5.18e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,861,0.013,S.H..H.Y..C,5.00,3,3,3,7.03e-04,5.20e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,862,0.014,[ST]..D.PL..[ST],4.54,7,7,7,0.13,5.26e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,863,0.014,A.R.Q..W.R,5.00,3,3,3,7.06e-04,5.26e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,864,0.014,S..MN..Y.Y,5.00,3,3,3,7.06e-04,5.28e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,865,0.014,FP..KT..E,5.00,4,4,4,0.006,5.39e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,866,0.014,IQ..WS..Q,5.00,3,3,3,7.13e-04,5.42e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,867,0.014,QC.KC..R,5.00,3,3,3,7.13e-04,5.42e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,867,0.014,QC..C.KR,5.00,3,3,3,7.13e-04,5.42e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,869,0.014,YS..MN..Y,5.00,3,3,3,7.14e-04,5.45e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,870,0.014,H[ST]GEK,4.77,7,5,5,0.025,5.46e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,871,0.014,R..[ST]..K..QC,4.77,5,4,4,0.006,5.48e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,872,0.014,H[ST].E.P,3.77,11,9,9,0.58,3.34e-09,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,873,0.014,Q.IWS..Q,5.00,3,3,3,7.19e-04,5.58e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,874,0.014,H..H.YS.C,5.00,3,3,3,7.20e-04,5.59e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,875,0.014,R.Q..W.R..E,5.00,3,3,3,7.20e-04,5.59e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,876,0.014,H..H..SYC,5.00,3,3,3,7.21e-04,5.62e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,877,0.015,HA.R..S.W,5.00,3,3,3,7.25e-04,5.70e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,878,0.015,H.G.Y.Q.M,5.00,3,3,3,7.25e-04,5.71e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,878,0.015,G.Y.Q.M.H,5.00,3,3,3,7.25e-04,5.71e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,880,0.015,MN..YSY,5.00,3,3,3,7.27e-04,5.76e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,881,0.015,F.L..T.S..N,5.00,4,4,4,0.006,5.81e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,882,0.015,P..C..C..SY,5.00,3,3,3,7.31e-04,5.84e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,883,0.015,YSYCK,5.00,3,3,3,7.33e-04,5.89e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,884,0.015,HRP..RT,5.00,5,4,4,0.006,5.92e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,885,0.015,P..C..CD,4.00,4,4,4,0.018,3.58e-09,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,886,0.016,"K.Y.C..C.{0,1}K",5.00,5,3,3,7.39e-04,6.05e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,887,0.016,PY.C..C..S,5.00,3,3,3,7.39e-04,6.05e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,887,0.016,P..C.YC..S,5.00,3,3,3,7.39e-04,6.05e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,889,0.016,EH.RI.S,5.00,4,4,4,0.007,6.09e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,890,0.016,R..Q.[MV]..R..[GS],4.54,5,5,5,0.025,6.11e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,891,0.016,P..C.I..K.F,5.00,3,3,3,7.42e-04,6.11e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,892,0.016,H.G..Q..WS,5.00,3,3,3,7.42e-04,6.13e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,893,0.016,E..RIHS,5.00,4,4,4,0.007,6.14e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,894,0.016,F..R.T.SE,5.00,4,4,4,0.007,6.14e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,895,0.016,G.Y.QHM,5.00,3,3,3,7.43e-04,6.15e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,896,0.016,CGK.F,4.00,4,4,4,0.018,3.70e-09,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,897,0.016,C..C.K..K,4.00,4,4,4,0.018,3.75e-09,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,898,0.016,"C.IC.{0,1}K.{1,2}F",5.00,3,3,3,7.48e-04,6.27e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,899,0.016,H.G..QS.W,5.00,3,3,3,7.51e-04,6.35e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,900,0.016,G..Q..W.R.Q,5.00,3,3,3,7.52e-04,6.36e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,900,0.016,Q..W.R.Q..G,5.00,3,3,3,7.52e-04,6.36e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,902,0.017,Q..N..Y..CK,5.00,3,3,3,7.54e-04,6.43e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,903,0.017,C..A..H.HH,5.00,3,3,3,7.55e-04,6.44e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,904,0.017,R.[HR]..E..[FHY],3.40,10,8,8,0.39,3.91e-09,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,905,0.017,F.L.KT..E,5.00,4,4,4,0.007,6.60e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,906,0.017,H[KR]..HTG,4.77,4,4,4,0.007,6.62e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,907,0.017,H..[HR].[HY].Y,3.54,5,5,5,0.059,3.97e-09,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,908,0.017,G.I..IW,4.00,3,3,3,0.003,3.99e-09,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,909,0.017,H[ST]G..P..C,4.77,9,4,4,0.007,6.67e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,910,0.017,HRY.Y.K,5.00,3,3,3,7.64e-04,6.67e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,911,0.017,P..C..C..A..H,5.00,3,3,3,7.64e-04,6.68e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,912,0.017,Q.MN.R..Y,5.00,3,3,3,7.66e-04,6.72e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,913,0.017,"P..C.{0,1}N.{0,1}C",4.00,6,5,5,0.059,4.04e-09,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,914,0.017,C.K.F..K.H,5.00,3,3,3,7.68e-04,6.78e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,915,0.018,Y.Q.M..R,4.00,4,4,4,0.019,4.09e-09,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,916,0.018,C.K.[FL][ST],3.54,9,7,7,0.25,4.11e-09,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,917,0.018,Y.Q.MN.R,5.00,3,3,3,7.72e-04,6.88e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,918,0.018,HM..R..Y.K,5.00,3,3,3,7.73e-04,6.91e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,919,0.018,K[HY].[HY].L..[HK],4.31,5,5,5,0.026,6.94e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,920,0.018,PLD.S,4.00,9,9,9,0.59,4.19e-09,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,921,0.018,C.K.F..KH,5.00,3,3,3,7.76e-04,6.99e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,921,0.018,C.K.FK..H,5.00,3,3,3,7.76e-04,6.99e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,923,0.018,S.H.N..Y..C,5.00,3,3,3,7.78e-04,7.05e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,924,0.018,KH[HK].[HY]..[DE],4.31,5,5,5,0.026,7.07e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,925,0.018,M.HR..Y.K,5.00,3,3,3,7.80e-04,7.09e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,926,0.018,Q.MN.RY,5.00,3,3,3,7.80e-04,7.12e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,927,0.018,[HK]R..H[ST]G,4.54,5,5,5,0.026,7.13e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,928,0.018,C.K.F.HK,5.00,3,3,3,7.81e-04,7.14e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,929,0.019,H.P..RTQ,5.00,4,4,4,0.007,7.21e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,930,0.019,R.H..E[KR],3.77,9,7,7,0.25,4.34e-09,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,931,0.019,C..C..R..H..S,5.00,4,3,3,7.85e-04,7.26e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,932,0.019,C.K.FKH,5.00,3,3,3,7.89e-04,7.37e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,933,0.019,P.DL..K[HR],4.77,5,5,5,0.026,7.40e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,934,0.019,H.GE..Y.C,5.00,5,3,3,7.93e-04,7.47e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,935,0.019,H.N..YS.C,5.00,3,3,3,7.93e-04,7.48e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,936,0.019,HM.H..S.C,5.00,3,3,3,7.94e-04,7.49e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,937,0.019,LDLS,4.00,10,9,9,0.60,4.50e-09,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,938,0.019,HR.L..TQ,5.00,4,4,4,0.007,7.54e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,938,0.019,H..L.RTQ,5.00,5,4,4,0.007,7.54e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,940,0.019,RI.S.W..L,5.00,3,3,3,7.96e-04,7.54e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,941,0.019,C..C..[AS]..[HR],3.54,5,5,5,0.061,4.53e-09,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,942,0.019,R..SIW..L,5.00,3,3,3,7.97e-04,7.58e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,943,0.019,G.K..QC..C,5.00,3,3,3,7.97e-04,7.59e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,944,0.020,C..CG,3.00,10,6,6,0.27,2.75e-07,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,945,0.020,L.EH.R.H,5.00,6,4,4,0.007,7.73e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,946,0.020,A..I..IW,4.00,3,3,3,0.003,4.65e-09,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,947,0.020,R.H.GE,4.00,8,6,6,0.14,4.66e-09,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,948,0.020,I.S.W.RL,5.00,3,3,3,8.04e-04,7.79e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,949,0.020,C..C..R..HS,5.00,3,3,3,8.04e-04,7.79e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,950,0.020,"Q.L.{1,2}L..K",4.00,11,10,10,0.83,4.70e-09,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,951,0.020,C..[AS][FY],2.54,14,11,11,1.66,2.82e-07,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,952,0.020,NH.YS.C,5.00,3,3,3,8.10e-04,7.94e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,953,0.020,"HK.{0,2}L..H..L",5.00,5,5,5,0.027,7.98e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,954,0.021,NH..SYC,5.00,3,3,3,8.11e-04,8.00e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,955,0.021,YS..M..R..Y,5.00,3,3,3,8.12e-04,8.01e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,956,0.021,"H.C..C.{0,1}K.{1,2}F",5.00,3,3,3,8.12e-04,8.02e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,956,0.021,"C..C.{0,1}K.{1,2}F.H",5.00,8,3,3,8.12e-04,8.02e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,958,0.021,[HR][IL]..GE[HK],4.31,8,6,6,0.069,8.05e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,959,0.021,D.P.DLS,5.00,5,5,5,0.027,8.06e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,960,0.021,C..C.K..[AS]..[GS],4.54,6,4,4,0.007,8.07e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,961,0.021,H[HK].[KR].H..[IL],4.31,5,5,5,0.027,8.08e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,962,0.021,HT..RP[FH],4.77,4,4,4,0.007,8.11e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,963,0.021,Y..H.NHR,5.00,3,3,3,8.17e-04,8.17e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,963,0.021,H.NHR..Y,5.00,3,3,3,8.17e-04,8.17e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,965,0.021,IWS..QE,5.00,3,3,3,8.17e-04,8.17e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,966,0.021,[KR].[HR].[KR].[HK]..E,4.07,7,7,7,0.14,8.19e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,967,0.021,S..M..RY.Y,5.00,3,3,3,8.19e-04,8.22e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,968,0.021,E..RIH,4.00,5,5,5,0.062,4.98e-09,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,969,0.021,"D.{1,2}RC.{0,1}K.R",5.00,4,4,4,0.007,8.30e-11,4,4,4
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,970,0.022,SIW.RL,5.00,3,3,3,8.25e-04,8.40e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,971,0.022,[ST].E[KR]P..C,4.54,7,5,5,0.027,8.50e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,972,0.022,YS..M..RY,5.00,3,3,3,8.28e-04,8.50e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,973,0.022,G.Y.Q..N..Y,5.00,3,3,3,8.30e-04,8.55e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,974,0.022,FPL.KT,5.00,4,4,4,0.007,8.60e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,975,0.022,D..LDLS,5.00,5,5,5,0.027,8.66e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,976,0.022,H.NHRY,5.00,3,3,3,8.34e-04,8.69e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,977,0.022,IWSRL,5.00,3,3,3,8.35e-04,8.73e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,978,0.023,G..Q..W.R..E,5.00,3,3,3,8.38e-04,8.81e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,979,0.023,"L.{1,2}H.RL..G",5.00,5,5,5,0.027,8.82e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,980,0.023,[AS]..[HR]..HL..H,4.54,5,5,5,0.027,8.85e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,981,0.023,P..C..C..SF,5.00,3,3,3,8.41e-04,8.90e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,982,0.023,"R.KQ.{0,2}A..R",5.00,5,5,5,0.028,9.00e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,983,0.023,AG..Q..W.R,5.00,3,3,3,8.44e-04,9.02e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,984,0.023,M..RYSY,5.00,3,3,3,8.45e-04,9.03e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,985,0.023,H..H..RI..I,5.00,3,3,3,8.46e-04,9.05e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,986,0.023,Q..W.R..E.G,5.00,3,3,3,8.49e-04,9.15e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,987,0.024,FPLRK,5.00,4,4,4,0.007,9.24e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,988,0.024,H[ST]G.KP,4.77,7,5,5,0.028,9.34e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,989,0.024,[ST]..DQP[LV],4.54,6,6,6,0.071,9.37e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,990,0.025,"E..Y.C..C.{0,1}K",5.00,5,3,3,8.66e-04,9.72e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,991,0.025,E[KR]P[FY].C,4.54,6,4,4,0.007,9.73e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,992,0.025,IQ.IW,4.00,3,3,3,0.003,5.86e-09,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,993,0.025,AGR.Q..W,5.00,3,3,3,8.68e-04,9.80e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,994,0.025,[HK][HR][HKR].[HY]..[DE],3.71,7,7,7,0.14,9.95e-11,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,995,0.026,"C.{0,2}P.C.K",4.00,5,5,5,0.064,6.04e-09,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,996,0.026,MNH..S.C,5.00,3,3,3,8.79e-04,1.02e-10,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,997,0.026,C.[KR].F..S,3.77,7,5,5,0.064,6.13e-09,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,998,0.026,F..R.T.S.P,5.00,4,4,4,0.007,1.03e-10,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,999,0.026,W.R.QE.G,5.00,3,3,3,8.82e-04,1.03e-10,1,29,29
slimfinder,CtBP-NoEFilter,FreqDisComp-5-8,l5w2o2a3,Sig,00:33:50,29,29,17505,1000,1000,0.026,Q..W.R.QE,5.00,3,3,3,8.82e-04,1.03e-10,1,29,29
slimfinder.occ.csv is too large to return (1.36 MB > 1 MB) in full output. Try http://rest.slimsuite.unsw.edu.au/retrieve&jobid=15120800036&rest=occ[&password=X].
slimfinder: 29 Seq, 29 UPC, 1000 Sig SLiMs in 4 Clouds

Cloud 1 (995 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E..[FY].C	H[ST]..[KR].[FY].C	H[ST]GEK	R..[ST]..K..QC	H[ST].E.P	H[ST]G.KP	KA.[KR][HR].H	HT..R.[FH].C	Y.[HK].G.[KR]P	HT..RP[FH]	R.H..E..[FY].C	H.R.H..E.P	H.R.H[ST].E	H.R.H.GE	R.[HR]..E.P[FHY]	L..H.R.H..E	R.H..E.P[FY]	H.R.H..E..[FY]	R.H.GE.P	R.H..E.P	H..E..[FY].C	R.[HR]..E.P	[HR].[KR].[HK].[AG]E	H.R.H..EK	[LV]..[HR].[KR].[HK]..E	H.R.H..E	R.H[ST]GE	H..E..[FY]QC	R.H.GEK	R.HT.E.P	[HR].[KR].[HK]..E[KR]	H..E..F.C..C	R.F.C..CG	R.H..E..[FY]	[FY].C.QC	H.R.HT.E	R.H..E..[FY]Q	[KR].[HK].[AG]E[KR]	K.H.R.H..E	R.H[ST].E	H..E..Y..D.C	E.PF.C..C	H..E..Y.CD	R.H..E..Y.C	R.H..E..F.C	R.[HR]..E..[FHY]	R.H..E[KR]	H.GE..Y.C	R.H.GE	HK.{0,2}L..H..L	[KR].[HR].[KR].[HK]..E	L.{1,2}H.RL..G	YC.{1,2}R	H.R.H.G..P	C.{0,1}D.{0,1}C.{1,2}R.{0,1}F	L..H.R.H[ST]	T.H.R.H[ST]	H[FLM]R.H[ST]	H.R.H[ST]G	H.R.H[ST]	H.R.H.G.K	H[KR]..[HY].[AG].[KR]	K.H.R.H[ST]	H[KR]..H.G..P	H[LM]R.HS	H.RIHS	H[KR]..H.G.[KR]	EH..IHS	R..Y.H[ST]G	[HR].[KR].[HK].[AG].[KR]	H.R.HS	E..RIHS	H[KR]..HTG	T.{1,2}K.{0,1}P..C..C	H.R..[ST]GE	L..H.R..[ST]G	L..H.R..[ST].E	HL..H.R..[ST]	EH.RI.S	[HR][IL]..GE[HK]	Y..H.N..Y..C	H.N..Y.YC	HMN..Y..C	Y..H.N..Y.Y	Y..HMN..Y	HMN..Y.Y	H.NH.Y..C	HL..H.{0,1}R.{1,2}H	H.N.RY..C	H.N.R..YC	Y..H.NH.Y	H.NH.Y.Y	QH.N..Y..C	Y..HMNH	HMNH.Y	Y..H.N.R..Y	Y..H.N.RY	H.N.RY.Y	L..H.[KR].H	H.N..Y..CK	Y.QH.N..Y	QH.N..Y.Y	Y..HMN.R	HMN.R..Y	HMN.RY	G.Y..H.N..Y	QHMN..Y	Y.QHMN	G.Y..HMN	H.N..Y.Y.K	S.H.N..Y..C	H.N..YS.C	Y..H.NHR	H.NHR..Y	H.NHRY	L..H.R.H.G	L..[HR].R[IL][HK]	HL..H.R.H	LK.[HR].R.[HK]	H[FLM]R.H	K.[HR].R[IL][HK]	L..H.R.H	H.{0,1}L..H.R.H	T.H.R.H	K.H.RIH	L..H.R[IL]H	EH.RIH	H.R.H.G	L..H.RIH	H.K.H.R.H	H.RIH	K.H.R.H.G	K.[HR].R.[HKR]	H[ILM][KR].H	L.E..RIH	L.E..R[IL]H	LK.H.R.H	L.EH.R.H	E..RIH	EH.{1,2}RI.S	E.{0,1}PN.K.R	K.{1,2}HL..H.R	H.{1,2}RI.S	K.{1,2}HL..H.{0,1}R	F.[HR]..HL..H	C..R..H.G.Y	[HK]R..H[ST]G	[AS]..[HR]..HL..H	L..H.{1,2}R.{0,1}H	HL..H.{1,2}R.{0,1}H	[HK]..HL..H.R	KH[HK].[HY]..[DE]	[HK][HR][HKR].[HY]..[DE]	L..H.{1,2}R.H	L.EH.{1,2}R.H	QC.{1,2}CG	R.{1,2}HT.E.P	L.{0,1}E.{0,1}H.{1,2}R.H	L..H[KR]..H.G	S..R..Y.H.G	H.{0,1}R.{1,2}H..E.P	R.{1,2}H..E.P	L..H.{0,1}R.{1,2}H..E	K..H.{0,1}L..H.R	HLK.H.R	H.[HY].L..[HK].[HR]	S.L..H[KR]..H	[HR]H[FILM]..H	[HR]H[FIL][KR].H	L..H..[ILM]H	[HR][HK][FILM]..H	LK.[HR]..[IL][HK]	LK.H..IH	H[HK]L..H..L	H[HK]L..H..[IL]	L..H..IH	L..H.{0,2}R.{1,2}H	K[HY].[HY].L..[HK]	H.G.Y..HM	H.G.Y.Q.M	K.{1,2}QC.{1,2}C	K.{1,2}QC.{1,2}CG	N.RY.YC	MN.R..YC	MN.RY..C	MN.RY.Y	NHRY..C	NHR..YC	NHRY.Y	MNHR..Y	MNHRY	Q..N.RY..C	Q..N.R..YC	N.R..YCK	N.RY..CK	Y.Q..N.R..Y	Y.Q..N.RY	Q..N.RY.Y	Q.MN.R..Y	Y.Q.MN.R	Q.MN.RY	[HR]H.[KR].H	TRH.R.H	H..[IL][HY]	K.H..IH	T.H[FL]R.H	H..[ILM][HY]	[FL]..R.R..Q.[MV]	K.{0,1}R.{0,1}R	H[HK].[KR].H..[IL]	[FM]..RK.[AG]..P	S.[IL]..K[MV].E	S.L..[HK]..E[HR]	R.R..Q..[AG].R	R.K.{1,2}K.A..R	R.R..Q.[MV][AG]	R..Q.[MV][AG].R	R.KQ.{0,2}A..R	R.R..Q.[MV]..R	Q[HK][MV]..R.S	R..Q.[MV]..R[KR]	R..Q.[MV]..R..[GS]	M.H.Y.YC	MN..Y.YC	M..RY.YC	H[KR]..YC	H..H.Y.YC	NH.Y.YC	HM..R..YC	M.HR..YC	HRY.YC	Q..N..Y.YC	H.Y.YCK	Q.M..R..YC	N..Y.YCK	M..R..YCK	H..HR..YC	RY.YCK	H.YSYC	M.H..SYC	N..YSYC	Y.{0,1}YC	HR..YCK	S..M..R..YC	RYSYC	M..R.SYC	H..H..SYC	YSYCK	NH..SYC	HM.H.Y..C	[HY].Q[FH][LM].[HK]	MNH.Y..C	Q.M.H.Y..C	M.HRY..C	Y..HM.H.Y	HM.H.Y.Y	MNH.Y.Y	M.H.Y..CK	Y.Q.M.H.Y	Q.M.H.Y.Y	M.HRY.Y	M.H.Y.Y.K	S..M.H.Y..C	M.H.YS.C	HM.HR..Y	Y..HM.HR	HM.HRY	Y.QHM.H	QHM.H.Y	G.Y..HM.H	Q.MNH.Y	Y.Q.MNH	S..M.H.Y.Y	YS..M.H.Y	M.H.YSY	Q.M.HR..Y	Y.Q.M.HR	Q.M.[HY]R	Q.M.HRY	G.Y.Q.M.H	M.HR..Y.K	HM.H..S.C	MNH..S.C	S.L.R[HR]K	EH.{1,2}RI	Y..H..H.Y..C	HM..RY..C	Y..H..H.Y.Y	Y.Q..N..Y..C	Q.MN..Y..C	Q.M..RY..C	Y..HM..R..Y	Y..HM..RY	HM..RY.Y	MN..Y..CK	Y.Q..N..Y.Y	QH..H.Y..C	M..RY..CK	H..HRY..C	Y.Q.MN..Y	Q.MN..Y.Y	Q..NH.Y..C	Y.Q.M..RY	H..H.Y..CK	Y..H..HR..Y	MN..Y.Y.K	Y.QH..H.Y	QH..H.Y.Y	Y..H..HRY	H..HRY.Y	NH.Y..CK	S..MN..Y..C	Q..NH.Y.Y	Y.Q..NH.Y	MN..YS.C	G.Y..H..H.Y	HRY..CK	S..M..RY..C	H..H.Y.Y.K	M..RYS.C	Y.QHM..R	QHM..RY	NH.Y.Y.K	Y..H..H..S.C	G.Y..HM..R	S.H..H.Y..C	S..MN..Y.Y	YS..MN..Y	H..H.YS.C	MN..YSY	G.Y.QHM	Q..N..Y..CK	H..[HR].[HY].Y	NH.YS.C	YS..M..RY	G.Y.Q..N..Y	Q.M..RY.Y	M..RY.Y.K	QHM..R..Y	HRY.Y.K	HM..R..Y.K	S..M..RY.Y	M..RYSY	Y.Q.M..R..Y	YS..M..R..Y	G.Y.Q.M..R	Y.Q.M..R	G..S.H..H.{0,2}R	[AG][GS]..Q.[IM]..R	GS..Q.M..R	IW.R..E..L	R.T..E.N.K	F..R.T..E.N	R.T..E.N..[LV]	F.L..T..E.N	F..R.T..E..L	T..E.N.K[LV]	C.{1,2}C.{1,2}R	[HK].GRI..[IV]	GRI..IW	GRI..[IV].S	GRI..[IV]..[KR]	GR.Q.IW	GRIQ..W	GRI.{1,2}I.{1,2}S	H.GR.Q..W	C.{1,2}CG	GRI.S.W	GR..SIW	GR.Q..W.R	H.GR..S.W	AGR.Q..W	HR.L.[HR]..S	HR.L.RT	HR.L..TQ	H..L.RTQ	F..R.T.S..N	F..RKT..E	FP.RKT	F.LRKT	F..RK..S..N	KT.S.PN	F..R.T..EP	F.LR.T..E	FP.R.T..E	F..RKT.S	FPLR.T	FP..KT..E	F..R.T.SE	F.L.KT..E	FPL.KT	FPLRK	F..R.T.S.P	V..R.{1,2}SP	H.{1,2}Y.{0,1}YC	H.{1,2}Y.{0,1}YC.{1,2}R	H..H..R.Q..W	H..H.G..Q..W	H..H..R..S.W	H.{1,2}EH.G.{0,1}R	H..H..RI..I	H.G.I..IW	HA..I..IW	RI..IW.R	G.I..IW.R	A..I..IW.R	A.RI..IW	I..IW.R.Q	H..R.Q.IW	IQ.IW.R	RIQ.IW	I..IW.R..E	AG.I..IW	H.G.IQ..W	H.G..Q.IW	G.IQ.IW	HA..IQ..W	A..IQ.IW	I..IW.RL	G.I..IW..L	A..I..IW..L	P..A..I..IW	IQ.IW..L	I.SIW.R	I..IWSR	R.Q.IW.R	RIQ..W.R	RI..[IV]..[KR]..E	G.I..IWS	G.IQ..W.R	G..Q.IW.R	IW.R.Q..G	G.I.SIW	A..I..IWS	A..I.SIW	H..R.Q..W.R	A..IQ..W.R	A.R.Q.IW	A.RIQ..W	IQ..W.R.Q	IQ.IWS	Q.IW.R.Q	IQSIW	G.I..[IV]..[KR]..E	I..[IV]..[KR]..E.G	IW.R..E.G	IQ..W.R..E	Q.IW.R..E	H.G..Q..W.R	IW.R.QE	AG.IQ..W	AG..Q.IW	HA.R.Q..W	R.Q.IW..L	IQ..W.RL	Q.IW.RL	[HK]..RI..[IV]..[KR]	R..SIW.R	IW.RLQ	HAG..Q..W	[HK].G.I..[IV].S	G.IQ..W..L	G..Q.IW..L	IW.RL.E	G.I.S.W.R	RI..[IV].S[KR]	A..IQ..W..L	A..I.S.W.R	R.Q.IWS	SIW.R.Q	IQS.W.R	IQ..WSR	P..A..IQ..W	IWSR.Q	Q.IWSR	QSIW.R	R.QSIW	A.R..SIW	[HK].G.I..[IV]..[KR]	Q.IW..LQ	Q.IW..L.E	H.G..Q..W..L	G.IQ..WS	G..Q.IWS	SIW.R..E	R.Q..W.R.Q	G.IQS.W	I..IW.R	G..QSIW	IWSR..E	P.H.G..Q..W	A..IQ..WS	G.I..[IV].S[KR]	A..IQS.W	AG.I.S.W	A.R.Q..W.R	Q.IWS..Q	R.Q..W.R..E	H.G..Q..WS	H.G..QS.W	G..Q..W.R.Q	Q..W.R.Q..G	G.I..IW	A..I..IW	SIW.RL	IWSRL	G..Q..W.R..E	AG..Q..W.R	Q..W.R..E.G	IQ.IW	Q..W.R.QE	H..RI..IW	RI..IW..L	I..IW..LQ	RI..IWS	RI.SIW	H..R..SIW	I..IW..L.E	I..IWS..Q	I..IWS.L	I.SIW..L	RI.S.W.R	IW..LQ..G	I.S.W.R.Q	H..R..S.W.R	IW..L.E.G	I.SIWS	IQ..W..L.E	I.S.W.R..E	IWS..Q..G	IW..LQE	RI..IW	R..SIW..L	I.S.W.RL	IWS..QE	W.R.QE.G	F.L..T.S..N	[ST]..D.PL..[ST]	C.{0,2}P.C.K	H..RIQ..W	H..RI.S.W	H.G.I.S.W	HA..I.S.W	[HK]..RI..[IV].S	RIQ..W..L	H..R.Q..W..L	RIQ..WS	RIQS.W	P.H..R.Q..W	A.RI.S.W	H..R.Q..WS	H..R.QS.W	K.K.K.[GS].[IV]	HA.R..S.W	RI.S.W..L	IQ..W..LQ	IQ..WS..Q	HRP..RT	H.P..RTQ	D.P[IL]DL	P[IL]DLS	P.DLS	P[ILMV][DE]L	QPL.[LV][ST]	D.PLDL	PLDLS	P[IL]D.[ST]	[ILM]DL[GS]	PLDL	P.[DE]L[ST]	P[ILMV].[LV][ST]	D.PL.L[ST]	QPL.L..K	P[IL].L[ST].[KR]	D.P.DL	P[IL]D.S	[DE].P[ILMV].L	[DE].P.[DE]L	QP[LV].[LV]	D..[IL]DL	[ILM]D[LV][ST]	P[ILMV].[LV][AS]	PLD.S	LDLS	D.P.DLS	D..LDLS	[ST]..DQP[LV]	Q..P[LMV]DL	P.DLS.{1,2}K	Q..P.DL.[LMV]	P.DL	Q..P.DL[ST]	P.DL..K.{0,2}R	P.DL[ST].K	P[IL]DL..[KR]	[DE].P.DL..[KR]	P.DL..[KR]	P.DL[ST]..[KR]	Q..P.DL	[IL]DLS.K	P.DL..K	P.DL..K[HR]	Q.L.{1,2}L..K	A..S..V[HK]..L	L..L.{1,2}N..K.K	A..S..V..[KR]L	Q.{0,2}P.DLS	A[IV].S..VK	(p = 0.00e+00)
29 UPC	29 Seq:	CBX4_HUMAN__O00257	COM1_HUMAN__Q99708	E1A_ADE02__P03254	ELK3_HUMAN__P41970	EVI1_HUMAN__Q03112	FOG1_HUMAN__Q8IX07	FOG2_HUMAN__Q8WW38	HAIR_DROME__P14003	HDAC4_HUMAN__P56524	HDAC5_HUMAN__Q9UQL6	HDAC7_MOUSE__Q8C2B3	HDAC9_MOUSE__Q99N13	HIC1_HUMAN__Q14526	IKZF1_HUMAN__Q13422	IKZF4_HUMAN__Q9H2S9	KLF3_HUMAN__P57682	KLF8_HUMAN__O95600	KNIR_DROME__P10734	LCOR_HUMAN__Q96JN0	NRIP1_HUMAN__P48552	SOX6_HUMAN__P35712	T7L1A_XENLA__P70062	TGIF1_HUMAN__Q15583	TRPS1_HUMAN__Q9UHF7	TTKB_DROME__P17789	ZEB1_HUMAN__P37275	ZEB2_HUMAN__O60315	ZFH1_DROME__P28166	cbx4_XENLA__Q91647

SLiMMaker Consensus: 
- Unable to make a SLiM with these settings and peptides

CGICKKAFKHKHHLIEHMRLHSGEKPYQCDKCGKRFSHSGSYSQHMNHRYSYCKRE
CQICKKAFKHKHHLIEHSRLHSGEKPYQCDKCGKRFSHSGSYSQHMNHRYSYCKRE
CIECPKAFKHKHHLTEHKRLHSGEKPFQCSKCLKRFSHSGSYSQHMNHRYSYCKPY
CDLCDKIFQKSSSLLRHKYEHTGKRPHECGICKKAFKHKHHLIEHMRLHSGEKPYQ
CDLCDKTFQKSSSLLRHKYEHTGKRPHQCQICKKAFKHKHHLIEHSRLHSGEKPYQ
CDQCDKAFAKQSSLARHKYEHSGQRPYQCIECPKAFKHKHHLTEHKRLHSGEKPFQ
WEGCTWKFARSDELTRHFRKHTGIKPFQCPDCDRSFSRSDHLALHRKRHMLV
WDGCSWKFARSDELTRHFRKHTGIKPFRCTDCNRSFSRSDHLSLHRRRHDTM
PVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLR
MKSPPDQPVKHLFTTGVVYDTFMLKHQCMCGNTHVHPEHAGRIQSIWSRLQETGLL
TCQTQVLNSSETPATGLVYDSVMLKHQCSCGDNSKHPEHAGRIQSIWSRLQERGLR
CDICGIICIGPNVLMVHKRSHTGERPFQCNQCGASFTQKGNLLRHIKLHSGEKPFK
CTECGKAFKYKHHLKEHLRIHSGEKPYECPNCKKRFSHSGSYSSHISSKKCISLIP
CTECGKAFKYKHHLKEHLRIHSGEKPYECPNCKKRFSHSGSYSSHISSKKCIGLIS
TWKFARSDELTRHFRKHTGIKPFQCPDCDRSFSRSDHLALHRKRHMLV
SWKFARSDELTRHFRKHTGIKPFRCTDCNRSFSRSDHLSLHRRRHDTM
----------MRHIICHGGVITEEMAASLLDQLIEEVLADNLPPPSHFEPPTLHEL
GASFTQKGNLLRHIKLHSGEKPFKCHLCNYACRRRDALTGHLRTHSVGKPHKCGYC
GASFTQKGNLLRHIKLHSGEKPFKCPFCNYACRRRDALTGHLRTHSVSSPTVGKPY
GKKFTQRGTMTRHMRSHLGLKPFACDACGMRFTRQYRLTEHMRIHSGEKPYECQVC
SYTFAYRTQLERHMTSHKSGRDQRHVTQSGCNRKFKCTECGKAFKYKHHLKEHLRI
SYTFAYRTQLERHMVTHKPGTDQHQMLTQGAGNRKFKCTECGKAFKYKHHLKEHLR
CKECDKAFKFKHHLKEHVRIHSGEKPFGCDNCGKRFSHSGSFSSHMTSKKCISMGL
SVPSMFNFRAPPNALPENLLRKGKERYTCRYCGKIFPRSANLTRHLRTHTGEQPYR
CTICGKKFTQRGTMTRHMRSHLGLKPFACDACGMRFTRQYRLTEHMRIHSGEKPYE
SVIVQPGKRPLPVESPDTQRKRRIHRCDYDGCNKVYTKSSHLKAHRRTHTGEKPYK
LQQEPAAMAQMQGEESLDLKRRRIHQCDFAGCSKVYTKSSHLKAHRRIHTGEKPYK
QLERHMTSHKSGRDQRHVTQSGCNRKFKCTECGKAFKYKHHLKEHLRIHSGEKPYE
LERHMVTHKPGTDQHQMLTQGAGNRKFKCTECGKAFKYKHHLKEHLRIHSGEKPYE
YDGCNKVYTKSSHLKAHRRTHTGEKPYKCTWEGCTWKFARSDELTRHFRKHTGIKP
FAGCSKVYTKSSHLKAHRRIHTGEKPYKCTWDGCSWKFARSDELTRHFRKHTGIKP
TSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVT
PSYKLPLPGPYDSRDDFPLRKTASEPNLKVRSRLKQKVAERRSSPLLRRKDGTVIS
PSYKYTLPGAQDSKDDFPLRKTASEPNLKVRSRLKQKVAERRSSPLLRRKDGNLVT
SFLPPVPSLPTEPPEHFPLRKTVSEPNLKLRYKPKKSLERRKNPLLRKESAPPSLR
DACGMRFTRQYRLTEHMRIHSGEKPYECQVCGGKFAQQRNLISHMKMHAVGGAAGA
TECGKAFKYKHHLKEHLRIHSGEKPYECPNCKKRFSHSGSYSSHISSKKCISLIPV
TECGKAFKYKHHLKEHLRIHSGEKPYECPNCKKRFSHSGSYSSHISSKKCIGLISV
KECDKAFKFKHHLKEHVRIHSGEKPFGCDNCGKRFSHSGSFSSHMTSKKCISMGLK
LKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEA
LKHQCSCGDNSKHPEHAGRIQSIWSRLQERGLRSQCECLRGRKASLEELQSVHSER
APKEAVTGNGIGGKMKIVKNKNKNGRIVIVMSKYMENGMQAVKIKSGEVAEGEARS
SPSTELPSSGVGGKMKIVKNKNKNGRIVIVMSKYMENGMQSVKIKSSEEDCDMGDV
QEELEKQRLEQQLLILRNKEKSKESAIASTEVKLRLQEFLLSKSKEPTPGGLNHSL
LDLSLPKQMKEPKSIIATKNKTKASSISLDHNSVSSSSENSDEPLNLTFIKKEFSN
EQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCI
MPELQGGQQEQELRQLLNKDKSKRSAVASSVVKQKLAEVILKKQQAALERTVHPSS
SGSGPGLAPARSPGPAADGPIDLSKKPRRPLPGAPAPALADYHECTACRVSFHSLE
NPSFTDDSSGDESSYSNCVPIDLSCKHRTEKSESDQPVSLDNFTQSLLNTWDPKVP
GGRRQAVECIEDLLNESGQPLDLSCKRPRP
YPTFNLPPHFSAVGSDNDIPLDLAIKHSRPGPTANGASKEKTKAPPNVKNEGPLNV
GAAPPMPIDSQASLTREDQPLDLSVKRDPLTPKSESSPPYIAPPSGEALNPEAINL
FPFPMDNQFSMNGDCVMDKPLDLSDRFSAIQRQEKSQGSETSKNKFRQVTLYEALK
AATTQNPVLSKLLMADQDSPLDLTVRKSQSEPSEQDGVLDLSTKKSPCAGSTSLSH
MEPQSPGEVKKLQKGSSESPFDLTTKRKDEKPLTPVPSKPPVTPATSQDQPLDLSM
GETTSVVPVHPPTVSAQEGPMDLSMKTSRSSVHSFNDSGSEDQEVEVAPRRKFYQL
QNLKKENPVATNSCKSEKLPEDLTVKSEKDKSFEGGVNDSTCLLCDDCPGDINALP
CRYCGKIFPRSANLTRHLRTHTGEQPYRCKYCDRSFSISSNLQRHVRNIHNKEKPF
CDVCGMVCIGPNVLMVHKRSHTGERPFHCNQCGASFTQKGNLLRHIKLHSGEKPFK
NTQGYLYTAEGAQEEPQVEPLDLSLPKQQGELLERSTITSVYQNSVYSVQEEPLNL
SHSSSYTPNSFSSEELQAEPLDLSLPKQMKEPKSIIATKNKTKASSISLDHNSVSS
PLTPVPSKPPVTPATSQDQPLDLSMGSRSRASGTKLTEPRKNHVFGGKKGSNVESR
SPGAGCPALQPDTPGSQPQPMDLRVGQRPTVEPPPEPALLTLQHPQRLHRHLFLAG
LPEKFFQTPEGLSHGIQMEPVDLTVNKRSSPPSAGNSPSSLKFPSSHRRASPGLSM
CDQCPKAFNWKSNLIRHQMSHDSGKHYECENCAKVFTDPSNLQRHIRSQHVGARAH
CHLCNYACRRRDALTGHLRTHSVGKPHKCGYCGRSYKQRSSLEEHKERCHNYLESM
YACRRRDALTGHLRTHSVSSPTVGKPYKCNYCGRSYKQQSTLEEHKERCHNYLQSL
GPGPAAALCASERRCSPLCGLDLSKKSPPGSAAPERPLAERELPPRPDSPPSAGPA
SPLDLTVRKSQSEPSEQDGVLDLSTKKSPCAGSTSLSHSPGCSSTQGNGRPGRPSQ
DYDGCNKVYTKSSHLKAHRRTHTGEKPYKCTWEGCTWKFARSDELTRHFRKHTGIK
DFAGCSKVYTKSSHLKAHRRIHTGEKPYKCTWDGCSWKFARSDELTRHFRKHTGIK
ENCAKVFTDPSNLQRHIRSQHVGARAHACPECGKTFATSSGLKQHKHIHSSVKPFI
CKECDQVFPDLQSLEKHMLSHTEEREYKCDQCPKAFNWKSNLIRHQMSHDSGKHYE
GLGPPFGGGGDKVAGAPGGLGELLRPYRCASCDKSYKDPATLRQHEKTHWLTRPYP
CDACGMRFTRQYRLTEHMRIHSGEKPYECQVCGGKFAQQRNLISHMKMHAVGGAAG
ENILDPRLLIAFQNRERQEQLMGYRKRGPKPKPLVVQVPTFARRSNVLTGLQDSST
ENILDPRLLVAFQNRERQEQIMGYRKRGPKPKNNLVSMPSFARRSNVLSGLHDSSG
FPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSS
FPLRKTASEPNLKVRSRLKQKVAERRSSPLLRRKDGTVISTFKKRAVEITGAGPGA
FPLRKTASEPNLKVRSRLKQKVAERRSSPLLRRKDGNLVTSFKKRVFEVAESSVSS
FTGSVPNIPTEMLPQHRALPLDSSPNQFSLYTSPSLPNISLGLQATVTVTNSHLTA
KGIVAASGSETEDEDSMDIPLDLSSSAGSGKRRRRGNLPKESVQILRDWLYEHRYN
KITVKAGDDTPVGYSVPIKPLDSSRQNGTEATSYYWCKFCSFSCESSSSLKLLEHY
VSNVEDQNDSDSTPPKKKMRKTENGMYACDLCDKIFQKSSSLLRHKYEHTGKRPHE
AGVLMPPKPRRGKAETHGHAGDPDLPYVCDQCDKAFAKQSSLARHKYEHSGQRPYQ
RPLPVESPDTQRKRRIHRCDYDGCNKVYTKSSHLKAHRRTHTGEKPYKCTWEGCTW
AQMQGEESLDLKRRRIHQCDFAGCSKVYTKSSHLKAHRRIHTGEKPYKCTWDGCSW
LNSKKHHQYQPHSKERAGKPPPPGKSGKYYYQLNSKKHHPYQPDPKMYDLQYQGGH
QLNSKKHHQYQPSGKDHNEKHHSSNKKKYYYQLNSKKHHHYQPDPKLYEQYTIEKE
RKGRVEYLVKWRGWSPKYNTWEPEENILDPRLLIAFQNRERQEQLMGYRKRGPKPK
RKGRVEYLVKWRGWSSKYNTWEPEENILDPRLLVAFQNRERQEQIMGYRKRGPKPK
KESPPVSDTPDEGDEPMPIPEDLSTTSGGQQSSKSDRVVASNVKVETQSDEENGRA
KIEPPEELLASDFSLPQVEPVDLSFHKPKAPLQPASMLQAPIRPPKPQSSPQTLVV
AAANLAGQPLGVSGASTPPPPDLSGQNSNQSLPATSNALSTSSSSSTSSSSGSLGP
PGHLSPEIDPKTGIPRPPHPSELSPYYPLSPGAVGQIPHPLGWLVPPQGQPMYSIP
VSIEEYLQRSDTAIIYPEAPEELSRLGTPEANGQEENDLPPGTPDAFAQLLTCPYC
-----------------------MHSPGAGCPALQPDTPGSQPQPMDLRVGQRPTV
CASCDKSYKDPATLRQHEKTHWLTRPYPCTICGKKFTQRGTMTRHMRSHLGLKPFA
EDVIPDSPITAFSFSGVNRLRRKENPHVRYIEQTHTKLEHSVCANEMRKVSKSSTH
VKDQKPDTNLPDVTKNLIRDRFAESPHHVGQSGTKVMSEPLSCAARLQAVASMVEK
RKFKCTECGKAFKYKHHLKEHLRIHSGEKPYECPNCKKRFSHSGSYSSHISSKKCI
RKFKCTECGKAFKYKHHLKEHLRIHSGEKPYECPNCKKRFSHSGSYSSHISSKKCI
CHLCDRCFGQQTNLDRHLKKHENGNMSGTATSSPHSELESTGAILDDKEDAYFTEI
CNQCGASFTQKGNLLRHIKLHSGEKPFKCHLCNYACRRRDALTGHLRTHSVGKPHK
CNQCGASFTQKGNLLRHIKLHSGEKPFKCPFCNYACRRRDALTGHLRTHSVSSPTV
DDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSAC
DDFPLRKTASEPNLKVRSRLKQKVAERRSSPLLRRKDGTVISTFKKRAVEITGAGP
DDFPLRKTASEPNLKVRSRLKQKVAERRSSPLLRRKDGNLVTSFKKRVFEVAESSV
FPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGL
GMKSPPDQPVKHLFTTGVVYDTFMLKHQCMCGNTHVHPEHAGRIQSIWSRLQETGL
PTCQTQVLNSSETPATGLVYDSVMLKHQCSCGDNSKHPEHAGRIQSIWSRLQERGL
LKHQCMCGNTHVHPEHAGRIQSIWSRLQETGLLSKCERIRGRKATLDEIQTVHSEY
QRQREQQRQEELEKQRLEQQLLILRNKEKSKESAIASTEVKLRLQEFLLSKSKEPT
MNASMSSLVSSRFSPHMVPPPHHSLHTSGIPHPAIVSPIVKQEPSSGNISPNLHTK
RKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALA
QKLEQQRQEQEVERHRREQQLPPLRGKDRGRERAVASTEVKQKLQEFLLSKSATKD
MRLSMDPPMPELQGGQQEQELRQLLNKDKSKRSAVASSVVKQKLAEVILKKQQAAL
YDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVT
YDSRDDFPLRKTASEPNLKVRSRLKQKVAERRSSPLLRRKDGTVISTFKKRAVEIT
QDSKDDFPLRKTASEPNLKVRSRLKQKVAERRSSPLLRRKDGNLVTSFKKRVFEVA
------MKSEDYPHETMAPDIHEERQYRCEDCDQLFESKAELADHQKFPCSTPHSA
PQDAGSRKLSPTKEAFGEQPLQLTTKPDLLAWDPARNTHPPSHHPHPHPHHHHHHH
YEPMDIKPSVIQRVPMEQQPLSLVIKKQIKEEEQPWRPW
SAALASPAAPAATHSEQAQPLSLTTKPEARAQLSLSHSAAFLASKSPSSSSFSGHL
HLAGLRRTYSTASETLNDQPLQLTTKSSHVPMPNRTRSPVYAGEPYNDLVYTNPRK
EDRVAGVVSLPQGPPPQPPPTIVVGRHSPAYAKEDPKPQEGLLRGTPGPSKEVLRV
EKFFQTPEGLSHGIQMEPVDLTVNKRSSPPSAGNSPSSLKFPSSHRRASPGLSMPS
SGTKVMSEPLSCAARLQAVASMVEKRASPATSPKPSVACSQLALLLSSEAHLQQYS
IPPGGFRHPYPALAMNASMSSLVSSRFSPHMVPPPHHSLHTSGIPHPAIVSPIVKQ
EAEERDSTEQEEAGPEILSNEHVGARASPSQGDSDERESLTREEDEDSEKEEEEED
QRRIRARLSLATGLSWGPFHGSVQTRASSPRQAEPSPALTLLLVDEACWLRTLPQA
DFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACS
DFPLRKTASEPNLKVRSRLKQKVAERRSSPLLRRKDGTVISTFKKRAVEITGAGPG
DFPLRKTASEPNLKVRSRLKQKVAERRSSPLLRRKDGNLVTSFKKRVFEVAESSVS
YMENGMQSVKIKSSEEDCDMGDVRRRFDSPGTLNGDKTCTAQEEKTEHWKKRVESR
APGKGSEKGPPNGMMPAPKEAVTGNGIGGKMKIVKNKNKNGRIVIVMSKYMENGMQ
SPSTEMSSSPSTELSSSPSTELPSSGVGGKMKIVKNKNKNGRIVIVMSKYMENGMQ
HLCNYACRRRDALTGHLRTHSVGKPHKCGYCGRSYKQRSSLEEHKERCHNYLESMG
ACRRRDALTGHLRTHSVSSPTVGKPYKCNYCGRSYKQQSTLEEHKERCHNYLQSLS
EGCTWKFARSDELTRHFRKHTGIKPFQCPDCDRSFSRSDHLALHRKRHMLV
DGCSWKFARSDELTRHFRKHTGIKPFRCTDCNRSFSRSDHLSLHRRRHDTM
GICKKAFKHKHHLIEHMRLHSGEKPYQCDKCGKRFSHSGSYSQHMNHRYSYCKREA
QICKKAFKHKHHLIEHSRLHSGEKPYQCDKCGKRFSHSGSYSQHMNHRYSYCKREA
IECPKAFKHKHHLTEHKRLHSGEKPFQCSKCLKRFSHSGSYSQHMNHRYSYCKPYR
--------MADGPRCKRRKQANPRRNNVTNYNTVVETNSDSDDEDKLHIVEEESVT
---MKQPIMADGPRCKRRKQANPRRKNVVNYDNVVDTGSETDEEDKLHIAEDDGIA
LLPPQLPGSNSSVGSNSAYDLDLSAPRSTSSPGSTTGDLSGAYPCMQCTASFASRE
CPFCNYACRRRDALTGHLRTHSVSSPTVGKPYKCNYCGRSYKQQSTLEEHKERCHN
PLPVESPDTQRKRRIHRCDYDGCNKVYTKSSHLKAHRRTHTGEKPYKCTWEGCTWK
QMQGEESLDLKRRRIHQCDFAGCSKVYTKSSHLKAHRRIHTGEKPYKCTWDGCSWK
TARSISTPTCLGGSPAAERPADLPPAAALPQPEVILLDSDLDEPIDLRCVKTRSEA
PAAALPQPEVILLDSDLDEPIDLRCVKTRSEAGEPPSSLQVKPETPASAAVAVAAA
PSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQI
MISSVDVKSEVPMGLEPISPLDLRTDLRMMMPVVDPVVREKQLQQELLLIQQQQQI
MQPLPGRLELPGSREAGEGPEDLADGGPLLYRPRGPLTDPGASPSNGCQDSTDTES
PKMALQAKQDGKKDVSHSSPVDLKIPQVRGMDLSWESRTGDQYSYSSLVMGSQTES
KNHNSANKMSPMCSPGSLTPGDLFAQLQHPPPQLPPHLHAQFMAAAASLAMQSART
GMYACDLCDKIFQKSSSLLRHKYEHTGKRPHECGICKKAFKHKHHLIEHMRLHSGE
GMYACDLCDKTFQKSSSLLRHKYEHTGKRPHQCQICKKAFKHKHHLIEHSRLHSGE
LPYVCDQCDKAFAKQSSLARHKYEHSGQRPYQCIECPKAFKHKHHLTEHKRLHSGE
KMSVSKAQSIYGIPHSTLEYKVKERLGTLKNPPKKKMKLMRSEGPDVSVKIELDPQ
RLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSV
RLKQKVAERRSSPLLRRKDGTVISTFKKRAVEITGAGPGASSVCNSAPGSGPSSPN
RLKQKVAERRSSPLLRRKDGNLVTSFKKRVFEVAESSVSSSSPGSGPSSPNNGPAG
EQEPLNVAEERQTPVEEHAPVEHAADLRCSRCSKQFNHPTELVQHEKVLCGLIKEE
SGEKPYQCDKCGKRFSHSGSYSQHMNHRYSYCKREAEERDSTEQEEAGPEILSNEH
SGEKPYQCDKCGKRFSHSGSYSQHMNHRYSYCKREAEEREAAEREAREKGHLEPTE
SGEKPFQCSKCLKRFSHSGSYSQHMNHRYSYCKPYRE
VSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPV
TPPSYKLPLPGPYDSRDDFPLRKTASEPNLKVRSRLKQKVAERRSSPLLRRKDGTV
TSPSYKYTLPGAQDSKDDFPLRKTASEPNLKVRSRLKQKVAERRSSPLLRRKDGNL
LSSFLPPVPSLPTEPPEHFPLRKTVSEPNLKLRYKPKKSLERRKNPLLRKESAPPS
DGCNKVYTKSSHLKAHRRTHTGEKPYKCTWEGCTWKFARSDELTRHFRKHTGIKPF
AGCSKVYTKSSHLKAHRRIHTGEKPYKCTWDGCSWKFARSDELTRHFRKHTGIKPF
CGYCGRSYKQRSSLEEHKERCHNYLESMGLPGTLYPVIKEETNHSEMAEDLCKIGS
CNYCGRSYKQQSTLEEHKERCHNYLQSLSTEAQALAGQPGDEIRDLEMVPDSMLHS
KCTECGKAFKYKHHLKEHLRIHSGEKPYECPNCKKRFSHSGSYSSHISSKKCISLI
KCTECGKAFKYKHHLKEHLRIHSGEKPYECPNCKKRFSHSGSYSSHISSKKCIGLI
KPYQCDKCGKRFSHSGSYSQHMNHRYSYCKREAEERDSTEQEEAGPEILSNEHVGA
KPYQCDKCGKRFSHSGSYSQHMNHRYSYCKREAEEREAAEREAREKGHLEPTELLM
KPFQCSKCLKRFSHSGSYSQHMNHRYSYCKPYRE
QSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIW
PVSLLSPEPTCQTQVLNSSETPATGLVYDSVMLKHQCSCGDNSKHPEHAGRIQSIW
MSGLDDMTDSDSCLSRKKIKKTESGMYACDLCDKTFQKSSSLLRHKYEHTGKRPHQ
APPASEILAKMSELVHSRLQQGAGAGAGGAQTGLFPGAPKGATCFECEITFSNVNN
VPQASEILAKMSELVHRRLRHGSSSYPPVIYSPLMPKGATCFECNITFNNLDNYLV
GAGGRGSEGSQSPGSSVDDAEDDPSRTLCEACNIRFSRHETYTVHKRYYCASRHDP
KKEKLRTLIDLVTDDKMIENHNISTPFSCQFCKESFPGPIPLHQHERYLCKMNEEI
SAYDLDLSAPRSTSSPGSTTGDLSGAYPCMQCTASFASREQLEQHEQLHSPCGPAA
KHSNPGSSGIQDAHPNQPGAAADAFLVKCTQCHKRFPEYQSLSEHIASEHPHDKLN
CKKAFKHKHHLIEHMRLHSGEKPYQCDKCGKRFSHSGSYSQHMNHRYSYCKREAEE
CKKAFKHKHHLIEHSRLHSGEKPYQCDKCGKRFSHSGSYSQHMNHRYSYCKREAEE
DKINGKPVDVKNPSVPLVDGESDPNKTTCEACNITFSRHETYMVHKQYYCATRHDP
GADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQ
RISPGIRGTHKLPRHRPLNRTQSAPLPQSTLAQLVIQQQHQQFLEKQKQYQQQIHM
FPQCTKSFSNARALEMHLNSHSGVKMEEFLPPGASLKCTVCSYTADSVINFHQHLF
CPECGKTFATSSGLKQHKHIHSSVKPFICEVCHKSYTQFSNLCRHKRMHADCRTQI
LVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQ
GERVATSMRTVGKLPRHRPLSRTQSSPLPQSPQALQQLVMQQQHQQFLEKQKQQQL
KERISPGIRGTHKLPRHRPLNRTQSAPLPQSTLAQLVIQQQHQQFLEKQKQYQQQI
FAQPLLTTERLSGSGLHRPLNRTRSEPLPPSATASPLLAPLQPRQDRLKPHVQLIK
QGSPGDSVLIPLAQVGHRPLSRTQSSPAAPVSLLSPEPTCQTQVLNSSETPATGLV
YSSHISSKKCISLIPVNGRPRTGLKTSQCSSPSLSASPGSPTRPQIRQKIENKPLQ
CPDCDRSFSRSDHLALHRKRHMLV
CTDCNRSFSRSDHLSLHRRRHDTM
LFPGAPKGATCFECEITFSNVNNYYVHKRLYCSGRRAPEDAPAARRPKAPPGPARA
DAEDDPSRTLCEACNIRFSRHETYTVHKRYYCASRHDPPPRRPAAPPGPPGPAAPP
DGESDPNKTTCEACNITFSRHETYMVHKQYYCATRHDPPLKRSASNKVPAMQRTMR
SLGAVLAAASYLQIPDLVALCKKRLKRHGKYCHLRGGGGGGGGYAPYGRPGRGLRA
LLTSSKAGSPINLSQHSLVIKWNSPPYVCSTQSEKLTNTASNHSMDLTKSKDPPGE
CPKAFKHKHHLTEHKRLHSGEKPFQCSKCLKRFSHSGSYSQHMNHRYSYCKPYRE
DTQSEKPGQPGVETDDWDGPGELEVFQKDGERKIQSRQQLPVGTTWGPFPGKMDLN
----MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLR
LDANPMENPALFNDIKIEPPEELLASDFSLPQVEPVDLSFHKPKAPLQPASMLQAP
PSNLQRHIRSQHVGARAHACPECGKTFATSSGLKQHKHIHSSVKPFICEVCHKSYT
KSGRDQRHVTQSGCNRKFKCTECGKAFKYKHHLKEHLRIHSGEKPYECPNCKKRFS
PGTDQHQMLTQGAGNRKFKCTECGKAFKYKHHLKEHLRIHSGEKPYECPNCKKRFS
RLQRHMISHDESALLRKFKCKECDKAFKFKHHLKEHVRIHSGEKPFGCDNCGKRFS
QQEFENIRQQNLKLITELMNERNTLQEENKKLSEQLQQKIENDQQHQAAELECEED
GAPGKGSEKGPPNGMMPAPKEAVTGNGIGGKMKIVKNKNKNGRIVIVMSKYMENGM
SSPSTEMSSSPSTELSSSPSTELPSSGVGGKMKIVKNKNKNGRIVIVMSKYMENGM
LYPSWSARDNYGKRKKRKREKQSPEMETHTKTKKMCVQHLPADKSCDSPASSHGSM
ERHRREQQLPPLRGKDRGRERAVASTEVKQKLQEFLLSKSATKDTPTNGKNHSVGR
TSDQEGDPGSKQPRKKRGRYRQYNSEILEEAISVVMSGKMSVSKAQSIYGIPHSTL
SAFSMVEEDFQQKLESENDLQEIHTIQECKECDQVFPDLQSLEKHMLSHTEEREYK
QASDVKQEANHLQGSDGQQSVKESKEHSCTKCDFITQVEEEISRHYRRAHSCYKCR
GSDQHVASHLPLHPIMHNKPHSEELPTLVSTIQQDADWDSVLSSQQRMESENNKLC
PSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASAT
GSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGT
GDNSKHPEHAGRIQSIWSRLQERGLRSQCECLRGRKASLEELQSVHSERHVLLYGT
CNHCHFGFQTQRELLQHQELHVPSGKLPRESDMEHSPSATEDSLQPATDLLTRSEL
CMQCTASFASREQLEQHEQLHSPCGPAAVSNVSQTCRICHKAFANVYRLQRHMISH
CQVCGGKFAQQRNLISHMKMHAVGGAAGAAGALAGLGGLPGVPGPDGKGKLDFPEG
EKEEGSDQHVASHLPLHPIMHNKPHSEELPTLVSTIQQDADWDSVLSSQQRMESEN
LGAQGKGQGHQYELNSKKHHQYQPHSKERAGKPPPPGKSGKYYYQLNSKKHHPYQP
LDLGPIPKSHQYQLNSKKHHQYQPSGKDHNEKHHSSNKKKYYYQLNSKKHHHYQPD
PPPPGKSGKYYYQLNSKKHHPYQPDPKMYDLQYQGGHKEAPSPTCPDLGAKSHPPD
KHHSSNKKKYYYQLNSKKHHHYQPDPKLYEQYTIEKESQISTDVRNRHRDSLTHTQ
YCSGRQREAAPVSEENEDSAHQISSLCPFPQCTKSFSNARALEMHLNSHSGVKMEE
SGSSNGTGNDYDDFDRENMMNDSSDLGNGKMCNESYSGNDDGSDDNQPNAGHTDDL
QRGTMTRHMRSHLGLKPFACDACGMRFTRQYRLTEHMRIHSGEKPYECQVCGGKFA
SVINFHQHLFSHLTQAAFRCNHCHFGFQTQRELLQHQELHVPSGKLPRESDMEHSP
GPNVLMVHKRSHTGERPFQCNQCGASFTQKGNLLRHIKLHSGEKPFKCHLCNYACR
GPNVLMVHKRSHTGERPFHCNQCGASFTQKGNLLRHIKLHSGEKPFKCPFCNYACR
WKFARSDELTRHFRKHTGIKPFQCPDCDRSFSRSDHLALHRKRHMLV
WKFARSDELTRHFRKHTGIKPFRCTDCNRSFSRSDHLSLHRRRHDTM
QATSPFACAADGEDAMTQDLTSREKEEGSDQHVASHLPLHPIMHNKPHSEELPTLV
KSSSLLRHKYEHTGKRPHECGICKKAFKHKHHLIEHMRLHSGEKPYQCDKCGKRFS
KSSSLLRHKYEHTGKRPHQCQICKKAFKHKHHLIEHSRLHSGEKPYQCDKCGKRFS
PRSTSSPGSTTGDLSGAYPCMQCTASFASREQLEQHEQLHSPCGPAAVSNVSQTCR
KQSSLARHKYEHSGQRPYQCIECPKAFKHKHHLTEHKRLHSGEKPFQCSKCLKRFS
SLLLQDSDCKASPEGREAHKHGLAALRSTSRNEYIHSGLYSSFTINSLQNPPDAFK
SIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLL
SIWSRLQETGLLSKCERIRGRKATLDEIQTVHSEYHTLLYGTSPLNRQKLDSKKLL
SIWSRLQERGLRSQCECLRGRKASLEELQSVHSERHVLLYGTNPLSRLKLDNGKLT
KESAAINQILGRRWHSLSREEQAKYYELARKERQLHSQLYPSWSARDNYGKRKKRK
SITSPSIAELHNSVTNCDPPLRLTKPSHFTNIKPVEKLDHSRSNTPSPLNLSSTSS
SSISLDHNSVSSSSENSDEPLNLTFIKKEFSNSNNLDNKSTNPVFSMNPFSAKPLY
ATQDILKALSKHPSVGDNKPVELQPERSSEERPFEKISDQSESSDLDDVSTPSGSD
VLPRAMPSSMGGGGGGSPSPVELRGALVGSVDPTLREQQLQQELLALKQQQQLQKQ
TDCNRSFSRSDHLSLHRRRHDTM
EQPEQRALGPVSMPNLVPEVIDLTCHEAGFPPSDDEDEEGEEFVLDYVEHPGHGCR
NLGPQLTGKSNEDGKLGPGVIDLTRPEDAEGSKAMNGSAAKLQQYYCWPTGGATVA
ADNLPPPSHFEPPTLHELYDLDVTAPEDPNEEAVSQIFPDSVMLAVQEGIDLLTFP
SSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAV
GKKDVSHSSPVDLKIPQVRGMDLSWESRTGDQYSYSSLVMGSQTESALSKKLRAIL
CVPIDLSCKHRTEKSESDQPVSLDNFTQSLLNTWDPKVPDVDIKEDQDTSKNSKLN
LPPRPDSPPSAGPAAYKEPPLALPSLPPLPFQKLEEAAPPSDPFRGGSGSPGPEPP
ERSTITSVYQNSVYSVQEEPLNLSCAKKEPQKDSCVTDSEPVVNVIPPSANPINIA
-----MHSMISSVDVKSEVPMGLEPISPLDLRTDLRMMMPVVDPVVREKQLQQELL
NRTTPVSTPPLLTSSKAGSPINLSQHSLVIKWNSPPYVCSTQSEKLTNTASNHSMD
YKKLFSDAQPLQPLQVYQAPLSLATVPHQALGRTQSSPAAPGGMKSPPDQPVKHLF
PSERCEERGGDAAVSPGGPPLGLAPPPRYPGSLDGPGAGGDGDDYKSSSEETGSSE
SEHRSLFLEAACHDSDSLEPLNLSSGSKTKSPSLPPKAKKPKGLEISAPPLVLSGT
SPSLPPKAKKPKGLEISAPPLVLSGTDIGSIALNSPALPSGSLTPAFFTAQTPNGL
NEKRGTSPVTQVKDEAAAQPLNLSSRPKTAEPVKSPTSPTQNLFPASKTSPVNLPN
VLPVGSTTNGSRSSTPSPSPLNLSSSRNTQGYLYTAEGAQEEPQVEPLDLSLPKQQ
FTNIKPVEKLDHSRSNTPSPLNLSSTSSKNSHSSSYTPNSFSSEELQAEPLDLSLP
LNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQEL
SPDPESYRSSSQAIKQEQEPLNVAEERQTPVEEHAPVEHAADLRCSRCSKQFNHPT
IQPVVVQPVPFMYTSHLQQPLMVSLSEEMENSSSSMQVPVIESYEKPISQKKIKIE
IENPSTALATVAAANLAGQPLGVSGASTPPPPDLSGQNSNQSLPATSNALSTSSSS
RLHRHLFLAGLHQQQRSAEPMRLSMDPPMPELQGGQQEQELRQLLNKDKSKRSAVA
TLLNGHMPVPIPSLDRAASPVLLSSNSQKS
----MLMFDPVPVKQEAMDPVSVSYPSNYMESMKPNKYGVIYSTPLPEKFFQTPEG
SLSKYEAQGSLTKSHSAQQPVLVSQTLDIHKRMQPLHIQIKSPQESTGDPGNSSSV
QSSPAAPGGMKSPPDQPVKHLFTTGVVYDTFMLKHQCMCGNTHVHPEHAGRIQSIW
AAPPASEILAKMSELVHSRLQQGAGAGAGGAQTGLFPGAPKGATCFECEITFSNVN
MVPQASEILAKMSELVHRRLRHGSSSYPPVIYSPLMPKGATCFECNITFNNLDNYL
KNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSL
RNKEKSKESAIASTEVKLRLQEFLLSKSKEPTPGGLNHSLPQHPKCWGAHHASLDQ
RGKDRGRERAVASTEVKQKLQEFLLSKSATKDTPTNGKNHSVGRHPKLWYTAAHHT
LNKDKSKRSAVASSVVKQKLAEVILKKQQAALERTVHPSSPSIPYRTLEPLDTEGA
NTWEPEENILDPRLLIAFQNRERQEQLMGYRKRGPKPKPLVVQVPTFARRSNVLTG
NTWEPEENILDPRLLVAFQNRERQEQIMGYRKRGPKPKNNLVSMPSFARRSNVLSG
ISSKKCIGLISVNGRMRNNIKTGSSPNSVSSSPTNSAITQLRNKLENGKPLSMSEQ
HRCDYDGCNKVYTKSSHLKAHRRTHTGEKPYKCTWEGCTWKFARSDELTRHFRKHT
HQCDFAGCSKVYTKSSHLKAHRRIHTGEKPYKCTWDGCSWKFARSDELTRHFRKHT
RQYRLTEHMRIHSGEKPYECQVCGGKFAQQRNLISHMKMHAVGGAAGAAGALAGLG
PFACAADGEDAMTQDLTSREKEEGSDQHVASHLPLHPIMHNKPHSEELPTLVSTIQ
QPLQVYQAPLSLATVPHQALGRTQSSPAAPGGMKSPPDQPVKHLFTTGVVYDTFML
KMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNH
YQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLML
AEDDPSRTLCEACNIRFSRHETYTVHKRYYCASRHDPPPRRPAAPPGPPGPAAPPA
GESDPNKTTCEACNITFSRHETYMVHKQYYCATRHDPPLKRSASNKVPAMQRTMRT
GPGVIDLTRPEDAEGSKAMNGSAAKLQQYYCWPTGGATVAEARVYRDARGRASSEP
RHETYMVHKQYYCATRHDPPLKRSASNKVPAMQRTMRTRKRRKMYEMCLPEQEQRP
SSPVPGELGLAGALFLPQYVFGPDAAPPASEILAKMSELVHSRLQQGAGAGAGGAQ
QPNIGPSFPVGPFLSQFSFPQDITMVPQASEILAKMSELVHRRLRHGSSSYPPVIY
CPQPRALSPELGTKAGPRRPHRWELPRSPSQGAQGPAPRRRLLETMKGIVAASGSE
-----------------MSSKQATSPFACAADGEDAMTQDLTSREKEEGSDQHVAS
PRLLIAFQNRERQEQLMGYRKRGPKPKPLVVQVPTFARRSNVLTGLQDSSTDNRAK
PRLLVAFQNRERQEQIMGYRKRGPKPKNNLVSMPSFARRSNVLSGLHDSSGENRTK
KYCDRSFSISSNLQRHVRNIHNKEKPFKCHLCDRCFGQQTNLDRHLKKHENGNMSG
MLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSE
MLKHQCSCGDNSKHPEHAGRIQSIWSRLQERGLRSQCECLRGRKASLEELQSVHSE
CEACNIRFSRHETYTVHKRYYCASRHDPPPRRPAAPPGPPGPAAPPAPSPAAPVRT
CEACNITFSRHETYMVHKQYYCATRHDPPLKRSASNKVPAMQRTMRTRKRRKMYEM
RCPQPRALSPELGTKAGPRRPHRWELPRSPSQGAQGPAPRRRLLETMKGIVAASGS
FECNMCGYHSQDRYEFSSHITRGEHRFHMS
FECNICGYHSQDRYEFSSHIVRGEHKVG
DQCPKAFNWKSNLIRHQMSHDSGKHYECENCAKVFTDPSNLQRHIRSQHVGARAHA
ARRSNVLTGLQDSSTDNRAKLDLGAQGKGQGHQYELNSKKHHQYQPHSKERAGKPP
ARRSNVLSGLHDSSGENRTKLDLGPIPKSHQYQLNSKKHHQYQPSGKDHNEKHHSS
PYYEEQARLSKIHLEKYPNYKYKPRPKRTCIVDGKKLRIGEYKQLMRSRRQEMRQF
RVATSMRTVGKLPRHRPLSRTQSSPLPQSPQALQQLVMQQQHQQFLEKQKQQQLQL
REAHKHGLAALRSTSRNEYIHSGLYSSFTINSLQNPPDAFKAIKTEKLEEPPEDSP
FLPQYVFGPDAAPPASEILAKMSELVHSRLQQGAGAGAGGAQTGLFPGAPKGATCF
SQFSFPQDITMVPQASEILAKMSELVHRRLRHGSSSYPPVIYSPLMPKGATCFECN
KTEGLMKDDRAESQASSLGQKVGESSEQVSEEKTNEA
HHHHHHHHAVGLNLSHVRKRCLSETHGEREPCKKRLTARSISTPTCLGGSPAAERP
SPVYAGEPYNDLVYTNPRKRCLSEANGNKELCKKTLTSRSVSAPGIVECKGGLTPL
KAQSIYGIPHSTLEYKVKERLGTLKNPPKKKMKLMRSEGPDVSVKIELDPQGEAAQ
TNHSEMAEDLCKIGSERSLVLDRLASNVAKRKSSMPQKFLGDKGLSDTPYDSSASY
GPEPGLSGSEIENLLERRTVLQLLLGNPNKGKSEKKEKTPLRDESTQEHSERALSE
RQREQQRQEELEKQRLEQQLLILRNKEKSKESAIASTEVKLRLQEFLLSKSKEPTP
GRTQSSPAAPGGMKSPPDQPVKHLFTTGVVYDTFMLKHQCMCGNTHVHPEHAGRIQ
RTFKKAAGAEEKKVEAPPKRREEEVSGVSDPQPQDAGSRKLSPTKEAFGEQPLQLT
TCMERGYIKEDLDPCPRPKRRQPYNAIFSPKGKEQKT
KRSASNKVPAMQRTMRTRKRRKMYEMCLPEQEQRPPLVQQRFLDVANLNNPCTSTQ
LKETPLKSDRRSNKPIMEKRRRARINNCLNELKTLILDATKKDPARHSKLEKADIL
IVQPGKRPLPVESPDTQRKRRIHRCDYDGCNKVYTKSSHLKAHRRTHTGEKPYKCT
QQEPAAMAQMQGEESLDLKRRRIHQCDFAGCSKVYTKSSHLKAHRRIHTGEKPYKC
DEDSMDIPLDLSSSAGSGKRRRRGNLPKESVQILRDWLYEHRYNAYPSEQEKALLS
-----------MADGPRCKRRKQANPRRNNVTNYNTVVETNSDSDDEDKLHIVEEE
------MKQPIMADGPRCKRRKQANPRRKNVVNYDNVVDTGSETDEEDKLHIAEDD
ECIEDLLNESGQPLDLSCKRPRP
HSSSERPTFIDRLANSLTKRKRSTPQKFVGEKQMRFSLSDLPYDVNSGGYEKDVEL
PYPTSDQEGDPGSKQPRKKRGRYRQYNSEILEEAISVVMSGKMSVSKAQSIYGIPH
LHLKKARLLQSSEDWNAAKRKRLSDSIMNLNVKKEALLAGMVDSVPKGKQDSTLLA
HSQLYPSWSARDNYGKRKKRKREKQSPEMETHTKTKKMCVQHLPADKSCDSPASSH
NTPTLPVQPSLLSSALMPKRKRGRPRKLSGSSNGTGNDYDDFDRENMMNDSSDLGN
PTLPVQPSLLSSALMPKRKRGRPRKLSGSSNGTGNDYDDFDRENMMNDSSDLGNGK
QIKCKDCGQMFSTTSSLNKHRRFCEGKNHFAAGGFFGQGISLPGTPAMDKTSMVNM
APARSPGPAADGPIDLSKKPRRPLPGAPAPALADYHECTACRVSFHSLEAYLAHKK
DSRISHEDEFGAGVLMPPKPRRGKAETHGHAGDPDLPYVCDQCDKAFAKQSSLARH
EQEVERHRREQQLPPLRGKDRGRERAVASTEVKQKLQEFLLSKSATKDTPTNGKNH
QLIKPAISPPQRPAKPSEKPRLRQIPSAEDLETDGGGVGPMANDGLEHRESGRGPP
QPYPTSDQEGDPGSKQPRKKRGRYRQYNSEILEEAISVVMSGKMSVSKAQSIYGIP
DGKLSSINNMGLNSCRNEKERTRFENLGPQLTGKSNEDGKLGPGVIDLTRPEDAEG
LHSQLYPSWSARDNYGKRKKRKREKQSPEMETHTKTKKMCVQHLPADKSCDSPASS
EDEEMDVEEEPRQESGERKVRVRTAINEEQQQQLKQHYSLNARPSRDEFRMIAARL
PVESPDTQRKRRIHRCDYDGCNKVYTKSSHLKAHRRTHTGEKPYKCTWEGCTWKFA
QGEESLDLKRRRIHQCDFAGCSKVYTKSSHLKAHRRIHTGEKPYKCTWDGCSWKFA
LEEPGAGYKKLFSDAQPLQPLQVYQAPLSLATVPHQALGRTQSSPAAPGGMKSPPD
CTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLL
CSCGDNSKHPEHAGRIQSIWSRLQERGLRSQCECLRGRKASLEELQSVHSERHVLL
CDKCGKRFSHSGSYSQHMNHRYSYCKREAEERDSTEQEEAGPEILSNEHVGARASP
CDKCGKRFSHSGSYSQHMNHRYSYCKREAEEREAAEREAREKGHLEPTELLMNRAY
RSYKQRSSLEEHKERCHNYLESMGLPGTLYPVIKEETNHSEMAEDLCKIGSERSLV
RSYKQQSTLEEHKERCHNYLQSLSTEAQALAGQPGDEIRDLEMVPDSMLHSSSERP
EKPLTPVPSKPPVTPATSQDQPLDLSMGSRSRASGTKLTEPRKNHVFGGKKGSNVE
DIKIEPPEELLASDFSLPQVEPVDLSFHKPKAPLQPASMLQAPIRPPKPQSSPQTL
IGGETTSVVPVHPPTVSAQEGPMDLSMKTSRSSVHSFNDSGSEDQEVEVAPRRKFY
SRNTQGYLYTAEGAQEEPQVEPLDLSLPKQQGELLERSTITSVYQNSVYSVQEEPL
KNSHSSSYTPNSFSSEELQAEPLDLSLPKQMKEPKSIIATKNKTKASSISLDHNSV
CPNCKKRFSHSGSYSSHISSKKCISLIPVNGRPRTGLKTSQCSSPSLSASPGSPTR
CPNCKKRFSHSGSYSSHISSKKCIGLISVNGRMRNNIKTGSSPNSVSSSPTNSAIT
CPFPQCRKSCPSASSLEIHMRSHSGERPFVCLICLSAFTTKANCERHLKVHTDTLS
CPFPQCTKSFSNARALEMHLNSHSGVKMEEFLPPGASLKCTVCSYTADSVINFHQH

Cloud 2 (3 SLiMs):	IK.E	[IV]K.[DE]P	[IV]K.E..[DE]	(p = 5.71e-05)
19 UPC	19 Seq:	COM1_HUMAN__Q99708	ELK3_HUMAN__P41970	FOG1_HUMAN__Q8IX07	FOG2_HUMAN__Q8WW38	HAIR_DROME__P14003	HDAC4_HUMAN__P56524	HDAC5_HUMAN__Q9UQL6	HDAC9_MOUSE__Q99N13	IKZF1_HUMAN__Q13422	IKZF4_HUMAN__Q9H2S9	KLF3_HUMAN__P57682	KLF8_HUMAN__O95600	NRIP1_HUMAN__P48552	SOX6_HUMAN__P35712	T7L1A_XENLA__P70062	TRPS1_HUMAN__Q9UHF7	ZEB1_HUMAN__P37275	ZEB2_HUMAN__O60315	ZFH1_DROME__P28166

SLiMMaker Consensus: [IV]K.E[EKP]{0,1}
- SLiM matches 27 of 29 sequences (93.1%).

IKEENAV
IKTEKLE
IKVEAVE
IKSEPSS
IKCEKNG
IKEEEQP
IKEETNH
IKVEMYS
IKIEPGI
IKIEPPE
IKSEPCD
IKKESE
IKNEKRG
IKEEPKI
IKTEPVD
IKTEPLD
IKKEFSN
IKREESR
IKQEQEP
VKEEPVD
VKQEAMD
VKTEKVD
VKKEPAE
VKQEPIE
VKDEEGE
VKREKLE
VKVDPTS
VKRDPLT
VKQEPSS

Cloud 3 (1 SLiMs):	G.{1,2}Y.C..C	(p = 0.002)
4 UPC	4 Seq:	EVI1_HUMAN__Q03112	IKZF4_HUMAN__Q9H2S9	ZEB1_HUMAN__P37275	ZFH1_DROME__P28166

SLiMMaker Consensus: G
- SLiM matches 4 of 4 sequences (100.0%).

GMYACDLCD
GAYPCMQCT
GKHYECENC
GKPYKCNYC

Cloud 4 (1 SLiMs):	D.{1,2}RC.{0,1}K.R	(p = 0.021)
4 UPC	4 Seq:	CBX4_HUMAN__O00257	ZEB1_HUMAN__P37275	ZEB2_HUMAN__O60315	cbx4_XENLA__Q91647

SLiMMaker Consensus: D....K.R
- SLiM matches 4 of 4 sequences (100.0%).

DLRCVKTRS
DLRCVKSRC
DGPRCKRRK
DGPRCKRRK


#Cloud Seq coverage/overlap
Cloud	Dataset	1	2	3	4
1:P..C..C.[KR].[FY]	1.000	1.000	1.000	1.000	1.000
2:IK.E	0.655	0.655	1.000	0.750	0.500
3:G.{1,2}Y.C..C	0.138	0.138	0.158	1.000	0.250
4:D.{1,2}RC.{0,1}K.R	0.138	0.138	0.105	0.250	1.000

#Probabilities of motif clouds overlapping Seq this much or more
Cloud	Dataset	1	2	3	4
1:P..C..C.[KR].[FY]	1.000	1.000	0.792	0.791	0.791
2:IK.E	1.000	0.792	0.000	0.535	0.819
3:G.{1,2}Y.C..C	1.000	0.791	0.535	0.000	0.448
4:D.{1,2}RC.{0,1}K.R	1.000	0.791	0.819	0.448	0.000

#Probabilities of motif clouds overlapping Seq this little or less
Cloud	Dataset	1	2	3	4
1:P..C..C.[KR].[FY]	1.000	1.000	0.785	0.815	0.815
2:IK.E	1.000	0.785	1.000	0.777	0.465
3:G.{1,2}Y.C..C	1.000	0.815	0.777	1.000	0.906
4:D.{1,2}RC.{0,1}K.R	1.000	0.815	0.465	0.906	1.000


#Cloud UPC coverage/overlap
Cloud	Dataset	1	2	3	4
1:P..C..C.[KR].[FY]	1.000	1.000	1.000	1.000	1.000
2:IK.E	0.655	0.655	1.000	0.750	0.500
3:G.{1,2}Y.C..C	0.138	0.138	0.158	1.000	0.250
4:D.{1,2}RC.{0,1}K.R	0.138	0.138	0.105	0.250	1.000

#Probabilities of motif clouds overlapping UPC this much or more
Cloud	Dataset	1	2	3	4
1:P..C..C.[KR].[FY]	1.000	1.000	0.792	0.791	0.791
2:IK.E	1.000	0.792	0.000	0.535	0.819
3:G.{1,2}Y.C..C	1.000	0.791	0.535	0.000	0.448
4:D.{1,2}RC.{0,1}K.R	1.000	0.791	0.819	0.448	0.000

#Probabilities of motif clouds overlapping UPC this little or less
Cloud	Dataset	1	2	3	4
1:P..C..C.[KR].[FY]	1.000	1.000	0.785	0.815	0.815
2:IK.E	1.000	0.785	1.000	0.777	0.465
3:G.{1,2}Y.C..C	1.000	0.815	0.777	1.000	0.906
4:D.{1,2}RC.{0,1}K.R	1.000	0.815	0.465	0.906	1.000

>CBX4_HUMAN__O00257 RecName: Full=E3 SUMO-protein ligase CBX4; EC=6.3.2.-; AltName: Full=Chromobox protein homolog 4; AltName: Full=Polycomb 2 homolog; Short=Pc2; Short=hPc2;
XELPAVGEHXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXTWEPEENXXDPRLLIAFQNRERQEQLMGYRKRGPKPKPLVVQVPTFARRSNVLTGLQDSSTDNRAKLDLGAQGKGQGHQYELNSKKHHQYQPHSKERAGKPPPPGKSGKYYYQLNSKKHHPYQPDPKMYDLQYQGGHKEAPSPTCPDLGAKSHPPDKWAQGAGAKGYLGAVKPLAGAAGAPGKGSEKGPPNGMMPAPKEAVTGNGIGGKMKIVKNKNKNGRIVIVMSKYMENGMQAVKIKSGEVAEGEARSPSHKKRAADERHPPADRTFKKAAGAEEKKVEAPPKRREEEVSGVSDPQPQDAGSRKLSPTKEAFGEQPLQLTTKPDLLAWDPARNTHPPSHXPXPXPXXXXXXXXXXXHAVGLNLSHVRKRCLSETHGEREPCKKRLTARSISTPTCLGGSPAAERPADLPPAAALPQPEVILLDSDLDEPIDLRCVKTRSEAGEPPSSLQVKPETPASXXVXVXXXXAPTTTAEKPPAEAQDEPAESLSEFKPXXXXXXXXXXXXXXXXXXXXXYVTV
>COM1_HUMAN__Q99708 RecName: Full=DNA endonuclease RBBP8; EC=3.1.-.-; AltName: Full=CtBP-interacting protein; Short=CtIP; AltName: Full=Retinoblastoma-binding protein 8; Short=RBBP-8; AltName: Full=Retinoblastoma-interacting protein and myosin-like; Short=RIM; AltName: Full=Sporulation in the absence of SPO11 protein 2 homolog; Short=SAE2;
XNISGSSCGSPNSADTSSDFKDLWTKLKECHDXEVQGLQVKVTXXKXXRXXXXXRLXXFXTKNQQLREQQKVLHXXIKXXXXXXXXXXXXRCAVTEEHMRKKQQEFENIRQQNLKLITELMNERNTLQEENKKLSEQLQQKIENDQQHQAAELECEEDVIPDSPITAFSFSGVNRLRRKENPHVRYIEQTHTKLEHSVCANEMRKVSKSSTHPQHNPNENEILVADTYDQSQSPMAKAHGTSSYTPDKSSFNLATVVAETLGLGVQEESETQGPMSPLGDELYHCLEGNHKKQPFEESTRNTEDSLRFSDSTSKTPPQEELPTRVSSPVFGATSSIKSGLDLNTSLSPSLLQPGKKKHLKTLPFSNTCISRLEKTRSKSEDSALFTHHSXGSEVNKIIIQSSNKQILINKNISESLGEQNRTEYGKDSNTDKHLEPLKSLGGRTSKRKKTEXXSXHEVSCPQASFDKENAFPFPMDNQFSMNGDCVMDKPLDLSDRFSAIQRQEKSQGSETSKNKFRQVTLYEALKTIPKGFSSSRKASDGNCTLPKDSPGEPCSQECIILQPLNKCSPDNKPSLQIKEENAVFKIPLRPRESLETENVLDDIKSAGSHEPIKIQTRSDHGGCELASVLQLNXCRTGKIKSLQNNQDVSFENIQWSIDPGADLSQYKMDVTVIDTKDGSQSKLGGETVDMDCTLVSETVLLKMKKQEQKGEKSSNEERKMNDSLEDMFDRTTHEEYESCLADSFSQAADEEEELSTATKKLHTHGDKQDKVKQKAFVEPYFKGDERETSLQNFPHIEVVRKKEERRXXXXXXXXXXXXXYAXXPAXEREKKLASCSRHRFRYIPXNTPENFWEVGFPSTQTCMERGYIKEDLDPCPRPKRRQPYNAIFSPKGKEQKT
>E1A_ADE02__P03254 RecName: Full=Early E1A protein {ECO:0000305}; AltName: Full=Early E1A 32 kDa protein;
XRHIICHGGXXXXXXXASXXXQXIEEVLADNLPPPSHFEPPTLHELYDLDVTAPEDPNEEAVSQIFPDSVMLAVQEGIDLLTFPPAPGSPEPPHLSRQPEQPEQRALGPVSMPNLVPEVIDLTCHEAGFPPSDDEDXXGXEFVLDYVEXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXSPVSEPEPEPEPEPEPARPTRRPKLVPAILRRPTSPVSRECNSSTDSCDSGPSNTPPEIHPVVPLCPIKPVAVRXXGRRXXXECIEDLLNXXGQPLDLSCKRPRP
>ELK3_HUMAN__P41970 RecName: Full=ETS domain-containing protein Elk-3; AltName: Full=ETS-related protein ERP; AltName: Full=ETS-related protein NET; AltName: Full=Serum response factor accessory protein 2; Short=SAP-2; Short=SRF accessory protein 2;
XESAXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXPHXXXXSRESLLLQDSDCKASPEGREAHKHGLAALRSTSRNEYIHSGLYSSFTINSLQNPPDAFKAIKTEKLEEPPEDSPPVEEVRTVIRFVTNKTDKHVTRPVVSLPSXXXXXXXXAXXXXXXXXXXXXXXXXNXAXISXAXPFXXRXPXLSPNSPLPSEHRSLFLEAACHDSDSLEPLNLSSGSKTKSPSLPPKAKKPKGLEISAPPLVLSGTDIGSIALNSPALPSXSLTPAFFTAQTPNGXLLTPXXXXXXXXXXXXXXXXXPLSPARLQGPSTLFQFPTLLNGHMPVPIPSLDRAASPVLLSSNSQKS
>EVI1_HUMAN__Q03112 RecName: Full=MDS1 and EVI1 complex locus protein EVI1; AltName: Full=Ecotropic virus integration site 1 protein homolog; Short=EVI-1;
XKSEDYPHETMAPDIHEERQYRCEDCDQLFESKAELADHQKFPCSTPHSAFSMVEEDFQQKLESENDLQEIHTIQECKECDQVFPDLQSLEKHMLSHTEEREYKCDQCPKAXXWKSNLIRHQMSHDSGKHYECENCAKVFTDPSNLQRHIRSQHVGARAHACPECGKTFATSSGLKQHKHIHXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXNKHRRFCEGXXHFXXXXFFGQGISLPGTPAMDKTSMVNMSHANPGLADYFGANRHPAGLTFPTAPXXXXSXPGLFPXGLYHRPPLIPASSPVKGLSSTEQTNKSQSPLMTHPQILPATQDILKALSKHPSVGDNKPVELQPERSSEERPFEKISDQSESSDLDDVSTPSGSDLETTSGSDLESDIESDKEKFKENGKMFKDKVSPLQNLASINNKKEYSNHSIFSPSLEEQTAVSGAVNXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXQSMYPFPDRDLRSLPLKMEPQSPGEVKKLQKGSSESPFDLTTKRKDEKPLTPVPSKPPVTPATSQDQPLDLSMGSRSRASGTKLTEPRKNHVFGGKKGSNVESRPASDGSLQHARPTPFFMDPIYRVEKRKLTDPLEALKEKYLRPSPGFLFHPQFQLPDQRTWMSAIENMAEKLESFSALKPEASELLQSVPSMFNFRAPPNALPENLLRKGXERXXXRYCXXXXXXXANLTRHLRTHTGEQPYRCKYCDRSFXISSNLQRHVRNIHNXEKXXXXXXXXXXXXXXTNLDRHLKKHENGNMSGTATSSPHSELESTGAILDDKEDAYFTEIRNFIGNSNHGSQSPRNVEERMNGSHFKDEKALVTSQNSDLLDDEEVEDEVLLDEEDEDNDITGKTGKEPVTSNLHEGNPEDDYEETSALEMSCKTSPVRYKEEEYKSGLSALDHIRHFTDSLKMRKMEDNQYSEAELSSFSTSHVPEELKQPLHRKSKSQAYAMMLSLSDKESLHSTXHXXSNVWHSMARAAAESSAIQSISHV
>FOG1_HUMAN__Q8IX07 RecName: Full=Zinc finger protein ZFPM1; AltName: Full=Friend of GATA protein 1; Short=FOG-1; Short=Friend of GATA 1; AltName: Full=Zinc finger protein 89A; AltName: Full=Zinc finger protein multitype 1;
XSRRKQSNPRQIKRSLGDMEAREEVQLVGASHMEQKATAPEAPSPPSADVNSPXXLXXXTSPGGPKELEGQEPEPRPTEEEPGSPWSGPDELEPVVQDGQRRIRARLSLATGLSWGPFHGSVQTRASSPRQAEPSPALTLXXXXXXXXXXXXPQAXXEAEANTEXHRKDDALWCRVTKPVXXGGLLSVLLTAEPHSTPGHPVKKEPAEPTCPAPAHDLQLLPQQAGXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXGTGSPAAAATDEKPKETYPNERVCPFPQCRKXXXSASSLEIHMRSXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXQPGSKGEIYSPGAGHPATKLPPDSLGSFQQQHTALQGPLASADLGLAPTPSPGLDRKALAEATNGEARAEPLAQNGGSSEPPAAPRSIKVEAVEEPEAAPILGPGEPGPQAPSRTPSPRSPAPARVKAELSSPTPGSSPVPGELGLAXXXFXXXYVFGPDAAPPASEILAKMSELVHSRLQQGAXAXAXGAQTGLFPGXXXXXXXXXXXXXXXXXXXXXXXXXXYCSGRRAPEDAPAARRPKAPPGPARAPPGQPAEPDAPRSSPGPGAREEGAGGAATPEDGAGGRGSEGSQSPGSSVDDAEDDPSRTLCEACNIRFSRHEXXTVHKRYYCASRHDPPPRRPAAXXGXXGXAAXPAPSPAAPVRTXXXRKLYELHAAGAPXXXXXGHAPAPESPRPGSGSGSGPGLAPARSPGPAADGPIDLSKKPRRPLPGAPAPALAXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXLLEXFXXXXXXLLGAPLAGPGVEARTPADRGPSPAPAPAASPQPGSRGPRDGLGPEXQEXXXGXXXSPAAAPEAVXXXXAXPSYSDKGVQTPSKGTPAPLPNGNHXXXXXXXXXXXXXXXXXXXXXXXXXXXAAEHVK
>FOG2_HUMAN__Q8WW38 RecName: Full=Zinc finger protein ZFPM2; AltName: Full=Friend of GATA protein 2; Short=FOG-2; Short=Friend of GATA 2; Short=hFOG-2; AltName: Full=Zinc finger protein 89B; AltName: Full=Zinc finger protein multitype 2;
XSRRKQSKPRQIKRPLEDAIEDXXXXCPSXETDIISKGDFPLEESFSTEFGPENLSCEEVEYFCNKGDDEGIQETAESDGDTQSEKPGQPGVETDDWDGPGELEVFQKDGERKIQSRQQLPVGTTWGPFPGKMDLNNNSLKTKAQVPMVLTAXXXXXXXVTWQXXXXXXXNXXXXXXXXXXXXXTTXXXXXXXXXXXXXXXXXXXXXXXXQMTLXXGXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXMYXCXXRQREAAPVSEENEDSAHQISSLCPFPQCTKSFSNARALEMHLNSHSGVKMEEFLXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXTXRELLQHQELHVPSGKLPRESDMEHSPSATEDSLQPATDLLTRSELPQSQKAMQTKDASSDTELDKCEKKTQLFLTNQRPEIQPTTNKQSFSYTKIKSEPSSPRLASSPVQPNIGPSFPVGPFLSQFSFPQDITMVPQASEILAKMSELVHRRLRHGSSSYPPVIYSXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXRWQQMAKSPEFPSVSEKMPEALSPNTGQTSINLLNPAAHSADPENPLLQTSCINSSTVLDLIGPNGKGHDKDFSTQTKKLSTSSNNDDKINGKPVDVKNPSVPLVDGESDPNKTTCEACNIXXXXXXXXXXHKQYYCATRHDPPLKRSASNKVPAMQRTMRTRKRRKMYEMCLPEQEQRPPLVQQRFLDVANLNNPCTSTQEPTEGLGECYHXXXXXXXXXVXXXXXXXXXXXXXXXXXXXXXXXXSXSXXEMXXXXXXXKKCLSQSERTTTSPKRXXXXXXXXXXXXXXXXXXXXXXXXQNFCPVTAHQRNDLGQLDGKVFPNPESERNSPDVSYERSIIKCEKNGNLKQPSPNGNLFSSHLAXXXXXXXXXXXXQLXXXXEEXXXXXXPQXXXXXXXXKAXXXDQLSPYYGIKPSDYISGSLVIHNTDIEQSRNAENESPKGQASSNGCAALKKDSLPLLPKNRGMVIVNGGLKQDERPAANPQQENISQNPQHEDDHKSPSWISENPLAANENVSPGIPSAEEQLSSIAKGVNGSSQAXTXXXXXXXXXXXXXXXXXXXXXXXXXXXXHAAEHVK
>HAIR_DROME__P14003 RecName: Full=Protein hairy;
XVTGVTAANMTNVLGTAVVPAQLKETPLKSDRRSNKPIMEKRRRARINNCLNELKTLILDATKKDPARHSKLEKADILEKTVKHLQELQRQQAAMQQAADPKIVNKFKAGFXXCXXEVSRFPGIEPAQRRRLLQHLSNCINGVKTELHQXXRXXXXQSIHAQMLPSPPSSPEQDSQQGAAAPYLFGIQQTASXXFLPNGMQVIPTKLPNGSIALVLPQSLPXXXXXXLLXHXXXQXXXAVXXXXXXXXXAQQQPMLVSMPQRTASTGSAXXHXSAGYESAPGXXXXCSYAPPSPANSSYEPMDIKPSVIQRVPMEQQPLSLVIKKQIKEEEQPWRPW
>HDAC4_HUMAN__P56524 RecName: Full=Histone deacetylase 4; Short=HD4; EC=3.5.1.98;
XSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAXSAVPMDLRLDHQFSLPVAEPALXEXQXQQEXXALXXXXXXXXXXLIXEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGXLXLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQXXHXQFLEKHKQXFXXXXLQMNKIIPKPSEPARQPESHPEXTXXXLREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDXXXAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDXXXLKHQCTCGSSSSHPEHAGRIQSIWSRLQEXGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKXXXXXXXXXXXXXXXXXXXXXXXTXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXFAVVRPPGHHAEXSTPXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXGTQQAFYSDPXXLXXXXHRYXXGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPXXXAXXXXXXXXXXXXXXXXXXXXXXXXXXXFXXXXXXPTPXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXLGNXXXPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEXPMXXEPPL
>HDAC5_HUMAN__Q9UQL6 RecName: Full=Histone deacetylase 5; Short=HD5; EC=3.5.1.98; AltName: Full=Antigen NY-CO-9;
XNSPNESDGMSGREPSLEILPRTSLHSIPVTVEVKPVLPRAMPSSMGXXXXGSPSPVELRGALVGSVDPTLREQQLQQELLALXXXXXXXXXLLFAEFQKQHDHLTRQHEVQLQKHLKQQQEMLAAKQQQEMLAAKRQQELEQXRXREXQRQEELEKQRLEQQLLILRNKEKSKESAIASTEVKLRLQEFLLSKSKEPTPGGLNHSLPQHPKCWGAHHASLDQSSPPQSGPPGTPPSYKLPLPGPYDSRDDFPLRKTASEPNLKVRSRLKQKVAERRSSPLLRRKDGTVISTFKKRAVEITGAGPGASSVCNSAPGSGPSXPNXXHSTIAENGFTGSVPNIPTEMLPQHRALPLDSSPNQFSLYTSPSLPNISLGLQATVTVTNSHLTASPKLSTQQEAERQALQSLRQGGTLTGKFMSTSXXXGCLLGVALEGDXSPHGHXSLLQHVLLXXXXXXXXTLIAVPLHGQSPLVTGERVATSMRTVGKLPRHRPLSRTQSSPLPQSPQALQXLVMXXXHXQFLEKQKXXXLQLGKILTKTGELPRQPTTHPEXTXXXLTEQQEVLLGEGALTMPREGSTESESTQEDLXXXDXXDDGXXXEDCIQVKDEEGESGAEEGPDLEEPGAGYKKLFSDAQPLQPLQVYQAPLSLATVPHQALGRTQSSPAAPGGMKSPPDQPVKHLFTTGVVXXXXXXXXXXXCXXTHVHPXHAGRIQSIWSRLQEXGLLSKCERIRGRKATLDEIQTXHSEYHTLLYGTSPLNRQKLDSKKLLGXIXQKXXXXLPCGXXXXXSDTVWNEMXSXXXXXXXXXXXXXXXXXXXXXXXXXXXXIIRPPGHHXXXXTXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXTQQAXYNDPXXXXXXXXXXXXXNFFPGSGAPEEVGXXPXVGYNVNVAWTGGXXXPXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXVXXXXXXXXXXXXXXXXXXXXXXXXXXXQXFAXGXGRSLREAQAGETEEAETVSAMALLSVGAEQXQXXXAREHSPRPAEEPMEQEPAL
>HDAC9_MOUSE__Q99N13 RecName: Full=Histone deacetylase 9; Short=HD9; EC=3.5.1.98; AltName: Full=Histone deacetylase 7B; Short=HD7b; AltName: Full=Histone deacetylase-related protein; AltName: Full=MEF2-interacting transcription repressor MITR;
XHSMISSVDVKSEVPMGLEPISPLDLRTDLRMMMPVVDPVVXXXXXXXXXXXXXXXXXXXXXXLIXXXXKQHENLTRQHQAQLQEHIKELLAIKQQQELLEKEQKLEQQRQEQEVERHRREQQLPPLRGKDRGRERAVASTEVKQKLQEFLLSKSATKDTPTNGKNHSVGRHPKLWYTAAHHTSLDQSSPPLSGTSPSYKYTLPGAQDSKDDFPLRKTASEPNLKVRSRLKQKVAERRSSPLLRRKDGNLVTSFKKRVFEVAESXVXXXXPGSGPSSPNNGPAGNVTENEASALPPTPHPEQLVPQQRILIHEDSMNLLSLYTSXXXXNITLGLPAVPSPLNASNSLKDKQKCETQMLRQGVPLPSQYGSXIAAXXSHVHVAMEGKPNSSHQALXQHXXLKEXMRQQKLLVAGGVPLHPQSPLATKERISPGIRGTHKLPRHRPLNRTQSAPLPQSTLAQLVIQXXHXQFLEKQKXYXXQIHMNKLLSKSIEQLKQPGSHLEXAXXELQGDQSMEDRAASKDNSARSDSSACVEDTLGQVGAVKVKEEPVDSDEDAQIQEMECGEQAAFMQQXXXXXXXXXXXIKVII
>HDAC7_MOUSE__Q8C2B3 RecName: Full=Histone deacetylase 7; Short=HD7; EC=3.5.1.98; AltName: Full=Histone deacetylase 7A; Short=HD7a;
XHSPGAGCPALQPDTPGSQPQPMDLRVGQRPTVEPPPEPALLTLQHPQRLHRHLFLAGLHQQQRSAEPMRLSMDPPMPELQGGQQEQELRQLLNKDKSKRSAVASSVVKQKLAEVILKKQQAALERTVHPSSPSIPYRTLEPLDTEGAARSVLSSFLPPVPSLPTEPPEHFPLRKTVSEPNLKLRYKPKKSLERRKNPLLRKESAPPSLRRRPAETLGDSXPXXXXTPASGCSSPNDSEHGPNPALGSEADGDRRTHSTLGPRGPVLGNPHAPLFLHHGLEPEAGGTLPSRLQPILLXXXXXXXXXXWTVXXXXXXXXHFAQPLLTTERLSGSGLHRPLNRTRSEPLPPSATASPLLAPLQPRQDRLKPHVQLIKPAISPPQRPAKPSEKPRLRQIPSAEDLETDGGGVGPMANDGLEHRESGRGPPEGRGSISLQQHQQVPPWEQQHLAGRLSQGSPGDSVLIPLAQVGHRPLSRTQSSPAAPVSLLSPEPTCQTQVLNSSETPATGLVYDSVMLKHQCSCGDNSKHPEHAGRIQSIWSRLQEXGLXSQCECLRGRKASLEELQSXHSERHVLLYXTNPLXXXXXDNGXXXXXXXXXXXXXXXXXXXXXXXDTIWNXLXSSXXXRWXXXXXXDXAFKXXXXXXXNGFAVVRPPGHHXXXXTXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXWDVXXXXGTQQTFYQDPSVLYISLHRHDDGNFFPGSGAVDEVGTGSGEGFNVNVAWAGGLDPPXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXPLSEESWKQKPNLSAXXSLXXXXXXXXXXXXXXXXXXXXXXXWLPRVPGADAEVEAVTXXXSLSVGILAEDRPSERLVXXXEPMNL
>HIC1_HUMAN__Q14526 RecName: Full=Hypermethylated in cancer 1 protein; Short=Hic-1; AltName: Full=Zinc finger and BTB domain-containing protein 29;
XTFPEADILLKSGECAGQTMLDTMEAPGHSRQLLLQLXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXYCHLRGXXXXXXGYAPYGRPGRGLRAATPVIQACYPSXVGXXXXXAAEXPSGPEAAVNTHCAELYAXXXGPAAXLCXXXXXXXXXCGLDLSKKSPPGSAAPERPLAERELPXRXDSXPSAGPAAYKEPPLALPSLPPLPFQKLEEAAPPSDPFRGGSGSPGPEPPGRPDGPSLLYRWMKHEPGLGSYGDELGRERGSPSERCEERGGDAAVSPGGPPLGLAPPPRYPGSLDGPXAXXDGDDYKSSSEETGSSEDPSPPGGHLEGYPCPHLAYGEPXXFXXXXXXXXXXXXXXXXXEQLNAHVEAHVXXXEALYGRAEXXEVXXGXAGLGPPFXXXGDKVAGAPGGLGEXLRPYRCASCDKSYKDPATLRQHEKTHWXTRPXPCTICGKKFTQRGTMTRHMRSHLXXXXXXXXXXXXXXXXXXRLTEHMRIHSXXKPXXCQVCGXXXXXXRNLISHMKMHAVXXAXXXXXXXAGLGGLPGVPGPDGKGKLDFPEGVFAVXRXTAEXLSLKQXDKAXXXXLLAQXXXXXXXXXXXXXXXXXXXXXXXXXXLXPDKAAEVLSQGAHLAAGPDGRTIDRFSPT
>IKZF1_HUMAN__Q13422 RecName: Full=DNA-binding protein Ikaros; AltName: Full=Ikaros family zinc finger protein 1; AltName: Full=Lymphoid transcription factor LyF-1;
XDADEGQDMSQVSGKESPPVSDTPDEGDEPMPIPEDLSTTSGGQQSSKSDRVVASNVKVETQSDEENGRACEMNGEECAEDLRMLDASGEKMNGSHRDQGSSALSGVGGIRXXXXXXXXXXXXXXXXXXXXXXXXXRSHTXERPFQCNQCGXXXXXXGNXLRHIKLHXXXXXXXXXXXXXXXXXXXXXXXHLRTHSXXKPXXCGYCGRSYKQRSSLEEHKERCHNYLESMGLPGTLYPVIKEETNHSEMAEDLCKIGSERSLVLDRLASNVAKRKSSMPQKFLGDKGLSDTPYDSSASYEKENEMMKSHVMDQAINNAINYLGAESLRPLVQTPPGGSEVVPVISPMYQLHKPLAEGTPRSNHSAQDSAVENLLLLSKAKLVPSEREASPSNSCQDSTDTESNNEEQRSGLIYLTNHIAPHARNGLSLKEEHRAYDLLRAASENSQDALRVVSTXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXFSSHITRGEHRFHMS
>IKZF4_HUMAN__Q9H2S9 RecName: Full=Zinc finger protein Eos; AltName: Full=Ikaros family zinc finger protein 4;
XHTPPALPRRFQGGGRVRTPGSHRQGKDNLERDPSGGCVPDFLPQAQDSNHFIMESLFCESSGDSSLEKEFLGAPVGPSVSTPNSQHSXPXRXLSANSIKVEMYSDEESSRLLGPDERLLEKDDSVIVEDSLSEPLGYCDGSGPEPHSPGGIRLPNXXXXXXXXXXXXXXXXXXXXHXRSHTXERPFHCNQCGXXXXXXGNXLRHIKLHXXXXXXXXXXXXXXXXXXXXXTGHLRTHSVSSPTVGKPYKCNYCGRSYKQQSTLEEHKERCHNYLQSLSTEAQALAGQPGDEIRDLEMVPDSMLHSSSERPTFIDRLANSLTKRKRSTPQKFVGEKQMRFSLSDLPYDVNSGGYEKDVELVAHHSLXXXXGSSLAXVXXXHLRXLRLPPTNCISXLTPVISSVYTQMQPLPGRLELPGSREAGEGPEDLADGGPLLYRPRGPLTDPGASPSNGCQDSTDTESNHEDRVAGVVSLPQGXXXQXXPTIVVGRHSPAYAKEDPKPQEGLLRGTPGPSKEVLRVVGESGXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXSSHIVRGEHKVG
>KLF3_HUMAN__P57682 RecName: Full=Krueppel-like factor 3; AltName: Full=Basic krueppel-like factor; AltName: Full=CACCC-box-binding protein BKLF; AltName: Full=TEF-2;
XLMFDPVPVKQEAMDPVSVSYPSNYMESXKPNKYGVIYSTPLPEKFFQTPEGLSHGIQMEPVDLTVNKRSSPPSAGNSPSSLKFPSSHRRASPGLSMPSSSPPIKKYSPPSPGVQPFGVPLSMPPVXAAALSRHXXXSXXXXXXXXXXXXXXXXXXXXXXLQQPLMVSLSEEMENSSSSMQVPVIESYEKPISQKKIKIEPGIEPQRTDYYPEEMSPPLMNSVSPPQALLQENHPSVIVQPGKRPLPVESPDTQRKRRIHRCDYDGCNKVYTKSSHLKAHRRTHTGEKPXKXXXXXXXXXXXXXXXXTRHFRKHTXXKPXQCPDCDRSFXRSDHLALHRKRHMLV
>KLF8_HUMAN__O95600 RecName: Full=Krueppel-like factor 8; AltName: Full=Basic krueppel-like factor 3; AltName: Full=Zinc finger protein 741;
XVDMDKLINNLEVQLNSEGGSMQVFKQVTASVRNRDPPEIEYRSNMTSPTLLDANPMENPALFNDIKIEPPEELLASDFSLPQVEPVDLSFHKPKAPLQPASMLQAPIRPPKPQSSPQTLVVSTSTSDMSTSANIPTVLTPGSVLTSSQSTGSQQILHVIHTIPSXSLXNKXXGXXTXPXXXXXXXXXYXXXPADGXXAAITVPLIGGDGKNAGSVKVDPTSMSPLEIPSDSEESTIESGSSALQSLQGLQQEPAAMAQMQGEESLDLKRRRIHQXDFAGCXXVXXKSSHLKAHRRIHTGEKPXXXXXXXXXXXXXXXXXXTRHFRKHTXXKPXXCTDCNRSFXRSDHLSLHRRRHDTM
>KNIR_DROME__P10734 RecName: Full=Zygotic gap protein knirps; AltName: Full=Nuclear receptor subfamily 0 group A member 1;
XNQTCXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXSKGXXRYGRRXXXFKIHCLLXXXEQAXXXXGKAPPLAGGVSVGGAPSASSPVGSPHTPGFGDMAAHLXXXHQXXXXXQVPRHPHMPLLGYPSYLXDXXXXXXXFSMMGXXPHQSPFQLPPHLLXXXYXAXXXXXAXSXXDXAYRQEMYKHRQSVDSVESQNRFSPASQPPVVQPTSSARQSPIDVCLEEDVHSVHSHQSSASLLHPIAIRATPTTPTSSSPLSFAAKMQSLSPVSVCSIGGETTSVVPVHPPTVSAQEGPMDLSMKTSRSSVHSFNDSGSEDQEVEVAPRRKFYQLEAECLTTSXXXXXHSAAHSPNTTTAHAEVKRQKLGGAEATHFXXFXXXXXXXXXXXXIFVCV
>LCOR_HUMAN__Q96JN0 RecName: Full=Ligand-dependent corepressor; Short=LCoR; AltName: Full=Mblk1-related protein 2;
XQRMIQQFAAEYTSKNSSTQDPSQPNSTKNQSLPKASPVTTSPTAATTQNPVLSKLLMADQDSPLDLTVRKSQSEPSEQDGVLDLSTKKSPCAGSTSLSHSPGCSSTQGNGRPGRPSQYRPDGLRSGDGVPPRSLQDGTREGFGHSTSLKVPLARSLQISEELLSRNQLSTAASLGPSGLQNHGQHLILSREASXXXXHYEXXLXRMKXXGXGXXXXISDLPFLAENSAFPKMALQAKQDGKKDVSHSSPVDLKIPQVRGMDLSWESRTGDQYSYSSLVMGSQTESALSKKLRAILPKQSRKSMLDAGPDSWGSDAEQSTSGQPYPTSDQEGDPGSKQPRKKRGRYRQYNSEILEEAISVVMSGKXXXSKAQSIYGIPHSTLEYKVKERLGTLKNPPKKKMKLMRSEGPDVSVKIELDPQGEAAQSANESKNE
>NRIP1_HUMAN__P48552 RecName: Full=Nuclear receptor-interacting protein 1; AltName: Full=Nuclear factor RIP140; AltName: Full=Receptor-interacting protein 140;
XTHGEELGSDVHQDSIXLTYXEGLLMHQAAGGSGTAVDKKSAGHNEEDQNFNISGSAFPTCQSNGPVLNTHTYQGSGMLHLKKARLLQSSEDWNAAKRKRLSDSIMNLNXXKEXXLAGMVDSVPKGKQDSTLLASLLXXXXXXXXXVXXSQQIXXXXKEQGYALSHDSLKXXKDLRCYXVASSHLKTLLKKSKVKDQKPDTNLPDVTKNLIRDRFAESPHHVGQSGTKVMSEPLSCAARLQAVASMVEKRASPATSPKPSVACSQLALLXXSEAHLQQYSREHALKTQNANQAASERLAAMARLQENGQKDVGSYQLPKGMSSHLNGQARTSSSKLMASKSSATVFQNPMGIIPSSPKNAGYKNSLERNNIKQAANNSLXXHXLKSQTIPKPMNGHSHSERGSIFEESSTPTTIDEYSDNNPSFTDDSSGDESSYSNCVPIDLSCKHRTEKSESDQPVSLDNFTQSLLNTWDPKVPDVDIKEDQDTSKNSKLNSHQKVTLXQXXLGHKNEENVEKNTSPQGVHNDVSKFNTQNYARTSVIESPSTNRTTPVSTPPLLTSSKAGSPINLSQHSLVIKWNSPPYVCSTQSEKLTNTASNHSMDLTKSKDPPGEKPAQNEGAQNSATFSASKLLQNLAQCGMQSSMSVEEQRPSKQLLTGNTDKPIGMIDRLNSPLLSNKTNAVEENKAFSSQPTGPEPGLSGSEIENLLERRTVLQLLLGNPNKGKSEKKEKTPLRDESTQEHSERALSEQILMVKIKSEPCDDLQIPNTNVHLSHDAKSAPFLGMAPAVQRSAPALPVSEDFKSEPVSPQDFSFSKNGLLSRLLRQNQDSYLADDSDRSHRNNEMALLESKNLCMVPKKRKLYTEPLENPFKKMKNNIVDAANNHSAPEVLYGSLLNQEELKFSRNDLEFKYPAGHGSASESEHRSWARESKSFNVLKQLLLSENCVRDLSPHRSNSVADSKKKGHKNNVTNSKPEFSISSLNGLMYSSTQPSSCMDNRTFSYPGVVKTPVSPTFPEHLGCAGSRPESGLLNGCSMPSEKGPIKWVITDAEKNEYEKDSPRLTKTNPILYYMLQKGGNSVTSRETQDKDIWREASSAESVSQVTAKEELLPTAETKASFFNLRSPYNSHMGNNASRPHSANGEVYGLLGSVLTIKKESE
>SOX6_HUMAN__P35712 RecName: Full=Transcription factor SOX-6;
XSSKQATSPFACAADGEDAMTQDLTSREKEEGSDQHVASHLPLHPIMHNKPHSEELPTLVSTIQQDADWDSVLSSQQRMESENNKLCSLYSFRNTSTSPHKPDEGSRDREIMTSVTFGTPERRKGSLADVVDTLKQKKLEEMTRTEQEDSSCMEKLLSKDWKEKMERLNTSELLGEIKGTPESLAEKERQLSTMITQLXSLREQLLAAHDEQKKLAASQIEKQRQQMDLARQQQEQIARXXXXLXXXQHKXXXLQXXIXXQGXMPPLMIPIFPHDQXTLAXXXXAQQXXLFPPGITYKXGDNYPVQFIPSTMAXXXASGLSPLQLQKGHVSHPQINQRLKGLSDRFGRNLDTFEHGGGHSYNHKQIEQLYAAQLASMQVSPGAKMPSTPQPPNTAGTVSPTGIKNEKRGTSPVTQVKDEAAAQPLNLSSRPKTAEPVKSPTSPTQNLFPASKTSPVNLPNKSSIPSPIGGSLGRGSSLDILSSLNSPALFGDQDTVMKAIQEARKMREQIXREXXXXQPHGVDGKLSSINNMGLNSCRNEKERTRFENLGPQLTGKSNEDGKLGPGVIDLTRPEDAEGSKAMNGSAAKLQQYYCWXTGXXXXAEARVYRDARGRASSEPHIKRPMNAFMVWAKDERRKILQAFPDMHNSNISKILGSRWKSMSNQEKQPYYEEQARLSKIHLEKYPNYKYKPRPKRTCIVDGKKLRIGEYKQLMRSRRQEMRQFFTVGQQPQIPITTGTGVVYPGAITMATTTPSPQMTSDCSSTSASPEPSLPVIQSTYGMKTDGGSLAGNEMINGEDEMEMYDDYEDDPKSDYSSENEAPEAVSAN
>T7L1A_XENLA__P70062 RecName: Full=Transcription factor 7-like 1-A; AltName: Full=HMG box transcription factor 3-A; Short=TCF-3-A; Short=xTcf-3;
XPQLNSGGGDELGANDELIRFKDEGEQEEKSPGEGSAEGDLADVKSSLVNESENHSSDSDSEVERRPPPREAFEKHRDYLTEALRRQQDAAFFKGPXXXXXXXXXXXXXXXXXXPNGALSPXARTYLQMKWPLLDSPSTAGLKDARSPSPAHLSNKVPVVQHPHHMHPLTPLITYSNEHFSPGTPPGHLSPEIDPKTGIPRPPHPSELSPYYPLSPGAVGQIPHPLGWLVPPQGQPMYSIPPGGFRHPYPALAMNASMXXLVXSRFSPHMVPPPHHSLHTSGIPHPAIVSPIVKQEPSSGNISPNLHTKSNMIVKKEEEKKPHIKKPLNAFMXXXXXXXXXXXXXXXXXXXXXXXXXXGRRWHSLSXXEQAKYYELARKERQLHSQLYPSWSARDNYGKRKKRKREKQSPEMETHTKTKKMCVQHLPADKSCDSPASSHGSMLDSPATPSAXLXSPXXPXATHSEQAQPLSLTTKPEARAQLSLSHSAAFLASKXPXXXXFSGHLSSPVGSPLLSRPIPLTXXILSPXXXXXXXXQXXXXXXXXXLSLVTKSSD
>TGIF1_HUMAN__Q15583 RecName: Full=Homeobox protein TGIF1; AltName: Full=5'-TG-3'-interacting factor 1;
XVLAQSRVSAGVGSPHCSGSXXXGSDSFPWPASHPGNPQCSFSTAFLASXXXSRGTLAYLPPAPWSSLATPSALLGSSCAPXXXXARCPQPRALSPELGTKAGPRRPHRWELPRSPSQGAQGPAPRRRLLETMKGIVAASGSETEDEDSMDIPLDLSSSAGSGKRRRRGNLPKESVQILRDWLXEHRYNAXXSEQEKALLSQQTXXXXXXXXXXXXXXXXXXLPDMLRKDGKDPNQFTISRRGAKISETSSVESVMGIKNFMPALEETPFHSCTAGPNPTLGRPLSPKPSSPGSVLARPSVICXTXVXXXXXXXXXXXXXVGXXXXXXIQQIAAKNFTDTSLMYPEDTCKSGPSTNTQSGLFNTPXXTXPDLNQDFSGFQXXVXXXXXXXXXXELQAKLTA
>TRPS1_HUMAN__Q9UHF7 RecName: Full=Zinc finger transcription factor Trps1; AltName: Full=Tricho-rhino-phalangeal syndrome type I protein; AltName: Full=Zinc finger protein GC79;
XVRKKNPPLRNVASEGEGQILEPIGTESKVSGKNKEFSADQMSENTDQSDAAELNHKEEHSLHVQDPSSSSKKDLKSAVLSEKAGFNYESPSKGGNFPSFPHDEVTDRNMLAFSSPAAGGVCEPLKSPQRAEADDPQDMACTPSGDSLETKEDQKMSPKATEETGQAQSGQANCQGLSPVSVASKNPQVPSDGGVRLNKSKTDLLVNDNPDPAPLSPELQDXXXXXXXXXXXXXXXXXXXXXFRKYXXXLHNRTRXDXELDSKXXAXXNXVQXXHSKDFQXXXRXXXXXVLXXXXXXRPVLLNGTYDXXXXXGGTFIGIGRKTXXXXXXXXXXXXXXXXXXXXXXXXTELEQHFLQTHPNKIKASLPSSEVAKPSEKNSNKSIPALQSSDSGDLGKWQDKITVKAGDDTPVGYSVPIKPLDSSRQNXTXXXXXXXXXXXXXXXXXXXXXXXLXHYGKQHGAVQSGGLNPELNDKLSRGSVINQNDLAKSSEGETMTKTDKSSSGAKKKDFSSKGAEDNXXXXXXXXXXXXXXXXXXXXXXXXVXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXLFHYESVHESQASDVKQEANHLQGSDGQQSVKESKEHSCTKCDFITXXXEXXXXXXXXXXXXXXXXXXXXXXXXXXXXXEHFNTVHCQEQDITTANGEEDGHAISTIKEEPKIDFRVYNLLTPDSKMGEPVSESVVKREKLEEKDGLKEKVWTESSSDDLRNVTWRGADILRGSPSYTQASLGLLTPVSGTQEQTKTLRDSPNVEAAHLARPIYGLAVETKGFLQGAPAGGEKSGALPQQYPASGENKSKDESQSLLRRRRXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXPRPLNIIKQNNGEQIIRXXTXKRLNPEALQAEQLNKQQRGSNEEQVNGSPLERRSEDHLTESHQREIPLPSLSKYEAQGSLTKSHSAQQPVLVSQTLDIHKRMQPLHIQIKSPQESTGDPGNSSSVSEGKGSSERGSPIEKYMRPAKHPNYSPPGSPIEKYQYXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXLSHVPGLPNPCQNYVPYPTFNLPPHFSAVGSDNDIPLDLAIKHSRPGPTANGASKEKTKAPPNVKNEGPLNVVKTEKVDRSTQDELXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXIQRGLHRNNAQVEKNGKPKE
>TTKB_DROME__P17789 RecName: Full=Protein tramtrack, beta isoform; AltName: Full=Repressor protein fushi tarazu; AltName: Full=Tramtrack p69;
XKMASQRFCXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXLKXXXXXXXXXXXXXXXXXXXXXXXXXLXXXXXXXXXXXXKGLTEVNDDKPSPAXXXXGXGATGSESTATTPQLQRIQPYLVPQRNRSQAGGLLASAANAGNTPTLPVQPSLLSSALMPKRKRGRPRKLSGSSNGTGNDYDDFDRENMMNDSSDLGNGKMCNESYSGNDDGSDDNQPNAGHTDDLNESRDSLPSKRSKNSKDHRVVSHHEDNSTSDGNDSDGEGLDTSYMEPQLMLDEYDEPVEFKYNPLTDNSSPTQDHTDGSHLNEQARQQAFLIAAQRKHXVETAAAXXXXXXXXXXXXXXXXXXXXXSXXSIPXLXPIGKVNAASTPLVSPAGSFSTATVKPRVQKRPKLGKQNGDVKPAVFSSQEYLDXYNSNXXXKLKAAGLSGSTPNLSAGLGTPSVKTKLNLSSNVGEGEAEGSVRDYCXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXAHVKIIHKIENPSTALXTVXXANLAGQPLGVSGASTPPPPDLSGQNSNQSLPATSNALSTXXXXXTXXXXGSLGPLTTSAPPXPXXXAQ
>ZEB1_HUMAN__P37275 RecName: Full=Zinc finger E-box-binding homeobox 1; AltName: Full=NIL-2-A zinc finger protein; AltName: Full=Negative regulator of IL2; AltName: Full=Transcription factor 8; Short=TCF-8;
XXDGPRCKRRKQANPRRNNVTNYNTVVETNSDSDDEDKLHIVEEESVTDAADCEGVPEDDLPTDQTVLPGRSSEREGNAKNCWEDDRKEGQEILGPEAQADEAGCTVKDDECESDAENEQNHDPNVEEFLQQQDTAVIFPEAPEEDQRQGTPEASGHDENGTPDAFSQLLTCPXXXXXXXXXXXXKEHIKYRXXXXXXXXXXXXXXXXXXXXTQLERHMTSHKSGRDQRHVTQSGXXXXXXXXXXXXXXXXXHHLKEHLRIHSGEKPYECPNCKKRFSHXGXYXXHIXSKKCISLIPVNGRPRTGLKTSQCSXPXLXASPGSPTRPQIRQKIENKPLQEQLSVNQIKTEPXDYEFXXIVVXSXIXXXXPLQNGVFTGGGPLQATSSPQGMVQXXVXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXLENNQANLASKEQETINASPIQQGGHSVISAISLPLXXXXXXXXIIINYSXEQPXQLQVVPQNLKKENPVATNSCKSEKLPEDLTVKSEKDKSFEGGVNXXXCXLXXXCPXXXNALPELKHYDLKQPTQXXXLPAAEAEKPESSVSSATGDGNLSPSQPPLKNLLSXXXXXXXXXXXXXXXEXSKIAXXXXXXXXXVKKXFEKMQAGQISVQSSEPSSPEPGKVNIPAKNNDQPQSANANEPQDSTVNLQSPLKMTNSPVLPVGSTTNGSRSSTPSPSPLNLSSSRNTQGYLYTAEGAQEEPQVEPLDLSLPKQQGELLERSTITSVYQNSVYSVQEEPLNLSCAKKEPQKDSCVTDSEPVVNVIPPSANXXNXAIPXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXTTVSPAVQEPPLKVIQPNGNQDERQDTSSEGVSNVEDQNDSDSTPPKKKMRKTENGMYACDLCDKIFQXSSSLLRHKYEHTGKRPHECGICKKAFKHKHHLIEHMRLHSGEKPYQCDKCGKRFSHSGSYSQHMNHRYSYCKREAEERDSTEQEEAGPEILSNEHVGARASPSQGDSDERESLTREEDEDSXKXXXXXDKXMXXLQXXKECEKPQGDEXXXXXXXXVXXXXVXXAXNXGXEAKTEGLMKDDRAESQASSLGQKVGESSEQVSEEKTNEA
>ZEB2_HUMAN__O60315 RecName: Full=Zinc finger E-box-binding homeobox 2; AltName: Full=Smad-interacting protein 1; Short=SMADIP1; AltName: Full=Zinc finger homeobox protein 1b;
XKQPIMADGPRCKRRKQANPRRKNVVNYDNVVDTGSETDEEDKLHIAEDDGIANPLDQETSPASVPNHESSPHVSQALLPREXXXDXIREGGVEHPWHNNEILQASVDGPEEMKEDYDTMGPEATIQTAINNGTVKNANCTSDFEEYFAKRKLEERDGHAVSIEEYLQRSDTAIIYPEAPEELSRLGTPEANGQEENDLPPGTPDAFAQLLTCXXXXXXXXXXXXXKEHIKYRHEXXXXXXXXXXXXXXXXXXTXLERHMVTHKPGTDQHQMLTQGAGNRKFKCTECGKXXXYXHHLKEHLRIHSGEKPYECPNCKKRFSHXGXYXXHIXSKKCIGLISVNGRMRNNIKTGSXPNXVXXSPTNSAITQLRNKLENGKPLSMSEQTGLLKIKTEXXXXXDXKVLMATXGFSGTSPFMNGGLGATSPLGVHPSAQSPMQHLGVGMEAPLLGFPTMNSNXSEVQKVLQIVDNTVSRQKMDCKAEEISKLKGYHMKDPCSQPEEQGVTSPNIPPVGLPVVSHNGATKSIIDYTLXXXXXXKACLQSLTTDSRRQISNIKKXXXXXLXXLVTXXKMIENHNXXXXXXCQXCXXSFXGXIXXHQHERYLXXXXEEIXXXLQPHENXVPNKAGXXXXXXXXXXXXVLSEXXMTSPINPYKXXXXXXXXXYAXXXXXXXXXXXKIXXXXXXXXXXXXXXXXQRKVYQYSNSRSPSLERSSKPLAPNSNPPTKDSLLPRSPVKPMDSITSPSIAELHNSVTNCDPPLRLTKPSHFTNIKPVEKLDHSRSNTPSPLNLSXTXXKNXHXXSYTPNSFSSEELQAEPLDLSLPKQMKEPKSIIATKNKTKASSISLDHNSVXXXXENSDEPLNLTFIKKEFSNSNNLDNKSTNPVFSMNPFSAKPLYTALPPQSAFPPATFMPPVQTSIPGLRPYPGLDQMSFLPHMAYTYPTGAATFADMQQRRKYQRKQGFQGELLDGAQDYMSGLDDMTDSDSCLSRKKIKKXXXGXXXXXLCXXXXXXXSSLLRHKYEHTGKRPHQCQICKKAFKHKHHLIEHSRLHSGEKPYQCDKCGKRFSHSGSYSQHMNHRYSYCKREAEEREAAEREAREKGHLEPTELLMNRAYLQSITPQGYSDSEERESMPRDGESEKEHEKEGEDGYGKLGRQDGDEXFXXXXXXSENKSMDTDPETIRDEEETGDHSMDDSSEDGKMETKSDHEEDNMEDGM
>ZFH1_DROME__P28166 RecName: Full=Zinc finger protein 1; AltName: Full=Zinc finger homeodomain protein 1;
XLSCLAPSSSRFGQEDTIIQQSMPSTSPFAMQFPSLASTLLHHNQSPKHSNPGSSGIQDAHPNQPGAAADAFLVKCXQCXXRFPEYQSLSEHIASEHPHDKLNCGAAQPESDAEDEQSNMSGSSRRYAKSPLASNNNSSTANANNNSTSSQSMNNNSELAKNHNSANKMSPMCSPGSLTPGDLFAQLQHPXXQLXPHLHAQFMXXXXSLAMQSARTASSPSQXXXXXLXXXXXLXXXXXHQMAMQQLLPPQLPGSNSSVGSNSAYDLDLSAPRSTSSPGSTTGDLSGAYPCMQCTASFASREQLEQHEQLHSPCGPXAXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXKEHVRIHSXXKPXXCDNCXKRXXHSGSFSSHMTSKKCISMGLKLNNNRALLKRLEKSPGSASSASRRSPSDHGKGKLPEQPSLPGLPHPMSYFASDAQVQGGSAAPAPFPPFXXXXXXXXXXXXXXXXXXXXXGLDPXXHPYSIQRLLQLSAAGQQQREXXRXEQXKXXQHDEEETPDEPKLVMDIEEPETKEMAPTPEATEAATPIKREESREASPDPESYRSSSQAIKQEQEPLNVAEERQTPVEEHAPVEHAADLRCSRCSKQFNHPTXXVXXXKXLXXXXKEELEQHFXXXQATSFALASASEXDXXDXXMDVXXEPRQESGERKVRVRTAINEEQXXXLKQHYSLNARPSRDEFRMIAARLXXXXXVVQVWFQNNRSRERKMQSFQNNQAAGAAPPMPIDSQASLTREDQPLDLSVKRDPLTPKSESSPPYIAPPSGEALNPEAINLSRKFSTSASMSPASISPSSAAALYFGAAPXXSXPNSQLDSTPRSGQAFPGLPPYMLPMSLPMEALFKMRPGGDFASNHALMNSIKLPDYRGTSLSPGGSEKRSWRDDDSRISHEDEFGAGVLMPPKPRRGKAETHGHAGDPDLPYVCDQCDKAFAKQSSLARHKYEHSGQRPYQCIECPKAFKHKHHLTEHKRLHSGEKPFQCSKCLKRXXHXGSYSQHMNHRYSYCKPYRE
>cbx4_XENLA__Q91647 SubName: Full=XPolycomb {ECO:0000313|EMBL:AAC59728.1};
XELPAVGEHXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXWEPEENXXDPRLLVAFQNRERQEQIMGYRKRGPKPKNNLVSMPSFARRSNVLSGLHDSSGENRTKLDLGPIPKSHQYQLNSKKHHQYQPSGKDHNEKHHSSNKKKYYYQLNSKKHHHYQPDPKLYEQYTIEKESQISTDVRNRHRDSLTHTQAADMGTQLKNGTDSVISGPERNGICNGVSSSPSTEMSSSPSTELSSSPSTELPSSGVGGKMKIVKNKNKNGRIVIVMSKYMENGMQSVKIKSSEEDCDMGDVRRRFDSPGTLNGDKTCTAQEEKTEHWKKRVESRVKIHEGSKSVDKGSVHLAGLRRTYSTASETLNDQPLQLTTKSSHVPMPNRTRSPVYAGEPYNDLVYTNPRKRCLSEANGNKELCKKTLTSRSVSAPGIVECKXGLTPLNVXLQEPDIILLDSDLDEXXDLRCVKSRCDSDQEVDKPEIQVTQNPQSVDVDVCEXXXXXXXXXXXXXXXXXXXXXXXXXXXITV
>CBX4_HUMAN__O00257-slimfinder Motifs
--------------------------------------------------------F--R-R--Q-MGYRK-G-KP------------------------------LDLG-------H-Y-L--K-H---------------------KY-Y-L--KKHH-Y--D----------------------------------------------------------------------------------------K-K-K-GRI-IV-SK--E-G----------------------------------------------------KRR----------------------------EQPL-LT-K----------------------------------------------------------C-K-LT----------------E-P-DL------------------D-PIDLRC-K-R-------------------------------------------------------------------------------
>CBX4_HUMAN__O00257-masked
XELPAVGEHXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXTWEPEENXXDPRLLIAFQNRERQEQLMGYRKRGPKPKPLVVQVPTFARRSNVLTGLQDSSTDNRAKLDLGAQGKGQGHQYELNSKKHHQYQPHSKERAGKPPPPGKSGKYYYQLNSKKHHPYQPDPKMYDLQYQGGHKEAPSPTCPDLGAKSHPPDKWAQGAGAKGYLGAVKPLAGAAGAPGKGSEKGPPNGMMPAPKEAVTGNGIGGKMKIVKNKNKNGRIVIVMSKYMENGMQAVKIKSGEVAEGEARSPSHKKRAADERHPPADRTFKKAAGAEEKKVEAPPKRREEEVSGVSDPQPQDAGSRKLSPTKEAFGEQPLQLTTKPDLLAWDPARNTHPPSHXPXPXPXXXXXXXXXXXHAVGLNLSHVRKRCLSETHGEREPCKKRLTARSISTPTCLGGSPAAERPADLPPAAALPQPEVILLDSDLDEPIDLRCVKTRSEAGEPPSSLQVKPETPASXXVXVXXXXAPTTTAEKPPAEAQDEPAESLSEFKPXXXXXXXXXXXXXXXXXXXXXYVTV
>CBX4_HUMAN__O00257 RecName: Full=E3 SUMO-protein ligase CBX4; EC=6.3.2.-; AltName: Full=Chromobox protein homolog 4; AltName: Full=Polycomb 2 homolog; Short=Pc2; Short=hPc2;
MELPAVGEHVFAVESIEKKRIRKGRVEYLVKWRGWSPKYNTWEPEENILDPRLLIAFQNRERQEQLMGYRKRGPKPKPLVVQVPTFARRSNVLTGLQDSSTDNRAKLDLGAQGKGQGHQYELNSKKHHQYQPHSKERAGKPPPPGKSGKYYYQLNSKKHHPYQPDPKMYDLQYQGGHKEAPSPTCPDLGAKSHPPDKWAQGAGAKGYLGAVKPLAGAAGAPGKGSEKGPPNGMMPAPKEAVTGNGIGGKMKIVKNKNKNGRIVIVMSKYMENGMQAVKIKSGEVAEGEARSPSHKKRAADERHPPADRTFKKAAGAEEKKVEAPPKRREEEVSGVSDPQPQDAGSRKLSPTKEAFGEQPLQLTTKPDLLAWDPARNTHPPSHHPHPHPHHHHHHHHHHHHAVGLNLSHVRKRCLSETHGEREPCKKRLTARSISTPTCLGGSPAAERPADLPPAAALPQPEVILLDSDLDEPIDLRCVKTRSEAGEPPSSLQVKPETPASAAVAVAAAAAPTTTAEKPPAEAQDEPAESLSEFKPFFGNIIITDVTANCLTVTFKEYVTV
>COM1_HUMAN__Q99708-slimfinder Motifs
---------------------------------------------------------------------------------------------------------------------------R-T--E-N-KL----------------------------------------R-R--E-PH----------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------D-PLDLS-R--------------------------------------------------------------------------------IK-E----------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------KRR----------------
>COM1_HUMAN__Q99708-masked
XNISGSSCGSPNSADTSSDFKDLWTKLKECHDXEVQGLQVKVTXXKXXRXXXXXRLXXFXTKNQQLREQQKVLHXXIKXXXXXXXXXXXXRCAVTEEHMRKKQQEFENIRQQNLKLITELMNERNTLQEENKKLSEQLQQKIENDQQHQAAELECEEDVIPDSPITAFSFSGVNRLRRKENPHVRYIEQTHTKLEHSVCANEMRKVSKSSTHPQHNPNENEILVADTYDQSQSPMAKAHGTSSYTPDKSSFNLATVVAETLGLGVQEESETQGPMSPLGDELYHCLEGNHKKQPFEESTRNTEDSLRFSDSTSKTPPQEELPTRVSSPVFGATSSIKSGLDLNTSLSPSLLQPGKKKHLKTLPFSNTCISRLEKTRSKSEDSALFTHHSXGSEVNKIIIQSSNKQILINKNISESLGEQNRTEYGKDSNTDKHLEPLKSLGGRTSKRKKTEXXSXHEVSCPQASFDKENAFPFPMDNQFSMNGDCVMDKPLDLSDRFSAIQRQEKSQGSETSKNKFRQVTLYEALKTIPKGFSSSRKASDGNCTLPKDSPGEPCSQECIILQPLNKCSPDNKPSLQIKEENAVFKIPLRPRESLETENVLDDIKSAGSHEPIKIQTRSDHGGCELASVLQLNXCRTGKIKSLQNNQDVSFENIQWSIDPGADLSQYKMDVTVIDTKDGSQSKLGGETVDMDCTLVSETVLLKMKKQEQKGEKSSNEERKMNDSLEDMFDRTTHEEYESCLADSFSQAADEEEELSTATKKLHTHGDKQDKVKQKAFVEPYFKGDERETSLQNFPHIEVVRKKEERRXXXXXXXXXXXXXYAXXPAXEREKKLASCSRHRFRYIPXNTPENFWEVGFPSTQTCMERGYIKEDLDPCPRPKRRQPYNAIFSPKGKEQKT
>COM1_HUMAN__Q99708 RecName: Full=DNA endonuclease RBBP8; EC=3.1.-.-; AltName: Full=CtBP-interacting protein; Short=CtIP; AltName: Full=Retinoblastoma-binding protein 8; Short=RBBP-8; AltName: Full=Retinoblastoma-interacting protein and myosin-like; Short=RIM; AltName: Full=Sporulation in the absence of SPO11 protein 2 homolog; Short=SAE2;
MNISGSSCGSPNSADTSSDFKDLWTKLKECHDREVQGLQVKVTKLKQERILDAQRLEEFFTKNQQLREQQKVLHETIKVLEDRLRAGLCDRCAVTEEHMRKKQQEFENIRQQNLKLITELMNERNTLQEENKKLSEQLQQKIENDQQHQAAELECEEDVIPDSPITAFSFSGVNRLRRKENPHVRYIEQTHTKLEHSVCANEMRKVSKSSTHPQHNPNENEILVADTYDQSQSPMAKAHGTSSYTPDKSSFNLATVVAETLGLGVQEESETQGPMSPLGDELYHCLEGNHKKQPFEESTRNTEDSLRFSDSTSKTPPQEELPTRVSSPVFGATSSIKSGLDLNTSLSPSLLQPGKKKHLKTLPFSNTCISRLEKTRSKSEDSALFTHHSLGSEVNKIIIQSSNKQILINKNISESLGEQNRTEYGKDSNTDKHLEPLKSLGGRTSKRKKTEEESEHEVSCPQASFDKENAFPFPMDNQFSMNGDCVMDKPLDLSDRFSAIQRQEKSQGSETSKNKFRQVTLYEALKTIPKGFSSSRKASDGNCTLPKDSPGEPCSQECIILQPLNKCSPDNKPSLQIKEENAVFKIPLRPRESLETENVLDDIKSAGSHEPIKIQTRSDHGGCELASVLQLNPCRTGKIKSLQNNQDVSFENIQWSIDPGADLSQYKMDVTVIDTKDGSQSKLGGETVDMDCTLVSETVLLKMKKQEQKGEKSSNEERKMNDSLEDMFDRTTHEEYESCLADSFSQAADEEEELSTATKKLHTHGDKQDKVKQKAFVEPYFKGDERETSLQNFPHIEVVRKKEERRKLLGHTCKECEIYYADMPAEEREKKLASCSRHRFRYIPPNTPENFWEVGFPSTQTCMERGYIKEDLDPCPRPKRRQPYNAIFSPKGKEQKT
>E1A_ADE02__P03254-slimfinder Motifs
-RHI--H-----------------------------------------LDVT-------------------------------------------------------------------IDLT----------------------------------------------------------------------------------------------------------------------------------------------------------QPLDLS-KR-R-
>E1A_ADE02__P03254-masked
XRHIICHGGXXXXXXXASXXXQXIEEVLADNLPPPSHFEPPTLHELYDLDVTAPEDPNEEAVSQIFPDSVMLAVQEGIDLLTFPPAPGSPEPPHLSRQPEQPEQRALGPVSMPNLVPEVIDLTCHEAGFPPSDDEDXXGXEFVLDYVEXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXSPVSEPEPEPEPEPEPARPTRRPKLVPAILRRPTSPVSRECNSSTDSCDSGPSNTPPEIHPVVPLCPIKPVAVRXXGRRXXXECIEDLLNXXGQPLDLSCKRPRP
>E1A_ADE02__P03254 RecName: Full=Early E1A protein {ECO:0000305}; AltName: Full=Early E1A 32 kDa protein;
MRHIICHGGVITEEMAASLLDQLIEEVLADNLPPPSHFEPPTLHELYDLDVTAPEDPNEEAVSQIFPDSVMLAVQEGIDLLTFPPAPGSPEPPHLSRQPEQPEQRALGPVSMPNLVPEVIDLTCHEAGFPPSDDEDEEGEEFVLDYVEHPGHGCRSCHYHRRNTGDPDIMCSLCYMRTCGMFVYSPVSEPEPEPEPEPEPARPTRRPKLVPAILRRPTSPVSRECNSSTDSCDSGPSNTPPEIHPVVPLCPIKPVAVRVGGRRQAVECIEDLLNESGQPLDLSCKRPRP
>ELK3_HUMAN__P41970-slimfinder Motifs
----------------------------------------------------------------------------------------------------------------------------------S--R--Y-HSGLY-----------------IK-E--E---------------------------------------------------------------------------------------------------------PL-LS-------------------------PL-LS-----------------------------------------------------------------------------------------PV-LS------
>ELK3_HUMAN__P41970-masked
XESAXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXPHXXXXSRESLLLQDSDCKASPEGREAHKHGLAALRSTSRNEYIHSGLYSSFTINSLQNPPDAFKAIKTEKLEEPPEDSPPVEEVRTVIRFVTNKTDKHVTRPVVSLPSXXXXXXXXAXXXXXXXXXXXXXXXXNXAXISXAXPFXXRXPXLSPNSPLPSEHRSLFLEAACHDSDSLEPLNLSSGSKTKSPSLPPKAKKPKGLEISAPPLVLSGTDIGSIALNSPALPSXSLTPAFFTAQTPNGXLLTPXXXXXXXXXXXXXXXXXPLSPARLQGPSTLFQFPTLLNGHMPVPIPSLDRAASPVLLSSNSQKS
>ELK3_HUMAN__P41970 RecName: Full=ETS domain-containing protein Elk-3; AltName: Full=ETS-related protein ERP; AltName: Full=ETS-related protein NET; AltName: Full=Serum response factor accessory protein 2; Short=SAP-2; Short=SRF accessory protein 2;
MESAITLWQFLLQLLLDQKHEHLICWTSNDGEFKLLKAEEVAKLWGLRKNKTNMNYDKLSRALRYYYDKNIIKKVIGQKFVYKFVSFPEILKMDPHAVEISRESLLLQDSDCKASPEGREAHKHGLAALRSTSRNEYIHSGLYSSFTINSLQNPPDAFKAIKTEKLEEPPEDSPPVEEVRTVIRFVTNKTDKHVTRPVVSLPSTSEAAAASAFLASSVSAKISSLMLPNAASISSASPFSSRSPSLSPNSPLPSEHRSLFLEAACHDSDSLEPLNLSSGSKTKSPSLPPKAKKPKGLEISAPPLVLSGTDIGSIALNSPALPSGSLTPAFFTAQTPNGLLLTPSPLLSSIHFWSSLSPVAPLSPARLQGPSTLFQFPTLLNGHMPVPIPSLDRAASPVLLSSNSQKS
>EVI1_HUMAN__Q03112-slimfinder Motifs
-----------------ER-Y-C-DCD--F----------------------------------------------C--CD--F------------H--ER-Y-CDQC-KA----------------GK-YEC-NC-K-FT--------------G-R-H-CPECGK-FA-SS-LK-HK-IH---------------------------------------------------K-RR----------------------------------------------------------------------------------------------------------------------------------PVEL-----------------------------------------------------------------------------------------------------------------------------------------------------------------------------------E-P-DLT-KR------------------T-QDQPLDLSM--------------------------------------------------------------------------------------------------------------------------------------------------------------LTRHLR-HTGE-PY-C-YCDRSFS-S--L----------------------------L-RHLK-H-----------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------
>EVI1_HUMAN__Q03112-masked
XKSEDYPHETMAPDIHEERQYRCEDCDQLFESKAELADHQKFPCSTPHSAFSMVEEDFQQKLESENDLQEIHTIQECKECDQVFPDLQSLEKHMLSHTEEREYKCDQCPKAXXWKSNLIRHQMSHDSGKHYECENCAKVFTDPSNLQRHIRSQHVGARAHACPECGKTFATSSGLKQHKHIHXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXNKHRRFCEGXXHFXXXXFFGQGISLPGTPAMDKTSMVNMSHANPGLADYFGANRHPAGLTFPTAPXXXXSXPGLFPXGLYHRPPLIPASSPVKGLSSTEQTNKSQSPLMTHPQILPATQDILKALSKHPSVGDNKPVELQPERSSEERPFEKISDQSESSDLDDVSTPSGSDLETTSGSDLESDIESDKEKFKENGKMFKDKVSPLQNLASINNKKEYSNHSIFSPSLEEQTAVSGAVNXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXQSMYPFPDRDLRSLPLKMEPQSPGEVKKLQKGSSESPFDLTTKRKDEKPLTPVPSKPPVTPATSQDQPLDLSMGSRSRASGTKLTEPRKNHVFGGKKGSNVESRPASDGSLQHARPTPFFMDPIYRVEKRKLTDPLEALKEKYLRPSPGFLFHPQFQLPDQRTWMSAIENMAEKLESFSALKPEASELLQSVPSMFNFRAPPNALPENLLRKGXERXXXRYCXXXXXXXANLTRHLRTHTGEQPYRCKYCDRSFXISSNLQRHVRNIHNXEKXXXXXXXXXXXXXXTNLDRHLKKHENGNMSGTATSSPHSELESTGAILDDKEDAYFTEIRNFIGNSNHGSQSPRNVEERMNGSHFKDEKALVTSQNSDLLDDEEVEDEVLLDEEDEDNDITGKTGKEPVTSNLHEGNPEDDYEETSALEMSCKTSPVRYKEEEYKSGLSALDHIRHFTDSLKMRKMEDNQYSEAELSSFSTSHVPEELKQPLHRKSKSQAYAMMLSLSDKESLHSTXHXXSNVWHSMARAAAESSAIQSISHV
>EVI1_HUMAN__Q03112 RecName: Full=MDS1 and EVI1 complex locus protein EVI1; AltName: Full=Ecotropic virus integration site 1 protein homolog; Short=EVI-1;
MKSEDYPHETMAPDIHEERQYRCEDCDQLFESKAELADHQKFPCSTPHSAFSMVEEDFQQKLESENDLQEIHTIQECKECDQVFPDLQSLEKHMLSHTEEREYKCDQCPKAFNWKSNLIRHQMSHDSGKHYECENCAKVFTDPSNLQRHIRSQHVGARAHACPECGKTFATSSGLKQHKHIHSSVKPFICEVCHKSYTQFSNLCRHKRMHADCRTQIKCKDCGQMFSTTSSLNKHRRFCEGKNHFAAGGFFGQGISLPGTPAMDKTSMVNMSHANPGLADYFGANRHPAGLTFPTAPGFSFSFPGLFPSGLYHRPPLIPASSPVKGLSSTEQTNKSQSPLMTHPQILPATQDILKALSKHPSVGDNKPVELQPERSSEERPFEKISDQSESSDLDDVSTPSGSDLETTSGSDLESDIESDKEKFKENGKMFKDKVSPLQNLASINNKKEYSNHSIFSPSLEEQTAVSGAVNDSIKAIASIAEKYFGSTGLVGLQDKKVGALPYPSMFPLPFFPAFSQSMYPFPDRDLRSLPLKMEPQSPGEVKKLQKGSSESPFDLTTKRKDEKPLTPVPSKPPVTPATSQDQPLDLSMGSRSRASGTKLTEPRKNHVFGGKKGSNVESRPASDGSLQHARPTPFFMDPIYRVEKRKLTDPLEALKEKYLRPSPGFLFHPQFQLPDQRTWMSAIENMAEKLESFSALKPEASELLQSVPSMFNFRAPPNALPENLLRKGKERYTCRYCGKIFPRSANLTRHLRTHTGEQPYRCKYCDRSFSISSNLQRHVRNIHNKEKPFKCHLCDRCFGQQTNLDRHLKKHENGNMSGTATSSPHSELESTGAILDDKEDAYFTEIRNFIGNSNHGSQSPRNVEERMNGSHFKDEKALVTSQNSDLLDDEEVEDEVLLDEEDEDNDITGKTGKEPVTSNLHEGNPEDDYEETSALEMSCKTSPVRYKEEEYKSGLSALDHIRHFTDSLKMRKMEDNQYSEAELSSFSTSHVPEELKQPLHRKSKSQAYAMMLSLSDKESLHSTSHSSSNVWHSMARAAAESSAIQSISHV
>FOG1_HUMAN__Q8IX07-slimfinder Motifs
-------------------------------------------------------------------------------------------------------------------------V--R--SP------------------------------------------------------------------------VK-EP-E-----------------------------------------------------------------------------------C--P-C-K------------------------------------------------------------------------------------------------------------------------------------------------------------------IK-E--E-----------------------------------------------------------------------S-I-AKMSELVH-RL--G-----------------------------------------YC--R---------------------------------------------------------------------------------C--C--RFS-------HK-YYCA-R----------------------------------------------------------------------------------D-PIDLS-K-RR-----------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------
>FOG1_HUMAN__Q8IX07-masked
XSRRKQSNPRQIKRSLGDMEAREEVQLVGASHMEQKATAPEAPSPPSADVNSPXXLXXXTSPGGPKELEGQEPEPRPTEEEPGSPWSGPDELEPVVQDGQRRIRARLSLATGLSWGPFHGSVQTRASSPRQAEPSPALTLXXXXXXXXXXXXPQAXXEAEANTEXHRKDDALWCRVTKPVXXGGLLSVLLTAEPHSTPGHPVKKEPAEPTCPAPAHDLQLLPQQAGXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXGTGSPAAAATDEKPKETYPNERVCPFPQCRKXXXSASSLEIHMRSXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXQPGSKGEIYSPGAGHPATKLPPDSLGSFQQQHTALQGPLASADLGLAPTPSPGLDRKALAEATNGEARAEPLAQNGGSSEPPAAPRSIKVEAVEEPEAAPILGPGEPGPQAPSRTPSPRSPAPARVKAELSSPTPGSSPVPGELGLAXXXFXXXYVFGPDAAPPASEILAKMSELVHSRLQQGAXAXAXGAQTGLFPGXXXXXXXXXXXXXXXXXXXXXXXXXXYCSGRRAPEDAPAARRPKAPPGPARAPPGQPAEPDAPRSSPGPGAREEGAGGAATPEDGAGGRGSEGSQSPGSSVDDAEDDPSRTLCEACNIRFSRHEXXTVHKRYYCASRHDPPPRRPAAXXGXXGXAAXPAPSPAAPVRTXXXRKLYELHAAGAPXXXXXGHAPAPESPRPGSGSGSGPGLAPARSPGPAADGPIDLSKKPRRPLPGAPAPALAXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXLLEXFXXXXXXLLGAPLAGPGVEARTPADRGPSPAPAPAASPQPGSRGPRDGLGPEXQEXXXGXXXSPAAAPEAVXXXXAXPSYSDKGVQTPSKGTPAPLPNGNHXXXXXXXXXXXXXXXXXXXXXXXXXXXAAEHVK
>FOG1_HUMAN__Q8IX07 RecName: Full=Zinc finger protein ZFPM1; AltName: Full=Friend of GATA protein 1; Short=FOG-1; Short=Friend of GATA 1; AltName: Full=Zinc finger protein 89A; AltName: Full=Zinc finger protein multitype 1;
MSRRKQSNPRQIKRSLGDMEAREEVQLVGASHMEQKATAPEAPSPPSADVNSPPPLPPPTSPGGPKELEGQEPEPRPTEEEPGSPWSGPDELEPVVQDGQRRIRARLSLATGLSWGPFHGSVQTRASSPRQAEPSPALTLLLVDEACWLRTLPQALTEAEANTEIHRKDDALWCRVTKPVPAGGLLSVLLTAEPHSTPGHPVKKEPAEPTCPAPAHDLQLLPQQAGMASILATAVINKDVFPCKDCGIWYRSERNLQAHLLYYCASRQGTGSPAAAATDEKPKETYPNERVCPFPQCRKSCPSASSLEIHMRSHSGERPFVCLICLSAFTTKANCERHLKVHTDTLSGVCHSCGFISTTRDILYSHLVTNHMVCQPGSKGEIYSPGAGHPATKLPPDSLGSFQQQHTALQGPLASADLGLAPTPSPGLDRKALAEATNGEARAEPLAQNGGSSEPPAAPRSIKVEAVEEPEAAPILGPGEPGPQAPSRTPSPRSPAPARVKAELSSPTPGSSPVPGELGLAGALFLPQYVFGPDAAPPASEILAKMSELVHSRLQQGAGAGAGGAQTGLFPGAPKGATCFECEITFSNVNNYYVHKRLYCSGRRAPEDAPAARRPKAPPGPARAPPGQPAEPDAPRSSPGPGAREEGAGGAATPEDGAGGRGSEGSQSPGSSVDDAEDDPSRTLCEACNIRFSRHETYTVHKRYYCASRHDPPPRRPAAPPGPPGPAAPPAPSPAAPVRTRRRRKLYELHAAGAPPPPPPGHAPAPESPRPGSGSGSGPGLAPARSPGPAADGPIDLSKKPRRPLPGAPAPALADYHECTACRVSFHSLEAYLAHKKYSCPAAPPPGALGLPAAACPYCPPNGPVRGDLLEHFRLAHGLLLGAPLAGPGVEARTPADRGPSPAPAPAASPQPGSRGPRDGLGPEPQEPPPGPPPSPAAAPEAVPPPPAPPSYSDKGVQTPSKGTPAPLPNGNHRYCRLCNIKFSSLSTFIAHKKYYCSSHAAEHVK
>FOG2_HUMAN__Q8WW38-slimfinder Motifs
-------------------------------------------------------------------------------------------------D-P-EL--------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------C--P-C-KSFS-------HL--HS--K-----------------------------------------------------L--H--LH------------------------------------------------------------------------------------IK-EP---------------------------------------S-I-AKMSELVHRRL-HG-S---------------------------------------------------------------------------------------------------------------------------------------------------------------------------HK-YYCATR-D-PL--S---------------KRR------------------------------------------------------------------------------------------------------------------------------------------------------------------------------IK-E------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------
>FOG2_HUMAN__Q8WW38-masked
XSRRKQSKPRQIKRPLEDAIEDXXXXCPSXETDIISKGDFPLEESFSTEFGPENLSCEEVEYFCNKGDDEGIQETAESDGDTQSEKPGQPGVETDDWDGPGELEVFQKDGERKIQSRQQLPVGTTWGPFPGKMDLNNNSLKTKAQVPMVLTAXXXXXXXVTWQXXXXXXXNXXXXXXXXXXXXXTTXXXXXXXXXXXXXXXXXXXXXXXXQMTLXXGXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXMYXCXXRQREAAPVSEENEDSAHQISSLCPFPQCTKSFSNARALEMHLNSHSGVKMEEFLXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXTXRELLQHQELHVPSGKLPRESDMEHSPSATEDSLQPATDLLTRSELPQSQKAMQTKDASSDTELDKCEKKTQLFLTNQRPEIQPTTNKQSFSYTKIKSEPSSPRLASSPVQPNIGPSFPVGPFLSQFSFPQDITMVPQASEILAKMSELVHRRLRHGSSSYPPVIYSXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXRWQQMAKSPEFPSVSEKMPEALSPNTGQTSINLLNPAAHSADPENPLLQTSCINSSTVLDLIGPNGKGHDKDFSTQTKKLSTSSNNDDKINGKPVDVKNPSVPLVDGESDPNKTTCEACNIXXXXXXXXXXHKQYYCATRHDPPLKRSASNKVPAMQRTMRTRKRRKMYEMCLPEQEQRPPLVQQRFLDVANLNNPCTSTQEPTEGLGECYHXXXXXXXXXVXXXXXXXXXXXXXXXXXXXXXXXXSXSXXEMXXXXXXXKKCLSQSERTTTSPKRXXXXXXXXXXXXXXXXXXXXXXXXQNFCPVTAHQRNDLGQLDGKVFPNPESERNSPDVSYERSIIKCEKNGNLKQPSPNGNLFSSHLAXXXXXXXXXXXXQLXXXXEEXXXXXXPQXXXXXXXXKAXXXDQLSPYYGIKPSDYISGSLVIHNTDIEQSRNAENESPKGQASSNGCAALKKDSLPLLPKNRGMVIVNGGLKQDERPAANPQQENISQNPQHEDDHKSPSWISENPLAANENVSPGIPSAEEQLSSIAKGVNGSSQAXTXXXXXXXXXXXXXXXXXXXXXXXXXXXXHAAEHVK
>FOG2_HUMAN__Q8WW38 RecName: Full=Zinc finger protein ZFPM2; AltName: Full=Friend of GATA protein 2; Short=FOG-2; Short=Friend of GATA 2; Short=hFOG-2; AltName: Full=Zinc finger protein 89B; AltName: Full=Zinc finger protein multitype 2;
MSRRKQSKPRQIKRPLEDAIEDEEEECPSEETDIISKGDFPLEESFSTEFGPENLSCEEVEYFCNKGDDEGIQETAESDGDTQSEKPGQPGVETDDWDGPGELEVFQKDGERKIQSRQQLPVGTTWGPFPGKMDLNNNSLKTKAQVPMVLTAGPKWLLDVTWQGVEDNKNNCIVYSKGGQLWCTTTKAISEGEELIAFVVDFDSRLQAASQMTLTEGMYPARLLDSIQLLPQQAAMASILPTAIVNKDIFPCKSCGIWYRSERNLQAHLMYYCSGRQREAAPVSEENEDSAHQISSLCPFPQCTKSFSNARALEMHLNSHSGVKMEEFLPPGASLKCTVCSYTADSVINFHQHLFSHLTQAAFRCNHCHFGFQTQRELLQHQELHVPSGKLPRESDMEHSPSATEDSLQPATDLLTRSELPQSQKAMQTKDASSDTELDKCEKKTQLFLTNQRPEIQPTTNKQSFSYTKIKSEPSSPRLASSPVQPNIGPSFPVGPFLSQFSFPQDITMVPQASEILAKMSELVHRRLRHGSSSYPPVIYSPLMPKGATCFECNITFNNLDNYLVHKKHYCSSRWQQMAKSPEFPSVSEKMPEALSPNTGQTSINLLNPAAHSADPENPLLQTSCINSSTVLDLIGPNGKGHDKDFSTQTKKLSTSSNNDDKINGKPVDVKNPSVPLVDGESDPNKTTCEACNITFSRHETYMVHKQYYCATRHDPPLKRSASNKVPAMQRTMRTRKRRKMYEMCLPEQEQRPPLVQQRFLDVANLNNPCTSTQEPTEGLGECYHPRCDIFPGIVSKHLETSLTINKCVPVSKCDTTHSSVSCLEMDVPIDLSKKCLSQSERTTTSPKRLLDYHECTVCKISFNKVENYLAHKQNFCPVTAHQRNDLGQLDGKVFPNPESERNSPDVSYERSIIKCEKNGNLKQPSPNGNLFSSHLATLQGLKVFSEAAQLIATKEENRHLFLPQCLYPGAIKKAKGADQLSPYYGIKPSDYISGSLVIHNTDIEQSRNAENESPKGQASSNGCAALKKDSLPLLPKNRGMVIVNGGLKQDERPAANPQQENISQNPQHEDDHKSPSWISENPLAANENVSPGIPSAEEQLSSIAKGVNGSSQAPTSGKYCRLCDIQFNNLSNFITHKKFYCSSHAAEHVK
>HAIR_DROME__P14003-slimfinder Motifs
----------------------------------------KRRR--------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------QPL-L--K--IK-E-------
>HAIR_DROME__P14003-masked
XVTGVTAANMTNVLGTAVVPAQLKETPLKSDRRSNKPIMEKRRRARINNCLNELKTLILDATKKDPARHSKLEKADILEKTVKHLQELQRQQAAMQQAADPKIVNKFKAGFXXCXXEVSRFPGIEPAQRRRLLQHLSNCINGVKTELHQXXRXXXXQSIHAQMLPSPPSSPEQDSQQGAAAPYLFGIQQTASXXFLPNGMQVIPTKLPNGSIALVLPQSLPXXXXXXLLXHXXXQXXXAVXXXXXXXXXAQQQPMLVSMPQRTASTGSAXXHXSAGYESAPGXXXXCSYAPPSPANSSYEPMDIKPSVIQRVPMEQQPLSLVIKKQIKEEEQPWRPW
>HAIR_DROME__P14003 RecName: Full=Protein hairy;
MVTGVTAANMTNVLGTAVVPAQLKETPLKSDRRSNKPIMEKRRRARINNCLNELKTLILDATKKDPARHSKLEKADILEKTVKHLQELQRQQAAMQQAADPKIVNKFKAGFADCVNEVSRFPGIEPAQRRRLLQHLSNCINGVKTELHQQQRQQQQQSIHAQMLPSPPSSPEQDSQQGAAAPYLFGIQQTASGYFLPNGMQVIPTKLPNGSIALVLPQSLPQQQQQQLLQHQQQQQQLAVAAAAAAAAAAQQQPMLVSMPQRTASTGSASSHSSAGYESAPGSSSSCSYAPPSPANSSYEPMDIKPSVIQRVPMEQQPLSLVIKKQIKEEEQPWRPW
>HDAC4_HUMAN__P56524-slimfinder Motifs
----------S--DQPVEL-------------------PL-VA----PMDL--------------------------------------------------------------------------------------------------Q-L--L-NK-K-K-SAV-S--VK-KL------------HR-L-H--S------------------------------------------FPLRKTASEPNLKLRSRLKQKVAERRSSPL-RRK-----------PLDVT---------------------------------------------------------------------------------------------------------------------------------------------------------------------HKLR-HRPL-RTQS------------------H-QFL-K-----------------------------------------------------------------VK-EP-E-------------------------------L-E--RIH--------------------HR-L-R--S-------------------------------K-QC-CG--S-HPEHAGRIQSIWSRLQE-GL---C-C-R----------------H--LY-------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------
>HDAC4_HUMAN__P56524-masked
XSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAXSAVPMDLRLDHQFSLPVAEPALXEXQXQQEXXALXXXXXXXXXXLIXEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGXLXLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQXXHXQFLEKHKQXFXXXXLQMNKIIPKPSEPARQPESHPEXTXXXLREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDXXXAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDXXXLKHQCTCGSSSSHPEHAGRIQSIWSRLQEXGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKXXXXXXXXXXXXXXXXXXXXXXXTXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXFAVVRPPGHHAEXSTPXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXGTQQAFYSDPXXLXXXXHRYXXGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPXXXAXXXXXXXXXXXXXXXXXXXXXXXXXXXFXXXXXXPTPXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXLGNXXXPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEXPMXXEPPL
>HDAC4_HUMAN__P56524 RecName: Full=Histone deacetylase 4; Short=HD4; EC=3.5.1.98;
MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL
>HDAC5_HUMAN__Q9UQL6-slimfinder Motifs
-------------------------------------------------------PVEL------------------------------------------------------------------------------------------------------QQLL-LRNK-K-KESAI-S--VK-RL------------------------------------------------------------S--DFPLRKTASEPNLKVRSRLKQKVAERRSSPL-RRK-------------------------------------------------------------------PLD-S------------------------------------------------------------------------------------------------------------------------------------HRPL-RTQS------------------H-QFL-K--------------------------------------------------------------------------------VK-E--E--------------------------QPL-V---PL-LA---H--L-RTQ----------S--DQPV--------------------------HP-HAGRIQSIWSRLQE-GL------------------------H--LY----------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------
>HDAC5_HUMAN__Q9UQL6-masked
XNSPNESDGMSGREPSLEILPRTSLHSIPVTVEVKPVLPRAMPSSMGXXXXGSPSPVELRGALVGSVDPTLREQQLQQELLALXXXXXXXXXLLFAEFQKQHDHLTRQHEVQLQKHLKQQQEMLAAKQQQEMLAAKRQQELEQXRXREXQRQEELEKQRLEQQLLILRNKEKSKESAIASTEVKLRLQEFLLSKSKEPTPGGLNHSLPQHPKCWGAHHASLDQSSPPQSGPPGTPPSYKLPLPGPYDSRDDFPLRKTASEPNLKVRSRLKQKVAERRSSPLLRRKDGTVISTFKKRAVEITGAGPGASSVCNSAPGSGPSXPNXXHSTIAENGFTGSVPNIPTEMLPQHRALPLDSSPNQFSLYTSPSLPNISLGLQATVTVTNSHLTASPKLSTQQEAERQALQSLRQGGTLTGKFMSTSXXXGCLLGVALEGDXSPHGHXSLLQHVLLXXXXXXXXTLIAVPLHGQSPLVTGERVATSMRTVGKLPRHRPLSRTQSSPLPQSPQALQXLVMXXXHXQFLEKQKXXXLQLGKILTKTGELPRQPTTHPEXTXXXLTEQQEVLLGEGALTMPREGSTESESTQEDLXXXDXXDDGXXXEDCIQVKDEEGESGAEEGPDLEEPGAGYKKLFSDAQPLQPLQVYQAPLSLATVPHQALGRTQSSPAAPGGMKSPPDQPVKHLFTTGVVXXXXXXXXXXXCXXTHVHPXHAGRIQSIWSRLQEXGLLSKCERIRGRKATLDEIQTXHSEYHTLLYGTSPLNRQKLDSKKLLGXIXQKXXXXLPCGXXXXXSDTVWNEMXSXXXXXXXXXXXXXXXXXXXXXXXXXXXXIIRPPGHHXXXXTXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXTQQAXYNDPXXXXXXXXXXXXXNFFPGSGAPEEVGXXPXVGYNVNVAWTGGXXXPXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXVXXXXXXXXXXXXXXXXXXXXXXXXXXXQXFAXGXGRSLREAQAGETEEAETVSAMALLSVGAEQXQXXXAREHSPRPAEEPMEQEPAL
>HDAC5_HUMAN__Q9UQL6 RecName: Full=Histone deacetylase 5; Short=HD5; EC=3.5.1.98; AltName: Full=Antigen NY-CO-9;
MNSPNESDGMSGREPSLEILPRTSLHSIPVTVEVKPVLPRAMPSSMGGGGGGSPSPVELRGALVGSVDPTLREQQLQQELLALKQQQQLQKQLLFAEFQKQHDHLTRQHEVQLQKHLKQQQEMLAAKQQQEMLAAKRQQELEQQRQREQQRQEELEKQRLEQQLLILRNKEKSKESAIASTEVKLRLQEFLLSKSKEPTPGGLNHSLPQHPKCWGAHHASLDQSSPPQSGPPGTPPSYKLPLPGPYDSRDDFPLRKTASEPNLKVRSRLKQKVAERRSSPLLRRKDGTVISTFKKRAVEITGAGPGASSVCNSAPGSGPSSPNSSHSTIAENGFTGSVPNIPTEMLPQHRALPLDSSPNQFSLYTSPSLPNISLGLQATVTVTNSHLTASPKLSTQQEAERQALQSLRQGGTLTGKFMSTSSIPGCLLGVALEGDGSPHGHASLLQHVLLLEQARQQSTLIAVPLHGQSPLVTGERVATSMRTVGKLPRHRPLSRTQSSPLPQSPQALQQLVMQQQHQQFLEKQKQQQLQLGKILTKTGELPRQPTTHPEETEEELTEQQEVLLGEGALTMPREGSTESESTQEDLEEEDEEDDGEEEEDCIQVKDEEGESGAEEGPDLEEPGAGYKKLFSDAQPLQPLQVYQAPLSLATVPHQALGRTQSSPAAPGGMKSPPDQPVKHLFTTGVVYDTFMLKHQCMCGNTHVHPEHAGRIQSIWSRLQETGLLSKCERIRGRKATLDEIQTVHSEYHTLLYGTSPLNRQKLDSKKLLGPISQKMYAVLPCGGIGVDSDTVWNEMHSSSAVRMAVGCLLELAFKVAAGELKNGFAIIRPPGHHAEESTAMGFCFFNSVAITAKLLQQKLNVGKVLIVDWDIHHGNGTQQAFYNDPSVLYISLHRYDNGNFFPGSGAPEEVGGGPGVGYNVNVAWTGGVDPPIGDVEYLTAFRTVVMPIAHEFSPDVVLVSAGFDAVEGHLSPLGGYSVTARCFGHLTRQLMTLAGGRVVLALEGGHDLTAICDASEACVSALLSVELQPLDEAVLQQKPNINAVATLEKVIEIQSKHWSCVQKFAAGLGRSLREAQAGETEEAETVSAMALLSVGAEQAQAAAAREHSPRPAEEPMEQEPAL
>HDAC9_MOUSE__Q99N13-slimfinder Motifs
------------E-PM-L----PLDL-----------------------------------------------------------------------------------------------Q-L--L--K-R-R-RAV-S--VK-KL-------------------------------------------------------------S--DFPLRKTASEPNLKVRSRLKQKVAERRSSPL-RRK----------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------HKL--HRPL-RTQS----------------H-QFL-K-----------------------------------------------------------------------VK-EP-D-------------------------------------
>HDAC9_MOUSE__Q99N13-masked
XHSMISSVDVKSEVPMGLEPISPLDLRTDLRMMMPVVDPVVXXXXXXXXXXXXXXXXXXXXXXLIXXXXKQHENLTRQHQAQLQEHIKELLAIKQQQELLEKEQKLEQQRQEQEVERHRREQQLPPLRGKDRGRERAVASTEVKQKLQEFLLSKSATKDTPTNGKNHSVGRHPKLWYTAAHHTSLDQSSPPLSGTSPSYKYTLPGAQDSKDDFPLRKTASEPNLKVRSRLKQKVAERRSSPLLRRKDGNLVTSFKKRVFEVAESXVXXXXPGSGPSSPNNGPAGNVTENEASALPPTPHPEQLVPQQRILIHEDSMNLLSLYTSXXXXNITLGLPAVPSPLNASNSLKDKQKCETQMLRQGVPLPSQYGSXIAAXXSHVHVAMEGKPNSSHQALXQHXXLKEXMRQQKLLVAGGVPLHPQSPLATKERISPGIRGTHKLPRHRPLNRTQSAPLPQSTLAQLVIQXXHXQFLEKQKXYXXQIHMNKLLSKSIEQLKQPGSHLEXAXXELQGDQSMEDRAASKDNSARSDSSACVEDTLGQVGAVKVKEEPVDSDEDAQIQEMECGEQAAFMQQXXXXXXXXXXXIKVII
>HDAC9_MOUSE__Q99N13 RecName: Full=Histone deacetylase 9; Short=HD9; EC=3.5.1.98; AltName: Full=Histone deacetylase 7B; Short=HD7b; AltName: Full=Histone deacetylase-related protein; AltName: Full=MEF2-interacting transcription repressor MITR;
MHSMISSVDVKSEVPMGLEPISPLDLRTDLRMMMPVVDPVVREKQLQQELLLIQQQQQIQKQLLIAEFQKQHENLTRQHQAQLQEHIKELLAIKQQQELLEKEQKLEQQRQEQEVERHRREQQLPPLRGKDRGRERAVASTEVKQKLQEFLLSKSATKDTPTNGKNHSVGRHPKLWYTAAHHTSLDQSSPPLSGTSPSYKYTLPGAQDSKDDFPLRKTASEPNLKVRSRLKQKVAERRSSPLLRRKDGNLVTSFKKRVFEVAESSVSSSSPGSGPSSPNNGPAGNVTENEASALPPTPHPEQLVPQQRILIHEDSMNLLSLYTSPSLPNITLGLPAVPSPLNASNSLKDKQKCETQMLRQGVPLPSQYGSSIAASSSHVHVAMEGKPNSSHQALLQHLLLKEQMRQQKLLVAGGVPLHPQSPLATKERISPGIRGTHKLPRHRPLNRTQSAPLPQSTLAQLVIQQQHQQFLEKQKQYQQQIHMNKLLSKSIEQLKQPGSHLEEAEEELQGDQSMEDRAASKDNSARSDSSACVEDTLGQVGAVKVKEEPVDSDEDAQIQEMECGEQAAFMQQVIGKDLAPGFVIKVII
>HDAC7_MOUSE__Q8C2B3-slimfinder Motifs
----------------GSQ-QPMDLRV----------------------------------------PM-LS--------------Q-L--L-NK-K-K-SAV-S--VK-KL----------------------------------------------------------FPLRKT-SEPNLKLR------------------------------------------------------------------------------------------------------------------------------------------------------HRPL-RT-S---------------------------------------------K-R-R----------------------------------------------------------------------------HRPL-RTQS-------------------------------------K-QC-CG--S-HPEHAGRIQSIWSRLQE-GL---C-C-R----------------H--LY--------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------
>HDAC7_MOUSE__Q8C2B3-masked
XHSPGAGCPALQPDTPGSQPQPMDLRVGQRPTVEPPPEPALLTLQHPQRLHRHLFLAGLHQQQRSAEPMRLSMDPPMPELQGGQQEQELRQLLNKDKSKRSAVASSVVKQKLAEVILKKQQAALERTVHPSSPSIPYRTLEPLDTEGAARSVLSSFLPPVPSLPTEPPEHFPLRKTVSEPNLKLRYKPKKSLERRKNPLLRKESAPPSLRRRPAETLGDSXPXXXXTPASGCSSPNDSEHGPNPALGSEADGDRRTHSTLGPRGPVLGNPHAPLFLHHGLEPEAGGTLPSRLQPILLXXXXXXXXXXWTVXXXXXXXXHFAQPLLTTERLSGSGLHRPLNRTRSEPLPPSATASPLLAPLQPRQDRLKPHVQLIKPAISPPQRPAKPSEKPRLRQIPSAEDLETDGGGVGPMANDGLEHRESGRGPPEGRGSISLQQHQQVPPWEQQHLAGRLSQGSPGDSVLIPLAQVGHRPLSRTQSSPAAPVSLLSPEPTCQTQVLNSSETPATGLVYDSVMLKHQCSCGDNSKHPEHAGRIQSIWSRLQEXGLXSQCECLRGRKASLEELQSXHSERHVLLYXTNPLXXXXXDNGXXXXXXXXXXXXXXXXXXXXXXXDTIWNXLXSSXXXRWXXXXXXDXAFKXXXXXXXNGFAVVRPPGHHXXXXTXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXWDVXXXXGTQQTFYQDPSVLYISLHRHDDGNFFPGSGAVDEVGTGSGEGFNVNVAWAGGLDPPXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXPLSEESWKQKPNLSAXXSLXXXXXXXXXXXXXXXXXXXXXXXWLPRVPGADAEVEAVTXXXSLSVGILAEDRPSERLVXXXEPMNL
>HDAC7_MOUSE__Q8C2B3 RecName: Full=Histone deacetylase 7; Short=HD7; EC=3.5.1.98; AltName: Full=Histone deacetylase 7A; Short=HD7a;
MHSPGAGCPALQPDTPGSQPQPMDLRVGQRPTVEPPPEPALLTLQHPQRLHRHLFLAGLHQQQRSAEPMRLSMDPPMPELQGGQQEQELRQLLNKDKSKRSAVASSVVKQKLAEVILKKQQAALERTVHPSSPSIPYRTLEPLDTEGAARSVLSSFLPPVPSLPTEPPEHFPLRKTVSEPNLKLRYKPKKSLERRKNPLLRKESAPPSLRRRPAETLGDSSPSSSSTPASGCSSPNDSEHGPNPALGSEADGDRRTHSTLGPRGPVLGNPHAPLFLHHGLEPEAGGTLPSRLQPILLLDPSVSHAPLWTVPGLGPLPFHFAQPLLTTERLSGSGLHRPLNRTRSEPLPPSATASPLLAPLQPRQDRLKPHVQLIKPAISPPQRPAKPSEKPRLRQIPSAEDLETDGGGVGPMANDGLEHRESGRGPPEGRGSISLQQHQQVPPWEQQHLAGRLSQGSPGDSVLIPLAQVGHRPLSRTQSSPAAPVSLLSPEPTCQTQVLNSSETPATGLVYDSVMLKHQCSCGDNSKHPEHAGRIQSIWSRLQERGLRSQCECLRGRKASLEELQSVHSERHVLLYGTNPLSRLKLDNGKLTGLLAQRTFVMLPCGGVGVDTDTIWNELHSSNAARWAAGSVTDLAFKVASRELKNGFAVVRPPGHHADHSTAMGFCFFNSVAIACRQLQQHGKASKILIVDWDVHHGNGTQQTFYQDPSVLYISLHRHDDGNFFPGSGAVDEVGTGSGEGFNVNVAWAGGLDPPMGDPEYLAAFRIVVMPIAREFAPDLVLVSAGFDAAEGHPAPLGGYHVSAKCFGYMTQQLMNLAGGAVVLALEGGHDLTAICDASEACVAALLGNKVDPLSEESWKQKPNLSAIRSLEAVVRVHRKYWGCMQRLASCPDSWLPRVPGADAEVEAVTALASLSVGILAEDRPSERLVEEEEPMNL
>HIC1_HUMAN__Q14526-slimfinder Motifs
----------------------------------------------------------------------------------------------------------------------------------------------------------YC--R----------------------------------------------------------------------------------LDLS-K---------------------------------E-PL-L------------------------------------------------------------------------------------PL-LA---------------------------------------------------------------------------------------------------------------------------------RPY-C--CDKSYK----L--H-K-H---RP--C-ICGK-FT-----TRHMR-H--------------------LTEHMRIHS--KP--C--CG--------L--H-KMH------------------------------------------------------------------------------------------------------------------------
>HIC1_HUMAN__Q14526-masked
XTFPEADILLKSGECAGQTMLDTMEAPGHSRQLLLQLXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXYCHLRGXXXXXXGYAPYGRPGRGLRAATPVIQACYPSXVGXXXXXAAEXPSGPEAAVNTHCAELYAXXXGPAAXLCXXXXXXXXXCGLDLSKKSPPGSAAPERPLAERELPXRXDSXPSAGPAAYKEPPLALPSLPPLPFQKLEEAAPPSDPFRGGSGSPGPEPPGRPDGPSLLYRWMKHEPGLGSYGDELGRERGSPSERCEERGGDAAVSPGGPPLGLAPPPRYPGSLDGPXAXXDGDDYKSSSEETGSSEDPSPPGGHLEGYPCPHLAYGEPXXFXXXXXXXXXXXXXXXXXEQLNAHVEAHVXXXEALYGRAEXXEVXXGXAGLGPPFXXXGDKVAGAPGGLGEXLRPYRCASCDKSYKDPATLRQHEKTHWXTRPXPCTICGKKFTQRGTMTRHMRSHLXXXXXXXXXXXXXXXXXXRLTEHMRIHSXXKPXXCQVCGXXXXXXRNLISHMKMHAVXXAXXXXXXXAGLGGLPGVPGPDGKGKLDFPEGVFAVXRXTAEXLSLKQXDKAXXXXLLAQXXXXXXXXXXXXXXXXXXXXXXXXXXLXPDKAAEVLSQGAHLAAGPDGRTIDRFSPT
>HIC1_HUMAN__Q14526 RecName: Full=Hypermethylated in cancer 1 protein; Short=Hic-1; AltName: Full=Zinc finger and BTB domain-containing protein 29;
MTFPEADILLKSGECAGQTMLDTMEAPGHSRQLLLQLNNQRTKGFLCDVIIVVQNALFRAHKNVLAASSAYLKSLVVHDNLLNLDHDMVSPAVFRLVLDFIYTGRLADGAEAAAAAAVAPGAEPSLGAVLAAASYLQIPDLVALCKKRLKRHGKYCHLRGGGGGGGGYAPYGRPGRGLRAATPVIQACYPSPVGPPPPPAAEPPSGPEAAVNTHCAELYASGPGPAAALCASERRCSPLCGLDLSKKSPPGSAAPERPLAERELPPRPDSPPSAGPAAYKEPPLALPSLPPLPFQKLEEAAPPSDPFRGGSGSPGPEPPGRPDGPSLLYRWMKHEPGLGSYGDELGRERGSPSERCEERGGDAAVSPGGPPLGLAPPPRYPGSLDGPGAGGDGDDYKSSSEETGSSEDPSPPGGHLEGYPCPHLAYGEPESFGDNLYVCIPCGKGFPSSEQLNAHVEAHVEEEEALYGRAEAAEVAAGAAGLGPPFGGGGDKVAGAPGGLGELLRPYRCASCDKSYKDPATLRQHEKTHWLTRPYPCTICGKKFTQRGTMTRHMRSHLGLKPFACDACGMRFTRQYRLTEHMRIHSGEKPYECQVCGGKFAQQRNLISHMKMHAVGGAAGAAGALAGLGGLPGVPGPDGKGKLDFPEGVFAVARLTAEQLSLKQQDKAAAAELLAQTTHFLHDPKVALESLYPLAKFTAELGLSPDKAAEVLSQGAHLAAGPDGRTIDRFSPT
>IKZF1_HUMAN__Q13422-slimfinder Motifs
---------------------------------P-DLS--------------------------------------------------------------------------------------------------R-HT-ERPFQCNQCG----------RHIKLH-----------------------HLR-HS--KP--C-YCGRSYK----L-EHK-R-H-YL------------IK-E--------------------L--L--N--K-K----------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------HI--GEH-----
>IKZF1_HUMAN__Q13422-masked
XDADEGQDMSQVSGKESPPVSDTPDEGDEPMPIPEDLSTTSGGQQSSKSDRVVASNVKVETQSDEENGRACEMNGEECAEDLRMLDASGEKMNGSHRDQGSSALSGVGGIRXXXXXXXXXXXXXXXXXXXXXXXXXRSHTXERPFQCNQCGXXXXXXGNXLRHIKLHXXXXXXXXXXXXXXXXXXXXXXXHLRTHSXXKPXXCGYCGRSYKQRSSLEEHKERCHNYLESMGLPGTLYPVIKEETNHSEMAEDLCKIGSERSLVLDRLASNVAKRKSSMPQKFLGDKGLSDTPYDSSASYEKENEMMKSHVMDQAINNAINYLGAESLRPLVQTPPGGSEVVPVISPMYQLHKPLAEGTPRSNHSAQDSAVENLLLLSKAKLVPSEREASPSNSCQDSTDTESNNEEQRSGLIYLTNHIAPHARNGLSLKEEHRAYDLLRAASENSQDALRVVSTXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXFSSHITRGEHRFHMS
>IKZF1_HUMAN__Q13422 RecName: Full=DNA-binding protein Ikaros; AltName: Full=Ikaros family zinc finger protein 1; AltName: Full=Lymphoid transcription factor LyF-1;
MDADEGQDMSQVSGKESPPVSDTPDEGDEPMPIPEDLSTTSGGQQSSKSDRVVASNVKVETQSDEENGRACEMNGEECAEDLRMLDASGEKMNGSHRDQGSSALSGVGGIRLPNGKLKCDICGIICIGPNVLMVHKRSHTGERPFQCNQCGASFTQKGNLLRHIKLHSGEKPFKCHLCNYACRRRDALTGHLRTHSVGKPHKCGYCGRSYKQRSSLEEHKERCHNYLESMGLPGTLYPVIKEETNHSEMAEDLCKIGSERSLVLDRLASNVAKRKSSMPQKFLGDKGLSDTPYDSSASYEKENEMMKSHVMDQAINNAINYLGAESLRPLVQTPPGGSEVVPVISPMYQLHKPLAEGTPRSNHSAQDSAVENLLLLSKAKLVPSEREASPSNSCQDSTDTESNNEEQRSGLIYLTNHIAPHARNGLSLKEEHRAYDLLRAASENSQDALRVVSTSGEQMKVYKCEHCRVLFLDHVMYTIHMGCHGFRDPFECNMCGYHSQDRYEFSSHITRGEHRFHMS
>IKZF4_HUMAN__Q9H2S9-slimfinder Motifs
--------------------------------------------------------------------------------------------------IK-E--------------------------------------------------------------------------H-R-HT-ERPF-CNQCG----------RHIKLH---------------------T-HLR-HS----T-GKPY-CNYCGRSYK----L-EHK-R-H-YL-----------------------------------------------KR-R-------------------------------------------------------------------------------------------------E-P-DL---------------------------------------------------------V--R-SP-----------------------------------------------------------------------------------HI--GEH---
>IKZF4_HUMAN__Q9H2S9-masked
XHTPPALPRRFQGGGRVRTPGSHRQGKDNLERDPSGGCVPDFLPQAQDSNHFIMESLFCESSGDSSLEKEFLGAPVGPSVSTPNSQHSXPXRXLSANSIKVEMYSDEESSRLLGPDERLLEKDDSVIVEDSLSEPLGYCDGSGPEPHSPGGIRLPNXXXXXXXXXXXXXXXXXXXXHXRSHTXERPFHCNQCGXXXXXXGNXLRHIKLHXXXXXXXXXXXXXXXXXXXXXTGHLRTHSVSSPTVGKPYKCNYCGRSYKQQSTLEEHKERCHNYLQSLSTEAQALAGQPGDEIRDLEMVPDSMLHSSSERPTFIDRLANSLTKRKRSTPQKFVGEKQMRFSLSDLPYDVNSGGYEKDVELVAHHSLXXXXGSSLAXVXXXHLRXLRLPPTNCISXLTPVISSVYTQMQPLPGRLELPGSREAGEGPEDLADGGPLLYRPRGPLTDPGASPSNGCQDSTDTESNHEDRVAGVVSLPQGXXXQXXPTIVVGRHSPAYAKEDPKPQEGLLRGTPGPSKEVLRVVGESGXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXSSHIVRGEHKVG
>IKZF4_HUMAN__Q9H2S9 RecName: Full=Zinc finger protein Eos; AltName: Full=Ikaros family zinc finger protein 4;
MHTPPALPRRFQGGGRVRTPGSHRQGKDNLERDPSGGCVPDFLPQAQDSNHFIMESLFCESSGDSSLEKEFLGAPVGPSVSTPNSQHSSPSRSLSANSIKVEMYSDEESSRLLGPDERLLEKDDSVIVEDSLSEPLGYCDGSGPEPHSPGGIRLPNGKLKCDVCGMVCIGPNVLMVHKRSHTGERPFHCNQCGASFTQKGNLLRHIKLHSGEKPFKCPFCNYACRRRDALTGHLRTHSVSSPTVGKPYKCNYCGRSYKQQSTLEEHKERCHNYLQSLSTEAQALAGQPGDEIRDLEMVPDSMLHSSSERPTFIDRLANSLTKRKRSTPQKFVGEKQMRFSLSDLPYDVNSGGYEKDVELVAHHSLEPGFGSSLAFVGAEHLRPLRLPPTNCISELTPVISSVYTQMQPLPGRLELPGSREAGEGPEDLADGGPLLYRPRGPLTDPGASPSNGCQDSTDTESNHEDRVAGVVSLPQGPPPQPPPTIVVGRHSPAYAKEDPKPQEGLLRGTPGPSKEVLRVVGESGEPVKAFKCEHCRILFLDHVMFTIHMGCHGFRDPFECNICGYHSQDRYEFSSHIVRGEHKVG
>KLF3_HUMAN__P57682-slimfinder Motifs
--------VK-E--DPV-VS-------------------------------------Q--PVDLTV-KR-SP------------------------------------------------------------------------------------------QPL-VS----------------------------IK-EP------------------------------------------------------KRR--------C-K-Y-K-SHLKAHRR-HTGEKP------------------TRHFR-HT--KP-QC-DCDRSFSRS-HL-LHRKRH---
>KLF3_HUMAN__P57682-masked
XLMFDPVPVKQEAMDPVSVSYPSNYMESXKPNKYGVIYSTPLPEKFFQTPEGLSHGIQMEPVDLTVNKRSSPPSAGNSPSSLKFPSSHRRASPGLSMPSSSPPIKKYSPPSPGVQPFGVPLSMPPVXAAALSRHXXXSXXXXXXXXXXXXXXXXXXXXXXLQQPLMVSLSEEMENSSSSMQVPVIESYEKPISQKKIKIEPGIEPQRTDYYPEEMSPPLMNSVSPPQALLQENHPSVIVQPGKRPLPVESPDTQRKRRIHRCDYDGCNKVYTKSSHLKAHRRTHTGEKPXKXXXXXXXXXXXXXXXXTRHFRKHTXXKPXQCPDCDRSFXRSDHLALHRKRHMLV
>KLF3_HUMAN__P57682 RecName: Full=Krueppel-like factor 3; AltName: Full=Basic krueppel-like factor; AltName: Full=CACCC-box-binding protein BKLF; AltName: Full=TEF-2;
MLMFDPVPVKQEAMDPVSVSYPSNYMESMKPNKYGVIYSTPLPEKFFQTPEGLSHGIQMEPVDLTVNKRSSPPSAGNSPSSLKFPSSHRRASPGLSMPSSSPPIKKYSPPSPGVQPFGVPLSMPPVMAAALSRHGIRSPGILPVIQPVVVQPVPFMYTSHLQQPLMVSLSEEMENSSSSMQVPVIESYEKPISQKKIKIEPGIEPQRTDYYPEEMSPPLMNSVSPPQALLQENHPSVIVQPGKRPLPVESPDTQRKRRIHRCDYDGCNKVYTKSSHLKAHRRTHTGEKPYKCTWEGCTWKFARSDELTRHFRKHTGIKPFQCPDCDRSFSRSDHLALHRKRHMLV
>KLF8_HUMAN__O95600-slimfinder Motifs
-----------------------------------------------------------------IK-EPPEEL--------Q--PVDLS--K--------------------------------------------------------------------------------------------------------------------------VK-DP------------------------------------------------KRRR--------------K-SHLKAHRRIHTGEKP------------------TRHFR-HT--KP--C-DC-RSFSRS-HL-LH-RRH---
>KLF8_HUMAN__O95600-masked
XVDMDKLINNLEVQLNSEGGSMQVFKQVTASVRNRDPPEIEYRSNMTSPTLLDANPMENPALFNDIKIEPPEELLASDFSLPQVEPVDLSFHKPKAPLQPASMLQAPIRPPKPQSSPQTLVVSTSTSDMSTSANIPTVLTPGSVLTSSQSTGSQQILHVIHTIPSXSLXNKXXGXXTXPXXXXXXXXXYXXXPADGXXAAITVPLIGGDGKNAGSVKVDPTSMSPLEIPSDSEESTIESGSSALQSLQGLQQEPAAMAQMQGEESLDLKRRRIHQXDFAGCXXVXXKSSHLKAHRRIHTGEKPXXXXXXXXXXXXXXXXXXTRHFRKHTXXKPXXCTDCNRSFXRSDHLSLHRRRHDTM
>KLF8_HUMAN__O95600 RecName: Full=Krueppel-like factor 8; AltName: Full=Basic krueppel-like factor 3; AltName: Full=Zinc finger protein 741;
MVDMDKLINNLEVQLNSEGGSMQVFKQVTASVRNRDPPEIEYRSNMTSPTLLDANPMENPALFNDIKIEPPEELLASDFSLPQVEPVDLSFHKPKAPLQPASMLQAPIRPPKPQSSPQTLVVSTSTSDMSTSANIPTVLTPGSVLTSSQSTGSQQILHVIHTIPSVSLPNKMGGLKTIPVVVQSLPMVYTTLPADGGPAAITVPLIGGDGKNAGSVKVDPTSMSPLEIPSDSEESTIESGSSALQSLQGLQQEPAAMAQMQGEESLDLKRRRIHQCDFAGCSKVYTKSSHLKAHRRIHTGEKPYKCTWDGCSWKFARSDELTRHFRKHTGIKPFRCTDCNRSFSRSDHLSLHRRRHDTM
>KNIR_DROME__P10734-slimfinder Motifs
---------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------QE-PMDLSMK--R-----------------------------------------------------------------------------------------
>KNIR_DROME__P10734-masked
XNQTCXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXSKGXXRYGRRXXXFKIHCLLXXXEQAXXXXGKAPPLAGGVSVGGAPSASSPVGSPHTPGFGDMAAHLXXXHQXXXXXQVPRHPHMPLLGYPSYLXDXXXXXXXFSMMGXXPHQSPFQLPPHLLXXXYXAXXXXXAXSXXDXAYRQEMYKHRQSVDSVESQNRFSPASQPPVVQPTSSARQSPIDVCLEEDVHSVHSHQSSASLLHPIAIRATPTTPTSSSPLSFAAKMQSLSPVSVCSIGGETTSVVPVHPPTVSAQEGPMDLSMKTSRSSVHSFNDSGSEDQEVEVAPRRKFYQLEAECLTTSXXXXXHSAAHSPNTTTAHAEVKRQKLGGAEATHFXXFXXXXXXXXXXXXIFVCV
>KNIR_DROME__P10734 RecName: Full=Zygotic gap protein knirps; AltName: Full=Nuclear receptor subfamily 0 group A member 1;
MNQTCKVCGEPAAGFHFGAFTCEGCKSFFGRSYNNISTISECKNEGKCIIDKKNRTTCKACRLRKCYNVGMSKGGSRYGRRSNWFKIHCLLQEHEQAAAAAGKAPPLAGGVSVGGAPSASSPVGSPHTPGFGDMAAHLHHHHQQQQQQQVPRHPHMPLLGYPSYLSDPSAALPFFSMMGGVPHQSPFQLPPHLLFPGYHASAAAAAASAADAAYRQEMYKHRQSVDSVESQNRFSPASQPPVVQPTSSARQSPIDVCLEEDVHSVHSHQSSASLLHPIAIRATPTTPTSSSPLSFAAKMQSLSPVSVCSIGGETTSVVPVHPPTVSAQEGPMDLSMKTSRSSVHSFNDSGSEDQEVEVAPRRKFYQLEAECLTTSSSSSSHSAAHSPNTTTAHAEVKRQKLGGAEATHFGGFAVAHNAASAMRGIFVCV
>LCOR_HUMAN__Q96JN0-slimfinder Motifs
------------------------------------------------------------QD-PLDLTVRK--------D--LDLS-K-----------------------------------------------------------------------------------------------------------------------------------------------------------------PVDL-------MDLS----------------------------------------------------------------------------KKR-R-R--------------------------------S-L--KV-ERL--L-N--K-K---------------------------------
>LCOR_HUMAN__Q96JN0-masked
XQRMIQQFAAEYTSKNSSTQDPSQPNSTKNQSLPKASPVTTSPTAATTQNPVLSKLLMADQDSPLDLTVRKSQSEPSEQDGVLDLSTKKSPCAGSTSLSHSPGCSSTQGNGRPGRPSQYRPDGLRSGDGVPPRSLQDGTREGFGHSTSLKVPLARSLQISEELLSRNQLSTAASLGPSGLQNHGQHLILSREASXXXXHYEXXLXRMKXXGXGXXXXISDLPFLAENSAFPKMALQAKQDGKKDVSHSSPVDLKIPQVRGMDLSWESRTGDQYSYSSLVMGSQTESALSKKLRAILPKQSRKSMLDAGPDSWGSDAEQSTSGQPYPTSDQEGDPGSKQPRKKRGRYRQYNSEILEEAISVVMSGKXXXSKAQSIYGIPHSTLEYKVKERLGTLKNPPKKKMKLMRSEGPDVSVKIELDPQGEAAQSANESKNE
>LCOR_HUMAN__Q96JN0 RecName: Full=Ligand-dependent corepressor; Short=LCoR; AltName: Full=Mblk1-related protein 2;
MQRMIQQFAAEYTSKNSSTQDPSQPNSTKNQSLPKASPVTTSPTAATTQNPVLSKLLMADQDSPLDLTVRKSQSEPSEQDGVLDLSTKKSPCAGSTSLSHSPGCSSTQGNGRPGRPSQYRPDGLRSGDGVPPRSLQDGTREGFGHSTSLKVPLARSLQISEELLSRNQLSTAASLGPSGLQNHGQHLILSREASWAKPHYEFNLSRMKFRGNGALSNISDLPFLAENSAFPKMALQAKQDGKKDVSHSSPVDLKIPQVRGMDLSWESRTGDQYSYSSLVMGSQTESALSKKLRAILPKQSRKSMLDAGPDSWGSDAEQSTSGQPYPTSDQEGDPGSKQPRKKRGRYRQYNSEILEEAISVVMSGKMSVSKAQSIYGIPHSTLEYKVKERLGTLKNPPKKKMKLMRSEGPDVSVKIELDPQGEAAQSANESKNE
>NRIP1_HUMAN__P48552-slimfinder Motifs
------------------------------------------------------------------------------------------------KR-R---------------------------------------------------------------------------------------------------------------R-R--E-PH--------------------------V--R-SP------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------PIDLS-KHR---S--DQPV-L--------------------------------------------------------------------------------------------------------PI-LS-----------PY-C--------------------------------------------------------------------------------------------------------------------------------L--L--N--K-K------------------------------IK-EP-D-------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------IK-E--
>NRIP1_HUMAN__P48552-masked
XTHGEELGSDVHQDSIXLTYXEGLLMHQAAGGSGTAVDKKSAGHNEEDQNFNISGSAFPTCQSNGPVLNTHTYQGSGMLHLKKARLLQSSEDWNAAKRKRLSDSIMNLNXXKEXXLAGMVDSVPKGKQDSTLLASLLXXXXXXXXXVXXSQQIXXXXKEQGYALSHDSLKXXKDLRCYXVASSHLKTLLKKSKVKDQKPDTNLPDVTKNLIRDRFAESPHHVGQSGTKVMSEPLSCAARLQAVASMVEKRASPATSPKPSVACSQLALLXXSEAHLQQYSREHALKTQNANQAASERLAAMARLQENGQKDVGSYQLPKGMSSHLNGQARTSSSKLMASKSSATVFQNPMGIIPSSPKNAGYKNSLERNNIKQAANNSLXXHXLKSQTIPKPMNGHSHSERGSIFEESSTPTTIDEYSDNNPSFTDDSSGDESSYSNCVPIDLSCKHRTEKSESDQPVSLDNFTQSLLNTWDPKVPDVDIKEDQDTSKNSKLNSHQKVTLXQXXLGHKNEENVEKNTSPQGVHNDVSKFNTQNYARTSVIESPSTNRTTPVSTPPLLTSSKAGSPINLSQHSLVIKWNSPPYVCSTQSEKLTNTASNHSMDLTKSKDPPGEKPAQNEGAQNSATFSASKLLQNLAQCGMQSSMSVEEQRPSKQLLTGNTDKPIGMIDRLNSPLLSNKTNAVEENKAFSSQPTGPEPGLSGSEIENLLERRTVLQLLLGNPNKGKSEKKEKTPLRDESTQEHSERALSEQILMVKIKSEPCDDLQIPNTNVHLSHDAKSAPFLGMAPAVQRSAPALPVSEDFKSEPVSPQDFSFSKNGLLSRLLRQNQDSYLADDSDRSHRNNEMALLESKNLCMVPKKRKLYTEPLENPFKKMKNNIVDAANNHSAPEVLYGSLLNQEELKFSRNDLEFKYPAGHGSASESEHRSWARESKSFNVLKQLLLSENCVRDLSPHRSNSVADSKKKGHKNNVTNSKPEFSISSLNGLMYSSTQPSSCMDNRTFSYPGVVKTPVSPTFPEHLGCAGSRPESGLLNGCSMPSEKGPIKWVITDAEKNEYEKDSPRLTKTNPILYYMLQKGGNSVTSRETQDKDIWREASSAESVSQVTAKEELLPTAETKASFFNLRSPYNSHMGNNASRPHSANGEVYGLLGSVLTIKKESE
>NRIP1_HUMAN__P48552 RecName: Full=Nuclear receptor-interacting protein 1; AltName: Full=Nuclear factor RIP140; AltName: Full=Receptor-interacting protein 140;
MTHGEELGSDVHQDSIVLTYLEGLLMHQAAGGSGTAVDKKSAGHNEEDQNFNISGSAFPTCQSNGPVLNTHTYQGSGMLHLKKARLLQSSEDWNAAKRKRLSDSIMNLNVKKEALLAGMVDSVPKGKQDSTLLASLLQSFSSRLQTVALSQQIRQSLKEQGYALSHDSLKVEKDLRCYGVASSHLKTLLKKSKVKDQKPDTNLPDVTKNLIRDRFAESPHHVGQSGTKVMSEPLSCAARLQAVASMVEKRASPATSPKPSVACSQLALLLSSEAHLQQYSREHALKTQNANQAASERLAAMARLQENGQKDVGSYQLPKGMSSHLNGQARTSSSKLMASKSSATVFQNPMGIIPSSPKNAGYKNSLERNNIKQAANNSLLLHLLKSQTIPKPMNGHSHSERGSIFEESSTPTTIDEYSDNNPSFTDDSSGDESSYSNCVPIDLSCKHRTEKSESDQPVSLDNFTQSLLNTWDPKVPDVDIKEDQDTSKNSKLNSHQKVTLLQLLLGHKNEENVEKNTSPQGVHNDVSKFNTQNYARTSVIESPSTNRTTPVSTPPLLTSSKAGSPINLSQHSLVIKWNSPPYVCSTQSEKLTNTASNHSMDLTKSKDPPGEKPAQNEGAQNSATFSASKLLQNLAQCGMQSSMSVEEQRPSKQLLTGNTDKPIGMIDRLNSPLLSNKTNAVEENKAFSSQPTGPEPGLSGSEIENLLERRTVLQLLLGNPNKGKSEKKEKTPLRDESTQEHSERALSEQILMVKIKSEPCDDLQIPNTNVHLSHDAKSAPFLGMAPAVQRSAPALPVSEDFKSEPVSPQDFSFSKNGLLSRLLRQNQDSYLADDSDRSHRNNEMALLESKNLCMVPKKRKLYTEPLENPFKKMKNNIVDAANNHSAPEVLYGSLLNQEELKFSRNDLEFKYPAGHGSASESEHRSWARESKSFNVLKQLLLSENCVRDLSPHRSNSVADSKKKGHKNNVTNSKPEFSISSLNGLMYSSTQPSSCMDNRTFSYPGVVKTPVSPTFPEHLGCAGSRPESGLLNGCSMPSEKGPIKWVITDAEKNEYEKDSPRLTKTNPILYYMLQKGGNSVTSRETQDKDIWREASSAESVSQVTAKEELLPTAETKASFFNLRSPYNSHMGNNASRPHSANGEVYGLLGSVLTIKKESE
>SOX6_HUMAN__P35712-slimfinder Motifs
--------PF-C---------------------------HL-LH--MH---HS-E-P---------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------IK-E----------------QPL-LS-R--------------------------------------------------------------------------------------------------------------K-R-R----------------------IDLT--------------------YYC-----------------------------------------------------------------------------------------------------------------G-Y-Q-M--R---------------------------------------------------------------------------------------------------------------
>SOX6_HUMAN__P35712-masked
XSSKQATSPFACAADGEDAMTQDLTSREKEEGSDQHVASHLPLHPIMHNKPHSEELPTLVSTIQQDADWDSVLSSQQRMESENNKLCSLYSFRNTSTSPHKPDEGSRDREIMTSVTFGTPERRKGSLADVVDTLKQKKLEEMTRTEQEDSSCMEKLLSKDWKEKMERLNTSELLGEIKGTPESLAEKERQLSTMITQLXSLREQLLAAHDEQKKLAASQIEKQRQQMDLARQQQEQIARXXXXLXXXQHKXXXLQXXIXXQGXMPPLMIPIFPHDQXTLAXXXXAQQXXLFPPGITYKXGDNYPVQFIPSTMAXXXASGLSPLQLQKGHVSHPQINQRLKGLSDRFGRNLDTFEHGGGHSYNHKQIEQLYAAQLASMQVSPGAKMPSTPQPPNTAGTVSPTGIKNEKRGTSPVTQVKDEAAAQPLNLSSRPKTAEPVKSPTSPTQNLFPASKTSPVNLPNKSSIPSPIGGSLGRGSSLDILSSLNSPALFGDQDTVMKAIQEARKMREQIXREXXXXQPHGVDGKLSSINNMGLNSCRNEKERTRFENLGPQLTGKSNEDGKLGPGVIDLTRPEDAEGSKAMNGSAAKLQQYYCWXTGXXXXAEARVYRDARGRASSEPHIKRPMNAFMVWAKDERRKILQAFPDMHNSNISKILGSRWKSMSNQEKQPYYEEQARLSKIHLEKYPNYKYKPRPKRTCIVDGKKLRIGEYKQLMRSRRQEMRQFFTVGQQPQIPITTGTGVVYPGAITMATTTPSPQMTSDCSSTSASPEPSLPVIQSTYGMKTDGGSLAGNEMINGEDEMEMYDDYEDDPKSDYSSENEAPEAVSAN
>SOX6_HUMAN__P35712 RecName: Full=Transcription factor SOX-6;
MSSKQATSPFACAADGEDAMTQDLTSREKEEGSDQHVASHLPLHPIMHNKPHSEELPTLVSTIQQDADWDSVLSSQQRMESENNKLCSLYSFRNTSTSPHKPDEGSRDREIMTSVTFGTPERRKGSLADVVDTLKQKKLEEMTRTEQEDSSCMEKLLSKDWKEKMERLNTSELLGEIKGTPESLAEKERQLSTMITQLISLREQLLAAHDEQKKLAASQIEKQRQQMDLARQQQEQIARQQQQLLQQQHKINLLQQQIQVQGHMPPLMIPIFPHDQRTLAAAAAAQQGFLFPPGITYKPGDNYPVQFIPSTMAAAAASGLSPLQLQKGHVSHPQINQRLKGLSDRFGRNLDTFEHGGGHSYNHKQIEQLYAAQLASMQVSPGAKMPSTPQPPNTAGTVSPTGIKNEKRGTSPVTQVKDEAAAQPLNLSSRPKTAEPVKSPTSPTQNLFPASKTSPVNLPNKSSIPSPIGGSLGRGSSLDILSSLNSPALFGDQDTVMKAIQEARKMREQIQREQQQQQPHGVDGKLSSINNMGLNSCRNEKERTRFENLGPQLTGKSNEDGKLGPGVIDLTRPEDAEGSKAMNGSAAKLQQYYCWPTGGATVAEARVYRDARGRASSEPHIKRPMNAFMVWAKDERRKILQAFPDMHNSNISKILGSRWKSMSNQEKQPYYEEQARLSKIHLEKYPNYKYKPRPKRTCIVDGKKLRIGEYKQLMRSRRQEMRQFFTVGQQPQIPITTGTGVVYPGAITMATTTPSPQMTSDCSSTSASPEPSLPVIQSTYGMKTDGGSLAGNEMINGEDEMEMYDDYEDDPKSDYSSENEAPEAVSAN
>T7L1A_XENLA__P70062-slimfinder Motifs
------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------P-ELS----------------------------------------------------V--R-SP------H--LH-------AI-S--VK-EP--------------------------------------------------------------------------------------H--LY------------KKR-R-K------------------------------------------------------------QPL-LT-K-------------------------------------------------------------------------------
>T7L1A_XENLA__P70062-masked
XPQLNSGGGDELGANDELIRFKDEGEQEEKSPGEGSAEGDLADVKSSLVNESENHSSDSDSEVERRPPPREAFEKHRDYLTEALRRQQDAAFFKGPXXXXXXXXXXXXXXXXXXPNGALSPXARTYLQMKWPLLDSPSTAGLKDARSPSPAHLSNKVPVVQHPHHMHPLTPLITYSNEHFSPGTPPGHLSPEIDPKTGIPRPPHPSELSPYYPLSPGAVGQIPHPLGWLVPPQGQPMYSIPPGGFRHPYPALAMNASMXXLVXSRFSPHMVPPPHHSLHTSGIPHPAIVSPIVKQEPSSGNISPNLHTKSNMIVKKEEEKKPHIKKPLNAFMXXXXXXXXXXXXXXXXXXXXXXXXXXGRRWHSLSXXEQAKYYELARKERQLHSQLYPSWSARDNYGKRKKRKREKQSPEMETHTKTKKMCVQHLPADKSCDSPASSHGSMLDSPATPSAXLXSPXXPXATHSEQAQPLSLTTKPEARAQLSLSHSAAFLASKXPXXXXFSGHLSSPVGSPLLSRPIPLTXXILSPXXXXXXXXQXXXXXXXXXLSLVTKSSD
>T7L1A_XENLA__P70062 RecName: Full=Transcription factor 7-like 1-A; AltName: Full=HMG box transcription factor 3-A; Short=TCF-3-A; Short=xTcf-3;
MPQLNSGGGDELGANDELIRFKDEGEQEEKSPGEGSAEGDLADVKSSLVNESENHSSDSDSEVERRPPPREAFEKHRDYLTEALRRQQDAAFFKGPPYAGYPFLMIPDLGGHYLPNGALSPSARTYLQMKWPLLDSPSTAGLKDARSPSPAHLSNKVPVVQHPHHMHPLTPLITYSNEHFSPGTPPGHLSPEIDPKTGIPRPPHPSELSPYYPLSPGAVGQIPHPLGWLVPPQGQPMYSIPPGGFRHPYPALAMNASMSSLVSSRFSPHMVPPPHHSLHTSGIPHPAIVSPIVKQEPSSGNISPNLHTKSNMIVKKEEEKKPHIKKPLNAFMLYMKEMRAKVVAECTLKESAAINQILGRRWHSLSREEQAKYYELARKERQLHSQLYPSWSARDNYGKRKKRKREKQSPEMETHTKTKKMCVQHLPADKSCDSPASSHGSMLDSPATPSAALASPAAPAATHSEQAQPLSLTTKPEARAQLSLSHSAAFLASKSPSSSSFSGHLSSPVGSPLLSRPIPLTSSILSPSGVFPSALQALPLLQAQPLSLVTKSSD
>TGIF1_HUMAN__Q15583-slimfinder Motifs
--------------------------------------------------------------------------------------------------------RR-H--E-P-------------------------------------D-PLDLS------KRRRR-----------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------
>TGIF1_HUMAN__Q15583-masked
XVLAQSRVSAGVGSPHCSGSXXXGSDSFPWPASHPGNPQCSFSTAFLASXXXSRGTLAYLPPAPWSSLATPSALLGSSCAPXXXXARCPQPRALSPELGTKAGPRRPHRWELPRSPSQGAQGPAPRRRLLETMKGIVAASGSETEDEDSMDIPLDLSSSAGSGKRRRRGNLPKESVQILRDWLXEHRYNAXXSEQEKALLSQQTXXXXXXXXXXXXXXXXXXLPDMLRKDGKDPNQFTISRRGAKISETSSVESVMGIKNFMPALEETPFHSCTAGPNPTLGRPLSPKPSSPGSVLARPSVICXTXVXXXXXXXXXXXXXVGXXXXXXIQQIAAKNFTDTSLMYPEDTCKSGPSTNTQSGLFNTPXXTXPDLNQDFSGFQXXVXXXXXXXXXXELQAKLTA
>TGIF1_HUMAN__Q15583 RecName: Full=Homeobox protein TGIF1; AltName: Full=5'-TG-3'-interacting factor 1;
MVLAQSRVSAGVGSPHCSGSGGGGSDSFPWPASHPGNPQCSFSTAFLASPRLSRGTLAYLPPAPWSSLATPSALLGSSCAPPPPPARCPQPRALSPELGTKAGPRRPHRWELPRSPSQGAQGPAPRRRLLETMKGIVAASGSETEDEDSMDIPLDLSSSAGSGKRRRRGNLPKESVQILRDWLYEHRYNAYPSEQEKALLSQQTHLSTLQVCNWFINARRRLLPDMLRKDGKDPNQFTISRRGAKISETSSVESVMGIKNFMPALEETPFHSCTAGPNPTLGRPLSPKPSSPGSVLARPSVICHTTVTALKDVPFSLCQSVGVGQNTDIQQIAAKNFTDTSLMYPEDTCKSGPSTNTQSGLFNTPPPTPPDLNQDFSGFQLLVDVALKRAAEMELQAKLTA
>TRPS1_HUMAN__Q9UHF7-slimfinder Motifs
----------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------PLD-S--------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------H-C--CD---------------------------------------------------------------IK-EP------------------------VK-E--E-------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------PV-VS-----------------------------------------------------------------------------------------------------------------------------------------D-PLDLA-KH-R---------------------------VK-E--D---------------------------------------------------------------------------
>TRPS1_HUMAN__Q9UHF7-masked
XVRKKNPPLRNVASEGEGQILEPIGTESKVSGKNKEFSADQMSENTDQSDAAELNHKEEHSLHVQDPSSSSKKDLKSAVLSEKAGFNYESPSKGGNFPSFPHDEVTDRNMLAFSSPAAGGVCEPLKSPQRAEADDPQDMACTPSGDSLETKEDQKMSPKATEETGQAQSGQANCQGLSPVSVASKNPQVPSDGGVRLNKSKTDLLVNDNPDPAPLSPELQDXXXXXXXXXXXXXXXXXXXXXFRKYXXXLHNRTRXDXELDSKXXAXXNXVQXXHSKDFQXXXRXXXXXVLXXXXXXRPVLLNGTYDXXXXXGGTFIGIGRKTXXXXXXXXXXXXXXXXXXXXXXXXTELEQHFLQTHPNKIKASLPSSEVAKPSEKNSNKSIPALQSSDSGDLGKWQDKITVKAGDDTPVGYSVPIKPLDSSRQNXTXXXXXXXXXXXXXXXXXXXXXXXLXHYGKQHGAVQSGGLNPELNDKLSRGSVINQNDLAKSSEGETMTKTDKSSSGAKKKDFSSKGAEDNXXXXXXXXXXXXXXXXXXXXXXXXVXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXLFHYESVHESQASDVKQEANHLQGSDGQQSVKESKEHSCTKCDFITXXXEXXXXXXXXXXXXXXXXXXXXXXXXXXXXXEHFNTVHCQEQDITTANGEEDGHAISTIKEEPKIDFRVYNLLTPDSKMGEPVSESVVKREKLEEKDGLKEKVWTESSSDDLRNVTWRGADILRGSPSYTQASLGLLTPVSGTQEQTKTLRDSPNVEAAHLARPIYGLAVETKGFLQGAPAGGEKSGALPQQYPASGENKSKDESQSLLRRRRXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXPRPLNIIKQNNGEQIIRXXTXKRLNPEALQAEQLNKQQRGSNEEQVNGSPLERRSEDHLTESHQREIPLPSLSKYEAQGSLTKSHSAQQPVLVSQTLDIHKRMQPLHIQIKSPQESTGDPGNSSSVSEGKGSSERGSPIEKYMRPAKHPNYSPPGSPIEKYQYXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXLSHVPGLPNPCQNYVPYPTFNLPPHFSAVGSDNDIPLDLAIKHSRPGPTANGASKEKTKAPPNVKNEGPLNVVKTEKVDRSTQDELXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXIQRGLHRNNAQVEKNGKPKE
>TRPS1_HUMAN__Q9UHF7 RecName: Full=Zinc finger transcription factor Trps1; AltName: Full=Tricho-rhino-phalangeal syndrome type I protein; AltName: Full=Zinc finger protein GC79;
MVRKKNPPLRNVASEGEGQILEPIGTESKVSGKNKEFSADQMSENTDQSDAAELNHKEEHSLHVQDPSSSSKKDLKSAVLSEKAGFNYESPSKGGNFPSFPHDEVTDRNMLAFSSPAAGGVCEPLKSPQRAEADDPQDMACTPSGDSLETKEDQKMSPKATEETGQAQSGQANCQGLSPVSVASKNPQVPSDGGVRLNKSKTDLLVNDNPDPAPLSPELQDFKCNICGYGYYGNDPTDLIKHFRKYHLGLHNRTRQDAELDSKILALHNMVQFSHSKDFQKVNRSVFSGVLQDINSSRPVLLNGTYDVQVTSGGTFIGIGRKTPDCQGNTKYFRCKFCNFTYMGNSSTELEQHFLQTHPNKIKASLPSSEVAKPSEKNSNKSIPALQSSDSGDLGKWQDKITVKAGDDTPVGYSVPIKPLDSSRQNGTEATSYYWCKFCSFSCESSSSLKLLEHYGKQHGAVQSGGLNPELNDKLSRGSVINQNDLAKSSEGETMTKTDKSSSGAKKKDFSSKGAEDNMVTSYNCQFCDFRYSKSHGPDVIVVGPLLRHYQQLHNIHKCTIKHCPFCPRGLCSPEKHLGEITYPFACRKSNCSHCALLLLHLSPGAAGSSRVKHQCHQCSFTTPDVDVLLFHYESVHESQASDVKQEANHLQGSDGQQSVKESKEHSCTKCDFITQVEEEISRHYRRAHSCYKCRQCSFTAADTQSLLEHFNTVHCQEQDITTANGEEDGHAISTIKEEPKIDFRVYNLLTPDSKMGEPVSESVVKREKLEEKDGLKEKVWTESSSDDLRNVTWRGADILRGSPSYTQASLGLLTPVSGTQEQTKTLRDSPNVEAAHLARPIYGLAVETKGFLQGAPAGGEKSGALPQQYPASGENKSKDESQSLLRRRRGSGVFCANCLTTKTSLWRKNANGGYVCNACGLYQKLHSTPRPLNIIKQNNGEQIIRRRTRKRLNPEALQAEQLNKQQRGSNEEQVNGSPLERRSEDHLTESHQREIPLPSLSKYEAQGSLTKSHSAQQPVLVSQTLDIHKRMQPLHIQIKSPQESTGDPGNSSSVSEGKGSSERGSPIEKYMRPAKHPNYSPPGSPIEKYQYPLFGLPFVHNDFQSEADWLRFWSKYKLSVPGNPHYLSHVPGLPNPCQNYVPYPTFNLPPHFSAVGSDNDIPLDLAIKHSRPGPTANGASKEKTKAPPNVKNEGPLNVVKTEKVDRSTQDELSTKCVHCGIVFLDEVMYALHMSCHGDSGPFQCSICQHLCTDKYDFTTHIQRGLHRNNAQVEKNGKPKE
>TTKB_DROME__P17789-slimfinder Motifs
------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------KRKR-R-----------------------------------C--SY------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------QPL-VS------P-DLS----------------------------------------------
>TTKB_DROME__P17789-masked
XKMASQRFCXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXLKXXXXXXXXXXXXXXXXXXXXXXXXXLXXXXXXXXXXXXKGLTEVNDDKPSPAXXXXGXGATGSESTATTPQLQRIQPYLVPQRNRSQAGGLLASAANAGNTPTLPVQPSLLSSALMPKRKRGRPRKLSGSSNGTGNDYDDFDRENMMNDSSDLGNGKMCNESYSGNDDGSDDNQPNAGHTDDLNESRDSLPSKRSKNSKDHRVVSHHEDNSTSDGNDSDGEGLDTSYMEPQLMLDEYDEPVEFKYNPLTDNSSPTQDHTDGSHLNEQARQQAFLIAAQRKHXVETAAAXXXXXXXXXXXXXXXXXXXXXSXXSIPXLXPIGKVNAASTPLVSPAGSFSTATVKPRVQKRPKLGKQNGDVKPAVFSSQEYLDXYNSNXXXKLKAAGLSGSTPNLSAGLGTPSVKTKLNLSSNVGEGEAEGSVRDYCXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXAHVKIIHKIENPSTALXTVXXANLAGQPLGVSGASTPPPPDLSGQNSNQSLPATSNALSTXXXXXTXXXXGSLGPLTTSAPPXPXXXAQ
>TTKB_DROME__P17789 RecName: Full=Protein tramtrack, beta isoform; AltName: Full=Repressor protein fushi tarazu; AltName: Full=Tramtrack p69;
MKMASQRFCLRWNNHQSNLLSVFDQLLHAETFTDVTLAVEGQHLKAHKMVLSACSPYFNTLFVSHPEKHPIVILKDVPYSDMKSLLDFMYRGEVSVDQERLTAFLRVAESLRIKGLTEVNDDKPSPAAAAAGAGATGSESTATTPQLQRIQPYLVPQRNRSQAGGLLASAANAGNTPTLPVQPSLLSSALMPKRKRGRPRKLSGSSNGTGNDYDDFDRENMMNDSSDLGNGKMCNESYSGNDDGSDDNQPNAGHTDDLNESRDSLPSKRSKNSKDHRVVSHHEDNSTSDGNDSDGEGLDTSYMEPQLMLDEYDEPVEFKYNPLTDNSSPTQDHTDGSHLNEQARQQAFLIAAQRKHQVETAAAAAASGIKLNIIGMAAGGAQVKSMVSIPKLTPIGKVNAASTPLVSPAGSFSTATVKPRVQKRPKLGKQNGDVKPAVFSSQEYLDIYNSNDGFKLKAAGLSGSTPNLSAGLGTPSVKTKLNLSSNVGEGEAEGSVRDYCTKEGEHTYRCKVCSRVYTHISNFCRHYVTSHKRNVKVYPCPFCFKEFTRKDNMTAHVKIIHKIENPSTALATVAAANLAGQPLGVSGASTPPPPDLSGQNSNQSLPATSNALSTSSSSSTSSSSGSLGPLTTSAPPAPAAAAQ
>ZEB1_HUMAN__P37275-slimfinder Motifs
--D--RCKRRKQA--R--------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------RHM--H------------------------------HHLKEHLRIHSGEKPYECPNCKKRFSHSG-Y-----------------R--T--K--QC----------------------------------IK-EP-D------------------------------------------------------------------------------------------------------------------------------------------------------------P-DLT-K-----------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------PL-LS-------------------Q--PLDLSL-K-----------------------E-PL-LS----------------------------------------------------------------------------------------------------------------------------------G-Y-CD-CDK-F--SSSL-RHKYEHTGKRPHEC-ICKKAFKHKHHL-EHMRLHSGEKPYQCDKCGKRFSHSGSYSQHMNHRYSYCKR----------------------V--R-SP-------------------------------------------------------------------------------------S-L--KV-E-------------
>ZEB1_HUMAN__P37275-masked
XXDGPRCKRRKQANPRRNNVTNYNTVVETNSDSDDEDKLHIVEEESVTDAADCEGVPEDDLPTDQTVLPGRSSEREGNAKNCWEDDRKEGQEILGPEAQADEAGCTVKDDECESDAENEQNHDPNVEEFLQQQDTAVIFPEAPEEDQRQGTPEASGHDENGTPDAFSQLLTCPXXXXXXXXXXXXKEHIKYRXXXXXXXXXXXXXXXXXXXXTQLERHMTSHKSGRDQRHVTQSGXXXXXXXXXXXXXXXXXHHLKEHLRIHSGEKPYECPNCKKRFSHXGXYXXHIXSKKCISLIPVNGRPRTGLKTSQCSXPXLXASPGSPTRPQIRQKIENKPLQEQLSVNQIKTEPXDYEFXXIVVXSXIXXXXPLQNGVFTGGGPLQATSSPQGMVQXXVXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXLENNQANLASKEQETINASPIQQGGHSVISAISLPLXXXXXXXXIIINYSXEQPXQLQVVPQNLKKENPVATNSCKSEKLPEDLTVKSEKDKSFEGGVNXXXCXLXXXCPXXXNALPELKHYDLKQPTQXXXLPAAEAEKPESSVSSATGDGNLSPSQPPLKNLLSXXXXXXXXXXXXXXXEXSKIAXXXXXXXXXVKKXFEKMQAGQISVQSSEPSSPEPGKVNIPAKNNDQPQSANANEPQDSTVNLQSPLKMTNSPVLPVGSTTNGSRSSTPSPSPLNLSSSRNTQGYLYTAEGAQEEPQVEPLDLSLPKQQGELLERSTITSVYQNSVYSVQEEPLNLSCAKKEPQKDSCVTDSEPVVNVIPPSANXXNXAIPXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXTTVSPAVQEPPLKVIQPNGNQDERQDTSSEGVSNVEDQNDSDSTPPKKKMRKTENGMYACDLCDKIFQXSSSLLRHKYEHTGKRPHECGICKKAFKHKHHLIEHMRLHSGEKPYQCDKCGKRFSHSGSYSQHMNHRYSYCKREAEERDSTEQEEAGPEILSNEHVGARASPSQGDSDERESLTREEDEDSXKXXXXXDKXMXXLQXXKECEKPQGDEXXXXXXXXVXXXXVXXAXNXGXEAKTEGLMKDDRAESQASSLGQKVGESSEQVSEEKTNEA
>ZEB1_HUMAN__P37275 RecName: Full=Zinc finger E-box-binding homeobox 1; AltName: Full=NIL-2-A zinc finger protein; AltName: Full=Negative regulator of IL2; AltName: Full=Transcription factor 8; Short=TCF-8;
MADGPRCKRRKQANPRRNNVTNYNTVVETNSDSDDEDKLHIVEEESVTDAADCEGVPEDDLPTDQTVLPGRSSEREGNAKNCWEDDRKEGQEILGPEAQADEAGCTVKDDECESDAENEQNHDPNVEEFLQQQDTAVIFPEAPEEDQRQGTPEASGHDENGTPDAFSQLLTCPYCDRGYKRFTSLKEHIKYRHEKNEDNFSCSLCSYTFAYRTQLERHMTSHKSGRDQRHVTQSGCNRKFKCTECGKAFKYKHHLKEHLRIHSGEKPYECPNCKKRFSHSGSYSSHISSKKCISLIPVNGRPRTGLKTSQCSSPSLSASPGSPTRPQIRQKIENKPLQEQLSVNQIKTEPVDYEFKPIVVASGINCSTPLQNGVFTGGGPLQATSSPQGMVQAVVLPTVGLVSPISINLSDIQNVLKVAVDGNVIRQVLENNQANLASKEQETINASPIQQGGHSVISAISLPLVDQDGTTKIIINYSLEQPSQLQVVPQNLKKENPVATNSCKSEKLPEDLTVKSEKDKSFEGGVNDSTCLLCDDCPGDINALPELKHYDLKQPTQPPPLPAAEAEKPESSVSSATGDGNLSPSQPPLKNLLSLLKAYYALNAQPSAEELSKIADSVNLPLDVVKKWFEKMQAGQISVQSSEPSSPEPGKVNIPAKNNDQPQSANANEPQDSTVNLQSPLKMTNSPVLPVGSTTNGSRSSTPSPSPLNLSSSRNTQGYLYTAEGAQEEPQVEPLDLSLPKQQGELLERSTITSVYQNSVYSVQEEPLNLSCAKKEPQKDSCVTDSEPVVNVIPPSANPINIAIPTVTAQLPTIVAIADQNSVPCLRALAANKQTILIPQVAYTYSTTVSPAVQEPPLKVIQPNGNQDERQDTSSEGVSNVEDQNDSDSTPPKKKMRKTENGMYACDLCDKIFQKSSSLLRHKYEHTGKRPHECGICKKAFKHKHHLIEHMRLHSGEKPYQCDKCGKRFSHSGSYSQHMNHRYSYCKREAEERDSTEQEEAGPEILSNEHVGARASPSQGDSDERESLTREEDEDSEKEEEEEDKEMEELQEEKECEKPQGDEEEEEEEEEVEEEEVEEAENEGEEAKTEGLMKDDRAESQASSLGQKVGESSEQVSEEKTNEA
>ZEB2_HUMAN__O60315-slimfinder Motifs
-------D--RCKRRKQA--R------------------------------------------------------------------------------------------------------------------------------------------------------------E-P-ELS-------------------------------------------------------------------------RHM--H----------------R-F-C--CGK-----HHLKEHLRIHSGEKPYECPNCKKRFSHSG-Y-----------------------KT-S-PN----------------------------------IK-E---------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------C--C--SF-----------------------------------------------------------------------------------------------------------------------------------------------------------------T--D-PL-LT-----------------------PL-LS----------------------Q--PLDLSL-K-----------K-K-K-S-I--------------D-PL-LT-IK-E-----------------------------------------------------------------------------------------------------------------------------------------------SSL-RHKYEHTGKRPHQC-ICKKAFKHKHHL-EH-RLHSGEKPYQCDKCGKRFSHSGSYSQHMNHRYSYCKR-----------------------------------------------------------------------------------------------------------------------------------
>ZEB2_HUMAN__O60315-masked
XKQPIMADGPRCKRRKQANPRRKNVVNYDNVVDTGSETDEEDKLHIAEDDGIANPLDQETSPASVPNHESSPHVSQALLPREXXXDXIREGGVEHPWHNNEILQASVDGPEEMKEDYDTMGPEATIQTAINNGTVKNANCTSDFEEYFAKRKLEERDGHAVSIEEYLQRSDTAIIYPEAPEELSRLGTPEANGQEENDLPPGTPDAFAQLLTCXXXXXXXXXXXXXKEHIKYRHEXXXXXXXXXXXXXXXXXXTXLERHMVTHKPGTDQHQMLTQGAGNRKFKCTECGKXXXYXHHLKEHLRIHSGEKPYECPNCKKRFSHXGXYXXHIXSKKCIGLISVNGRMRNNIKTGSXPNXVXXSPTNSAITQLRNKLENGKPLSMSEQTGLLKIKTEXXXXXDXKVLMATXGFSGTSPFMNGGLGATSPLGVHPSAQSPMQHLGVGMEAPLLGFPTMNSNXSEVQKVLQIVDNTVSRQKMDCKAEEISKLKGYHMKDPCSQPEEQGVTSPNIPPVGLPVVSHNGATKSIIDYTLXXXXXXKACLQSLTTDSRRQISNIKKXXXXXLXXLVTXXKMIENHNXXXXXXCQXCXXSFXGXIXXHQHERYLXXXXEEIXXXLQPHENXVPNKAGXXXXXXXXXXXXVLSEXXMTSPINPYKXXXXXXXXXYAXXXXXXXXXXXKIXXXXXXXXXXXXXXXXQRKVYQYSNSRSPSLERSSKPLAPNSNPPTKDSLLPRSPVKPMDSITSPSIAELHNSVTNCDPPLRLTKPSHFTNIKPVEKLDHSRSNTPSPLNLSXTXXKNXHXXSYTPNSFSSEELQAEPLDLSLPKQMKEPKSIIATKNKTKASSISLDHNSVXXXXENSDEPLNLTFIKKEFSNSNNLDNKSTNPVFSMNPFSAKPLYTALPPQSAFPPATFMPPVQTSIPGLRPYPGLDQMSFLPHMAYTYPTGAATFADMQQRRKYQRKQGFQGELLDGAQDYMSGLDDMTDSDSCLSRKKIKKXXXGXXXXXLCXXXXXXXSSLLRHKYEHTGKRPHQCQICKKAFKHKHHLIEHSRLHSGEKPYQCDKCGKRFSHSGSYSQHMNHRYSYCKREAEEREAAEREAREKGHLEPTELLMNRAYLQSITPQGYSDSEERESMPRDGESEKEHEKEGEDGYGKLGRQDGDEXFXXXXXXSENKSMDTDPETIRDEEETGDHSMDDSSEDGKMETKSDHEEDNMEDGM
>ZEB2_HUMAN__O60315 RecName: Full=Zinc finger E-box-binding homeobox 2; AltName: Full=Smad-interacting protein 1; Short=SMADIP1; AltName: Full=Zinc finger homeobox protein 1b;
MKQPIMADGPRCKRRKQANPRRKNVVNYDNVVDTGSETDEEDKLHIAEDDGIANPLDQETSPASVPNHESSPHVSQALLPREEEEDEIREGGVEHPWHNNEILQASVDGPEEMKEDYDTMGPEATIQTAINNGTVKNANCTSDFEEYFAKRKLEERDGHAVSIEEYLQRSDTAIIYPEAPEELSRLGTPEANGQEENDLPPGTPDAFAQLLTCPYCDRGYKRLTSLKEHIKYRHEKNEENFSCPLCSYTFAYRTQLERHMVTHKPGTDQHQMLTQGAGNRKFKCTECGKAFKYKHHLKEHLRIHSGEKPYECPNCKKRFSHSGSYSSHISSKKCIGLISVNGRMRNNIKTGSSPNSVSSSPTNSAITQLRNKLENGKPLSMSEQTGLLKIKTEPLDFNDYKVLMATHGFSGTSPFMNGGLGATSPLGVHPSAQSPMQHLGVGMEAPLLGFPTMNSNLSEVQKVLQIVDNTVSRQKMDCKAEEISKLKGYHMKDPCSQPEEQGVTSPNIPPVGLPVVSHNGATKSIIDYTLEKVNEAKACLQSLTTDSRRQISNIKKEKLRTLIDLVTDDKMIENHNISTPFSCQFCKESFPGPIPLHQHERYLCKMNEEIKAVLQPHENIVPNKAGVFVDNKALLLSSVLSEKGMTSPINPYKDHMSVLKAYYAMNMEPNSDELLKISIAVGLPQEFVKEWFEQRKVYQYSNSRSPSLERSSKPLAPNSNPPTKDSLLPRSPVKPMDSITSPSIAELHNSVTNCDPPLRLTKPSHFTNIKPVEKLDHSRSNTPSPLNLSSTSSKNSHSSSYTPNSFSSEELQAEPLDLSLPKQMKEPKSIIATKNKTKASSISLDHNSVSSSSENSDEPLNLTFIKKEFSNSNNLDNKSTNPVFSMNPFSAKPLYTALPPQSAFPPATFMPPVQTSIPGLRPYPGLDQMSFLPHMAYTYPTGAATFADMQQRRKYQRKQGFQGELLDGAQDYMSGLDDMTDSDSCLSRKKIKKTESGMYACDLCDKTFQKSSSLLRHKYEHTGKRPHQCQICKKAFKHKHHLIEHSRLHSGEKPYQCDKCGKRFSHSGSYSQHMNHRYSYCKREAEEREAAEREAREKGHLEPTELLMNRAYLQSITPQGYSDSEERESMPRDGESEKEHEKEGEDGYGKLGRQDGDEEFEEEEEESENKSMDTDPETIRDEEETGDHSMDDSSEDGKMETKSDHEEDNMEDGM
>ZFH1_DROME__P28166-slimfinder Motifs
---------------------------------------------------------------------------C--C--RF------------------------------------------------------------------------------------------------P-DL-----------------------------------------------------------------------------------LDLS----------------G-Y-C-QC--SF-----L--H--LH-----------------------------------------------------------KEH-RIHS--KP--CDNC-KR--HSGS-----------------------------------------------------------------------------------------------------------------------------------------------------------------------------------IK-E------------------IK-E--PL-VA--------------------C--C-K-F-H-----------------------------------------------------------K-R-R-----------------------------------------------------------------------------T--DQPLDLSVKRDP--------------------------------------------------------------------------------------------------------------------------------------------------------K-RR--------------PY-CDQCDKAFA--SSL-RHKYEHSG-RPYQC-EC-KAFKHKHHLTEHKRLHSGEKPFQC-KC-KR--H-GSYSQHMNHRYSYCK----
>ZFH1_DROME__P28166-masked
XLSCLAPSSSRFGQEDTIIQQSMPSTSPFAMQFPSLASTLLHHNQSPKHSNPGSSGIQDAHPNQPGAAADAFLVKCXQCXXRFPEYQSLSEHIASEHPHDKLNCGAAQPESDAEDEQSNMSGSSRRYAKSPLASNNNSSTANANNNSTSSQSMNNNSELAKNHNSANKMSPMCSPGSLTPGDLFAQLQHPXXQLXPHLHAQFMXXXXSLAMQSARTASSPSQXXXXXLXXXXXLXXXXXHQMAMQQLLPPQLPGSNSSVGSNSAYDLDLSAPRSTSSPGSTTGDLSGAYPCMQCTASFASREQLEQHEQLHSPCGPXAXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXKEHVRIHSXXKPXXCDNCXKRXXHSGSFSSHMTSKKCISMGLKLNNNRALLKRLEKSPGSASSASRRSPSDHGKGKLPEQPSLPGLPHPMSYFASDAQVQGGSAAPAPFPPFXXXXXXXXXXXXXXXXXXXXXGLDPXXHPYSIQRLLQLSAAGQQQREXXRXEQXKXXQHDEEETPDEPKLVMDIEEPETKEMAPTPEATEAATPIKREESREASPDPESYRSSSQAIKQEQEPLNVAEERQTPVEEHAPVEHAADLRCSRCSKQFNHPTXXVXXXKXLXXXXKEELEQHFXXXQATSFALASASEXDXXDXXMDVXXEPRQESGERKVRVRTAINEEQXXXLKQHYSLNARPSRDEFRMIAARLXXXXXVVQVWFQNNRSRERKMQSFQNNQAAGAAPPMPIDSQASLTREDQPLDLSVKRDPLTPKSESSPPYIAPPSGEALNPEAINLSRKFSTSASMSPASISPSSAAALYFGAAPXXSXPNSQLDSTPRSGQAFPGLPPYMLPMSLPMEALFKMRPGGDFASNHALMNSIKLPDYRGTSLSPGGSEKRSWRDDDSRISHEDEFGAGVLMPPKPRRGKAETHGHAGDPDLPYVCDQCDKAFAKQSSLARHKYEHSGQRPYQCIECPKAFKHKHHLTEHKRLHSGEKPFQCSKCLKRXXHXGSYSQHMNHRYSYCKPYRE
>ZFH1_DROME__P28166 RecName: Full=Zinc finger protein 1; AltName: Full=Zinc finger homeodomain protein 1;
MLSCLAPSSSRFGQEDTIIQQSMPSTSPFAMQFPSLASTLLHHNQSPKHSNPGSSGIQDAHPNQPGAAADAFLVKCTQCHKRFPEYQSLSEHIASEHPHDKLNCGAAQPESDAEDEQSNMSGSSRRYAKSPLASNNNSSTANANNNSTSSQSMNNNSELAKNHNSANKMSPMCSPGSLTPGDLFAQLQHPPPQLPPHLHAQFMAAAASLAMQSARTASSPSQQQQQQLQQQQQLQQQQQHQMAMQQLLPPQLPGSNSSVGSNSAYDLDLSAPRSTSSPGSTTGDLSGAYPCMQCTASFASREQLEQHEQLHSPCGPAAVSNVSQTCRICHKAFANVYRLQRHMISHDESALLRKFKCKECDKAFKFKHHLKEHVRIHSGEKPFGCDNCGKRFSHSGSFSSHMTSKKCISMGLKLNNNRALLKRLEKSPGSASSASRRSPSDHGKGKLPEQPSLPGLPHPMSYFASDAQVQGGSAAPAPFPPFHPNYMNAALLAFPHNFMAAAAGLDPRVHPYSIQRLLQLSAAGQQQREEEREEQQKQQQHDEEETPDEPKLVMDIEEPETKEMAPTPEATEAATPIKREESREASPDPESYRSSSQAIKQEQEPLNVAEERQTPVEEHAPVEHAADLRCSRCSKQFNHPTELVQHEKVLCGLIKEELEQHFQQQQATSFALASASEEDEEDEEMDVEEEPRQESGERKVRVRTAINEEQQQQLKQHYSLNARPSRDEFRMIAARLQLDPRVVQVWFQNNRSRERKMQSFQNNQAAGAAPPMPIDSQASLTREDQPLDLSVKRDPLTPKSESSPPYIAPPSGEALNPEAINLSRKFSTSASMSPASISPSSAAALYFGAAPPPSPPNSQLDSTPRSGQAFPGLPPYMLPMSLPMEALFKMRPGGDFASNHALMNSIKLPDYRGTSLSPGGSEKRSWRDDDSRISHEDEFGAGVLMPPKPRRGKAETHGHAGDPDLPYVCDQCDKAFAKQSSLARHKYEHSGQRPYQCIECPKAFKHKHHLTEHKRLHSGEKPFQCSKCLKRFSHSGSYSQHMNHRYSYCKPYRE
>cbx4_XENLA__Q91647-slimfinder Motifs
--------------------------------------------------------F--R-R--Q-MGYRK-G-KP------------------------------LDLG-----H-Y-L--K-H--------------------KY-Y-L--KKHH-Y--D-----------------------------------------------------------------------------------------------K-K-K-GRI-IV-SK--E-G-----------------V--R--SP-------------------------------------------------------T--DQPL-LT-K------------------------------------------C-K-LT---------------------------------------D-RC-K-R---------------------------------------------------------
>cbx4_XENLA__Q91647-masked
XELPAVGEHXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXWEPEENXXDPRLLVAFQNRERQEQIMGYRKRGPKPKNNLVSMPSFARRSNVLSGLHDSSGENRTKLDLGPIPKSHQYQLNSKKHHQYQPSGKDHNEKHHSSNKKKYYYQLNSKKHHHYQPDPKLYEQYTIEKESQISTDVRNRHRDSLTHTQAADMGTQLKNGTDSVISGPERNGICNGVSSSPSTEMSSSPSTELSSSPSTELPSSGVGGKMKIVKNKNKNGRIVIVMSKYMENGMQSVKIKSSEEDCDMGDVRRRFDSPGTLNGDKTCTAQEEKTEHWKKRVESRVKIHEGSKSVDKGSVHLAGLRRTYSTASETLNDQPLQLTTKSSHVPMPNRTRSPVYAGEPYNDLVYTNPRKRCLSEANGNKELCKKTLTSRSVSAPGIVECKXGLTPLNVXLQEPDIILLDSDLDEXXDLRCVKSRCDSDQEVDKPEIQVTQNPQSVDVDVCEXXXXXXXXXXXXXXXXXXXXXXXXXXXITV
>cbx4_XENLA__Q91647 SubName: Full=XPolycomb {ECO:0000313|EMBL:AAC59728.1};
MELPAVGEHVFAVESIEKKRIRKGRVEYLVKWRGWSSKYNTWEPEENILDPRLLVAFQNRERQEQIMGYRKRGPKPKNNLVSMPSFARRSNVLSGLHDSSGENRTKLDLGPIPKSHQYQLNSKKHHQYQPSGKDHNEKHHSSNKKKYYYQLNSKKHHHYQPDPKLYEQYTIEKESQISTDVRNRHRDSLTHTQAADMGTQLKNGTDSVISGPERNGICNGVSSSPSTEMSSSPSTELSSSPSTELPSSGVGGKMKIVKNKNKNGRIVIVMSKYMENGMQSVKIKSSEEDCDMGDVRRRFDSPGTLNGDKTCTAQEEKTEHWKKRVESRVKIHEGSKSVDKGSVHLAGLRRTYSTASETLNDQPLQLTTKSSHVPMPNRTRSPVYAGEPYNDLVYTNPRKRCLSEANGNKELCKKTLTSRSVSAPGIVECKGGLTPLNVPLQEPDIILLDSDLDEPIDLRCVKSRCDSDQEVDKPEIQVTQNPQSVDVDVCESQFKPFFGNIVITDVTANCLTVTFKEYITV
slimfinder.l5w2o2a3.CtBP-NoEFilter.motifaln.fas is too large to return (6.47 MB > 1 MB) in full output. Try http://rest.slimsuite.unsw.edu.au/retrieve&jobid=15120800036&rest=motifaln[&password=X].
slimfinder.l5w2o2a3.CtBP-NoEFilter.maskaln.fas is too large to return (6.47 MB > 1 MB) in full output. Try http://rest.slimsuite.unsw.edu.au/retrieve&jobid=15120800036&rest=maskaln[&password=X].
ID   CBX4_HUMAN              Reviewed;         560 AA.
AC   O00257; B1PJR7; Q6TPI8; Q96C04;
DT   24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 3.
DT   11-NOV-2015, entry version 153.
DE   RecName: Full=E3 SUMO-protein ligase CBX4;
DE            EC=6.3.2.-;
DE   AltName: Full=Chromobox protein homolog 4;
DE   AltName: Full=Polycomb 2 homolog;
DE            Short=Pc2;
DE            Short=hPc2;
GN   Name=CBX4;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Fetal brain;
RX   PubMed=9315667;
RA   Satijn D.P.E., Olson D.J., van der Vlag J., Hamer K.M., Lambrechts C.,
RA   Masselink H., Gunster M.J., Sewalt R.G.A.B., van Driel R., Otte A.P.;
RT   "Interference with the expression of a novel human polycomb protein,
RT   hPc2, results in cellular transformation and apoptosis.";
RL   Mol. Cell. Biol. 17:6076-6086(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND SUBCELLULAR LOCATION.
RX   PubMed=19266028; DOI=10.1371/journal.pgen.1000397;
RA   Salichs E., Ledda A., Mularoni L., Alba M.M., de la Luna S.;
RT   "Genome-wide analysis of histidine repeats reveals their role in the
RT   localization of human proteins to the nuclear speckles compartment.";
RL   PLoS Genet. 5:E1000397-E1000397(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RA   Liu M., Cheng J., Wang L.;
RT   "Cloning and identification of NS5ATP1-binding protein 16.";
RL   Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16625196; DOI=10.1038/nature04689;
RA   Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA   Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA   Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA   Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA   DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R.,
RA   Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
RA   Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
RA   Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
RA   Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
RA   Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
RA   Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
RA   Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA   Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA   Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT   "DNA sequence of human chromosome 17 and analysis of rearrangement in
RT   the human lineage.";
RL   Nature 440:1045-1049(2006).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Colon;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 457-560 (ISOFORM 1).
RX   PubMed=9199346;
RA   Satijn D.P.E., Gunster M.J., van der Vlag J., Hamer K.M., Schul W.,
RA   Alkema M.J., Saurin A.J., Freemont P.S., van Driel R., Otte A.P.;
RT   "RING1 is associated with the polycomb group protein complex and acts
RT   as a transcriptional repressor.";
RL   Mol. Cell. Biol. 17:4105-4113(1997).
RN   [7]
RP   INTERACTION WITH SUV39H1.
RX   PubMed=12101246; DOI=10.1128/MCB.22.15.5539-5553.2002;
RA   Sewalt R.G.A.B., Lachner M., Vargas M., Hamer K.M., den Blaauwen J.L.,
RA   Hendrix T., Melcher M., Schweizer D., Jenuwein T., Otte A.P.;
RT   "Selective interactions between vertebrate polycomb homologs and the
RT   SUV39H1 histone lysine methyltransferase suggest that histone H3-K9
RT   methylation contributes to chromosomal targeting of Polycomb group
RT   proteins.";
RL   Mol. Cell. Biol. 22:5539-5553(2002).
RN   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN A PRC1-LIKE
RP   HPRC-H COMPLEX WITH BMI1; CBX2; CBX8; PHC1; PHC2; PHC3; RING1 AND
RP   RNF2.
RX   PubMed=12167701; DOI=10.1128/MCB.22.17.6070-6078.2002;
RA   Levine S.S., Weiss A., Erdjument-Bromage H., Shao Z., Tempst P.,
RA   Kingston R.E.;
RT   "The core of the polycomb repressive complex is compositionally and
RT   functionally conserved in flies and humans.";
RL   Mol. Cell. Biol. 22:6070-6078(2002).
RN   [9]
RP   FUNCTION, SUMOYLATION, AND SUBCELLULAR LOCATION.
RX   PubMed=12679040; DOI=10.1016/S0092-8674(03)00159-4;
RA   Kagey M.H., Melhuish T.A., Wotton D.;
RT   "The polycomb protein Pc2 is a SUMO E3.";
RL   Cell 113:127-137(2003).
RN   [10]
RP   SUMOYLATION AT LYS-494.
RX   PubMed=15592428; DOI=10.1038/sj.emboj.7600506;
RA   Kagey M.H., Melhuish T.A., Powers S.E., Wotton D.;
RT   "Multiple activities contribute to Pc2 E3 function.";
RL   EMBO J. 24:108-119(2005).
RN   [11]
RP   FUNCTION.
RX   PubMed=16061479; DOI=10.1074/jbc.M504477200;
RA   Long J., Zuo D., Park M.;
RT   "Pc2-mediated sumoylation of Smad-interacting protein 1 attenuates
RT   transcriptional repression of E-cadherin.";
RL   J. Biol. Chem. 280:35477-35489(2005).
RN   [12]
RP   FUNCTION, INTERACTION WITH HIPK2, SUMOYLATION, SUBCELLULAR LOCATION,
RP   AND PHOSPHORYLATION AT THR-497.
RX   PubMed=17018294; DOI=10.1016/j.molcel.2006.08.004;
RA   Roscic A., Moeller A., Calzado M.A., Renner F., Wimmer V.C.,
RA   Gresko E., Luedi K.S., Schmitz M.L.;
RT   "Phosphorylation-dependent control of Pc2 SUMO E3 ligase activity by
RT   its substrate protein HIPK2.";
RL   Mol. Cell 24:77-89(2006).
RN   [13]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [14]
RP   IDENTIFICATION IN A PRC1-LIKE COMPLEX.
RX   PubMed=19636380; DOI=10.1371/journal.pone.0006380;
RA   Maertens G.N., El Messaoudi-Aubert S., Racek T., Stock J.K.,
RA   Nicholls J., Rodriguez-Niedenfuhr M., Gil J., Peters G.;
RT   "Several distinct polycomb complexes regulate and co-localize on the
RT   INK4a tumor suppressor locus.";
RL   PLoS ONE 4:E6380-E6380(2009).
RN   [15]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-149, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19608861; DOI=10.1126/science.1175371;
RA   Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA   Walther T.C., Olsen J.V., Mann M.;
RT   "Lysine acetylation targets protein complexes and co-regulates major
RT   cellular functions.";
RL   Science 325:834-840(2009).
RN   [16]
RP   FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY (ISOFORM 2),
RP   IDENTIFICATION IN A PRC1-LIKE COMPLEX, SELF-ASSOCIATION, SUBCELLULAR
RP   LOCATION, AND MUTAGENESIS OF SER-434.
RX   PubMed=21282530; DOI=10.1074/mcp.M110.002642;
RA   Vandamme J., Volkel P., Rosnoblet C., Le Faou P., Angrand P.O.;
RT   "Interaction proteomics analysis of polycomb proteins defines distinct
RT   PRC1 Complexes in mammalian cells.";
RL   Mol. Cell. Proteomics 0:0-0(2011).
RN   [17]
RP   FUNCTION IN ZNF131 SUMOYLATION, SUBCELLULAR LOCATION, AND MUTAGENESIS
RP   OF LYS-494 AND THR-497.
RX   PubMed=22467880; DOI=10.1074/jbc.M111.336354;
RA   Oh Y., Chung K.C.;
RT   "Small ubiquitin-like modifier (SUMO) modification of zinc finger
RT   protein 131 potentiates its negative effect on estrogen signaling.";
RL   J. Biol. Chem. 287:17517-17529(2012).
RN   [18]
RP   FUNCTION.
RX   PubMed=22825850; DOI=10.1074/jbc.M112.390120;
RA   Pelisch F., Pozzi B., Risso G., Munoz M.J., Srebrow A.;
RT   "DNA damage-induced heterogeneous nuclear ribonucleoprotein K
RT   SUMOylation regulates p53 transcriptional activation.";
RL   J. Biol. Chem. 287:30789-30799(2012).
RN   [19]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-467, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
RA   Wang L., Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human
RT   liver phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [20]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-106; LYS-114; LYS-149;
RP   LYS-205; LYS-212 AND LYS-280, AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=25218447; DOI=10.1038/nsmb.2890;
RA   Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA   Vertegaal A.C.;
RT   "Uncovering global SUMOylation signaling networks in a site-specific
RT   manner.";
RL   Nat. Struct. Mol. Biol. 21:927-936(2014).
RN   [21]
RP   STRUCTURE BY NMR OF 8-65.
RG   Structural genomics consortium (SGC);
RT   "Solution NMR structure of the chromo domain of the chromobox protein
RT   homolog 4.";
RL   Submitted (FEB-2009) to the PDB data bank.
RN   [22]
RP   X-RAY CRYSTALLOGRAPHY (1.51 ANGSTROMS) OF 8-62.
RG   Structural genomics consortium (SGC);
RT   "Crystal structure of human chromobox homolog 4 (cbx4).";
RL   Submitted (SEP-2009) to the PDB data bank.
CC   -!- FUNCTION: E3 SUMO-protein ligase which facilitates SUMO1
CC       conjugation by UBE2I. Involved in the sumoylation of HNRNPK, a
CC       p53/TP53 transcriptional coactivator, hence indirectly regulates
CC       p53/TP53 transcriptional activation resulting in p21/CDKN1A
CC       expression. Monosumoylates ZNF131.
CC   -!- FUNCTION: Component of a Polycomb group (PcG) multiprotein PRC1-
CC       like complex, a complex class required to maintain the
CC       transcriptionally repressive state of many genes, including Hox
CC       genes, throughout development. PcG PRC1 complex acts via chromatin
CC       remodeling and modification of histones; it mediates
CC       monoubiquitination of histone H2A 'Lys-119', rendering chromatin
CC       heritably changed in its expressibility.
CC   -!- PATHWAY: Protein modification; protein sumoylation.
CC   -!- SUBUNIT: Interacts with histone H3-K9Me3. Interacts with CHTOP (By
CC       similarity). Component of a PRC1-like complex. Self-associates.
CC       Interacts with SUV39H1 and HIPK2. Interacts with CSNK2B.
CC       {ECO:0000250, ECO:0000269|PubMed:12101246,
CC       ECO:0000269|PubMed:12167701, ECO:0000269|PubMed:17018294,
CC       ECO:0000269|PubMed:19636380, ECO:0000269|PubMed:21282530}.
CC   -!- INTERACTION:
CC       P35226:BMI1; NbExp=4; IntAct=EBI-722425, EBI-2341576;
CC       P68400:CSNK2A1; NbExp=2; IntAct=EBI-4392727, EBI-347804;
CC       P67870:CSNK2B; NbExp=2; IntAct=EBI-4392727, EBI-348169;
CC       Q16665:HIF1A; NbExp=15; IntAct=EBI-722425, EBI-447269;
CC       Q9BYE7:PCGF6; NbExp=2; IntAct=EBI-4392727, EBI-1048026;
CC       Q99496:RNF2; NbExp=2; IntAct=EBI-4392727, EBI-722416;
CC       P31946:YWHAB; NbExp=2; IntAct=EBI-722425, EBI-359815;
CC       P62258:YWHAE; NbExp=2; IntAct=EBI-4392727, EBI-356498;
CC       P63104:YWHAZ; NbExp=2; IntAct=EBI-4392727, EBI-347088;
CC   -!- SUBCELLULAR LOCATION: Nucleus. Nucleus speckle. Note=Localization
CC       to nuclear polycomb bodies is required for ZNF131 sumoylation.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=O00257-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=O00257-3; Sequence=VSP_041599;
CC   -!- TISSUE SPECIFICITY: Ubiquitous.
CC   -!- DOMAIN: The polyhistidine repeat may act as a targeting signal to
CC       nuclear speckles. {ECO:0000269|PubMed:19266028}.
CC   -!- PTM: Phosphorylated on Thr-497 by HIPK2 upon DNA damage. This
CC       phosphorylation stimulates E3 SUMO-protein ligase activity and
CC       promotes sumoylation on Lys-494, as well as sumoylation of other
CC       target proteins, such as HNRNPK. {ECO:0000269|PubMed:12679040,
CC       ECO:0000269|PubMed:15592428, ECO:0000269|PubMed:17018294}.
CC   -!- MISCELLANEOUS: The human orthologs of the Drosophila Polycomb
CC       group protein Pc are CBX2, CBX4, CBX6, CBX7 and CBX8. These show
CC       distinct nuclear localizations, contribute differently to
CC       transcriptional repression, and appear to be part of distinct
CC       PRC1-like protein complexes. The hPRC-H complex purified in
CC       PubMed:12167701 probably presents a mixture of different complexes
CC       containing different Polycomb group proteins.
CC   -!- SIMILARITY: Contains 1 chromo domain. {ECO:0000255|PROSITE-
CC       ProRule:PRU00053}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH14967.1; Type=Miscellaneous discrepancy; Note=Aberrant splicing.; Evidence={ECO:0000305};
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DR   EMBL; AF013956; AAB80718.1; -; mRNA.
DR   EMBL; EU439707; ACA49234.1; -; mRNA.
DR   EMBL; AY390430; AAQ97596.1; -; mRNA.
DR   EMBL; AC100791; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC014967; AAH14967.1; ALT_SEQ; mRNA.
DR   EMBL; U94344; AAB62734.1; -; mRNA.
DR   CCDS; CCDS32758.1; -. [O00257-1]
DR   RefSeq; NP_003646.2; NM_003655.2. [O00257-1]
DR   UniGene; Hs.405046; -.
DR   PDB; 2K28; NMR; -; A=8-65.
DR   PDB; 3I8Z; X-ray; 1.51 A; A=8-62.
DR   PDBsum; 2K28; -.
DR   PDBsum; 3I8Z; -.
DR   ProteinModelPortal; O00257; -.
DR   SMR; O00257; 11-60.
DR   BioGrid; 114105; 75.
DR   DIP; DIP-42042N; -.
DR   IntAct; O00257; 47.
DR   MINT; MINT-1196265; -.
DR   STRING; 9606.ENSP00000269397; -.
DR   BindingDB; O00257; -.
DR   ChEMBL; CHEMBL3232685; -.
DR   PhosphoSite; O00257; -.
DR   BioMuta; CBX4; -.
DR   MaxQB; O00257; -.
DR   PaxDb; O00257; -.
DR   PRIDE; O00257; -.
DR   Ensembl; ENST00000269397; ENSP00000269397; ENSG00000141582. [O00257-1]
DR   GeneID; 8535; -.
DR   KEGG; hsa:8535; -.
DR   UCSC; uc002jxe.3; human. [O00257-1]
DR   CTD; 8535; -.
DR   GeneCards; CBX4; -.
DR   H-InvDB; HIX0014237; -.
DR   HGNC; HGNC:1554; CBX4.
DR   HPA; HPA008228; -.
DR   MIM; 603079; gene.
DR   neXtProt; NX_O00257; -.
DR   PharmGKB; PA26129; -.
DR   eggNOG; ENOG410IPQ6; Eukaryota.
DR   eggNOG; ENOG410ZQCR; LUCA.
DR   GeneTree; ENSGT00530000063056; -.
DR   HOGENOM; HOG000206923; -.
DR   HOVERGEN; HBG005257; -.
DR   InParanoid; O00257; -.
DR   KO; K11452; -.
DR   OMA; HHHHAVD; -.
DR   OrthoDB; EOG7PCJGP; -.
DR   PhylomeDB; O00257; -.
DR   TreeFam; TF106456; -.
DR   Reactome; R-HSA-2559580; Oxidative Stress Induced Senescence.
DR   Reactome; R-HSA-3108214; SUMOylation of DNA damage response and repair proteins.
DR   UniPathway; UPA00886; -.
DR   ChiTaRS; CBX4; human.
DR   EvolutionaryTrace; O00257; -.
DR   GenomeRNAi; 8535; -.
DR   NextBio; 31968; -.
DR   PRO; PR:O00257; -.
DR   Proteomes; UP000005640; Chromosome 17.
DR   Bgee; O00257; -.
DR   CleanEx; HS_CBX4; -.
DR   ExpressionAtlas; O00257; baseline and differential.
DR   Genevisible; O00257; HS.
DR   GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0031519; C:PcG protein complex; IDA:UniProtKB.
DR   GO; GO:0035102; C:PRC1 complex; IDA:UniProtKB.
DR   GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
DR   GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003727; F:single-stranded RNA binding; IEA:Ensembl.
DR   GO; GO:0032183; F:SUMO binding; IDA:MGI.
DR   GO; GO:0019789; F:SUMO transferase activity; EXP:Reactome.
DR   GO; GO:0003714; F:transcription corepressor activity; TAS:ProtInc.
DR   GO; GO:0044212; F:transcription regulatory region DNA binding; IEA:Ensembl.
DR   GO; GO:0044267; P:cellular protein metabolic process; TAS:Reactome.
DR   GO; GO:0016568; P:chromatin modification; IEA:UniProtKB-KW.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; TAS:ProtInc.
DR   GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IMP:UniProtKB.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR   GO; GO:0043687; P:post-translational protein modification; TAS:Reactome.
DR   GO; GO:0016925; P:protein sumoylation; TAS:Reactome.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
DR   InterPro; IPR000953; Chromo/shadow_dom.
DR   InterPro; IPR017984; Chromo_dom_subgr.
DR   InterPro; IPR023780; Chromo_domain.
DR   InterPro; IPR016197; Chromodomain-like.
DR   InterPro; IPR023779; Chromodomain_CS.
DR   Pfam; PF00385; Chromo; 1.
DR   PRINTS; PR00504; CHROMODOMAIN.
DR   SMART; SM00298; CHROMO; 1.
DR   SUPFAM; SSF54160; SSF54160; 1.
DR   PROSITE; PS00598; CHROMO_1; 1.
DR   PROSITE; PS50013; CHROMO_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative splicing; Chromatin regulator;
KW   Complete proteome; Isopeptide bond; Ligase; Nucleus; Phosphoprotein;
KW   Reference proteome; Repressor; Transcription;
KW   Transcription regulation; Ubl conjugation; Ubl conjugation pathway.
FT   CHAIN         1    560       E3 SUMO-protein ligase CBX4.
FT                                /FTId=PRO_0000080206.
FT   DOMAIN       11     69       Chromo. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00053}.
FT   REGION        1    539       Interaction with BMI1.
FT   REGION      540    560       Interaction with RNF2.
FT   COMPBIAS    378    400       His-rich.
FT   COMPBIAS    389    400       Poly-His.
FT   COMPBIAS    499    510       Poly-Ala.
FT   MOD_RES     149    149       N6-acetyllysine; alternate.
FT                                {ECO:0000244|PubMed:19608861}.
FT   MOD_RES     467    467       Phosphoserine.
FT                                {ECO:0000244|PubMed:24275569}.
FT   MOD_RES     497    497       Phosphothreonine; by HIPK2.
FT                                {ECO:0000269|PubMed:17018294}.
FT   CROSSLNK    106    106       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:25218447}.
FT   CROSSLNK    114    114       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:25218447}.
FT   CROSSLNK    149    149       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2);
FT                                alternate. {ECO:0000244|PubMed:25218447}.
FT   CROSSLNK    205    205       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:25218447}.
FT   CROSSLNK    212    212       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:25218447}.
FT   CROSSLNK    280    280       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:25218447}.
FT   CROSSLNK    494    494       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO).
FT   VAR_SEQ     127    396       Missing (in isoform 2).
FT                                {ECO:0000303|Ref.3}.
FT                                /FTId=VSP_041599.
FT   MUTAGEN     434    434       S->A: Abolishes interaction with YWHAZ
FT                                and YWHAE; impairs interaction with PCGF6
FT                                and BMI1; no effect on interaction with
FT                                RNF2. {ECO:0000269|PubMed:21282530}.
FT   MUTAGEN     494    494       K->R: No effect on ZNF131 sumoylation.
FT                                {ECO:0000269|PubMed:22467880}.
FT   MUTAGEN     497    497       T->A: Small decrease in ZNF131
FT                                sumoylation.
FT                                {ECO:0000269|PubMed:22467880}.
FT   CONFLICT    137    138       Missing (in Ref. 1; AAB80718).
FT                                {ECO:0000305}.
FT   CONFLICT    142    142       P -> R (in Ref. 1; AAB80718).
FT                                {ECO:0000305}.
FT   CONFLICT    458    458       P -> R (in Ref. 1; AAB80718 and 5;
FT                                AAB62734). {ECO:0000305}.
FT   CONFLICT    477    477       C -> S (in Ref. 1; AAB80718 and 5;
FT                                AAB62734). {ECO:0000305}.
FT   CONFLICT    480    480       T -> S (in Ref. 1; AAB80718 and 5;
FT                                AAB62734). {ECO:0000305}.
FT   CONFLICT    505    505       V -> VAA (in Ref. 3; ACA49234).
FT                                {ECO:0000305}.
FT   STRAND       13     22       {ECO:0000244|PDB:3I8Z}.
FT   STRAND       25     32       {ECO:0000244|PDB:3I8Z}.
FT   HELIX        37     39       {ECO:0000244|PDB:3I8Z}.
FT   STRAND       41     44       {ECO:0000244|PDB:3I8Z}.
FT   HELIX        45     48       {ECO:0000244|PDB:3I8Z}.
FT   HELIX        51     53       {ECO:0000244|PDB:3I8Z}.
SQ   SEQUENCE   560 AA;  61368 MW;  DF5C8C4C0CCB1F31 CRC64;
     MELPAVGEHV FAVESIEKKR IRKGRVEYLV KWRGWSPKYN TWEPEENILD PRLLIAFQNR
     ERQEQLMGYR KRGPKPKPLV VQVPTFARRS NVLTGLQDSS TDNRAKLDLG AQGKGQGHQY
     ELNSKKHHQY QPHSKERAGK PPPPGKSGKY YYQLNSKKHH PYQPDPKMYD LQYQGGHKEA
     PSPTCPDLGA KSHPPDKWAQ GAGAKGYLGA VKPLAGAAGA PGKGSEKGPP NGMMPAPKEA
     VTGNGIGGKM KIVKNKNKNG RIVIVMSKYM ENGMQAVKIK SGEVAEGEAR SPSHKKRAAD
     ERHPPADRTF KKAAGAEEKK VEAPPKRREE EVSGVSDPQP QDAGSRKLSP TKEAFGEQPL
     QLTTKPDLLA WDPARNTHPP SHHPHPHPHH HHHHHHHHHH AVGLNLSHVR KRCLSETHGE
     REPCKKRLTA RSISTPTCLG GSPAAERPAD LPPAAALPQP EVILLDSDLD EPIDLRCVKT
     RSEAGEPPSS LQVKPETPAS AAVAVAAAAA PTTTAEKPPA EAQDEPAESL SEFKPFFGNI
     IITDVTANCL TVTFKEYVTV
//
ID   COM1_HUMAN              Reviewed;         897 AA.
AC   Q99708; A6NKN2; A8K8W6; E7ETY1; O75371; Q8NHQ3;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 2.
DT   11-NOV-2015, entry version 147.
DE   RecName: Full=DNA endonuclease RBBP8;
DE            EC=3.1.-.-;
DE   AltName: Full=CtBP-interacting protein;
DE            Short=CtIP;
DE   AltName: Full=Retinoblastoma-binding protein 8;
DE            Short=RBBP-8;
DE   AltName: Full=Retinoblastoma-interacting protein and myosin-like;
DE            Short=RIM;
DE   AltName: Full=Sporulation in the absence of SPO11 protein 2 homolog;
DE            Short=SAE2;
GN   Name=RBBP8; Synonyms=CTIP;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND INTERACTION WITH RB1.
RX   PubMed=9721205; DOI=10.1006/geno.1998.5368;
RA   Fusco C., Reymond A., Zervos A.S.;
RT   "Molecular cloning and characterization of a novel retinoblastoma-
RT   binding protein.";
RL   Genomics 51:351-358(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND INTERACTION WITH CTBP1.
RX   PubMed=9535825; DOI=10.1074/jbc.273.15.8549;
RA   Schaeper U., Subramanian T., Lim L., Boyd J.M., Chinnadurai G.;
RT   "Interaction between a cellular protein that binds to the C-terminal
RT   region of adenovirus E1A (CtBP) and a novel cellular protein is
RT   disrupted by E1A through a conserved PLDLS motif.";
RL   J. Biol. Chem. 273:8549-8552(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Testis;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   TISSUE=Endometrial cancer;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA   Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA   Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16177791; DOI=10.1038/nature03983;
RA   Nusbaum C., Zody M.C., Borowsky M.L., Kamal M., Kodira C.D.,
RA   Taylor T.D., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K.,
RA   FitzGerald M.G., Yang X., Abouelleil A., Allen N.R., Anderson S.,
RA   Bloom T., Bugalter B., Butler J., Cook A., DeCaprio D., Engels R.,
RA   Garber M., Gnirke A., Hafez N., Hall J.L., Norman C.H., Itoh T.,
RA   Jaffe D.B., Kuroki Y., Lehoczky J., Lui A., Macdonald P., Mauceli E.,
RA   Mikkelsen T.S., Naylor J.W., Nicol R., Nguyen C., Noguchi H.,
RA   O'Leary S.B., Piqani B., Smith C.L., Talamas J.A., Topham K.,
RA   Totoki Y., Toyoda A., Wain H.M., Young S.K., Zeng Q., Zimmer A.R.,
RA   Fujiyama A., Hattori M., Birren B.W., Sakaki Y., Lander E.S.;
RT   "DNA sequence and analysis of human chromosome 18.";
RL   Nature 437:551-555(2005).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Testis;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [8]
RP   FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH BRCA1.
RX   PubMed=10764811; DOI=10.1074/jbc.M909494199;
RA   Yu X., Baer R.;
RT   "Nuclear localization and cell cycle-specific expression of CtIP, a
RT   protein that associates with the BRCA1 tumor suppressor.";
RL   J. Biol. Chem. 275:18541-18549(2000).
RN   [9]
RP   FUNCTION, PHOSPHORYLATION AT SER-664 AND SER-745, AND MUTAGENESIS OF
RP   SER-664 AND SER-745.
RX   PubMed=10910365; DOI=10.1038/35018134;
RA   Li S., Ting N.S.Y., Zheng L., Chen P.-L., Ziv Y., Shiloh Y.,
RA   Lee E.Y.-H.P., Lee W.-H.;
RT   "Functional link of BRCA1 and ataxia telangiectasia gene product in
RT   DNA damage response.";
RL   Nature 406:210-215(2000).
RN   [10]
RP   INTERACTION WITH LMO4.
RX   PubMed=11751867; DOI=10.1074/jbc.M110603200;
RA   Sum E.Y., Peng B., Yu X., Chen J., Byrne J., Lindeman G.J.,
RA   Visvader J.E.;
RT   "The LIM domain protein LMO4 interacts with the cofactor CtIP and the
RT   tumor suppressor BRCA1 and inhibits BRCA1 activity.";
RL   J. Biol. Chem. 277:7849-7856(2002).
RN   [11]
RP   INTERACTION WITH SIAH1, AND UBIQUITINATION.
RX   PubMed=14654780; DOI=10.1038/sj.onc.1206994;
RA   Germani A., Prabel A., Mourah S., Podgorniak M.-P., Di Carlo A.,
RA   Ehrlich R., Gisselbrecht S., Varin-Blank N., Calvo F.,
RA   Bruzzoni-Giovanelli H.;
RT   "SIAH-1 interacts with CtIP and promotes its degradation by the
RT   proteasome pathway.";
RL   Oncogene 22:8845-8851(2003).
RN   [12]
RP   SUBUNIT, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=15084581; DOI=10.1074/jbc.M313974200;
RA   Dubin M.J., Stokes P.H., Sum E.Y., Williams R.S., Valova V.A.,
RA   Robinson P.J., Lindeman G.J., Glover J.N., Visvader J.E.,
RA   Matthews J.M.;
RT   "Dimerization of CtIP, a BRCA1- and CtBP-interacting protein, is
RT   mediated by an N-terminal coiled-coil motif.";
RL   J. Biol. Chem. 279:26932-26938(2004).
RN   [13]
RP   FUNCTION, PHOSPHORYLATION AT SER-327, INTERACTION WITH BRCA1, AND
RP   MUTAGENESIS OF SER-327.
RX   PubMed=15485915; DOI=10.1128/MCB.24.21.9478-9486.2004;
RA   Yu X., Chen J.;
RT   "DNA damage-induced cell cycle checkpoint control requires CtIP, a
RT   phosphorylation-dependent binding partner of BRCA1 C-terminal
RT   domains.";
RL   Mol. Cell. Biol. 24:9478-9486(2004).
RN   [14]
RP   INTERACTION WITH BRCA1, FUNCTION, UBIQUITINATION, AND MUTAGENESIS OF
RP   SER-327.
RX   PubMed=16818604; DOI=10.1101/gad.1431006;
RA   Yu X., Fu S., Lai M., Baer R., Chen J.;
RT   "BRCA1 ubiquitinates its phosphorylation-dependent binding partner
RT   CtIP.";
RL   Genes Dev. 20:1721-1726(2006).
RN   [15]
RP   FUNCTION.
RX   PubMed=16581787; DOI=10.1128/MCB.26.8.3124-3134.2006;
RA   Liu F., Lee W.H.;
RT   "CtIP activates its own and cyclin D1 promoters via the E2F/RB pathway
RT   during G1/S progression.";
RL   Mol. Cell. Biol. 26:3124-3134(2006).
RN   [16]
RP   FUNCTION, PHOSPHORYLATION, SUBCELLULAR LOCATION, AND INTERACTION WITH
RP   BRCA1; MRE11A AND RAD50.
RX   PubMed=17965729; DOI=10.1038/nature06337;
RA   Sartori A.A., Lukas C., Coates J., Mistrik M., Fu S., Bartek J.,
RA   Baer R., Lukas J., Jackson S.P.;
RT   "Human CtIP promotes DNA end resection.";
RL   Nature 450:509-514(2007).
RN   [17]
RP   ASSOCIATION WITH OVARIAN CANCER SURVIVAL.
RX   PubMed=19270026; DOI=10.1093/hmg/ddp107;
RA   Quaye L., Dafou D., Ramus S.J., Song H., Gentry-Maharaj A.,
RA   Notaridou M., Hogdall E., Kjaer S.K., Christensen L., Hogdall C.,
RA   Easton D.F., Jacobs I., Menon U., Pharoah P.D., Gayther S.A.;
RT   "Functional complementation studies identify candidate genes and
RT   common genetic variants associated with ovarian cancer survival.";
RL   Hum. Mol. Genet. 18:1869-1878(2009).
RN   [18]
RP   FUNCTION, DNA-BINDING, PHOSPHORYLATION AT THR-847, AND MUTAGENESIS OF
RP   THR-847.
RX   PubMed=19202191; DOI=10.1074/jbc.M808906200;
RA   Huertas P., Jackson S.P.;
RT   "Human CtIP mediates cell cycle control of DNA end resection and
RT   double strand break repair.";
RL   J. Biol. Chem. 284:9558-9565(2009).
RN   [19]
RP   FUNCTION, INTERACTION WITH MRE11A; RAD50 AND NBN, AND MUTAGENESIS OF
RP   HIS-31; VAL-35; LYS-41 AND LEU-45.
RX   PubMed=19759395; DOI=10.1074/jbc.M109.023424;
RA   Yuan J., Chen J.;
RT   "N terminus of CtIP is critical for homologous recombination-mediated
RT   double-strand break repair.";
RL   J. Biol. Chem. 284:31746-31752(2009).
RN   [20]
RP   FUNCTION, AND MUTAGENESIS OF LYS-513 AND LYS-515.
RX   PubMed=20064462; DOI=10.1016/j.molcel.2009.12.002;
RA   You Z., Shi L.Z., Zhu Q., Wu P., Zhang Y.W., Basilio A., Tonnu N.,
RA   Verma I.M., Berns M.W., Hunter T.;
RT   "CtIP links DNA double-strand break sensing to resection.";
RL   Mol. Cell 36:954-969(2009).
RN   [21]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA   Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA   Rodionov V., Han D.K.;
RT   "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT   reveals system-wide modulation of protein-protein interactions.";
RL   Sci. Signal. 2:RA46-RA46(2009).
RN   [22]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-723, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA   Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full
RT   phosphorylation site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [23]
RP   FUNCTION, ACETYLATION AT LYS-432; LYS-526 AND LYS-604, INTERACTION
RP   WITH SIRT6, IDENTIFICATION BY MASS SPECTROMETRY, AND MUTAGENESIS OF
RP   LYS-432; LYS-526 AND LYS-604.
RX   PubMed=20829486; DOI=10.1126/science.1192049;
RA   Kaidi A., Weinert B.T., Choudhary C., Jackson S.P.;
RT   "Human SIRT6 promotes DNA end resection through CtIP deacetylation.";
RL   Science 329:1348-1353(2010).
RN   [24]
RP   ASSOCIATION WITH BREAST CANCER.
RX   PubMed=21799032; DOI=10.1158/0008-5472.CAN-11-0773;
RA   Rebbeck T.R., Mitra N., Domchek S.M., Wan F., Friebel T.M., Tran T.V.,
RA   Singer C.F., Tea M.K., Blum J.L., Tung N., Olopade O.I., Weitzel J.N.,
RA   Lynch H.T., Snyder C.L., Garber J.E., Antoniou A.C., Peock S.,
RA   Evans D.G., Paterson J., Kennedy M.J., Donaldson A., Dorkins H.,
RA   Easton D.F., Rubinstein W.S., Daly M.B., Isaacs C., Nevanlinna H.,
RA   Couch F.J., Andrulis I.L., Freidman E., Laitman Y., Ganz P.A.,
RA   Tomlinson G.E., Neuhausen S.L., Narod S.A., Phelan C.M., Greenberg R.,
RA   Nathanson K.L.;
RT   "Modification of BRCA1-associated breast and ovarian cancer risk by
RT   BRCA1-interacting genes.";
RL   Cancer Res. 71:5792-5805(2011).
RN   [25]
RP   INVOLVEMENT IN JWDS, AND INVOLVEMENT IN SCKL2.
RX   PubMed=21998596; DOI=10.1371/journal.pgen.1002310;
RA   Jackson S.P., Borglum A.D.;
RT   "CtIP mutations cause Seckel and Jawad syndromes.";
RL   PLoS Genet. 7:E1002310-E1002310(2011).
RN   [26]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-869, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25218447; DOI=10.1038/nsmb.2890;
RA   Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA   Vertegaal A.C.;
RT   "Uncovering global SUMOylation signaling networks in a site-specific
RT   manner.";
RL   Nat. Struct. Mol. Biol. 21:927-936(2014).
CC   -!- FUNCTION: Endonuclease that cooperates with the MRE11-RAD50-NBN
CC       (MRN) complex in processing meiotic and mitotic double-strand
CC       breaks (DSBs) by ensuring both resection and intrachromosomal
CC       association of the broken ends. Functions downstream of the MRN
CC       complex and ATM, promotes ATR activation and its recruitment to
CC       DSBs in the S/G2 phase facilitating the generation of ssDNA.
CC       Component of the BRCA1-RBBP8 complex that regulates CHEK1
CC       activation and controls cell cycle G2/M checkpoints on DNA damage.
CC       Promotes microhomology-mediated alternative end joining (A-NHEJ)
CC       during class-switch recombination and plays an essential role in
CC       chromosomal translocations. {ECO:0000269|PubMed:10764811,
CC       ECO:0000269|PubMed:10910365, ECO:0000269|PubMed:15485915,
CC       ECO:0000269|PubMed:16581787, ECO:0000269|PubMed:16818604,
CC       ECO:0000269|PubMed:17965729, ECO:0000269|PubMed:19202191,
CC       ECO:0000269|PubMed:19759395, ECO:0000269|PubMed:20064462,
CC       ECO:0000269|PubMed:20829486}.
CC   -!- SUBUNIT: Homodimer; dimerizes via the coiled coil domain.
CC       Interacts (via the PXDLS motif) with CTBP1; the interaction is
CC       disrupted via binding of the adenovirus E1A to CTBP1. Component of
CC       the BRCA1-RBBBP8 complex. Interacts (the Ser-327 phosphorylated
CC       form) with BRCA1 (via the C-terminal BRCA1 domains): the
CC       interaction occurs in the G2 phase, ubiquitinates RBBP8 and
CC       involves RBBP8 in BRCA1-dependent G2/M checkpoint control on DNA
CC       damage. Interacts with RB1. Interacts with the MRN complex.
CC       Interacts directly with MRE11A; the interaction is required for
CC       efficient homologous recombination (HR) and regulation of the MRN
CC       complex. Interacts directly with RAD50. Interacts directly with
CC       NBN. Interacts with SIRT6; the interaction deacetylates RBBP8 upon
CC       DNA damage. Interacts with LM04 (via the LIM zinc-binding 1
CC       domain). {ECO:0000269|PubMed:10764811,
CC       ECO:0000269|PubMed:11751867, ECO:0000269|PubMed:14654780,
CC       ECO:0000269|PubMed:15084581, ECO:0000269|PubMed:15485915,
CC       ECO:0000269|PubMed:16818604, ECO:0000269|PubMed:17965729,
CC       ECO:0000269|PubMed:19759395, ECO:0000269|PubMed:20829486,
CC       ECO:0000269|PubMed:9535825, ECO:0000269|PubMed:9721205}.
CC   -!- INTERACTION:
CC       P38398:BRCA1; NbExp=9; IntAct=EBI-745715, EBI-349905;
CC       Q9UQ84:EXO1; NbExp=3; IntAct=EBI-745715, EBI-944667;
CC       P25800:LMO1; NbExp=3; IntAct=EBI-10203615, EBI-8639312;
CC       P61968:LMO4; NbExp=3; IntAct=EBI-10203615, EBI-2798728;
CC       Q13526:PIN1; NbExp=3; IntAct=EBI-10203615, EBI-714158;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10764811,
CC       ECO:0000269|PubMed:17965729}. Note=Associates with sites of DNA
CC       damage in S/G2 phase. Ubiquitinated RBBP8 binds to chromatin
CC       following DNA damage.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q99708-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q99708-2; Sequence=VSP_043220;
CC       Name=3;
CC         IsoId=Q99708-3; Sequence=VSP_045247, VSP_045248;
CC         Note=No experimental confirmation available. Ref.4 (BX648221)
CC         sequence is in conflict in position: 862:S->G. {ECO:0000305};
CC   -!- INDUCTION: Levels increase dramatically as dividing cells traverse
CC       the G1/S boubdary. Down-regulated in tamoxifen-resistant breast
CC       cancer cells.
CC   -!- DOMAIN: The PXDLS motif binds to a cleft in CtBP proteins.
CC   -!- DOMAIN: The damage-recruitment motif is required for DNA binding
CC       and translocation to sites of DNA damage.
CC   -!- PTM: Acetylated. Deacetylation by SIRT6 upon DNA damage promotes
CC       DNA end resection. {ECO:0000269|PubMed:20829486}.
CC   -!- PTM: Hyperphosphorylation upon ionizing radiation results in
CC       dissociation from BRCA1. Phosphorylation at Thr-847 by CDK1 is
CC       essential for the recruitment to DNA and the DNA repair function.
CC       Phosphorylated on Ser-327 as cells enter G2 phase. This
CC       phosphorylation is required for binding BRCA1 and for the G2/M DNA
CC       damage transition checkpoint control.
CC       {ECO:0000269|PubMed:10910365, ECO:0000269|PubMed:15485915,
CC       ECO:0000269|PubMed:17965729, ECO:0000269|PubMed:19202191}.
CC   -!- PTM: Ubiquitinated. Ubiquitination at multiple sites by BRCA1 (via
CC       its N-terminal RING domain) does not lead to its proteosomal
CC       degradation but instead the ubiquitinated RBBP8 binds to chromatin
CC       following DNA damage and may play a role in G2/M checkpoint
CC       control. {ECO:0000269|PubMed:14654780,
CC       ECO:0000269|PubMed:16818604}.
CC   -!- DISEASE: Seckel syndrome 2 (SCKL2) [MIM:606744]: A rare autosomal
CC       recessive disorder characterized by proportionate dwarfism of
CC       prenatal onset associated with low birth weight, growth
CC       retardation, severe microcephaly with a bird-headed like
CC       appearance, and mental retardation. {ECO:0000269|PubMed:21998596}.
CC       Note=The disease is caused by mutations affecting the gene
CC       represented in this entry.
CC   -!- DISEASE: Jawad syndrome (JWDS) [MIM:251255]: A syndrome
CC       characterized by congenital microcephaly, moderately severe mental
CC       retardation, and symmetrical digital anomalies. Digital
CC       malformations of variable degree include hallux valgus, syndactyly
CC       of toes 4 and 5, short fifth fingers, single flexion crease of
CC       fifth fingers, polydactyly and synpolydactyly.
CC       {ECO:0000269|PubMed:21998596}. Note=The disease is caused by
CC       mutations affecting the gene represented in this entry.
CC   -!- DISEASE: Note=Genetic variability in RBBP8 is noted as a factor in
CC       BRCA1-associated breast cancer risk. Exhibits sensitivity to
CC       tamoxifen in certain breast cancer cell lines.
CC   -!- SIMILARITY: Belongs to the COM1/SAE2/CtIP family. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC       and Haematology;
CC       URL="http://atlasgeneticsoncology.org/Genes/RBBP8ID42066ch18q11.html";
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DR   EMBL; AF043431; AAC34368.1; -; mRNA.
DR   EMBL; U72066; AAC14371.1; -; mRNA.
DR   EMBL; AK292481; BAF85170.1; -; mRNA.
DR   EMBL; BX648221; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AC091147; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC106033; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471088; EAX01144.1; -; Genomic_DNA.
DR   EMBL; BC030590; AAH30590.1; -; mRNA.
DR   CCDS; CCDS11874.1; -. [Q99708-3]
DR   CCDS; CCDS11875.1; -. [Q99708-1]
DR   RefSeq; NP_002885.1; NM_002894.2. [Q99708-1]
DR   RefSeq; NP_976036.1; NM_203291.1. [Q99708-1]
DR   RefSeq; NP_976037.1; NM_203292.1. [Q99708-3]
DR   RefSeq; XP_006722582.1; XM_006722519.1. [Q99708-1]
DR   RefSeq; XP_006722583.1; XM_006722520.1. [Q99708-1]
DR   RefSeq; XP_006722584.1; XM_006722521.1. [Q99708-1]
DR   RefSeq; XP_011524434.1; XM_011526132.1. [Q99708-1]
DR   UniGene; Hs.546282; -.
DR   PDB; 2L4Z; NMR; -; A=641-685.
DR   PDB; 4D2H; X-ray; 1.90 A; A/B/C/D/E/F/G/H=18-52.
DR   PDBsum; 2L4Z; -.
DR   PDBsum; 4D2H; -.
DR   ProteinModelPortal; Q99708; -.
DR   SMR; Q99708; 18-52, 641-677.
DR   BioGrid; 111867; 43.
DR   DIP; DIP-24244N; -.
DR   IntAct; Q99708; 27.
DR   MINT; MINT-102295; -.
DR   STRING; 9606.ENSP00000323050; -.
DR   PhosphoSite; Q99708; -.
DR   BioMuta; RBBP8; -.
DR   DMDM; 116242745; -.
DR   MaxQB; Q99708; -.
DR   PaxDb; Q99708; -.
DR   PRIDE; Q99708; -.
DR   DNASU; 5932; -.
DR   Ensembl; ENST00000327155; ENSP00000323050; ENSG00000101773. [Q99708-1]
DR   Ensembl; ENST00000399722; ENSP00000382628; ENSG00000101773. [Q99708-1]
DR   Ensembl; ENST00000399725; ENSP00000382630; ENSG00000101773. [Q99708-3]
DR   GeneID; 5932; -.
DR   KEGG; hsa:5932; -.
DR   UCSC; uc002ktw.3; human. [Q99708-1]
DR   UCSC; uc002ktz.3; human.
DR   CTD; 5932; -.
DR   GeneCards; RBBP8; -.
DR   GeneReviews; RBBP8; -.
DR   HGNC; HGNC:9891; RBBP8.
DR   HPA; HPA039890; -.
DR   HPA; HPA052946; -.
DR   MIM; 251255; phenotype.
DR   MIM; 604124; gene.
DR   MIM; 606744; phenotype.
DR   neXtProt; NX_Q99708; -.
DR   Orphanet; 313795; Jawad syndrome.
DR   Orphanet; 808; Seckel syndrome.
DR   PharmGKB; PA34255; -.
DR   eggNOG; ENOG410IJ39; Eukaryota.
DR   eggNOG; ENOG410ZSBE; LUCA.
DR   GeneTree; ENSGT00530000063835; -.
DR   HOGENOM; HOG000293331; -.
DR   HOVERGEN; HBG057046; -.
DR   InParanoid; Q99708; -.
DR   OrthoDB; EOG771274; -.
DR   PhylomeDB; Q99708; -.
DR   TreeFam; TF106469; -.
DR   Reactome; R-HSA-912446; Meiotic recombination.
DR   ChiTaRS; RBBP8; human.
DR   EvolutionaryTrace; Q99708; -.
DR   GeneWiki; RBBP8; -.
DR   GenomeRNAi; 5932; -.
DR   NextBio; 23118; -.
DR   PRO; PR:Q99708; -.
DR   Proteomes; UP000005640; Chromosome 18.
DR   Bgee; Q99708; -.
DR   CleanEx; HS_RBBP8; -.
DR   ExpressionAtlas; Q99708; baseline and differential.
DR   Genevisible; Q99708; HS.
DR   GO; GO:0005730; C:nucleolus; IDA:HPA.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; TAS:ProtInc.
DR   GO; GO:0017053; C:transcriptional repressor complex; IDA:BHF-UCL.
DR   GO; GO:0003684; F:damaged DNA binding; IDA:UniProtKB.
DR   GO; GO:0001103; F:RNA polymerase II repressing transcription factor binding; IPI:BHF-UCL.
DR   GO; GO:0001106; F:RNA polymerase II transcription corepressor activity; IDA:BHF-UCL.
DR   GO; GO:0000014; F:single-stranded DNA endodeoxyribonuclease activity; IMP:UniProtKB.
DR   GO; GO:0001835; P:blastocyst hatching; IEA:Ensembl.
DR   GO; GO:0000075; P:cell cycle checkpoint; TAS:ProtInc.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0010792; P:DNA double-strand break processing involved in repair via single-strand annealing; IMP:UniProtKB.
DR   GO; GO:0006281; P:DNA repair; TAS:ProtInc.
DR   GO; GO:0000724; P:double-strand break repair via homologous recombination; IDA:UniProtKB.
DR   GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IEA:Ensembl.
DR   GO; GO:0031572; P:G2 DNA damage checkpoint; IDA:UniProtKB.
DR   GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0007067; P:mitotic nuclear division; IEA:UniProtKB-KW.
DR   GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:GOC.
DR   GO; GO:0006289; P:nucleotide-excision repair; IMP:CACAO.
DR   GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; TAS:ProtInc.
DR   GO; GO:0032355; P:response to estradiol; IEA:Ensembl.
DR   InterPro; IPR013882; Com1/Ctip_fam.
DR   InterPro; IPR019518; CtIP_N.
DR   Pfam; PF10482; CtIP_N; 1.
DR   Pfam; PF08573; SAE2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative splicing; Cell cycle;
KW   Cell division; Coiled coil; Complete proteome; DNA damage; DNA repair;
KW   DNA-binding; Dwarfism; Endonuclease; Hydrolase; Isopeptide bond;
KW   Meiosis; Mental retardation; Mitosis; Nuclease; Nucleus;
KW   Phosphoprotein; Polymorphism; Reference proteome; Ubl conjugation.
FT   CHAIN         1    897       DNA endonuclease RBBP8.
FT                                /FTId=PRO_0000097179.
FT   REGION       22     45       Essential for binding to the MRN complex
FT                                and for RPA focus formation on DNA
FT                                damage.
FT   REGION      509    557       Damage-recruitment motif.
FT   COILED       28    157       {ECO:0000255}.
FT   MOTIF       490    494       PXDLS motif.
FT   COMPBIAS    750    753       Poly-Glu.
FT   MOD_RES     233    233       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q80YR6}.
FT   MOD_RES     326    326       Phosphoserine.
FT                                {ECO:0000269|PubMed:17965729}.
FT   MOD_RES     327    327       Phosphoserine.
FT                                {ECO:0000269|PubMed:15485915}.
FT   MOD_RES     349    349       Phosphoserine.
FT                                {ECO:0000269|PubMed:17965729}.
FT   MOD_RES     432    432       N6-acetyllysine.
FT                                {ECO:0000269|PubMed:20829486}.
FT   MOD_RES     526    526       N6-acetyllysine.
FT                                {ECO:0000269|PubMed:20829486}.
FT   MOD_RES     604    604       N6-acetyllysine.
FT                                {ECO:0000269|PubMed:20829486}.
FT   MOD_RES     664    664       Phosphoserine; by ATM.
FT                                {ECO:0000269|PubMed:10910365}.
FT   MOD_RES     679    679       Phosphoserine.
FT                                {ECO:0000269|PubMed:17965729}.
FT   MOD_RES     723    723       Phosphoserine.
FT                                {ECO:0000244|PubMed:20068231}.
FT   MOD_RES     745    745       Phosphoserine; by ATM.
FT                                {ECO:0000269|PubMed:10910365}.
FT   MOD_RES     847    847       Phosphothreonine; by CDK1.
FT                                {ECO:0000269|PubMed:19202191}.
FT   CROSSLNK    869    869       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:25218447}.
FT   VAR_SEQ     714    714       S -> SMLFYI (in isoform 2).
FT                                {ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_043220.
FT   VAR_SEQ     786    867       RETSLQNFPHIEVVRKKEERRKLLGHTCKECEIYYADMPAE
FT                                EREKKLASCSRHRFRYIPPNTPENFWEVGFPSTQTCMERGY
FT                                -> SIMQICQQKKEKRNWLPAQDTDSATFHPTHQRIFGKLV
FT                                FLPLRLVWKEVILRKILILVLVQKDVSLTTQYFLQKARSRR
FT                                HRR (in isoform 3).
FT                                {ECO:0000303|PubMed:17974005}.
FT                                /FTId=VSP_045247.
FT   VAR_SEQ     868    897       Missing (in isoform 3).
FT                                {ECO:0000303|PubMed:17974005}.
FT                                /FTId=VSP_045248.
FT   VARIANT     357    357       K -> N (in dbSNP:rs34678569).
FT                                /FTId=VAR_051308.
FT   VARIANT     387    387       H -> Y (in dbSNP:rs1804732).
FT                                /FTId=VAR_028308.
FT   MUTAGEN      31     31       H->A: No effect on RPA focus formation on
FT                                DNA damage.
FT                                {ECO:0000269|PubMed:19759395}.
FT   MUTAGEN      35     35       V->A: No effect on RPA focus formation on
FT                                DNA damage.
FT                                {ECO:0000269|PubMed:19759395}.
FT   MUTAGEN      41     41       K->A: No effect on RPA focus formation on
FT                                DNA damage.
FT                                {ECO:0000269|PubMed:19759395}.
FT   MUTAGEN      45     45       L->A: No effect on RPA focus formation on
FT                                DNA damage.
FT                                {ECO:0000269|PubMed:19759395}.
FT   MUTAGEN     327    327       S->A: Abolishes BRCA1 interaction and
FT                                ubiquitination. No activation of CHEK1
FT                                after DNA damage.
FT                                {ECO:0000269|PubMed:15485915,
FT                                ECO:0000269|PubMed:16818604}.
FT   MUTAGEN     432    432       K->R: Greatly reduced acetylation.
FT                                Alleviates resection defects caused by
FT                                depletion of SIRT6; when associated with
FT                                R-526 and R-604.
FT                                {ECO:0000269|PubMed:20829486}.
FT   MUTAGEN     513    513       K->A: Abolishes damage recruitment
FT                                capability.
FT                                {ECO:0000269|PubMed:20064462}.
FT   MUTAGEN     515    515       K->A: Abolishes damage recruitment
FT                                capability.
FT                                {ECO:0000269|PubMed:20064462}.
FT   MUTAGEN     526    526       K->R: Greatly reduced acetylation.
FT                                Alleviates resection defects caused by
FT                                depletion of SIRT6; when associated with
FT                                R-432 and R-604.
FT                                {ECO:0000269|PubMed:20829486}.
FT   MUTAGEN     604    604       K->R: Greatly reduced acetylation.
FT                                Alleviates resection defects caused by
FT                                depletion of SIRT6; when associated with
FT                                R-432 and R-526.
FT                                {ECO:0000269|PubMed:20829486}.
FT   MUTAGEN     664    664       S->A: Abrogates dissociation of BRCA1.
FT                                {ECO:0000269|PubMed:10910365}.
FT   MUTAGEN     745    745       S->A: Abrogates dissociation of BRCA1.
FT                                {ECO:0000269|PubMed:10910365}.
FT   MUTAGEN     847    847       T->A: Impairs DNA resection.
FT                                {ECO:0000269|PubMed:19202191}.
FT   MUTAGEN     847    847       T->E: Mimics constitutive
FT                                phosphorylation.
FT                                {ECO:0000269|PubMed:19202191}.
FT   CONFLICT      4      4       S -> L (in Ref. 1; AAC14371).
FT                                {ECO:0000305}.
FT   CONFLICT     74     74       H -> Q (in Ref. 4; BX648221).
FT                                {ECO:0000305}.
FT   CONFLICT     92     92       C -> Y (in Ref. 3; BAF85170).
FT                                {ECO:0000305}.
FT   CONFLICT    123    123       E -> G (in Ref. 3; BAF85170).
FT                                {ECO:0000305}.
FT   CONFLICT    341    341       D -> G (in Ref. 4; BX648221).
FT                                {ECO:0000305}.
FT   CONFLICT    515    515       K -> R (in Ref. 4; BX648221).
FT                                {ECO:0000305}.
FT   CONFLICT    521    521       L -> P (in Ref. 3; BAF85170).
FT                                {ECO:0000305}.
FT   CONFLICT    642    642       L -> P (in Ref. 4; BX648221).
FT                                {ECO:0000305}.
FT   HELIX        18     50       {ECO:0000244|PDB:4D2H}.
FT   STRAND      648    650       {ECO:0000244|PDB:2L4Z}.
FT   HELIX       651    653       {ECO:0000244|PDB:2L4Z}.
FT   TURN        662    666       {ECO:0000244|PDB:2L4Z}.
FT   STRAND      677    679       {ECO:0000244|PDB:2L4Z}.
SQ   SEQUENCE   897 AA;  101942 MW;  E028DE56DE55C0F2 CRC64;
     MNISGSSCGS PNSADTSSDF KDLWTKLKEC HDREVQGLQV KVTKLKQERI LDAQRLEEFF
     TKNQQLREQQ KVLHETIKVL EDRLRAGLCD RCAVTEEHMR KKQQEFENIR QQNLKLITEL
     MNERNTLQEE NKKLSEQLQQ KIENDQQHQA AELECEEDVI PDSPITAFSF SGVNRLRRKE
     NPHVRYIEQT HTKLEHSVCA NEMRKVSKSS THPQHNPNEN EILVADTYDQ SQSPMAKAHG
     TSSYTPDKSS FNLATVVAET LGLGVQEESE TQGPMSPLGD ELYHCLEGNH KKQPFEESTR
     NTEDSLRFSD STSKTPPQEE LPTRVSSPVF GATSSIKSGL DLNTSLSPSL LQPGKKKHLK
     TLPFSNTCIS RLEKTRSKSE DSALFTHHSL GSEVNKIIIQ SSNKQILINK NISESLGEQN
     RTEYGKDSNT DKHLEPLKSL GGRTSKRKKT EEESEHEVSC PQASFDKENA FPFPMDNQFS
     MNGDCVMDKP LDLSDRFSAI QRQEKSQGSE TSKNKFRQVT LYEALKTIPK GFSSSRKASD
     GNCTLPKDSP GEPCSQECII LQPLNKCSPD NKPSLQIKEE NAVFKIPLRP RESLETENVL
     DDIKSAGSHE PIKIQTRSDH GGCELASVLQ LNPCRTGKIK SLQNNQDVSF ENIQWSIDPG
     ADLSQYKMDV TVIDTKDGSQ SKLGGETVDM DCTLVSETVL LKMKKQEQKG EKSSNEERKM
     NDSLEDMFDR TTHEEYESCL ADSFSQAADE EEELSTATKK LHTHGDKQDK VKQKAFVEPY
     FKGDERETSL QNFPHIEVVR KKEERRKLLG HTCKECEIYY ADMPAEEREK KLASCSRHRF
     RYIPPNTPEN FWEVGFPSTQ TCMERGYIKE DLDPCPRPKR RQPYNAIFSP KGKEQKT
//
ID   E1A_ADE02               Reviewed;         289 AA.
AC   P03254; P24934; Q67788;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   11-NOV-2015, entry version 96.
DE   RecName: Full=Early E1A protein {ECO:0000305};
DE   AltName: Full=Early E1A 32 kDa protein;
OS   Human adenovirus C serotype 2 (HAdV-2) (Human adenovirus 2).
OC   Viruses; dsDNA viruses, no RNA stage; Adenoviridae; Mastadenovirus.
OX   NCBI_TaxID=10515;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS EARLY E1A 32 KDA PROTEIN
RP   AND EARLY E1A 26 KDA PROTEIN).
RX   PubMed=551290; DOI=10.1038/281694a0;
RA   Perricaudet M., Akusjaervi G., Virtanen A., Pettersson U.;
RT   "Structure of two spliced mRNAs from the transforming region of human
RT   subgroup C adenoviruses.";
RL   Nature 281:694-696(1979).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS EARLY E1A 32 KDA PROTEIN;
RP   EARLY E1A 26 KDA PROTEIN AND EARLY E1A 6 KDA PROTEIN).
RX   PubMed=7142161;
RA   Gingeras T.R., Sciaky D., Gelinas R.E., Bing-Dong J., Yen C.E.,
RA   Kelly M.M., Bullock P.A., Parsons B.L., O'Neill K.E., Roberts R.J.;
RT   "Nucleotide sequences from the adenovirus-2 genome.";
RL   J. Biol. Chem. 257:13475-13491(1982).
RN   [3]
RP   INTERACTION WITH HOST ATF7, AND MUTAGENESIS OF CYS-157; THR-178 AND
RP   SER-185.
RX   PubMed=8417352;
RA   Chatton B., Bocco J.L., Gaire M., Hauss C., Reimund B., Goetz J.,
RA   Kedinger C.;
RT   "Transcriptional activation by the adenovirus larger E1a product is
RT   mediated by members of the cellular transcription factor ATF family
RT   which can directly associate with E1a.";
RL   Mol. Cell. Biol. 13:561-570(1993).
CC   -!- FUNCTION: Plays a role in viral genome replication by driving
CC       entry of quiescent cells into the cell cycle. Stimulation of
CC       progression from G1 to S phase allows the virus to efficiently use
CC       the cellular DNA replicating machinery to achieve viral genome
CC       replication. E1A protein has both transforming and trans-
CC       activating activities. Induces the disassembly of the E2F1
CC       transcription factor from RB1 by direct competition for the same
CC       binding site on RB1, with subsequent transcriptional activation of
CC       E2F1-regulated S-phase genes and of the E2 region of the
CC       adenoviral genome. Release of E2F1 leads to the ARF-mediated
CC       inhibition of MDM2 and causes TP53/p53 to accumulate because it is
CC       not targeted for degradation by MDM2-mediated ubiquitination
CC       anymore. This increase in TP53, in turn, would arrest the cell
CC       proliferation and direct its death but this effect is counteracted
CC       by the viral protein E1B-55K. Inactivation of the ability of RB1
CC       to arrest the cell cycle is critical for cellular transformation,
CC       uncontrolled cellular growth and proliferation induced by viral
CC       infection. Interaction with RBX1 and CUL1 inhibits ubiquitination
CC       of the proteins targeted by SCF(FBXW7) ubiquitin ligase complex,
CC       and may be linked to unregulated host cell proliferation. The
CC       tumorigenesis-restraining activity of E1A may be related to the
CC       disruption of the host CtBP-CtIP complex through the CtBP binding
CC       motif. Interacts with host TBP protein; this interaction probably
CC       disrupts the TBP-TATA complex. {ECO:0000250|UniProtKB:P03255}.
CC   -!- SUBUNIT: Interacts with host UBE2I; this interaction interferes
CC       with polySUMOylation. Interacts with host RB1; this interaction
CC       induces the aberrant dissociation of RB1-E2F1 complex thereby
CC       disrupting the activity of RB1 and activating E2F1-regulated
CC       genes. Interacts with host ATF7; the interaction enhances ATF7-
CC       mediated viral transactivation activity which requires the zinc
CC       binding domains of both proteins. Isoform early E1A 32 kDa protein
CC       and isoform early E1A 26 kDa protein interact (via N-terminus)
CC       with CUL1 and E3 ubiquitin ligase RBX1; these interactions inhibit
CC       RBX1-CUL1-dependent elongation reaction of ubiquitin chains and
CC       attenuate ubiquitination of SCF(FBXW7) target proteins. Interacts
CC       (via PXLXP motif) with host ZMYND11/BS69 (via MYND-type zinc
CC       finger); this interaction inhibits E1A mediated transactivation.
CC       Interacts with host EP300; this interaction stimulates the
CC       acetylation of RB1 by recruiting EP300 and RB1 into a multimeric-
CC       protein complex. Interacts with host CTBP1 and CTBP2; this
CC       interaction seems to potentiate viral replication. Interacts with
CC       host DCAF7. Interacts with host DYRK1A. Interacts with host KPNA4;
CC       this interaction allows E1A import into the host nucleus.
CC       Interacts with host EP400; this interaction stabilizes MYC.
CC       {ECO:0000250|UniProtKB:P03255}.
CC   -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000250|UniProtKB:P03255}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC         Comment=Isoforms are derived from the E1 region of the genome.;
CC       Name=early E1A 32 kDa protein; Synonyms=289R, L-E1A;
CC         IsoId=P03254-1; Sequence=Displayed;
CC       Name=early E1A 26 kDa protein; Synonyms=243R, S-E1A;
CC         IsoId=P03254-2; Sequence=VSP_000197;
CC       Name=early E1A 6 kDa protein;
CC         IsoId=P03254-3; Sequence=VSP_028916, VSP_028917;
CC   -!- SIMILARITY: Belongs to the adenoviridae E1A protein family.
CC       {ECO:0000305}.
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DR   EMBL; J01917; AAA92197.1; -; Genomic_DNA.
DR   EMBL; J01917; AAA92198.1; -; Genomic_DNA.
DR   EMBL; J01917; AAA92199.1; -; Genomic_DNA.
DR   PIR; A03824; Q2AD2.
DR   RefSeq; AP_000161.1; AC_000007.1.
DR   DIP; DIP-570N; -.
DR   IntAct; P03254; 1.
DR   MINT; MINT-198575; -.
DR   Proteomes; UP000008167; Genome.
DR   GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0039695; P:DNA-templated viral transcription; IDA:UniProtKB.
DR   GO; GO:0039645; P:modulation by virus of host G1/S transition checkpoint; IEA:UniProtKB-KW.
DR   GO; GO:0039649; P:modulation by virus of host ubiquitin-protein ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
DR   GO; GO:0039657; P:suppression by virus of host gene expression; IEA:UniProtKB-KW.
DR   GO; GO:0039563; P:suppression by virus of host STAT1 activity; IEA:UniProtKB-KW.
DR   GO; GO:0039502; P:suppression by virus of host type I interferon-mediated signaling pathway; IEA:UniProtKB-KW.
DR   InterPro; IPR014410; Aden_E1A.
DR   Pfam; PF02703; Adeno_E1A; 1.
PE   1: Evidence at protein level;
KW   Activator; Alternative splicing; Complete proteome; Early protein;
KW   Eukaryotic host gene expression shutoff by virus;
KW   Eukaryotic host transcription shutoff by virus;
KW   G1/S host cell cycle checkpoint dysregulation by virus;
KW   Host gene expression shutoff by virus; Host nucleus;
KW   Host-virus interaction;
KW   Inhibition of eukaryotic host transcription initiation by virus;
KW   Inhibition of host innate immune response by virus;
KW   Inhibition of host interferon signaling pathway by virus;
KW   Inhibition of host STAT1 by virus; Metal-binding;
KW   Modulation of host cell cycle by virus;
KW   Modulation of host E3 ubiquitin ligases by virus;
KW   Modulation of host ubiquitin pathway by virus; Oncogene;
KW   Phosphoprotein; Reference proteome; Transcription;
KW   Transcription regulation; Viral immunoevasion; Zinc; Zinc-finger.
FT   CHAIN         1    289       Early E1A protein.
FT                                /FTId=PRO_0000221692.
FT   ZN_FING     154    174       {ECO:0000250|UniProtKB:P03255}.
FT   REGION       41     49       Interaction with RB1 in competition with
FT                                E2F1. {ECO:0000250}.
FT   REGION       76    140       Interaction with UBE2I. {ECO:0000250}.
FT   MOTIF       113    117       PXLXP motif, interaction with host
FT                                ZMYND11. {ECO:0000250}.
FT   MOTIF       122    126       LXCXE motif, interaction with host RB1.
FT                                {ECO:0000255}.
FT   MOTIF       258    289       Bipartite nuclear localization signal.
FT                                {ECO:0000250|UniProtKB:P03255,
FT                                ECO:0000255}.
FT   MOTIF       279    283       PXDLS motif, CTBP-binding.
FT                                {ECO:0000250|UniProtKB:P03255}.
FT   MOD_RES      89     89       Phosphoserine; by host. {ECO:0000250}.
FT   MOD_RES     219    219       Phosphoserine; by host. {ECO:0000250}.
FT   MOD_RES     231    231       Phosphoserine; by host. {ECO:0000250}.
FT   VAR_SEQ      29     55       ADNLPPPSHFEPPTLHELYDLDVTAPE -> CLNLSLSPSQ
FT                                NRSLQDLPGVLNWCLLS (in isoform early E1A 6
FT                                kDa protein). {ECO:0000305}.
FT                                /FTId=VSP_028916.
FT   VAR_SEQ      56    289       Missing (in isoform early E1A 6 kDa
FT                                protein). {ECO:0000305}.
FT                                /FTId=VSP_028917.
FT   VAR_SEQ     140    185       Missing (in isoform early E1A 26 kDa
FT                                protein). {ECO:0000305}.
FT                                /FTId=VSP_000197.
FT   MUTAGEN     157    157       C->S: Abolishes ATF7-mediated
FT                                transcriptional activation.
FT                                {ECO:0000269|PubMed:8417352}.
FT   MUTAGEN     178    178       T->P: No effect on ATF7-mediated
FT                                transcriptional activation.
FT                                {ECO:0000269|PubMed:8417352}.
FT   MUTAGEN     185    185       S->R: Abolishes ATF7-mediated
FT                                transcriptional activation.
FT                                {ECO:0000269|PubMed:8417352}.
FT   CONFLICT     68     68       D -> E (in Ref. 2; AAA92197/AAA92199).
FT                                {ECO:0000305}.
FT   CONFLICT     81     81       L -> F (in Ref. 2; AAA92197/AAA92199).
FT                                {ECO:0000305}.
SQ   SEQUENCE   289 AA;  31851 MW;  4264747DAD74FFC5 CRC64;
     MRHIICHGGV ITEEMAASLL DQLIEEVLAD NLPPPSHFEP PTLHELYDLD VTAPEDPNEE
     AVSQIFPDSV MLAVQEGIDL LTFPPAPGSP EPPHLSRQPE QPEQRALGPV SMPNLVPEVI
     DLTCHEAGFP PSDDEDEEGE EFVLDYVEHP GHGCRSCHYH RRNTGDPDIM CSLCYMRTCG
     MFVYSPVSEP EPEPEPEPEP ARPTRRPKLV PAILRRPTSP VSRECNSSTD SCDSGPSNTP
     PEIHPVVPLC PIKPVAVRVG GRRQAVECIE DLLNESGQPL DLSCKRPRP
//
ID   ELK3_HUMAN              Reviewed;         407 AA.
AC   P41970; B2R6S6; Q6FG57; Q6GU29; Q9UD17;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 2.
DT   11-NOV-2015, entry version 142.
DE   RecName: Full=ETS domain-containing protein Elk-3;
DE   AltName: Full=ETS-related protein ERP;
DE   AltName: Full=ETS-related protein NET;
DE   AltName: Full=Serum response factor accessory protein 2;
DE            Short=SAP-2;
DE            Short=SRF accessory protein 2;
GN   Name=ELK3; Synonyms=NET, SAP2;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=7958835; DOI=10.1101/gad.8.13.1502;
RA   Giovane A., Pintzas A., Maira S.-M., Sobieszczuk P., Wasylyk B.;
RT   "Net, a new ets transcription factor that is activated by Ras.";
RL   Genes Dev. 8:1502-1513(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Placenta;
RX   PubMed=7540136;
RA   Price M.A., Rogers A.E., Treisman R.;
RT   "Comparative analysis of the ternary complex factors Elk-1, SAP-1a and
RT   SAP-2 (ERP/NET).";
RL   EMBO J. 14:2589-2601(1995).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT   "Cloning of human full open reading frames in Gateway(TM) system entry
RT   vector (pDONR201).";
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-115, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA   Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA   Greff Z., Keri G., Stemmann O., Mann M.;
RT   "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT   the kinome across the cell cycle.";
RL   Mol. Cell 31:438-448(2008).
CC   -!- FUNCTION: May be a negative regulator of transcription, but can
CC       activate transcription when coexpressed with Ras, Src or Mos.
CC       Forms a ternary complex with the serum response factor and the ETS
CC       and SRF motifs of the Fos serum response element.
CC   -!- SUBUNIT: Interacts with CTBP1.
CC   -!- INTERACTION:
CC       P16333:NCK1; NbExp=3; IntAct=EBI-1758534, EBI-389883;
CC       P27986:PIK3R1; NbExp=2; IntAct=EBI-1758534, EBI-79464;
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- SIMILARITY: Belongs to the ETS family. {ECO:0000305}.
CC   -!- SIMILARITY: Contains 1 ETS DNA-binding domain.
CC       {ECO:0000255|PROSITE-ProRule:PRU00237}.
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DR   EMBL; Z36715; CAA85309.1; -; mRNA.
DR   EMBL; CR542251; CAG47047.1; -; mRNA.
DR   EMBL; AK312694; BAG35573.1; -; mRNA.
DR   EMBL; CH471054; EAW97561.1; -; Genomic_DNA.
DR   EMBL; BC017371; AAH17371.1; -; mRNA.
DR   CCDS; CCDS9060.1; -.
DR   PIR; I38062; I38062.
DR   RefSeq; NP_005221.2; NM_005230.3.
DR   RefSeq; XP_006719338.1; XM_006719275.2.
DR   UniGene; Hs.46523; -.
DR   UniGene; Hs.718709; -.
DR   ProteinModelPortal; P41970; -.
DR   SMR; P41970; 2-151.
DR   BioGrid; 108319; 3.
DR   IntAct; P41970; 4.
DR   MINT; MINT-7242082; -.
DR   STRING; 9606.ENSP00000228741; -.
DR   PhosphoSite; P41970; -.
DR   BioMuta; ELK3; -.
DR   DMDM; 116241349; -.
DR   MaxQB; P41970; -.
DR   PaxDb; P41970; -.
DR   PRIDE; P41970; -.
DR   DNASU; 2004; -.
DR   Ensembl; ENST00000228741; ENSP00000228741; ENSG00000111145.
DR   GeneID; 2004; -.
DR   UCSC; uc001teo.1; human.
DR   CTD; 2004; -.
DR   GeneCards; ELK3; -.
DR   HGNC; HGNC:3325; ELK3.
DR   HPA; HPA001600; -.
DR   MIM; 600247; gene.
DR   neXtProt; NX_P41970; -.
DR   PharmGKB; PA27752; -.
DR   eggNOG; KOG3806; Eukaryota.
DR   eggNOG; ENOG410Z0ZF; LUCA.
DR   GeneTree; ENSGT00760000118996; -.
DR   HOGENOM; HOG000237332; -.
DR   HOVERGEN; HBG004344; -.
DR   InParanoid; P41970; -.
DR   OMA; EISAPPM; -.
DR   OrthoDB; EOG7NPFTD; -.
DR   PhylomeDB; P41970; -.
DR   TreeFam; TF317732; -.
DR   SignaLink; P41970; -.
DR   GeneWiki; ELK3; -.
DR   GenomeRNAi; 2004; -.
DR   NextBio; 8109; -.
DR   PRO; PR:P41970; -.
DR   Proteomes; UP000005640; Chromosome 12.
DR   Bgee; P41970; -.
DR   CleanEx; HS_ELK3; -.
DR   ExpressionAtlas; P41970; baseline and differential.
DR   Genevisible; P41970; HS.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR   GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; IC:HGNC.
DR   GO; GO:0032422; F:purine-rich negative regulatory element binding; IDA:HGNC.
DR   GO; GO:0000978; F:RNA polymerase II core promoter proximal region sequence-specific DNA binding; IDA:NTNU_SB.
DR   GO; GO:0003714; F:transcription corepressor activity; IDA:HGNC.
DR   GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; NAS:ProtInc.
DR   GO; GO:0001077; F:transcriptional activator activity, RNA polymerase II core promoter proximal region sequence-specific binding; IDA:NTNU_SB.
DR   GO; GO:0001525; P:angiogenesis; IEA:Ensembl.
DR   GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:HGNC.
DR   GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:NTNU_SB.
DR   GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR   GO; GO:0006366; P:transcription from RNA polymerase II promoter; IDA:GOC.
DR   GO; GO:0042060; P:wound healing; IEA:Ensembl.
DR   Gene3D; 1.10.10.10; -; 1.
DR   InterPro; IPR000418; Ets_dom.
DR   InterPro; IPR011991; WHTH_DNA-bd_dom.
DR   Pfam; PF00178; Ets; 1.
DR   PRINTS; PR00454; ETSDOMAIN.
DR   SMART; SM00413; ETS; 1.
DR   PROSITE; PS00345; ETS_DOMAIN_1; 1.
DR   PROSITE; PS00346; ETS_DOMAIN_2; 1.
DR   PROSITE; PS50061; ETS_DOMAIN_3; 1.
PE   1: Evidence at protein level;
KW   Activator; Complete proteome; DNA-binding; Nucleus; Phosphoprotein;
KW   Polymorphism; Reference proteome; Repressor; Transcription;
KW   Transcription regulation.
FT   CHAIN         1    407       ETS domain-containing protein Elk-3.
FT                                /FTId=PRO_0000204097.
FT   DNA_BIND      5     85       ETS. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00237}.
FT   MOTIF       273    277       CTBP-binding motif.
FT   COMPBIAS    207    212       Poly-Ala.
FT   MOD_RES     115    115       Phosphoserine.
FT                                {ECO:0000244|PubMed:18691976}.
FT   VARIANT     169    169       P -> L (in dbSNP:rs35332676).
FT                                /FTId=VAR_048946.
FT   CONFLICT    114    114       A -> V (in Ref. 1; CAA85309).
FT                                {ECO:0000305}.
FT   CONFLICT    117    117       E -> G (in Ref. 3; CAG47047).
FT                                {ECO:0000305}.
FT   CONFLICT    128    128       A -> V (in Ref. 1; CAA85309).
FT                                {ECO:0000305}.
FT   CONFLICT    152    152       Q -> E (in Ref. 1; CAA85309).
FT                                {ECO:0000305}.
FT   CONFLICT    163    163       T -> R (in Ref. 1; CAA85309).
FT                                {ECO:0000305}.
FT   CONFLICT    249    249       N -> K (in Ref. 1; CAA85309).
FT                                {ECO:0000305}.
SQ   SEQUENCE   407 AA;  44240 MW;  DD4515270ECED1E3 CRC64;
     MESAITLWQF LLQLLLDQKH EHLICWTSND GEFKLLKAEE VAKLWGLRKN KTNMNYDKLS
     RALRYYYDKN IIKKVIGQKF VYKFVSFPEI LKMDPHAVEI SRESLLLQDS DCKASPEGRE
     AHKHGLAALR STSRNEYIHS GLYSSFTINS LQNPPDAFKA IKTEKLEEPP EDSPPVEEVR
     TVIRFVTNKT DKHVTRPVVS LPSTSEAAAA SAFLASSVSA KISSLMLPNA ASISSASPFS
     SRSPSLSPNS PLPSEHRSLF LEAACHDSDS LEPLNLSSGS KTKSPSLPPK AKKPKGLEIS
     APPLVLSGTD IGSIALNSPA LPSGSLTPAF FTAQTPNGLL LTPSPLLSSI HFWSSLSPVA
     PLSPARLQGP STLFQFPTLL NGHMPVPIPS LDRAASPVLL SSNSQKS
//
ID   EVI1_HUMAN              Reviewed;        1051 AA.
AC   Q03112; A1L4F3; A8KA00; B7Z8W7; B7ZLQ3; B7ZLQ4; C9JAK0; D3DNP7;
AC   Q16122; Q5HYI1; Q6MZS6; Q8NEI5; Q99917;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   17-APR-2007, sequence version 2.
DT   11-NOV-2015, entry version 153.
DE   RecName: Full=MDS1 and EVI1 complex locus protein EVI1;
DE   AltName: Full=Ecotropic virus integration site 1 protein homolog;
DE            Short=EVI-1;
GN   Name=MECOM; Synonyms=EVI1;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND ALTERNATIVE SPLICING.
RX   PubMed=2115646;
RA   Morishita K., Parganas E., Douglass E.C., Ihle J.N.;
RT   "Unique expression of the human Evi-1 gene in an endometrial carcinoma
RT   cell line: sequence of cDNAs and structure of alternatively spliced
RT   transcripts.";
RL   Oncogene 5:963-971(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), AND CHROMOSOMAL TRANSLOCATION
RP   WITH RUNX1 IN CHRONIC MYELOCYTIC LEUKEMIA.
RX   PubMed=8313895;
RA   Mitani K., Ogawa S., Tanaka T., Miyoshi H., Kurokawa M., Mano H.,
RA   Yazaki Y., Ohki M., Hirai H.;
RT   "Generation of the AML1-EVI-1 fusion gene in the t(3;21)(q26;q22)
RT   causes blastic crisis in chronic myelocytic leukemia.";
RL   EMBO J. 13:504-510(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE [LARGE
RP   SCALE MRNA] OF 1-759 (ISOFORM 2).
RC   TISSUE=Trachea;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
RC   TISSUE=Adipose tissue, and Fetal kidney;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA   Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA   Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16641997; DOI=10.1038/nature04728;
RA   Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R.,
RA   Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R.,
RA   Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V.,
RA   Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.,
RA   Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B.,
RA   Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S.,
RA   Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q.,
RA   Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
RA   Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C.,
RA   Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G.,
RA   Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B.,
RA   Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R.,
RA   Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J.,
RA   Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A.,
RA   Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA   Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA   Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA   Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J.,
RA   Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H.,
RA   Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G.,
RA   Gibbs R.A.;
RT   "The DNA sequence, annotation and analysis of human chromosome 3.";
RL   Nature 440:1194-1198(2006).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4 AND 6), AND
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 516-1051 (ISOFORM 5).
RC   TISSUE=Lung;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 970-1007 (ISOFORM 1).
RX   PubMed=8700545;
RA   Ogawa S., Kurokawa M., Tanaka T., Mitani K., Inazawa J., Hangaishi A.,
RA   Tanaka K., Matsuo Y., Minowada J., Tsubota T., Yazaki Y., Hirai H.;
RT   "Structurally altered Evi-1 protein generated in the 3q21q26
RT   syndrome.";
RL   Oncogene 13:183-191(1996).
RN   [9]
RP   FUNCTION IN TGF-BETA SIGNALING, INTERACTION WITH SMAD3 AND SMAD4, AND
RP   SUBCELLULAR LOCATION.
RX   PubMed=9665135; DOI=10.1038/27945;
RA   Kurokawa M., Mitani K., Irie K., Matsuyama T., Takahashi T., Chiba S.,
RA   Yazaki Y., Matsumoto K., Hirai H.;
RT   "The oncoprotein Evi-1 represses TGF-beta signalling by inhibiting
RT   Smad3.";
RL   Nature 394:92-96(1998).
RN   [10]
RP   FUNCTION, AND INTERACTION WITH MAPK8 AND MAPK9.
RX   PubMed=10856240; DOI=10.1093/emboj/19.12.2958;
RA   Kurokawa M., Mitani K., Yamagata T., Takahashi T., Izutsu K.,
RA   Ogawa S., Moriguchi T., Nishida E., Yazaki Y., Hirai H.;
RT   "The evi-1 oncoprotein inhibits c-Jun N-terminal kinase and prevents
RT   stress-induced cell death.";
RL   EMBO J. 19:2958-2968(2000).
RN   [11]
RP   FUNCTION, ACETYLATION, INTERACTION WITH CREBBP; CTBP1; KAT2B AND
RP   HISTONE DEACETYLASES, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP   555-ASP-LEU-556 AND 586-ASP-LEU-587.
RX   PubMed=11568182; DOI=10.1074/jbc.M106733200;
RA   Chakraborty S., Senyuk V., Sitailo S., Chi Y., Nucifora G.;
RT   "Interaction of EVI1 with cAMP-responsive element-binding protein-
RT   binding protein (CBP) and p300/CBP-associated factor (P/CAF) results
RT   in reversible acetylation of EVI1 and in co-localization in nuclear
RT   speckles.";
RL   J. Biol. Chem. 276:44936-44943(2001).
RN   [12]
RP   FUNCTION, ALTERNATIVE SPLICING (ISOFORMS 1 AND 2),
RP   HOMOOLIGOMERIZATION, INTERACTION WITH CTBP1 AND SMAD3, AND SUBCELLULAR
RP   LOCATION.
RX   PubMed=15897867; DOI=10.1038/sj.onc.1208754;
RA   Nitta E., Izutsu K., Yamaguchi Y., Imai Y., Ogawa S., Chiba S.,
RA   Kurokawa M., Hirai H.;
RT   "Oligomerization of Evi-1 regulated by the PR domain contributes to
RT   recruitment of corepressor CtBP.";
RL   Oncogene 24:6165-6173(2005).
RN   [13]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA   Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA   Mann M.;
RT   "Global, in vivo, and site-specific phosphorylation dynamics in
RT   signaling networks.";
RL   Cell 127:635-648(2006).
RN   [14]
RP   FUNCTION IN APOPTOSIS.
RX   PubMed=16462766; DOI=10.1038/sj.onc.1209403;
RA   Liu Y., Chen L., Ko T.C., Fields A.P., Thompson E.A.;
RT   "Evi1 is a survival factor which conveys resistance to both TGFbeta-
RT   and taxol-mediated cell death via PI3K/AKT.";
RL   Oncogene 25:3565-3575(2006).
RN   [15]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18220336; DOI=10.1021/pr0705441;
RA   Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
RA   Yates J.R. III;
RT   "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
RT   efficient phosphoproteomic analysis.";
RL   J. Proteome Res. 7:1346-1351(2008).
RN   [16]
RP   FUNCTION.
RX   PubMed=19767769; DOI=10.1038/onc.2009.288;
RA   Shimabe M., Goyama S., Watanabe-Okochi N., Yoshimi A., Ichikawa M.,
RA   Imai Y., Kurokawa M.;
RT   "Pbx1 is a downstream target of Evi-1 in hematopoietic
RT   stem/progenitors and leukemic cells.";
RL   Oncogene 28:4364-4374(2009).
RN   [17]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-860, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA   Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full
RT   phosphorylation site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [18]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-2; LYS-367; LYS-497;
RP   LYS-533; LYS-547; LYS-564; LYS-599; LYS-948; LYS-953 AND LYS-973,
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-190 (ISOFORM 2), SUMOYLATION
RP   [LARGE SCALE ANALYSIS] AT LYS-66 (ISOFORM 4), AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25218447; DOI=10.1038/nsmb.2890;
RA   Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA   Vertegaal A.C.;
RT   "Uncovering global SUMOylation signaling networks in a site-specific
RT   manner.";
RL   Nat. Struct. Mol. Biol. 21:927-936(2014).
CC   -!- FUNCTION: Functions as a transcriptional regulator binding to DNA
CC       sequences in the promoter region of target genes and regulating
CC       positively or negatively their expression. Oncogene which plays a
CC       role in development, cell proliferation and differentiation. May
CC       also play a role in apoptosis through regulation of the JNK and
CC       TGF-beta signaling. Involved in hematopoiesis.
CC       {ECO:0000269|PubMed:10856240, ECO:0000269|PubMed:11568182,
CC       ECO:0000269|PubMed:15897867, ECO:0000269|PubMed:16462766,
CC       ECO:0000269|PubMed:19767769, ECO:0000269|PubMed:9665135}.
CC   -!- SUBUNIT: Homooligomer. Interacts with SUV39H1 (via SET domain);
CC       enhances MECOM transcriptional repression activity (By
CC       similarity). Interacts with CTBP1. Interacts with SMAD3 (via MH2
CC       domain); the interaction is direct. Interacts with SMAD4; through
CC       interaction with SMAD3. Interacts with CREBBP, KAT2B and histone
CC       deacetylases. Interacts with MAPK8 and MAPK9; inhibits JNK
CC       signaling. {ECO:0000250, ECO:0000269|PubMed:10856240,
CC       ECO:0000269|PubMed:11568182, ECO:0000269|PubMed:15897867,
CC       ECO:0000269|PubMed:9665135}.
CC   -!- INTERACTION:
CC       P56546:Ctbp2 (xeno); NbExp=3; IntAct=EBI-1384862, EBI-1384883;
CC       Q96EB6:SIRT1; NbExp=2; IntAct=EBI-1384862, EBI-1802965;
CC       Q9UBK9:UXT; NbExp=5; IntAct=EBI-1384862, EBI-357355;
CC   -!- SUBCELLULAR LOCATION: Nucleus. Nucleus speckle.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative promoter usage, Alternative splicing; Named isoforms=6;
CC       Name=1; Synonyms=Long, Evi-1a;
CC         IsoId=Q03112-1; Sequence=Displayed;
CC       Name=2; Synonyms=Evi-1c, Mds1/Evi1;
CC         IsoId=Q03112-3; Sequence=VSP_038733;
CC         Note=Produced by alternative promoter usage. Contains an
CC         additional SET domain at positions 79-194. Unable to form
CC         homooligomers, to interact with CTBP1 and SMAD3 and to repress
CC         TGF-beta signaling. Contains a glycyl lysine isopeptide
CC         (Lys-Gly) (interchain with G-Cter in SUMO2) at position 190.
CC         {ECO:0000244|PubMed:25218447};
CC       Name=3; Synonyms=Mds1;
CC         IsoId=Q13465-1; Sequence=External;
CC         Note=Produced by alternative promoter usage.;
CC       Name=4;
CC         IsoId=Q03112-4; Sequence=VSP_038734, VSP_038735;
CC         Note=Contains a glycyl lysine isopeptide (Lys-Gly) (interchain
CC         with G-Cter in SUMO2) at position 66.
CC         {ECO:0000244|PubMed:25218447};
CC       Name=5;
CC         IsoId=Q03112-5; Sequence=VSP_038736;
CC       Name=6;
CC         IsoId=Q03112-6; Sequence=VSP_038735, VSP_038736;
CC   -!- DOMAIN: Both zinc finger regions are required for the
CC       transcriptional activation of PBX1.
CC   -!- PTM: Phosphorylated. {ECO:0000250}.
CC   -!- PTM: May be acetylated by CREBBP and KAT2B.
CC       {ECO:0000269|PubMed:11568182}.
CC   -!- DISEASE: Note=A chromosomal aberration involving EVI1 is a cause
CC       of chronic myelogenous leukemia (CML). Translocation
CC       t(3;21)(q26;q22) with RUNX1/AML1.
CC   -!- SIMILARITY: Contains 10 C2H2-type zinc fingers.
CC       {ECO:0000255|PROSITE-ProRule:PRU00042}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB29907.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=AAB37456.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
CC       Sequence=AAI30521.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=BAH14103.1; Type=Miscellaneous discrepancy; Note=Aberrant splicing.; Evidence={ECO:0000305};
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DR   EMBL; X54989; CAA38735.1; -; mRNA.
DR   EMBL; S69002; AAB29907.1; ALT_INIT; mRNA.
DR   EMBL; AK292865; BAF85554.1; -; mRNA.
DR   EMBL; AK304098; BAH14103.1; ALT_SEQ; mRNA.
DR   EMBL; BX640908; CAE45952.1; -; mRNA.
DR   EMBL; BX647613; CAI46086.1; -; mRNA.
DR   EMBL; AC007849; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC024099; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC069220; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC074033; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC078985; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471052; EAW78553.1; -; Genomic_DNA.
DR   EMBL; CH471052; EAW78556.1; -; Genomic_DNA.
DR   EMBL; CH471052; EAW78557.1; -; Genomic_DNA.
DR   EMBL; BC031019; AAH31019.1; -; mRNA.
DR   EMBL; BC130520; AAI30521.1; ALT_INIT; mRNA.
DR   EMBL; BC143951; AAI43952.1; -; mRNA.
DR   EMBL; BC143952; AAI43953.1; -; mRNA.
DR   EMBL; S82592; AAB37456.1; ALT_SEQ; mRNA.
DR   CCDS; CCDS3205.1; -. [Q03112-1]
DR   CCDS; CCDS54669.1; -. [Q03112-5]
DR   CCDS; CCDS54670.1; -. [Q03112-4]
DR   PIR; A60191; A60191.
DR   PIR; S41705; S41705.
DR   RefSeq; NP_001098547.3; NM_001105077.3. [Q03112-4]
DR   RefSeq; NP_001098548.2; NM_001105078.3. [Q03112-1]
DR   RefSeq; NP_001157471.1; NM_001163999.1. [Q03112-6]
DR   RefSeq; NP_001157472.1; NM_001164000.1. [Q03112-5]
DR   RefSeq; NP_001192123.1; NM_001205194.1. [Q03112-1]
DR   RefSeq; NP_004982.2; NM_004991.3. [Q03112-3]
DR   RefSeq; NP_005232.2; NM_005241.3. [Q03112-1]
DR   RefSeq; XP_005247276.1; XM_005247219.2.
DR   RefSeq; XP_005247277.1; XM_005247220.2.
DR   RefSeq; XP_005247278.1; XM_005247221.2.
DR   RefSeq; XP_005247280.1; XM_005247223.2. [Q03112-1]
DR   RefSeq; XP_011510849.1; XM_011512547.1. [Q03112-4]
DR   RefSeq; XP_011510850.1; XM_011512548.1. [Q03112-4]
DR   UniGene; Hs.744090; -.
DR   ProteinModelPortal; Q03112; -.
DR   SMR; Q03112; 19-237, 733-813.
DR   BioGrid; 108423; 21.
DR   DIP; DIP-38639N; -.
DR   IntAct; Q03112; 3.
DR   STRING; 9606.ENSP00000264674; -.
DR   PhosphoSite; Q03112; -.
DR   BioMuta; ARHGAP32; -.
DR   DMDM; 145559472; -.
DR   MaxQB; Q03112; -.
DR   PaxDb; Q03112; -.
DR   PRIDE; Q03112; -.
DR   DNASU; 2122; -.
DR   Ensembl; ENST00000264674; ENSP00000264674; ENSG00000085276. [Q03112-4]
DR   Ensembl; ENST00000464456; ENSP00000419770; ENSG00000085276. [Q03112-5]
DR   Ensembl; ENST00000468789; ENSP00000419995; ENSG00000085276. [Q03112-1]
DR   Ensembl; ENST00000628990; ENSP00000486104; ENSG00000085276. [Q03112-1]
DR   GeneID; 2122; -.
DR   KEGG; hsa:2122; -.
DR   UCSC; uc003ffi.3; human. [Q03112-1]
DR   UCSC; uc003ffj.3; human. [Q03112-4]
DR   UCSC; uc003ffk.2; human. [Q03112-5]
DR   UCSC; uc011bpi.1; human. [Q03112-6]
DR   UCSC; uc011bpj.1; human. [Q03112-3]
DR   CTD; 2122; -.
DR   GeneCards; MECOM; -.
DR   H-InvDB; HIX0003836; -.
DR   HGNC; HGNC:3498; MECOM.
DR   HPA; HPA046537; -.
DR   HPA; HPA052977; -.
DR   MIM; 165215; gene.
DR   neXtProt; NX_Q03112; -.
DR   Orphanet; 402020; 'Acute myeloid leukemia with inv3(p21;q26.2) or t(3;3)(p21;q26.2)'.
DR   Orphanet; 52688; Myelodysplastic syndrome.
DR   PharmGKB; PA27912; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   eggNOG; COG5048; LUCA.
DR   GeneTree; ENSGT00530000063676; -.
DR   HOVERGEN; HBG005619; -.
DR   InParanoid; Q03112; -.
DR   KO; K04462; -.
DR   OrthoDB; EOG72G16H; -.
DR   PhylomeDB; Q03112; -.
DR   TreeFam; TF315309; -.
DR   Reactome; R-HSA-3214841; PKMTs methylate histone lysines.
DR   SignaLink; Q03112; -.
DR   ChiTaRS; MECOM; human.
DR   GeneWiki; MECOM; -.
DR   GenomeRNAi; 2122; -.
DR   NextBio; 8579; -.
DR   Proteomes; UP000005640; Chromosome 3.
DR   Bgee; Q03112; -.
DR   CleanEx; HS_EVI1; -.
DR   ExpressionAtlas; Q03112; baseline and differential.
DR   Genevisible; Q03112; HS.
DR   GO; GO:0016235; C:aggresome; IDA:HPA.
DR   GO; GO:0005737; C:cytoplasm; IDA:HPA.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR   GO; GO:0016607; C:nuclear speck; IDA:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR   GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IDA:UniProtKB.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0006325; P:chromatin organization; TAS:Reactome.
DR   GO; GO:0035115; P:embryonic forelimb morphogenesis; IEA:Ensembl.
DR   GO; GO:0035116; P:embryonic hindlimb morphogenesis; IEA:Ensembl.
DR   GO; GO:0030900; P:forebrain development; IEA:Ensembl.
DR   GO; GO:0071425; P:hematopoietic stem cell proliferation; ISS:UniProtKB.
DR   GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR   GO; GO:0006954; P:inflammatory response; IEA:Ensembl.
DR   GO; GO:0046329; P:negative regulation of JNK cascade; IMP:UniProtKB.
DR   GO; GO:0043069; P:negative regulation of programmed cell death; IMP:UniProtKB.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR   GO; GO:0001780; P:neutrophil homeostasis; IEA:Ensembl.
DR   GO; GO:0060039; P:pericardium development; IEA:Ensembl.
DR   GO; GO:0090336; P:positive regulation of brown fat cell differentiation; IEA:Ensembl.
DR   GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IEA:Ensembl.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR   GO; GO:0009791; P:post-embryonic development; IEA:Ensembl.
DR   GO; GO:0051726; P:regulation of cell cycle; IDA:UniProtKB.
DR   GO; GO:0042127; P:regulation of cell proliferation; IEA:Ensembl.
DR   GO; GO:0072001; P:renal system development; IEA:Ensembl.
DR   GO; GO:0009617; P:response to bacterium; IEA:Ensembl.
DR   GO; GO:0019827; P:stem cell population maintenance; IEA:Ensembl.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.160.60; -; 8.
DR   InterPro; IPR030413; Evi1/Prdm16.
DR   InterPro; IPR007087; Znf_C2H2.
DR   InterPro; IPR015880; Znf_C2H2-like.
DR   InterPro; IPR013087; Znf_C2H2/integrase_DNA-bd.
DR   PANTHER; PTHR24393; PTHR24393; 1.
DR   Pfam; PF00096; zf-C2H2; 3.
DR   SMART; SM00355; ZnF_C2H2; 10.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 8.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 10.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative promoter usage; Alternative splicing;
KW   Apoptosis; Chromosomal rearrangement; Complete proteome;
KW   Developmental protein; Differentiation; DNA-binding; Isopeptide bond;
KW   Metal-binding; Nucleus; Phosphoprotein; Polymorphism; Proto-oncogene;
KW   Reference proteome; Repeat; Transcription; Transcription regulation;
KW   Ubl conjugation; Zinc; Zinc-finger.
FT   CHAIN         1   1051       MDS1 and EVI1 complex locus protein EVI1.
FT                                /FTId=PRO_0000047273.
FT   ZN_FING      21     44       C2H2-type 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING      75     97       C2H2-type 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     103    125       C2H2-type 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     131    154       C2H2-type 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     160    182       C2H2-type 5. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     188    210       C2H2-type 6. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     217    239       C2H2-type 7. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     733    755       C2H2-type 8. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     761    784       C2H2-type 9. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     790    812       C2H2-type 10. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   REGION        1    252       Interaction with MAPK9, SMAD3 and
FT                                probably SUV39H1.
FT   MOTIF       421    434       Nuclear localization signal.
FT                                {ECO:0000255}.
FT   MOTIF       553    557       CTBP-binding motif 1. {ECO:0000250}.
FT   MOTIF       584    588       CTBP-binding motif 2. {ECO:0000250}.
FT   COMPBIAS    886    937       Asp/Glu-rich (acidic).
FT   MOD_RES     436    436       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P14404}.
FT   MOD_RES     552    552       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P14404}.
FT   MOD_RES     860    860       Phosphoserine.
FT                                {ECO:0000244|PubMed:20068231}.
FT   CROSSLNK      2      2       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:25218447}.
FT   CROSSLNK    367    367       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:25218447}.
FT   CROSSLNK    497    497       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:25218447}.
FT   CROSSLNK    533    533       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:25218447}.
FT   CROSSLNK    547    547       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:25218447}.
FT   CROSSLNK    564    564       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:25218447}.
FT   CROSSLNK    599    599       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:25218447}.
FT   CROSSLNK    948    948       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:25218447}.
FT   CROSSLNK    953    953       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:25218447}.
FT   CROSSLNK    973    973       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:25218447}.
FT   VAR_SEQ       1      1       M -> MRSKGRARKLATNNECVYGNYPEIPLEEMPDADGVA
FT                                STPSLNIQEPCSPATSSEAFTPKEGSPYKAPIYIPDDIPIP
FT                                AEFELRESNMPGAGLGIWTKRKIEVGEKFGPYVGEQRSNLK
FT                                DPSYGWEILDEFYNVKFCIDASQPDVGSWLKYIRFAGCYDQ
FT                                HNLVACQINDQIFYRVVADIAPGEELLLFM (in
FT                                isoform 2).
FT                                {ECO:0000303|PubMed:14702039}.
FT                                /FTId=VSP_038733.
FT   VAR_SEQ       1      1       M -> MILDEFYNVKFCIDASQPDVGSWLKYIRFAGCYDQH
FT                                NLVACQINDQIFYRVVADIAPGEELLLFM (in isoform
FT                                4). {ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_038734.
FT   VAR_SEQ     138    138       K -> KQ (in isoform 4 and isoform 6).
FT                                {ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_038735.
FT   VAR_SEQ     672    680       Missing (in isoform 5 and isoform 6).
FT                                {ECO:0000303|PubMed:15489334,
FT                                ECO:0000303|PubMed:17974005,
FT                                ECO:0000303|PubMed:8313895}.
FT                                /FTId=VSP_038736.
FT   VARIANT     107    107       Q -> R (in dbSNP:rs34896995).
FT                                /FTId=VAR_061928.
FT   MUTAGEN     555    556       DL->AS: Partial loss of interaction with
FT                                CTBP1. Loss of interaction with CTBP1;
FT                                when associated with 586-A-S-587.
FT                                {ECO:0000269|PubMed:11568182}.
FT   MUTAGEN     586    587       DL->AS: Partial loss of interaction with
FT                                CTBP1. Loss of interaction with CTBP1;
FT                                when associated with 555-A-S-556.
FT                                {ECO:0000269|PubMed:11568182}.
FT   CONFLICT     20     20       Q -> R (in Ref. 4; CAE45952).
FT                                {ECO:0000305}.
FT   CONFLICT    175    175       L -> P (in Ref. 4; CAE45952).
FT                                {ECO:0000305}.
FT   CONFLICT    301    301       F -> S (in Ref. 3; BAF85554).
FT                                {ECO:0000305}.
FT   CONFLICT    303    303       F -> V (in Ref. 1; CAA38735).
FT                                {ECO:0000305}.
FT   CONFLICT    443    443       S -> P (in Ref. 4; CAI46086).
FT                                {ECO:0000305}.
FT   CONFLICT    543    543       K -> R (in Ref. 4; CAE45952).
FT                                {ECO:0000305}.
FT   CONFLICT    730    730       K -> R (in Ref. 3; BAF85554).
FT                                {ECO:0000305}.
FT   CONFLICT    741    741       I -> V (in Ref. 4; CAI46086).
FT                                {ECO:0000305}.
FT   CONFLICT    796    796       D -> Y (in Ref. 1; CAA38735).
FT                                {ECO:0000305}.
FT   CONFLICT    875    875       D -> E (in Ref. 1; CAA38735).
FT                                {ECO:0000305}.
FT   CONFLICT    881    881       T -> P (in Ref. 1; CAA38735).
FT                                {ECO:0000305}.
FT   CONFLICT    906    906       N -> Y (in Ref. 1; CAA38735).
FT                                {ECO:0000305}.
FT   CONFLICT    992    992       V -> A (in Ref. 3; BAF85554).
FT                                {ECO:0000305}.
FT   CONFLICT   1013   1013       L -> P (in Ref. 4; CAE45952).
FT                                {ECO:0000305}.
SQ   SEQUENCE   1051 AA;  118276 MW;  BD132C53EA08D263 CRC64;
     MKSEDYPHET MAPDIHEERQ YRCEDCDQLF ESKAELADHQ KFPCSTPHSA FSMVEEDFQQ
     KLESENDLQE IHTIQECKEC DQVFPDLQSL EKHMLSHTEE REYKCDQCPK AFNWKSNLIR
     HQMSHDSGKH YECENCAKVF TDPSNLQRHI RSQHVGARAH ACPECGKTFA TSSGLKQHKH
     IHSSVKPFIC EVCHKSYTQF SNLCRHKRMH ADCRTQIKCK DCGQMFSTTS SLNKHRRFCE
     GKNHFAAGGF FGQGISLPGT PAMDKTSMVN MSHANPGLAD YFGANRHPAG LTFPTAPGFS
     FSFPGLFPSG LYHRPPLIPA SSPVKGLSST EQTNKSQSPL MTHPQILPAT QDILKALSKH
     PSVGDNKPVE LQPERSSEER PFEKISDQSE SSDLDDVSTP SGSDLETTSG SDLESDIESD
     KEKFKENGKM FKDKVSPLQN LASINNKKEY SNHSIFSPSL EEQTAVSGAV NDSIKAIASI
     AEKYFGSTGL VGLQDKKVGA LPYPSMFPLP FFPAFSQSMY PFPDRDLRSL PLKMEPQSPG
     EVKKLQKGSS ESPFDLTTKR KDEKPLTPVP SKPPVTPATS QDQPLDLSMG SRSRASGTKL
     TEPRKNHVFG GKKGSNVESR PASDGSLQHA RPTPFFMDPI YRVEKRKLTD PLEALKEKYL
     RPSPGFLFHP QFQLPDQRTW MSAIENMAEK LESFSALKPE ASELLQSVPS MFNFRAPPNA
     LPENLLRKGK ERYTCRYCGK IFPRSANLTR HLRTHTGEQP YRCKYCDRSF SISSNLQRHV
     RNIHNKEKPF KCHLCDRCFG QQTNLDRHLK KHENGNMSGT ATSSPHSELE STGAILDDKE
     DAYFTEIRNF IGNSNHGSQS PRNVEERMNG SHFKDEKALV TSQNSDLLDD EEVEDEVLLD
     EEDEDNDITG KTGKEPVTSN LHEGNPEDDY EETSALEMSC KTSPVRYKEE EYKSGLSALD
     HIRHFTDSLK MRKMEDNQYS EAELSSFSTS HVPEELKQPL HRKSKSQAYA MMLSLSDKES
     LHSTSHSSSN VWHSMARAAA ESSAIQSISH V
//
ID   FOG1_HUMAN              Reviewed;        1006 AA.
AC   Q8IX07;
DT   15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 2.
DT   11-NOV-2015, entry version 120.
DE   RecName: Full=Zinc finger protein ZFPM1;
DE   AltName: Full=Friend of GATA protein 1;
DE            Short=FOG-1;
DE            Short=Friend of GATA 1;
DE   AltName: Full=Zinc finger protein 89A;
DE   AltName: Full=Zinc finger protein multitype 1;
GN   Name=ZFPM1; Synonyms=FOG1, ZFN89A;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND INTERACTION WITH
RP   GATA1 AND GATA2.
RC   TISSUE=Megakaryocyte;
RX   PubMed=12483298; DOI=10.1007/s00439-002-0832-1;
RA   Freson K., Thys C., Wittewrongel C., Vermylen J., Hoylaerts M.F.,
RA   Van Geet C.;
RT   "Molecular cloning and characterization of the GATA1 cofactor human
RT   FOG1 and assessment of its binding to GATA1 proteins carrying D218
RT   substitutions.";
RL   Hum. Genet. 112:42-49(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15616553; DOI=10.1038/nature03187;
RA   Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X.,
RA   Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A.,
RA   Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.,
RA   Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L.,
RA   Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A.,
RA   Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D.,
RA   Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J.,
RA   Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA   Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I.,
RA   Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W.,
RA   Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A.,
RA   Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S.,
RA   Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA   Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA   Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L.,
RA   Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A.,
RA   Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L.,
RA   Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N.,
RA   Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M.,
RA   Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L.,
RA   Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D.,
RA   Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P.,
RA   Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M.,
RA   Rubin E.M., Pennacchio L.A.;
RT   "The sequence and analysis of duplication-rich human chromosome 16.";
RL   Nature 432:988-994(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Prostate cancer;
RX   PubMed=17487921; DOI=10.1002/elps.200600782;
RA   Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.;
RT   "Toward a global characterization of the phosphoproteome in prostate
RT   cancer cells: identification of phosphoproteins in the LNCaP cell
RT   line.";
RL   Electrophoresis 28:2027-2034(2007).
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic kidney;
RX   PubMed=17525332; DOI=10.1126/science.1140321;
RA   Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
RA   Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
RA   Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
RT   "ATM and ATR substrate analysis reveals extensive protein networks
RT   responsive to DNA damage.";
RL   Science 316:1160-1166(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-786, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA   Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT   a refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-901 AND SER-909, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA   Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA   Rodionov V., Han D.K.;
RT   "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT   reveals system-wide modulation of protein-protein interactions.";
RL   Sci. Signal. 2:RA46-RA46(2009).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-671; SER-786; SER-901
RP   AND SER-914, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
RA   Wang L., Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human
RT   liver phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
CC   -!- FUNCTION: Transcription regulator that plays an essential role in
CC       erythroid and megakaryocytic cell differentiation. Essential
CC       cofactor that acts via the formation of a heterodimer with
CC       transcription factors of the GATA family GATA1, GATA2 and GATA3.
CC       Such heterodimer can both activate or repress transcriptional
CC       activity, depending on the cell and promoter context. The
CC       heterodimer formed with GATA proteins is essential to activate
CC       expression of genes such as NFE2, ITGA2B, alpha- and beta-globin,
CC       while it represses expression of KLF1. May be involved in
CC       regulation of some genes in gonads. May also be involved in
CC       cardiac development, in a non-redundant way with ZFPM2/FOG2 (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with corepressor CTBP2; this interaction is
CC       however not essential for corepressor activity (By similarity).
CC       Interacts with the N-terminal zinc-finger of GATA1, GATA2 and
CC       probably GATA3. {ECO:0000250, ECO:0000269|PubMed:12483298}.
CC   -!- INTERACTION:
CC       P49841:GSK3B; NbExp=2; IntAct=EBI-3942619, EBI-373586;
CC       Q09028:RBBP4; NbExp=4; IntAct=EBI-3942619, EBI-620823;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Mainly expressed in hematopoietic tissues.
CC       Also expressed in adult cerebellum, stomach, lymph node, liver and
CC       pancreas. Expressed in fetal heart, liver and spleen.
CC       {ECO:0000269|PubMed:12483298}.
CC   -!- DOMAIN: The CCHC-type zinc fingers 1, 5, 6 and 9 directly bind to
CC       GATA-type zinc fingers. The Tyr residue adjacent to the last Cys
CC       of the CCHC-type zinc finger is essential for the interaction with
CC       GATA-type zinc fingers (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the FOG (Friend of GATA) family.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Contains 4 C2H2-type zinc fingers.
CC       {ECO:0000255|PROSITE-ProRule:PRU00042}.
CC   -!- SIMILARITY: Contains 5 C2HC-type zinc fingers. {ECO:0000305}.
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DR   EMBL; AF488691; AAN45858.1; -; mRNA.
DR   EMBL; AC116552; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC135049; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471184; EAW66806.1; -; Genomic_DNA.
DR   CCDS; CCDS32502.1; -.
DR   RefSeq; NP_722520.2; NM_153813.2.
DR   UniGene; Hs.632218; -.
DR   PDB; 2XU7; X-ray; 1.90 A; C/D=1-15.
DR   PDBsum; 2XU7; -.
DR   ProteinModelPortal; Q8IX07; -.
DR   SMR; Q8IX07; 85-209, 315-347.
DR   BioGrid; 127806; 10.
DR   DIP; DIP-48415N; -.
DR   IntAct; Q8IX07; 3.
DR   STRING; 9606.ENSP00000326630; -.
DR   PhosphoSite; Q8IX07; -.
DR   BioMuta; ZFPM1; -.
DR   DMDM; 296434508; -.
DR   MaxQB; Q8IX07; -.
DR   PaxDb; Q8IX07; -.
DR   PRIDE; Q8IX07; -.
DR   Ensembl; ENST00000319555; ENSP00000326630; ENSG00000179588.
DR   GeneID; 161882; -.
DR   KEGG; hsa:161882; -.
DR   UCSC; uc002fkv.3; human.
DR   CTD; 161882; -.
DR   GeneCards; ZFPM1; -.
DR   HGNC; HGNC:19762; ZFPM1.
DR   HPA; HPA046603; -.
DR   MIM; 601950; gene.
DR   neXtProt; NX_Q8IX07; -.
DR   PharmGKB; PA134920282; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   eggNOG; COG5048; LUCA.
DR   GeneTree; ENSGT00530000063823; -.
DR   HOGENOM; HOG000112626; -.
DR   HOVERGEN; HBG101018; -.
DR   InParanoid; Q8IX07; -.
DR   KO; K17441; -.
DR   OMA; YSCPAAP; -.
DR   OrthoDB; EOG74TWXR; -.
DR   PhylomeDB; Q8IX07; -.
DR   TreeFam; TF331342; -.
DR   Reactome; R-HSA-983231; Factors involved in megakaryocyte development and platelet production.
DR   ChiTaRS; ZFPM1; human.
DR   GeneWiki; ZFPM1; -.
DR   GenomeRNAi; 161882; -.
DR   NextBio; 88126; -.
DR   PRO; PR:Q8IX07; -.
DR   Proteomes; UP000005640; Chromosome 16.
DR   Bgee; Q8IX07; -.
DR   CleanEx; HS_ZFPM1; -.
DR   ExpressionAtlas; Q8IX07; baseline and differential.
DR   Genevisible; Q8IX07; HS.
DR   GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0005667; C:transcription factor complex; IDA:BHF-UCL.
DR   GO; GO:0017053; C:transcriptional repressor complex; IDA:BHF-UCL.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0001085; F:RNA polymerase II transcription factor binding; IPI:BHF-UCL.
DR   GO; GO:0008134; F:transcription factor binding; IPI:BHF-UCL.
DR   GO; GO:0001078; F:transcriptional repressor activity, RNA polymerase II core promoter proximal region sequence-specific binding; IDA:BHF-UCL.
DR   GO; GO:0060413; P:atrial septum morphogenesis; ISS:BHF-UCL.
DR   GO; GO:0003181; P:atrioventricular valve morphogenesis; ISS:BHF-UCL.
DR   GO; GO:0007596; P:blood coagulation; TAS:Reactome.
DR   GO; GO:0055008; P:cardiac muscle tissue morphogenesis; ISS:BHF-UCL.
DR   GO; GO:0060318; P:definitive erythrocyte differentiation; IEA:Ensembl.
DR   GO; GO:0035162; P:embryonic hemopoiesis; ISS:BHF-UCL.
DR   GO; GO:0030218; P:erythrocyte differentiation; ISS:BHF-UCL.
DR   GO; GO:0030851; P:granulocyte differentiation; IEA:Ensembl.
DR   GO; GO:0007507; P:heart development; IBA:GO_Central.
DR   GO; GO:0035855; P:megakaryocyte development; IEA:Ensembl.
DR   GO; GO:0030219; P:megakaryocyte differentiation; ISS:BHF-UCL.
DR   GO; GO:0003192; P:mitral valve formation; ISS:BHF-UCL.
DR   GO; GO:0045599; P:negative regulation of fat cell differentiation; ISS:BHF-UCL.
DR   GO; GO:0045403; P:negative regulation of interleukin-4 biosynthetic process; IDA:BHF-UCL.
DR   GO; GO:0060377; P:negative regulation of mast cell differentiation; ISS:BHF-UCL.
DR   GO; GO:0032091; P:negative regulation of protein binding; ISS:BHF-UCL.
DR   GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:GOC.
DR   GO; GO:0003151; P:outflow tract morphogenesis; ISS:BHF-UCL.
DR   GO; GO:0030220; P:platelet formation; IGI:BHF-UCL.
DR   GO; GO:0045078; P:positive regulation of interferon-gamma biosynthetic process; IDA:BHF-UCL.
DR   GO; GO:0060319; P:primitive erythrocyte differentiation; IEA:Ensembl.
DR   GO; GO:0032642; P:regulation of chemokine production; IEA:Ensembl.
DR   GO; GO:0010724; P:regulation of definitive erythrocyte differentiation; IDA:BHF-UCL.
DR   GO; GO:0002295; P:T-helper cell lineage commitment; IC:BHF-UCL.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
DR   GO; GO:0071733; P:transcriptional activation by promoter-enhancer looping; ISS:BHF-UCL.
DR   GO; GO:0003195; P:tricuspid valve formation; ISS:BHF-UCL.
DR   GO; GO:0060412; P:ventricular septum morphogenesis; ISS:BHF-UCL.
DR   Gene3D; 3.30.160.60; -; 2.
DR   InterPro; IPR007087; Znf_C2H2.
DR   InterPro; IPR015880; Znf_C2H2-like.
DR   InterPro; IPR013087; Znf_C2H2/integrase_DNA-bd.
DR   SMART; SM00355; ZnF_C2H2; 9.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 2.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 2.
PE   1: Evidence at protein level;
KW   3D-structure; Activator; Complete proteome; DNA-binding;
KW   Metal-binding; Nucleus; Phosphoprotein; Polymorphism;
KW   Reference proteome; Repeat; Repressor; Transcription;
KW   Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN         1   1006       Zinc finger protein ZFPM1.
FT                                /FTId=PRO_0000221041.
FT   ZN_FING     241    264       C2HC-type 1.
FT   ZN_FING     290    314       C2H2-type 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     320    342       C2H2-type 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     348    371       C2H2-type 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     577    699       C2HC-type 2.
FT   ZN_FING     683    705       C2HC-type 3.
FT   ZN_FING     817    839       C2HC-type 4.
FT   ZN_FING     854    877       C2H2-type 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     974   1000       C2HC-type 5.
FT   REGION      330    341       Interaction with TACC3. {ECO:0000250}.
FT   REGION      794    800       Interaction with CTBP2. {ECO:0000250}.
FT   MOD_RES     128    128       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:O35615}.
FT   MOD_RES     272    272       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:O35615}.
FT   MOD_RES     491    491       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:O35615}.
FT   MOD_RES     494    494       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:O35615}.
FT   MOD_RES     671    671       Phosphoserine.
FT                                {ECO:0000244|PubMed:24275569}.
FT   MOD_RES     786    786       Phosphoserine.
FT                                {ECO:0000244|PubMed:18669648,
FT                                ECO:0000244|PubMed:24275569}.
FT   MOD_RES     901    901       Phosphoserine.
FT                                {ECO:0000244|PubMed:19690332,
FT                                ECO:0000244|PubMed:24275569}.
FT   MOD_RES     909    909       Phosphoserine.
FT                                {ECO:0000244|PubMed:19690332}.
FT   MOD_RES     914    914       Phosphoserine.
FT                                {ECO:0000244|PubMed:24275569}.
FT   MOD_RES     935    935       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:O35615}.
FT   VARIANT      70     70       G -> A (in dbSNP:rs34916016).
FT                                /FTId=VAR_057491.
FT   CONFLICT     22     22       R -> G (in Ref. 1; AAN45858).
FT                                {ECO:0000305}.
FT   CONFLICT    444    447       EPLA -> AP (in Ref. 1; AAN45858).
FT                                {ECO:0000305}.
SQ   SEQUENCE   1006 AA;  104888 MW;  E9C2363503A64898 CRC64;
     MSRRKQSNPR QIKRSLGDME AREEVQLVGA SHMEQKATAP EAPSPPSADV NSPPPLPPPT
     SPGGPKELEG QEPEPRPTEE EPGSPWSGPD ELEPVVQDGQ RRIRARLSLA TGLSWGPFHG
     SVQTRASSPR QAEPSPALTL LLVDEACWLR TLPQALTEAE ANTEIHRKDD ALWCRVTKPV
     PAGGLLSVLL TAEPHSTPGH PVKKEPAEPT CPAPAHDLQL LPQQAGMASI LATAVINKDV
     FPCKDCGIWY RSERNLQAHL LYYCASRQGT GSPAAAATDE KPKETYPNER VCPFPQCRKS
     CPSASSLEIH MRSHSGERPF VCLICLSAFT TKANCERHLK VHTDTLSGVC HSCGFISTTR
     DILYSHLVTN HMVCQPGSKG EIYSPGAGHP ATKLPPDSLG SFQQQHTALQ GPLASADLGL
     APTPSPGLDR KALAEATNGE ARAEPLAQNG GSSEPPAAPR SIKVEAVEEP EAAPILGPGE
     PGPQAPSRTP SPRSPAPARV KAELSSPTPG SSPVPGELGL AGALFLPQYV FGPDAAPPAS
     EILAKMSELV HSRLQQGAGA GAGGAQTGLF PGAPKGATCF ECEITFSNVN NYYVHKRLYC
     SGRRAPEDAP AARRPKAPPG PARAPPGQPA EPDAPRSSPG PGAREEGAGG AATPEDGAGG
     RGSEGSQSPG SSVDDAEDDP SRTLCEACNI RFSRHETYTV HKRYYCASRH DPPPRRPAAP
     PGPPGPAAPP APSPAAPVRT RRRRKLYELH AAGAPPPPPP GHAPAPESPR PGSGSGSGPG
     LAPARSPGPA ADGPIDLSKK PRRPLPGAPA PALADYHECT ACRVSFHSLE AYLAHKKYSC
     PAAPPPGALG LPAAACPYCP PNGPVRGDLL EHFRLAHGLL LGAPLAGPGV EARTPADRGP
     SPAPAPAASP QPGSRGPRDG LGPEPQEPPP GPPPSPAAAP EAVPPPPAPP SYSDKGVQTP
     SKGTPAPLPN GNHRYCRLCN IKFSSLSTFI AHKKYYCSSH AAEHVK
//
ID   FOG2_HUMAN              Reviewed;        1151 AA.
AC   Q8WW38; Q32MA6; Q9NPL7; Q9NPS4; Q9UNI5;
DT   15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 3.
DT   11-NOV-2015, entry version 116.
DE   RecName: Full=Zinc finger protein ZFPM2;
DE   AltName: Full=Friend of GATA protein 2;
DE            Short=FOG-2;
DE            Short=Friend of GATA 2;
DE            Short=hFOG-2;
DE   AltName: Full=Zinc finger protein 89B;
DE   AltName: Full=Zinc finger protein multitype 2;
GN   Name=ZFPM2; Synonyms=FOG2, ZNF89B;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY,
RP   INTERACTION WITH CTBP2, AND POSSIBLE INTERACTION WITH GATA1.
RC   TISSUE=Erythroleukemia;
RX   PubMed=10438528; DOI=10.1074/jbc.274.33.23491;
RA   Holmes M., Turner J., Fox A.H., Chisholm O., Crossley M., Chong B.;
RT   "hFOG-2, a novel zinc finger protein, binds the co-repressor mCtBP2
RT   and modulates GATA-mediated activation.";
RL   J. Biol. Chem. 274:23491-23498(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Prostate;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-287 (ISOFORM 2), AND
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 641-1151 (ISOFORM 1).
RG   The European IMAGE consortium;
RL   Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   SUMOYLATION AT LYS-324; LYS-471; LYS-915 AND LYS-955, AND SUBCELLULAR
RP   LOCATION.
RX   PubMed=23226341; DOI=10.1371/journal.pone.0050637;
RA   Perdomo J., Jiang X.M., Carter D.R., Khachigian L.M., Chong B.H.;
RT   "SUMOylation regulates the transcriptional repression activity of FOG-
RT   2 and its association with GATA-4.";
RL   PLoS ONE 7:E50637-E50637(2012).
RN   [5]
RP   INTERACTION WITH GATA4, INVOLVEMENT IN SRXY9, VARIANTS SRXY9 GLN-260;
RP   ARG-402 AND ILE-544, VARIANTS GLY-403 AND ASP-782, AND
RP   CHARACTERIZATION OF VARIANTS GLN-260 AND ARG-402.
RX   PubMed=24549039; DOI=10.1093/hmg/ddu074;
RA   Bashamboo A., Brauner R., Bignon-Topalovic J., Lortat-Jacob S.,
RA   Karageorgou V., Lourenco D., Guffanti A., McElreavey K.;
RT   "Mutations in the FOG2/ZFPM2 gene are associated with anomalies of
RT   human testis determination.";
RL   Hum. Mol. Genet. 23:3657-3665(2014).
RN   [6]
RP   VARIANTS TOF GLY-30 AND GLY-657, AND CHARACTERIZATION OF VARIANTS TOF
RP   GLY-30 AND GLY-657.
RX   PubMed=14517948; DOI=10.1002/humu.10261;
RA   Pizzuti A., Sarkozy A., Newton A.L., Conti E., Flex E., Digilio M.C.,
RA   Amati F., Gianni D., Tandoi C., Marino B., Crossley M.,
RA   Dallapiccola B.;
RT   "Mutations of ZFPM2/FOG2 gene in sporadic cases of tetralogy of
RT   Fallot.";
RL   Hum. Mutat. 22:372-377(2003).
RN   [7]
RP   INVOLVEMENT IN DIH3.
RX   PubMed=16103912; DOI=10.1371/journal.pgen.0010010;
RA   Ackerman K.G., Herron B.J., Vargas S.O., Huang H., Tevosian S.G.,
RA   Kochilas L., Rao C., Pober B.R., Babiuk R.P., Epstein J.A.,
RA   Greer J.J., Beier D.R.;
RT   "Fog2 is required for normal diaphragm and lung development in mice
RT   and humans.";
RL   PLoS Genet. 1:58-65(2005).
RN   [8]
RP   VARIANT TOF ILE-544, AND VARIANTS CTHM GLY-30 AND VAL-227.
RX   PubMed=20807224; DOI=10.1111/j.1399-0004.2010.01523.x;
RA   De Luca A., Sarkozy A., Ferese R., Consoli F., Lepri F., Dentici M.L.,
RA   Vergara P., De Zorzi A., Versacci P., Digilio M.C., Marino B.,
RA   Dallapiccola B.;
RT   "New mutations in ZFPM2/FOG2 gene in tetralogy of Fallot and double
RT   outlet right ventricle.";
RL   Clin. Genet. 80:184-190(2011).
CC   -!- FUNCTION: Transcription regulator that plays a central role in
CC       heart morphogenesis and development of coronary vessels from
CC       epicardium, by regulating genes that are essential during
CC       cardiogenesis. Essential cofactor that acts via the formation of a
CC       heterodimer with transcription factors of the GATA family GATA4,
CC       GATA5 and GATA6. Such heterodimer can both activate or repress
CC       transcriptional activity, depending on the cell and promoter
CC       context. Also required in gonadal differentiation, possibly be
CC       regulating expression of SRY. Probably acts a corepressor of NR2F2
CC       (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with the N-terminal zinc-finger of GATA4, GATA5
CC       and probably GATA6. Interacts with retinoid nuclear receptor RXRA
CC       when ligand bound (By similarity). Interacts with corepressor
CC       CTBP2; this interaction is however not essential for corepressor
CC       activity. Able to bind GATA1 in vitro. Interacts with NR2F2 and
CC       NR2F6 (By similarity). Interacts with ATOH8; mediates indirect
CC       interaction with GATA4 (By similarity).
CC       {ECO:0000250|UniProtKB:Q8WW38, ECO:0000269|PubMed:10438528,
CC       ECO:0000269|PubMed:24549039}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23226341}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8WW38-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8WW38-2; Sequence=VSP_009701, VSP_009702;
CC         Note=Sequence incomplete. No experimental confirmation
CC         available.;
CC   -!- TISSUE SPECIFICITY: Widely expressed at low level.
CC       {ECO:0000269|PubMed:10438528}.
CC   -!- DOMAIN: The CCHC-type zinc fingers 1, 5, 6 and 8 directly bind to
CC       GATA-type zinc fingers. The Tyr residue adjacent to the last Cys
CC       of the CCHC-type zinc finger is essential for the interaction with
CC       GATA-type zinc fingers (By similarity). {ECO:0000250}.
CC   -!- PTM: Sumoylation reduces transcriptional repression activity.
CC       {ECO:0000269|PubMed:23226341}.
CC   -!- DISEASE: Tetralogy of Fallot (TOF) [MIM:187500]: A congenital
CC       heart anomaly which consists of pulmonary stenosis, ventricular
CC       septal defect, dextroposition of the aorta (aorta is on the right
CC       side instead of the left) and hypertrophy of the right ventricle.
CC       In this condition, blood from both ventricles (oxygen-rich and
CC       oxygen-poor) is pumped into the body often causing cyanosis.
CC       {ECO:0000269|PubMed:14517948, ECO:0000269|PubMed:20807224}.
CC       Note=The disease may be caused by mutations affecting the gene
CC       represented in this entry.
CC   -!- DISEASE: Diaphragmatic hernia 3 (DIH3) [MIM:610187]: Form of
CC       congenital diaphragmatic hernia (CDH). CDH refers to a group of
CC       congenital defects in the structural integrity of the diaphragm
CC       associated with often lethal pulmonary hypoplasia and pulmonary
CC       hypertension. {ECO:0000269|PubMed:16103912}. Note=The disease is
CC       caused by mutations affecting the gene represented in this entry.
CC   -!- DISEASE: 46,XY sex reversal 9 (SRXY9) [MIM:616067]: A disorder of
CC       sex development. Affected individuals have a 46,XY karyotype but
CC       present as phenotypically normal females or have ambiguous
CC       external genitalia. {ECO:0000269|PubMed:24549039}. Note=The
CC       disease is caused by mutations affecting the gene represented in
CC       this entry.
CC   -!- DISEASE: Conotruncal heart malformations (CTHM) [MIM:217095]: A
CC       group of congenital heart defects involving the outflow tracts.
CC       Examples include truncus arteriosus communis, double-outlet right
CC       ventricle and transposition of great arteries. Truncus arteriosus
CC       communis is characterized by a single outflow tract instead of a
CC       separate aorta and pulmonary artery. In transposition of the great
CC       arteries, the aorta arises from the right ventricle and the
CC       pulmonary artery from the left ventricle. In double outlet of the
CC       right ventricle, both the pulmonary artery and aorta arise from
CC       the right ventricle. {ECO:0000269|PubMed:20807224}. Note=The
CC       disease is caused by mutations affecting the gene represented in
CC       this entry.
CC   -!- SIMILARITY: Belongs to the FOG (Friend of GATA) family.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Contains 3 C2H2-type zinc fingers.
CC       {ECO:0000255|PROSITE-ProRule:PRU00042}.
CC   -!- SIMILARITY: Contains 5 C2HC-type zinc fingers. {ECO:0000305}.
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DR   EMBL; AF119334; AAD49558.1; -; mRNA.
DR   EMBL; BC020928; AAH20928.1; -; mRNA.
DR   EMBL; BC109222; AAI09223.1; -; mRNA.
DR   EMBL; AL389987; CAB97539.1; -; mRNA.
DR   EMBL; AL389989; CAB97541.1; -; mRNA.
DR   CCDS; CCDS47908.1; -. [Q8WW38-1]
DR   RefSeq; NP_036214.2; NM_012082.3. [Q8WW38-1]
DR   UniGene; Hs.431009; -.
DR   ProteinModelPortal; Q8WW38; -.
DR   SMR; Q8WW38; 251-276, 290-325, 352-395, 548-574, 687-713, 1112-1145.
DR   BioGrid; 116986; 14.
DR   IntAct; Q8WW38; 2.
DR   STRING; 9606.ENSP00000384179; -.
DR   PhosphoSite; Q8WW38; -.
DR   BioMuta; ZFPM2; -.
DR   DMDM; 126302543; -.
DR   MaxQB; Q8WW38; -.
DR   PaxDb; Q8WW38; -.
DR   PRIDE; Q8WW38; -.
DR   Ensembl; ENST00000407775; ENSP00000384179; ENSG00000169946. [Q8WW38-1]
DR   GeneID; 23414; -.
DR   KEGG; hsa:23414; -.
DR   UCSC; uc003ymd.3; human. [Q8WW38-1]
DR   CTD; 23414; -.
DR   GeneCards; ZFPM2; -.
DR   HGNC; HGNC:16700; ZFPM2.
DR   HPA; HPA004094; -.
DR   MIM; 187500; phenotype.
DR   MIM; 217095; phenotype.
DR   MIM; 603693; gene.
DR   MIM; 610187; phenotype.
DR   MIM; 616067; phenotype.
DR   neXtProt; NX_Q8WW38; -.
DR   Orphanet; 251510; 46,XY partial gonadal dysgenesis.
DR   Orphanet; 2140; Congenital diaphragmatic hernia.
DR   Orphanet; 3303; Tetralogy of Fallot.
DR   PharmGKB; PA134947303; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   eggNOG; COG5048; LUCA.
DR   GeneTree; ENSGT00530000063823; -.
DR   HOGENOM; HOG000057275; -.
DR   HOVERGEN; HBG048953; -.
DR   InParanoid; Q8WW38; -.
DR   KO; K17442; -.
DR   OMA; IYSPLMP; -.
DR   OrthoDB; EOG74TWXR; -.
DR   PhylomeDB; Q8WW38; -.
DR   TreeFam; TF331342; -.
DR   Reactome; R-HSA-983231; Factors involved in megakaryocyte development and platelet production.
DR   ChiTaRS; ZFPM2; human.
DR   GeneWiki; ZFPM2; -.
DR   GenomeRNAi; 23414; -.
DR   NextBio; 45615; -.
DR   PRO; PR:Q8WW38; -.
DR   Proteomes; UP000005640; Chromosome 8.
DR   Bgee; Q8WW38; -.
DR   CleanEx; HS_ZFPM2; -.
DR   ExpressionAtlas; Q8WW38; baseline and differential.
DR   Genevisible; Q8WW38; HS.
DR   GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0001105; F:RNA polymerase II transcription coactivator activity; NAS:BHF-UCL.
DR   GO; GO:0001085; F:RNA polymerase II transcription factor binding; IBA:GO_Central.
DR   GO; GO:0003714; F:transcription corepressor activity; IDA:BHF-UCL.
DR   GO; GO:0008134; F:transcription factor binding; IPI:BHF-UCL.
DR   GO; GO:0001078; F:transcriptional repressor activity, RNA polymerase II core promoter proximal region sequence-specific binding; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; NAS:BHF-UCL.
DR   GO; GO:0007596; P:blood coagulation; TAS:Reactome.
DR   GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR   GO; GO:0048568; P:embryonic organ development; IEA:Ensembl.
DR   GO; GO:0007506; P:gonadal mesoderm development; IEA:UniProtKB-KW.
DR   GO; GO:0007507; P:heart development; IBA:GO_Central.
DR   GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR   GO; GO:0030324; P:lung development; IEA:Ensembl.
DR   GO; GO:0060548; P:negative regulation of cell death; IEA:Ensembl.
DR   GO; GO:0045599; P:negative regulation of fat cell differentiation; IMP:UniProtKB.
DR   GO; GO:2000195; P:negative regulation of female gonad development; IEA:Ensembl.
DR   GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IBA:GO_Central.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR   GO; GO:0003148; P:outflow tract septum morphogenesis; IMP:BHF-UCL.
DR   GO; GO:2000020; P:positive regulation of male gonad development; IEA:Ensembl.
DR   GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:BHF-UCL.
DR   GO; GO:0003221; P:right ventricular cardiac muscle tissue morphogenesis; IMP:BHF-UCL.
DR   GO; GO:0001570; P:vasculogenesis; IEA:Ensembl.
DR   GO; GO:0060412; P:ventricular septum morphogenesis; IMP:BHF-UCL.
DR   Gene3D; 3.30.160.60; -; 1.
DR   InterPro; IPR007087; Znf_C2H2.
DR   InterPro; IPR015880; Znf_C2H2-like.
DR   InterPro; IPR013087; Znf_C2H2/integrase_DNA-bd.
DR   SMART; SM00355; ZnF_C2H2; 8.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 2.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 2.
PE   1: Evidence at protein level;
KW   Activator; Alternative splicing; Cardiomyopathy; Complete proteome;
KW   Differentiation; Disease mutation; DNA-binding;
KW   Gonadal differentiation; Isopeptide bond; Metal-binding; Nucleus;
KW   Polymorphism; Reference proteome; Repeat; Repressor; Transcription;
KW   Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT   CHAIN         1   1151       Zinc finger protein ZFPM2.
FT                                /FTId=PRO_0000221043.
FT   ZN_FING     250    273       C2HC-type 1.
FT   ZN_FING     296    320       C2H2-type 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     335    357       C2H2-type 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     363    385       C2H2-type 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     548    571       C2HC-type 2.
FT   ZN_FING     687    710       C2HC-type 3.
FT   ZN_FING     854    877       C2HC-type 4.
FT   ZN_FING    1119   1142       C2HC-type 5.
FT   REGION      829    835       Interaction with CTBP2. {ECO:0000305}.
FT   MOTIF       736    740       Nuclear localization signal.
FT                                {ECO:0000250}.
FT   CROSSLNK    324    324       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO1).
FT   CROSSLNK    471    471       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO1).
FT   CROSSLNK    915    915       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO1).
FT   CROSSLNK    955    955       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO1).
FT   VAR_SEQ       1    132       Missing (in isoform 2).
FT                                {ECO:0000303|Ref.3}.
FT                                /FTId=VSP_009701.
FT   VAR_SEQ     247    287       KDIFPCKSCGIWYRSERNLQAHLMYYCSGRQREAAPVSEEN
FT                                -> SKCSVLCSPALEVMGIYGRKKCLLTRNQEQTFFLQKKK
FT                                KKK (in isoform 2). {ECO:0000303|Ref.3}.
FT                                /FTId=VSP_009702.
FT   VARIANT      30     30       E -> G (in TOF and CTHM; does not affect
FT                                its ability to interact with GATA4;
FT                                dbSNP:rs121908601).
FT                                {ECO:0000269|PubMed:14517948,
FT                                ECO:0000269|PubMed:20807224}.
FT                                /FTId=VAR_017942.
FT   VARIANT     227    227       I -> V (in CTHM).
FT                                {ECO:0000269|PubMed:20807224}.
FT                                /FTId=VAR_072074.
FT   VARIANT     260    260       R -> Q (in SRXY9; results in reduced
FT                                transactivation activity on the AMH
FT                                promoter; does not affect its ability to
FT                                interact with GATA4).
FT                                {ECO:0000269|PubMed:24549039}.
FT                                /FTId=VAR_071104.
FT   VARIANT     402    402       S -> R (in SRXY9; results in reduced
FT                                transactivation activity on the AMH
FT                                promoter; abolished its ability to
FT                                interact with GATA4).
FT                                {ECO:0000269|PubMed:24549039}.
FT                                /FTId=VAR_071105.
FT   VARIANT     403    403       A -> G (in dbSNP:rs11993776).
FT                                {ECO:0000269|PubMed:24549039}.
FT                                /FTId=VAR_024178.
FT   VARIANT     544    544       M -> I (in SRXY9 and TOF; reduced its
FT                                ability to interact with GATA4).
FT                                {ECO:0000269|PubMed:20807224,
FT                                ECO:0000269|PubMed:24549039}.
FT                                /FTId=VAR_072075.
FT   VARIANT     657    657       S -> G (in TOF; slightly impairs its
FT                                ability to interact with GATA4;
FT                                dbSNP:rs28374544).
FT                                {ECO:0000269|PubMed:14517948}.
FT                                /FTId=VAR_017943.
FT   VARIANT     782    782       E -> D (in dbSNP:rs2920048).
FT                                {ECO:0000269|PubMed:24549039}.
FT                                /FTId=VAR_017944.
FT   VARIANT    1055   1055       A -> V (in dbSNP:rs16873741).
FT                                /FTId=VAR_030760.
FT   CONFLICT    198    198       F -> L (in Ref. 3; CAB97541).
FT                                {ECO:0000305}.
FT   CONFLICT    939    939       L -> P (in Ref. 1; AAD49558).
FT                                {ECO:0000305}.
SQ   SEQUENCE   1151 AA;  128159 MW;  680E31BA1D044C35 CRC64;
     MSRRKQSKPR QIKRPLEDAI EDEEEECPSE ETDIISKGDF PLEESFSTEF GPENLSCEEV
     EYFCNKGDDE GIQETAESDG DTQSEKPGQP GVETDDWDGP GELEVFQKDG ERKIQSRQQL
     PVGTTWGPFP GKMDLNNNSL KTKAQVPMVL TAGPKWLLDV TWQGVEDNKN NCIVYSKGGQ
     LWCTTTKAIS EGEELIAFVV DFDSRLQAAS QMTLTEGMYP ARLLDSIQLL PQQAAMASIL
     PTAIVNKDIF PCKSCGIWYR SERNLQAHLM YYCSGRQREA APVSEENEDS AHQISSLCPF
     PQCTKSFSNA RALEMHLNSH SGVKMEEFLP PGASLKCTVC SYTADSVINF HQHLFSHLTQ
     AAFRCNHCHF GFQTQRELLQ HQELHVPSGK LPRESDMEHS PSATEDSLQP ATDLLTRSEL
     PQSQKAMQTK DASSDTELDK CEKKTQLFLT NQRPEIQPTT NKQSFSYTKI KSEPSSPRLA
     SSPVQPNIGP SFPVGPFLSQ FSFPQDITMV PQASEILAKM SELVHRRLRH GSSSYPPVIY
     SPLMPKGATC FECNITFNNL DNYLVHKKHY CSSRWQQMAK SPEFPSVSEK MPEALSPNTG
     QTSINLLNPA AHSADPENPL LQTSCINSST VLDLIGPNGK GHDKDFSTQT KKLSTSSNND
     DKINGKPVDV KNPSVPLVDG ESDPNKTTCE ACNITFSRHE TYMVHKQYYC ATRHDPPLKR
     SASNKVPAMQ RTMRTRKRRK MYEMCLPEQE QRPPLVQQRF LDVANLNNPC TSTQEPTEGL
     GECYHPRCDI FPGIVSKHLE TSLTINKCVP VSKCDTTHSS VSCLEMDVPI DLSKKCLSQS
     ERTTTSPKRL LDYHECTVCK ISFNKVENYL AHKQNFCPVT AHQRNDLGQL DGKVFPNPES
     ERNSPDVSYE RSIIKCEKNG NLKQPSPNGN LFSSHLATLQ GLKVFSEAAQ LIATKEENRH
     LFLPQCLYPG AIKKAKGADQ LSPYYGIKPS DYISGSLVIH NTDIEQSRNA ENESPKGQAS
     SNGCAALKKD SLPLLPKNRG MVIVNGGLKQ DERPAANPQQ ENISQNPQHE DDHKSPSWIS
     ENPLAANENV SPGIPSAEEQ LSSIAKGVNG SSQAPTSGKY CRLCDIQFNN LSNFITHKKF
     YCSSHAAEHV K
//
ID   HAIR_DROME              Reviewed;         337 AA.
AC   P14003; A4V1N7; Q95NH3; Q95NU9; Q9VSN8;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   18-APR-2006, sequence version 2.
DT   11-NOV-2015, entry version 154.
DE   RecName: Full=Protein hairy;
GN   Name=h; ORFNames=CG6494;
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
OC   Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha;
OC   Ephydroidea; Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND VARIANT SER-292.
RC   STRAIN=Oregon-R;
RX   PubMed=2479541;
RA   Rushlow C.A., Hogan A., Pierchin S.M., Howe K.M., Lardelli M.,
RA   Ish-Horowicz D.;
RT   "The Drosophila hairy protein acts in both segmentation and bristle
RT   patterning and shows homology to N-myc.";
RL   EMBO J. 8:3095-3103(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT SER-21.
RC   STRAIN=R3-105, R3-107, R3-19, R3-2, R3-24, R3-48, R3-53, R3-6, R3-74,
RC   and R3-95;
RX   PubMed=12242230;
RA   Robin C., Lyman R.F., Long A.D., Langley C.H., Mackay T.F.C.;
RT   "hairy. A quantitative trait locus for Drosophila sensory bristle
RT   number.";
RL   Genetics 162:155-164(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley;
RX   PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA   Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA   Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA   George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA   Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
RA   Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
RA   Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
RA   Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
RA   Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
RA   Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
RA   Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
RA   Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
RA   Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
RA   de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
RA   Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
RA   Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
RA   Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
RA   Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
RA   Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
RA   Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
RA   Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
RA   Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
RA   Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
RA   Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
RA   Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
RA   Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
RA   Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
RA   Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
RA   Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA   Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
RA   Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
RA   Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
RA   Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
RA   Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
RA   Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
RA   Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=Berkeley;
RX   PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
RA   Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
RA   Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a
RT   systematic review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Berkeley; TISSUE=Embryo;
RX   PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA   Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M.,
RA   George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H.,
RA   Rubin G.M., Celniker S.E.;
RT   "A Drosophila full-length cDNA resource.";
RL   Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN   [6]
RP   DOMAIN WRPW MOTIF.
RX   PubMed=8001118; DOI=10.1016/0092-8674(94)90070-1;
RA   Paroush Z., Finley R.L. Jr., Kidd T., Wainwright S.M., Ingham P.W.,
RA   Brent R., Ish-Horowicz D.;
RT   "Groucho is required for Drosophila neurogenesis, segmentation, and
RT   sex determination and interacts directly with hairy-related bHLH
RT   proteins.";
RL   Cell 79:805-815(1994).
RN   [7]
RP   FUNCTION, INTERACTION WITH GRO, AND DOMAIN WRPW MOTIF.
RX   PubMed=8649374;
RA   Fisher A.L., Ohsako S., Caudy M.;
RT   "The WRPW motif of the hairy-related basic helix-loop-helix repressor
RT   proteins acts as a 4-amino-acid transcription repression and protein-
RT   protein interaction domain.";
RL   Mol. Cell. Biol. 16:2670-2677(1996).
RN   [8]
RP   DNA-BINDING, INTERACTION WITH TOPORS, AND UBIQUITINATION.
RX   PubMed=14871887; DOI=10.1074/jbc.M310097200;
RA   Secombe J., Parkhurst S.M.;
RT   "Drosophila Topors is a RING finger-containing protein that functions
RT   as a ubiquitin-protein isopeptide ligase for the hairy basic helix-
RT   loop-helix repressor protein.";
RL   J. Biol. Chem. 279:17126-17133(2004).
CC   -!- FUNCTION: Pair-rule protein that regulates embryonic segmentation
CC       and adult bristle patterning. Transcriptional repressor of genes
CC       that require a bHLH protein for their transcription (e.g. the
CC       Fushi tarazu gene). {ECO:0000269|PubMed:8649374}.
CC   -!- SUBUNIT: Transcription repression requires formation of a complex
CC       with a corepressor protein (Groucho). Interacts with gro (via WPRW
CC       motif) and Topors. {ECO:0000269|PubMed:14871887,
CC       ECO:0000269|PubMed:8649374}.
CC   -!- INTERACTION:
CC       O46036:CtBP; NbExp=4; IntAct=EBI-123011, EBI-159330;
CC       Q9VNJ0:dgrn; NbExp=5; IntAct=EBI-123011, EBI-186615;
CC       P16371:gro; NbExp=3; IntAct=EBI-123011, EBI-153866;
CC       Q9V8P9:Topors; NbExp=4; IntAct=EBI-123011, EBI-147805;
CC       P83949:Ubx; NbExp=3; IntAct=EBI-123011, EBI-202590;
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- DOMAIN: Has a particular type of basic domain (presence of a
CC       helix-interrupting proline) that binds to the N-box (CACNAG),
CC       rather than the canonical E-box (CANNTG).
CC   -!- DOMAIN: The C-terminal WRPW motif is a transcriptional repression
CC       domain necessary for the interaction with Groucho, a
CC       transcriptional corepressor recruited to specific target DNA by
CC       Hairy-related proteins.
CC   -!- PTM: Ubiquitinated by Topors. {ECO:0000269|PubMed:14871887}.
CC   -!- SIMILARITY: Contains 1 bHLH (basic helix-loop-helix) domain.
CC       {ECO:0000255|PROSITE-ProRule:PRU00981}.
CC   -!- SIMILARITY: Contains 1 Orange domain. {ECO:0000255|PROSITE-
CC       ProRule:PRU00380}.
CC   -----------------------------------------------------------------------
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DR   EMBL; X15904; CAA34018.1; -; Genomic_DNA.
DR   EMBL; X15905; CAA34019.1; -; mRNA.
DR   EMBL; AY055833; AAL17767.1; -; Genomic_DNA.
DR   EMBL; AY055834; AAL17768.1; -; Genomic_DNA.
DR   EMBL; AY055835; AAL17769.1; -; Genomic_DNA.
DR   EMBL; AY055836; AAL17770.1; -; Genomic_DNA.
DR   EMBL; AY055837; AAL17771.1; -; Genomic_DNA.
DR   EMBL; AY055838; AAL17772.1; -; Genomic_DNA.
DR   EMBL; AY055839; AAL17773.1; -; Genomic_DNA.
DR   EMBL; AY055840; AAL17774.1; -; Genomic_DNA.
DR   EMBL; AY055841; AAL17775.1; -; Genomic_DNA.
DR   EMBL; AY055842; AAL17776.1; -; Genomic_DNA.
DR   EMBL; AE014296; AAF50378.1; -; Genomic_DNA.
DR   EMBL; AE014296; AAX52752.1; -; Genomic_DNA.
DR   EMBL; AY119633; AAM50287.1; -; mRNA.
DR   PIR; S06956; S06956.
DR   RefSeq; NP_001014577.1; NM_001014577.2.
DR   RefSeq; NP_523977.2; NM_079253.4.
DR   UniGene; Dm.2554; -.
DR   ProteinModelPortal; P14003; -.
DR   SMR; P14003; 23-92.
DR   BioGrid; 64402; 11.
DR   DIP; DIP-637N; -.
DR   IntAct; P14003; 8.
DR   MINT; MINT-1542874; -.
DR   STRING; 7227.FBpp0099504; -.
DR   PaxDb; P14003; -.
DR   GeneID; 38995; -.
DR   KEGG; dme:Dmel_CG6494; -.
DR   UCSC; CG6494-RA; d. melanogaster.
DR   CTD; 38995; -.
DR   FlyBase; FBgn0001168; h.
DR   eggNOG; KOG4304; Eukaryota.
DR   eggNOG; ENOG4111F0X; LUCA.
DR   InParanoid; P14003; -.
DR   KO; K09090; -.
DR   OMA; EEQPWRP; -.
DR   OrthoDB; EOG780RN7; -.
DR   PhylomeDB; P14003; -.
DR   Reactome; R-DME-210744; Regulation of gene expression in late stage (branching morphogenesis) pancreatic bud precursor cells.
DR   Reactome; R-DME-2122947; NOTCH1 Intracellular Domain Regulates Transcription.
DR   SignaLink; P14003; -.
DR   GenomeRNAi; 38995; -.
DR   NextBio; 811370; -.
DR   PRO; PR:P14003; -.
DR   Proteomes; UP000000803; Chromosome 3L.
DR   Bgee; P14003; -.
DR   Genevisible; P14003; DM.
DR   GO; GO:0005634; C:nucleus; IC:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR   GO; GO:0070888; F:E-box binding; IDA:FlyBase.
DR   GO; GO:0000978; F:RNA polymerase II core promoter proximal region sequence-specific DNA binding; IDA:FlyBase.
DR   GO; GO:0008134; F:transcription factor binding; IPI:FlyBase.
DR   GO; GO:0001078; F:transcriptional repressor activity, RNA polymerase II core promoter proximal region sequence-specific binding; IDA:FlyBase.
DR   GO; GO:0000902; P:cell morphogenesis; IMP:FlyBase.
DR   GO; GO:0061024; P:membrane organization; TAS:FlyBase.
DR   GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR   GO; GO:0007399; P:nervous system development; TAS:FlyBase.
DR   GO; GO:0007424; P:open tracheal system development; IMP:FlyBase.
DR   GO; GO:0007366; P:periodic partitioning by pair rule gene; NAS:FlyBase.
DR   GO; GO:0035289; P:posterior head segmentation; TAS:FlyBase.
DR   GO; GO:0007460; P:R8 cell fate commitment; NAS:FlyBase.
DR   GO; GO:0031323; P:regulation of cellular metabolic process; IMP:FlyBase.
DR   GO; GO:0001666; P:response to hypoxia; IMP:FlyBase.
DR   GO; GO:0007431; P:salivary gland development; TAS:FlyBase.
DR   GO; GO:0007435; P:salivary gland morphogenesis; IMP:FlyBase.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
DR   GO; GO:0035290; P:trunk segmentation; TAS:FlyBase.
DR   GO; GO:0035239; P:tube morphogenesis; IMP:FlyBase.
DR   Gene3D; 4.10.280.10; -; 1.
DR   InterPro; IPR011598; bHLH_dom.
DR   InterPro; IPR003650; Orange_dom.
DR   Pfam; PF07527; Hairy_orange; 1.
DR   Pfam; PF00010; HLH; 1.
DR   SMART; SM00353; HLH; 1.
DR   SMART; SM00511; ORANGE; 1.
DR   SUPFAM; SSF47459; SSF47459; 1.
DR   PROSITE; PS50888; BHLH; 1.
DR   PROSITE; PS51054; ORANGE; 1.
PE   1: Evidence at protein level;
KW   Complete proteome; Developmental protein; DNA-binding; Nucleus;
KW   Pair-rule protein; Polymorphism; Reference proteome; Repressor;
KW   Transcription; Transcription regulation; Ubl conjugation.
FT   CHAIN         1    337       Protein hairy.
FT                                /FTId=PRO_0000127181.
FT   DOMAIN       31     88       bHLH. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00981}.
FT   DOMAIN      107    136       Orange. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00380}.
FT   REGION       29     48       Interaction with Topors.
FT   MOTIF       334    337       WRPW motif.
FT   COMPBIAS    149    157       Gln-rich.
FT   COMPBIAS    222    237       Gln-rich.
FT   COMPBIAS    241    250       Poly-Ala.
FT   VARIANT      21     21       A -> S (in strain: R3-6, R3-105 and R3-
FT                                107). {ECO:0000269|PubMed:12242230}.
FT   VARIANT     292    292       P -> S. {ECO:0000269|PubMed:2479541}.
SQ   SEQUENCE   337 AA;  37005 MW;  49BECAF7F2D69FC4 CRC64;
     MVTGVTAANM TNVLGTAVVP AQLKETPLKS DRRSNKPIME KRRRARINNC LNELKTLILD
     ATKKDPARHS KLEKADILEK TVKHLQELQR QQAAMQQAAD PKIVNKFKAG FADCVNEVSR
     FPGIEPAQRR RLLQHLSNCI NGVKTELHQQ QRQQQQQSIH AQMLPSPPSS PEQDSQQGAA
     APYLFGIQQT ASGYFLPNGM QVIPTKLPNG SIALVLPQSL PQQQQQQLLQ HQQQQQQLAV
     AAAAAAAAAA QQQPMLVSMP QRTASTGSAS SHSSAGYESA PGSSSSCSYA PPSPANSSYE
     PMDIKPSVIQ RVPMEQQPLS LVIKKQIKEE EQPWRPW
//
ID   HDAC4_HUMAN             Reviewed;        1084 AA.
AC   P56524; E9PGB9; F5GX36; Q86YH7; Q9UND6;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   22-SEP-2009, sequence version 3.
DT   11-NOV-2015, entry version 166.
DE   RecName: Full=Histone deacetylase 4;
DE            Short=HD4;
DE            EC=3.5.1.98;
GN   Name=HDAC4; Synonyms=KIAA0288;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Leukemia;
RX   PubMed=10220385; DOI=10.1073/pnas.96.9.4868;
RA   Grozinger C.M., Hassig C.A., Schreiber S.L.;
RT   "Three proteins define a class of human histone deacetylases related
RT   to yeast Hda1p.";
RL   Proc. Natl. Acad. Sci. U.S.A. 96:4868-4873(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
RX   PubMed=9179496; DOI=10.1093/dnares/4.1.53;
RA   Ohara O., Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N.,
RA   Nomura N.;
RT   "Construction and characterization of human brain cDNA libraries
RT   suitable for analysis of cDNA clones encoding relatively large
RT   proteins.";
RL   DNA Res. 4:53-59(1997).
RN   [3]
RP   SEQUENCE REVISION TO N-TERMINUS.
RA   Ohara O., Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N.,
RA   Nomura N.;
RL   Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15815621; DOI=10.1038/nature03466;
RA   Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
RA   Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA   Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA   Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA   Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA   Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA   Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA   Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA   Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA   Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA   McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA   Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
RA   Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA   Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA   Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA   Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA   Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA   Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA   Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA   Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA   McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA   Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA   Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
RA   Waterston R.H., Wilson R.K.;
RT   "Generation and annotation of the DNA sequences of human chromosomes 2
RT   and 4.";
RL   Nature 434:724-731(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Testis;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [7]
RP   SUBCELLULAR LOCATION, AND INTERACTION WITH MEF2A.
RX   PubMed=10487761; DOI=10.1093/emboj/18.18.5099;
RA   Miska E.A., Karlsson C., Langley E., Nielsen S.J., Pines J.,
RA   Kouzarides T.;
RT   "HDAC4 deacetylase associates with and represses the MEF2
RT   transcription factor.";
RL   EMBO J. 18:5099-5107(1999).
RN   [8]
RP   FUNCTION, INTERACTION WITH MEF2C AND MEF2D, AND MUTAGENESIS OF
RP   HIS-803.
RX   PubMed=10523670;
RA   Wang A.H., Bertos N.R., Vezmar M., Pelletier N., Crosato M.,
RA   Heng H.H., Th'ng J., Han J., Yang X.-J.;
RT   "HDAC4, a human histone deacetylase related to yeast HDA1, is a
RT   transcriptional corepressor.";
RL   Mol. Cell. Biol. 19:7816-7827(1999).
RN   [9]
RP   PHOSPHORYLATION AT SER-246; SER-467 AND SER-632, AND MUTAGENESIS OF
RP   SER-246; SER-467 AND SER-632.
RX   PubMed=10958686; DOI=10.1128/MCB.20.18.6904-6912.2000;
RA   Wang A.H., Kruhlak M.J., Wu J., Bertos N.R., Vezmar M., Posner B.I.,
RA   Bazett-Jones D.P., Yang X.-J.;
RT   "Regulation of histone deacetylase 4 by binding of 14-3-3 proteins.";
RL   Mol. Cell. Biol. 20:6904-6912(2000).
RN   [10]
RP   SUBCELLULAR LOCATION, PHOSPHORYLATION, AND MUTAGENESIS OF SER-467 AND
RP   SER-632.
RX   PubMed=11470791; DOI=10.1074/jbc.M105086200;
RA   Zhao X., Ito A., Kane C.D., Liao T.-S., Bolger T.A., Lemrow S.M.,
RA   Means A.R., Yao T.-P.;
RT   "The modular nature of histone deacetylase HDAC4 confers
RT   phosphorylation-dependent intracellular trafficking.";
RL   J. Biol. Chem. 276:35042-35048(2001).
RN   [11]
RP   NUCLEAR EXPORT SIGNAL, AND MUTAGENESIS OF VAL-1056 AND LEU-1062.
RX   PubMed=11509672; DOI=10.1128/MCB.21.18.6312-6321.2001;
RA   McKinsey T.A., Zhang C.-L., Olson E.N.;
RT   "Identification of a signal-responsive nuclear export sequence in
RT   class II histone deacetylases.";
RL   Mol. Cell. Biol. 21:6312-6321(2001).
RN   [12]
RP   INTERACTION WITH NR2C1.
RX   PubMed=11463856; DOI=10.1210/me.15.8.1318;
RA   Franco P.J., Farooqui M., Seto E., Wei L.-N.;
RT   "The orphan nuclear receptor TR2 interacts directly with both class I
RT   and class II histone deacetylases.";
RL   Mol. Endocrinol. 15:1318-1328(2001).
RN   [13]
RP   HOMODIMERIZATION, SUMOYLATION AT LYS-559, AND MUTAGENESIS OF LYS-559.
RX   PubMed=12032081; DOI=10.1093/emboj/21.11.2682;
RA   Kirsh O., Seeler J.-S., Pichler A., Gast A., Mueller S., Miska E.,
RA   Mathieu M., Harel-Bellan A., Kouzarides T., Melchior F., Dejean A.;
RT   "The SUMO E3 ligase RanBP2 promotes modification of the HDAC4
RT   deacetylase.";
RL   EMBO J. 21:2682-2691(2002).
RN   [14]
RP   INTERACTION WITH KDM5B.
RX   PubMed=17373667; DOI=10.1002/ijc.22673;
RA   Barrett A., Santangelo S., Tan K., Catchpole S., Roberts K.,
RA   Spencer-Dene B., Hall D., Scibetta A., Burchell J., Verdin E.,
RA   Freemont P., Taylor-Papadimitriou J.;
RT   "Breast cancer associated transcriptional repressor PLU-1/JARID1B
RT   interacts directly with histone deacetylases.";
RL   Int. J. Cancer 121:265-275(2007).
RN   [15]
RP   PHOSPHORYLATION BY CAMK2D.
RX   PubMed=17179159; DOI=10.1074/jbc.M604281200;
RA   Little G.H., Bai Y., Williams T., Poizat C.;
RT   "Nuclear calcium/calmodulin-dependent protein kinase IIdelta
RT   preferentially transmits signals to histone deacetylase 4 in cardiac
RT   cells.";
RL   J. Biol. Chem. 282:7219-7231(2007).
RN   [16]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-632 AND SER-633, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [17]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-350, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA   Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA   Rodionov V., Han D.K.;
RT   "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT   reveals system-wide modulation of protein-protein interactions.";
RL   Sci. Signal. 2:RA46-RA46(2009).
RN   [18]
RP   INVOLVEMENT IN BDMR.
RX   PubMed=20691407; DOI=10.1016/j.ajhg.2010.07.011;
RA   Williams S.R., Aldred M.A., Der Kaloustian V.M., Halal F., Gowans G.,
RA   McLeod D.R., Zondag S., Toriello H.V., Magenis R.E., Elsea S.H.;
RT   "Haploinsufficiency of HDAC4 causes brachydactyly mental retardation
RT   syndrome, with brachydactyly type E, developmental delays, and
RT   behavioral problems.";
RL   Am. J. Hum. Genet. 87:219-228(2010).
RN   [19]
RP   INTERACTION WITH MORC2.
RX   PubMed=20110259; DOI=10.1093/nar/gkq006;
RA   Shao Y., Li Y., Zhang J., Liu D., Liu F., Zhao Y., Shen T., Li F.;
RT   "Involvement of histone deacetylation in MORC2-mediated down-
RT   regulation of carbonic anhydrase IX.";
RL   Nucleic Acids Res. 38:2813-2824(2010).
RN   [20]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA   Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full
RT   phosphorylation site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [21]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA   Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA   Blagoev B.;
RT   "System-wide temporal characterization of the proteome and
RT   phosphoproteome of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [22]
RP   FUNCTION, AND INTERACTION WITH EP300.
RX   PubMed=24413532; DOI=10.1158/0008-5472.CAN-13-2020;
RA   Kang H.J., Lee M.H., Kang H.L., Kim S.H., Ahn J.R., Na H., Na T.Y.,
RA   Kim Y.N., Seong J.K., Lee M.O.;
RT   "Differential regulation of estrogen receptor alpha expression in
RT   breast cancer cells by metastasis-associated protein 1.";
RL   Cancer Res. 74:1484-1494(2014).
RN   [23]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-632, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
RA   Wang L., Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human
RT   liver phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [24]
RP   X-RAY CRYSTALLOGRAPHY (1.57 ANGSTROMS) OF 343-359 IN COMPLEX WITH
RP   ANKRA2, AND PHOSPHORYLATION AT SER-350.
RX   PubMed=22649097; DOI=10.1126/scisignal.2002979;
RA   Xu C., Jin J., Bian C., Lam R., Tian R., Weist R., You L., Nie J.,
RA   Bochkarev A., Tempel W., Tan C.S., Wasney G.A., Vedadi M., Gish G.D.,
RA   Arrowsmith C.H., Pawson T., Yang X.J., Min J.;
RT   "Sequence-specific recognition of a PxLPxI/L motif by an ankyrin
RT   repeat tumbler lock.";
RL   Sci. Signal. 5:RA39-RA39(2012).
RN   [25]
RP   VARIANT [LARGE SCALE ANALYSIS] ARG-727.
RX   PubMed=16959974; DOI=10.1126/science.1133427;
RA   Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA   Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
RA   Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
RA   Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
RA   Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
RA   Vogelstein B., Kinzler K.W., Velculescu V.E.;
RT   "The consensus coding sequences of human breast and colorectal
RT   cancers.";
RL   Science 314:268-274(2006).
RN   [26]
RP   VARIANT ILE-754.
RX   PubMed=24169519; DOI=10.1038/ejhg.2013.243;
RA   Piton A., Poquet H., Redin C., Masurel A., Lauer J., Muller J.,
RA   Thevenon J., Herenger Y., Chancenotte S., Bonnet M., Pinoit J.M.,
RA   Huet F., Thauvin-Robinet C., Jaeger A.S., Le Gras S., Jost B.,
RA   Gerard B., Peoc'h K., Launay J.M., Faivre L., Mandel J.L.;
RT   "20 ans apres: a second mutation in MAOA identified by targeted high-
RT   throughput sequencing in a family with altered behavior and
RT   cognition.";
RL   Eur. J. Hum. Genet. 22:776-783(2014).
CC   -!- FUNCTION: Responsible for the deacetylation of lysine residues on
CC       the N-terminal part of the core histones (H2A, H2B, H3 and H4).
CC       Histone deacetylation gives a tag for epigenetic repression and
CC       plays an important role in transcriptional regulation, cell cycle
CC       progression and developmental events. Histone deacetylases act via
CC       the formation of large multiprotein complexes. Involved in muscle
CC       maturation via its interaction with the myocyte enhancer factors
CC       such as MEF2A, MEF2C and MEF2D. Involved in the MTA1-mediated
CC       epigenetic regulation of ESR1 expression in breast cancer.
CC       {ECO:0000269|PubMed:10523670, ECO:0000269|PubMed:24413532}.
CC   -!- CATALYTIC ACTIVITY: Hydrolysis of an N(6)-acetyl-lysine residue of
CC       a histone to yield a deacetylated histone.
CC   -!- SUBUNIT: Interacts with HDAC7 (By similarity). Homodimer.
CC       Homodimerization via its N-terminal domain. Interacts with MEF2C,
CC       AHRR, and NR2C1. Interacts with a 14-3-3 chaperone protein in a
CC       phosphorylation dependent manner. Interacts with BTBD14B (By
CC       similarity). Interacts with KDM5B. Interacts with MYOCD (By
CC       similarity). Interacts with MORC2. Interacts with ANKRA2.
CC       Interacts with EP300 in the presence of TFAP2C. {ECO:0000250,
CC       ECO:0000269|PubMed:10487761, ECO:0000269|PubMed:10523670,
CC       ECO:0000269|PubMed:11463856, ECO:0000269|PubMed:17373667,
CC       ECO:0000269|PubMed:20110259, ECO:0000269|PubMed:22649097,
CC       ECO:0000269|PubMed:24413532}.
CC   -!- INTERACTION:
CC       Q9H9E1:ANKRA2; NbExp=3; IntAct=EBI-308629, EBI-10215533;
CC       P10275:AR; NbExp=4; IntAct=EBI-308629, EBI-608057;
CC       P15336:ATF2; NbExp=2; IntAct=EBI-308629, EBI-1170906;
CC       P41182:BCL6; NbExp=3; IntAct=EBI-308629, EBI-765407;
CC       Q9HCU9:BRMS1; NbExp=2; IntAct=EBI-308629, EBI-714781;
CC       Q96JN2-2:CCDC136; NbExp=3; IntAct=EBI-308629, EBI-10171416;
CC       Q01850:CDR2; NbExp=3; IntAct=EBI-308629, EBI-1181367;
CC       O95967:EFEMP2; NbExp=3; IntAct=EBI-308629, EBI-743414;
CC       Q08379:GOLGA2; NbExp=3; IntAct=EBI-308629, EBI-618309;
CC       P08393:ICP0 (xeno); NbExp=3; IntAct=EBI-308629, EBI-6148881;
CC       Q15323:KRT31; NbExp=3; IntAct=EBI-308629, EBI-948001;
CC       O76015:KRT38; NbExp=3; IntAct=EBI-308629, EBI-1047263;
CC       Q6A162:KRT40; NbExp=3; IntAct=EBI-308629, EBI-10171697;
CC       O95751:LDOC1; NbExp=3; IntAct=EBI-308629, EBI-740738;
CC       A9UHW6:MIF4GD; NbExp=4; IntAct=EBI-308629, EBI-373498;
CC       Q5JR59:MTUS2; NbExp=3; IntAct=EBI-308629, EBI-742948;
CC       Q8ND90:PNMA1; NbExp=3; IntAct=EBI-308629, EBI-302345;
CC       Q6NUQ1:RINT1; NbExp=3; IntAct=EBI-308629, EBI-726876;
CC       Q13761:RUNX3; NbExp=9; IntAct=EBI-308629, EBI-925990;
CC       P31947:SFN; NbExp=4; IntAct=EBI-308629, EBI-476295;
CC       P63279:UBE2I; NbExp=3; IntAct=EBI-308629, EBI-80168;
CC       P31946:YWHAB; NbExp=3; IntAct=EBI-308629, EBI-359815;
CC       P62258:YWHAE; NbExp=4; IntAct=EBI-308629, EBI-356498;
CC       P61981:YWHAG; NbExp=6; IntAct=EBI-308629, EBI-359832;
CC       Q04917:YWHAH; NbExp=3; IntAct=EBI-308629, EBI-306940;
CC       P63104:YWHAZ; NbExp=5; IntAct=EBI-308629, EBI-347088;
CC   -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Shuttles between
CC       the nucleus and the cytoplasm. Upon muscle cells differentiation,
CC       it accumulates in the nuclei of myotubes, suggesting a positive
CC       role of nuclear HDAC4 in muscle differentiation. The export to
CC       cytoplasm depends on the interaction with a 14-3-3 chaperone
CC       protein and is due to its phosphorylation at Ser-246, Ser-467 and
CC       Ser-632 by CaMK4 and SIK1. The nuclear localization probably
CC       depends on sumoylation.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P56524-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P56524-2; Sequence=VSP_057290, VSP_057291;
CC         Note=No experimental confirmation available.;
CC   -!- TISSUE SPECIFICITY: Ubiquitous.
CC   -!- DOMAIN: The nuclear export sequence mediates the shuttling between
CC       the nucleus and the cytoplasm.
CC   -!- PTM: Phosphorylated by CaMK4 at Ser-246, Ser-467 and Ser-632.
CC       Phosphorylation at other residues by CaMK2D is required for the
CC       interaction with 14-3-3. Phosphorylation at Ser-350 impairs the
CC       binding of ANKRA2 but generates a high-affinity docking site for
CC       14-3-3. {ECO:0000269|PubMed:10958686,
CC       ECO:0000269|PubMed:22649097}.
CC   -!- PTM: Sumoylation on Lys-559 is promoted by the E3 SUMO-protein
CC       ligase RANBP2, and prevented by phosphorylation by CaMK4.
CC       {ECO:0000269|PubMed:12032081}.
CC   -!- DISEASE: Brachydactyly-mental retardation syndrome (BDMR)
CC       [MIM:600430]: A syndrome resembling the physical anomalies found
CC       in Albright hereditary osteodystrophy. Common features are mild
CC       facial dysmorphism, congenital heart defects, distinct
CC       brachydactyly type E, mental retardation, developmental delay,
CC       seizures, autism spectrum disorder, and stocky build. Soft tissue
CC       ossification is absent, and there are no abnormalities in
CC       parathyroid hormone or calcium metabolism.
CC       {ECO:0000269|PubMed:20691407}. Note=The disease is caused by
CC       mutations affecting the gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the histone deacetylase family. HD type 2
CC       subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA22957.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AF132607; AAD29046.1; -; mRNA.
DR   EMBL; AB006626; BAA22957.2; ALT_INIT; mRNA.
DR   EMBL; AC017028; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC062017; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; KF510800; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; KF510801; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471063; EAW71165.1; -; Genomic_DNA.
DR   EMBL; BC039904; AAH39904.1; -; mRNA.
DR   CCDS; CCDS2529.1; -. [P56524-1]
DR   RefSeq; NP_006028.2; NM_006037.3. [P56524-1]
DR   UniGene; Hs.20516; -.
DR   PDB; 2H8N; X-ray; 2.60 A; A/B/C/D=62-153.
DR   PDB; 2O94; X-ray; 3.00 A; A/B/C/D=62-153.
DR   PDB; 2VQJ; X-ray; 2.10 A; A=648-1057.
DR   PDB; 2VQM; X-ray; 1.80 A; A=648-1057.
DR   PDB; 2VQO; X-ray; 2.15 A; A/B=648-1057.
DR   PDB; 2VQQ; X-ray; 1.90 A; A/B=648-1057.
DR   PDB; 2VQV; X-ray; 3.30 A; A/B=648-1057.
DR   PDB; 2VQW; X-ray; 3.00 A; G=648-1057.
DR   PDB; 3UXG; X-ray; 1.85 A; B=343-359.
DR   PDB; 3UZD; X-ray; 1.86 A; B=343-359.
DR   PDB; 3V31; X-ray; 1.57 A; B=343-359.
DR   PDB; 4CBT; X-ray; 3.03 A; A/B/C=648-1033.
DR   PDB; 4CBY; X-ray; 2.72 A; A/B/C/D=648-1033.
DR   PDBsum; 2H8N; -.
DR   PDBsum; 2O94; -.
DR   PDBsum; 2VQJ; -.
DR   PDBsum; 2VQM; -.
DR   PDBsum; 2VQO; -.
DR   PDBsum; 2VQQ; -.
DR   PDBsum; 2VQV; -.
DR   PDBsum; 2VQW; -.
DR   PDBsum; 3UXG; -.
DR   PDBsum; 3UZD; -.
DR   PDBsum; 3V31; -.
DR   PDBsum; 4CBT; -.
DR   PDBsum; 4CBY; -.
DR   ProteinModelPortal; P56524; -.
DR   SMR; P56524; 62-129, 650-1051.
DR   BioGrid; 115106; 138.
DR   DIP; DIP-34565N; -.
DR   IntAct; P56524; 43.
DR   MINT; MINT-104901; -.
DR   STRING; 9606.ENSP00000264606; -.
DR   BindingDB; P56524; -.
DR   ChEMBL; CHEMBL3524; -.
DR   GuidetoPHARMACOLOGY; 2659; -.
DR   PhosphoSite; P56524; -.
DR   BioMuta; HDAC4; -.
DR   DMDM; 259016348; -.
DR   MaxQB; P56524; -.
DR   PaxDb; P56524; -.
DR   PRIDE; P56524; -.
DR   Ensembl; ENST00000345617; ENSP00000264606; ENSG00000068024. [P56524-1]
DR   Ensembl; ENST00000543185; ENSP00000440481; ENSG00000068024. [P56524-2]
DR   GeneID; 9759; -.
DR   KEGG; hsa:9759; -.
DR   UCSC; uc002vyk.4; human. [P56524-1]
DR   CTD; 9759; -.
DR   GeneCards; HDAC4; -.
DR   GeneReviews; HDAC4; -.
DR   HGNC; HGNC:14063; HDAC4.
DR   HPA; CAB004431; -.
DR   HPA; HPA048723; -.
DR   MIM; 600430; phenotype.
DR   MIM; 605314; gene.
DR   neXtProt; NX_P56524; -.
DR   Orphanet; 1001; 2q37 microdeletion syndrome.
DR   PharmGKB; PA29229; -.
DR   eggNOG; KOG1343; Eukaryota.
DR   eggNOG; COG0123; LUCA.
DR   GeneTree; ENSGT00530000062809; -.
DR   HOGENOM; HOG000232065; -.
DR   HOVERGEN; HBG057100; -.
DR   InParanoid; P56524; -.
DR   KO; K11406; -.
DR   OMA; SRQHESH; -.
DR   OrthoDB; EOG7RFTH5; -.
DR   PhylomeDB; P56524; -.
DR   TreeFam; TF106174; -.
DR   BRENDA; 3.5.1.98; 2681.
DR   Reactome; R-HSA-2122947; NOTCH1 Intracellular Domain Regulates Transcription.
DR   Reactome; R-HSA-2644606; Constitutive Signaling by NOTCH1 PEST Domain Mutants.
DR   Reactome; R-HSA-2894862; Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
DR   ChiTaRS; HDAC4; human.
DR   EvolutionaryTrace; P56524; -.
DR   GeneWiki; HDAC4; -.
DR   GenomeRNAi; 9759; -.
DR   NextBio; 35507317; -.
DR   PRO; PR:P56524; -.
DR   Proteomes; UP000005640; Chromosome 2.
DR   Bgee; P56524; -.
DR   CleanEx; HS_HDAC4; -.
DR   ExpressionAtlas; P56524; baseline and differential.
DR   Genevisible; P56524; HS.
DR   GO; GO:0031672; C:A band; IEA:Ensembl.
DR   GO; GO:0042641; C:actomyosin; IEA:Ensembl.
DR   GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0000118; C:histone deacetylase complex; IDA:BHF-UCL.
DR   GO; GO:0031594; C:neuromuscular junction; IEA:Ensembl.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0017053; C:transcriptional repressor complex; IDA:BHF-UCL.
DR   GO; GO:0030018; C:Z disc; IEA:Ensembl.
DR   GO; GO:0033613; F:activating transcription factor binding; IPI:BHF-UCL.
DR   GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
DR   GO; GO:0001047; F:core promoter binding; IDA:UniProtKB.
DR   GO; GO:0004407; F:histone deacetylase activity; IDA:BHF-UCL.
DR   GO; GO:0042826; F:histone deacetylase binding; IPI:BHF-UCL.
DR   GO; GO:0032041; F:NAD-dependent histone deacetylase activity (H3-K14 specific); IEA:UniProtKB-EC.
DR   GO; GO:0030955; F:potassium ion binding; IDA:BHF-UCL.
DR   GO; GO:0033558; F:protein deacetylase activity; IDA:BHF-UCL.
DR   GO; GO:0070491; F:repressing transcription factor binding; IPI:BHF-UCL.
DR   GO; GO:0001025; F:RNA polymerase III transcription factor binding; IPI:UniProtKB.
DR   GO; GO:0003714; F:transcription corepressor activity; IEA:Ensembl.
DR   GO; GO:0008134; F:transcription factor binding; IPI:BHF-UCL.
DR   GO; GO:0008270; F:zinc ion binding; IDA:BHF-UCL.
DR   GO; GO:0042113; P:B cell activation; TAS:UniProtKB.
DR   GO; GO:0030183; P:B cell differentiation; TAS:UniProtKB.
DR   GO; GO:0014898; P:cardiac muscle hypertrophy in response to stress; TAS:BHF-UCL.
DR   GO; GO:0071260; P:cellular response to mechanical stimulus; IEA:Ensembl.
DR   GO; GO:0071374; P:cellular response to parathyroid hormone stimulus; IEA:Ensembl.
DR   GO; GO:0071356; P:cellular response to tumor necrosis factor; IEA:Ensembl.
DR   GO; GO:0006338; P:chromatin remodeling; IDA:BHF-UCL.
DR   GO; GO:0016575; P:histone deacetylation; IDA:BHF-UCL.
DR   GO; GO:0070932; P:histone H3 deacetylation; IDA:BHF-UCL.
DR   GO; GO:0070933; P:histone H4 deacetylation; IDA:BHF-UCL.
DR   GO; GO:0006954; P:inflammatory response; TAS:UniProtKB.
DR   GO; GO:0008285; P:negative regulation of cell proliferation; IEA:Ensembl.
DR   GO; GO:0045820; P:negative regulation of glycolytic process; ISS:BHF-UCL.
DR   GO; GO:0010832; P:negative regulation of myotube differentiation; IMP:BHF-UCL.
DR   GO; GO:0045668; P:negative regulation of osteoblast differentiation; IEA:Ensembl.
DR   GO; GO:0043433; P:negative regulation of sequence-specific DNA binding transcription factor activity; IMP:BHF-UCL.
DR   GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:BHF-UCL.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:BHF-UCL.
DR   GO; GO:0007399; P:nervous system development; TAS:UniProtKB.
DR   GO; GO:0002076; P:osteoblast development; IEA:Ensembl.
DR   GO; GO:0034983; P:peptidyl-lysine deacetylation; IDA:BHF-UCL.
DR   GO; GO:0008284; P:positive regulation of cell proliferation; IMP:BHF-UCL.
DR   GO; GO:0010592; P:positive regulation of lamellipodium assembly; IEA:Ensembl.
DR   GO; GO:0043525; P:positive regulation of neuron apoptotic process; IEA:Ensembl.
DR   GO; GO:0033235; P:positive regulation of protein sumoylation; IDA:UniProtKB.
DR   GO; GO:1903428; P:positive regulation of reactive oxygen species biosynthetic process; IEA:Ensembl.
DR   GO; GO:0051091; P:positive regulation of sequence-specific DNA binding transcription factor activity; IMP:BHF-UCL.
DR   GO; GO:0014911; P:positive regulation of smooth muscle cell migration; IEA:Ensembl.
DR   GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; IEA:Ensembl.
DR   GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IMP:BHF-UCL.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:BHF-UCL.
DR   GO; GO:0010882; P:regulation of cardiac muscle contraction by calcium ion signaling; IEA:Ensembl.
DR   GO; GO:0040029; P:regulation of gene expression, epigenetic; IMP:UniProtKB.
DR   GO; GO:0043393; P:regulation of protein binding; IMP:BHF-UCL.
DR   GO; GO:0048742; P:regulation of skeletal muscle fiber development; IEA:Ensembl.
DR   GO; GO:0014894; P:response to denervation involved in regulation of muscle adaptation; ISS:BHF-UCL.
DR   GO; GO:0042493; P:response to drug; IEA:Ensembl.
DR   GO; GO:0070555; P:response to interleukin-1; IMP:BHF-UCL.
DR   GO; GO:0001501; P:skeletal system development; IEA:Ensembl.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.800.20; -; 1.
DR   InterPro; IPR000286; His_deacetylse.
DR   InterPro; IPR023801; His_deacetylse_dom.
DR   InterPro; IPR024643; Hist_deacetylase_Gln_rich_N.
DR   InterPro; IPR017320; Histone_deAcase_II_euk.
DR   PANTHER; PTHR10625; PTHR10625; 1.
DR   Pfam; PF12203; HDAC4_Gln; 1.
DR   Pfam; PF00850; Hist_deacetyl; 1.
DR   PIRSF; PIRSF037911; HDAC_II_euk; 1.
DR   PRINTS; PR01270; HDASUPER.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Autism spectrum disorder;
KW   Chromatin regulator; Coiled coil; Complete proteome; Cytoplasm;
KW   Hydrolase; Isopeptide bond; Mental retardation; Metal-binding;
KW   Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repressor;
KW   Transcription; Transcription regulation; Ubl conjugation; Zinc.
FT   CHAIN         1   1084       Histone deacetylase 4.
FT                                /FTId=PRO_0000114699.
FT   REGION      118    313       Interaction with MEF2A.
FT   REGION      655   1084       Histone deacetylase.
FT   COILED       67    177       {ECO:0000255}.
FT   MOTIF      1051   1084       Nuclear export signal. {ECO:0000250}.
FT   ACT_SITE    803    803       {ECO:0000250}.
FT   METAL       667    667       Zinc. {ECO:0000250}.
FT   METAL       669    669       Zinc. {ECO:0000250}.
FT   METAL       675    675       Zinc. {ECO:0000250}.
FT   METAL       751    751       Zinc. {ECO:0000250}.
FT   MOD_RES     210    210       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q6NZM9}.
FT   MOD_RES     246    246       Phosphoserine; by CaMK4 and SIK1.
FT                                {ECO:0000269|PubMed:10958686}.
FT   MOD_RES     350    350       Phosphoserine.
FT                                {ECO:0000244|PubMed:19690332,
FT                                ECO:0000269|PubMed:22649097}.
FT   MOD_RES     467    467       Phosphoserine; by CaMK4 and SIK1.
FT                                {ECO:0000269|PubMed:10958686}.
FT   MOD_RES     565    565       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q6NZM9}.
FT   MOD_RES     632    632       Phosphoserine; by CaMK4.
FT                                {ECO:0000244|PubMed:18669648,
FT                                ECO:0000244|PubMed:24275569,
FT                                ECO:0000269|PubMed:10958686}.
FT   MOD_RES     633    633       Phosphoserine.
FT                                {ECO:0000244|PubMed:18669648}.
FT   CROSSLNK    559    559       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO).
FT   VAR_SEQ       1    117       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_057290.
FT   VAR_SEQ     431    431       T -> TDWYLS (in isoform 2).
FT                                {ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_057291.
FT   VARIANT     727    727       P -> R (in a breast cancer sample;
FT                                somatic mutation).
FT                                {ECO:0000269|PubMed:16959974}.
FT                                /FTId=VAR_036042.
FT   VARIANT     754    754       V -> I. {ECO:0000269|PubMed:24169519}.
FT                                /FTId=VAR_071965.
FT   MUTAGEN     246    246       S->A: Reduces phosphorylation and its
FT                                subsequent nuclear export.
FT                                {ECO:0000269|PubMed:10958686}.
FT   MUTAGEN     467    467       S->A: Reduces phosphorylation and its
FT                                subsequent nuclear export.
FT                                {ECO:0000269|PubMed:10958686,
FT                                ECO:0000269|PubMed:11470791}.
FT   MUTAGEN     559    559       K->R: Abolishes sumoylation and reduces
FT                                the histone deacetylase activity.
FT                                {ECO:0000269|PubMed:12032081}.
FT   MUTAGEN     632    632       S->A: Reduces phosphorylation and its
FT                                subsequent nuclear export.
FT                                {ECO:0000269|PubMed:10958686,
FT                                ECO:0000269|PubMed:11470791}.
FT   MUTAGEN     803    803       H->L: Abolishes histone deacetylase
FT                                activity. {ECO:0000269|PubMed:10523670}.
FT   MUTAGEN    1056   1056       V->A: Reduces CaMK-dependent nuclear
FT                                export. {ECO:0000269|PubMed:11509672}.
FT   MUTAGEN    1062   1062       L->A: Reduces CaMK-dependent nuclear
FT                                export. {ECO:0000269|PubMed:11509672}.
FT   CONFLICT    373    373       A -> T (in Ref. 1; AAD29046 and 2;
FT                                BAA22957). {ECO:0000305}.
FT   HELIX        64    112       {ECO:0000244|PDB:2H8N}.
FT   HELIX       115    121       {ECO:0000244|PDB:2H8N}.
FT   TURN        122    125       {ECO:0000244|PDB:2H8N}.
FT   HELIX       126    128       {ECO:0000244|PDB:2H8N}.
FT   TURN        354    357       {ECO:0000244|PDB:3UXG}.
FT   STRAND      652    657       {ECO:0000244|PDB:2VQM}.
FT   HELIX       660    662       {ECO:0000244|PDB:2VQM}.
FT   STRAND      673    675       {ECO:0000244|PDB:2VQJ}.
FT   HELIX       681    691       {ECO:0000244|PDB:2VQM}.
FT   HELIX       694    697       {ECO:0000244|PDB:2VQM}.
FT   STRAND      698    701       {ECO:0000244|PDB:2VQM}.
FT   HELIX       708    711       {ECO:0000244|PDB:2VQM}.
FT   TURN        712    714       {ECO:0000244|PDB:2VQM}.
FT   HELIX       717    724       {ECO:0000244|PDB:2VQM}.
FT   HELIX       727    730       {ECO:0000244|PDB:2VQM}.
FT   HELIX       737    745       {ECO:0000244|PDB:2VQM}.
FT   STRAND      746    748       {ECO:0000244|PDB:2VQM}.
FT   STRAND      754    756       {ECO:0000244|PDB:2VQM}.
FT   HELIX       762    786       {ECO:0000244|PDB:2VQM}.
FT   STRAND      789    795       {ECO:0000244|PDB:2VQM}.
FT   STRAND      813    815       {ECO:0000244|PDB:2VQM}.
FT   HELIX       817    828       {ECO:0000244|PDB:2VQM}.
FT   STRAND      834    838       {ECO:0000244|PDB:2VQM}.
FT   STRAND      840    842       {ECO:0000244|PDB:2VQM}.
FT   HELIX       845    851       {ECO:0000244|PDB:2VQM}.
FT   STRAND      857    864       {ECO:0000244|PDB:2VQM}.
FT   HELIX       866    868       {ECO:0000244|PDB:2VQM}.
FT   STRAND      870    872       {ECO:0000244|PDB:4CBT}.
FT   HELIX       883    885       {ECO:0000244|PDB:2VQM}.
FT   STRAND      889    894       {ECO:0000244|PDB:2VQM}.
FT   STRAND      898    900       {ECO:0000244|PDB:2VQM}.
FT   HELIX       904    913       {ECO:0000244|PDB:2VQM}.
FT   HELIX       915    922       {ECO:0000244|PDB:2VQM}.
FT   STRAND      925    931       {ECO:0000244|PDB:2VQM}.
FT   STRAND      936    938       {ECO:0000244|PDB:2VQM}.
FT   TURN        940    943       {ECO:0000244|PDB:2VQM}.
FT   HELIX       950    961       {ECO:0000244|PDB:2VQM}.
FT   HELIX       964    966       {ECO:0000244|PDB:2VQM}.
FT   STRAND      968    972       {ECO:0000244|PDB:2VQM}.
FT   HELIX       978    992       {ECO:0000244|PDB:2VQM}.
FT   HELIX      1002   1006       {ECO:0000244|PDB:2VQM}.
FT   HELIX      1011   1025       {ECO:0000244|PDB:2VQM}.
FT   HELIX      1029   1031       {ECO:0000244|PDB:2VQM}.
FT   HELIX      1042   1047       {ECO:0000244|PDB:2VQM}.
SQ   SEQUENCE   1084 AA;  119040 MW;  BB7FD37652D12398 CRC64;
     MSSQSHPDGL SGRDQPVELL NPARVNHMPS TVDVATALPL QVAPSAVPMD LRLDHQFSLP
     VAEPALREQQ LQQELLALKQ KQQIQRQILI AEFQRQHEQL SRQHEAQLHE HIKQQQEMLA
     MKHQQELLEH QRKLERHRQE QELEKQHREQ KLQQLKNKEK GKESAVASTE VKMKLQEFVL
     NKKKALAHRN LNHCISSDPR YWYGKTQHSS LDQSSPPQSG VSTSYNHPVL GMYDAKDDFP
     LRKTASEPNL KLRSRLKQKV AERRSSPLLR RKDGPVVTAL KKRPLDVTDS ACSSAPGSGP
     SSPNNSSGSV SAENGIAPAV PSIPAETSLA HRLVAREGSA APLPLYTSPS LPNITLGLPA
     TGPSAGTAGQ QDAERLTLPA LQQRLSLFPG THLTPYLSTS PLERDGGAAH SPLLQHMVLL
     EQPPAQAPLV TGLGALPLHA QSLVGADRVS PSIHKLRQHR PLGRTQSAPL PQNAQALQHL
     VIQQQHQQFL EKHKQQFQQQ QLQMNKIIPK PSEPARQPES HPEETEEELR EHQALLDEPY
     LDRLPGQKEA HAQAGVQVKQ EPIESDEEEA EPPREVEPGQ RQPSEQELLF RQQALLLEQQ
     RIHQLRNYQA SMEAAGIPVS FGGHRPLSRA QSSPASATFP VSVQEPPTKP RFTTGLVYDT
     LMLKHQCTCG SSSSHPEHAG RIQSIWSRLQ ETGLRGKCEC IRGRKATLEE LQTVHSEAHT
     LLYGTNPLNR QKLDSKKLLG SLASVFVRLP CGGVGVDSDT IWNEVHSAGA ARLAVGCVVE
     LVFKVATGEL KNGFAVVRPP GHHAEESTPM GFCYFNSVAV AAKLLQQRLS VSKILIVDWD
     VHHGNGTQQA FYSDPSVLYM SLHRYDDGNF FPGSGAPDEV GTGPGVGFNV NMAFTGGLDP
     PMGDAEYLAA FRTVVMPIAS EFAPDVVLVS SGFDAVEGHP TPLGGYNLSA RCFGYLTKQL
     MGLAGGRIVL ALEGGHDLTA ICDASEACVS ALLGNELDPL PEKVLQQRPN ANAVRSMEKV
     MEIHSKYWRC LQRTTSTAGR SLIEAQTCEN EEAETVTAMA SLSVGVKPAE KRPDEEPMEE
     EPPL
//
ID   HDAC5_HUMAN             Reviewed;        1122 AA.
AC   Q9UQL6; C9JFV9; O60340; O60528; Q96DY4;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 2.
DT   11-NOV-2015, entry version 167.
DE   RecName: Full=Histone deacetylase 5;
DE            Short=HD5;
DE            EC=3.5.1.98;
DE   AltName: Full=Antigen NY-CO-9;
GN   Name=HDAC5; Synonyms=KIAA0600;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   PubMed=10220385; DOI=10.1073/pnas.96.9.4868;
RA   Grozinger C.M., Hassig C.A., Schreiber S.L.;
RT   "Three proteins define a class of human histone deacetylases related
RT   to yeast Hda1p.";
RL   Proc. Natl. Acad. Sci. U.S.A. 96:4868-4873(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Brain;
RX   PubMed=9628581; DOI=10.1093/dnares/5.1.31;
RA   Nagase T., Ishikawa K., Miyajima N., Tanaka A., Kotani H., Nomura N.,
RA   Ohara O.;
RT   "Prediction of the coding sequences of unidentified human genes. IX.
RT   The complete sequences of 100 new cDNA clones from brain which can
RT   code for large proteins in vitro.";
RL   DNA Res. 5:31-39(1998).
RN   [3]
RP   SEQUENCE REVISION.
RX   PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA   Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT   "Construction of expression-ready cDNA clones for KIAA genes: manual
RT   curation of 330 KIAA cDNA clones.";
RL   DNA Res. 9:99-106(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16625196; DOI=10.1038/nature04689;
RA   Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA   Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA   Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA   Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA   DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R.,
RA   Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
RA   Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
RA   Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
RA   Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
RA   Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
RA   Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
RA   Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA   Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA   Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT   "DNA sequence of human chromosome 17 and analysis of rearrangement in
RT   the human lineage.";
RL   Nature 440:1045-1049(2006).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Eye, and Testis;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-176 (ISOFORM 3).
RC   TISSUE=Neuroblastoma;
RA   Li W.B., Gruber C., Jessee J., Polayes D.;
RT   "Full-length cDNA libraries and normalization.";
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 189-1122 (ISOFORM 1).
RC   TISSUE=Colon carcinoma;
RX   PubMed=9610721;
RX   DOI=10.1002/(SICI)1097-0215(19980529)76:5<652::AID-IJC7>3.0.CO;2-P;
RA   Scanlan M.J., Chen Y.-T., Williamson B., Gure A.O., Stockert E.,
RA   Gordan J.D., Tuereci O., Sahin U., Pfreundschuh M., Old L.J.;
RT   "Characterization of human colon cancer antigens recognized by
RT   autologous antibodies.";
RL   Int. J. Cancer 76:652-658(1998).
RN   [8]
RP   GENE ORGANIZATION.
RX   PubMed=11018260; DOI=10.1016/S0167-4781(00)00191-3;
RA   Mahlknecht U., Schnittger S., Ottmann O.G., Schoch C., Mosebach M.,
RA   Hiddemann W., Hoelzer D.;
RT   "Chromosomal organization and localization of the human histone
RT   deacetylase 5 gene (HDAC5).";
RL   Biochim. Biophys. Acta 1493:342-348(2000).
RN   [9]
RP   INTERACTION WITH BCOR.
RX   PubMed=10898795;
RA   Huynh K.D., Fischle W., Verdin E., Bardwell V.J.;
RT   "BCoR, a novel corepressor involved in BCL-6 repression.";
RL   Genes Dev. 14:1810-1823(2000).
RN   [10]
RP   SUBCELLULAR LOCATION, PHOSPHORYLATION, AND MUTAGENESIS OF SER-259;
RP   SER-279; SER-498; SER-661 AND SER-713.
RX   PubMed=11081517; DOI=10.1038/35040593;
RA   McKinsey T.A., Zhang C.-L., Lu J., Olson E.N.;
RT   "Signal-dependent nuclear export of a histone deacetylase regulates
RT   muscle differentiation.";
RL   Nature 408:106-111(2000).
RN   [11]
RP   INTERACTION WITH 14-3-3, AND PHOSPHORYLATION AT SER-259 AND SER-498.
RX   PubMed=11114197; DOI=10.1073/pnas.260501497;
RA   McKinsey T.A., Zhang C.-L., Olson E.N.;
RT   "Activation of the myocyte enhancer factor-2 transcription factor by
RT   calcium/calmodulin-dependent protein kinase-stimulated binding of 14-
RT   3-3 to histone deacetylase 5.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:14400-14405(2000).
RN   [12]
RP   NUCLEAR EXPORT SIGNAL, AND MUTAGENESIS OF VAL-1086 AND LEU-1092.
RX   PubMed=11509672; DOI=10.1128/MCB.21.18.6312-6321.2001;
RA   McKinsey T.A., Zhang C.-L., Olson E.N.;
RT   "Identification of a signal-responsive nuclear export sequence in
RT   class II histone deacetylases.";
RL   Mol. Cell. Biol. 21:6312-6321(2001).
RN   [13]
RP   UBIQUITINATION.
RX   PubMed=12354939; DOI=10.1073/pnas.172511699;
RA   Hook S.S., Orian A., Cowley S.M., Eisenman R.N.;
RT   "Histone deacetylase 6 binds polyubiquitin through its zinc finger
RT   (PAZ domain) and copurifies with deubiquitinating enzymes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:13425-13430(2002).
RN   [14]
RP   INTERACTION WITH BCL6.
RX   PubMed=12504096; DOI=10.1016/S0006-291X(02)02873-5;
RA   Mascle X., Albagli O., Lemercier C.;
RT   "Point mutations in BCL6 DNA-binding domain reveal distinct roles for
RT   the six zinc fingers.";
RL   Biochem. Biophys. Res. Commun. 300:391-396(2003).
RN   [15]
RP   INTERACTION WITH KDM5B.
RX   PubMed=17373667; DOI=10.1002/ijc.22673;
RA   Barrett A., Santangelo S., Tan K., Catchpole S., Roberts K.,
RA   Spencer-Dene B., Hall D., Scibetta A., Burchell J., Verdin E.,
RA   Freemont P., Taylor-Papadimitriou J.;
RT   "Breast cancer associated transcriptional repressor PLU-1/JARID1B
RT   interacts directly with histone deacetylases.";
RL   Int. J. Cancer 121:265-275(2007).
RN   [16]
RP   INTERACTION WITH DDIT3.
RX   PubMed=17872950; DOI=10.1074/jbc.M703735200;
RA   Ohoka N., Hattori T., Kitagawa M., Onozaki K., Hayashi H.;
RT   "Critical and functional regulation of CHOP (C/EBP homologous protein)
RT   through the N-terminal portion.";
RL   J. Biol. Chem. 282:35687-35694(2007).
RN   [17]
RP   PHOSPHORYLATION AT SER-259 AND SER-498, SUBCELLULAR LOCATION, AND
RP   MUTAGENESIS OF SER-259 AND SER-498.
RX   PubMed=18184930; DOI=10.2337/db07-0843;
RA   McGee S.L., van Denderen B.J., Howlett K.F., Mollica J.,
RA   Schertzer J.D., Kemp B.E., Hargreaves M.;
RT   "AMP-activated protein kinase regulates GLUT4 transcription by
RT   phosphorylating histone deacetylase 5.";
RL   Diabetes 57:860-867(2008).
RN   [18]
RP   PHOSPHORYLATION AT SER-259 AND SER-498.
RX   PubMed=18332134; DOI=10.1074/jbc.M800264200;
RA   Ha C.H., Wang W., Jhun B.S., Wong C., Hausser A., Pfizenmaier K.,
RA   McKinsey T.A., Olson E.N., Jin Z.G.;
RT   "Protein kinase D-dependent phosphorylation and nuclear export of
RT   histone deacetylase 5 mediates vascular endothelial growth factor-
RT   induced gene expression and angiogenesis.";
RL   J. Biol. Chem. 283:14590-14599(2008).
RN   [19]
RP   INTERACTION WITH BAHD1.
RX   PubMed=19666599; DOI=10.1073/pnas.0901259106;
RA   Bierne H., Tham T.N., Batsche E., Dumay A., Leguillou M.,
RA   Kerneis-Golsteyn S., Regnault B., Seeler J.S., Muchardt C.,
RA   Feunteun J., Cossart P.;
RT   "Human BAHD1 promotes heterochromatic gene silencing.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:13826-13831(2009).
RN   [20]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-533, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19608861; DOI=10.1126/science.1175371;
RA   Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA   Walther T.C., Olsen J.V., Mann M.;
RT   "Lysine acetylation targets protein complexes and co-regulates major
RT   cellular functions.";
RL   Science 325:834-840(2009).
RN   [21]
RP   PHOSPHORYLATION AT THR-292, AND MUTAGENESIS OF SER-259; SER-291 AND
RP   THR-292.
RX   PubMed=20188095; DOI=10.1016/j.febslet.2010.02.057;
RA   Harrison B.C., Huynh K., Lundgaard G.L., Helmke S.M., Perryman M.B.,
RA   McKinsey T.A.;
RT   "Protein kinase C-related kinase targets nuclear localization signals
RT   in a subset of class IIa histone deacetylases.";
RL   FEBS Lett. 584:1103-1110(2010).
RN   [22]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA   Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [23]
RP   FUNCTION, AND INTERACTION WITH EP300.
RX   PubMed=24413532; DOI=10.1158/0008-5472.CAN-13-2020;
RA   Kang H.J., Lee M.H., Kang H.L., Kim S.H., Ahn J.R., Na H., Na T.Y.,
RA   Kim Y.N., Seong J.K., Lee M.O.;
RT   "Differential regulation of estrogen receptor alpha expression in
RT   breast cancer cells by metastasis-associated protein 1.";
RL   Cancer Res. 74:1484-1494(2014).
RN   [24]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
RA   Wang L., Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human
RT   liver phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
CC   -!- FUNCTION: Responsible for the deacetylation of lysine residues on
CC       the N-terminal part of the core histones (H2A, H2B, H3 and H4).
CC       Histone deacetylation gives a tag for epigenetic repression and
CC       plays an important role in transcriptional regulation, cell cycle
CC       progression and developmental events. Histone deacetylases act via
CC       the formation of large multiprotein complexes. Involved in muscle
CC       maturation by repressing transcription of myocyte enhancer MEF2C.
CC       During muscle differentiation, it shuttles into the cytoplasm,
CC       allowing the expression of myocyte enhancer factors. Involved in
CC       the MTA1-mediated epigenetic regulation of ESR1 expression in
CC       breast cancer. {ECO:0000269|PubMed:24413532}.
CC   -!- CATALYTIC ACTIVITY: Hydrolysis of an N(6)-acetyl-lysine residue of
CC       a histone to yield a deacetylated histone.
CC   -!- SUBUNIT: Interacts with AHRR, BAHD1, BCOR, HDAC7, HDAC9, CTBP1,
CC       MEF2C, NCOR2, NRIP1, PHB2 and a 14-3-3 chaperone protein.
CC       Interacts with BCL6, DDIT3/CHOP, GRK5, KDM5B and MYOCD. Interacts
CC       with EP300 in the presence of TFAP2C.
CC       {ECO:0000269|PubMed:10898795, ECO:0000269|PubMed:11114197,
CC       ECO:0000269|PubMed:12504096, ECO:0000269|PubMed:17373667,
CC       ECO:0000269|PubMed:17872950, ECO:0000269|PubMed:19666599,
CC       ECO:0000269|PubMed:24413532}.
CC   -!- INTERACTION:
CC       Q9HCU9:BRMS1; NbExp=2; IntAct=EBI-715576, EBI-714781;
CC       P08393:ICP0 (xeno); NbExp=3; IntAct=EBI-715576, EBI-6148881;
CC       Q13761:RUNX3; NbExp=5; IntAct=EBI-715576, EBI-925990;
CC       P31947:SFN; NbExp=3; IntAct=EBI-715576, EBI-476295;
CC       P63104:YWHAZ; NbExp=2; IntAct=EBI-715576, EBI-347088;
CC   -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Shuttles between
CC       the nucleus and the cytoplasm. In muscle cells, it shuttles into
CC       the cytoplasm during myocyte differentiation. The export to
CC       cytoplasm depends on the interaction with a 14-3-3 chaperone
CC       protein and is due to its phosphorylation at Ser-259 and Ser-498
CC       by AMPK, CaMK1 and SIK1.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q9UQL6-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9UQL6-2; Sequence=VSP_002081;
CC         Note=No experimental confirmation available.;
CC       Name=3;
CC         IsoId=Q9UQL6-3; Sequence=VSP_039180;
CC   -!- TISSUE SPECIFICITY: Ubiquitous.
CC   -!- DOMAIN: The nuclear export sequence mediates the shuttling between
CC       the nucleus and the cytoplasm. {ECO:0000250}.
CC   -!- PTM: Phosphorylated by AMPK, CaMK1, SIK1 and PRKD1 at Ser-259 and
CC       Ser-498. The phosphorylation is required for the export to the
CC       cytoplasm and inhibition. Phosphorylated by the PKC kinases PKN1
CC       and PKN2, impairing nuclear import. Phosphorylated by GRK5,
CC       leading to nuclear export of HDAC5 and allowing MEF2-mediated
CC       transcription (By similarity). {ECO:0000250}.
CC   -!- PTM: Ubiquitinated. Polyubiquitination however does not lead to
CC       its degradation. {ECO:0000269|PubMed:12354939}.
CC   -!- SIMILARITY: Belongs to the histone deacetylase family. HD type 2
CC       subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC18040.1; Type=Frameshift; Positions=1085; Evidence={ECO:0000305};
CC       Sequence=BAA25526.2; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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DR   EMBL; AF132608; AAD29047.1; -; mRNA.
DR   EMBL; AB011172; BAA25526.2; ALT_INIT; mRNA.
DR   EMBL; AC023855; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC013140; AAH13140.1; ALT_TERM; mRNA.
DR   EMBL; BC051824; AAH51824.1; -; mRNA.
DR   EMBL; BX458255; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AF039691; AAC18040.1; ALT_FRAME; mRNA.
DR   EMBL; BK000028; DAA00017.1; -; Genomic_DNA.
DR   CCDS; CCDS32663.1; -. [Q9UQL6-3]
DR   CCDS; CCDS45696.1; -. [Q9UQL6-1]
DR   RefSeq; NP_001015053.1; NM_001015053.1. [Q9UQL6-3]
DR   RefSeq; NP_005465.2; NM_005474.4. [Q9UQL6-1]
DR   RefSeq; XP_005256961.1; XM_005256904.3. [Q9UQL6-3]
DR   RefSeq; XP_005256963.1; XM_005256906.3. [Q9UQL6-1]
DR   UniGene; Hs.438782; -.
DR   ProteinModelPortal; Q9UQL6; -.
DR   SMR; Q9UQL6; 96-133, 681-1061.
DR   BioGrid; 115331; 343.
DR   DIP; DIP-38260N; -.
DR   IntAct; Q9UQL6; 28.
DR   MINT; MINT-1407477; -.
DR   STRING; 9606.ENSP00000225983; -.
DR   BindingDB; Q9UQL6; -.
DR   ChEMBL; CHEMBL3038483; -.
DR   GuidetoPHARMACOLOGY; 2660; -.
DR   PhosphoSite; Q9UQL6; -.
DR   BioMuta; HDAC5; -.
DR   DMDM; 296434519; -.
DR   MaxQB; Q9UQL6; -.
DR   PaxDb; Q9UQL6; -.
DR   PRIDE; Q9UQL6; -.
DR   Ensembl; ENST00000225983; ENSP00000225983; ENSG00000108840. [Q9UQL6-3]
DR   Ensembl; ENST00000336057; ENSP00000337290; ENSG00000108840. [Q9UQL6-2]
DR   Ensembl; ENST00000586802; ENSP00000468004; ENSG00000108840. [Q9UQL6-1]
DR   GeneID; 10014; -.
DR   KEGG; hsa:10014; -.
DR   UCSC; uc002ifd.1; human. [Q9UQL6-1]
DR   UCSC; uc002iff.1; human. [Q9UQL6-3]
DR   UCSC; uc010czp.1; human. [Q9UQL6-2]
DR   CTD; 10014; -.
DR   GeneCards; HDAC5; -.
DR   H-InvDB; HIX0013862; -.
DR   HGNC; HGNC:14068; HDAC5.
DR   HPA; CAB019400; -.
DR   HPA; HPA030991; -.
DR   MIM; 605315; gene.
DR   neXtProt; NX_Q9UQL6; -.
DR   PharmGKB; PA29230; -.
DR   eggNOG; KOG1343; Eukaryota.
DR   eggNOG; COG0123; LUCA.
DR   GeneTree; ENSGT00530000062809; -.
DR   HOGENOM; HOG000232065; -.
DR   HOVERGEN; HBG057100; -.
DR   InParanoid; Q9UQL6; -.
DR   KO; K11406; -.
DR   OMA; AANMRTV; -.
DR   OrthoDB; EOG7RFTH5; -.
DR   PhylomeDB; Q9UQL6; -.
DR   TreeFam; TF106174; -.
DR   Reactome; R-HSA-2122947; NOTCH1 Intracellular Domain Regulates Transcription.
DR   Reactome; R-HSA-2644606; Constitutive Signaling by NOTCH1 PEST Domain Mutants.
DR   Reactome; R-HSA-2894862; Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
DR   ChiTaRS; HDAC5; human.
DR   GeneWiki; Histone_deacetylase_5; -.
DR   GenomeRNAi; 10014; -.
DR   NextBio; 37831; -.
DR   PRO; PR:Q9UQL6; -.
DR   Proteomes; UP000005640; Chromosome 17.
DR   Bgee; Q9UQL6; -.
DR   CleanEx; HS_HDAC5; -.
DR   ExpressionAtlas; Q9UQL6; baseline and differential.
DR   Genevisible; Q9UQL6; HS.
DR   GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR   GO; GO:0000118; C:histone deacetylase complex; TAS:UniProtKB.
DR   GO; GO:0016604; C:nuclear body; IEA:Ensembl.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
DR   GO; GO:0001047; F:core promoter binding; IDA:UniProtKB.
DR   GO; GO:0004407; F:histone deacetylase activity; IDA:BHF-UCL.
DR   GO; GO:0042826; F:histone deacetylase binding; IPI:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0032041; F:NAD-dependent histone deacetylase activity (H3-K14 specific); IEA:UniProtKB-EC.
DR   GO; GO:0033558; F:protein deacetylase activity; IMP:UniProtKB.
DR   GO; GO:0005080; F:protein kinase C binding; IPI:UniProtKB.
DR   GO; GO:0070491; F:repressing transcription factor binding; IPI:BHF-UCL.
DR   GO; GO:0001025; F:RNA polymerase III transcription factor binding; IPI:UniProtKB.
DR   GO; GO:0003714; F:transcription corepressor activity; IEA:Ensembl.
DR   GO; GO:0008134; F:transcription factor binding; IPI:BHF-UCL.
DR   GO; GO:0042113; P:B cell activation; TAS:UniProtKB.
DR   GO; GO:0030183; P:B cell differentiation; TAS:UniProtKB.
DR   GO; GO:0032869; P:cellular response to insulin stimulus; NAS:BHF-UCL.
DR   GO; GO:0071222; P:cellular response to lipopolysaccharide; IEA:Ensembl.
DR   GO; GO:0016568; P:chromatin modification; TAS:UniProtKB.
DR   GO; GO:0006325; P:chromatin organization; TAS:UniProtKB.
DR   GO; GO:0006338; P:chromatin remodeling; TAS:ProtInc.
DR   GO; GO:0006342; P:chromatin silencing; TAS:ProtInc.
DR   GO; GO:0007507; P:heart development; IEA:Ensembl.
DR   GO; GO:0016575; P:histone deacetylation; IDA:BHF-UCL.
DR   GO; GO:0006954; P:inflammatory response; TAS:UniProtKB.
DR   GO; GO:0033555; P:multicellular organismal response to stress; IEA:Ensembl.
DR   GO; GO:0090051; P:negative regulation of cell migration involved in sprouting angiogenesis; IMP:BHF-UCL.
DR   GO; GO:0010832; P:negative regulation of myotube differentiation; IMP:BHF-UCL.
DR   GO; GO:0045668; P:negative regulation of osteoblast differentiation; IEA:Ensembl.
DR   GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IMP:UniProtKB.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; TAS:UniProtKB.
DR   GO; GO:0030182; P:neuron differentiation; IEA:Ensembl.
DR   GO; GO:0007219; P:Notch signaling pathway; TAS:Reactome.
DR   GO; GO:0002076; P:osteoblast development; IEA:Ensembl.
DR   GO; GO:0051091; P:positive regulation of sequence-specific DNA binding transcription factor activity; IMP:BHF-UCL.
DR   GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IMP:BHF-UCL.
DR   GO; GO:0006476; P:protein deacetylation; IMP:UniProtKB.
DR   GO; GO:0040029; P:regulation of gene expression, epigenetic; IMP:UniProtKB.
DR   GO; GO:0010830; P:regulation of myotube differentiation; ISS:UniProtKB.
DR   GO; GO:0043393; P:regulation of protein binding; IMP:BHF-UCL.
DR   GO; GO:0048742; P:regulation of skeletal muscle fiber development; IEA:Ensembl.
DR   GO; GO:0014823; P:response to activity; IEA:Ensembl.
DR   GO; GO:0042220; P:response to cocaine; IEA:Ensembl.
DR   GO; GO:0042493; P:response to drug; IEA:Ensembl.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.800.20; -; 1.
DR   InterPro; IPR000286; His_deacetylse.
DR   InterPro; IPR023801; His_deacetylse_dom.
DR   InterPro; IPR024643; Hist_deacetylase_Gln_rich_N.
DR   InterPro; IPR017320; Histone_deAcase_II_euk.
DR   InterPro; IPR030703; Histone_deacetylase_5.
DR   PANTHER; PTHR10625; PTHR10625; 2.
DR   PANTHER; PTHR10625:SF57; PTHR10625:SF57; 2.
DR   Pfam; PF12203; HDAC4_Gln; 1.
DR   Pfam; PF00850; Hist_deacetyl; 1.
DR   PIRSF; PIRSF037911; HDAC_II_euk; 1.
DR   PRINTS; PR01270; HDASUPER.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Chromatin regulator;
KW   Complete proteome; Cytoplasm; Hydrolase; Metal-binding; Nucleus;
KW   Phosphoprotein; Polymorphism; Reference proteome; Repressor;
KW   Transcription; Transcription regulation; Ubl conjugation; Zinc.
FT   CHAIN         1   1122       Histone deacetylase 5.
FT                                /FTId=PRO_0000114701.
FT   REGION      684   1028       Histone deacetylase.
FT   MOTIF      1081   1122       Nuclear export signal.
FT   COMPBIAS     47     52       Poly-Gly.
FT   COMPBIAS     85     92       Poly-Gln.
FT   COMPBIAS    596    599       Poly-Glu.
FT   COMPBIAS   1099   1104       Poly-Ala.
FT   ACT_SITE    833    833       {ECO:0000250}.
FT   METAL       696    696       Zinc. {ECO:0000250}.
FT   METAL       698    698       Zinc. {ECO:0000250}.
FT   METAL       704    704       Zinc. {ECO:0000250}.
FT   METAL       781    781       Zinc. {ECO:0000250}.
FT   MOD_RES     259    259       Phosphoserine; by AMPK, CaMK1, SIK1 and
FT                                PKD/PRKD1. {ECO:0000269|PubMed:11114197,
FT                                ECO:0000269|PubMed:18184930,
FT                                ECO:0000269|PubMed:18332134}.
FT   MOD_RES     292    292       Phosphothreonine; by PKC.
FT                                {ECO:0000269|PubMed:20188095}.
FT   MOD_RES     498    498       Phosphoserine; by AMPK, CaMK1, SIK1 and
FT                                PKD/PRKD1. {ECO:0000269|PubMed:11114197,
FT                                ECO:0000269|PubMed:18184930,
FT                                ECO:0000269|PubMed:18332134}.
FT   MOD_RES     533    533       N6-acetyllysine.
FT                                {ECO:0000244|PubMed:19608861}.
FT   MOD_RES     661    661       Phosphoserine.
FT                                {ECO:0000269|PubMed:11081517}.
FT   VAR_SEQ       7      7       S -> SA (in isoform 3).
FT                                {ECO:0000303|Ref.6}.
FT                                /FTId=VSP_039180.
FT   VAR_SEQ     684    768       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:9628581}.
FT                                /FTId=VSP_002081.
FT   VARIANT     137    137       R -> Q (in dbSNP:rs438096).
FT                                /FTId=VAR_055903.
FT   VARIANT     565    565       G -> A (in dbSNP:rs33916560).
FT                                /FTId=VAR_055904.
FT   MUTAGEN     259    259       S->A: Reduces AMPK- and caMK-dependent
FT                                phosphorylation and the subsequent
FT                                nuclear export. Abolishes nuclear export;
FT                                when associated with A-498. Does not
FT                                affect phosphorylation by PKN1 and PKN2.
FT                                {ECO:0000269|PubMed:11081517,
FT                                ECO:0000269|PubMed:18184930,
FT                                ECO:0000269|PubMed:20188095}.
FT   MUTAGEN     279    279       S->A: No effect.
FT                                {ECO:0000269|PubMed:11081517}.
FT   MUTAGEN     291    291       S->A: Does not affect phosphorylation by
FT                                PKC. {ECO:0000269|PubMed:20188095}.
FT   MUTAGEN     292    292       T->A: Abolishes phosphorylation by PKC.
FT                                {ECO:0000269|PubMed:20188095}.
FT   MUTAGEN     498    498       S->A: Reduces AMPK- and CaMK-dependent
FT                                phosphorylation and the subsequent
FT                                nuclear export. Abolishes nuclear export;
FT                                when associated with A-259.
FT                                {ECO:0000269|PubMed:11081517,
FT                                ECO:0000269|PubMed:18184930}.
FT   MUTAGEN     661    661       S->A: No effect.
FT                                {ECO:0000269|PubMed:11081517}.
FT   MUTAGEN     713    713       S->A: No effect.
FT                                {ECO:0000269|PubMed:11081517}.
FT   MUTAGEN    1086   1086       V->A: Reduces CaMK-dependent nuclear
FT                                export. {ECO:0000269|PubMed:11509672}.
FT   MUTAGEN    1092   1092       L->A: Reduces CaMK-dependent nuclear
FT                                export. {ECO:0000269|PubMed:11509672}.
FT   CONFLICT     37     37       V -> L (in Ref. 6; BX458255).
FT                                {ECO:0000305}.
FT   CONFLICT    139    139       Q -> R (in Ref. 6; BX458255).
FT                                {ECO:0000305}.
FT   CONFLICT    147    147       R -> G (in Ref. 6; BX458255).
FT                                {ECO:0000305}.
FT   CONFLICT    593    593       D -> E (in Ref. 1; AAD29047, 5; AAH51824
FT                                and 7; AAC18040). {ECO:0000305}.
FT   CONFLICT    671    671       S -> N (in Ref. 7; AAC18040).
FT                                {ECO:0000305}.
FT   CONFLICT    684    684       G -> S (in Ref. 7; AAC18040).
FT                                {ECO:0000305}.
FT   CONFLICT   1026   1026       E -> K (in Ref. 7; AAC18040).
FT                                {ECO:0000305}.
FT   CONFLICT   1074   1074       E -> G (in Ref. 7; AAC18040).
FT                                {ECO:0000305}.
FT   CONFLICT   1093   1093       S -> L (in Ref. 7; AAC18040).
FT                                {ECO:0000305}.
SQ   SEQUENCE   1122 AA;  121978 MW;  CF4BE774E3588FEC CRC64;
     MNSPNESDGM SGREPSLEIL PRTSLHSIPV TVEVKPVLPR AMPSSMGGGG GGSPSPVELR
     GALVGSVDPT LREQQLQQEL LALKQQQQLQ KQLLFAEFQK QHDHLTRQHE VQLQKHLKQQ
     QEMLAAKQQQ EMLAAKRQQE LEQQRQREQQ RQEELEKQRL EQQLLILRNK EKSKESAIAS
     TEVKLRLQEF LLSKSKEPTP GGLNHSLPQH PKCWGAHHAS LDQSSPPQSG PPGTPPSYKL
     PLPGPYDSRD DFPLRKTASE PNLKVRSRLK QKVAERRSSP LLRRKDGTVI STFKKRAVEI
     TGAGPGASSV CNSAPGSGPS SPNSSHSTIA ENGFTGSVPN IPTEMLPQHR ALPLDSSPNQ
     FSLYTSPSLP NISLGLQATV TVTNSHLTAS PKLSTQQEAE RQALQSLRQG GTLTGKFMST
     SSIPGCLLGV ALEGDGSPHG HASLLQHVLL LEQARQQSTL IAVPLHGQSP LVTGERVATS
     MRTVGKLPRH RPLSRTQSSP LPQSPQALQQ LVMQQQHQQF LEKQKQQQLQ LGKILTKTGE
     LPRQPTTHPE ETEEELTEQQ EVLLGEGALT MPREGSTESE STQEDLEEED EEDDGEEEED
     CIQVKDEEGE SGAEEGPDLE EPGAGYKKLF SDAQPLQPLQ VYQAPLSLAT VPHQALGRTQ
     SSPAAPGGMK SPPDQPVKHL FTTGVVYDTF MLKHQCMCGN THVHPEHAGR IQSIWSRLQE
     TGLLSKCERI RGRKATLDEI QTVHSEYHTL LYGTSPLNRQ KLDSKKLLGP ISQKMYAVLP
     CGGIGVDSDT VWNEMHSSSA VRMAVGCLLE LAFKVAAGEL KNGFAIIRPP GHHAEESTAM
     GFCFFNSVAI TAKLLQQKLN VGKVLIVDWD IHHGNGTQQA FYNDPSVLYI SLHRYDNGNF
     FPGSGAPEEV GGGPGVGYNV NVAWTGGVDP PIGDVEYLTA FRTVVMPIAH EFSPDVVLVS
     AGFDAVEGHL SPLGGYSVTA RCFGHLTRQL MTLAGGRVVL ALEGGHDLTA ICDASEACVS
     ALLSVELQPL DEAVLQQKPN INAVATLEKV IEIQSKHWSC VQKFAAGLGR SLREAQAGET
     EEAETVSAMA LLSVGAEQAQ AAAAREHSPR PAEEPMEQEP AL
//
ID   HDAC9_MOUSE             Reviewed;         588 AA.
AC   Q99N13; Q4QQN7; Q8R4Y6; Q9EPT2;
DT   18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT   20-MAR-2007, sequence version 2.
DT   11-NOV-2015, entry version 132.
DE   RecName: Full=Histone deacetylase 9;
DE            Short=HD9;
DE            EC=3.5.1.98;
DE   AltName: Full=Histone deacetylase 7B;
DE            Short=HD7b;
DE   AltName: Full=Histone deacetylase-related protein;
DE   AltName: Full=MEF2-interacting transcription repressor MITR;
GN   Name=Hdac9; Synonyms=Hdac7b, Hdrp, Mitr;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), HOMODIMERIZATION, INTERACTION
RP   WITH CTBP1; HDAC1; HDAC3; HDAC4 AND HDAC5, AND MUTAGENESIS OF
RP   25-ASP-LEU-26.
RC   STRAIN=NIH Swiss; TISSUE=Embryonic heart;
RX   PubMed=11022042; DOI=10.1074/jbc.M007364200;
RA   Zhang C.L., McKinsey T.A., Lu J.R., Olson E.N.;
RT   "Association of COOH-terminal-binding protein (CtBP) and MEF2-
RT   interacting transcription repressor (MITR) contributes to
RT   transcriptional repression of the MEF2 transcription factor.";
RL   J. Biol. Chem. 276:35-39(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=Swiss Webster / NIH;
RA   Zhou X., Richon V.M., Rifkind R.A., Marks P.A.;
RT   "Cloning of the mouse HDRP cDNA.";
RL   Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Retina;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   FUNCTION, PHOSPHORYLATION AT SER-220 AND SER-450, TISSUE SPECIFICITY,
RP   DEVELOPMENTAL STAGE, AND SUBCELLULAR LOCATION.
RX   PubMed=11390982; DOI=10.1073/pnas.131198498;
RA   Zhang C.L., McKinsey T.A., Olson E.N.;
RT   "The transcriptional corepressor MITR is a signal-responsive inhibitor
RT   of myogenesis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:7354-7359(2001).
RN   [5]
RP   PHOSPHORYLATION AT SER-220 AND SER-450, FUNCTION, AND DISRUPTION
RP   PHENOTYPE.
RX   PubMed=12202037; DOI=10.1016/S0092-8674(02)00861-9;
RA   Zhang C.L., McKinsey T.A., Chang S., Antos C.L., Hill J.A.,
RA   Olson E.N.;
RT   "Class II histone deacetylases act as signal-responsive repressors of
RT   cardiac hypertrophy.";
RL   Cell 110:479-488(2002).
RN   [6]
RP   PHOSPHORYLATION AT SER-240, AND SUBCELLULAR LOCATION.
RX   PubMed=15546868; DOI=10.1074/jbc.M411894200;
RA   Deng X., Ewton D.Z., Mercer S.E., Friedman E.;
RT   "Mirk/dyrk1B decreases the nuclear accumulation of class II histone
RT   deacetylases during skeletal muscle differentiation.";
RL   J. Biol. Chem. 280:4894-4905(2005).
RN   [7]
RP   FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, DOWN-REGULATION BY
RP   DENERVATION, INTERACTION WITH HDAC1 AND HDAC3, AND SUBCELLULAR
RP   LOCATION.
RX   PubMed=15711539; DOI=10.1038/nn1408;
RA   Mejat A., Ramond F., Bassel-Duby R., Khochbin S., Olson E.N.,
RA   Schaeffer L.;
RT   "Histone deacetylase 9 couples neuronal activity to muscle chromatin
RT   acetylation and gene expression.";
RL   Nat. Neurosci. 8:313-321(2005).
RN   [8]
RP   DOWN-REGULATION BY NEURONAL APOPTOSIS, FUNCTION, AND INTERACTION WITH
RP   HDAC1 AND MAPK10.
RX   PubMed=16611996; DOI=10.1128/MCB.26.9.3550-3564.2006;
RA   Morrison B.E., Majdzadeh N., Zhang X., Lyles A., Bassel-Duby R.,
RA   Olson E.N., D'Mello S.R.;
RT   "Neuroprotection by histone deacetylase-related protein.";
RL   Mol. Cell. Biol. 26:3550-3564(2006).
RN   [9]
RP   INDUCTION BY MEF2, AND DEVELOPMENTAL STAGE.
RX   PubMed=17101791; DOI=10.1128/MCB.01415-06;
RA   Haberland M., Arnold M.A., McAnally J., Phan D., Kim Y., Olson E.N.;
RT   "Regulation of HDAC9 gene expression by MEF2 establishes a negative-
RT   feedback loop in the transcriptional circuitry of muscle
RT   differentiation.";
RL   Mol. Cell. Biol. 27:518-525(2007).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-552, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and
RT   expression.";
RL   Cell 143:1174-1189(2010).
RN   [11]
RP   X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 139-158 IN COMPLEX WITH MEF2
RP   AND DNA.
RX   PubMed=15567413; DOI=10.1016/j.jmb.2004.10.033;
RA   Han A., He J., Wu Y., Liu J.O., Chen L.;
RT   "Mechanism of recruitment of class II histone deacetylases by myocyte
RT   enhancer factor-2.";
RL   J. Mol. Biol. 345:91-102(2005).
CC   -!- FUNCTION: Devoided of intrinsic deacetylase activity, promotes the
CC       deacetylation of lysine residues on the N-terminal part of the
CC       core histones (H2A, H2B, H3 and H4) by recruiting HDAC1 and HDAC3.
CC       Histone deacetylation gives a tag for epigenetic repression and
CC       plays an important role in transcriptional regulation, cell cycle
CC       progression and developmental events. Represses MEF2-dependent
CC       transcription, inhibits skeletal myogenesis and may be involved in
CC       heart development. Protects neurons from apoptosis, both by
CC       inhibiting JUN phosphorylation by MAPK10 and by repressing JUN
CC       transcription via HDAC1 recruitment to JUN promoter.
CC       {ECO:0000269|PubMed:11390982, ECO:0000269|PubMed:12202037,
CC       ECO:0000269|PubMed:15711539, ECO:0000269|PubMed:16611996}.
CC   -!- CATALYTIC ACTIVITY: Hydrolysis of an N(6)-acetyl-lysine residue of
CC       a histone to yield a deacetylated histone.
CC   -!- SUBUNIT: Homodimer. Interacts with ETV6 (By similarity). Interacts
CC       with MEF2, HDAC1, HDAC3, HDAC4, HDAC5, CTBP1 and MAPK10. The
CC       phosphorylated form interacts with 14-3-3. Interacts with FOXP3 in
CC       the absence of T-cell stimulation (By similarity).
CC       {ECO:0000250|UniProtKB:Q9UKV0, ECO:0000269|PubMed:11022042,
CC       ECO:0000269|PubMed:15567413, ECO:0000269|PubMed:15711539,
CC       ECO:0000269|PubMed:16611996}.
CC   -!- INTERACTION:
CC       P60335:Pcbp1; NbExp=6; IntAct=EBI-645361, EBI-309059;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11390982,
CC       ECO:0000269|PubMed:15546868, ECO:0000269|PubMed:15711539}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q99N13-1; Sequence=Displayed;
CC       Name=2; Synonyms=Hdrpa;
CC         IsoId=Q99N13-2; Sequence=VSP_023769;
CC         Note=No experimental confirmation available.;
CC       Name=3;
CC         IsoId=Q99N13-3; Sequence=VSP_029173;
CC   -!- TISSUE SPECIFICITY: Expressed at high levels in heart, brain and
CC       spleen. Expressed in skeletal muscle.
CC       {ECO:0000269|PubMed:11390982, ECO:0000269|PubMed:15711539}.
CC   -!- DEVELOPMENTAL STAGE: At E10.5, expressed in heart, skeletal muscle
CC       and neural lineages. At E11.5, expressed in heart, dorsal root
CC       ganglia and neural tube. At E12.5, expressed in heart, skeletal
CC       muscle, dorsal root ganglia, neural tube and retina. Strongly up-
CC       regulated in muscle between E14 and E19 as a result of motor
CC       innervation. {ECO:0000269|PubMed:11390982,
CC       ECO:0000269|PubMed:15711539, ECO:0000269|PubMed:17101791}.
CC   -!- INDUCTION: By MEF2 during muscle differentiation. Down-regulated
CC       by muscle denervation. Down-regulated by trichostatin A or sodium
CC       butyrate, and during neuronal apoptosis (at protein level).
CC       {ECO:0000269|PubMed:17101791}.
CC   -!- PTM: Sumoylated. {ECO:0000250}.
CC   -!- PTM: Phosphorylated on Ser-220 and Ser-450; which promotes 14-3-3-
CC       binding, impairs interaction with MEF2, and antagonizes
CC       antimyogenic activity. Phosphorylated on Ser-240 by DYRK1B; which
CC       impairs nuclear accumulation. Phosphorylated by the PKC kinases
CC       PKN1 and PKN2, impairing nuclear import.
CC       {ECO:0000269|PubMed:11390982, ECO:0000269|PubMed:12202037,
CC       ECO:0000269|PubMed:15546868}.
CC   -!- DISRUPTION PHENOTYPE: Mice do not present any abnormality at early
CC       age but develop cardiac hypertrophy by eight months of age.
CC       {ECO:0000269|PubMed:12202037}.
CC   -!- SIMILARITY: Belongs to the histone deacetylase family. HD type 2
CC       subfamily. {ECO:0000305}.
CC   -----------------------------------------------------------------------
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DR   EMBL; AF324492; AAG48332.1; -; mRNA.
DR   EMBL; AF235053; AAK15027.1; -; mRNA.
DR   EMBL; AF279371; AAL86358.1; -; mRNA.
DR   EMBL; BC098187; AAH98187.1; -; mRNA.
DR   CCDS; CCDS36432.1; -. [Q99N13-1]
DR   RefSeq; NP_077038.2; NM_024124.3.
DR   UniGene; Mm.310551; -.
DR   UniGene; Mm.483009; -.
DR   PDB; 1TQE; X-ray; 2.70 A; X/Y=139-158.
DR   PDBsum; 1TQE; -.
DR   ProteinModelPortal; Q99N13; -.
DR   SMR; Q99N13; 37-101.
DR   BioGrid; 219748; 8.
DR   DIP; DIP-41905N; -.
DR   IntAct; Q99N13; 5.
DR   MINT; MINT-146908; -.
DR   STRING; 10090.ENSMUSP00000106443; -.
DR   PhosphoSite; Q99N13; -.
DR   MaxQB; Q99N13; -.
DR   PaxDb; Q99N13; -.
DR   PRIDE; Q99N13; -.
DR   GeneID; 79221; -.
DR   UCSC; uc007nja.1; mouse. [Q99N13-3]
DR   UCSC; uc007njb.1; mouse. [Q99N13-2]
DR   UCSC; uc007njc.2; mouse. [Q99N13-1]
DR   CTD; 9734; -.
DR   MGI; MGI:1931221; Hdac9.
DR   eggNOG; KOG1343; Eukaryota.
DR   eggNOG; COG0123; LUCA.
DR   HOGENOM; HOG000232065; -.
DR   HOVERGEN; HBG057100; -.
DR   InParanoid; Q99N13; -.
DR   OrthoDB; EOG7RFTH5; -.
DR   PhylomeDB; Q99N13; -.
DR   TreeFam; TF106174; -.
DR   EvolutionaryTrace; Q99N13; -.
DR   NextBio; 349885; -.
DR   PRO; PR:Q99N13; -.
DR   Proteomes; UP000000589; Unplaced.
DR   Bgee; Q99N13; -.
DR   CleanEx; MM_HDAC9; -.
DR   GO; GO:0005737; C:cytoplasm; TAS:UniProtKB.
DR   GO; GO:0000118; C:histone deacetylase complex; TAS:UniProtKB.
DR   GO; GO:0035097; C:histone methyltransferase complex; IDA:BHF-UCL.
DR   GO; GO:0005634; C:nucleus; TAS:UniProtKB.
DR   GO; GO:0005667; C:transcription factor complex; ISO:MGI.
DR   GO; GO:0004407; F:histone deacetylase activity; TAS:UniProtKB.
DR   GO; GO:0042826; F:histone deacetylase binding; ISO:MGI.
DR   GO; GO:0033558; F:protein deacetylase activity; ISO:MGI.
DR   GO; GO:0005080; F:protein kinase C binding; ISO:MGI.
DR   GO; GO:0070491; F:repressing transcription factor binding; IPI:BHF-UCL.
DR   GO; GO:0003714; F:transcription corepressor activity; IDA:MGI.
DR   GO; GO:0008134; F:transcription factor binding; TAS:UniProtKB.
DR   GO; GO:0042113; P:B cell activation; TAS:UniProtKB.
DR   GO; GO:0030183; P:B cell differentiation; TAS:UniProtKB.
DR   GO; GO:0032869; P:cellular response to insulin stimulus; ISO:MGI.
DR   GO; GO:0016568; P:chromatin modification; TAS:UniProtKB.
DR   GO; GO:0007507; P:heart development; IGI:MGI.
DR   GO; GO:0016575; P:histone deacetylation; ISO:MGI.
DR   GO; GO:0070932; P:histone H3 deacetylation; ISO:MGI.
DR   GO; GO:0070933; P:histone H4 deacetylation; ISO:MGI.
DR   GO; GO:0006954; P:inflammatory response; TAS:UniProtKB.
DR   GO; GO:0045843; P:negative regulation of striated muscle tissue development; TAS:UniProtKB.
DR   GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:MGI.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; TAS:UniProtKB.
DR   GO; GO:0007399; P:nervous system development; TAS:UniProtKB.
DR   GO; GO:0034983; P:peptidyl-lysine deacetylation; ISO:MGI.
DR   GO; GO:0090050; P:positive regulation of cell migration involved in sprouting angiogenesis; ISO:MGI.
DR   GO; GO:0048742; P:regulation of skeletal muscle fiber development; IGI:MGI.
DR   GO; GO:0051153; P:regulation of striated muscle cell differentiation; IGI:MGI.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
DR   InterPro; IPR000286; His_deacetylse.
DR   InterPro; IPR024643; Hist_deacetylase_Gln_rich_N.
DR   PANTHER; PTHR10625; PTHR10625; 1.
DR   Pfam; PF12203; HDAC4_Gln; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Chromatin regulator;
KW   Complete proteome; Hydrolase; Nucleus; Phosphoprotein;
KW   Reference proteome; Repressor; Transcription;
KW   Transcription regulation; Ubl conjugation.
FT   CHAIN         1    588       Histone deacetylase 9.
FT                                /FTId=PRO_0000114711.
FT   REGION       23     27       Interaction with CTBP1.
FT   REGION      136    154       Interaction with MEF2.
FT   REGION      175    343       Interaction with MAPK10.
FT   REGION      218    261       Interaction with ETV6. {ECO:0000250}.
FT   MOD_RES      22     22       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9UKV0}.
FT   MOD_RES     220    220       Phosphoserine.
FT                                {ECO:0000269|PubMed:11390982,
FT                                ECO:0000269|PubMed:12202037}.
FT   MOD_RES     240    240       Phosphoserine; by DYRK1B.
FT                                {ECO:0000269|PubMed:15546868}.
FT   MOD_RES     450    450       Phosphoserine.
FT                                {ECO:0000269|PubMed:11390982,
FT                                ECO:0000269|PubMed:12202037}.
FT   MOD_RES     552    552       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   VAR_SEQ     177    178       Missing (in isoform 3).
FT                                {ECO:0000303|PubMed:11022042}.
FT                                /FTId=VSP_029173.
FT   VAR_SEQ     219    262       Missing (in isoform 2).
FT                                {ECO:0000303|Ref.2}.
FT                                /FTId=VSP_023769.
FT   MUTAGEN      25     26       DL->AS: Abolishes binding to CTBP1 and
FT                                impairs function in transcription
FT                                repression.
FT                                {ECO:0000269|PubMed:11022042}.
FT   CONFLICT    120    120       R -> K (in Ref. 2; AAK15027/AAL86358).
FT                                {ECO:0000305}.
FT   CONFLICT    136    136       R -> K (in Ref. 2; AAK15027/AAL86358).
FT                                {ECO:0000305}.
FT   CONFLICT    388    388       N -> T (in Ref. 3; AAH98187).
FT                                {ECO:0000305}.
FT   CONFLICT    523    523       N -> T (in Ref. 1; AAG48332).
FT                                {ECO:0000305}.
FT   HELIX       143    153       {ECO:0000244|PDB:1TQE}.
SQ   SEQUENCE   588 AA;  65687 MW;  4ED7FA9F02BD4621 CRC64;
     MHSMISSVDV KSEVPMGLEP ISPLDLRTDL RMMMPVVDPV VREKQLQQEL LLIQQQQQIQ
     KQLLIAEFQK QHENLTRQHQ AQLQEHIKEL LAIKQQQELL EKEQKLEQQR QEQEVERHRR
     EQQLPPLRGK DRGRERAVAS TEVKQKLQEF LLSKSATKDT PTNGKNHSVG RHPKLWYTAA
     HHTSLDQSSP PLSGTSPSYK YTLPGAQDSK DDFPLRKTAS EPNLKVRSRL KQKVAERRSS
     PLLRRKDGNL VTSFKKRVFE VAESSVSSSS PGSGPSSPNN GPAGNVTENE ASALPPTPHP
     EQLVPQQRIL IHEDSMNLLS LYTSPSLPNI TLGLPAVPSP LNASNSLKDK QKCETQMLRQ
     GVPLPSQYGS SIAASSSHVH VAMEGKPNSS HQALLQHLLL KEQMRQQKLL VAGGVPLHPQ
     SPLATKERIS PGIRGTHKLP RHRPLNRTQS APLPQSTLAQ LVIQQQHQQF LEKQKQYQQQ
     IHMNKLLSKS IEQLKQPGSH LEEAEEELQG DQSMEDRAAS KDNSARSDSS ACVEDTLGQV
     GAVKVKEEPV DSDEDAQIQE MECGEQAAFM QQVIGKDLAP GFVIKVII
//
ID   HDAC7_MOUSE             Reviewed;         938 AA.
AC   Q8C2B3; Q8C2C9; Q8C8X4; Q8CB80; Q8CDA3; Q9JL72;
DT   16-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2003, sequence version 2.
DT   11-NOV-2015, entry version 136.
DE   RecName: Full=Histone deacetylase 7;
DE            Short=HD7;
DE            EC=3.5.1.98;
DE   AltName: Full=Histone deacetylase 7A;
DE            Short=HD7a;
GN   Name=Hdac7; Synonyms=Hdac7a;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR
RP   LOCATION, TISSUE SPECIFICITY, AND INTERACTION WITH NCOR2 AND SIN3A.
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RX   PubMed=10640276;
RA   Kao H.-Y., Downes M., Ordentlich P., Evans R.M.;
RT   "Isolation of a novel histone deacetylase reveals that class I and
RT   class II deacetylases promote SMRT-mediated repression.";
RL   Genes Dev. 14:55-66(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3; 4; 5 AND 6).
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Bone, Retina, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   INTERACTION WITH HDAC1; HDAC2; HDAC3; HDAC4; HDAC5; NCOR1; NCOR2;
RP   SIN3A; SIN3B; RBBP4; RBBP7; MTA1L1; SAP30 AND MBD3, AND MUTAGENESIS OF
RP   HIS-657; ASP-692; ASP-694 AND HIS-717.
RX   PubMed=10984530; DOI=10.1073/pnas.97.19.10330;
RA   Downes M., Ordentlich P., Kao H.-Y., Alvarez J.G.A., Evans R.M.;
RT   "Identification of a nuclear domain with deacetylase activity.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:10330-10335(2000).
RN   [5]
RP   SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH MEF2C, AND
RP   MUTAGENESIS OF HIS-657.
RX   PubMed=11279209; DOI=10.1074/jbc.M101508200;
RA   Dressel U., Bailey P.J., Wang S.-C.M., Downes M., Evans R.M.,
RA   Muscat G.E.O.;
RT   "A dynamic role for HDAC7 in MEF2-mediated muscle differentiation.";
RL   J. Biol. Chem. 276:17007-17013(2001).
RN   [6]
RP   SUBCELLULAR LOCATION, PHOSPHORYLATION, INTERACTION WITH YWHAE; MEF2A;
RP   MEF2B AND MEF2C, AND MUTAGENESIS OF SER-178; SER-344 AND SER-479.
RX   PubMed=11585834; DOI=10.1074/jbc.M107631200;
RA   Kao H.-Y., Verdel A., Tsai C.-C., Simon C., Juguilon H., Khochbin S.;
RT   "Mechanism for nucleocytoplasmic shuttling of histone deacetylase 7.";
RL   J. Biol. Chem. 276:47496-47507(2001).
RN   [7]
RP   NUCLEAR EXPORT SIGNAL.
RX   PubMed=11509672; DOI=10.1128/MCB.21.18.6312-6321.2001;
RA   McKinsey T.A., Zhang C.-L., Olson E.N.;
RT   "Identification of a signal-responsive nuclear export sequence in
RT   class II histone deacetylases.";
RL   Mol. Cell. Biol. 21:6312-6321(2001).
RN   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [9]
RP   PHOSPHORYLATION AT SER-178; SER-344 AND SER-479.
RX   PubMed=18509061; DOI=10.1073/pnas.0802857105;
RA   Wang S., Li X., Parra M., Verdin E., Bassel-Duby R., Olson E.N.;
RT   "Control of endothelial cell proliferation and migration by VEGF
RT   signaling to histone deacetylase 7.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:7738-7743(2008).
RN   [10]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
RN   [11]
RP   INTERACTION WITH FOXP3.
RX   PubMed=19696312; DOI=10.1126/science.1176077;
RA   Pan F., Yu H., Dang E.V., Barbi J., Pan X., Grosso J.F., Jinasena D.,
RA   Sharma S.M., McCadden E.M., Getnet D., Drake C.G., Liu J.O.,
RA   Ostrowski M.C., Pardoll D.M.;
RT   "Eos mediates Foxp3-dependent gene silencing in CD4+ regulatory T
RT   cells.";
RL   Science 325:1142-1146(2009).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-582, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brown adipose tissue, Heart, Kidney, Lung, and Spleen;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and
RT   expression.";
RL   Cell 143:1174-1189(2010).
RN   [13]
RP   INTERACTION WITH ZMYND15.
RX   PubMed=20675388; DOI=10.1074/jbc.M110.116418;
RA   Yan W., Si Y., Slaymaker S., Li J., Zheng H., Young D.L., Aslanian A.,
RA   Saunders L., Verdin E., Charo I.F.;
RT   "Zmynd15 encodes a histone deacetylase-dependent transcriptional
RT   repressor essential for spermiogenesis and male fertility.";
RL   J. Biol. Chem. 285:31418-31426(2010).
CC   -!- FUNCTION: Responsible for the deacetylation of lysine residues on
CC       the N-terminal part of the core histones (H2A, H2B, H3 and H4).
CC       Histone deacetylation gives a tag for epigenetic repression and
CC       plays an important role in transcriptional regulation, cell cycle
CC       progression and developmental events. Histone deacetylases act via
CC       the formation of large multiprotein complexes. Involved in muscle
CC       maturation by repressing transcription of myocyte enhancer factors
CC       such as MEF2A, MEF2B and MEF2C. During muscle differentiation, it
CC       shuttles into the cytoplasm, allowing the expression of myocyte
CC       enhancer factors. Positively regulates the transcriptional
CC       repressor activity of FOXP3 (By similarity).
CC       {ECO:0000250|UniProtKB:Q8WUI4, ECO:0000269|PubMed:10640276}.
CC   -!- CATALYTIC ACTIVITY: Hydrolysis of an N(6)-acetyl-lysine residue of
CC       a histone to yield a deacetylated histone.
CC   -!- SUBUNIT: Interacts with KDM5B (By similarity). Interacts with KAT5
CC       and EDNRA. Interacts with HDAC1, HDAC2, HDAC3, HDAC4, HDAC5,
CC       NCOR1, NCOR2, SIN3A, SIN3B, RBBP4, RBBP7, MTA1L1, SAP30 and MBD3.
CC       Interacts with the 14-3-3 protein YWHAE, MEF2A, MEF2B and MEF2C.
CC       Interacts with ZMYND15. Interacts with PML (By similarity).
CC       Interacts with FOXP3. {ECO:0000250|UniProtKB:Q8WUI4,
CC       ECO:0000269|PubMed:10640276, ECO:0000269|PubMed:10984530,
CC       ECO:0000269|PubMed:11279209, ECO:0000269|PubMed:11585834,
CC       ECO:0000269|PubMed:19696312, ECO:0000269|PubMed:20675388}.
CC   -!- INTERACTION:
CC       P62259:Ywhae; NbExp=6; IntAct=EBI-643830, EBI-356480;
CC   -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=In the nucleus, it
CC       associates with distinct subnuclear dot-like structures. Shuttles
CC       between the nucleus and the cytoplasm. In muscle cells, it
CC       shuttles into the cytoplasm during myocyte differentiation. The
CC       export to cytoplasm depends on the interaction with the 14-3-3
CC       protein YWHAE and is due to its phosphorylation.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=6;
CC       Name=1;
CC         IsoId=Q8C2B3-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8C2B3-2; Sequence=VSP_007432, VSP_007434, VSP_007435;
CC       Name=3;
CC         IsoId=Q8C2B3-3; Sequence=VSP_007432, VSP_007434;
CC       Name=4;
CC         IsoId=Q8C2B3-4; Sequence=VSP_007433, VSP_007434, VSP_007435;
CC       Name=5;
CC         IsoId=Q8C2B3-5; Sequence=VSP_007432;
CC       Name=6;
CC         IsoId=Q8C2B3-6; Sequence=VSP_007433;
CC   -!- TISSUE SPECIFICITY: Highly expressed in heart and lung. Expressed
CC       at intermediate level in muscle. {ECO:0000269|PubMed:10640276,
CC       ECO:0000269|PubMed:11279209}.
CC   -!- DOMAIN: The nuclear export sequence mediates the shuttling between
CC       the nucleus and the cytoplasm. {ECO:0000250}.
CC   -!- PTM: May be phosphorylated by CaMK1. Phosphorylated by the PKC
CC       kinases PKN1 and PKN2, impairing nuclear import. Phosphorylation
CC       at Ser-178 by MARK2, MARK3 and PRKD1 promotes interaction with 14-
CC       3-3 proteins and export from the nucleus. Phosphorylation at Ser-
CC       178 is a prerequisite for phosphorylation at Ser-204 (By
CC       similarity). {ECO:0000250}.
CC   -!- MISCELLANEOUS: Its activity is inhibited by Trichostatin A (TSA),
CC       a known histone deacetylase inhibitor.
CC   -!- SIMILARITY: Belongs to the histone deacetylase family. HD type 2
CC       subfamily. {ECO:0000305}.
CC   -----------------------------------------------------------------------
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DR   EMBL; AF207749; AAF31419.1; -; mRNA.
DR   EMBL; AK030863; BAC27161.1; -; mRNA.
DR   EMBL; AK036586; BAC29493.1; -; mRNA.
DR   EMBL; AK044287; BAC31856.1; -; mRNA.
DR   EMBL; AK088828; BAC40598.1; -; mRNA.
DR   EMBL; AK088945; BAC40666.1; -; mRNA.
DR   EMBL; BC057332; AAH57332.1; -; mRNA.
DR   CCDS; CCDS37188.1; -. [Q8C2B3-1]
DR   CCDS; CCDS57004.1; -. [Q8C2B3-5]
DR   CCDS; CCDS57005.1; -. [Q8C2B3-2]
DR   CCDS; CCDS57006.1; -. [Q8C2B3-3]
DR   CCDS; CCDS57007.1; -. [Q8C2B3-4]
DR   RefSeq; NP_001191204.1; NM_001204275.1. [Q8C2B3-3]
DR   RefSeq; NP_001191205.1; NM_001204276.1. [Q8C2B3-2]
DR   RefSeq; NP_001191206.1; NM_001204277.1. [Q8C2B3-4]
DR   RefSeq; NP_001191207.1; NM_001204278.1. [Q8C2B3-5]
DR   RefSeq; NP_062518.2; NM_019572.3. [Q8C2B3-1]
DR   RefSeq; XP_006521268.1; XM_006521205.2.
DR   RefSeq; XP_006521270.1; XM_006521207.2. [Q8C2B3-3]
DR   RefSeq; XP_006521271.1; XM_006521208.2. [Q8C2B3-3]
DR   RefSeq; XP_006521272.1; XM_006521209.2. [Q8C2B3-3]
DR   RefSeq; XP_006521273.1; XM_006521210.1. [Q8C2B3-3]
DR   RefSeq; XP_011244002.1; XM_011245700.1. [Q8C2B3-5]
DR   UniGene; Mm.384027; -.
DR   ProteinModelPortal; Q8C2B3; -.
DR   SMR; Q8C2B3; 507-887.
DR   BioGrid; 207862; 5.
DR   DIP; DIP-42594N; -.
DR   IntAct; Q8C2B3; 4.
DR   MINT; MINT-1551781; -.
DR   STRING; 10090.ENSMUSP00000112110; -.
DR   PhosphoSite; Q8C2B3; -.
DR   MaxQB; Q8C2B3; -.
DR   PaxDb; Q8C2B3; -.
DR   PRIDE; Q8C2B3; -.
DR   Ensembl; ENSMUST00000079838; ENSMUSP00000078766; ENSMUSG00000022475. [Q8C2B3-4]
DR   Ensembl; ENSMUST00000088402; ENSMUSP00000085744; ENSMUSG00000022475. [Q8C2B3-1]
DR   Ensembl; ENSMUST00000116408; ENSMUSP00000112109; ENSMUSG00000022475. [Q8C2B3-5]
DR   Ensembl; ENSMUST00000116409; ENSMUSP00000112110; ENSMUSG00000022475. [Q8C2B3-3]
DR   Ensembl; ENSMUST00000118294; ENSMUSP00000113380; ENSMUSG00000022475. [Q8C2B3-2]
DR   GeneID; 56233; -.
DR   KEGG; mmu:56233; -.
DR   UCSC; uc007xle.2; mouse. [Q8C2B3-1]
DR   UCSC; uc007xlf.2; mouse. [Q8C2B3-2]
DR   UCSC; uc007xlg.2; mouse. [Q8C2B3-4]
DR   UCSC; uc007xlh.2; mouse. [Q8C2B3-3]
DR   CTD; 51564; -.
DR   MGI; MGI:1891835; Hdac7.
DR   eggNOG; KOG1343; Eukaryota.
DR   eggNOG; COG0123; LUCA.
DR   GeneTree; ENSGT00530000062809; -.
DR   HOGENOM; HOG000232065; -.
DR   HOVERGEN; HBG057100; -.
DR   InParanoid; Q8C2B3; -.
DR   KO; K11408; -.
DR   OMA; AFRIVVM; -.
DR   OrthoDB; EOG7RFTH5; -.
DR   PhylomeDB; Q8C2B3; -.
DR   TreeFam; TF106173; -.
DR   Reactome; R-MMU-2122947; NOTCH1 Intracellular Domain Regulates Transcription.
DR   Reactome; R-MMU-3108214; SUMOylation of DNA damage response and repair proteins.
DR   ChiTaRS; Hdac7; mouse.
DR   NextBio; 312136; -.
DR   PMAP-CutDB; Q8C2B3; -.
DR   PRO; PR:Q8C2B3; -.
DR   Proteomes; UP000000589; Chromosome 15.
DR   Bgee; Q8C2B3; -.
DR   CleanEx; MM_HDAC7; -.
DR   ExpressionAtlas; Q8C2B3; baseline and differential.
DR   Genevisible; Q8C2B3; MM.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0000118; C:histone deacetylase complex; TAS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0071889; F:14-3-3 protein binding; ISS:UniProtKB.
DR   GO; GO:0033613; F:activating transcription factor binding; ISO:MGI.
DR   GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR   GO; GO:0004407; F:histone deacetylase activity; TAS:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0032041; F:NAD-dependent histone deacetylase activity (H3-K14 specific); IEA:UniProtKB-EC.
DR   GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR   GO; GO:0005080; F:protein kinase C binding; ISO:MGI.
DR   GO; GO:0070491; F:repressing transcription factor binding; ISO:MGI.
DR   GO; GO:0003714; F:transcription corepressor activity; IDA:MGI.
DR   GO; GO:0008134; F:transcription factor binding; TAS:UniProtKB.
DR   GO; GO:0042113; P:B cell activation; TAS:UniProtKB.
DR   GO; GO:0030183; P:B cell differentiation; TAS:UniProtKB.
DR   GO; GO:0007043; P:cell-cell junction assembly; IMP:MGI.
DR   GO; GO:0016568; P:chromatin modification; TAS:UniProtKB.
DR   GO; GO:0016575; P:histone deacetylation; TAS:GOC.
DR   GO; GO:0006954; P:inflammatory response; TAS:UniProtKB.
DR   GO; GO:0032703; P:negative regulation of interleukin-2 production; ISO:MGI.
DR   GO; GO:1901223; P:negative regulation of NIK/NF-kappaB signaling; ISO:MGI.
DR   GO; GO:0045668; P:negative regulation of osteoblast differentiation; ISO:MGI.
DR   GO; GO:0045843; P:negative regulation of striated muscle tissue development; TAS:UniProtKB.
DR   GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:MGI.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; TAS:UniProtKB.
DR   GO; GO:0007399; P:nervous system development; TAS:UniProtKB.
DR   GO; GO:0090050; P:positive regulation of cell migration involved in sprouting angiogenesis; ISO:MGI.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
DR   GO; GO:0001570; P:vasculogenesis; IMP:MGI.
DR   Gene3D; 3.40.800.20; -; 1.
DR   InterPro; IPR000286; His_deacetylse.
DR   InterPro; IPR023801; His_deacetylse_dom.
DR   PANTHER; PTHR10625; PTHR10625; 2.
DR   Pfam; PF00850; Hist_deacetyl; 1.
DR   PRINTS; PR01270; HDASUPER.
PE   1: Evidence at protein level;
KW   Alternative splicing; Chromatin regulator; Complete proteome;
KW   Cytoplasm; Hydrolase; Metal-binding; Nucleus; Phosphoprotein;
KW   Reference proteome; Repeat; Repressor; Transcription;
KW   Transcription regulation; Zinc.
FT   CHAIN         1    938       Histone deacetylase 7.
FT                                /FTId=PRO_0000114706.
FT   REGION        1    121       Interaction with MEF2C.
FT   REGION        2    254       Transcription repression 1.
FT   REGION       72    172       Interaction with MEF2A.
FT   REGION      241    533       Transcription repression 2.
FT   REGION      505    852       Histone deacetylase.
FT   REGION      864    938       Interaction with SIN3A.
FT   MOTIF       904    938       Nuclear export signal. {ECO:0000250}.
FT   COMPBIAS    220    226       Poly-Ser.
FT   ACT_SITE    657    657       {ECO:0000250}.
FT   METAL       520    520       Zinc. {ECO:0000250}.
FT   METAL       522    522       Zinc. {ECO:0000250}.
FT   METAL       528    528       Zinc. {ECO:0000250}.
FT   METAL       605    605       Zinc. {ECO:0000250}.
FT   SITE        830    830       Contributes to catalysis. {ECO:0000250}.
FT   MOD_RES     132    132       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q8WUI4}.
FT   MOD_RES     178    178       Phosphoserine; by MARK2, MARK3 and
FT                                PKD/PRKD1. {ECO:0000305|PubMed:18509061}.
FT   MOD_RES     204    204       Phosphoserine; by PKD/PRKD2.
FT                                {ECO:0000250}.
FT   MOD_RES     344    344       Phosphoserine; by PKD/PRKD1.
FT                                {ECO:0000269|PubMed:18509061}.
FT   MOD_RES     350    350       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q8WUI4}.
FT   MOD_RES     479    479       Phosphoserine; by PKD/PRKD1.
FT                                {ECO:0000269|PubMed:18509061}.
FT   MOD_RES     582    582       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   VAR_SEQ       1     22       Missing (in isoform 2, isoform 3 and
FT                                isoform 5).
FT                                {ECO:0000303|PubMed:16141072}.
FT                                /FTId=VSP_007432.
FT   VAR_SEQ     138    161       Missing (in isoform 4 and isoform 6).
FT                                {ECO:0000303|PubMed:16141072}.
FT                                /FTId=VSP_007433.
FT   VAR_SEQ     249    249       E -> EALLGQRLRLQETSLAPFALPTVSLLPAITLGLPAP
FT                                AR (in isoform 2, isoform 3 and isoform
FT                                4). {ECO:0000303|PubMed:16141072}.
FT                                /FTId=VSP_007434.
FT   VAR_SEQ     376    382       Missing (in isoform 2 and isoform 4).
FT                                {ECO:0000303|PubMed:16141072}.
FT                                /FTId=VSP_007435.
FT   MUTAGEN     178    178       S->A: Strong reduction of CaMK1-dependent
FT                                nuclear export. Reduces interaction with
FT                                YWHAE. {ECO:0000269|PubMed:11585834}.
FT   MUTAGEN     344    344       S->A: Strong reduction of CaMK1-dependent
FT                                nuclear export. Reduces interaction with
FT                                YWHAE. {ECO:0000269|PubMed:11585834}.
FT   MUTAGEN     479    479       S->A: Strong reduction of CaMK1-dependent
FT                                nuclear export. Reduces interaction with
FT                                YWHAE. {ECO:0000269|PubMed:11585834}.
FT   MUTAGEN     657    657       H->A: Abolishes deacetylase activity, but
FT                                not the interaction with HDAC2 and HDAC3.
FT                                {ECO:0000269|PubMed:10984530,
FT                                ECO:0000269|PubMed:11279209}.
FT   MUTAGEN     692    692       D->A: Disrupts the dot-like nuclear
FT                                pattern. {ECO:0000269|PubMed:10984530}.
FT   MUTAGEN     694    694       D->A: Disrupts the dot-like nuclear
FT                                pattern. Abolishes deacetylase activity,
FT                                but not the interaction with HDAC2 and
FT                                HDAC3. {ECO:0000269|PubMed:10984530}.
FT   MUTAGEN     717    717       H->A: Abolishes deacetylase activity, but
FT                                not the interaction with HDAC2 and HDAC3.
FT                                {ECO:0000269|PubMed:10984530}.
FT   CONFLICT    169    169       E -> G (in Ref. 2; BAC27161).
FT                                {ECO:0000305}.
FT   CONFLICT    183    183       K -> M (in Ref. 2; BAC29493).
FT                                {ECO:0000305}.
FT   CONFLICT    228    228       P -> T (in Ref. 2; BAC27161).
FT                                {ECO:0000305}.
FT   CONFLICT    487    487       L -> M (in Ref. 1; AAF31419 and 2;
FT                                BAC40598/BAC40666). {ECO:0000305}.
FT   CONFLICT    645    645       K -> R (in Ref. 2; BAC29493).
FT                                {ECO:0000305}.
FT   CONFLICT    661    661       S -> P (in Ref. 2; BAC40598).
FT                                {ECO:0000305}.
FT   CONFLICT    737    737       G -> A (in Ref. 1; AAF31419).
FT                                {ECO:0000305}.
SQ   SEQUENCE   938 AA;  101287 MW;  8D4B455CE6F95483 CRC64;
     MHSPGAGCPA LQPDTPGSQP QPMDLRVGQR PTVEPPPEPA LLTLQHPQRL HRHLFLAGLH
     QQQRSAEPMR LSMDPPMPEL QGGQQEQELR QLLNKDKSKR SAVASSVVKQ KLAEVILKKQ
     QAALERTVHP SSPSIPYRTL EPLDTEGAAR SVLSSFLPPV PSLPTEPPEH FPLRKTVSEP
     NLKLRYKPKK SLERRKNPLL RKESAPPSLR RRPAETLGDS SPSSSSTPAS GCSSPNDSEH
     GPNPALGSEA DGDRRTHSTL GPRGPVLGNP HAPLFLHHGL EPEAGGTLPS RLQPILLLDP
     SVSHAPLWTV PGLGPLPFHF AQPLLTTERL SGSGLHRPLN RTRSEPLPPS ATASPLLAPL
     QPRQDRLKPH VQLIKPAISP PQRPAKPSEK PRLRQIPSAE DLETDGGGVG PMANDGLEHR
     ESGRGPPEGR GSISLQQHQQ VPPWEQQHLA GRLSQGSPGD SVLIPLAQVG HRPLSRTQSS
     PAAPVSLLSP EPTCQTQVLN SSETPATGLV YDSVMLKHQC SCGDNSKHPE HAGRIQSIWS
     RLQERGLRSQ CECLRGRKAS LEELQSVHSE RHVLLYGTNP LSRLKLDNGK LTGLLAQRTF
     VMLPCGGVGV DTDTIWNELH SSNAARWAAG SVTDLAFKVA SRELKNGFAV VRPPGHHADH
     STAMGFCFFN SVAIACRQLQ QHGKASKILI VDWDVHHGNG TQQTFYQDPS VLYISLHRHD
     DGNFFPGSGA VDEVGTGSGE GFNVNVAWAG GLDPPMGDPE YLAAFRIVVM PIAREFAPDL
     VLVSAGFDAA EGHPAPLGGY HVSAKCFGYM TQQLMNLAGG AVVLALEGGH DLTAICDASE
     ACVAALLGNK VDPLSEESWK QKPNLSAIRS LEAVVRVHRK YWGCMQRLAS CPDSWLPRVP
     GADAEVEAVT ALASLSVGIL AEDRPSERLV EEEEPMNL
//
ID   HIC1_HUMAN              Reviewed;         733 AA.
AC   Q14526; D3DTI4;
DT   02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 5.
DT   11-NOV-2015, entry version 147.
DE   RecName: Full=Hypermethylated in cancer 1 protein;
DE            Short=Hic-1;
DE   AltName: Full=Zinc finger and BTB domain-containing protein 29;
GN   Name=HIC1; Synonyms=ZBTB29;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 2), AND VARIANT GLY-725.
RX   PubMed=7585125; DOI=10.1038/nm0695-570;
RA   Wales M.M., Biel M.A., el Deiry W., Nelkin B.D., Issa J.-P.,
RA   Cavenee W.K., Kuerbitz S.J., Baylin S.B.;
RT   "p53 activates expression of HIC-1, a new candidate tumour suppressor
RT   gene on 17p13.3.";
RL   Nat. Med. 1:570-577(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16625196; DOI=10.1038/nature04689;
RA   Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA   Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA   Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA   Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA   DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R.,
RA   Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
RA   Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
RA   Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
RA   Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
RA   Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
RA   Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
RA   Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA   Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA   Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT   "DNA sequence of human chromosome 17 and analysis of rearrangement in
RT   the human lineage.";
RL   Nature 440:1045-1049(2006).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   SELF-ASSOCIATION.
RX   PubMed=10611298; DOI=10.1073/pnas.96.26.14831;
RA   Deltour S., Guerardel C., Leprince D.;
RT   "Recruitment of SMRT/N-CoR-mSin3A-HDAC-repressing complexes is not a
RT   general mechanism for BTB/POZ transcriptional repressors: the case of
RT   HIC-1 and gammaFBP-B.";
RL   Proc. Natl. Acad. Sci. U.S.A. 96:14831-14836(1999).
RN   [5]
RP   ALTERNATIVE SPLICING, INTERACTION WITH HIC2, AND SUBCELLULAR LOCATION.
RX   PubMed=11554746; DOI=10.1006/bbrc.2001.5624;
RA   Deltour S., Pinte S., Guerardel C., Leprince D.;
RT   "Characterization of HRG22, a human homologue of the putative tumor
RT   suppressor gene HIC1.";
RL   Biochem. Biophys. Res. Commun. 287:427-434(2001).
RN   [6]
RP   FUNCTION, SELF-ASSOCIATION, AND INTERACTION WITH CTBP1.
RX   PubMed=12052894; DOI=10.1128/MCB.22.13.4890-4901.2002;
RA   Deltour S., Pinte S., Guerardel C., Wasylyk B., Leprince D.;
RT   "The human candidate tumor suppressor gene HIC1 recruits CtBP through
RT   a degenerate GLDLSKK motif.";
RL   Mol. Cell. Biol. 22:4890-4901(2002).
RN   [7]
RP   FUNCTION, DNA-BINDING, AND MUTAGENESIS OF CYS-540.
RX   PubMed=15231840; DOI=10.1074/jbc.M401610200;
RA   Pinte S., Stankovic-Valentin N., Deltour S., Rood B.R., Guerardel C.,
RA   Leprince D.;
RT   "The tumor suppressor gene HIC1 (hypermethylated in cancer 1) is a
RT   sequence-specific transcriptional repressor: definition of its
RT   consensus binding sequence and analysis of its DNA binding and
RT   repressive properties.";
RL   J. Biol. Chem. 279:38313-38324(2004).
RN   [8]
RP   FUNCTION.
RX   PubMed=16269335; DOI=10.1016/j.cell.2005.08.011;
RA   Chen W.Y., Wang D.H., Yen R.C., Luo J., Gu W., Baylin S.B.;
RT   "Tumor suppressor HIC1 directly regulates SIRT1 to modulate p53-
RT   dependent DNA-damage responses.";
RL   Cell 123:437-448(2005).
RN   [9]
RP   FUNCTION.
RX   PubMed=16690027; DOI=10.1016/j.bbrc.2006.04.052;
RA   Briones V.R., Chen S., Riegel A.T., Lechleider R.J.;
RT   "Mechanism of fibroblast growth factor-binding protein 1 repression by
RT   TGF-beta.";
RL   Biochem. Biophys. Res. Commun. 345:595-601(2006).
RN   [10]
RP   FUNCTION IN WNT SIGNALING, AND INTERACTION WITH TCF7L2.
RX   PubMed=16724116; DOI=10.1038/sj.emboj.7601147;
RA   Valenta T., Lukas J., Doubravska L., Fafilek B., Korinek V.;
RT   "HIC1 attenuates Wnt signaling by recruitment of TCF-4 and beta-
RT   catenin to the nuclear bodies.";
RL   EMBO J. 25:2326-2337(2006).
RN   [11]
RP   INTERACTION WITH CTBP1 AND CTBP2, AND MUTAGENESIS OF LEU-244.
RX   PubMed=16762039; DOI=10.1111/j.1742-4658.2006.05301.x;
RA   Stankovic-Valentin N., Verger A., Deltour-Balerdi S., Quinlan K.G.,
RA   Crossley M., Leprince D.;
RT   "A L225A substitution in the human tumour suppressor HIC1 abolishes
RT   its interaction with the corepressor CtBP.";
RL   FEBS J. 273:2879-2890(2006).
RN   [12]
RP   SUMOYLATION AT LYS-333, ACETYLATION AT LYS-333, AND MUTAGENESIS OF
RP   LYS-333; GLU-335 AND PRO-336.
RX   PubMed=17283066; DOI=10.1128/MCB.01098-06;
RA   Stankovic-Valentin N., Deltour S., Seeler J., Pinte S., Vergoten G.,
RA   Guerardel C., Dejean A., Leprince D.;
RT   "An acetylation/deacetylation-SUMOylation switch through a
RT   phylogenetically conserved psiKXEP motif in the tumor suppressor HIC1
RT   regulates transcriptional repression activity.";
RL   Mol. Cell. Biol. 27:2661-2675(2007).
RN   [13]
RP   FUNCTION, AND INTERACTION WITH CTBP1.
RX   PubMed=17213307; DOI=10.1073/pnas.0610590104;
RA   Zhang Q., Wang S.Y., Fleuriel C., Leprince D., Rocheleau J.V.,
RA   Piston D.W., Goodman R.H.;
RT   "Metabolic regulation of SIRT1 transcription via a HIC1:CtBP
RT   corepressor complex.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:829-833(2007).
RN   [14]
RP   FUNCTION.
RX   PubMed=18347096; DOI=10.1101/gad.1640908;
RA   Briggs K.J., Corcoran-Schwartz I.M., Zhang W., Harcke T.,
RA   Devereux W.L., Baylin S.B., Eberhart C.G., Watkins D.N.;
RT   "Cooperation between the Hic1 and Ptch1 tumor suppressors in
RT   medulloblastoma.";
RL   Genes Dev. 22:770-785(2008).
RN   [15]
RP   ERRATUM.
RA   Briggs K.J., Corcoran-Schwartz I.M., Zhang W., Harcke T.,
RA   Devereux W.L., Baylin S.B., Eberhart C.G., Watkins D.N.;
RL   Genes Dev. 22:1410-1410(2008).
RN   [16]
RP   FUNCTION, AND INTERACTION WITH ARID1A.
RX   PubMed=19486893; DOI=10.1016/j.bbrc.2009.05.115;
RA   Van Rechem C., Boulay G., Leprince D.;
RT   "HIC1 interacts with a specific subunit of SWI/SNF complexes,
RT   ARID1A/BAF250A.";
RL   Biochem. Biophys. Res. Commun. 385:586-590(2009).
RN   [17]
RP   FUNCTION.
RX   PubMed=19525223; DOI=10.1074/jbc.M109.022350;
RA   Van Rechem C., Rood B.R., Touka M., Pinte S., Jenal M., Guerardel C.,
RA   Ramsey K., Monte D., Begue A., Tschan M.P., Stephan D.A., Leprince D.;
RT   "Scavenger chemokine (CXC motif) receptor 7 (CXCR7) is a direct target
RT   gene of HIC1 (hypermethylated in cancer 1).";
RL   J. Biol. Chem. 284:20927-20935(2009).
RN   [18]
RP   FUNCTION, INTERACTION WITH MTA1 AND MBD3, AND MUTAGENESIS OF LYS-333;
RP   GLU-335 AND PRO-336.
RX   PubMed=20547755; DOI=10.1128/MCB.00582-09;
RA   Van Rechem C., Boulay G., Pinte S., Stankovic-Valentin N.,
RA   Guerardel C., Leprince D.;
RT   "Differential regulation of HIC1 target genes by CtBP and NuRD, via an
RT   acetylation/SUMOylation switch, in quiescent versus proliferating
RT   cells.";
RL   Mol. Cell. Biol. 30:4045-4059(2010).
RN   [19]
RP   FUNCTION.
RX   PubMed=20154726; DOI=10.1038/onc.2010.12;
RA   Zhang W., Zeng X., Briggs K.J., Beaty R., Simons B., Chiu Yen R.W.,
RA   Tyler M.A., Tsai H.C., Ye Y., Gesell G.S., Herman J.G., Baylin S.B.,
RA   Watkins D.N.;
RT   "A potential tumor suppressor role for Hic1 in breast cancer through
RT   transcriptional repression of ephrin-A1.";
RL   Oncogene 29:2467-2476(2010).
RN   [20]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-237; SER-248 AND
RP   SER-366, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
RA   Wang L., Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human
RT   liver phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
CC   -!- FUNCTION: Transcriptional repressor. Recognizes and binds to the
CC       consensus sequence '5-[CG]NG[CG]GGGCA[CA]CC-3'. May act as a tumor
CC       suppressor. May be involved in development of head, face, limbs
CC       and ventral body wall. Involved in down-regulation of SIRT1 and
CC       thereby is involved in regulation of p53/TP53-dependent apoptotic
CC       DNA-damage responses. The specific target gene promoter
CC       association seems to be depend on corepressors, such as CTBP1 or
CC       CTBP2 and MTA1. The regulation of SIRT1 transcription in response
CC       to nutrient deprivation seems to involve CTBP1. In cooperation
CC       with MTA1 (indicative for an association with the NuRD complex)
CC       represses transcription from CCND1/cyclin-D1 and CDKN1C/p57Kip2
CC       specifically in quiescent cells. Involved in regulation of the Wnt
CC       signaling pathway probably by association with TCF7L2 and
CC       preventing TCF7L2 and CTNNB1 association with promoters of TCF-
CC       responsive genes. Seems to repress transcription from E2F1 and
CC       ATOH1 which involves ARID1A, indicative for the participation of a
CC       distinct SWI/SNF-type chromatin-remodeling complex. Probably
CC       represses transcription from ACKR3, FGFBP1 and EFNA1.
CC       {ECO:0000269|PubMed:12052894, ECO:0000269|PubMed:15231840,
CC       ECO:0000269|PubMed:16269335, ECO:0000269|PubMed:16690027,
CC       ECO:0000269|PubMed:16724116, ECO:0000269|PubMed:17213307,
CC       ECO:0000269|PubMed:18347096, ECO:0000269|PubMed:19486893,
CC       ECO:0000269|PubMed:19525223, ECO:0000269|PubMed:20154726,
CC       ECO:0000269|PubMed:20547755}.
CC   -!- SUBUNIT: Self-associates. Interacts with HIC2. Interacts with
CC       CTBP1 and CTBP2. Interacts with TCF7L2 and ARID1A. Interacts with
CC       MTA1 and MBD3; indicative for an association with the NuRD
CC       complex. {ECO:0000269|PubMed:11554746,
CC       ECO:0000269|PubMed:12052894, ECO:0000269|PubMed:16724116,
CC       ECO:0000269|PubMed:16762039, ECO:0000269|PubMed:17213307,
CC       ECO:0000269|PubMed:19486893, ECO:0000269|PubMed:20547755}.
CC   -!- INTERACTION:
CC       O14497:ARID1A; NbExp=2; IntAct=EBI-2507362, EBI-637887;
CC       Q13363:CTBP1; NbExp=4; IntAct=EBI-2507362, EBI-908846;
CC       O88712:Ctbp1 (xeno); NbExp=10; IntAct=EBI-2507362, EBI-604547;
CC       P56545:CTBP2; NbExp=2; IntAct=EBI-2507362, EBI-741533;
CC       P56546:Ctbp2 (xeno); NbExp=2; IntAct=EBI-2507362, EBI-1384883;
CC       Q9NQB0:TCF7L2; NbExp=6; IntAct=EBI-2507362, EBI-924724;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11554746}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC         Comment=Additional isoforms seem to exist.;
CC       Name=1;
CC         IsoId=Q14526-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q14526-2; Sequence=VSP_006826;
CC   -!- TISSUE SPECIFICITY: Ubiquitously expressed with highest levels
CC       found in lung, colon, prostate, thymus, testis and ovary.
CC       Expression is absent or decreased in many tumor cells.
CC   -!- DOMAIN: The BTB domain inhibits the binding to a single consensus
CC       binding site, but mediates cooperative binding to multiple binding
CC       sites.
CC   -!- PTM: Acetylated on several residues, including Lys-333. Lys-333 is
CC       deacetylated by SIRT1. {ECO:0000269|PubMed:17283066}.
CC   -!- PTM: Sumoylated on Lys-333 by a PIAS family member, which enhances
CC       interaction with MTA1, positively regulates transcriptional
CC       repression activity and is enhanced by HDAC4.
CC       {ECO:0000269|PubMed:17283066}.
CC   -!- MISCELLANEOUS: The HIC1 gene is frequently found epigenetically
CC       silenced or deleted in different types of solid tumors.
CC   -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC       family. Hic subfamily. {ECO:0000305}.
CC   -!- SIMILARITY: Contains 1 BTB (POZ) domain. {ECO:0000255|PROSITE-
CC       ProRule:PRU00037}.
CC   -!- SIMILARITY: Contains 5 C2H2-type zinc fingers.
CC       {ECO:0000255|PROSITE-ProRule:PRU00042}.
CC   -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC       and Haematology;
CC       URL="http://atlasgeneticsoncology.org/Genes/HIC1ID40819ch17p13.html";
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DR   EMBL; L41919; AAD09201.1; -; Genomic_DNA.
DR   EMBL; AC090617; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471108; EAW90562.1; -; Genomic_DNA.
DR   EMBL; CH471108; EAW90563.1; -; Genomic_DNA.
DR   CCDS; CCDS42229.1; -. [Q14526-1]
DR   CCDS; CCDS42230.1; -. [Q14526-2]
DR   RefSeq; NP_001091672.1; NM_001098202.1. [Q14526-1]
DR   RefSeq; NP_006488.2; NM_006497.3. [Q14526-2]
DR   UniGene; Hs.695682; -.
DR   UniGene; Hs.72956; -.
DR   ProteinModelPortal; Q14526; -.
DR   SMR; Q14526; 25-145, 429-613.
DR   BioGrid; 109337; 26.
DR   IntAct; Q14526; 11.
DR   MINT; MINT-2730619; -.
DR   STRING; 9606.ENSP00000314080; -.
DR   PhosphoSite; Q14526; -.
DR   BioMuta; HIC1; -.
DR   DMDM; 296439502; -.
DR   PaxDb; Q14526; -.
DR   PRIDE; Q14526; -.
DR   DNASU; 3090; -.
DR   Ensembl; ENST00000322941; ENSP00000314080; ENSG00000177374. [Q14526-1]
DR   Ensembl; ENST00000399849; ENSP00000382742; ENSG00000177374. [Q14526-2]
DR   Ensembl; ENST00000619757; ENSP00000477858; ENSG00000177374. [Q14526-2]
DR   GeneID; 3090; -.
DR   KEGG; hsa:3090; -.
DR   UCSC; uc002fty.4; human. [Q14526-1]
DR   CTD; 3090; -.
DR   GeneCards; HIC1; -.
DR   H-InvDB; HIX0039113; -.
DR   HGNC; HGNC:4909; HIC1.
DR   HPA; HPA043372; -.
DR   MIM; 603825; gene.
DR   neXtProt; NX_Q14526; -.
DR   Orphanet; 531; Miller-Dieker syndrome.
DR   PharmGKB; PA29282; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   eggNOG; COG5048; LUCA.
DR   GeneTree; ENSGT00800000124025; -.
DR   HOGENOM; HOG000026793; -.
DR   HOVERGEN; HBG031606; -.
DR   InParanoid; Q14526; -.
DR   OMA; PPDPFRG; -.
DR   OrthoDB; EOG74J97F; -.
DR   PhylomeDB; Q14526; -.
DR   TreeFam; TF333488; -.
DR   SignaLink; Q14526; -.
DR   GeneWiki; HIC1; -.
DR   GenomeRNAi; 3090; -.
DR   NextBio; 12259; -.
DR   PRO; PR:Q14526; -.
DR   Proteomes; UP000005640; Chromosome 17.
DR   Bgee; Q14526; -.
DR   CleanEx; HS_HIC1; -.
DR   ExpressionAtlas; Q14526; baseline and differential.
DR   Genevisible; Q14526; HS.
DR   GO; GO:0000785; C:chromatin; ISS:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; IDA:HPA.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0042826; F:histone deacetylase binding; IDA:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
DR   GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IDA:UniProtKB.
DR   GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; IDA:UniProtKB.
DR   GO; GO:0007275; P:multicellular organismal development; IEA:UniProtKB-KW.
DR   GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
DR   GO; GO:0030178; P:negative regulation of Wnt signaling pathway; IDA:UniProtKB.
DR   GO; GO:0043517; P:positive regulation of DNA damage response, signal transduction by p53 class mediator; ISS:UniProtKB.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; TAS:UniProtKB.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
DR   GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.160.60; -; 4.
DR   InterPro; IPR000210; BTB/POZ_dom.
DR   InterPro; IPR028424; HIC1.
DR   InterPro; IPR011333; POZ_dom.
DR   InterPro; IPR007087; Znf_C2H2.
DR   InterPro; IPR015880; Znf_C2H2-like.
DR   InterPro; IPR013087; Znf_C2H2/integrase_DNA-bd.
DR   PANTHER; PTHR24409:SF69; PTHR24409:SF69; 1.
DR   Pfam; PF00651; BTB; 1.
DR   Pfam; PF00096; zf-C2H2; 1.
DR   SMART; SM00225; BTB; 1.
DR   SMART; SM00355; ZnF_C2H2; 5.
DR   SUPFAM; SSF54695; SSF54695; 1.
DR   PROSITE; PS50097; BTB; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 5.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 5.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Complete proteome;
KW   Developmental protein; DNA-binding; Isopeptide bond; Metal-binding;
KW   Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repeat;
KW   Repressor; Transcription; Transcription regulation; Tumor suppressor;
KW   Ubl conjugation; Wnt signaling pathway; Zinc; Zinc-finger.
FT   CHAIN         1    733       Hypermethylated in cancer 1 protein.
FT                                /FTId=PRO_0000046942.
FT   DOMAIN       47    110       BTB. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00037}.
FT   ZN_FING     439    459       C2H2-type 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     509    529       C2H2-type 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     537    557       C2H2-type 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     565    585       C2H2-type 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     593    613       C2H2-type 5. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   REGION      154    315       Mediates HDAC-dependent transcriptional
FT                                repression.
FT   REGION      241    247       Interaction with CTBP1.
FT   COMPBIAS    110    119       Poly-Ala.
FT   COMPBIAS    160    167       Poly-Gly.
FT   COMPBIAS    195    199       Poly-Pro.
FT   MOD_RES     237    237       Phosphoserine.
FT                                {ECO:0000244|PubMed:24275569}.
FT   MOD_RES     248    248       Phosphoserine.
FT                                {ECO:0000244|PubMed:24275569}.
FT   MOD_RES     333    333       N6-acetyllysine; alternate.
FT                                {ECO:0000269|PubMed:17283066}.
FT   MOD_RES     366    366       Phosphoserine.
FT                                {ECO:0000244|PubMed:24275569}.
FT   MOD_RES     704    704       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9R1Y5}.
FT   CROSSLNK    333    333       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO);
FT                                alternate.
FT   VAR_SEQ       1     19       Missing (in isoform 2). {ECO:0000305}.
FT                                /FTId=VSP_006826.
FT   VARIANT     725    725       R -> G (in dbSNP:rs1063317).
FT                                {ECO:0000269|PubMed:7585125}.
FT                                /FTId=VAR_063109.
FT   MUTAGEN     244    244       L->A: Abolishes interaction with CTBP1
FT                                and CTBP2. Impairs transcriptional
FT                                repression.
FT                                {ECO:0000269|PubMed:16762039}.
FT   MUTAGEN     333    333       K->Q: Mimicks acetylation. Impairs
FT                                interaction with RBBP4 and MTA1 and no
FT                                effect on interaction with CTBP2. Reduces
FT                                transcriptional repression.
FT                                {ECO:0000269|PubMed:17283066,
FT                                ECO:0000269|PubMed:20547755}.
FT   MUTAGEN     333    333       K->R: Abolishes sumoylation; impairs
FT                                transcriptional repression activity.
FT                                {ECO:0000269|PubMed:17283066,
FT                                ECO:0000269|PubMed:20547755}.
FT   MUTAGEN     335    335       E->A: Impairs transcriptional repression
FT                                activity. Decreases interaction with
FT                                MTA1. {ECO:0000269|PubMed:17283066,
FT                                ECO:0000269|PubMed:20547755}.
FT   MUTAGEN     336    336       P->A: Impairs K-333 acetylation; no
FT                                effect on sumoylation. Decreases
FT                                interaction with MTA1.
FT                                {ECO:0000269|PubMed:17283066,
FT                                ECO:0000269|PubMed:20547755}.
FT   MUTAGEN     540    540       C->S: Abolishes repression activity.
FT                                {ECO:0000269|PubMed:15231840}.
FT   CONFLICT    190    190       P -> R (in Ref. 1; AAD09201).
FT                                {ECO:0000305}.
SQ   SEQUENCE   733 AA;  76508 MW;  6DDD0F49C4E490D3 CRC64;
     MTFPEADILL KSGECAGQTM LDTMEAPGHS RQLLLQLNNQ RTKGFLCDVI IVVQNALFRA
     HKNVLAASSA YLKSLVVHDN LLNLDHDMVS PAVFRLVLDF IYTGRLADGA EAAAAAAVAP
     GAEPSLGAVL AAASYLQIPD LVALCKKRLK RHGKYCHLRG GGGGGGGYAP YGRPGRGLRA
     ATPVIQACYP SPVGPPPPPA AEPPSGPEAA VNTHCAELYA SGPGPAAALC ASERRCSPLC
     GLDLSKKSPP GSAAPERPLA ERELPPRPDS PPSAGPAAYK EPPLALPSLP PLPFQKLEEA
     APPSDPFRGG SGSPGPEPPG RPDGPSLLYR WMKHEPGLGS YGDELGRERG SPSERCEERG
     GDAAVSPGGP PLGLAPPPRY PGSLDGPGAG GDGDDYKSSS EETGSSEDPS PPGGHLEGYP
     CPHLAYGEPE SFGDNLYVCI PCGKGFPSSE QLNAHVEAHV EEEEALYGRA EAAEVAAGAA
     GLGPPFGGGG DKVAGAPGGL GELLRPYRCA SCDKSYKDPA TLRQHEKTHW LTRPYPCTIC
     GKKFTQRGTM TRHMRSHLGL KPFACDACGM RFTRQYRLTE HMRIHSGEKP YECQVCGGKF
     AQQRNLISHM KMHAVGGAAG AAGALAGLGG LPGVPGPDGK GKLDFPEGVF AVARLTAEQL
     SLKQQDKAAA AELLAQTTHF LHDPKVALES LYPLAKFTAE LGLSPDKAAE VLSQGAHLAA
     GPDGRTIDRF SPT
//
ID   IKZF1_HUMAN             Reviewed;         519 AA.
AC   Q13422; A4D260; B4E0Z1; D3DVM5; O00598; Q53XL2; Q69BM4; Q8WVA3;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   11-NOV-2015, entry version 150.
DE   RecName: Full=DNA-binding protein Ikaros;
DE   AltName: Full=Ikaros family zinc finger protein 1;
DE   AltName: Full=Lymphoid transcription factor LyF-1;
GN   Name=IKZF1; Synonyms=IK1, IKAROS, LYF1, ZNFN1A1;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], ALTERNATIVE SPLICING, AND TISSUE
RP   SPECIFICITY.
RC   TISSUE=Bone marrow;
RX   PubMed=8964602; DOI=10.1016/0165-2478(95)02479-4;
RA   Nietfeld W., Meyerhans A.;
RT   "Cloning and sequencing of hIk-1, a cDNA encoding a human homologue of
RT   mouse Ikaros/LyF-1.";
RL   Immunol. Lett. 49:139-141(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], ALTERNATIVE SPLICING, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=8543809;
RA   Molnar A., Wu P., Largespada D.A., Vortkamp A., Scherer S.,
RA   Copeland N.G., Jenkins N.A., Bruns G., Georgopoulos K.;
RT   "The Ikaros gene encodes a family of lymphocyte-restricted zinc finger
RT   DNA binding proteins, highly conserved in human and mouse.";
RL   J. Immunol. 156:585-592(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM IKX).
RA   Sanchez-Tapia E.M., Rodriguez R.E., Gonzalez-Sarmiento R.;
RT   "Molecular misreading is involved in generation of Ikaros diversity.";
RL   Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM IK2).
RC   TISSUE=Thymus;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM IK7).
RA   Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA   Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA   Phelan M., Farmer A.;
RT   "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT   vector.";
RL   Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12853948; DOI=10.1038/nature01782;
RA   Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA   Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R.,
RA   Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E.,
RA   Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H.,
RA   Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A.,
RA   Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J.,
RA   Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A.,
RA   Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S.,
RA   Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M.,
RA   Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C.,
RA   Latreille P., Miller N., Johnson D., Murray J., Woessner J.P.,
RA   Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J.,
RA   Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L.,
RA   Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R.,
RA   Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA   Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K.,
RA   Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S.,
RA   Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M.,
RA   Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R.,
RA   Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D.,
RA   Waterston R.H., Wilson R.K.;
RT   "The DNA sequence of human chromosome 7.";
RL   Nature 424:157-164(2003).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12690205; DOI=10.1126/science.1083423;
RA   Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA   Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA   Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA   Kanematsu E., Gentles S., Christopoulos C.C., Choufani S.,
RA   Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z.,
RA   Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C.,
RA   Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J.,
RA   Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F.,
RA   Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F.,
RA   Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H.,
RA   Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G.,
RA   Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P.,
RA   Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J.,
RA   Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F.,
RA   Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B.,
RA   Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA   Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W.,
RA   Mural R.J., Adams M.D., Tsui L.-C.;
RT   "Human chromosome 7: DNA sequence and biology.";
RL   Science 300:767-772(2003).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [9]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM IK7).
RC   TISSUE=Lymph;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [10]
RP   IDENTIFICATION IN THE NURD COMPLEX, IDENTIFICATION IN THE BAF COMPLEX,
RP   INTERACTION WITH SMARCA4 AND CHD4, AND FUNCTION.
RX   PubMed=10204490; DOI=10.1016/S1074-7613(00)80034-5;
RA   Kim J., Sif S., Jones B., Jackson A., Koipally J., Heller E.,
RA   Winandy S., Viel A., Sawyer A., Ikeda T., Kingston R.,
RA   Georgopoulos K.;
RT   "Ikaros DNA-binding proteins direct formation of chromatin remodeling
RT   complexes in lymphocytes.";
RL   Immunity 10:345-355(1999).
RN   [11]
RP   INVOLVEMENT IN B-CELL NON-HODGKIN LYMPHOMA, AND CHROMOSOMAL
RP   TRANSLOCATION WITH BCL6.
RX   PubMed=10753856;
RA   Hosokawa Y., Maeda Y., Ichinohasama R., Miura I., Taniwaki M.,
RA   Seto M.;
RT   "The Ikaros gene, a central regulator of lymphoid differentiation,
RT   fuses to the BCL6 gene as a result of t(3;7)(q27;p12) translocation in
RT   a patient with diffuse large B-cell lymphoma.";
RL   Blood 95:2719-2721(2000).
RN   [12]
RP   INTERACTION WITH IKZF4 AND IKZF5.
RX   PubMed=10978333; DOI=10.1074/jbc.M005457200;
RA   Perdomo J., Holmes M., Chong B., Crossley M.;
RT   "Eos and pegasus, two members of the Ikaros family of proteins with
RT   distinct DNA binding activities.";
RL   J. Biol. Chem. 275:38347-38354(2000).
RN   [13]
RP   FUNCTION, ALTERNATIVE SPLICING, SUBCELLULAR LOCATION, AND SUBUNIT.
RX   PubMed=17135265; DOI=10.1074/jbc.M605627200;
RA   Ronni T., Payne K.J., Ho S., Bradley M.N., Dorsam G., Dovat S.;
RT   "Human Ikaros function in activated T cells is regulated by
RT   coordinated expression of its largest isoforms.";
RL   J. Biol. Chem. 282:2538-2547(2007).
RN   [14]
RP   FUNCTION, AND ALTERNATIVE SPLICING.
RX   PubMed=17934067; DOI=10.1182/blood-2007-07-098202;
RA   Dijon M., Bardin F., Murati A., Batoz M., Chabannon C., Tonnelle C.;
RT   "The role of Ikaros in human erythroid differentiation.";
RL   Blood 111:1138-1146(2008).
RN   [15]
RP   FUNCTION IN GAMMA SATELLITE DNA BINDING.
RX   PubMed=19141594; DOI=10.1101/gr.086496.108;
RA   Kim J.-H., Ebersole T., Kouprina N., Noskov V.N., Ohzeki J.-I.,
RA   Masumoto H., Mravinac B., Sullivan B.A., Pavlicek A., Dovat S.,
RA   Pack S.D., Kwon Y.-W., Flanagan P.T., Loukinov D., Lobanenkov V.,
RA   Larionov V.;
RT   "Human gamma-satellite DNA maintains open chromatin structure and
RT   protects a transgene from epigenetic silencing.";
RL   Genome Res. 19:533-544(2009).
RN   [16]
RP   INVOLVEMENT IN ACUTE LYMPHOBLASIC LEUKEMIA.
RX   PubMed=19129520; DOI=10.1056/NEJMoa0808253;
RA   Mullighan C.G., Su X., Zhang J., Radtke I., Phillips L.A.,
RA   Miller C.B., Ma J., Liu W., Cheng C., Schulman B.A., Harvey R.C.,
RA   Chen I.-M., Clifford R.J., Carroll W.L., Reaman G., Bowman W.P.,
RA   Devidas M., Gerhard D.S., Yang W., Relling M.V., Shurtleff S.A.,
RA   Campana D., Borowitz M.J., Pui C.H., Smith M., Hunger S.P.,
RA   Willman C.L., Downing J.R.;
RT   "Deletion of IKZF1 and prognosis in acute lymphoblastic leukemia.";
RL   N. Engl. J. Med. 360:470-480(2009).
RN   [17]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-63; SER-258; SER-361 AND
RP   SER-364, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA   Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA   Rodionov V., Han D.K.;
RT   "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT   reveals system-wide modulation of protein-protein interactions.";
RL   Sci. Signal. 2:RA46-RA46(2009).
RN   [18]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA   Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [19]
RP   FUNCTION IN DNA BINDING, SUBCELLULAR LOCATION, PHOSPHORYLATION, AND
RP   ALTERNATIVE SPLICING.
RX   PubMed=22106042; DOI=10.1002/pbc.23406;
RA   Li Z., Song C., Ouyang H., Lai L., Payne K.J., Dovat S.;
RT   "Cell cycle-specific function of Ikaros in human leukemia.";
RL   Pediatr. Blood Cancer 59:69-76(2012).
RN   [20]
RP   PHOSPHORYLATION AT SER-361 AND SER-364 BY SYK, AND SUBCELLULAR
RP   LOCATION.
RX   PubMed=23071339; DOI=10.1073/pnas.1209828109;
RA   Uckun F.M., Ma H., Zhang J., Ozer Z., Dovat S., Mao C., Ishkhanian R.,
RA   Goodman P., Qazi S.;
RT   "Serine phosphorylation by SYK is critical for nuclear localization
RT   and transcription factor function of Ikaros.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:18072-18077(2012).
RN   [21]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-445, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
RA   Wang L., Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human
RT   liver phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
CC   -!- FUNCTION: Transcription regulator of hematopoietic cell
CC       differentiation (PubMed:17934067). Binds gamma-satellite DNA
CC       (PubMed:17135265, PubMed:19141594). Plays a role in the
CC       development of lymphocytes, B- and T-cells. Binds and activates
CC       the enhancer (delta-A element) of the CD3-delta gene. Repressor of
CC       the TDT (fikzfterminal deoxynucleotidyltransferase) gene during
CC       thymocyte differentiation. Regulates transcription through
CC       association with both HDAC-dependent and HDAC-independent
CC       complexes. Targets the 2 chromatin-remodeling complexes, NuRD and
CC       BAF (SWI/SNF), in a single complex (PYR complex), to the beta-
CC       globin locus in adult erythrocytes. Increases normal apoptosis in
CC       adult erythroid cells. Confers early temporal competence to
CC       retinal progenitor cells (RPCs) (By similarity). Function is
CC       isoform-specific and is modulated by dominant-negative inactive
CC       isoforms (PubMed:17135265, PubMed:17934067).
CC       {ECO:0000250|UniProtKB:Q03267, ECO:0000269|PubMed:10204490,
CC       ECO:0000269|PubMed:17135265, ECO:0000269|PubMed:17934067,
CC       ECO:0000269|PubMed:19141594}.
CC   -!- SUBUNIT: Heterodimer formed by the various isoforms; this
CC       modulates transcription regulator activity (PubMed:17135265,
CC       PubMed:17934067). Heterodimer with other IKAROS family members.
CC       Interacts with IKZF4 AND IKZF5 (PubMed:10978333). Component of the
CC       chromatin-remodeling NuRD repressor complex which includes at
CC       least HDAC1, HDAC2, RBBP4, RBBP7, IKZF1, MTA2, MBD2, MBD3, MTA1L1,
CC       CHD3 and CHD4. Interacts directly with the CHD4 component of the
CC       NuRD complex. Component of the BAF (SWI/SNF) gene activator
CC       complex which includes ACTB, ARID1A, ARID1B, IKZF1, ARID1A,
CC       ARID1B, SMARCA2, SMARCA4 and at least one BAF subunit. Interacts
CC       directly with the SMARCA4 component of the BAF complex (By
CC       similarity). Interacts with SUMO1; the interaction sumoylates
CC       IKAROS, promoted by PIAS2 and PIAS3. Interacts with PIAS2 (isoform
CC       alpha); the interaction promotes sumoylation and reduces
CC       transcription repression. Interacts, to a lesser extent, with
CC       PIAS3. Interacts with PPP1CC; the interaction targets PPP1CC to
CC       pericentromeric heterochromatin, dephosphorylates IKAROS,
CC       stabilizes it and prevents it from degradation. Interacts with
CC       IKZF3 (By similarity). {ECO:0000250, ECO:0000269|PubMed:10204490,
CC       ECO:0000269|PubMed:10978333, ECO:0000305|PubMed:17135265,
CC       ECO:0000305|PubMed:17934067}.
CC   -!- INTERACTION:
CC       A8K932:-; NbExp=3; IntAct=EBI-745305, EBI-10174671;
CC       Q8WTP8:AEN; NbExp=3; IntAct=EBI-745305, EBI-8637627;
CC       Q96Q83:ALKBH3; NbExp=3; IntAct=EBI-745305, EBI-6658697;
CC       Q9BXS5:AP1M1; NbExp=3; IntAct=EBI-745305, EBI-541426;
CC       Q9H6L4:ARMC7; NbExp=3; IntAct=EBI-745305, EBI-742909;
CC       Q13895:BYSL; NbExp=5; IntAct=EBI-745305, EBI-358049;
CC       Q9NUL5:C19orf66; NbExp=3; IntAct=EBI-745305, EBI-10313866;
CC       Q9NX04:C1orf109; NbExp=3; IntAct=EBI-745305, EBI-8643161;
CC       Q8IYL3:C1orf174; NbExp=3; IntAct=EBI-745305, EBI-715898;
CC       Q9H7E9:C8orf33; NbExp=3; IntAct=EBI-745305, EBI-715389;
CC       Q9HC52:CBX8; NbExp=3; IntAct=EBI-745305, EBI-712912;
CC       Q8IYX8-2:CEP57L1; NbExp=3; IntAct=EBI-745305, EBI-10181988;
CC       P61024:CKS1B; NbExp=3; IntAct=EBI-745305, EBI-456371;
CC       Q13363-2:CTBP1; NbExp=3; IntAct=EBI-745305, EBI-10171858;
CC       P56545:CTBP2; NbExp=5; IntAct=EBI-745305, EBI-741533;
CC       Q8IY44:CTBP2; NbExp=3; IntAct=EBI-745305, EBI-10171902;
CC       O43602:DCX; NbExp=4; IntAct=EBI-745305, EBI-8646694;
CC       P26196:DDX6; NbExp=3; IntAct=EBI-745305, EBI-351257;
CC       Q92630:DYRK2; NbExp=3; IntAct=EBI-745305, EBI-749432;
CC       Q3B820:FAM161A; NbExp=3; IntAct=EBI-745305, EBI-719941;
CC       Q7L5A3:FAM214B; NbExp=4; IntAct=EBI-745305, EBI-745689;
CC       Q9Y247:FAM50B; NbExp=4; IntAct=EBI-745305, EBI-742802;
CC       Q5TZK3:FAM74A6; NbExp=3; IntAct=EBI-745305, EBI-10247271;
CC       P61328:FGF12; NbExp=3; IntAct=EBI-745305, EBI-6657662;
CC       Q96NE9:FRMD6; NbExp=3; IntAct=EBI-745305, EBI-741729;
CC       O76003:GLRX3; NbExp=3; IntAct=EBI-745305, EBI-374781;
CC       Q8NEA9:GMCL1P1; NbExp=3; IntAct=EBI-745305, EBI-745707;
CC       Q9H1K1:ISCU; NbExp=3; IntAct=EBI-745305, EBI-1047335;
CC       Q8TAP4:LMO3; NbExp=3; IntAct=EBI-745305, EBI-742259;
CC       Q9Y4Z0:LSM4; NbExp=3; IntAct=EBI-745305, EBI-372521;
CC       Q9UI95:MAD2L2; NbExp=3; IntAct=EBI-745305, EBI-77889;
CC       Q96EZ8:MCRS1; NbExp=3; IntAct=EBI-745305, EBI-348259;
CC       Q9UBU8:MORF4L1; NbExp=3; IntAct=EBI-745305, EBI-399246;
CC       Q15014:MORF4L2; NbExp=3; IntAct=EBI-745305, EBI-399257;
CC       Q13330:MTA1; NbExp=3; IntAct=EBI-745305, EBI-714236;
CC       Q9HC98:NEK6; NbExp=3; IntAct=EBI-745305, EBI-740364;
CC       Q9BVI4:NOC4L; NbExp=3; IntAct=EBI-745305, EBI-395927;
CC       Q13526:PIN1; NbExp=3; IntAct=EBI-745305, EBI-714158;
CC       Q96T60:PNKP; NbExp=3; IntAct=EBI-745305, EBI-1045072;
CC       O43741:PRKAB2; NbExp=3; IntAct=EBI-745305, EBI-1053424;
CC       P25786:PSMA1; NbExp=3; IntAct=EBI-745305, EBI-359352;
CC       P25789:PSMA4; NbExp=3; IntAct=EBI-745305, EBI-359310;
CC       Q7Z474:PSMA4; NbExp=3; IntAct=EBI-745305, EBI-10257551;
CC       O75771:RAD51D; NbExp=4; IntAct=EBI-745305, EBI-1055693;
CC       P57060:RWDD2B; NbExp=4; IntAct=EBI-745305, EBI-724442;
CC       Q9BWG6:SCNM1; NbExp=3; IntAct=EBI-745305, EBI-748391;
CC       O00560:SDCBP; NbExp=3; IntAct=EBI-745305, EBI-727004;
CC       Q9H788:SH2D4A; NbExp=3; IntAct=EBI-745305, EBI-747035;
CC       P62306:SNRPF; NbExp=3; IntAct=EBI-745305, EBI-356900;
CC       Q13573:SNW1; NbExp=3; IntAct=EBI-745305, EBI-632715;
CC       Q9H0A9:SPATC1L; NbExp=3; IntAct=EBI-745305, EBI-372911;
CC       Q9BSW7:SYT17; NbExp=3; IntAct=EBI-745305, EBI-745392;
CC       Q7KZS0:UBE2I; NbExp=3; IntAct=EBI-745305, EBI-10180829;
CC       Q15007:WTAP; NbExp=3; IntAct=EBI-745305, EBI-751647;
CC       Q96NC0:ZMAT2; NbExp=3; IntAct=EBI-745305, EBI-2682299;
CC       Q8TAU3:ZNF417; NbExp=3; IntAct=EBI-745305, EBI-740727;
CC       Q9P0T4:ZNF581; NbExp=3; IntAct=EBI-745305, EBI-745520;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17135265,
CC       ECO:0000269|PubMed:22106042, ECO:0000269|PubMed:23071339}. Note=In
CC       resting lymphocytes, distributed diffusely throughout the nucleus.
CC       Localizes to pericentromeric heterochromatin in proliferating
CC       cells. This localization requires DNA binding which is regulated
CC       by phosphorylation / dephosphorylation events.
CC       {ECO:0000269|PubMed:17135265, ECO:0000269|PubMed:22106042}.
CC   -!- SUBCELLULAR LOCATION: Isoform Ik2: Nucleus. Note=In resting
CC       lymphocytes, distributed diffusely throughout the nucleus.
CC       Localizes to pericentromeric heterochromatin in proliferating
CC       cells. This localization requires DNA binding which is regulated
CC       by phosphorylation / dephosphorylation events (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Isoform Ik6: Cytoplasm {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=8;
CC       Name=Ik1;
CC         IsoId=Q13422-1; Sequence=Displayed;
CC       Name=Ik2;
CC         IsoId=Q13422-2; Sequence=VSP_006848;
CC       Name=Ik3;
CC         IsoId=Q13422-3; Sequence=VSP_006850;
CC       Name=Ik4;
CC         IsoId=Q13422-4; Sequence=VSP_006847, VSP_006850;
CC       Name=Ik5;
CC         IsoId=Q13422-5; Sequence=VSP_006852;
CC       Name=Ik6;
CC         IsoId=Q13422-6; Sequence=VSP_006849;
CC       Name=Ik7;
CC         IsoId=Q13422-7; Sequence=VSP_006851;
CC       Name=Ikx;
CC         IsoId=Q13422-8; Sequence=VSP_006851, VSP_053404, VSP_053405;
CC   -!- TISSUE SPECIFICITY: Abundantly expressed in thymus, spleen and
CC       peripheral blood Leukocytes and lymph nodes. Lower expression in
CC       bone marrow and small intestine. {ECO:0000269|PubMed:8543809,
CC       ECO:0000269|PubMed:8964602}.
CC   -!- DOMAIN: The N-terminal zinc-fingers 2 and 3 are required for DNA
CC       binding as well as for targeting IKFZ1 to pericentromeric
CC       heterochromatin. {ECO:0000250}.
CC   -!- DOMAIN: The C-terminal zinc-finger domain is required for
CC       dimerization. {ECO:0000250}.
CC   -!- PTM: Phosphorylation controls cell-cycle progression from late
CC       G(1) stage to S stage. Hyperphosphorylated during G2/M phase.
CC       Dephosphorylated state during late G(1) phase. Phosphorylation on
CC       Thr-140 is required for DNA and pericentromeric location during
CC       mitosis. CK2 is the main kinase, in vitro. GSK3 and CDK may also
CC       contribute to phosphorylation of the C-terminal serine and
CC       threonine residues. Phosphorylation on these C-terminal residues
CC       reduces the DNA-binding ability. Phosphorylation/dephosphorylation
CC       events on Ser-13 and Ser-295 regulate TDT expression during
CC       thymocyte differentiation. Dephosphorylation by protein
CC       phosphatase 1 regulates stability and pericentromeric
CC       heterochromatin location. Phosphorylated in both lymphoid and non-
CC       lymphoid tissues (By similarity). Phosphorylation at Ser-361 and
CC       Ser-364 downstream of SYK induces nuclear translocation.
CC       {ECO:0000250, ECO:0000269|PubMed:22106042,
CC       ECO:0000269|PubMed:23071339}.
CC   -!- PTM: Sumoylated. Simulataneous sumoylation on the 2 sites results
CC       in a loss of both HDAC-dependent and HDAC-independent repression.
CC       Has no effect on pericentromeric heterochromatin location.
CC       Desumoylated by SENP1 (By similarity). {ECO:0000250}.
CC   -!- PTM: Polyubiquitinated. {ECO:0000250}.
CC   -!- DISEASE: Note=Defects in IKZF1 are frequent occurrences (28.6%) in
CC       acute lymphoblasic leukemia (ALL). Such alterations or deletions
CC       lead to poor prognosis for ALL.
CC   -!- DISEASE: Note=Chromosomal aberrations involving IKZF1 are a cause
CC       of B-cell non-Hodgkin lymphomas (B-cell NHL). Translocation
CC       t(3;7)(q27;p12), with BCL6.
CC   -!- SIMILARITY: Belongs to the Ikaros C2H2-type zinc-finger protein
CC       family. {ECO:0000305}.
CC   -!- SIMILARITY: Contains 6 C2H2-type zinc fingers.
CC       {ECO:0000255|PROSITE-ProRule:PRU00042}.
CC   -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC       and Haematology;
CC       URL="http://atlasgeneticsoncology.org/Genes/IkarosID258.html";
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DR   EMBL; U40462; AAC50459.1; -; mRNA.
DR   EMBL; S80876; AAB50683.1; -; mRNA.
DR   EMBL; AY377974; AAR84585.1; -; mRNA.
DR   EMBL; AK303586; BAG64603.1; -; mRNA.
DR   EMBL; BT009836; AAP88838.1; -; mRNA.
DR   EMBL; AC124014; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC233268; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471128; EAW60977.1; -; Genomic_DNA.
DR   EMBL; CH471128; EAW60978.1; -; Genomic_DNA.
DR   EMBL; CH471128; EAW60981.1; -; Genomic_DNA.
DR   EMBL; CH236955; EAL23900.1; -; Genomic_DNA.
DR   EMBL; CH471128; EAW60979.1; -; Genomic_DNA.
DR   EMBL; BC018349; AAH18349.1; -; mRNA.
DR   CCDS; CCDS59055.1; -. [Q13422-7]
DR   CCDS; CCDS69299.1; -. [Q13422-5]
DR   CCDS; CCDS75596.1; -. [Q13422-1]
DR   CCDS; CCDS75597.1; -. [Q13422-3]
DR   CCDS; CCDS78233.1; -. [Q13422-2]
DR   RefSeq; NP_001207694.1; NM_001220765.2. [Q13422-7]
DR   RefSeq; NP_001207696.1; NM_001220767.2.
DR   RefSeq; NP_001207697.1; NM_001220768.2. [Q13422-3]
DR   RefSeq; NP_001207699.1; NM_001220770.2.
DR   RefSeq; NP_001207700.1; NM_001220771.2. [Q13422-5]
DR   RefSeq; NP_001278766.1; NM_001291837.1. [Q13422-7]
DR   RefSeq; NP_001278767.1; NM_001291838.1. [Q13422-2]
DR   RefSeq; NP_001278768.1; NM_001291839.1.
DR   RefSeq; NP_001278769.1; NM_001291840.1. [Q13422-6]
DR   RefSeq; NP_001278770.1; NM_001291841.1.
DR   RefSeq; NP_001278771.1; NM_001291842.1.
DR   RefSeq; NP_001278772.1; NM_001291843.1.
DR   RefSeq; NP_001278773.1; NM_001291844.1.
DR   RefSeq; NP_006051.1; NM_006060.5. [Q13422-1]
DR   RefSeq; XP_011513370.1; XM_011515068.1. [Q13422-1]
DR   RefSeq; XP_011513371.1; XM_011515069.1. [Q13422-1]
DR   RefSeq; XP_011513377.1; XM_011515075.1. [Q13422-2]
DR   RefSeq; XP_011513378.1; XM_011515076.1. [Q13422-2]
DR   UniGene; Hs.435949; -.
DR   UniGene; Hs.488251; -.
DR   UniGene; Hs.646004; -.
DR   UniGene; Hs.731495; -.
DR   ProteinModelPortal; Q13422; -.
DR   SMR; Q13422; 112-220, 460-509.
DR   BioGrid; 115604; 118.
DR   DIP; DIP-41110N; -.
DR   IntAct; Q13422; 68.
DR   MINT; MINT-129252; -.
DR   STRING; 9606.ENSP00000331614; -.
DR   PhosphoSite; Q13422; -.
DR   BioMuta; IKZF1; -.
DR   DMDM; 3913926; -.
DR   MaxQB; Q13422; -.
DR   PaxDb; Q13422; -.
DR   PRIDE; Q13422; -.
DR   DNASU; 10320; -.
DR   Ensembl; ENST00000331340; ENSP00000331614; ENSG00000185811. [Q13422-1]
DR   Ensembl; ENST00000343574; ENSP00000342750; ENSG00000185811. [Q13422-2]
DR   Ensembl; ENST00000349824; ENSP00000342485; ENSG00000185811. [Q13422-5]
DR   Ensembl; ENST00000357364; ENSP00000349928; ENSG00000185811. [Q13422-3]
DR   Ensembl; ENST00000359197; ENSP00000352123; ENSG00000185811. [Q13422-7]
DR   Ensembl; ENST00000438033; ENSP00000396554; ENSG00000185811. [Q13422-2]
DR   Ensembl; ENST00000439701; ENSP00000413025; ENSG00000185811. [Q13422-7]
DR   GeneID; 10320; -.
DR   KEGG; hsa:10320; -.
DR   UCSC; uc003tow.4; human. [Q13422-1]
DR   UCSC; uc003tox.4; human. [Q13422-7]
DR   UCSC; uc003tpa.4; human. [Q13422-6]
DR   UCSC; uc011kck.2; human. [Q13422-2]
DR   UCSC; uc022acq.1; human. [Q13422-5]
DR   UCSC; uc022acs.1; human. [Q13422-4]
DR   UCSC; uc022acx.1; human. [Q13422-3]
DR   CTD; 10320; -.
DR   GeneCards; IKZF1; -.
DR   HGNC; HGNC:13176; IKZF1.
DR   HPA; CAB009247; -.
DR   HPA; HPA035221; -.
DR   HPA; HPA035222; -.
DR   MIM; 603023; gene.
DR   neXtProt; NX_Q13422; -.
DR   Orphanet; 317473; Pancytopenia due to IKZF1 mutations.
DR   Orphanet; 99860; Precursor B-cell acute lymphoblastic leukemia.
DR   PharmGKB; PA37748; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   eggNOG; COG5048; LUCA.
DR   GeneTree; ENSGT00550000074392; -.
DR   HOVERGEN; HBG004752; -.
DR   InParanoid; Q13422; -.
DR   KO; K09220; -.
DR   OMA; GDKCLSD; -.
DR   PhylomeDB; Q13422; -.
DR   TreeFam; TF331189; -.
DR   SignaLink; Q13422; -.
DR   ChiTaRS; IKZF1; human.
DR   GeneWiki; IKZF1; -.
DR   GenomeRNAi; 10320; -.
DR   NextBio; 39123; -.
DR   PRO; PR:Q13422; -.
DR   Proteomes; UP000005640; Chromosome 7.
DR   Bgee; Q13422; -.
DR   CleanEx; HS_IKZF1; -.
DR   ExpressionAtlas; Q13422; baseline and differential.
DR   Genevisible; Q13422; HS.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0005721; C:pericentric heterochromatin; IEA:Ensembl.
DR   GO; GO:0043234; C:protein complex; IDA:MGI.
DR   GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IEA:Ensembl.
DR   GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0044212; F:transcription regulatory region DNA binding; IBA:GO_Central.
DR   GO; GO:0035881; P:amacrine cell differentiation; IEA:Ensembl.
DR   GO; GO:0030183; P:B cell differentiation; IEA:Ensembl.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0016568; P:chromatin modification; IEA:UniProtKB-KW.
DR   GO; GO:0030218; P:erythrocyte differentiation; IMP:UniProtKB.
DR   GO; GO:0030900; P:forebrain development; IEA:Ensembl.
DR   GO; GO:0048535; P:lymph node development; IEA:Ensembl.
DR   GO; GO:0030098; P:lymphocyte differentiation; IMP:UniProtKB.
DR   GO; GO:0007498; P:mesoderm development; TAS:ProtInc.
DR   GO; GO:0001779; P:natural killer cell differentiation; IEA:Ensembl.
DR   GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IBA:GO_Central.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR   GO; GO:0048541; P:Peyer's patch development; IEA:Ensembl.
DR   GO; GO:0045579; P:positive regulation of B cell differentiation; IEA:Ensembl.
DR   GO; GO:0040018; P:positive regulation of multicellular organism growth; IEA:Ensembl.
DR   GO; GO:0045660; P:positive regulation of neutrophil differentiation; IEA:Ensembl.
DR   GO; GO:0051138; P:positive regulation of NK T cell differentiation; IEA:Ensembl.
DR   GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IBA:GO_Central.
DR   GO; GO:0060040; P:retinal bipolar neuron differentiation; IEA:Ensembl.
DR   GO; GO:0030217; P:T cell differentiation; IEA:Ensembl.
DR   GO; GO:0048538; P:thymus development; IEA:Ensembl.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.160.60; -; 4.
DR   InterPro; IPR007087; Znf_C2H2.
DR   InterPro; IPR015880; Znf_C2H2-like.
DR   InterPro; IPR013087; Znf_C2H2/integrase_DNA-bd.
DR   Pfam; PF00096; zf-C2H2; 1.
DR   SMART; SM00355; ZnF_C2H2; 6.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 5.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 4.
PE   1: Evidence at protein level;
KW   Activator; Alternative splicing; Cell cycle; Chromatin regulator;
KW   Chromosomal rearrangement; Complete proteome; Cytoplasm;
KW   Developmental protein; DNA-binding; Isopeptide bond; Metal-binding;
KW   Nucleus; Phosphoprotein; Reference proteome; Repeat; Repressor;
KW   Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW   Zinc-finger.
FT   CHAIN         1    519       DNA-binding protein Ikaros.
FT                                /FTId=PRO_0000047094.
FT   ZN_FING     117    139       C2H2-type 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     145    167       C2H2-type 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     173    195       C2H2-type 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     201    224       C2H2-type 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     462    484       C2H2-type 5. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     490    514       C2H2-type 6. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   REGION      154    163       Required for both high-affinity DNA
FT                                binding and pericentromeric
FT                                heterochromatin localization.
FT                                {ECO:0000250}.
FT   REGION      180    195       Required for both high-affinity DNA
FT                                binding and pericentromeric
FT                                heterochromatin localization.
FT                                {ECO:0000250}.
FT   REGION      468    471       Required for binding PP1CC.
FT                                {ECO:0000250}.
FT   COMPBIAS    373    376       Poly-Leu.
FT   SITE        159    159       Required for both pericentromeric
FT                                heterochromatin localization and complete
FT                                DNA binding. {ECO:0000250}.
FT   SITE        162    162       Required for both pericentromeric
FT                                heterochromatin localization and complete
FT                                DNA binding. {ECO:0000250}.
FT   SITE        188    188       Required for both pericentromeric
FT                                heterochromatin localization and DNA
FT                                binding. {ECO:0000250}.
FT   MOD_RES      13     13       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q03267}.
FT   MOD_RES      23     23       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:Q03267}.
FT   MOD_RES      63     63       Phosphoserine.
FT                                {ECO:0000244|PubMed:19690332}.
FT   MOD_RES     101    101       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q03267}.
FT   MOD_RES     140    140       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:Q03267}.
FT   MOD_RES     168    168       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q03267}.
FT   MOD_RES     196    196       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q03267}.
FT   MOD_RES     258    258       Phosphoserine.
FT                                {ECO:0000244|PubMed:19690332}.
FT   MOD_RES     295    295       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q03267}.
FT   MOD_RES     361    361       Phosphoserine.
FT                                {ECO:0000244|PubMed:19690332,
FT                                ECO:0000269|PubMed:23071339}.
FT   MOD_RES     364    364       Phosphoserine.
FT                                {ECO:0000244|PubMed:19690332,
FT                                ECO:0000269|PubMed:23071339}.
FT   MOD_RES     389    389       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q03267}.
FT   MOD_RES     391    391       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q03267}.
FT   MOD_RES     393    393       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q03267}.
FT   MOD_RES     397    397       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q03267}.
FT   MOD_RES     398    398       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:Q03267}.
FT   MOD_RES     402    402       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q03267}.
FT   MOD_RES     445    445       Phosphoserine.
FT                                {ECO:0000244|PubMed:24275569}.
FT   CROSSLNK     58     58       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO).
FT                                {ECO:0000250}.
FT   CROSSLNK    241    241       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO).
FT                                {ECO:0000250}.
FT   VAR_SEQ      10     53       Missing (in isoform Ik4). {ECO:0000305}.
FT                                /FTId=VSP_006847.
FT   VAR_SEQ      54    283       Missing (in isoform Ik6). {ECO:0000305}.
FT                                /FTId=VSP_006849.
FT   VAR_SEQ      54    140       Missing (in isoform Ik2).
FT                                {ECO:0000303|PubMed:14702039}.
FT                                /FTId=VSP_006848.
FT   VAR_SEQ     141    283       Missing (in isoform Ik5). {ECO:0000305}.
FT                                /FTId=VSP_006852.
FT   VAR_SEQ     197    283       Missing (in isoform Ik3 and isoform Ik4).
FT                                {ECO:0000305}.
FT                                /FTId=VSP_006850.
FT   VAR_SEQ     197    238       Missing (in isoform Ik7 and isoform Ikx).
FT                                {ECO:0000303|PubMed:15489334,
FT                                ECO:0000303|Ref.3, ECO:0000303|Ref.5}.
FT                                /FTId=VSP_006851.
FT   VAR_SEQ     260    268       RSLVLDRLA -> ISRAGQTSK (in isoform Ikx).
FT                                {ECO:0000303|Ref.3}.
FT                                /FTId=VSP_053404.
FT   VAR_SEQ     269    519       Missing (in isoform Ikx).
FT                                {ECO:0000303|Ref.3}.
FT                                /FTId=VSP_053405.
FT   CONFLICT     11     12       QV -> FS (in Ref. 2; AAB50683).
FT                                {ECO:0000305}.
FT   CONFLICT    214    214       S -> T (in Ref. 2; AAB50683).
FT                                {ECO:0000305}.
FT   CONFLICT    245    245       N -> K (in Ref. 2; AAB50683).
FT                                {ECO:0000305}.
FT   CONFLICT    296    296       Missing (in Ref. 2; AAB50683).
FT                                {ECO:0000305}.
FT   CONFLICT    298    298       S -> T (in Ref. 2; AAB50683).
FT                                {ECO:0000305}.
FT   CONFLICT    352    355       KPLA -> RRS (in Ref. 2; AAB50683).
FT                                {ECO:0000305}.
FT   CONFLICT    372    372       N -> Y (in Ref. 2; AAB50683).
FT                                {ECO:0000305}.
FT   CONFLICT    420    426       PHARNGL -> RRAQRV (in Ref. 2; AAB50683).
FT                                {ECO:0000305}.
SQ   SEQUENCE   519 AA;  57528 MW;  7B0129C4E3FE41A8 CRC64;
     MDADEGQDMS QVSGKESPPV SDTPDEGDEP MPIPEDLSTT SGGQQSSKSD RVVASNVKVE
     TQSDEENGRA CEMNGEECAE DLRMLDASGE KMNGSHRDQG SSALSGVGGI RLPNGKLKCD
     ICGIICIGPN VLMVHKRSHT GERPFQCNQC GASFTQKGNL LRHIKLHSGE KPFKCHLCNY
     ACRRRDALTG HLRTHSVGKP HKCGYCGRSY KQRSSLEEHK ERCHNYLESM GLPGTLYPVI
     KEETNHSEMA EDLCKIGSER SLVLDRLASN VAKRKSSMPQ KFLGDKGLSD TPYDSSASYE
     KENEMMKSHV MDQAINNAIN YLGAESLRPL VQTPPGGSEV VPVISPMYQL HKPLAEGTPR
     SNHSAQDSAV ENLLLLSKAK LVPSEREASP SNSCQDSTDT ESNNEEQRSG LIYLTNHIAP
     HARNGLSLKE EHRAYDLLRA ASENSQDALR VVSTSGEQMK VYKCEHCRVL FLDHVMYTIH
     MGCHGFRDPF ECNMCGYHSQ DRYEFSSHIT RGEHRFHMS
//
ID   IKZF4_HUMAN             Reviewed;         585 AA.
AC   Q9H2S9; Q96JP3;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 2.
DT   11-NOV-2015, entry version 115.
DE   RecName: Full=Zinc finger protein Eos;
DE   AltName: Full=Ikaros family zinc finger protein 4;
GN   Name=IKZF4; Synonyms=KIAA1782, ZNFN1A4;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Brain;
RX   PubMed=11347906; DOI=10.1093/dnares/8.2.85;
RA   Nagase T., Nakayama M., Nakajima D., Kikuno R., Ohara O.;
RT   "Prediction of the coding sequences of unidentified human genes. XX.
RT   The complete sequences of 100 new cDNA clones from brain which code
RT   for large proteins in vitro.";
RL   DNA Res. 8:85-95(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA   Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA   Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 53-585 (ISOFORM 1), FUNCTION, TISSUE
RP   SPECIFICITY, AND INTERACTION WITH IKZF1; IKZF2; IKZF3 AND IKZF5.
RX   PubMed=10978333; DOI=10.1074/jbc.M005457200;
RA   Perdomo J., Holmes M., Chong B., Crossley M.;
RT   "Eos and pegasus, two members of the Ikaros family of proteins with
RT   distinct DNA binding activities.";
RL   J. Biol. Chem. 275:38347-38354(2000).
RN   [4]
RP   FUNCTION.
RX   PubMed=12015313; DOI=10.1074/jbc.M201694200;
RA   Koipally J., Georgopoulos K.;
RT   "A molecular dissection of the repression circuitry of Ikaros.";
RL   J. Biol. Chem. 277:27697-27705(2002).
RN   [5]
RP   FUNCTION, INTERACTION WITH CTBP2, SUBCELLULAR LOCATION, AND
RP   MUTAGENESIS OF 425-PRO--ASP-427.
RX   PubMed=12444977; DOI=10.1046/j.1432-1033.2002.03313.x;
RA   Perdomo J., Crossley M.;
RT   "The Ikaros family protein Eos associates with C-terminal-binding
RT   protein corepressors.";
RL   Eur. J. Biochem. 269:5885-5892(2002).
RN   [6]
RP   STRUCTURE BY NMR OF 155-216 IN COMPLEX WITH ZINC IONS.
RG   Northeast structural genomics consortium (NESG);
RT   "Solution NMR structure of zinc finger protein EOS from Homo sapiens,
RT   Northeast structural genomics consortium (NESG) target HR7992A.";
RL   Submitted (SEP-2013) to the PDB data bank.
CC   -!- FUNCTION: DNA-binding protein that binds to the 5'GGGAATRCC-3'
CC       Ikaros-binding sequence. Transcriptional repressor. Interacts with
CC       SPI1 and MITF to repress transcription of the CTSK and ACP5
CC       promoters via recruitment of corepressors SIN3A and CTBP2. May be
CC       involved in the development of central and peripheral nervous
CC       systems. Essential for the inhibitory function of regulatory T-
CC       cells (Treg). Mediates FOXP3-mediated gene silencing in regulatory
CC       T-cells (Treg) via recruitment of corepressor CTBP1 (By
CC       similarity). {ECO:0000250|UniProtKB:Q8C208,
CC       ECO:0000269|PubMed:10978333, ECO:0000269|PubMed:12015313,
CC       ECO:0000269|PubMed:12444977}.
CC   -!- SUBUNIT: Self-associates. Interacts with other family members;
CC       IKZF1, IKZF2, IKZF3 and IKZF5. Interacts with CTBP2. Interacts
CC       with SPI1, MITF, FOXP3 and CTBP1 (By similarity).
CC       {ECO:0000250|UniProtKB:Q8C208, ECO:0000269|PubMed:12444977}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12444977}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9H2S9-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9H2S9-2; Sequence=VSP_027688;
CC         Note=No experimental confirmation available.;
CC   -!- TISSUE SPECIFICITY: Highly expressed in skeletal muscle, low
CC       levels of expression in heart, thymus, kidney, liver, and spleen.
CC       Expressed in the hematopoietic cell lines MOLT-4, NALM-6 and K-
CC       562. Highly expressed in THP-1 and M-07e cell lines, which have
CC       characteristics of myeloid and early megakaryocytic cells
CC       respectively. {ECO:0000269|PubMed:10978333}.
CC   -!- DOMAIN: The N-terminal zinc fingers are involved in sequence-
CC       specific DNA binding and heterotypic associations with other
CC       family members.
CC   -!- DOMAIN: C-terminal zinc fingers mediate homodimerization.
CC   -!- MISCELLANEOUS: 'Eos' means 'rising sun' in Greek.
CC   -!- SIMILARITY: Belongs to the Ikaros C2H2-type zinc-finger protein
CC       family. {ECO:0000305}.
CC   -!- SIMILARITY: Contains 6 C2H2-type zinc fingers.
CC       {ECO:0000255|PROSITE-ProRule:PRU00042}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAG39221.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=BAB47411.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AB058685; BAB47411.1; ALT_INIT; mRNA.
DR   EMBL; BX647761; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AF230809; AAG39221.1; ALT_INIT; mRNA.
DR   CCDS; CCDS44917.1; -. [Q9H2S9-1]
DR   RefSeq; NP_071910.3; NM_022465.3. [Q9H2S9-1]
DR   RefSeq; XP_011536969.1; XM_011538667.1. [Q9H2S9-2]
DR   UniGene; Hs.553221; -.
DR   PDB; 2MA7; NMR; -; A=155-216.
DR   PDBsum; 2MA7; -.
DR   DisProt; DP00376; -.
DR   ProteinModelPortal; Q9H2S9; -.
DR   SMR; Q9H2S9; 99-137, 154-267, 521-561.
DR   BioGrid; 122146; 16.
DR   IntAct; Q9H2S9; 2.
DR   STRING; 9606.ENSP00000262032; -.
DR   PhosphoSite; Q9H2S9; -.
DR   BioMuta; IKZF4; -.
DR   DMDM; 158564025; -.
DR   MaxQB; Q9H2S9; -.
DR   PaxDb; Q9H2S9; -.
DR   PRIDE; Q9H2S9; -.
DR   DNASU; 64375; -.
DR   Ensembl; ENST00000262032; ENSP00000262032; ENSG00000123411. [Q9H2S9-1]
DR   Ensembl; ENST00000431367; ENSP00000412101; ENSG00000123411. [Q9H2S9-1]
DR   Ensembl; ENST00000547167; ENSP00000448419; ENSG00000123411. [Q9H2S9-1]
DR   GeneID; 64375; -.
DR   KEGG; hsa:64375; -.
DR   UCSC; uc001sjb.1; human. [Q9H2S9-1]
DR   UCSC; uc001sje.1; human. [Q9H2S9-2]
DR   CTD; 64375; -.
DR   GeneCards; IKZF4; -.
DR   HGNC; HGNC:13179; IKZF4.
DR   HPA; HPA049016; -.
DR   MIM; 606239; gene.
DR   neXtProt; NX_Q9H2S9; -.
DR   PharmGKB; PA162391948; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   eggNOG; COG5048; LUCA.
DR   GeneTree; ENSGT00550000074392; -.
DR   HOGENOM; HOG000049114; -.
DR   HOVERGEN; HBG004752; -.
DR   InParanoid; Q9H2S9; -.
DR   KO; K09220; -.
DR   OMA; QPSSDKM; -.
DR   OrthoDB; EOG79GT61; -.
DR   PhylomeDB; Q9H2S9; -.
DR   TreeFam; TF331189; -.
DR   GeneWiki; IKZF4; -.
DR   GenomeRNAi; 64375; -.
DR   NextBio; 66301; -.
DR   PRO; PR:Q9H2S9; -.
DR   Proteomes; UP000005640; Chromosome 12.
DR   Bgee; Q9H2S9; -.
DR   CleanEx; HS_IKZF4; -.
DR   ExpressionAtlas; Q9H2S9; baseline and differential.
DR   Genevisible; Q9H2S9; HS.
DR   GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; TAS:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IEA:Ensembl.
DR   GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; TAS:UniProtKB.
DR   GO; GO:0044212; F:transcription regulatory region DNA binding; IBA:GO_Central.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; TAS:UniProtKB.
DR   GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IBA:GO_Central.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.160.60; -; 4.
DR   InterPro; IPR007087; Znf_C2H2.
DR   InterPro; IPR015880; Znf_C2H2-like.
DR   InterPro; IPR013087; Znf_C2H2/integrase_DNA-bd.
DR   SMART; SM00355; ZnF_C2H2; 6.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 5.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 4.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative splicing; Complete proteome;
KW   DNA-binding; Metal-binding; Nucleus; Phosphoprotein;
KW   Reference proteome; Repeat; Repressor; Transcription;
KW   Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN         1    585       Zinc finger protein Eos.
FT                                /FTId=PRO_0000299468.
FT   ZN_FING     159    181       C2H2-type 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     187    209       C2H2-type 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     215    237       C2H2-type 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     248    271       C2H2-type 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     530    552       C2H2-type 5. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     558    582       C2H2-type 6. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   REGION      281    585       Interaction with FOXP3.
FT                                {ECO:0000250|UniProtKB:Q8C208}.
FT   MOTIF       425    429       CTBP-binding motif PEDLA.
FT   MOD_RES     105    105       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9UKS7}.
FT   MOD_RES     335    335       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q9UKS7}.
FT   VAR_SEQ       1     61       MHTPPALPRRFQGGGRVRTPGSHRQGKDNLERDPSGGCVPD
FT                                FLPQAQDSNHFIMESLFCES -> MDSRYLQLQLYLPSCSL
FT                                LQG (in isoform 2).
FT                                {ECO:0000303|PubMed:11347906}.
FT                                /FTId=VSP_027688.
FT   MUTAGEN     425    427       PED->AAA: No effect on CTBP2 interaction.
FT                                {ECO:0000269|PubMed:12444977}.
FT   CONFLICT    145    145       E -> K (in Ref. 3; AAG39221).
FT                                {ECO:0000305}.
FT   CONFLICT    310    310       P -> A (in Ref. 3; AAG39221).
FT                                {ECO:0000305}.
FT   CONFLICT    361    361       A -> G (in Ref. 3; AAG39221).
FT                                {ECO:0000305}.
FT   CONFLICT    390    390       N -> H (in Ref. 3; AAG39221).
FT                                {ECO:0000305}.
FT   CONFLICT    524    524       G -> S (in Ref. 3; AAG39221).
FT                                {ECO:0000305}.
FT   HELIX       173    181       {ECO:0000244|PDB:2MA7}.
FT   STRAND      187    189       {ECO:0000244|PDB:2MA7}.
FT   TURN        190    193       {ECO:0000244|PDB:2MA7}.
FT   STRAND      194    197       {ECO:0000244|PDB:2MA7}.
FT   HELIX       199    205       {ECO:0000244|PDB:2MA7}.
FT   TURN        206    209       {ECO:0000244|PDB:2MA7}.
SQ   SEQUENCE   585 AA;  64106 MW;  42AE169A3E2E14D3 CRC64;
     MHTPPALPRR FQGGGRVRTP GSHRQGKDNL ERDPSGGCVP DFLPQAQDSN HFIMESLFCE
     SSGDSSLEKE FLGAPVGPSV STPNSQHSSP SRSLSANSIK VEMYSDEESS RLLGPDERLL
     EKDDSVIVED SLSEPLGYCD GSGPEPHSPG GIRLPNGKLK CDVCGMVCIG PNVLMVHKRS
     HTGERPFHCN QCGASFTQKG NLLRHIKLHS GEKPFKCPFC NYACRRRDAL TGHLRTHSVS
     SPTVGKPYKC NYCGRSYKQQ STLEEHKERC HNYLQSLSTE AQALAGQPGD EIRDLEMVPD
     SMLHSSSERP TFIDRLANSL TKRKRSTPQK FVGEKQMRFS LSDLPYDVNS GGYEKDVELV
     AHHSLEPGFG SSLAFVGAEH LRPLRLPPTN CISELTPVIS SVYTQMQPLP GRLELPGSRE
     AGEGPEDLAD GGPLLYRPRG PLTDPGASPS NGCQDSTDTE SNHEDRVAGV VSLPQGPPPQ
     PPPTIVVGRH SPAYAKEDPK PQEGLLRGTP GPSKEVLRVV GESGEPVKAF KCEHCRILFL
     DHVMFTIHMG CHGFRDPFEC NICGYHSQDR YEFSSHIVRG EHKVG
//
ID   KLF3_HUMAN              Reviewed;         345 AA.
AC   P57682; Q6PIR1; Q86TN0; Q9P2X6;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 1.
DT   11-NOV-2015, entry version 140.
DE   RecName: Full=Krueppel-like factor 3;
DE   AltName: Full=Basic krueppel-like factor;
DE   AltName: Full=CACCC-box-binding protein BKLF;
DE   AltName: Full=TEF-2;
GN   Name=KLF3; Synonyms=BKLF;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA   Matsumoto N., Yoshida T., Terada M.;
RL   Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Liver;
RX   PubMed=12812068;
RA   Wang M.J., Qu X.H., Wang L.S., Zhai Y., Wu S.L., He F.C.;
RT   "cDNA cloning, subcellular localization and tissue expression of a new
RT   human Kruppel-like transcription factor: human basic Kruppel-like
RT   factor (hBKLF).";
RL   Yi Chuan Xue Bao 30:1-9(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Hippocampus;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-250, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA   Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA   Mann M.;
RT   "Global, in vivo, and site-specific phosphorylation dynamics in
RT   signaling networks.";
RL   Cell 127:635-648(2006).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-92 AND SER-101, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-92 AND SER-111, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA   Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full
RT   phosphorylation site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
RA   Wang L., Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human
RT   liver phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [8]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-198, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25218447; DOI=10.1038/nsmb.2890;
RA   Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA   Vertegaal A.C.;
RT   "Uncovering global SUMOylation signaling networks in a site-specific
RT   manner.";
RL   Nat. Struct. Mol. Biol. 21:927-936(2014).
CC   -!- FUNCTION: Binds to the CACCC box of erythroid cell-expressed
CC       genes. May play a role in hematopoiesis (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- INTERACTION:
CC       Q92997:DVL3; NbExp=3; IntAct=EBI-8472267, EBI-739789;
CC       A2ABF9:EHMT2; NbExp=3; IntAct=EBI-8472267, EBI-10174566;
CC       Q13643:FHL3; NbExp=4; IntAct=EBI-8472267, EBI-741101;
CC       Q68G74:LHX8; NbExp=3; IntAct=EBI-8472267, EBI-8474075;
CC       Q12933:TRAF2; NbExp=3; IntAct=EBI-8472267, EBI-355744;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P57682-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P57682-2; Sequence=VSP_014532;
CC         Note=May be due to intron retention. No experimental
CC         confirmation available.;
CC   -!- PTM: Sumoylated with SUMO1. Sumoylation is enhanced by PIAS1,
CC       PIAS2alpha and PIAS2beta, and PIAS4, but not by Pc2. Enhances
CC       transcriptional repression, but has no effect on DNA binding.
CC       Sumoylation on Lys-198 is the major site (By similarity).
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC       family. {ECO:0000305}.
CC   -!- SIMILARITY: Contains 3 C2H2-type zinc fingers.
CC       {ECO:0000255|PROSITE-ProRule:PRU00042}.
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DR   EMBL; AB024523; BAA92271.1; -; mRNA.
DR   EMBL; AF285837; AAK27329.1; -; mRNA.
DR   EMBL; BC030662; AAH30662.1; -; mRNA.
DR   EMBL; BC051687; AAH51687.1; -; mRNA.
DR   CCDS; CCDS3444.1; -. [P57682-1]
DR   RefSeq; NP_057615.3; NM_016531.5. [P57682-1]
DR   UniGene; Hs.298658; -.
DR   ProteinModelPortal; P57682; -.
DR   SMR; P57682; 251-345.
DR   BioGrid; 119426; 9.
DR   IntAct; P57682; 8.
DR   MINT; MINT-4786517; -.
DR   STRING; 9606.ENSP00000261438; -.
DR   PhosphoSite; P57682; -.
DR   BioMuta; KLF3; -.
DR   DMDM; 12644533; -.
DR   MaxQB; P57682; -.
DR   PaxDb; P57682; -.
DR   PRIDE; P57682; -.
DR   DNASU; 51274; -.
DR   Ensembl; ENST00000261438; ENSP00000261438; ENSG00000109787. [P57682-1]
DR   Ensembl; ENST00000514033; ENSP00000421252; ENSG00000109787. [P57682-2]
DR   GeneID; 51274; -.
DR   KEGG; hsa:51274; -.
DR   UCSC; uc003gtg.2; human. [P57682-1]
DR   CTD; 51274; -.
DR   GeneCards; KLF3; -.
DR   HGNC; HGNC:16516; KLF3.
DR   HPA; HPA049512; -.
DR   MIM; 609392; gene.
DR   neXtProt; NX_P57682; -.
DR   PharmGKB; PA30137; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   eggNOG; COG5048; LUCA.
DR   GeneTree; ENSGT00760000118998; -.
DR   HOGENOM; HOG000232138; -.
DR   HOVERGEN; HBG003941; -.
DR   InParanoid; P57682; -.
DR   KO; K15605; -.
DR   OMA; MKKYSPP; -.
DR   OrthoDB; EOG747PJ4; -.
DR   PhylomeDB; P57682; -.
DR   TreeFam; TF350556; -.
DR   ChiTaRS; KLF3; human.
DR   GeneWiki; KLF3; -.
DR   GenomeRNAi; 51274; -.
DR   NextBio; 54481; -.
DR   PRO; PR:P57682; -.
DR   Proteomes; UP000005640; Chromosome 4.
DR   Bgee; P57682; -.
DR   CleanEx; HS_KLF3; -.
DR   ExpressionAtlas; P57682; baseline and differential.
DR   Genevisible; P57682; HS.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; NAS:ProtInc.
DR   GO; GO:1901653; P:cellular response to peptide; IEA:Ensembl.
DR   GO; GO:0007275; P:multicellular organismal development; TAS:ProtInc.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.160.60; -; 3.
DR   InterPro; IPR007087; Znf_C2H2.
DR   InterPro; IPR015880; Znf_C2H2-like.
DR   InterPro; IPR013087; Znf_C2H2/integrase_DNA-bd.
DR   Pfam; PF00096; zf-C2H2; 1.
DR   SMART; SM00355; ZnF_C2H2; 3.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 3.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 3.
PE   1: Evidence at protein level;
KW   Activator; Alternative splicing; Complete proteome; DNA-binding;
KW   Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein; Polymorphism;
KW   Reference proteome; Repeat; Repressor; Transcription;
KW   Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT   CHAIN         1    345       Krueppel-like factor 3.
FT                                /FTId=PRO_0000047165.
FT   ZN_FING     260    284       C2H2-type 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     290    314       C2H2-type 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     320    342       C2H2-type 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   REGION        1     74       Repressor domain.
FT   MOTIF        61     65       CTBP-binding motif.
FT   COMPBIAS      1    251       Pro-rich.
FT   MOD_RES      92     92       Phosphoserine.
FT                                {ECO:0000244|PubMed:18669648,
FT                                ECO:0000244|PubMed:20068231}.
FT   MOD_RES     101    101       Phosphoserine.
FT                                {ECO:0000244|PubMed:18669648}.
FT   MOD_RES     108    108       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q60980}.
FT   MOD_RES     111    111       Phosphoserine.
FT                                {ECO:0000244|PubMed:20068231}.
FT   MOD_RES     216    216       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q60980}.
FT   MOD_RES     224    224       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q60980}.
FT   MOD_RES     250    250       Phosphoserine.
FT                                {ECO:0000244|PubMed:17081983}.
FT   CROSSLNK     10     10       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO).
FT                                {ECO:0000250}.
FT   CROSSLNK    198    198       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:25218447}.
FT   VAR_SEQ     233    345       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_014532.
FT   VARIANT     207    207       R -> S (in dbSNP:rs17616226).
FT                                /FTId=VAR_052715.
FT   CONFLICT     85     85       P -> R (in Ref. 3; AAH51687).
FT                                {ECO:0000305}.
FT   CONFLICT    116    116       P -> H (in Ref. 3; AAH51687).
FT                                {ECO:0000305}.
FT   CONFLICT    305    305       D -> G (in Ref. 3; AAH30662).
FT                                {ECO:0000305}.
SQ   SEQUENCE   345 AA;  38829 MW;  A490D642AB8F1FDC CRC64;
     MLMFDPVPVK QEAMDPVSVS YPSNYMESMK PNKYGVIYST PLPEKFFQTP EGLSHGIQME
     PVDLTVNKRS SPPSAGNSPS SLKFPSSHRR ASPGLSMPSS SPPIKKYSPP SPGVQPFGVP
     LSMPPVMAAA LSRHGIRSPG ILPVIQPVVV QPVPFMYTSH LQQPLMVSLS EEMENSSSSM
     QVPVIESYEK PISQKKIKIE PGIEPQRTDY YPEEMSPPLM NSVSPPQALL QENHPSVIVQ
     PGKRPLPVES PDTQRKRRIH RCDYDGCNKV YTKSSHLKAH RRTHTGEKPY KCTWEGCTWK
     FARSDELTRH FRKHTGIKPF QCPDCDRSFS RSDHLALHRK RHMLV
//
ID   KLF8_HUMAN              Reviewed;         359 AA.
AC   O95600; B4DJN3; E7EQQ8; L0R3U8; L0R4U2; Q2M246; Q59GV5; Q5HYQ5;
AC   Q5JXP7; Q6MZJ7; Q9UGC4;
DT   02-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT   02-NOV-2001, sequence version 2.
DT   11-NOV-2015, entry version 131.
DE   RecName: Full=Krueppel-like factor 8;
DE   AltName: Full=Basic krueppel-like factor 3;
DE   AltName: Full=Zinc finger protein 741;
GN   Name=KLF8; Synonyms=BKLF3, ZNF741;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA   Gorski J.L., MacDonald M., Vananthwerp M., Burright E.N., Bialecki M.;
RL   Submitted (JUN-1995) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3 AND 4), AND ALTERNATIVE
RP   SPLICING.
RX   PubMed=23134681; DOI=10.1096/fj.12-220319;
RA   Camacho-Vanegas O., Till J., Miranda-Lorenzo I., Ozturk B.,
RA   Camacho S.C., Martignetti J.A.;
RT   "Shaking the family tree: Identification of novel and biologically
RT   active alternatively spliced isoforms across the KLF family of
RT   transcription factors.";
RL   FASEB J. 27:432-436(2013).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Thalamus;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
RA   Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA   Ohara O., Nagase T., Kikuno R.F.;
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Uterus;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA   Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA   Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15772651; DOI=10.1038/nature03440;
RA   Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA   Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A.,
RA   Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G.,
RA   Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S.,
RA   Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R.,
RA   Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L.,
RA   Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A.,
RA   Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S.,
RA   Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R.,
RA   Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M.,
RA   Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N.,
RA   Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D.,
RA   Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W.,
RA   Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C.,
RA   Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C.,
RA   Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA   Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA   Corby N., Connor R.E., David R., Davies J., Davis C., Davis J.,
RA   Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S.,
RA   Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I.,
RA   Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L.,
RA   Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P.,
RA   Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S.,
RA   Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A.,
RA   Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J.,
RA   Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J.,
RA   Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S.,
RA   de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z.,
RA   Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C.,
RA   Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W.,
RA   Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA   Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA   McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T.,
RA   Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I.,
RA   Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N.,
RA   Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J.,
RA   Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E.,
RA   Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S.,
RA   Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA   Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA   Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA   Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T.,
RA   Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S.,
RA   Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L.,
RA   Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A.,
RA   Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L.,
RA   Williams G., Williams L., Williamson A., Williamson H., Wilming L.,
RA   Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H.,
RA   Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A.,
RA   Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA   Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A.,
RA   Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T.,
RA   Gibbs R.A., Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence of the human X chromosome.";
RL   Nature 434:325-337(2005).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [8]
RP   FUNCTION, SUBUNIT, AND TISSUE SPECIFICITY.
RX   PubMed=10756197; DOI=10.1093/nar/28.9.1955;
RA   van Vliet J., Turner J., Crossley M.;
RT   "Human Kruppel-like factor 8: a CACCC-box binding protein that
RT   associates with CtBP and represses transcription.";
RL   Nucleic Acids Res. 28:1955-1962(2000).
RN   [9]
RP   FUNCTION.
RX   PubMed=12820964; DOI=10.1016/S1097-2765(03)00179-5;
RA   Zhao J., Bian Z.C., Yee K., Chen B.P., Chien S., Guan J.L.;
RT   "Identification of transcription factor KLF8 as a downstream target of
RT   focal adhesion kinase in its regulation of cyclin D1 and cell cycle
RT   progression.";
RL   Mol. Cell 11:1503-1515(2003).
RN   [10]
RP   SUMOYLATION AT LYS-67, INTERACTION WITH PIAS1; PIAS2 AND PIAS4,
RP   FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF LYS-67 AND LYS-217.
RX   PubMed=16617055; DOI=10.1074/jbc.M513135200;
RA   Wei H., Wang X., Gan B., Urvalek A.M., Melkoumian Z.K., Guan J.-L.,
RA   Zhao J.;
RT   "Sumoylation delimits KLF8 transcriptional activity associated with
RT   the cell cycle regulation.";
RL   J. Biol. Chem. 281:16664-16671(2006).
CC   -!- FUNCTION: Transcriptional repressor and activator. Binds to CACCC-
CC       boxes promoter elements. Also binds the GT-box of cyclin D1
CC       promoter and mediates cell cycle progression at G(1) phase as a
CC       downstream target of focal adhesion kinase (FAK).
CC       {ECO:0000269|PubMed:10756197, ECO:0000269|PubMed:12820964,
CC       ECO:0000269|PubMed:16617055}.
CC   -!- SUBUNIT: Interacts with corepressor CtBP2. Interacts with PIAS1,
CC       PIAS2, AND PIAS4; the interaction with each ligase sumoylates
CC       KLF8. {ECO:0000269|PubMed:10756197, ECO:0000269|PubMed:16617055}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16617055}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=O95600-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=O95600-3; Sequence=VSP_045460;
CC       Name=3;
CC         IsoId=O95600-4; Sequence=VSP_047480, VSP_045460;
CC       Name=4;
CC         IsoId=O95600-5; Sequence=VSP_047481;
CC   -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:10756197}.
CC   -!- PTM: Sumoylation at Lys-67 represses transcriptional activity and
CC       reduces cell cycle progression into the G(1) phase. Has no effect
CC       on subcellular location. {ECO:0000269|PubMed:16617055}.
CC   -!- SIMILARITY: Belongs to the Sp1 C2H2-type zinc-finger protein
CC       family. {ECO:0000305}.
CC   -!- SIMILARITY: Contains 3 C2H2-type zinc fingers.
CC       {ECO:0000255|PROSITE-ProRule:PRU00042}.
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DR   EMBL; U28282; AAC99849.1; -; mRNA.
DR   EMBL; HF546207; CCO02793.1; -; mRNA.
DR   EMBL; HF546208; CCO02794.1; -; mRNA.
DR   EMBL; HF546209; CCO02795.1; -; mRNA.
DR   EMBL; AK296156; BAG58895.1; -; mRNA.
DR   EMBL; AB209004; BAD92241.1; ALT_SEQ; mRNA.
DR   EMBL; BX641066; CAE46033.1; ALT_SEQ; mRNA.
DR   EMBL; BX322609; CAI41397.1; -; Genomic_DNA.
DR   EMBL; AL050309; CAI41397.1; JOINED; Genomic_DNA.
DR   EMBL; AL050309; CAI42343.1; -; Genomic_DNA.
DR   EMBL; BX322609; CAI42343.1; JOINED; Genomic_DNA.
DR   EMBL; BC105130; AAI05131.1; -; mRNA.
DR   EMBL; BC112109; AAI12110.1; -; mRNA.
DR   CCDS; CCDS14373.1; -. [O95600-1]
DR   CCDS; CCDS55428.1; -. [O95600-3]
DR   RefSeq; NP_001152768.1; NM_001159296.1. [O95600-3]
DR   RefSeq; NP_009181.2; NM_007250.4. [O95600-1]
DR   RefSeq; XP_005262034.1; XM_005261977.1. [O95600-1]
DR   RefSeq; XP_005262035.1; XM_005261978.2. [O95600-1]
DR   RefSeq; XP_005262036.1; XM_005261979.2. [O95600-1]
DR   RefSeq; XP_006724638.1; XM_006724575.2. [O95600-3]
DR   RefSeq; XP_011529062.1; XM_011530760.1. [O95600-4]
DR   UniGene; Hs.646614; -.
DR   ProteinModelPortal; O95600; -.
DR   SMR; O95600; 274-356.
DR   BioGrid; 116435; 8.
DR   IntAct; O95600; 1.
DR   MINT; MINT-7969747; -.
DR   STRING; 9606.ENSP00000417303; -.
DR   PhosphoSite; O95600; -.
DR   BioMuta; KLF8; -.
DR   PaxDb; O95600; -.
DR   PRIDE; O95600; -.
DR   DNASU; 11279; -.
DR   Ensembl; ENST00000374928; ENSP00000364063; ENSG00000102349. [O95600-3]
DR   Ensembl; ENST00000468660; ENSP00000417303; ENSG00000102349. [O95600-1]
DR   GeneID; 11279; -.
DR   KEGG; hsa:11279; -.
DR   UCSC; uc004dur.3; human. [O95600-1]
DR   UCSC; uc011mop.2; human.
DR   CTD; 11279; -.
DR   GeneCards; KLF8; -.
DR   HGNC; HGNC:6351; KLF8.
DR   MIM; 300286; gene.
DR   neXtProt; NX_O95600; -.
DR   PharmGKB; PA30141; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   eggNOG; COG5048; LUCA.
DR   GeneTree; ENSGT00760000118998; -.
DR   HOVERGEN; HBG003941; -.
DR   InParanoid; O95600; -.
DR   KO; K09205; -.
DR   OMA; SMLQAPV; -.
DR   OrthoDB; EOG7Z69CW; -.
DR   PhylomeDB; O95600; -.
DR   TreeFam; TF350556; -.
DR   GeneWiki; KLF8; -.
DR   GenomeRNAi; 11279; -.
DR   NextBio; 42937; -.
DR   PRO; PR:O95600; -.
DR   Proteomes; UP000005640; Chromosome X.
DR   Bgee; O95600; -.
DR   CleanEx; HS_KLF8; -.
DR   ExpressionAtlas; O95600; baseline and differential.
DR   Genevisible; O95600; HS.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.160.60; -; 3.
DR   InterPro; IPR007087; Znf_C2H2.
DR   InterPro; IPR015880; Znf_C2H2-like.
DR   InterPro; IPR013087; Znf_C2H2/integrase_DNA-bd.
DR   Pfam; PF00096; zf-C2H2; 1.
DR   SMART; SM00355; ZnF_C2H2; 3.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 3.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 3.
PE   1: Evidence at protein level;
KW   Alternative splicing; Complete proteome; DNA-binding; Isopeptide bond;
KW   Metal-binding; Nucleus; Reference proteome; Repeat; Repressor;
KW   Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW   Zinc-finger.
FT   CHAIN         1    359       Krueppel-like factor 8.
FT                                /FTId=PRO_0000047176.
FT   ZN_FING     274    298       C2H2-type 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     304    328       C2H2-type 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     334    356       C2H2-type 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   CROSSLNK     67     67       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO).
FT   VAR_SEQ       1     27       MVDMDKLINNLEVQLNSEGGSMQVFKQ -> MSLPEDGMSS
FT                                GHFRSPQLVTWS (in isoform 3).
FT                                {ECO:0000303|PubMed:23134681}.
FT                                /FTId=VSP_047480.
FT   VAR_SEQ     216    299       Missing (in isoform 4).
FT                                {ECO:0000303|PubMed:23134681}.
FT                                /FTId=VSP_047481.
FT   VAR_SEQ     254    359       PAAMAQMQGEESLDLKRRRIHQCDFAGCSKVYTKSSHLKAH
FT                                RRIHTGEKPYKCTWDGCSWKFARSDELTRHFRKHTGIKPFR
FT                                CTDCNRSFSRSDHLSLHRRRHDTM -> REAL (in
FT                                isoform 2 and isoform 3).
FT                                {ECO:0000303|PubMed:14702039,
FT                                ECO:0000303|PubMed:23134681}.
FT                                /FTId=VSP_045460.
FT   MUTAGEN      67     67       K->R: Abolishes sumoylation. No change in
FT                                nuclear location. Increases
FT                                transcriptional activity and cell cycle
FT                                progression. Abolishes sumoylation; when
FT                                associated with R-217.
FT                                {ECO:0000269|PubMed:16617055}.
FT   MUTAGEN     217    217       K->R: No change in sumoylation. Abolishes
FT                                sumoylation; when associated with R-67.
FT                                {ECO:0000269|PubMed:16617055}.
FT   CONFLICT    167    167       S -> I (in Ref. 3; BAG58895).
FT                                {ECO:0000305}.
FT   CONFLICT    263    263       E -> G (in Ref. 1; AAC99849).
FT                                {ECO:0000305}.
SQ   SEQUENCE   359 AA;  39314 MW;  F8FDCC1FD477C04F CRC64;
     MVDMDKLINN LEVQLNSEGG SMQVFKQVTA SVRNRDPPEI EYRSNMTSPT LLDANPMENP
     ALFNDIKIEP PEELLASDFS LPQVEPVDLS FHKPKAPLQP ASMLQAPIRP PKPQSSPQTL
     VVSTSTSDMS TSANIPTVLT PGSVLTSSQS TGSQQILHVI HTIPSVSLPN KMGGLKTIPV
     VVQSLPMVYT TLPADGGPAA ITVPLIGGDG KNAGSVKVDP TSMSPLEIPS DSEESTIESG
     SSALQSLQGL QQEPAAMAQM QGEESLDLKR RRIHQCDFAG CSKVYTKSSH LKAHRRIHTG
     EKPYKCTWDG CSWKFARSDE LTRHFRKHTG IKPFRCTDCN RSFSRSDHLS LHRRRHDTM
//
ID   KNIR_DROME              Reviewed;         429 AA.
AC   P10734; Q540X6; Q9VPC6;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   11-NOV-2015, entry version 149.
DE   RecName: Full=Zygotic gap protein knirps;
DE   AltName: Full=Nuclear receptor subfamily 0 group A member 1;
GN   Name=kni; Synonyms=NR0A1; ORFNames=CG4717;
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
OC   Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha;
OC   Ephydroidea; Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Oregon-R; TISSUE=Salivary gland;
RX   PubMed=2904128; DOI=10.1038/336489a0;
RA   Nauber U., Pankratz M.J., Kilnlin A., Seyffert E., Klemm U.,
RA   Jackle H.;
RT   "Abdominal segmentation of the Drosophila embryo requires a hormone
RT   receptor-like protein encoded by the gap gene knirps.";
RL   Nature 336:489-492(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley;
RX   PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA   Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA   Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA   George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA   Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
RA   Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
RA   Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
RA   Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
RA   Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
RA   Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
RA   Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
RA   Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
RA   Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
RA   de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
RA   Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
RA   Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
RA   Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
RA   Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
RA   Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
RA   Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
RA   Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
RA   Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
RA   Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
RA   Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
RA   Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
RA   Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
RA   Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
RA   Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
RA   Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA   Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
RA   Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
RA   Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
RA   Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
RA   Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
RA   Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
RA   Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=Berkeley;
RX   PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
RA   Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
RA   Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a
RT   systematic review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Berkeley; TISSUE=Head;
RX   PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA   Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M.,
RA   George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H.,
RA   Rubin G.M., Celniker S.E.;
RT   "A Drosophila full-length cDNA resource.";
RL   Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN   [5]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=8670869;
RA   Arnosti D.N., Gray S., Barolo S., Zhou J., Levine M.;
RT   "The gap protein knirps mediates both quenching and direct repression
RT   in the Drosophila embryo.";
RL   EMBO J. 15:3659-3666(1996).
CC   -!- FUNCTION: Transcriptional repressor. Binds to multiple sites in
CC       the eve stripe 3 enhancer element. Plays an essential role in the
CC       segmentation process both by refining the expression patterns of
CC       gap genes and by establishing pair-rules stripes of gene
CC       expression. {ECO:0000269|PubMed:8670869}.
CC   -!- INTERACTION:
CC       O46036:CtBP; NbExp=2; IntAct=EBI-170297, EBI-159330;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-
CC       ProRule:PRU00407, ECO:0000269|PubMed:8670869}.
CC   -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR0
CC       subfamily. {ECO:0000305}.
CC   -!- SIMILARITY: Contains 1 nuclear receptor DNA-binding domain.
CC       {ECO:0000255|PROSITE-ProRule:PRU00407}.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; X13331; CAA31709.1; -; Genomic_DNA.
DR   EMBL; AE014296; AAF51629.2; -; Genomic_DNA.
DR   EMBL; AY118798; AAM50658.1; -; mRNA.
DR   PIR; S01919; S01919.
DR   RefSeq; NP_524187.1; NM_079463.3.
DR   UniGene; Dm.2511; -.
DR   ProteinModelPortal; P10734; -.
DR   SMR; P10734; 5-72.
DR   BioGrid; 65544; 13.
DR   DIP; DIP-17716N; -.
DR   IntAct; P10734; 6.
DR   MINT; MINT-750168; -.
DR   STRING; 7227.FBpp0077941; -.
DR   PaxDb; P10734; -.
DR   PRIDE; P10734; -.
DR   GeneID; 40287; -.
DR   CTD; 40287; -.
DR   FlyBase; FBgn0001320; kni.
DR   eggNOG; ENOG410IXHB; Eukaryota.
DR   eggNOG; ENOG4111HXR; LUCA.
DR   InParanoid; P10734; -.
DR   OMA; MSKGGSR; -.
DR   OrthoDB; EOG7KDF9R; -.
DR   PhylomeDB; P10734; -.
DR   SignaLink; P10734; -.
DR   GenomeRNAi; 40287; -.
DR   NextBio; 817990; -.
DR   PRO; PR:P10734; -.
DR   Proteomes; UP000000803; Chromosome 3L.
DR   Bgee; P10734; -.
DR   ExpressionAtlas; P10734; differential.
DR   Genevisible; P10734; DM.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0070491; F:repressing transcription factor binding; IPI:FlyBase.
DR   GO; GO:0004879; F:RNA polymerase II transcription factor activity, ligand-activated sequence-specific DNA binding; NAS:FlyBase.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR   GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IDA:FlyBase.
DR   GO; GO:0001078; F:transcriptional repressor activity, RNA polymerase II core promoter proximal region sequence-specific binding; IDA:FlyBase.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0046845; P:branched duct epithelial cell fate determination, open tracheal system; TAS:FlyBase.
DR   GO; GO:0048813; P:dendrite morphogenesis; IMP:FlyBase.
DR   GO; GO:0008544; P:epidermis development; IMP:FlyBase.
DR   GO; GO:0007427; P:epithelial cell migration, open tracheal system; TAS:FlyBase.
DR   GO; GO:0030522; P:intracellular receptor signaling pathway; NAS:GOC.
DR   GO; GO:0007517; P:muscle organ development; IMP:FlyBase.
DR   GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; TAS:FlyBase.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:FlyBase.
DR   GO; GO:0007424; P:open tracheal system development; TAS:FlyBase.
DR   GO; GO:0007088; P:regulation of mitotic nuclear division; IMP:FlyBase.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:FlyBase.
DR   GO; GO:0035151; P:regulation of tube size, open tracheal system; TAS:FlyBase.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
DR   GO; GO:0035290; P:trunk segmentation; TAS:FlyBase.
DR   GO; GO:0007354; P:zygotic determination of anterior/posterior axis, embryo; NAS:FlyBase.
DR   Gene3D; 3.30.50.10; -; 1.
DR   InterPro; IPR001628; Znf_hrmn_rcpt.
DR   InterPro; IPR013088; Znf_NHR/GATA.
DR   Pfam; PF00105; zf-C4; 1.
DR   PRINTS; PR00047; STROIDFINGER.
DR   SMART; SM00399; ZnF_C4; 1.
DR   PROSITE; PS00031; NUCLEAR_REC_DBD_1; 1.
DR   PROSITE; PS51030; NUCLEAR_REC_DBD_2; 1.
PE   1: Evidence at protein level;
KW   Complete proteome; Developmental protein; DNA-binding; Metal-binding;
KW   Nucleus; Receptor; Reference proteome; Repressor; Transcription;
KW   Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN         1    429       Zygotic gap protein knirps.
FT                                /FTId=PRO_0000053743.
FT   DNA_BIND      2     78       Nuclear receptor. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00407}.
FT   ZN_FING       5     25       NR C4-type. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00407}.
FT   ZN_FING      42     66       NR C4-type. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00407}.
FT   COMPBIAS     97    101       Poly-Ala.
FT   COMPBIAS    137    142       Poly-His.
FT   COMPBIAS    143    149       Poly-Gln.
FT   COMPBIAS    200    213       Poly-Ala.
FT   COMPBIAS    375    382       Poly-Ser.
SQ   SEQUENCE   429 AA;  45611 MW;  79CEE86A66AB00C7 CRC64;
     MNQTCKVCGE PAAGFHFGAF TCEGCKSFFG RSYNNISTIS ECKNEGKCII DKKNRTTCKA
     CRLRKCYNVG MSKGGSRYGR RSNWFKIHCL LQEHEQAAAA AGKAPPLAGG VSVGGAPSAS
     SPVGSPHTPG FGDMAAHLHH HHQQQQQQQV PRHPHMPLLG YPSYLSDPSA ALPFFSMMGG
     VPHQSPFQLP PHLLFPGYHA SAAAAAASAA DAAYRQEMYK HRQSVDSVES QNRFSPASQP
     PVVQPTSSAR QSPIDVCLEE DVHSVHSHQS SASLLHPIAI RATPTTPTSS SPLSFAAKMQ
     SLSPVSVCSI GGETTSVVPV HPPTVSAQEG PMDLSMKTSR SSVHSFNDSG SEDQEVEVAP
     RRKFYQLEAE CLTTSSSSSS HSAAHSPNTT TAHAEVKRQK LGGAEATHFG GFAVAHNAAS
     AMRGIFVCV
//
ID   LCOR_HUMAN              Reviewed;         433 AA.
AC   Q96JN0; D3DR47; Q5VW16; Q7Z723; Q86T32; Q86T33; Q8N3L6;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2006, sequence version 2.
DT   11-NOV-2015, entry version 103.
DE   RecName: Full=Ligand-dependent corepressor;
DE            Short=LCoR;
DE   AltName: Full=Mblk1-related protein 2;
GN   Name=LCOR; Synonyms=KIAA1795, MLR2;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
RX   PubMed=11347906; DOI=10.1093/dnares/8.2.85;
RA   Nagase T., Nakayama M., Nakajima D., Kikuno R., Ohara O.;
RT   "Prediction of the coding sequences of unidentified human genes. XX.
RT   The complete sequences of 100 new cDNA clones from brain which code
RT   for large proteins in vitro.";
RL   DNA Res. 8:85-95(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Bone marrow, and Skeletal muscle;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA   Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA   Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15164054; DOI=10.1038/nature02462;
RA   Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA   Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA   Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA   Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA   Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J.,
RA   Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
RA   Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA   Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
RA   Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
RA   Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
RA   Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
RA   Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
RA   Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
RA   Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
RA   Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
RA   Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
RA   Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
RA   Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
RA   Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA   Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
RA   Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
RA   Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
RA   Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
RA   Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
RA   Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT   "The DNA sequence and comparative analysis of human chromosome 10.";
RL   Nature 429:375-381(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Lung;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   FUNCTION, INTERACTION WITH CTBP1; ESR1; ESR2; HDAC3 AND HDAC6,
RP   SUBCELLULAR LOCATION, MUTAGENESIS OF 56-LEU-LEU-57, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=12535528; DOI=10.1016/S1097-2765(03)00014-5;
RA   Fernandes I., Bastien Y., Wai T., Nygard K., Lin R., Cormier O.,
RA   Lee H.S., Eng F., Bertos N.R., Pelletier N., Mader S., Han V.K.M.,
RA   Yang X.-J., White J.H.;
RT   "Ligand-dependent nuclear receptor corepressor LCoR functions by
RT   histone deacetylase-dependent and -independent mechanisms.";
RL   Mol. Cell 11:139-150(2003).
RN   [7]
RP   IDENTIFICATION IN A COREPRESSOR COMPLEX, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RX   PubMed=12700765; DOI=10.1038/nature01550;
RA   Shi Y., Sawada J., Sui G., Affar E.B., Whetstine J.R., Lan F.,
RA   Ogawa H., Luke M.P.-S., Nakatani Y., Shi Y.;
RT   "Coordinated histone modifications mediated by a CtBP co-repressor
RT   complex.";
RL   Nature 422:735-738(2003).
RN   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [9]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA   Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT   a refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-63 AND SER-249, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA   Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full
RT   phosphorylation site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [11]
RP   STRUCTURE BY NMR OF 343-405.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structures of the HTH domain of human LCOR protein.";
RL   Submitted (NOV-2005) to the PDB data bank.
CC   -!- FUNCTION: May act as transcription activator that binds DNA
CC       elements with the sequence 5'-CCCTATCGATCGATCTCTACCT-3' (By
CC       similarity). Repressor of ligand-dependent transcription
CC       activation by target nuclear receptors. Repressor of ligand-
CC       dependent transcription activation by ESR1, ESR2, NR3C1, PGR,
CC       RARA, RARB, RARG, RXRA and VDR. {ECO:0000250,
CC       ECO:0000269|PubMed:12535528}.
CC   -!- SUBUNIT: Interacts with ESR1 and ESR2 in the presence of
CC       estradiol. Interacts with CTBP1, HDAC3 and HDAC6. Component of a
CC       large corepressor complex that contains about 20 proteins,
CC       including CTBP1, CTBP2, HDAC1 and HDAC2.
CC       {ECO:0000269|PubMed:12535528, ECO:0000269|PubMed:12700765}.
CC   -!- INTERACTION:
CC       P56545:CTBP2; NbExp=3; IntAct=EBI-8833163, EBI-741533;
CC       Q8IY44:CTBP2; NbExp=3; IntAct=EBI-8833163, EBI-10171902;
CC       Q08379:GOLGA2; NbExp=3; IntAct=EBI-8833163, EBI-618309;
CC       Q13077:TRAF1; NbExp=3; IntAct=EBI-8833163, EBI-359224;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-
CC       ProRule:PRU00320, ECO:0000269|PubMed:12535528}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q96JN0-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q96JN0-2; Sequence=VSP_018585, VSP_018586;
CC   -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:12535528}.
CC   -!- SIMILARITY: Contains 1 HTH psq-type DNA-binding domain.
CC       {ECO:0000255|PROSITE-ProRule:PRU00320}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB47424.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; AB058698; BAB47424.1; ALT_INIT; mRNA.
DR   EMBL; AL834245; CAD38921.2; -; mRNA.
DR   EMBL; AL832106; CAD91159.1; -; mRNA.
DR   EMBL; AL832044; CAD91160.1; -; mRNA.
DR   EMBL; AL442123; CAH70915.1; -; Genomic_DNA.
DR   EMBL; CH471066; EAW49963.1; -; Genomic_DNA.
DR   EMBL; CH471066; EAW49965.1; -; Genomic_DNA.
DR   EMBL; CH471066; EAW49966.1; -; Genomic_DNA.
DR   EMBL; BC053359; AAH53359.1; -; mRNA.
DR   CCDS; CCDS53561.1; -. [Q96JN0-2]
DR   CCDS; CCDS7451.1; -. [Q96JN0-1]
DR   RefSeq; NP_001164236.1; NM_001170765.1. [Q96JN0-1]
DR   RefSeq; NP_001164237.1; NM_001170766.1. [Q96JN0-2]
DR   RefSeq; NP_115816.2; NM_032440.3. [Q96JN0-1]
DR   RefSeq; XP_006718097.1; XM_006718034.2. [Q96JN0-1]
DR   UniGene; Hs.745068; -.
DR   PDB; 2COB; NMR; -; A=343-405.
DR   PDBsum; 2COB; -.
DR   ProteinModelPortal; Q96JN0; -.
DR   SMR; Q96JN0; 346-405.
DR   BioGrid; 124093; 23.
DR   IntAct; Q96JN0; 4.
DR   STRING; 9606.ENSP00000348298; -.
DR   PhosphoSite; Q96JN0; -.
DR   BioMuta; LCOR; -.
DR   DMDM; 108936028; -.
DR   MaxQB; Q96JN0; -.
DR   PaxDb; Q96JN0; -.
DR   PRIDE; Q96JN0; -.
DR   DNASU; 84458; -.
DR   Ensembl; ENST00000356016; ENSP00000348298; ENSG00000196233. [Q96JN0-1]
DR   Ensembl; ENST00000371097; ENSP00000360138; ENSG00000196233. [Q96JN0-1]
DR   Ensembl; ENST00000371103; ENSP00000360144; ENSG00000196233. [Q96JN0-1]
DR   Ensembl; ENST00000540664; ENSP00000443431; ENSG00000196233. [Q96JN0-2]
DR   GeneID; 84458; -.
DR   KEGG; hsa:84458; -.
DR   UCSC; uc001kmr.3; human. [Q96JN0-2]
DR   UCSC; uc001kms.2; human. [Q96JN0-1]
DR   CTD; 84458; -.
DR   GeneCards; LCOR; -.
DR   HGNC; HGNC:29503; LCOR.
DR   HPA; HPA031428; -.
DR   HPA; HPA031429; -.
DR   MIM; 607698; gene.
DR   neXtProt; NX_Q96JN0; -.
DR   PharmGKB; PA145148487; -.
DR   eggNOG; KOG4565; Eukaryota.
DR   eggNOG; ENOG4111GCI; LUCA.
DR   GeneTree; ENSGT00520000055615; -.
DR   HOVERGEN; HBG079596; -.
DR   InParanoid; Q96JN0; -.
DR   OMA; HYEFNFS; -.
DR   OrthoDB; EOG73RBBB; -.
DR   PhylomeDB; Q96JN0; -.
DR   TreeFam; TF319589; -.
DR   ChiTaRS; LCOR; human.
DR   EvolutionaryTrace; Q96JN0; -.
DR   GeneWiki; LCOR; -.
DR   GenomeRNAi; 84458; -.
DR   NextBio; 74251; -.
DR   PRO; PR:Q96JN0; -.
DR   Proteomes; UP000005640; Chromosome 10.
DR   Bgee; Q96JN0; -.
DR   CleanEx; HS_LCOR; -.
DR   Genevisible; Q96JN0; HS.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IEA:Ensembl.
DR   GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IEA:Ensembl.
DR   GO; GO:0006366; P:transcription from RNA polymerase II promoter; IEA:Ensembl.
DR   InterPro; IPR009057; Homeodomain-like.
DR   InterPro; IPR007889; HTH_Psq.
DR   Pfam; PF05225; HTH_psq; 1.
DR   SUPFAM; SSF46689; SSF46689; 1.
DR   PROSITE; PS50960; HTH_PSQ; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Activator; Alternative splicing; Complete proteome;
KW   DNA-binding; Nucleus; Phosphoprotein; Reference proteome; Repressor;
KW   Transcription; Transcription regulation.
FT   CHAIN         1    433       Ligand-dependent corepressor.
FT                                /FTId=PRO_0000236807.
FT   DOMAIN      340    392       HTH psq-type. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00320}.
FT   DNA_BIND    368    388       H-T-H motif. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00320}.
FT   MOTIF        53     57       Interaction with nuclear receptors.
FT   MOTIF       339    345       Nuclear localization signal.
FT                                {ECO:0000255}.
FT   MOD_RES      63     63       Phosphoserine.
FT                                {ECO:0000244|PubMed:20068231}.
FT   MOD_RES     249    249       Phosphoserine.
FT                                {ECO:0000244|PubMed:20068231}.
FT   VAR_SEQ     405    406       RS -> SG (in isoform 2).
FT                                {ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_018585.
FT   VAR_SEQ     407    433       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_018586.
FT   MUTAGEN      56     57       LL->AA: Loss of estradiol-dependent
FT                                interaction with ESR1 and ESR2.
FT                                {ECO:0000269|PubMed:12535528}.
FT   CONFLICT      6      6       Q -> P (in Ref. 2; CAD91159).
FT                                {ECO:0000305}.
FT   CONFLICT    321    321       S -> P (in Ref. 2; CAD38921).
FT                                {ECO:0000305}.
FT   HELIX       351    362       {ECO:0000244|PDB:2COB}.
FT   HELIX       368    375       {ECO:0000244|PDB:2COB}.
FT   HELIX       379    389       {ECO:0000244|PDB:2COB}.
FT   TURN        390    393       {ECO:0000244|PDB:2COB}.
SQ   SEQUENCE   433 AA;  47007 MW;  5F934FE687417740 CRC64;
     MQRMIQQFAA EYTSKNSSTQ DPSQPNSTKN QSLPKASPVT TSPTAATTQN PVLSKLLMAD
     QDSPLDLTVR KSQSEPSEQD GVLDLSTKKS PCAGSTSLSH SPGCSSTQGN GRPGRPSQYR
     PDGLRSGDGV PPRSLQDGTR EGFGHSTSLK VPLARSLQIS EELLSRNQLS TAASLGPSGL
     QNHGQHLILS REASWAKPHY EFNLSRMKFR GNGALSNISD LPFLAENSAF PKMALQAKQD
     GKKDVSHSSP VDLKIPQVRG MDLSWESRTG DQYSYSSLVM GSQTESALSK KLRAILPKQS
     RKSMLDAGPD SWGSDAEQST SGQPYPTSDQ EGDPGSKQPR KKRGRYRQYN SEILEEAISV
     VMSGKMSVSK AQSIYGIPHS TLEYKVKERL GTLKNPPKKK MKLMRSEGPD VSVKIELDPQ
     GEAAQSANES KNE
//
ID   NRIP1_HUMAN             Reviewed;        1158 AA.
AC   P48552; Q8IWE8;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 2.
DT   11-NOV-2015, entry version 140.
DE   RecName: Full=Nuclear receptor-interacting protein 1;
DE   AltName: Full=Nuclear factor RIP140;
DE   AltName: Full=Receptor-interacting protein 140;
GN   Name=NRIP1;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH ESR1,
RP   SUBCELLULAR LOCATION, AND VARIANT GLY-448.
RC   TISSUE=Mammary gland;
RX   PubMed=7641693;
RA   Cavailles V., Dauvois S., L'Horset F., Lopez G., Hoare S.,
RA   Kushner P.J., Parker M.G.;
RT   "Nuclear factor RIP140 modulates transcriptional activation by the
RT   estrogen receptor.";
RL   EMBO J. 14:3741-3751(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=10830953; DOI=10.1038/35012518;
RA   Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T.,
RA   Park H.-S., Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y.,
RA   Soeda E., Ohki M., Takagi T., Sakaki Y., Taudien S., Blechschmidt K.,
RA   Polley A., Menzel U., Delabar J., Kumpf K., Lehmann R., Patterson D.,
RA   Reichwald K., Rump A., Schillhabel M., Schudy A., Zimmermann W.,
RA   Rosenthal A., Kudoh J., Shibuya K., Kawasaki K., Asakawa S.,
RA   Shintani A., Sasaki T., Nagamine K., Mitsuyama S., Antonarakis S.E.,
RA   Minoshima S., Shimizu N., Nordsiek G., Hornischer K., Brandt P.,
RA   Scharfe M., Schoen O., Desario A., Reichelt J., Kauer G., Bloecker H.,
RA   Ramser J., Beck A., Klages S., Hennig S., Riesselmann L., Dagand E.,
RA   Wehrmeyer S., Borzym K., Gardiner K., Nizetic D., Francis F.,
RA   Lehrach H., Reinhardt R., Yaspo M.-L.;
RT   "The DNA sequence of human chromosome 21.";
RL   Nature 405:311-319(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Skin;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   INTERACTION WITH NR2C2.
RX   PubMed=9556573; DOI=10.1074/jbc.273.18.10948;
RA   Yan Z.H., Karam W.G., Staudinger J.L., Medvedev A., Ghanayem B.I.,
RA   Jetten A.M.;
RT   "Regulation of peroxisome proliferator-activated receptor alpha-
RT   induced transactivation by the nuclear orphan receptor TAK1/TR4.";
RL   J. Biol. Chem. 273:10948-10957(1998).
RN   [5]
RP   FUNCTION, AND INTERACTION WITH NR3C1.
RX   PubMed=10364267; DOI=10.1074/jbc.274.25.18121;
RA   Subramaniam N., Treuter E., Okret S.;
RT   "Receptor interacting protein RIP140 inhibits both positive and
RT   negative gene regulation by glucocorticoids.";
RL   J. Biol. Chem. 274:18121-18127(1999).
RN   [6]
RP   FUNCTION, INTERACTION WITH CTBP1, MUTAGENESIS OF 440-PRO--LEU-443 AND
RP   LYS-446, AND ACETYLATION AT LYS-446.
RX   PubMed=11509661; DOI=10.1128/MCB.21.18.6181-6188.2001;
RA   Vo N., Fjeld C., Goodman R.H.;
RT   "Acetylation of nuclear hormone receptor-interacting protein RIP140
RT   regulates binding of the transcriptional corepressor CtBP.";
RL   Mol. Cell. Biol. 21:6181-6188(2001).
RN   [7]
RP   INTERACTION WITH NR3C1 AND YWHAH, IDENTIFICATION IN A COMPLEX WITH
RP   NR3C1 AND YWHAH, AND SUBCELLULAR LOCATION.
RX   PubMed=11266503; DOI=10.1210/me.15.4.501;
RA   Zilliacus J., Holter E., Wakui H., Tazawa H., Treuter E.,
RA   Gustafsson J.-A.;
RT   "Regulation of glucocorticoid receptor activity by 14-3-3-dependent
RT   intracellular relocalization of the corepressor RIP140.";
RL   Mol. Endocrinol. 15:501-511(2001).
RN   [8]
RP   FUNCTION, AND INTERACTION WITH NR3C2.
RX   PubMed=11518808; DOI=10.1210/me.15.9.1586;
RA   Zennaro M.-C., Souque A., Viengchareun S., Poisson E., Lombes M.;
RT   "A new human MR splice variant is a ligand-independent transactivator
RT   modulating corticosteroid action.";
RL   Mol. Endocrinol. 15:1586-1598(2001).
RN   [9]
RP   INTERACTION WITH NR3C1, AND SUBCELLULAR LOCATION.
RX   PubMed=12773562; DOI=10.1128/MCB.23.12.4187-4198.2003;
RA   Tazawa H., Osman W., Shoji Y., Treuter E., Gustafsson J.-A.,
RA   Zilliacus J.;
RT   "Regulation of subnuclear localization is associated with a mechanism
RT   for nuclear receptor corepression by RIP140.";
RL   Mol. Cell. Biol. 23:4187-4198(2003).
RN   [10]
RP   FUNCTION, AND INTERACTION WITH ESR1; FOS AND JUN.
RX   PubMed=12554755; DOI=10.1210/me.2002-0324;
RA   Teyssier C., Belguise K., Galtier F., Cavailles V., Chalbos D.;
RT   "Receptor-interacting protein 140 binds c-Jun and inhibits estradiol-
RT   induced activator protein-1 activity by reversing glucocorticoid
RT   receptor-interacting protein 1 effect.";
RL   Mol. Endocrinol. 17:287-299(2003).
RN   [11]
RP   INTERACTION WITH CTBP1 AND CTBP2, MUTAGENESIS OF 442-ASP--LEU-443;
RP   567-ASN--LEU-568 AND 948-ASP--LEU-949, AND IDENTIFICATION OF
RP   REPRESSION DOMAINS.
RX   PubMed=14736873; DOI=10.1074/jbc.M313906200;
RA   Christian M., Tullet J.M.A., Parker M.G.;
RT   "Characterization of four autonomous repression domains in the
RT   corepressor receptor interacting protein 140.";
RL   J. Biol. Chem. 279:15645-15651(2004).
RN   [12]
RP   FUNCTION, INTERACTION WITH CTBP1; CTBP2; HDAC1; HDAC2; HDAC5 AND
RP   HDAC6, MUTAGENESIS OF 442-ASP--LEU-443 AND 567-ASN--LEU-568, AND
RP   SUBCELLULAR LOCATION.
RX   PubMed=15060175; DOI=10.1093/nar/gkh524;
RA   Castet A., Boulahtouf A., Versini G., Bonnet S., Augereau P.,
RA   Vignon F., Khochbin S., Jalaguier S., Cavailles V.;
RT   "Multiple domains of the receptor-interacting protein 140 contribute
RT   to transcription inhibition.";
RL   Nucleic Acids Res. 32:1957-1966(2004).
RN   [13]
RP   INTERACTION WITH NR2C2.
RX   PubMed=16887930; DOI=10.1074/mcp.M600180-MCP200;
RA   Huq M.D., Gupta P., Tsai N.P., Wei L.N.;
RT   "Modulation of testicular receptor 4 activity by mitogen-activated
RT   protein kinase-mediated phosphorylation.";
RL   Mol. Cell. Proteomics 5:2072-2082(2006).
RN   [14]
RP   INTERACTION WITH ZNF366.
RX   PubMed=17085477; DOI=10.1093/nar/gkl875;
RA   Lopez-Garcia J., Periyasamy M., Thomas R.S., Christian M., Leao M.,
RA   Jat P., Kindle K.B., Heery D.M., Parker M.G., Buluwela L.,
RA   Kamalati T., Ali S.;
RT   "ZNF366 is an estrogen receptor corepressor that acts through CtBP and
RT   histone deacetylases.";
RL   Nucleic Acids Res. 34:6126-6136(2006).
RN   [15]
RP   FUNCTION, INTERACTION WITH RORA, AND INDUCTION.
RX   PubMed=21628546; DOI=10.1177/0748730411401579;
RA   Poliandri A.H., Gamsby J.J., Christian M., Spinella M.J., Loros J.J.,
RA   Dunlap J.C., Parker M.G.;
RT   "Modulation of clock gene expression by the transcriptional
RT   coregulator receptor interacting protein 140 (RIP140).";
RL   J. Biol. Rhythms 26:187-199(2011).
RN   [16]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218; SER-671 AND
RP   SER-807, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
RA   Wang L., Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human
RT   liver phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [17]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-756 AND LYS-1105, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25218447; DOI=10.1038/nsmb.2890;
RA   Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA   Vertegaal A.C.;
RT   "Uncovering global SUMOylation signaling networks in a site-specific
RT   manner.";
RL   Nat. Struct. Mol. Biol. 21:927-936(2014).
RN   [18]
RP   X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 366-390 IN COMPLEX WITH
RP   ESRRG.
RX   PubMed=16990259; DOI=10.1074/jbc.M608410200;
RA   Wang L., Zuercher W.J., Consler T.G., Lambert M.H., Miller A.B.,
RA   Orband-Miller L.A., McKee D.D., Willson T.M., Nolte R.T.;
RT   "X-ray crystal structures of the estrogen-related receptor-gamma
RT   ligand binding domain in three functional states reveal the molecular
RT   basis of small molecule regulation.";
RL   J. Biol. Chem. 281:37773-37781(2006).
RN   [19]
RP   VARIANTS ARG-221; VAL-441; GLY-448; LEU-803 AND PHE-1079.
RX   PubMed=16131398; DOI=10.1186/1743-1050-2-11;
RA   Caballero V., Ruiz R., Sainz J.A., Cruz M., Lopez-Nevot M.A.,
RA   Galan J.J., Real L.M., de Castro F., Lopez-Villaverde V., Ruiz A.;
RT   "Preliminary molecular genetic analysis of the receptor interacting
RT   protein 140 (RIP140) in women affected by endometriosis.";
RL   J. Exp. Clin. Assist. Reprod. 2:11-11(2005).
CC   -!- FUNCTION: Modulates transcriptional activation by steroid
CC       receptors such as NR3C1, NR3C2 and ESR1. Also modulates
CC       transcriptional repression by nuclear hormone receptors. Positive
CC       regulator of the circadian clock gene expression: stimulates
CC       transcription of ARNTL/BMAL1, CLOCK and CRY1 by acting as a
CC       coactivator for RORA and RORC. {ECO:0000269|PubMed:10364267,
CC       ECO:0000269|PubMed:11509661, ECO:0000269|PubMed:11518808,
CC       ECO:0000269|PubMed:12554755, ECO:0000269|PubMed:15060175,
CC       ECO:0000269|PubMed:21628546, ECO:0000269|PubMed:7641693}.
CC   -!- SUBUNIT: Interacts with RARA and RXRB homodimers and RARA/RXRB
CC       heterodimers in the presence of ligand. Interacts with HDAC1 and
CC       HDAC3 via its N-terminal domain. Interacts with NR2C1 (sumoylated
CC       form and via the ligand-binding domain); the interaction results
CC       in promoting the repressor activity of NR2C1 (By similarity).
CC       Interacts with CTBP1, CTBP2, ESR1, HDAC1, HDAC2, HDAC5, HDAC6,
CC       NR2C2, NR3C1, NR3C2, YWHAH, JUN and FOS. Found in a complex with
CC       both NR3C1 and YWHAH. Interacts with ZNF366. Interacts with RORA.
CC       {ECO:0000250|UniProtKB:Q8CBD1, ECO:0000269|PubMed:10364267,
CC       ECO:0000269|PubMed:11266503, ECO:0000269|PubMed:11509661,
CC       ECO:0000269|PubMed:11518808, ECO:0000269|PubMed:12554755,
CC       ECO:0000269|PubMed:12773562, ECO:0000269|PubMed:14736873,
CC       ECO:0000269|PubMed:15060175, ECO:0000269|PubMed:16887930,
CC       ECO:0000269|PubMed:16990259, ECO:0000269|PubMed:17085477,
CC       ECO:0000269|PubMed:21628546, ECO:0000269|PubMed:7641693,
CC       ECO:0000269|PubMed:9556573}.
CC   -!- INTERACTION:
CC       O15145:ARPC3; NbExp=3; IntAct=EBI-746484, EBI-351829;
CC       Q8NHQ1:CEP70; NbExp=3; IntAct=EBI-746484, EBI-739624;
CC       P26358:DNMT1; NbExp=3; IntAct=EBI-746484, EBI-719459;
CC       Q13642:FHL1; NbExp=6; IntAct=EBI-746484, EBI-912547;
CC       O15379:HDAC3; NbExp=2; IntAct=EBI-746484, EBI-607682;
CC       O95751:LDOC1; NbExp=3; IntAct=EBI-746484, EBI-740738;
CC       Q99873:PRMT1; NbExp=4; IntAct=EBI-746484, EBI-78738;
CC       P10276:RARA; NbExp=4; IntAct=EBI-746484, EBI-413374;
CC       P10276-2:RARA; NbExp=3; IntAct=EBI-746484, EBI-10197061;
CC       Q8N895:ZNF366; NbExp=2; IntAct=EBI-746484, EBI-2813661;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11266503,
CC       ECO:0000269|PubMed:12773562, ECO:0000269|PubMed:15060175,
CC       ECO:0000269|PubMed:7641693}. Note=Localized to discrete foci and
CC       redistributes to larger nuclear domains upon binding to ligand-
CC       bound NR3C1.
CC   -!- INDUCTION: Expressed in a circadian manner in the liver (at
CC       protein level). {ECO:0000269|PubMed:21628546}.
CC   -!- DOMAIN: Contains 9 Leu-Xaa-Xaa-Leu-Leu (LXXLL) motifs, which have
CC       different affinities for nuclear receptors. The C-terminal
CC       LTKTNPILYYMLQK motif is required for ligand-dependent interaction
CC       with RAAR and RXRB homodimers and heterodimers, for the
CC       corepressor activity, and for the formation of an HDAC3 complex
CC       with RARA/RXRB (By similarity). Contains at least four autonomous
CC       repression domains (RD1-4). RD1 functions via a histone
CC       deacetylase (HDAC)-independent mechanism, whereas RD2, RD3 and RD4
CC       can function by HDAC-dependent or independent mechanisms,
CC       depending on cell type. RD2 is dependent on CTBP binding.
CC       {ECO:0000250}.
CC   -!- PTM: Acetylation regulates its nuclear translocation and
CC       corepressive activity (By similarity). Acetylation abolishes
CC       interaction with CTBP1. Phosphorylation enhances interaction with
CC       YWHAH. {ECO:0000250, ECO:0000269|PubMed:11509661}.
CC   -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC       and Haematology;
CC       URL="http://atlasgeneticsoncology.org/Genes/NRIP1ID44067ch21q11.html";
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DR   EMBL; X84373; CAA59108.1; -; mRNA.
DR   EMBL; AF248484; AAF62185.1; -; Genomic_DNA.
DR   EMBL; AF127577; AAF35255.1; -; Genomic_DNA.
DR   EMBL; AL163207; CAB90396.1; -; Genomic_DNA.
DR   EMBL; BC040361; AAH40361.1; -; mRNA.
DR   CCDS; CCDS13568.1; -.
DR   PIR; S57348; S57348.
DR   RefSeq; NP_003480.2; NM_003489.3.
DR   RefSeq; XP_005261120.1; XM_005261063.2.
DR   RefSeq; XP_005261122.1; XM_005261065.2.
DR   RefSeq; XP_011528049.1; XM_011529747.1.
DR   RefSeq; XP_011528050.1; XM_011529748.1.
DR   RefSeq; XP_011528051.1; XM_011529749.1.
DR   RefSeq; XP_011528052.1; XM_011529750.1.
DR   RefSeq; XP_011528053.1; XM_011529751.1.
DR   RefSeq; XP_011528054.1; XM_011529752.1.
DR   UniGene; Hs.155017; -.
DR   PDB; 2GPO; X-ray; 1.95 A; C=366-390.
DR   PDB; 2GPP; X-ray; 2.60 A; C/D=366-390.
DR   PDB; 4S14; X-ray; 3.54 A; C=499-510.
DR   PDB; 4S15; X-ray; 1.90 A; C/D=499-510.
DR   PDBsum; 2GPO; -.
DR   PDBsum; 2GPP; -.
DR   PDBsum; 4S14; -.
DR   PDBsum; 4S15; -.
DR   ProteinModelPortal; P48552; -.
DR   BioGrid; 113843; 56.
DR   DIP; DIP-5964N; -.
DR   IntAct; P48552; 22.
DR   MINT; MINT-192711; -.
DR   STRING; 9606.ENSP00000327213; -.
DR   PhosphoSite; P48552; -.
DR   BioMuta; NRIP1; -.
DR   DMDM; 9988061; -.
DR   MaxQB; P48552; -.
DR   PaxDb; P48552; -.
DR   PRIDE; P48552; -.
DR   DNASU; 8204; -.
DR   Ensembl; ENST00000318948; ENSP00000327213; ENSG00000180530.
DR   Ensembl; ENST00000400199; ENSP00000383060; ENSG00000180530.
DR   Ensembl; ENST00000400202; ENSP00000383063; ENSG00000180530.
DR   GeneID; 8204; -.
DR   KEGG; hsa:8204; -.
DR   UCSC; uc002yjx.2; human.
DR   CTD; 8204; -.
DR   GeneCards; NRIP1; -.
DR   H-InvDB; HIX0027827; -.
DR   HGNC; HGNC:8001; NRIP1.
DR   HPA; HPA046571; -.
DR   HPA; HPA060036; -.
DR   MIM; 602490; gene.
DR   neXtProt; NX_P48552; -.
DR   PharmGKB; PA31780; -.
DR   eggNOG; ENOG410IFW7; Eukaryota.
DR   eggNOG; ENOG410XPVS; LUCA.
DR   GeneTree; ENSGT00390000007999; -.
DR   HOGENOM; HOG000236277; -.
DR   HOVERGEN; HBG052667; -.
DR   InParanoid; P48552; -.
DR   KO; K17965; -.
DR   OMA; VEKDLRC; -.
DR   OrthoDB; EOG7H1JJQ; -.
DR   PhylomeDB; P48552; -.
DR   TreeFam; TF332210; -.
DR   Reactome; R-HSA-1368082; RORA activates gene expression.
DR   Reactome; R-HSA-1368108; BMAL1:CLOCK,NPAS2 activates circadian gene expression.
DR   Reactome; R-HSA-400253; Circadian Clock.
DR   SignaLink; P48552; -.
DR   ChiTaRS; NRIP1; human.
DR   EvolutionaryTrace; P48552; -.
DR   GeneWiki; NRIP1; -.
DR   GenomeRNAi; 8204; -.
DR   NextBio; 30914; -.
DR   PRO; PR:P48552; -.
DR   Proteomes; UP000005640; Chromosome 21.
DR   Bgee; P48552; -.
DR   CleanEx; HS_NRIP1; -.
DR   ExpressionAtlas; P48552; baseline and differential.
DR   Genevisible; P48552; HS.
DR   GO; GO:0030054; C:cell junction; IDA:HPA.
DR   GO; GO:0000118; C:histone deacetylase complex; IEA:Ensembl.
DR   GO; GO:0000790; C:nuclear chromatin; IDA:BHF-UCL.
DR   GO; GO:0016607; C:nuclear speck; IEA:Ensembl.
DR   GO; GO:0005730; C:nucleolus; IDA:HPA.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0050681; F:androgen receptor binding; NAS:UniProtKB.
DR   GO; GO:0001046; F:core promoter sequence-specific DNA binding; IDA:UniProtKB.
DR   GO; GO:0030331; F:estrogen receptor binding; IPI:UniProtKB.
DR   GO; GO:0035259; F:glucocorticoid receptor binding; IPI:UniProtKB.
DR   GO; GO:0035257; F:nuclear hormone receptor binding; IPI:UniProtKB.
DR   GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB.
DR   GO; GO:0003714; F:transcription corepressor activity; IDA:UniProtKB.
DR   GO; GO:0030521; P:androgen receptor signaling pathway; NAS:UniProtKB.
DR   GO; GO:0071392; P:cellular response to estradiol stimulus; IDA:BHF-UCL.
DR   GO; GO:0032922; P:circadian regulation of gene expression; IMP:UniProtKB.
DR   GO; GO:0007623; P:circadian rhythm; IEP:UniProtKB.
DR   GO; GO:0019915; P:lipid storage; IEA:Ensembl.
DR   GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
DR   GO; GO:0001543; P:ovarian follicle rupture; IEA:Ensembl.
DR   GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; NAS:UniProtKB.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
DR   InterPro; IPR026649; NRIP1.
DR   InterPro; IPR031405; NRIP1_RD1.
DR   InterPro; IPR031406; NRIP1_RD2.
DR   InterPro; IPR031407; NRIP1_RD3.
DR   InterPro; IPR031408; NRIP1_RD4.
DR   PANTHER; PTHR15088; PTHR15088; 1.
DR   Pfam; PF15687; NRIP1_repr_1; 1.
DR   Pfam; PF15688; NRIP1_repr_2; 1.
DR   Pfam; PF15689; NRIP1_repr_3; 1.
DR   Pfam; PF15690; NRIP1_repr_4; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Activator; Biological rhythms;
KW   Complete proteome; Isopeptide bond; Nucleus; Phosphoprotein;
KW   Polymorphism; Reference proteome; Repeat; Transcription;
KW   Transcription regulation; Ubl conjugation.
FT   CHAIN         1   1158       Nuclear receptor-interacting protein 1.
FT                                /FTId=PRO_0000057951.
FT   REGION        1    415       Interaction with ZNF366.
FT   REGION       78    333       Repression domain 1.
FT   REGION      410    700       Repression domain 2.
FT   REGION      431    472       Required for targeting to small nuclear
FT                                foci.
FT   REGION      735    885       Repression domain 3.
FT   REGION      753   1158       Interaction with ZNF366.
FT   REGION     1118   1158       Repression domain 4.
FT   MOTIF        21     25       LXXLL motif 1.
FT   MOTIF       133    137       LXXLL motif 2.
FT   MOTIF       185    189       LXXLL motif 3.
FT   MOTIF       266    270       LXXLL motif 4.
FT   MOTIF       380    384       LXXLL motif 5.
FT   MOTIF       440    446       CTBP-binding; principal site.
FT   MOTIF       500    504       LXXLL motif 6.
FT   MOTIF       565    569       CTBP-binding.
FT   MOTIF       599    603       CTBP-binding. {ECO:0000255}.
FT   MOTIF       713    717       LXXLL motif 7.
FT   MOTIF       819    823       LXXLL motif 8.
FT   MOTIF       936    940       LXXLL motif 9.
FT   MOTIF       946    950       CTBP-binding.
FT   MOTIF      1061   1074       Ligand-dependent nuclear receptor
FT                                binding. {ECO:0000250}.
FT   MOD_RES     104    104       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q8CBD1}.
FT   MOD_RES     111    111       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q8CBD1}.
FT   MOD_RES     158    158       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q8CBD1}.
FT   MOD_RES     207    207       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:Q8CBD1}.
FT   MOD_RES     218    218       Phosphoserine.
FT                                {ECO:0000244|PubMed:24275569}.
FT   MOD_RES     286    286       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q8CBD1}.
FT   MOD_RES     310    310       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q8CBD1}.
FT   MOD_RES     356    356       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q8CBD1}.
FT   MOD_RES     378    378       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q8CBD1}.
FT   MOD_RES     446    446       N6-acetyllysine.
FT                                {ECO:0000269|PubMed:11509661}.
FT   MOD_RES     481    481       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q8CBD1}.
FT   MOD_RES     487    487       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q8CBD1}.
FT   MOD_RES     518    518       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q8CBD1}.
FT   MOD_RES     528    528       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q8CBD1}.
FT   MOD_RES     542    542       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q8CBD1}.
FT   MOD_RES     606    606       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q8CBD1}.
FT   MOD_RES     671    671       Phosphoserine.
FT                                {ECO:0000244|PubMed:24275569}.
FT   MOD_RES     807    807       Phosphoserine.
FT                                {ECO:0000244|PubMed:24275569}.
FT   MOD_RES     931    931       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q8CBD1}.
FT   MOD_RES    1001   1001       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q8CBD1}.
FT   CROSSLNK    756    756       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:25218447}.
FT   CROSSLNK   1105   1105       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:25218447}.
FT   VARIANT      37     37       V -> I (in dbSNP:rs9941840).
FT                                /FTId=VAR_051241.
FT   VARIANT     221    221       H -> R (in dbSNP:rs139263261).
FT                                {ECO:0000269|PubMed:16131398}.
FT                                /FTId=VAR_023706.
FT   VARIANT     315    315       Y -> F (in dbSNP:rs2228507).
FT                                /FTId=VAR_034142.
FT   VARIANT     441    441       I -> V (in dbSNP:rs150468995).
FT                                {ECO:0000269|PubMed:16131398}.
FT                                /FTId=VAR_023707.
FT   VARIANT     448    448       R -> G (common polymorphism;
FT                                dbSNP:rs2229742).
FT                                {ECO:0000269|PubMed:16131398,
FT                                ECO:0000269|PubMed:7641693}.
FT                                /FTId=VAR_023708.
FT   VARIANT     567    567       N -> S (in dbSNP:rs9975169).
FT                                /FTId=VAR_051242.
FT   VARIANT     803    803       S -> L (in dbSNP:rs61750208).
FT                                {ECO:0000269|PubMed:16131398}.
FT                                /FTId=VAR_023709.
FT   VARIANT    1079   1079       V -> F. {ECO:0000269|PubMed:16131398}.
FT                                /FTId=VAR_023710.
FT   MUTAGEN     440    443       PIDL->AAAA: Abolishes interaction with
FT                                CTBP1. {ECO:0000269|PubMed:11509661}.
FT   MUTAGEN     440    442       PID->AIA: Abolishes interaction with
FT                                CTBP1 and attenuates nuclear hormone
FT                                receptor-dependent transcription
FT                                repression.
FT   MUTAGEN     442    443       DL->AA: Reduces, but does not completely
FT                                abolish, interaction with CTBP. Reduces
FT                                transcriptional repression.
FT                                {ECO:0000269|PubMed:14736873,
FT                                ECO:0000269|PubMed:15060175}.
FT   MUTAGEN     442    443       DL->AS: Disrupts interaction with CTBP1,
FT                                and CTBP2 to a lesser extent. Disrupts
FT                                transcriptional repression; when
FT                                associated with 567-AS-568.
FT                                {ECO:0000269|PubMed:14736873,
FT                                ECO:0000269|PubMed:15060175}.
FT   MUTAGEN     446    446       K->Q: Disrupts interaction with CTBP1.
FT                                Decreases lysine acetylation. Disrupts
FT                                nuclear hormone receptor-dependent
FT                                transcription repression.
FT                                {ECO:0000269|PubMed:11509661}.
FT   MUTAGEN     446    446       K->R: Does not disrupt nuclear hormone
FT                                receptor-dependent transcription
FT                                repression.
FT                                {ECO:0000269|PubMed:11509661}.
FT   MUTAGEN     567    568       NL->AA: Disrupts transcriptional
FT                                repression. {ECO:0000269|PubMed:14736873,
FT                                ECO:0000269|PubMed:15060175}.
FT   MUTAGEN     567    568       NL->AS: Disrupts interaction with CTBP1
FT                                and CTBP2. Disrupts transcriptional
FT                                repression; when associated with 442-AS-
FT                                443. {ECO:0000269|PubMed:14736873,
FT                                ECO:0000269|PubMed:15060175}.
FT   MUTAGEN     599    603       SMDLT->PIAAS: Does not further disrupt
FT                                transcriptional repression; when
FT                                associated with 442-AA-443 and 567-AA-
FT                                568.
FT   MUTAGEN     948    949       DL->AA: Abolishes CTBP binding but
FT                                retains transcriptional repressor
FT                                activity. {ECO:0000269|PubMed:14736873}.
FT   CONFLICT    124    124       P -> R (in Ref. 1; CAA59108).
FT                                {ECO:0000305}.
FT   CONFLICT    721    726       NKGKSE -> TKGRVK (in Ref. 1; CAA59108).
FT                                {ECO:0000305}.
FT   CONFLICT    954    954       S -> I (in Ref. 3; AAH40361).
FT                                {ECO:0000305}.
FT   CONFLICT   1080   1080       T -> A (in Ref. 1; CAA59108).
FT                                {ECO:0000305}.
FT   HELIX       379    385       {ECO:0000244|PDB:2GPO}.
FT   HELIX       500    505       {ECO:0000244|PDB:4S15}.
SQ   SEQUENCE   1158 AA;  126942 MW;  81FC424968E9A5F6 CRC64;
     MTHGEELGSD VHQDSIVLTY LEGLLMHQAA GGSGTAVDKK SAGHNEEDQN FNISGSAFPT
     CQSNGPVLNT HTYQGSGMLH LKKARLLQSS EDWNAAKRKR LSDSIMNLNV KKEALLAGMV
     DSVPKGKQDS TLLASLLQSF SSRLQTVALS QQIRQSLKEQ GYALSHDSLK VEKDLRCYGV
     ASSHLKTLLK KSKVKDQKPD TNLPDVTKNL IRDRFAESPH HVGQSGTKVM SEPLSCAARL
     QAVASMVEKR ASPATSPKPS VACSQLALLL SSEAHLQQYS REHALKTQNA NQAASERLAA
     MARLQENGQK DVGSYQLPKG MSSHLNGQAR TSSSKLMASK SSATVFQNPM GIIPSSPKNA
     GYKNSLERNN IKQAANNSLL LHLLKSQTIP KPMNGHSHSE RGSIFEESST PTTIDEYSDN
     NPSFTDDSSG DESSYSNCVP IDLSCKHRTE KSESDQPVSL DNFTQSLLNT WDPKVPDVDI
     KEDQDTSKNS KLNSHQKVTL LQLLLGHKNE ENVEKNTSPQ GVHNDVSKFN TQNYARTSVI
     ESPSTNRTTP VSTPPLLTSS KAGSPINLSQ HSLVIKWNSP PYVCSTQSEK LTNTASNHSM
     DLTKSKDPPG EKPAQNEGAQ NSATFSASKL LQNLAQCGMQ SSMSVEEQRP SKQLLTGNTD
     KPIGMIDRLN SPLLSNKTNA VEENKAFSSQ PTGPEPGLSG SEIENLLERR TVLQLLLGNP
     NKGKSEKKEK TPLRDESTQE HSERALSEQI LMVKIKSEPC DDLQIPNTNV HLSHDAKSAP
     FLGMAPAVQR SAPALPVSED FKSEPVSPQD FSFSKNGLLS RLLRQNQDSY LADDSDRSHR
     NNEMALLESK NLCMVPKKRK LYTEPLENPF KKMKNNIVDA ANNHSAPEVL YGSLLNQEEL
     KFSRNDLEFK YPAGHGSASE SEHRSWARES KSFNVLKQLL LSENCVRDLS PHRSNSVADS
     KKKGHKNNVT NSKPEFSISS LNGLMYSSTQ PSSCMDNRTF SYPGVVKTPV SPTFPEHLGC
     AGSRPESGLL NGCSMPSEKG PIKWVITDAE KNEYEKDSPR LTKTNPILYY MLQKGGNSVT
     SRETQDKDIW REASSAESVS QVTAKEELLP TAETKASFFN LRSPYNSHMG NNASRPHSAN
     GEVYGLLGSV LTIKKESE
//
ID   SOX6_HUMAN              Reviewed;         828 AA.
AC   P35712; Q86VX7; Q9BXQ3; Q9BXQ4; Q9BXQ5; Q9H0I8;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 3.
DT   11-NOV-2015, entry version 147.
DE   RecName: Full=Transcription factor SOX-6;
GN   Name=SOX6;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 3), ALTERNATIVE
RP   SPLICING, AND TISSUE SPECIFICITY.
RC   TISSUE=Lymphocyte, and Myoblast;
RX   PubMed=11255018; DOI=10.1016/S0378-1119(01)00346-8;
RA   Cohen-Barak O., Hagiwara N., Arlt M.F., Horton J.P., Brilliant M.H.;
RT   "Cloning, characterization and chromosome mapping of the human SOX6
RT   gene.";
RL   Gene 265:157-164(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Testis;
RX   PubMed=11230166; DOI=10.1101/gr.GR1547R;
RA   Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA   Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H.,
RA   Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N.,
RA   Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D.,
RA   Wambutt R., Korn B., Klein M., Poustka A.;
RT   "Towards a catalog of human genes and proteins: sequencing and
RT   analysis of 500 novel complete protein coding human cDNAs.";
RL   Genome Res. 11:422-435(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16554811; DOI=10.1038/nature04632;
RA   Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA   Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
RA   Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
RA   FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
RA   Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
RA   Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
RA   Sakaki Y.;
RT   "Human chromosome 11 DNA sequence and analysis including novel gene
RT   identification.";
RL   Nature 440:497-500(2006).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4).
RC   TISSUE=Testis;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 632-685 (ISOFORMS 1/2/3).
RX   PubMed=1614875; DOI=10.1093/nar/20.11.2887;
RA   Denny P., Swift S., Brand N., Dabhade N., Barton P., Ashworth A.;
RT   "A conserved family of genes related to the testis determining gene,
RT   SRY.";
RL   Nucleic Acids Res. 20:2887-2887(1992).
RN   [7]
RP   SUMOYLATION AT LYS-404 AND LYS-417, MUTAGENESIS OF LYS-404 AND
RP   LYS-417, AND SUBCELLULAR LOCATION.
RX   PubMed=16442531; DOI=10.1016/j.febslet.2006.01.031;
RA   Fernandez-Lloris R., Osses N., Jaffray E., Shen L.N., Vaughan O.A.,
RA   Girwood D., Bartrons R., Rosa J.L., Hay R.T., Ventura F.;
RT   "Repression of SOX6 transcriptional activity by SUMO modification.";
RL   FEBS Lett. 580:1215-1221(2006).
RN   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA   Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT   a refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [9]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
RA   Wang L., Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human
RT   liver phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
CC   -!- FUNCTION: Transcriptional activator. Binds specifically to the DNA
CC       sequence 5'-AACAAT-3'. Plays a key role in several developmental
CC       processes, including neurogenesis and skeleton formation.
CC   -!- SUBUNIT: Interacts with DAZAP2. {ECO:0000250}.
CC   -!- INTERACTION:
CC       O15266:SHOX; NbExp=3; IntAct=EBI-3505706, EBI-3505698;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-
CC       ProRule:PRU00267, ECO:0000269|PubMed:16442531}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=P35712-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P35712-2; Sequence=VSP_039693, VSP_039694, VSP_039695;
CC       Name=3;
CC         IsoId=P35712-3; Sequence=VSP_039696;
CC       Name=4;
CC         IsoId=P35712-4; Sequence=VSP_039694, VSP_039695;
CC         Note=No experimental confirmation available.;
CC   -!- TISSUE SPECIFICITY: Expressed in a wide variety of tissues, most
CC       abundantly in skeletal muscle. {ECO:0000269|PubMed:11255018}.
CC   -!- PTM: Sumoylation inhibits the transcriptional activity.
CC       {ECO:0000269|PubMed:16442531}.
CC   -!- SIMILARITY: Contains 1 HMG box DNA-binding domain.
CC       {ECO:0000255|PROSITE-ProRule:PRU00267}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BC037866; Type=Frameshift; Positions=505; Evidence={ECO:0000305};
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DR   EMBL; AF309034; AAK26115.1; -; mRNA.
DR   EMBL; AF309476; AAK26243.1; -; Genomic_DNA.
DR   EMBL; AF309471; AAK26243.1; JOINED; Genomic_DNA.
DR   EMBL; AF309472; AAK26243.1; JOINED; Genomic_DNA.
DR   EMBL; AF309473; AAK26243.1; JOINED; Genomic_DNA.
DR   EMBL; AF309474; AAK26243.1; JOINED; Genomic_DNA.
DR   EMBL; AF309475; AAK26243.1; JOINED; Genomic_DNA.
DR   EMBL; AF309476; AAK26244.1; -; Genomic_DNA.
DR   EMBL; AF309471; AAK26244.1; JOINED; Genomic_DNA.
DR   EMBL; AF309472; AAK26244.1; JOINED; Genomic_DNA.
DR   EMBL; AF309473; AAK26244.1; JOINED; Genomic_DNA.
DR   EMBL; AF309474; AAK26244.1; JOINED; Genomic_DNA.
DR   EMBL; AF309475; AAK26244.1; JOINED; Genomic_DNA.
DR   EMBL; AL136780; CAB66714.1; -; mRNA.
DR   EMBL; AC009869; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC013595; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC027016; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC068405; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC103794; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471064; EAW68458.1; -; Genomic_DNA.
DR   EMBL; BC037866; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; BC047064; AAH47064.2; -; mRNA.
DR   EMBL; X65663; CAA46614.1; -; mRNA.
DR   CCDS; CCDS53604.1; -. [P35712-4]
DR   CCDS; CCDS53605.1; -. [P35712-2]
DR   CCDS; CCDS7821.1; -. [P35712-3]
DR   RefSeq; NP_001139283.1; NM_001145811.1. [P35712-4]
DR   RefSeq; NP_001139291.1; NM_001145819.1.
DR   RefSeq; NP_059978.1; NM_017508.2. [P35712-2]
DR   RefSeq; NP_201583.2; NM_033326.3. [P35712-3]
DR   UniGene; Hs.368226; -.
DR   ProteinModelPortal; P35712; -.
DR   SMR; P35712; 619-688.
DR   BioGrid; 120714; 11.
DR   IntAct; P35712; 3.
DR   MINT; MINT-4719252; -.
DR   STRING; 9606.ENSP00000324948; -.
DR   PhosphoSite; P35712; -.
DR   BioMuta; SOX6; -.
DR   DMDM; 215274178; -.
DR   MaxQB; P35712; -.
DR   PaxDb; P35712; -.
DR   PRIDE; P35712; -.
DR   DNASU; 55553; -.
DR   Ensembl; ENST00000316399; ENSP00000324948; ENSG00000110693. [P35712-3]
DR   Ensembl; ENST00000396356; ENSP00000379644; ENSG00000110693. [P35712-3]
DR   Ensembl; ENST00000527619; ENSP00000434455; ENSG00000110693. [P35712-2]
DR   Ensembl; ENST00000528252; ENSP00000432134; ENSG00000110693. [P35712-4]
DR   Ensembl; ENST00000528429; ENSP00000433233; ENSG00000110693. [P35712-1]
DR   GeneID; 55553; -.
DR   KEGG; hsa:55553; -.
DR   UCSC; uc001mmd.3; human. [P35712-2]
DR   UCSC; uc001mme.3; human. [P35712-1]
DR   UCSC; uc001mmf.3; human. [P35712-4]
DR   UCSC; uc001mmg.3; human. [P35712-3]
DR   CTD; 55553; -.
DR   GeneCards; SOX6; -.
DR   HGNC; HGNC:16421; SOX6.
DR   HPA; HPA001923; -.
DR   HPA; HPA003908; -.
DR   MIM; 607257; gene.
DR   neXtProt; NX_P35712; -.
DR   PharmGKB; PA38137; -.
DR   eggNOG; KOG0528; Eukaryota.
DR   eggNOG; ENOG410YZNG; LUCA.
DR   GeneTree; ENSGT00760000119274; -.
DR   HOGENOM; HOG000056455; -.
DR   HOVERGEN; HBG003915; -.
DR   InParanoid; P35712; -.
DR   KO; K09269; -.
DR   OMA; QQRMESE; -.
DR   OrthoDB; EOG70087H; -.
DR   PhylomeDB; P35712; -.
DR   TreeFam; TF320471; -.
DR   Reactome; R-HSA-3769402; deactivation of the beta-catenin transactivating complex.
DR   ChiTaRS; SOX6; human.
DR   GeneWiki; SOX6; -.
DR   GenomeRNAi; 55553; -.
DR   NextBio; 60012; -.
DR   PRO; PR:P35712; -.
DR   Proteomes; UP000005640; Chromosome 11.
DR   Bgee; P35712; -.
DR   CleanEx; HS_SOX6; -.
DR   ExpressionAtlas; P35712; baseline and differential.
DR   Genevisible; P35712; HS.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; NAS:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; NAS:UniProtKB.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IEA:Ensembl.
DR   GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; NAS:UniProtKB.
DR   GO; GO:0044212; F:transcription regulatory region DNA binding; IEA:Ensembl.
DR   GO; GO:0055007; P:cardiac muscle cell differentiation; IEA:Ensembl.
DR   GO; GO:0051216; P:cartilage development; IEA:Ensembl.
DR   GO; GO:0000902; P:cell morphogenesis; IEA:Ensembl.
DR   GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; IDA:UniProtKB.
DR   GO; GO:0048821; P:erythrocyte development; IEA:Ensembl.
DR   GO; GO:0016458; P:gene silencing; IEA:Ensembl.
DR   GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR   GO; GO:0007517; P:muscle organ development; NAS:UniProtKB.
DR   GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IEA:Ensembl.
DR   GO; GO:0021778; P:oligodendrocyte cell fate specification; IEA:Ensembl.
DR   GO; GO:0061036; P:positive regulation of cartilage development; IDA:UniProtKB.
DR   GO; GO:0032332; P:positive regulation of chondrocyte differentiation; IDA:UniProtKB.
DR   GO; GO:2000741; P:positive regulation of mesenchymal stem cell differentiation; IDA:UniProtKB.
DR   GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IEA:Ensembl.
DR   GO; GO:0009791; P:post-embryonic development; IEA:Ensembl.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; NAS:UniProtKB.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.30.10; -; 1.
DR   InterPro; IPR009071; HMG_box_dom.
DR   InterPro; IPR027153; SOX-6.
DR   PANTHER; PTHR10270:SF89; PTHR10270:SF89; 3.
DR   Pfam; PF00505; HMG_box; 1.
DR   SMART; SM00398; HMG; 1.
DR   SUPFAM; SSF47095; SSF47095; 1.
DR   PROSITE; PS50118; HMG_BOX_2; 1.
PE   1: Evidence at protein level;
KW   Activator; Alternative splicing; Coiled coil; Complete proteome;
KW   Developmental protein; DNA-binding; Isopeptide bond; Nucleus;
KW   Phosphoprotein; Reference proteome; Transcription;
KW   Transcription regulation; Ubl conjugation.
FT   CHAIN         1    828       Transcription factor SOX-6.
FT                                /FTId=PRO_0000048729.
FT   DNA_BIND    621    689       HMG box. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00267}.
FT   COILED      184    262       {ECO:0000255}.
FT   COMPBIAS    219    261       Gln-rich.
FT   COMPBIAS    280    285       Poly-Ala.
FT   COMPBIAS    313    317       Poly-Ala.
FT   MOD_RES     119    119       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:P40645}.
FT   MOD_RES     399    399       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P40645}.
FT   MOD_RES     401    401       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:P40645}.
FT   MOD_RES     439    439       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P40645}.
FT   MOD_RES     442    442       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P40645}.
FT   CROSSLNK    404    404       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO).
FT   CROSSLNK    417    417       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO).
FT   VAR_SEQ       1      1       M -> MGRM (in isoform 2).
FT                                {ECO:0000303|PubMed:11230166}.
FT                                /FTId=VSP_039693.
FT   VAR_SEQ     327    367       Missing (in isoform 2 and isoform 4).
FT                                {ECO:0000303|PubMed:11230166,
FT                                ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_039694.
FT   VAR_SEQ     477    477       S -> SLGKWKSQHQEETYE (in isoform 2 and
FT                                isoform 4). {ECO:0000303|PubMed:11230166,
FT                                ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_039695.
FT   VAR_SEQ     578    597       Missing (in isoform 3).
FT                                {ECO:0000303|PubMed:11255018}.
FT                                /FTId=VSP_039696.
FT   MUTAGEN     404    404       K->R: Partial loss of sumoylation.
FT                                Complete loss of sumoylation; when
FT                                associated with R-417.
FT                                {ECO:0000269|PubMed:16442531}.
FT   MUTAGEN     417    417       K->R: Partial loss of sumoylation.
FT                                Complete loss of sumoylation; when
FT                                associated with R-404.
FT                                {ECO:0000269|PubMed:16442531}.
FT   CONFLICT    330    330       V -> A (in Ref. 1; AAK26115).
FT                                {ECO:0000305}.
FT   CONFLICT    633    633       K -> R (in Ref. 6; CAA46614).
FT                                {ECO:0000305}.
SQ   SEQUENCE   828 AA;  91921 MW;  38CA781528C839CF CRC64;
     MSSKQATSPF ACAADGEDAM TQDLTSREKE EGSDQHVASH LPLHPIMHNK PHSEELPTLV
     STIQQDADWD SVLSSQQRME SENNKLCSLY SFRNTSTSPH KPDEGSRDRE IMTSVTFGTP
     ERRKGSLADV VDTLKQKKLE EMTRTEQEDS SCMEKLLSKD WKEKMERLNT SELLGEIKGT
     PESLAEKERQ LSTMITQLIS LREQLLAAHD EQKKLAASQI EKQRQQMDLA RQQQEQIARQ
     QQQLLQQQHK INLLQQQIQV QGHMPPLMIP IFPHDQRTLA AAAAAQQGFL FPPGITYKPG
     DNYPVQFIPS TMAAAAASGL SPLQLQKGHV SHPQINQRLK GLSDRFGRNL DTFEHGGGHS
     YNHKQIEQLY AAQLASMQVS PGAKMPSTPQ PPNTAGTVSP TGIKNEKRGT SPVTQVKDEA
     AAQPLNLSSR PKTAEPVKSP TSPTQNLFPA SKTSPVNLPN KSSIPSPIGG SLGRGSSLDI
     LSSLNSPALF GDQDTVMKAI QEARKMREQI QREQQQQQPH GVDGKLSSIN NMGLNSCRNE
     KERTRFENLG PQLTGKSNED GKLGPGVIDL TRPEDAEGSK AMNGSAAKLQ QYYCWPTGGA
     TVAEARVYRD ARGRASSEPH IKRPMNAFMV WAKDERRKIL QAFPDMHNSN ISKILGSRWK
     SMSNQEKQPY YEEQARLSKI HLEKYPNYKY KPRPKRTCIV DGKKLRIGEY KQLMRSRRQE
     MRQFFTVGQQ PQIPITTGTG VVYPGAITMA TTTPSPQMTS DCSSTSASPE PSLPVIQSTY
     GMKTDGGSLA GNEMINGEDE MEMYDDYEDD PKSDYSSENE APEAVSAN
//
ID   T7L1A_XENLA             Reviewed;         554 AA.
AC   P70062;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   14-OCT-2015, entry version 96.
DE   RecName: Full=Transcription factor 7-like 1-A;
DE   AltName: Full=HMG box transcription factor 3-A;
DE            Short=TCF-3-A;
DE            Short=xTcf-3;
GN   Name=tcf7l1-a; Synonyms=tcf3, tcf3a;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Amphibia; Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus;
OC   Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DNA-BINDING, AND SUBCELLULAR
RP   LOCATION.
RX   PubMed=8756721; DOI=10.1016/S0092-8674(00)80112-9;
RA   Molenaar M., van de Wetering M., Peterson-Maduro J., Godsave S.,
RA   Korinkek V., Roose J., Destree O., Clevers H.;
RT   "XTcf-3 transcription factor mediates beta-catenin-induced axis
RT   formation in Xenopus embryos.";
RL   Cell 86:391-399(1996).
RN   [2]
RP   FUNCTION, DNA-BINDING, AND INTERACTION WITH CTNNB1-A.
RX   PubMed=9308964; DOI=10.1101/gad.11.18.2359;
RA   Brannon M., Gomperts M., Sumoy L., Moon R.T., Kimelman D.;
RT   "A beta-catenin/XTcf-3 complex binds to the siamois promoter to
RT   regulate dorsal axis specification in Xenopus.";
RL   Genes Dev. 11:2359-2370(1997).
RN   [3]
RP   FUNCTION, AND INTERACTION WITH AES AND TLE4-A.
RX   PubMed=9783587; DOI=10.1038/26989;
RA   Roose J., Molenaar M., Peterson J., Hurenkamp J., Brantjes H.,
RA   Moerer P., van de Wetering M., Destree O., Clevers H.;
RT   "The Xenopus Wnt effector XTcf-3 interacts with Groucho-related
RT   transcriptional repressors.";
RL   Nature 395:608-612(1998).
RN   [4]
RP   FUNCTION, INTERACTION WITH CTBP-B, AND MUTAGENESIS OF 469-PRO-LEU-470
RP   AND 545-PRO-LEU-546.
RX   PubMed=10375506;
RA   Brannon M., Brown J.D., Bates R., Kimelman D., Moon R.T.;
RT   "XCtBP is a XTcf-3 co-repressor with roles throughout Xenopus
RT   development.";
RL   Development 126:3159-3170(1999).
RN   [5]
RP   FUNCTION.
RX   PubMed=10495268; DOI=10.1016/S0925-4773(99)00136-7;
RA   McGrew L.L., Takemaru K., Bates R., Moon R.T.;
RT   "Direct regulation of the Xenopus engrailed-2 promoter by the Wnt
RT   signaling pathway, and a molecular screen for Wnt-responsive genes,
RT   confirm a role for Wnt signaling during neural patterning in
RT   Xenopus.";
RL   Mech. Dev. 87:21-32(1999).
RN   [6]
RP   FUNCTION.
RX   PubMed=10559484; DOI=10.1016/S0925-4773(99)00210-5;
RA   Marikawa Y., Elinson R.P.;
RT   "Relationship of vegetal cortical dorsal factors in the Xenopus egg
RT   with the Wnt/beta-catenin signaling pathway.";
RL   Mech. Dev. 89:93-102(1999).
RN   [7]
RP   FUNCTION.
RX   PubMed=11493528;
RA   Hamilton F.S., Wheeler G.N., Hoppler S.;
RT   "Difference in XTcf-3 dependency accounts for change in response to
RT   beta-catenin-mediated Wnt signalling in Xenopus blastula.";
RL   Development 128:2063-2073(2001).
RN   [8]
RP   FUNCTION.
RX   PubMed=11356018; DOI=10.1006/dbio.2001.0253;
RA   Darken R.S., Wilson P.A.;
RT   "Axis induction by wnt signaling: target promoter responsiveness
RT   regulates competence.";
RL   Dev. Biol. 234:42-54(2001).
RN   [9]
RP   FUNCTION, INTERACTION WITH CSNK1E; CTNNB1-A AND GSK3B, SUBCELLULAR
RP   LOCATION, AND PHOSPHORYLATION.
RX   PubMed=11524435; DOI=10.1083/jcb.200102074;
RA   Lee E., Salic A., Kirschner M.W.;
RT   "Physiological regulation of beta-catenin stability by Tcf3 and
RT   CK1epsilon.";
RL   J. Cell Biol. 154:983-993(2001).
RN   [10]
RP   FUNCTION, AND DNA-BINDING.
RX   PubMed=11238923; DOI=10.1128/MCB.21.5.1866-1873.2001;
RA   Snider L., Thirlwell H., Miller J.R., Moon R.T., Groudine M.,
RA   Tapscott S.J.;
RT   "Inhibition of Tcf3 binding by I-mfa domain proteins.";
RL   Mol. Cell. Biol. 21:1866-1873(2001).
RN   [11]
RP   FUNCTION.
RX   PubMed=12445388; DOI=10.1016/S0960-9822(02)01280-0;
RA   Roeel G., Hamilton F.S., Gent Y., Bain A.A., Destree O., Hoppler S.;
RT   "Lef-1 and Tcf-3 transcription factors mediate tissue-specific Wnt
RT   signaling during Xenopus development.";
RL   Curr. Biol. 12:1941-1945(2002).
RN   [12]
RP   FUNCTION.
RX   PubMed=12163405;
RA   Houston D.W., Kofron M., Resnik E., Langland R., Destree O., Wylie C.,
RA   Heasman J.;
RT   "Repression of organizer genes in dorsal and ventral Xenopus cells
RT   mediated by maternal XTcf3.";
RL   Development 129:4015-4025(2002).
RN   [13]
RP   FUNCTION.
RX   PubMed=11934150;
RA   Rex M., Hilton E., Old R.W.;
RT   "Multiple interactions between maternally-activated signalling
RT   pathways control Xenopus nodal-related genes.";
RL   Int. J. Dev. Biol. 46:217-226(2002).
RN   [14]
RP   DNA-BINDING.
RX   PubMed=12049769; DOI=10.1016/S0925-4773(02)00121-1;
RA   Yang J., Mei W., Otto A., Xiao L., Tao Q., Geng X., Rupp R.A.W.,
RA   Ding X.;
RT   "Repression through a distal TCF-3 binding site restricts Xenopus myf-
RT   5 expression in gastrula mesoderm.";
RL   Mech. Dev. 115:79-89(2002).
RN   [15]
RP   FUNCTION.
RX   PubMed=14568102; DOI=10.1016/j.mod.2003.08.004;
RA   Hilton E., Rex M., Old R.;
RT   "VegT activation of the early zygotic gene Xnr5 requires lifting of
RT   Tcf-mediated repression in the Xenopus blastula.";
RL   Mech. Dev. 120:1127-1138(2003).
RN   [16]
RP   FUNCTION, AND INTERACTION WITH DACT1-A.
RX   PubMed=15329348; DOI=10.1242/dev.01369;
RA   Hikasa H., Sokol S.Y.;
RT   "The involvement of Frodo in TCF-dependent signaling and neural tissue
RT   development.";
RL   Development 131:4725-4734(2004).
RN   [17]
RP   FUNCTION.
RX   PubMed=15747128; DOI=10.1007/s00427-005-0474-0;
RA   Tsuji S., Hashimoto C.;
RT   "Choice of either beta-catenin or Groucho/TLE as a co-factor for Xtcf-
RT   3 determines dorsal-ventral cell fate of diencephalon during Xenopus
RT   development.";
RL   Dev. Genes Evol. 215:275-284(2005).
RN   [18]
RP   FUNCTION.
RX   PubMed=15923623; DOI=10.1128/MCB.25.12.5061-5072.2005;
RA   Snider L., Tapscott S.J.;
RT   "XIC is required for Siamois activity and dorsoanterior development.";
RL   Mol. Cell. Biol. 25:5061-5072(2005).
RN   [19]
RP   X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 1-61.
RX   PubMed=11136974; DOI=10.1016/S0092-8674(00)00192-6;
RA   Graham T.A., Weaver C., Mao F., Kimelman D., Xu W.;
RT   "Crystal structure of a beta-catenin/Tcf complex.";
RL   Cell 103:885-896(2000).
CC   -!- FUNCTION: Participates in the Wnt signaling pathway. Binds to DNA
CC       and acts as a repressor in the absence of ctnnb1-A and possibly
CC       ctnnb1-B, and as an activator in the presence of these proteins.
CC       Required early in development for the establishment of the dorsal
CC       body axis in response to maternal Wnt signaling. Also required
CC       during development of the CNS for the establishment of dorsal-
CC       ventral patterning in the prospective diencephalon.
CC       {ECO:0000269|PubMed:10375506, ECO:0000269|PubMed:10495268,
CC       ECO:0000269|PubMed:10559484, ECO:0000269|PubMed:11238923,
CC       ECO:0000269|PubMed:11356018, ECO:0000269|PubMed:11493528,
CC       ECO:0000269|PubMed:11524435, ECO:0000269|PubMed:11934150,
CC       ECO:0000269|PubMed:12163405, ECO:0000269|PubMed:12445388,
CC       ECO:0000269|PubMed:14568102, ECO:0000269|PubMed:15329348,
CC       ECO:0000269|PubMed:15747128, ECO:0000269|PubMed:15923623,
CC       ECO:0000269|PubMed:8756721, ECO:0000269|PubMed:9308964,
CC       ECO:0000269|PubMed:9783587}.
CC   -!- SUBUNIT: Interacts with csnk1e, ctnnb1-A, ctbp-B, dact1-A and
CC       gsk3b. May interact with ase and tle4-A.
CC       {ECO:0000269|PubMed:10375506, ECO:0000269|PubMed:11524435,
CC       ECO:0000269|PubMed:15329348, ECO:0000269|PubMed:9308964,
CC       ECO:0000269|PubMed:9783587}.
CC   -!- INTERACTION:
CC       Q8JJ48:dact1-a; NbExp=3; IntAct=EBI-6259044, EBI-6259065;
CC       A0SNQ7:tshz3; NbExp=2; IntAct=EBI-6259044, EBI-7373787;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC   -!- PTM: Phosphorylated. Phosphorylation by csnk1e promotes binding to
CC       ctnnb1-A while phosphorylation by gsk3b may reverse this effect.
CC       {ECO:0000269|PubMed:11524435}.
CC   -!- SIMILARITY: Belongs to the TCF/LEF family. {ECO:0000305}.
CC   -!- SIMILARITY: Contains 1 HMG box DNA-binding domain.
CC       {ECO:0000255|PROSITE-ProRule:PRU00267}.
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DR   EMBL; X99308; CAA67686.1; -; mRNA.
DR   RefSeq; NP_001081483.1; NM_001088014.1.
DR   UniGene; Xl.1100; -.
DR   PDB; 1G3J; X-ray; 2.10 A; B/D=1-61.
DR   PDBsum; 1G3J; -.
DR   ProteinModelPortal; P70062; -.
DR   SMR; P70062; 2-52, 323-398.
DR   IntAct; P70062; 5.
DR   MINT; MINT-4790980; -.
DR   GeneID; 397863; -.
DR   KEGG; xla:397863; -.
DR   CTD; 397863; -.
DR   Xenbase; XB-GENE-6252329; tcf7l1.
DR   HOVERGEN; HBG000419; -.
DR   KO; K04490; -.
DR   EvolutionaryTrace; P70062; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IC:UniProtKB.
DR   GO; GO:0005667; C:transcription factor complex; IPI:UniProtKB.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
DR   GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IEA:InterPro.
DR   GO; GO:0008134; F:transcription factor binding; IPI:UniProtKB.
DR   GO; GO:0060070; P:canonical Wnt signaling pathway; IEA:InterPro.
DR   GO; GO:0007275; P:multicellular organismal development; IEA:UniProtKB-KW.
DR   GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.30.10; -; 1.
DR   Gene3D; 4.10.900.10; -; 1.
DR   InterPro; IPR027397; Catenin_binding_dom.
DR   InterPro; IPR013558; CTNNB1-bd_N.
DR   InterPro; IPR009071; HMG_box_dom.
DR   InterPro; IPR024940; TCF/LEF.
DR   InterPro; IPR028778; Tcf7l1.
DR   PANTHER; PTHR10373; PTHR10373; 1.
DR   PANTHER; PTHR10373:SF25; PTHR10373:SF25; 1.
DR   Pfam; PF08347; CTNNB1_binding; 1.
DR   Pfam; PF00505; HMG_box; 1.
DR   SMART; SM00398; HMG; 1.
DR   SUPFAM; SSF47095; SSF47095; 1.
DR   PROSITE; PS50118; HMG_BOX_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Activator; Cytoplasm; Developmental protein;
KW   DNA-binding; Nucleus; Phosphoprotein; Repressor; Transcription;
KW   Transcription regulation; Wnt signaling pathway.
FT   CHAIN         1    554       Transcription factor 7-like 1-A.
FT                                /FTId=PRO_0000048616.
FT   DNA_BIND    324    392       HMG box. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00267}.
FT   REGION        1     61       Interaction with CTNNB1-A.
FT   REGION      109    312       Interaction with AES and TLE4-A.
FT   REGION      408    554       Interaction with CTBP-B.
FT   COMPBIAS    148    291       Pro-rich.
FT   COMPBIAS    483    528       Ser-rich.
FT   MUTAGEN     469    470       PL->AS: May abrogate binding to CTBP-B.
FT                                {ECO:0000269|PubMed:10375506}.
FT   MUTAGEN     545    546       PL->AS: May abrogate binding to CTBP-B.
FT                                {ECO:0000269|PubMed:10375506}.
FT   HELIX        42     49       {ECO:0000244|PDB:1G3J}.
SQ   SEQUENCE   554 AA;  60300 MW;  90B24D134AE4EBDD CRC64;
     MPQLNSGGGD ELGANDELIR FKDEGEQEEK SPGEGSAEGD LADVKSSLVN ESENHSSDSD
     SEVERRPPPR EAFEKHRDYL TEALRRQQDA AFFKGPPYAG YPFLMIPDLG GHYLPNGALS
     PSARTYLQMK WPLLDSPSTA GLKDARSPSP AHLSNKVPVV QHPHHMHPLT PLITYSNEHF
     SPGTPPGHLS PEIDPKTGIP RPPHPSELSP YYPLSPGAVG QIPHPLGWLV PPQGQPMYSI
     PPGGFRHPYP ALAMNASMSS LVSSRFSPHM VPPPHHSLHT SGIPHPAIVS PIVKQEPSSG
     NISPNLHTKS NMIVKKEEEK KPHIKKPLNA FMLYMKEMRA KVVAECTLKE SAAINQILGR
     RWHSLSREEQ AKYYELARKE RQLHSQLYPS WSARDNYGKR KKRKREKQSP EMETHTKTKK
     MCVQHLPADK SCDSPASSHG SMLDSPATPS AALASPAAPA ATHSEQAQPL SLTTKPEARA
     QLSLSHSAAF LASKSPSSSS FSGHLSSPVG SPLLSRPIPL TSSILSPSGV FPSALQALPL
     LQAQPLSLVT KSSD
//
ID   TGIF1_HUMAN             Reviewed;         401 AA.
AC   Q15583; A6NE42; A6NLU7; F8VZB6; Q6ICR0; Q8N5X9; Q9NRS0;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 3.
DT   11-NOV-2015, entry version 169.
DE   RecName: Full=Homeobox protein TGIF1;
DE   AltName: Full=5'-TG-3'-interacting factor 1;
GN   Name=TGIF1; Synonyms=TGIF;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC   TISSUE=Liver;
RX   PubMed=8537382; DOI=10.1074/jbc.270.52.31178;
RA   Bertolino E., Reimund B., Wildt-Perinic D., Clerc R.G.;
RT   "A novel homeobox protein which recognizes a TGT core and functionally
RT   interferes with a retinoid-responsive motif.";
RL   J. Biol. Chem. 270:31178-31188(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND VARIANT SER-292.
RC   TISSUE=Brain;
RX   PubMed=10764806; DOI=10.1074/jbc.M908382199;
RA   Yang Y., Hwang C.K., D'Souza U.M., Lee S.-H., Junn E., Mouradian M.M.;
RT   "Three-amino acid extension loop homeodomain proteins Meis2 and TGIF
RT   differentially regulate transcription.";
RL   J. Biol. Chem. 275:20734-20741(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT
RP   SER-292.
RA   Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT   "Cloning of human full open reading frames in Gateway(TM) system entry
RT   vector (pDONR201).";
RL   Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16177791; DOI=10.1038/nature03983;
RA   Nusbaum C., Zody M.C., Borowsky M.L., Kamal M., Kodira C.D.,
RA   Taylor T.D., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K.,
RA   FitzGerald M.G., Yang X., Abouelleil A., Allen N.R., Anderson S.,
RA   Bloom T., Bugalter B., Butler J., Cook A., DeCaprio D., Engels R.,
RA   Garber M., Gnirke A., Hafez N., Hall J.L., Norman C.H., Itoh T.,
RA   Jaffe D.B., Kuroki Y., Lehoczky J., Lui A., Macdonald P., Mauceli E.,
RA   Mikkelsen T.S., Naylor J.W., Nicol R., Nguyen C., Noguchi H.,
RA   O'Leary S.B., Piqani B., Smith C.L., Talamas J.A., Topham K.,
RA   Totoki Y., Toyoda A., Wain H.M., Young S.K., Zeng Q., Zimmer A.R.,
RA   Fujiyama A., Hattori M., Birren B.W., Sakaki Y., Lander E.S.;
RT   "DNA sequence and analysis of human chromosome 18.";
RL   Nature 437:551-555(2005).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-137 (ISOFORM 4).
RC   TISSUE=Brain, Placenta, and Rhabdomyosarcoma;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [8]
RP   STRUCTURE BY NMR OF 171-248.
RG   Northeast structural genomics consortium (NESG);
RT   "Solution NMR structure of homeobox domain (171-248) of human homeobox
RT   protein TGIF1, northeast structural genomics consortium target
RT   hr4411b.";
RL   Submitted (OCT-2011) to the PDB data bank.
RN   [9]
RP   VARIANTS HPE4 CYS-157; ARG-192; ALA-280 AND PHE-291.
RX   PubMed=10835638; DOI=10.1038/76074;
RA   Gripp K.W., Wotton D., Edwards M.C., Roessler E., Ades L.,
RA   Meinecke P., Richieri-Costa A., Zackai E.H., Massague J., Muenke M.,
RA   Elledge S.J.;
RT   "Mutations in TGIF cause holoprosencephaly and link NODAL signalling
RT   to human neural axis determination.";
RL   Nat. Genet. 25:205-208(2000).
RN   [10]
RP   VARIANT HPE4 LEU-236.
RX   PubMed=15221788; DOI=10.1002/humu.20056;
RA   Dubourg C., Lazaro L., Pasquier L., Bendavid C., Blayau M.,
RA   Le Duff F., Durou M.-R., Odent S., David V.;
RT   "Molecular screening of SHH, ZIC2, SIX3, and TGIF genes in patients
RT   with features of holoprosencephaly spectrum: mutation review and
RT   genotype-phenotype correlations.";
RL   Hum. Mutat. 24:43-51(2004).
CC   -!- FUNCTION: Binds to a retinoid X receptor (RXR) responsive element
CC       from the cellular retinol-binding protein II promoter (CRBPII-
CC       RXRE). Inhibits the 9-cis-retinoic acid-dependent RXR alpha
CC       transcription activation of the retinoic acid responsive element.
CC       Active transcriptional corepressor of SMAD2. Links the nodal
CC       signaling pathway to the bifurcation of the forebrain and the
CC       establishment of ventral midline structures. May participate in
CC       the transmission of nuclear signals during development and in the
CC       adult, as illustrated by the down-modulation of the RXR alpha
CC       activities.
CC   -!- SUBUNIT: Interacts with CTBP, SMAD2, SMAD3 and HDAC1.
CC   -!- INTERACTION:
CC       Q13363-2:CTBP1; NbExp=3; IntAct=EBI-714215, EBI-10171858;
CC       P56545:CTBP2; NbExp=5; IntAct=EBI-714215, EBI-741533;
CC       O00214:LGALS8; NbExp=10; IntAct=EBI-714215, EBI-740058;
CC       Q99750:MDFI; NbExp=4; IntAct=EBI-714215, EBI-724076;
CC       P29590:PML; NbExp=3; IntAct=EBI-714215, EBI-295890;
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q15583-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q15583-2; Sequence=VSP_013020, VSP_013021;
CC       Name=3;
CC         IsoId=Q15583-3; Sequence=VSP_043108, VSP_043109;
CC       Name=4;
CC         IsoId=Q15583-4; Sequence=VSP_046848;
CC         Note=No experimental confirmation available.;
CC   -!- DISEASE: Holoprosencephaly 4 (HPE4) [MIM:142946]: A structural
CC       anomaly of the brain, in which the developing forebrain fails to
CC       correctly separate into right and left hemispheres.
CC       Holoprosencephaly is genetically heterogeneous and associated with
CC       several distinct facies and phenotypic variability.
CC       {ECO:0000269|PubMed:10835638, ECO:0000269|PubMed:15221788}.
CC       Note=The disease is caused by mutations affecting the gene
CC       represented in this entry.
CC   -!- SIMILARITY: Belongs to the TALE/TGIF homeobox family.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Contains 1 homeobox DNA-binding domain.
CC       {ECO:0000255|PROSITE-ProRule:PRU00108}.
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DR   EMBL; X89750; CAA61897.1; -; mRNA.
DR   EMBL; AF179900; AAF81643.1; -; mRNA.
DR   EMBL; CR450333; CAG29329.1; -; mRNA.
DR   EMBL; AK291112; BAF83801.1; -; mRNA.
DR   EMBL; AP001025; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471113; EAX01672.1; -; Genomic_DNA.
DR   EMBL; BC000814; AAH00814.1; -; mRNA.
DR   EMBL; BC031268; AAH31268.1; -; mRNA.
DR   EMBL; BE296707; -; NOT_ANNOTATED_CDS; mRNA.
DR   CCDS; CCDS11832.1; -. [Q15583-3]
DR   CCDS; CCDS11833.1; -. [Q15583-2]
DR   CCDS; CCDS11834.1; -. [Q15583-1]
DR   CCDS; CCDS11835.1; -. [Q15583-4]
DR   RefSeq; NP_001265611.1; NM_001278682.1.
DR   RefSeq; NP_001265613.1; NM_001278684.1. [Q15583-2]
DR   RefSeq; NP_001265615.1; NM_001278686.1. [Q15583-4]
DR   RefSeq; NP_003235.1; NM_003244.3. [Q15583-2]
DR   RefSeq; NP_733796.2; NM_170695.3. [Q15583-1]
DR   RefSeq; NP_775299.1; NM_173207.2. [Q15583-3]
DR   RefSeq; NP_775300.1; NM_173208.2. [Q15583-2]
DR   RefSeq; NP_775301.1; NM_173209.2. [Q15583-4]
DR   RefSeq; NP_775302.1; NM_173210.2. [Q15583-4]
DR   RefSeq; NP_775303.1; NM_173211.1. [Q15583-4]
DR   RefSeq; NP_777480.1; NM_174886.2. [Q15583-4]
DR   RefSeq; XP_011524037.1; XM_011525735.1. [Q15583-4]
DR   UniGene; Hs.373550; -.
DR   PDB; 2LK2; NMR; -; A=171-248.
DR   PDBsum; 2LK2; -.
DR   ProteinModelPortal; Q15583; -.
DR   SMR; Q15583; 171-248.
DR   BioGrid; 112908; 21.
DR   IntAct; Q15583; 9.
DR   MINT; MINT-145985; -.
DR   STRING; 9606.ENSP00000327959; -.
DR   PhosphoSite; Q15583; -.
DR   BioMuta; TGIF1; -.
DR   DMDM; 215274200; -.
DR   MaxQB; Q15583; -.
DR   PaxDb; Q15583; -.
DR   PRIDE; Q15583; -.
DR   Ensembl; ENST00000330513; ENSP00000327959; ENSG00000177426. [Q15583-1]
DR   Ensembl; ENST00000343820; ENSP00000339631; ENSG00000177426. [Q15583-2]
DR   Ensembl; ENST00000345133; ENSP00000343969; ENSG00000177426. [Q15583-4]
DR   Ensembl; ENST00000400167; ENSP00000383031; ENSG00000177426. [Q15583-4]
DR   Ensembl; ENST00000401449; ENSP00000385206; ENSG00000177426. [Q15583-4]
DR   Ensembl; ENST00000405385; ENSP00000384970; ENSG00000177426. [Q15583-4]
DR   Ensembl; ENST00000407501; ENSP00000384133; ENSG00000177426. [Q15583-2]
DR   Ensembl; ENST00000472042; ENSP00000449501; ENSG00000177426. [Q15583-4]
DR   Ensembl; ENST00000548489; ENSP00000447747; ENSG00000177426. [Q15583-4]
DR   Ensembl; ENST00000551541; ENSP00000450025; ENSG00000177426. [Q15583-4]
DR   Ensembl; ENST00000618001; ENSP00000483499; ENSG00000177426. [Q15583-3]
DR   GeneID; 7050; -.
DR   KEGG; hsa:7050; -.
DR   UCSC; uc002klu.3; human. [Q15583-1]
DR   UCSC; uc002klv.3; human. [Q15583-3]
DR   UCSC; uc002klw.3; human. [Q15583-2]
DR   CTD; 7050; -.
DR   GeneCards; TGIF1; -.
DR   GeneReviews; TGIF1; -.
DR   H-InvDB; HIX0174209; -.
DR   HGNC; HGNC:11776; TGIF1.
DR   HPA; CAB004596; -.
DR   HPA; HPA062160; -.
DR   MIM; 142946; phenotype.
DR   MIM; 602630; gene.
DR   neXtProt; NX_Q15583; -.
DR   Orphanet; 93925; Alobar holoprosencephaly.
DR   Orphanet; 93924; Lobar holoprosencephaly.
DR   Orphanet; 280200; Microform holoprosencephaly.
DR   Orphanet; 93926; Midline interhemispheric variant of holoprosencephaly.
DR   Orphanet; 220386; Semilobar holoprosencephaly.
DR   Orphanet; 280195; Septopreoptic holoprosencephaly.
DR   PharmGKB; PA36489; -.
DR   eggNOG; KOG0773; Eukaryota.
DR   eggNOG; ENOG410XPMQ; LUCA.
DR   GeneTree; ENSGT00550000074260; -.
DR   HOGENOM; HOG000232039; -.
DR   HOVERGEN; HBG001143; -.
DR   InParanoid; Q15583; -.
DR   KO; K19383; -.
DR   OMA; IAANNFT; -.
DR   PhylomeDB; Q15583; -.
DR   TreeFam; TF318093; -.
DR   Reactome; R-HSA-2173795; Downregulation of SMAD2/3:SMAD4 transcriptional activity.
DR   Reactome; R-HSA-2173796; SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription.
DR   SignaLink; Q15583; -.
DR   EvolutionaryTrace; Q15583; -.
DR   GeneWiki; Homeobox_protein_TGIF1; -.
DR   GenomeRNAi; 7050; -.
DR   NextBio; 27551; -.
DR   PRO; PR:Q15583; -.
DR   Proteomes; UP000005640; Chromosome 18.
DR   Bgee; Q15583; -.
DR   CleanEx; HS_TGIF1; -.
DR   ExpressionAtlas; Q15583; baseline and differential.
DR   Genevisible; Q15583; HS.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
DR   GO; GO:0000978; F:RNA polymerase II core promoter proximal region sequence-specific DNA binding; IDA:NTNU_SB.
DR   GO; GO:0003714; F:transcription corepressor activity; TAS:ProtInc.
DR   GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; TAS:ProtInc.
DR   GO; GO:0001078; F:transcriptional repressor activity, RNA polymerase II core promoter proximal region sequence-specific binding; IDA:NTNU_SB.
DR   GO; GO:0007368; P:determination of left/right symmetry; IEA:Ensembl.
DR   GO; GO:0009953; P:dorsal/ventral pattern formation; IEA:Ensembl.
DR   GO; GO:0010467; P:gene expression; TAS:Reactome.
DR   GO; GO:0007275; P:multicellular organismal development; TAS:ProtInc.
DR   GO; GO:0008285; P:negative regulation of cell proliferation; IEA:Ensembl.
DR   GO; GO:0048387; P:negative regulation of retinoic acid receptor signaling pathway; IEA:Ensembl.
DR   GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:NTNU_SB.
DR   GO; GO:0001843; P:neural tube closure; IEA:Ensembl.
DR   GO; GO:0038092; P:nodal signaling pathway; IEA:Ensembl.
DR   GO; GO:0048146; P:positive regulation of fibroblast proliferation; IEA:Ensembl.
DR   GO; GO:0045666; P:positive regulation of neuron differentiation; IEA:Ensembl.
DR   GO; GO:0010470; P:regulation of gastrulation; IEA:Ensembl.
DR   GO; GO:0042493; P:response to drug; IEA:Ensembl.
DR   GO; GO:0060041; P:retina development in camera-type eye; IEA:Ensembl.
DR   GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; TAS:Reactome.
DR   GO; GO:0006351; P:transcription, DNA-templated; TAS:Reactome.
DR   GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; TAS:Reactome.
DR   Gene3D; 1.10.10.60; -; 1.
DR   InterPro; IPR001356; Homeobox_dom.
DR   InterPro; IPR008422; Homeobox_KN_domain.
DR   InterPro; IPR009057; Homeodomain-like.
DR   Pfam; PF05920; Homeobox_KN; 1.
DR   SMART; SM00389; HOX; 1.
DR   SUPFAM; SSF46689; SSF46689; 1.
DR   PROSITE; PS50071; HOMEOBOX_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Complete proteome;
KW   Disease mutation; DNA-binding; Holoprosencephaly; Homeobox; Nucleus;
KW   Polymorphism; Reference proteome; Repressor; Transcription;
KW   Transcription regulation.
FT   CHAIN         1    401       Homeobox protein TGIF1.
FT                                /FTId=PRO_0000049318.
FT   DNA_BIND    164    226       Homeobox; TALE-type.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00108}.
FT   MOTIF       153    157       CTBP-binding motif.
FT   COMPBIAS    165    168       Poly-Arg.
FT   VAR_SEQ       1    149       Missing (in isoform 4).
FT                                {ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_046848.
FT   VAR_SEQ       1    129       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:10764806,
FT                                ECO:0000303|PubMed:15489334,
FT                                ECO:0000303|PubMed:8537382,
FT                                ECO:0000303|Ref.3}.
FT                                /FTId=VSP_013020.
FT   VAR_SEQ       1    115       Missing (in isoform 3).
FT                                {ECO:0000303|PubMed:14702039}.
FT                                /FTId=VSP_043108.
FT   VAR_SEQ     116    134       PSQGAQGPAPRRRLLETMK -> MTCSGKSCALARSSLTSS
FT                                Q (in isoform 3).
FT                                {ECO:0000303|PubMed:14702039}.
FT                                /FTId=VSP_043109.
FT   VAR_SEQ     130    133       LETM -> MKGK (in isoform 2).
FT                                {ECO:0000303|PubMed:10764806,
FT                                ECO:0000303|PubMed:15489334,
FT                                ECO:0000303|PubMed:8537382,
FT                                ECO:0000303|Ref.3}.
FT                                /FTId=VSP_013021.
FT   VARIANT     157    157       S -> C (in HPE4).
FT                                {ECO:0000269|PubMed:10835638}.
FT                                /FTId=VAR_009961.
FT   VARIANT     192    192       P -> R (in HPE4).
FT                                {ECO:0000269|PubMed:10835638}.
FT                                /FTId=VAR_009962.
FT   VARIANT     236    236       Q -> L (in HPE4).
FT                                {ECO:0000269|PubMed:15221788}.
FT                                /FTId=VAR_023803.
FT   VARIANT     280    280       T -> A (in HPE4).
FT                                {ECO:0000269|PubMed:10835638}.
FT                                /FTId=VAR_009963.
FT   VARIANT     289    289       P -> S (in dbSNP:rs11571512).
FT                                /FTId=VAR_047363.
FT   VARIANT     291    291       S -> F (in HPE4).
FT                                {ECO:0000269|PubMed:10835638}.
FT                                /FTId=VAR_009964.
FT   VARIANT     292    292       P -> L (in dbSNP:rs2229333).
FT                                /FTId=VAR_020151.
FT   VARIANT     292    292       P -> S (in dbSNP:rs4468717).
FT                                {ECO:0000269|PubMed:10764806,
FT                                ECO:0000269|Ref.3}.
FT                                /FTId=VAR_061268.
FT   CONFLICT     96     96       P -> Q (in Ref. 7; AAH31268).
FT                                {ECO:0000305}.
FT   HELIX       173    185       {ECO:0000244|PDB:2LK2}.
FT   HELIX       188    190       {ECO:0000244|PDB:2LK2}.
FT   HELIX       194    203       {ECO:0000244|PDB:2LK2}.
FT   STRAND      204    206       {ECO:0000244|PDB:2LK2}.
FT   HELIX       208    230       {ECO:0000244|PDB:2LK2}.
SQ   SEQUENCE   401 AA;  43013 MW;  4D9C76AFB37A29F0 CRC64;
     MVLAQSRVSA GVGSPHCSGS GGGGSDSFPW PASHPGNPQC SFSTAFLASP RLSRGTLAYL
     PPAPWSSLAT PSALLGSSCA PPPPPARCPQ PRALSPELGT KAGPRRPHRW ELPRSPSQGA
     QGPAPRRRLL ETMKGIVAAS GSETEDEDSM DIPLDLSSSA GSGKRRRRGN LPKESVQILR
     DWLYEHRYNA YPSEQEKALL SQQTHLSTLQ VCNWFINARR RLLPDMLRKD GKDPNQFTIS
     RRGAKISETS SVESVMGIKN FMPALEETPF HSCTAGPNPT LGRPLSPKPS SPGSVLARPS
     VICHTTVTAL KDVPFSLCQS VGVGQNTDIQ QIAAKNFTDT SLMYPEDTCK SGPSTNTQSG
     LFNTPPPTPP DLNQDFSGFQ LLVDVALKRA AEMELQAKLT A
//
ID   TRPS1_HUMAN             Reviewed;        1281 AA.
AC   Q9UHF7; B4E1Z5; Q08AU2; Q9NWE1; Q9UHH6;
DT   27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   27-MAR-2002, sequence version 2.
DT   11-NOV-2015, entry version 140.
DE   RecName: Full=Zinc finger transcription factor Trps1;
DE   AltName: Full=Tricho-rhino-phalangeal syndrome type I protein;
DE   AltName: Full=Zinc finger protein GC79;
GN   Name=TRPS1;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RX   PubMed=10615131; DOI=10.1038/71717;
RA   Momeni P., Gloeckner G., Schmidt O., von Holtum D., Albrecht B.,
RA   Gillessen-Kaesbach G., Hennekam R.C.M., Meinecke P., Zabel B.,
RA   Rosenthal A., Horsthemke B., Luedecke H.-J.;
RT   "Mutations in a new gene, encoding a zinc-finger protein, cause
RT   tricho-rhino-phalangeal syndrome type I.";
RL   Nat. Genet. 24:71-74(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Prostate;
RX   PubMed=10974077; DOI=10.1093/jnci/92.17.1414;
RA   Chang G.T.G., Steenbeek M., Schippers E., Blok L.J., van Weerden W.M.,
RA   van Alewijk D.C.J.G., Eussen B.H.J., van Steenbrugge G.J.,
RA   Brinkmann A.O.;
RT   "Characterization of a zinc-finger protein and its association with
RT   apoptosis in prostate cancer cells.";
RL   J. Natl. Cancer Inst. 92:1414-1421(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 495-1281 (ISOFORM 1).
RC   TISSUE=Embryo, and Trachea;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16421571; DOI=10.1038/nature04406;
RA   Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S.,
RA   Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A.,
RA   Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X.,
RA   Allen N.R., Anderson S., Asakawa T., Blechschmidt K., Bloom T.,
RA   Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K.,
RA   DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G.,
RA   Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B.,
RA   Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA   Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA   Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C.,
RA   O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K.,
RA   Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R.,
RA   Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K.,
RA   Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q.,
RA   Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N.,
RA   Lander E.S.;
RT   "DNA sequence and analysis of human chromosome 8.";
RL   Nature 439:331-335(2006).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   FUNCTION, INTERACTION WITH RNF4, AND SUBCELLULAR LOCATION.
RX   PubMed=12885770; DOI=10.1074/jbc.M306259200;
RA   Kaiser F.J., Moeroey T., Chang G.T., Horsthemke B., Luedecke H.J.;
RT   "The RING finger protein RNF4, a co-regulator of transcription,
RT   interacts with the TRPS1 transcription factor.";
RL   J. Biol. Chem. 278:38780-38785(2003).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1085, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA   Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA   Mann M.;
RT   "Global, in vivo, and site-specific phosphorylation dynamics in
RT   signaling networks.";
RL   Cell 127:635-648(2006).
RN   [8]
RP   SUMOYLATION AT LYS-1192 AND LYS-1201, FUNCTION, AND MUTAGENESIS OF
RP   LYS-1192 AND LYS-1201.
RX   PubMed=17391059; DOI=10.1515/BC.2007.051;
RA   Kaiser F.J., Ludecke H.J., Weger S.;
RT   "SUMOylation modulates transcriptional repression by TRPS1.";
RL   Biol. Chem. 388:381-390(2007).
RN   [9]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA   Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT   a refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [10]
RP   INTERACTION WITH GLI3.
RX   PubMed=19389374; DOI=10.1016/j.ydbio.2009.01.012;
RA   Wuelling M., Kaiser F.J., Buelens L.A., Braunholz D., Shivdasani R.A.,
RA   Depping R., Vortkamp A.;
RT   "Trps1, a regulator of chondrocyte proliferation and differentiation,
RT   interacts with the activator form of Gli3.";
RL   Dev. Biol. 328:40-53(2009).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-751; SER-1041 AND
RP   SER-1085, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA   Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full
RT   phosphorylation site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [12]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA   Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [13]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-766; LYS-850 AND LYS-1201,
RP   AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25218447; DOI=10.1038/nsmb.2890;
RA   Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA   Vertegaal A.C.;
RT   "Uncovering global SUMOylation signaling networks in a site-specific
RT   manner.";
RL   Nat. Struct. Mol. Biol. 21:927-936(2014).
RN   [14]
RP   VARIANTS TRPS3 ASP-894; PRO-901; GLN-908; PRO-908 AND THR-919.
RX   PubMed=11112658; DOI=10.1086/316926;
RA   Luedecke H.-J., Schaper J., Meinecke P., Momeni P., Gross S.,
RA   von Holtum D., Hirche H., Abramowicz M.J., Albrecht B., Apacik C.,
RA   Christen H.-J., Claussen U., Devriendt K., Fastnacht E., Forderer A.,
RA   Friedrich U., Goodship T.H.J., Greiwe M., Hamm H., Hennekam R.C.M.,
RA   Hinkel G.K., Hoeltzenbein M., Kayserili H., Majewski F., Mathieu M.,
RA   McLeod R., Midro A.T., Moog U., Nagai T., Niikawa N., Oerstavik K.H.,
RA   Ploechl E., Seitz C., Schmidtke J., Tranebjaerg L., Tsukahara M.,
RA   Wittwer B., Zabel B., Gillessen-Kaesbach G., Horsthemke B.;
RT   "Genotypic and phenotypic spectrum in tricho-rhino-phalangeal syndrome
RT   types I and III.";
RL   Am. J. Hum. Genet. 68:81-91(2001).
RN   [15]
RP   VARIANT TRPS3 GLN-908.
RX   PubMed=11807863; DOI=10.1002/ajmg.10081;
RA   Kobayashi H., Hino M., Shimodahira M., Iwakura T., Ishihara T.,
RA   Ikekubo K., Ogawa Y., Nakao K., Kurahachi H.;
RT   "Missense mutation of TRPS1 in a family of tricho-rhino-phalangeal
RT   syndrome type III.";
RL   Am. J. Med. Genet. 107:26-29(2002).
RN   [16]
RP   VARIANTS TRPS1 CYS-952 AND HIS-952, AND CHARACTERIZATION OF VARIANTS
RP   TRPS1 CYS-952 AND HIS-952.
RX   PubMed=14560312; DOI=10.1038/sj.ejhg.5201094;
RA   Kaiser F.J., Brega P., Raff M.L., Byers P.H., Gallati S., Kay T.T.,
RA   de Almeida S., Horsthemke B., Luedecke H.-J.;
RT   "Novel missense mutations in the TRPS1 transcription factor define the
RT   nuclear localization signal.";
RL   Eur. J. Hum. Genet. 12:121-126(2004).
CC   -!- FUNCTION: Transcriptional repressor. Binds specifically to GATA
CC       sequences and represses expression of GATA-regulated genes at
CC       selected sites and stages in vertebrate development. Regulates
CC       chondrocyte proliferation and differentiation. Executes multiple
CC       functions in proliferating chondrocytes, expanding the region of
CC       distal chondrocytes, activating proliferation in columnar cells
CC       and supporting the differentiation of columnar into hypertrophic
CC       chondrocytes. {ECO:0000269|PubMed:12885770,
CC       ECO:0000269|PubMed:17391059}.
CC   -!- SUBUNIT: Interacts with RNF4; regulates TRPS1 repressor activity.
CC       Interacts specifically with the activator form of GLI3 (GLI3A) but
CC       not with the repressor form (GLI3R). {ECO:0000269|PubMed:12885770,
CC       ECO:0000269|PubMed:19389374}.
CC   -!- INTERACTION:
CC       Q9Q2G4:ORF (xeno); NbExp=3; IntAct=EBI-2556151, EBI-6248094;
CC       P78317:RNF4; NbExp=2; IntAct=EBI-2556151, EBI-2340927;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12885770}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q9UHF7-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9UHF7-2; Sequence=VSP_037549;
CC       Name=3;
CC         IsoId=Q9UHF7-3; Sequence=VSP_037550;
CC   -!- TISSUE SPECIFICITY: Ubiquitously expressed in the adult. Found in
CC       fetal brain, lung, kidney, liver, spleen and thymus. More highly
CC       expressed in androgen-dependent than in androgen-independent
CC       prostate cancer cells.
CC   -!- PTM: Sumoylated. Sumoylation in the repressor domain inhibits the
CC       transcription repression activity. Sumoylation on Lys-1201 is the
CC       major site. Appears to be sumoylated on multiple sites.
CC       {ECO:0000269|PubMed:17391059}.
CC   -!- DISEASE: Tricho-rhino-phalangeal syndrome 1 (TRPS1) [MIM:190350]:
CC       Autosomal dominant disorder characterized by craniofacial and
CC       skeletal abnormalities. It is allelic with tricho-rhino-phalangeal
CC       type 3. Typical features include sparse scalp hair, a bulbous tip
CC       of the nose, protruding ears, a long flat philtrum and a thin
CC       upper vermilion border. Skeletal defects include cone-shaped
CC       epiphyses at the phalanges, hip malformations and short stature.
CC       {ECO:0000269|PubMed:14560312}. Note=The disease is caused by
CC       mutations affecting the gene represented in this entry.
CC   -!- DISEASE: Tricho-rhino-phalangeal syndrome 2 (TRPS2) [MIM:150230]:
CC       A syndrome that combines the clinical features of tricho-rhino-
CC       phalangeal syndrome type 1 and multiple exostoses type 1. Affected
CC       individuals manifest multiple dysmorphic facial features including
CC       large, laterally protruding ears, a bulbous nose, an elongated
CC       upper lip, as well as sparse scalp hair, winged scapulae, multiple
CC       cartilaginous exostoses, redundant skin, and mental retardation.
CC       Note=The gene represented in this entry is involved in disease
CC       pathogenesis. A chromosomal aberration resulting in the loss of
CC       functional copies of TRPS1 and EXT1 has been found in TRPS2
CC       patients.
CC   -!- DISEASE: Tricho-rhino-phalangeal syndrome 3 (TRPS3) [MIM:190351]:
CC       Autosomal dominant disorder characterized by craniofacial and
CC       skeletal abnormalities. It is allelic with tricho-rhino-phalangeal
CC       type 1. In TRPS3 a more severe brachydactyly and growth
CC       retardation are observed. {ECO:0000269|PubMed:11112658,
CC       ECO:0000269|PubMed:11807863}. Note=The disease is caused by
CC       mutations affecting the gene represented in this entry.
CC   -!- SIMILARITY: Contains 7 C2H2-type zinc fingers.
CC       {ECO:0000255|PROSITE-ProRule:PRU00042}.
CC   -!- SIMILARITY: Contains 1 GATA-type zinc finger.
CC       {ECO:0000255|PROSITE-ProRule:PRU00094}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAI25021.1; Type=Erroneous termination; Positions=854; Note=Translated as Gln.; Evidence={ECO:0000305};
CC       Sequence=BAA91441.1; Type=Frameshift; Positions=1276; Evidence={ECO:0000305};
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DR   EMBL; AF183810; AAF23614.1; -; mRNA.
DR   EMBL; AF264784; AAG21134.1; -; mRNA.
DR   EMBL; AK000948; BAA91441.1; ALT_FRAME; mRNA.
DR   EMBL; AK304046; BAG64957.1; -; mRNA.
DR   EMBL; AF178030; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC125020; AAI25021.1; ALT_SEQ; mRNA.
DR   CCDS; CCDS6318.2; -. [Q9UHF7-2]
DR   CCDS; CCDS64957.1; -. [Q9UHF7-3]
DR   RefSeq; NP_001269831.1; NM_001282902.2. [Q9UHF7-3]
DR   RefSeq; NP_001269832.1; NM_001282903.2.
DR   RefSeq; NP_054831.2; NM_014112.4. [Q9UHF7-2]
DR   RefSeq; XP_005251106.1; XM_005251049.2. [Q9UHF7-1]
DR   RefSeq; XP_006716688.1; XM_006716625.1. [Q9UHF7-2]
DR   RefSeq; XP_011515566.1; XM_011517264.1. [Q9UHF7-2]
DR   RefSeq; XP_011515567.1; XM_011517265.1. [Q9UHF7-2]
DR   RefSeq; XP_011515568.1; XM_011517266.1. [Q9UHF7-2]
DR   RefSeq; XP_011515570.1; XM_011517268.1. [Q9UHF7-1]
DR   UniGene; Hs.657018; -.
DR   ProteinModelPortal; Q9UHF7; -.
DR   SMR; Q9UHF7; 893-938.
DR   BioGrid; 113078; 13.
DR   IntAct; Q9UHF7; 6.
DR   MINT; MINT-271027; -.
DR   STRING; 9606.ENSP00000379065; -.
DR   PhosphoSite; Q9UHF7; -.
DR   DMDM; 20140909; -.
DR   MaxQB; Q9UHF7; -.
DR   PaxDb; Q9UHF7; -.
DR   PRIDE; Q9UHF7; -.
DR   Ensembl; ENST00000220888; ENSP00000220888; ENSG00000104447. [Q9UHF7-1]
DR   Ensembl; ENST00000395715; ENSP00000379065; ENSG00000104447. [Q9UHF7-2]
DR   Ensembl; ENST00000520276; ENSP00000428680; ENSG00000104447. [Q9UHF7-3]
DR   GeneID; 7227; -.
DR   KEGG; hsa:7227; -.
DR   UCSC; uc003yny.3; human. [Q9UHF7-2]
DR   UCSC; uc003ynz.3; human. [Q9UHF7-1]
DR   UCSC; uc011lhy.2; human. [Q9UHF7-3]
DR   CTD; 7227; -.
DR   GeneCards; TRPS1; -.
DR   HGNC; HGNC:12340; TRPS1.
DR   MIM; 150230; phenotype.
DR   MIM; 190350; phenotype.
DR   MIM; 190351; phenotype.
DR   MIM; 604386; gene.
DR   neXtProt; NX_Q9UHF7; -.
DR   Orphanet; 502; Langer-Giedion syndrome.
DR   Orphanet; 77258; Trichorhinophalangeal syndrome type 1 and 3.
DR   PharmGKB; PA37013; -.
DR   eggNOG; KOG1601; Eukaryota.
DR   eggNOG; COG5641; LUCA.
DR   GeneTree; ENSGT00760000119221; -.
DR   HOGENOM; HOG000146438; -.
DR   HOVERGEN; HBG067120; -.
DR   InParanoid; Q9UHF7; -.
DR   OMA; ENKEHSC; -.
DR   OrthoDB; EOG72ZCD8; -.
DR   PhylomeDB; Q9UHF7; -.
DR   TreeFam; TF350812; -.
DR   ChiTaRS; TRPS1; human.
DR   GeneWiki; Tricho-rhino-phalangeal_syndrome_Type_1; -.
DR   GenomeRNAi; 7227; -.
DR   NextBio; 28303; -.
DR   PRO; PR:Q9UHF7; -.
DR   Proteomes; UP000005640; Chromosome 8.
DR   Bgee; Q9UHF7; -.
DR   CleanEx; HS_TRPS1; -.
DR   ExpressionAtlas; Q9UHF7; baseline and differential.
DR   Genevisible; Q9UHF7; HS.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0005667; C:transcription factor complex; IBA:GO_Central.
DR   GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR   GO; GO:0000977; F:RNA polymerase II regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0001085; F:RNA polymerase II transcription factor binding; IBA:GO_Central.
DR   GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; TAS:ProtInc.
DR   GO; GO:0001228; F:transcriptional activator activity, RNA polymerase II transcription regulatory region sequence-specific binding; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; TAS:ProtInc.
DR   GO; GO:0048646; P:anatomical structure formation involved in morphogenesis; IBA:GO_Central.
DR   GO; GO:0048468; P:cell development; IBA:GO_Central.
DR   GO; GO:0045165; P:cell fate commitment; IBA:GO_Central.
DR   GO; GO:0002062; P:chondrocyte differentiation; IEA:Ensembl.
DR   GO; GO:0048565; P:digestive tract development; IBA:GO_Central.
DR   GO; GO:0007507; P:heart development; IBA:GO_Central.
DR   GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
DR   GO; GO:0006607; P:NLS-bearing protein import into nucleus; TAS:ProtInc.
DR   GO; GO:0009887; P:organ morphogenesis; IBA:GO_Central.
DR   GO; GO:1902043; P:positive regulation of extrinsic apoptotic signaling pathway via death domain receptors; IEA:Ensembl.
DR   GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IBA:GOC.
DR   GO; GO:0032330; P:regulation of chondrocyte differentiation; ISS:UniProtKB.
DR   GO; GO:0001501; P:skeletal system development; TAS:ProtInc.
DR   GO; GO:0009888; P:tissue development; IBA:GO_Central.
DR   GO; GO:0006366; P:transcription from RNA polymerase II promoter; TAS:ProtInc.
DR   GO; GO:0007178; P:transmembrane receptor protein serine/threonine kinase signaling pathway; IEA:Ensembl.
DR   Gene3D; 3.30.50.10; -; 1.
DR   InterPro; IPR028440; Trps1.
DR   InterPro; IPR007087; Znf_C2H2.
DR   InterPro; IPR015880; Znf_C2H2-like.
DR   InterPro; IPR000679; Znf_GATA.
DR   InterPro; IPR013088; Znf_NHR/GATA.
DR   PANTHER; PTHR10071:SF176; PTHR10071:SF176; 2.
DR   Pfam; PF00320; GATA; 1.
DR   PRINTS; PR00619; GATAZNFINGER.
DR   SMART; SM00355; ZnF_C2H2; 9.
DR   SMART; SM00401; ZnF_GATA; 1.
DR   PROSITE; PS00344; GATA_ZN_FINGER_1; 1.
DR   PROSITE; PS50114; GATA_ZN_FINGER_2; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 2.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Complete proteome; Disease mutation;
KW   DNA-binding; Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein;
KW   Reference proteome; Repeat; Repressor; Transcription;
KW   Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT   CHAIN         1   1281       Zinc finger transcription factor Trps1.
FT                                /FTId=PRO_0000083508.
FT   ZN_FING     222    247       C2H2-type 1; atypical.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00042}.
FT   ZN_FING     333    358       C2H2-type 2; atypical.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00042}.
FT   ZN_FING     614    637       C2H2-type 3; atypical.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00042}.
FT   ZN_FING     666    689       C2H2-type 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     692    715       C2H2-type 5. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     896    920       GATA-type. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00094}.
FT   ZN_FING    1215   1237       C2H2-type 6. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING    1243   1267       C2H2-type 7. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   REGION      635    819       Mediates interaction with GLI3.
FT   REGION      985   1184       Mediates interaction with RNF4.
FT                                {ECO:0000250}.
FT   REGION     1163   1281       Transcriptional repressor domain.
FT                                {ECO:0000250}.
FT   MOD_RES     127    127       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q925H1}.
FT   MOD_RES     216    216       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q925H1}.
FT   MOD_RES     751    751       Phosphothreonine.
FT                                {ECO:0000244|PubMed:20068231}.
FT   MOD_RES    1041   1041       Phosphoserine.
FT                                {ECO:0000244|PubMed:20068231}.
FT   MOD_RES    1085   1085       Phosphoserine.
FT                                {ECO:0000244|PubMed:17081983,
FT                                ECO:0000244|PubMed:20068231}.
FT   CROSSLNK    766    766       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:25218447}.
FT   CROSSLNK    850    850       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:25218447}.
FT   CROSSLNK   1192   1192       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO).
FT   CROSSLNK   1201   1201       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO);
FT                                alternate.
FT   CROSSLNK   1201   1201       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2);
FT                                alternate. {ECO:0000244|PubMed:25218447}.
FT   VAR_SEQ       1      1       M -> MPYEVNAGYDFTNM (in isoform 2).
FT                                {ECO:0000303|PubMed:10615131}.
FT                                /FTId=VSP_037549.
FT   VAR_SEQ       1      1       M -> MQSNM (in isoform 3).
FT                                {ECO:0000303|PubMed:14702039}.
FT                                /FTId=VSP_037550.
FT   VARIANT     654    654       S -> L (in dbSNP:rs7002384).
FT                                /FTId=VAR_038197.
FT   VARIANT     894    894       V -> D (in TRPS3; in heterozygous status
FT                                has a milder effect causing TRPS1).
FT                                {ECO:0000269|PubMed:11112658}.
FT                                /FTId=VAR_012807.
FT   VARIANT     901    901       T -> P (in TRPS3; severe).
FT                                {ECO:0000269|PubMed:11112658}.
FT                                /FTId=VAR_012808.
FT   VARIANT     908    908       R -> P (in TRPS3; severe).
FT                                {ECO:0000269|PubMed:11112658}.
FT                                /FTId=VAR_012809.
FT   VARIANT     908    908       R -> Q (in TRPS3).
FT                                {ECO:0000269|PubMed:11112658,
FT                                ECO:0000269|PubMed:11807863}.
FT                                /FTId=VAR_012810.
FT   VARIANT     919    919       A -> T (in TRPS3).
FT                                {ECO:0000269|PubMed:11112658}.
FT                                /FTId=VAR_012811.
FT   VARIANT     952    952       R -> C (in TRPS1; prevents the transport
FT                                into the nucleus and thus reduces the
FT                                nuclear TRPS1 concentration consistent
FT                                with haploinsufficiency).
FT                                {ECO:0000269|PubMed:14560312}.
FT                                /FTId=VAR_038198.
FT   VARIANT     952    952       R -> H (in TRPS1; prevents the transport
FT                                into the nucleus and thus reduces the
FT                                nuclear TRPS1 concentration consistent
FT                                with haploinsufficiency).
FT                                {ECO:0000269|PubMed:14560312}.
FT                                /FTId=VAR_038199.
FT   MUTAGEN    1192   1192       K->R: Very little change in sumoylation
FT                                and 30% reduction in repression activity.
FT                                Almost complete loss of sumoylation and
FT                                70% reduction in repression activity;
FT                                when associated with R-1201.
FT                                {ECO:0000269|PubMed:17391059}.
FT   MUTAGEN    1201   1201       K->R: Great loss of sumoylation and 30%
FT                                reduction in repression activity. Almost
FT                                complete loss of sumoylation and 70%
FT                                reduction in repression activity; when
FT                                associated with R-1192.
FT                                {ECO:0000269|PubMed:17391059}.
FT   CONFLICT    115    115       S -> F (in Ref. 1; AAF23614).
FT                                {ECO:0000305}.
FT   CONFLICT    582    582       T -> A (in Ref. 3; BAG64957).
FT                                {ECO:0000305}.
SQ   SEQUENCE   1281 AA;  141521 MW;  2157B04F5BEB71CC CRC64;
     MVRKKNPPLR NVASEGEGQI LEPIGTESKV SGKNKEFSAD QMSENTDQSD AAELNHKEEH
     SLHVQDPSSS SKKDLKSAVL SEKAGFNYES PSKGGNFPSF PHDEVTDRNM LAFSSPAAGG
     VCEPLKSPQR AEADDPQDMA CTPSGDSLET KEDQKMSPKA TEETGQAQSG QANCQGLSPV
     SVASKNPQVP SDGGVRLNKS KTDLLVNDNP DPAPLSPELQ DFKCNICGYG YYGNDPTDLI
     KHFRKYHLGL HNRTRQDAEL DSKILALHNM VQFSHSKDFQ KVNRSVFSGV LQDINSSRPV
     LLNGTYDVQV TSGGTFIGIG RKTPDCQGNT KYFRCKFCNF TYMGNSSTEL EQHFLQTHPN
     KIKASLPSSE VAKPSEKNSN KSIPALQSSD SGDLGKWQDK ITVKAGDDTP VGYSVPIKPL
     DSSRQNGTEA TSYYWCKFCS FSCESSSSLK LLEHYGKQHG AVQSGGLNPE LNDKLSRGSV
     INQNDLAKSS EGETMTKTDK SSSGAKKKDF SSKGAEDNMV TSYNCQFCDF RYSKSHGPDV
     IVVGPLLRHY QQLHNIHKCT IKHCPFCPRG LCSPEKHLGE ITYPFACRKS NCSHCALLLL
     HLSPGAAGSS RVKHQCHQCS FTTPDVDVLL FHYESVHESQ ASDVKQEANH LQGSDGQQSV
     KESKEHSCTK CDFITQVEEE ISRHYRRAHS CYKCRQCSFT AADTQSLLEH FNTVHCQEQD
     ITTANGEEDG HAISTIKEEP KIDFRVYNLL TPDSKMGEPV SESVVKREKL EEKDGLKEKV
     WTESSSDDLR NVTWRGADIL RGSPSYTQAS LGLLTPVSGT QEQTKTLRDS PNVEAAHLAR
     PIYGLAVETK GFLQGAPAGG EKSGALPQQY PASGENKSKD ESQSLLRRRR GSGVFCANCL
     TTKTSLWRKN ANGGYVCNAC GLYQKLHSTP RPLNIIKQNN GEQIIRRRTR KRLNPEALQA
     EQLNKQQRGS NEEQVNGSPL ERRSEDHLTE SHQREIPLPS LSKYEAQGSL TKSHSAQQPV
     LVSQTLDIHK RMQPLHIQIK SPQESTGDPG NSSSVSEGKG SSERGSPIEK YMRPAKHPNY
     SPPGSPIEKY QYPLFGLPFV HNDFQSEADW LRFWSKYKLS VPGNPHYLSH VPGLPNPCQN
     YVPYPTFNLP PHFSAVGSDN DIPLDLAIKH SRPGPTANGA SKEKTKAPPN VKNEGPLNVV
     KTEKVDRSTQ DELSTKCVHC GIVFLDEVMY ALHMSCHGDS GPFQCSICQH LCTDKYDFTT
     HIQRGLHRNN AQVEKNGKPK E
//
ID   TTKB_DROME              Reviewed;         643 AA.
AC   P17789; A4V3Q4; Q32KE0; Q9V9V1; Q9V9V3;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   02-MAY-2002, sequence version 2.
DT   11-NOV-2015, entry version 157.
DE   RecName: Full=Protein tramtrack, beta isoform;
DE   AltName: Full=Repressor protein fushi tarazu;
DE   AltName: Full=Tramtrack p69;
GN   Name=ttk; Synonyms=FTZ-F2; ORFNames=CG1856;
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
OC   Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha;
OC   Ephydroidea; Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND DEVELOPMENTAL STAGE.
RC   TISSUE=Embryo;
RX   PubMed=2104801;
RA   Harrison S.D., Travers A.A.;
RT   "The tramtrack gene encodes a Drosophila finger protein that interacts
RT   with the ftz transcriptional regulatory region and shows a novel
RT   embryonic expression pattern.";
RL   EMBO J. 9:207-216(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND DEVELOPMENTAL STAGE.
RC   TISSUE=Embryo;
RX   PubMed=8223261;
RA   Brown J.L., Wu C.;
RT   "Repression of Drosophila pair-rule segmentation genes by ectopic
RT   expression of tramtrack.";
RL   Development 117:45-58(1993).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RX   PubMed=8504931; DOI=10.1101/gad.7.6.1085;
RA   Xiong W.C., Montell C.;
RT   "Tramtrack is a transcriptional repressor required for cell fate
RT   determination in the Drosophila eye.";
RL   Genes Dev. 7:1085-1096(1993).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley;
RX   PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA   Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA   Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA   George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA   Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
RA   Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
RA   Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
RA   Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
RA   Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
RA   Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
RA   Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
RA   Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
RA   Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
RA   de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
RA   Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
RA   Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
RA   Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
RA   Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
RA   Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
RA   Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
RA   Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
RA   Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
RA   Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
RA   Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
RA   Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
RA   Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
RA   Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
RA   Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
RA   Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA   Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
RA   Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
RA   Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
RA   Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
RA   Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
RA   Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
RA   Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [5]
RP   GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
RC   STRAIN=Berkeley;
RX   PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
RA   Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
RA   Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a
RT   systematic review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Berkeley; TISSUE=Embryo;
RX   PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA   Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M.,
RA   George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H.,
RA   Rubin G.M., Celniker S.E.;
RT   "A Drosophila full-length cDNA resource.";
RL   Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Berkeley; TISSUE=Embryo;
RA   Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A.,
RA   Pacleb J.M., Park S., Wan K.H., Yu C., Celniker S.E.;
RL   Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
RN   [8]
RP   DNA-BINDING.
RX   PubMed=1640455; DOI=10.1016/0022-2836(92)90952-G;
RA   Fairall L., Harrison S.D., Travers A.A., Rhodes D.;
RT   "Sequence-specific DNA binding by a two zinc-finger peptide from the
RT   Drosophila melanogaster Tramtrack protein.";
RL   J. Mol. Biol. 226:349-366(1992).
RN   [9]
RP   FUNCTION, INTERACTION WITH TRL, AND HOMODIMERIZATION.
RX   PubMed=12384587; DOI=10.1093/nar/gkf570;
RA   Pagans S., Ortiz-Lombardia M., Espinas M.L., Bernues J., Azorin F.;
RT   "The Drosophila transcription factor tramtrack (TTK) interacts with
RT   Trithorax-like (GAGA) and represses GAGA-mediated activation.";
RL   Nucleic Acids Res. 30:4406-4413(2002).
RN   [10]
RP   FUNCTION, AND INTERACTION WITH PHYL.
RX   PubMed=17962185; DOI=10.1074/jbc.M707765200;
RA   Cooper S.E., Murawsky C.M., Lowe N., Travers A.A.;
RT   "Two modes of degradation of the tramtrack transcription factors by
RT   Siah homologues.";
RL   J. Biol. Chem. 283:1076-1083(2008).
RN   [11]
RP   X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 499-561.
RX   PubMed=8247159; DOI=10.1038/366483a0;
RA   Fairall L., Schwabe J.W.R., Chapman L., Finch J.T., Rhodes D.;
RT   "The crystal structure of a two zinc-finger peptide reveals an
RT   extension to the rules for zinc-finger/DNA recognition.";
RL   Nature 366:483-487(1993).
CC   -!- FUNCTION: Binds to a number of sites in the transcriptional
CC       regulatory region of ftz. Isoform beta is required to repress
CC       inappropriate segmentation gene transcription and repress genes
CC       incompatible with development of photoreceptor cell fates.
CC       Probable repressor of the transcription of the segmentation genes
CC       ftz, eve, h, odd, run, and en. Inhibits Trl-dependent activation
CC       of eve. May bind to the region AGGGC/TGG. Degradation of ttk is
CC       directed by binding of sinah or sina, via the adapter molecule
CC       phyl which binds to the BTB domain of ttk. A second method of
CC       degradation exists that is phyl-independent, this is mediated by
CC       recognition of motifs in the C-terminus of ttk.
CC       {ECO:0000269|PubMed:12384587, ECO:0000269|PubMed:17962185,
CC       ECO:0000269|PubMed:2104801, ECO:0000269|PubMed:8223261,
CC       ECO:0000269|PubMed:8504931}.
CC   -!- SUBUNIT: Can form homodimers. Interacts with Trl in vivo via the
CC       BTB domain. Interacts with phyl. {ECO:0000269|PubMed:12384587,
CC       ECO:0000269|PubMed:17962185}.
CC   -!- INTERACTION:
CC       Q0E8J0:MEP-1; NbExp=6; IntAct=EBI-6173284, EBI-91014;
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=Beta; Synonyms=p69, C, D, F;
CC         IsoId=P17789-1; Sequence=Displayed;
CC       Name=Alpha; Synonyms=p88, A, E;
CC         IsoId=P42282-1; Sequence=External;
CC   -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC       Expressed in preblastoderm embryos, followed by complete decay
CC       upon formation of the cellular blastoderm when ftz striped
CC       expression is at its peak. {ECO:0000269|PubMed:2104801,
CC       ECO:0000269|PubMed:8223261}.
CC   -!- SIMILARITY: Contains 1 BTB (POZ) domain. {ECO:0000255|PROSITE-
CC       ProRule:PRU00037}.
CC   -!- SIMILARITY: Contains 2 C2H2-type zinc fingers.
CC       {ECO:0000255|PROSITE-ProRule:PRU00042}.
CC   -!- CAUTION: It is uncertain whether Met-1 or Met-3 is the initiator.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA28544.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=ABB36443.1; Type=Frameshift; Positions=83, 426; Evidence={ECO:0000305};
CC       Sequence=CAA34981.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; X17121; CAA34981.1; ALT_INIT; mRNA.
DR   EMBL; M62856; AAA28544.1; ALT_INIT; mRNA.
DR   EMBL; X71627; CAA50634.1; -; mRNA.
DR   EMBL; AE014297; AAF57181.1; -; Genomic_DNA.
DR   EMBL; AE014297; AAF57182.3; -; Genomic_DNA.
DR   EMBL; AE014297; AAN14283.1; -; Genomic_DNA.
DR   EMBL; AY122169; AAM52681.1; -; mRNA.
DR   EMBL; BT001723; AAN71478.1; -; mRNA.
DR   EMBL; BT023939; ABB36443.1; ALT_FRAME; mRNA.
DR   PIR; S36017; S36017.
DR   RefSeq; NP_001189330.1; NM_001202401.1. [P17789-1]
DR   RefSeq; NP_524911.3; NM_080172.4. [P17789-1]
DR   RefSeq; NP_733446.1; NM_170567.3. [P17789-1]
DR   RefSeq; NP_733447.1; NM_170568.3. [P17789-1]
DR   UniGene; Dm.1526; -.
DR   PDB; 2DRP; X-ray; 2.80 A; A/D=501-563.
DR   PDBsum; 2DRP; -.
DR   ProteinModelPortal; P17789; -.
DR   SMR; P17789; 15-116, 501-562.
DR   BioGrid; 71315; 56.
DR   IntAct; P17789; 3.
DR   STRING; 7227.FBpp0085186; -.
DR   PaxDb; P17789; -.
DR   PRIDE; P17789; -.
DR   GeneID; 48317; -.
DR   CTD; 7272; -.
DR   FlyBase; FBgn0003870; ttk.
DR   eggNOG; ENOG410IFVR; Eukaryota.
DR   eggNOG; ENOG410XPVE; LUCA.
DR   OMA; VFSSQEY; -.
DR   EvolutionaryTrace; P17789; -.
DR   GenomeRNAi; 48317; -.
DR   NextBio; 839310; -.
DR   Proteomes; UP000000803; Chromosome 3R.
DR   Bgee; P17789; -.
DR   ExpressionAtlas; P17789; differential.
DR   Genevisible; P17789; DM.
DR   GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR   GO; GO:0005700; C:polytene chromosome; IDA:FlyBase.
DR   GO; GO:0017053; C:transcriptional repressor complex; IPI:FlyBase.
DR   GO; GO:0003682; F:chromatin binding; IDA:FlyBase.
DR   GO; GO:0003677; F:DNA binding; IDA:FlyBase.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0031208; F:POZ domain binding; IDA:FlyBase.
DR   GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
DR   GO; GO:0000978; F:RNA polymerase II core promoter proximal region sequence-specific DNA binding; IDA:FlyBase.
DR   GO; GO:0000980; F:RNA polymerase II distal enhancer sequence-specific DNA binding; IDA:FlyBase.
DR   GO; GO:0001078; F:transcriptional repressor activity, RNA polymerase II core promoter proximal region sequence-specific binding; IDA:FlyBase.
DR   GO; GO:0007298; P:border follicle cell migration; IMP:FlyBase.
DR   GO; GO:0048854; P:brain morphogenesis; IMP:FlyBase.
DR   GO; GO:0035147; P:branch fusion, open tracheal system; IMP:FlyBase.
DR   GO; GO:0060446; P:branching involved in open tracheal system development; IMP:FlyBase.
DR   GO; GO:0001709; P:cell fate determination; TAS:FlyBase.
DR   GO; GO:0040003; P:chitin-based cuticle development; IMP:FlyBase.
DR   GO; GO:0042675; P:compound eye cone cell differentiation; IMP:FlyBase.
DR   GO; GO:0048750; P:compound eye corneal lens morphogenesis; IMP:FlyBase.
DR   GO; GO:0048813; P:dendrite morphogenesis; IMP:FlyBase.
DR   GO; GO:0046843; P:dorsal appendage formation; IMP:FlyBase.
DR   GO; GO:0035001; P:dorsal trunk growth, open tracheal system; IMP:FlyBase.
DR   GO; GO:0007476; P:imaginal disc-derived wing morphogenesis; IMP:FlyBase.
DR   GO; GO:0002121; P:inter-male aggressive behavior; IMP:FlyBase.
DR   GO; GO:0031987; P:locomotion involved in locomotory behavior; IMP:FlyBase.
DR   GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:GOC.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:FlyBase.
DR   GO; GO:0048666; P:neuron development; IMP:FlyBase.
DR   GO; GO:0030707; P:ovarian follicle cell development; IMP:FlyBase.
DR   GO; GO:0007422; P:peripheral nervous system development; TAS:FlyBase.
DR   GO; GO:0043388; P:positive regulation of DNA binding; IDA:FlyBase.
DR   GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:FlyBase.
DR   GO; GO:0048053; P:R1/R6 development; IMP:FlyBase.
DR   GO; GO:0045467; P:R7 cell development; IMP:FlyBase.
DR   GO; GO:0008360; P:regulation of cell shape; IMP:FlyBase.
DR   GO; GO:0042682; P:regulation of compound eye cone cell fate specification; IMP:FlyBase.
DR   GO; GO:0016476; P:regulation of embryonic cell shape; IMP:FlyBase.
DR   GO; GO:0035151; P:regulation of tube size, open tracheal system; IMP:FlyBase.
DR   GO; GO:0001964; P:startle response; IMP:FlyBase.
DR   GO; GO:0007426; P:tracheal outgrowth, open tracheal system; IMP:FlyBase.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.160.60; -; 2.
DR   InterPro; IPR017956; AT_hook_DNA-bd_motif.
DR   InterPro; IPR000210; BTB/POZ_dom.
DR   InterPro; IPR011333; POZ_dom.
DR   InterPro; IPR007087; Znf_C2H2.
DR   InterPro; IPR015880; Znf_C2H2-like.
DR   InterPro; IPR013087; Znf_C2H2/integrase_DNA-bd.
DR   Pfam; PF00651; BTB; 1.
DR   SMART; SM00384; AT_hook; 1.
DR   SMART; SM00225; BTB; 1.
DR   SMART; SM00355; ZnF_C2H2; 2.
DR   SUPFAM; SSF54695; SSF54695; 1.
DR   PROSITE; PS50097; BTB; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 2.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 2.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Complete proteome; DNA-binding;
KW   Metal-binding; Nucleus; Reference proteome; Repeat; Transcription;
KW   Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN         1    643       Protein tramtrack, beta isoform.
FT                                /FTId=PRO_0000047079.
FT   DOMAIN       33     98       BTB. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00037}.
FT   ZN_FING     508    531       C2H2-type 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     538    561       C2H2-type 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   CONFLICT    255    255       T -> M (in Ref. 2; AAA28544).
FT                                {ECO:0000305}.
FT   CONFLICT    281    281       H -> Q (in Ref. 2; AAA28544).
FT                                {ECO:0000305}.
FT   CONFLICT    501    501       T -> I (in Ref. 2; AAA28544).
FT                                {ECO:0000305}.
FT   STRAND      501    504       {ECO:0000244|PDB:2DRP}.
FT   STRAND      507    509       {ECO:0000244|PDB:2DRP}.
FT   TURN        511    513       {ECO:0000244|PDB:2DRP}.
FT   STRAND      516    519       {ECO:0000244|PDB:2DRP}.
FT   HELIX       520    530       {ECO:0000244|PDB:2DRP}.
FT   STRAND      531    534       {ECO:0000244|PDB:2DRP}.
FT   TURN        541    543       {ECO:0000244|PDB:2DRP}.
FT   STRAND      546    548       {ECO:0000244|PDB:2DRP}.
FT   HELIX       550    560       {ECO:0000244|PDB:2DRP}.
SQ   SEQUENCE   643 AA;  68771 MW;  98DAEA1A5E97DC59 CRC64;
     MKMASQRFCL RWNNHQSNLL SVFDQLLHAE TFTDVTLAVE GQHLKAHKMV LSACSPYFNT
     LFVSHPEKHP IVILKDVPYS DMKSLLDFMY RGEVSVDQER LTAFLRVAES LRIKGLTEVN
     DDKPSPAAAA AGAGATGSES TATTPQLQRI QPYLVPQRNR SQAGGLLASA ANAGNTPTLP
     VQPSLLSSAL MPKRKRGRPR KLSGSSNGTG NDYDDFDREN MMNDSSDLGN GKMCNESYSG
     NDDGSDDNQP NAGHTDDLNE SRDSLPSKRS KNSKDHRVVS HHEDNSTSDG NDSDGEGLDT
     SYMEPQLMLD EYDEPVEFKY NPLTDNSSPT QDHTDGSHLN EQARQQAFLI AAQRKHQVET
     AAAAAASGIK LNIIGMAAGG AQVKSMVSIP KLTPIGKVNA ASTPLVSPAG SFSTATVKPR
     VQKRPKLGKQ NGDVKPAVFS SQEYLDIYNS NDGFKLKAAG LSGSTPNLSA GLGTPSVKTK
     LNLSSNVGEG EAEGSVRDYC TKEGEHTYRC KVCSRVYTHI SNFCRHYVTS HKRNVKVYPC
     PFCFKEFTRK DNMTAHVKII HKIENPSTAL ATVAAANLAG QPLGVSGAST PPPPDLSGQN
     SNQSLPATSN ALSTSSSSST SSSSGSLGPL TTSAPPAPAA AAQ
//
ID   ZEB1_HUMAN              Reviewed;        1124 AA.
AC   P37275; B4DJV0; B4DUW9; E9PCM7; F5H4I8; Q12924; Q13800; Q2KJ05;
AC   Q5T968; Q5VZ84; Q8NB68;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1999, sequence version 2.
DT   11-NOV-2015, entry version 164.
DE   RecName: Full=Zinc finger E-box-binding homeobox 1;
DE   AltName: Full=NIL-2-A zinc finger protein;
DE   AltName: Full=Negative regulator of IL2;
DE   AltName: Full=Transcription factor 8;
DE            Short=TCF-8;
GN   Name=ZEB1; Synonyms=AREB6, TCF8;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   PubMed=8138542;
RA   Watanabe Y., Kawakami K., Hirayama Y., Nagano K.;
RT   "Transcription factors positively and negatively regulating the Na,K-
RT   ATPase alpha 1 subunit gene.";
RL   J. Biochem. 114:849-855(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA   Bachman N.J., Scarpulla R.C.;
RT   "A human zinc finger homeodomain protein homologous to the chicken
RT   delta-crystallin enhancer binding protein, delta EF1.";
RL   Submitted (JUL-1994) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4), AND
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-798 (ISOFORM 5).
RC   TISSUE=Brain, and Thalamus;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15164054; DOI=10.1038/nature02462;
RA   Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA   Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA   Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA   Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA   Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J.,
RA   Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
RA   Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA   Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
RA   Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
RA   Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
RA   Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
RA   Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
RA   Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
RA   Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
RA   Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
RA   Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
RA   Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
RA   Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
RA   Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA   Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
RA   Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
RA   Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
RA   Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
RA   Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
RA   Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT   "The DNA sequence and comparative analysis of human chromosome 10.";
RL   Nature 429:375-381(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 390-1124.
RX   PubMed=1840704; DOI=10.1126/science.1840704;
RA   Williams T.M., Moolten D., Burlein J., Romano J., Bhaerman R.,
RA   Godillot A., Mellon M., Rauscher F.J. III, Kant J.A.;
RT   "Identification of a zinc finger protein that inhibits IL-2 gene
RT   expression.";
RL   Science 254:1791-1794(1991).
RN   [8]
RP   INVOLVEMENT IN PPCD3.
RX   PubMed=16252232; DOI=10.1086/497348;
RA   Krafchak C.M., Pawar H., Moroi S.E., Sugar A., Lichter P.R.,
RA   Mackey D.A., Mian S., Nairus T., Elner V., Schteingart M.T.,
RA   Downs C.A., Kijek T.G., Johnson J.M., Trager E.H., Rozsa F.W.,
RA   Mandal M.N.A., Epstein M.P., Vollrath D., Ayyagari R., Boehnke M.,
RA   Richards J.E.;
RT   "Mutations in TCF8 cause posterior polymorphous corneal dystrophy and
RT   ectopic expression of COL4A3 by corneal endothelial cells.";
RL   Am. J. Hum. Genet. 77:694-708(2005).
RN   [9]
RP   SUMOYLATION AT LYS-347 AND LYS-774.
RX   PubMed=16061479; DOI=10.1074/jbc.M504477200;
RA   Long J., Zuo D., Park M.;
RT   "Pc2-mediated sumoylation of Smad-interacting protein 1 attenuates
RT   transcriptional repression of E-cadherin.";
RL   J. Biol. Chem. 280:35477-35489(2005).
RN   [10]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA   Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA   Mann M.;
RT   "Global, in vivo, and site-specific phosphorylation dynamics in
RT   signaling networks.";
RL   Cell 127:635-648(2006).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-322, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [12]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA   Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT   a refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [13]
RP   FUNCTION.
RX   PubMed=19935649; DOI=10.1038/ncb1998;
RA   Wellner U., Schubert J., Burk U.C., Schmalhofer O., Zhu F.,
RA   Sonntag A., Waldvogel B., Vannier C., Darling D., zur Hausen A.,
RA   Brunton V.G., Morton J., Sansom O., Schuler J., Stemmler M.P.,
RA   Herzberger C., Hopt U., Keck T., Brabletz S., Brabletz T.;
RT   "The EMT-activator ZEB1 promotes tumorigenicity by repressing
RT   stemness-inhibiting microRNAs.";
RL   Nat. Cell Biol. 11:1487-1495(2009).
RN   [14]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-642; SER-679 AND
RP   THR-702, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA   Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA   Rodionov V., Han D.K.;
RT   "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT   reveals system-wide modulation of protein-protein interactions.";
RL   Sci. Signal. 2:RA46-RA46(2009).
RN   [15]
RP   FUNCTION.
RX   PubMed=20175752; DOI=10.1042/BJ20091578;
RA   Papadopoulou V., Postigo A., Sanchez-Tillo E., Porter A.C.,
RA   Wagner S.D.;
RT   "ZEB1 and CtBP form a repressive complex at a distal promoter element
RT   of the BCL6 locus.";
RL   Biochem. J. 427:541-550(2010).
RN   [16]
RP   FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH SMARCA4, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=20418909; DOI=10.1038/onc.2010.102;
RA   Sanchez-Tillo E., Lazaro A., Torrent R., Cuatrecasas M., Vaquero E.C.,
RA   Castells A., Engel P., Postigo A.;
RT   "ZEB1 represses E-cadherin and induces an EMT by recruiting the
RT   SWI/SNF chromatin-remodeling protein BRG1.";
RL   Oncogene 29:3490-3500(2010).
RN   [17]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-679, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA   Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full
RT   phosphorylation site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [18]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA   Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [19]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-493; LYS-504 AND LYS-515,
RP   AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25218447; DOI=10.1038/nsmb.2890;
RA   Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA   Vertegaal A.C.;
RT   "Uncovering global SUMOylation signaling networks in a site-specific
RT   manner.";
RL   Nat. Struct. Mol. Biol. 21:927-936(2014).
RN   [20]
RP   STRUCTURE BY NMR OF 583-642.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of the homeobox domain from human NIL-2-A zinc
RT   finger protein, transcription factor 8.";
RL   Submitted (APR-2007) to the PDB data bank.
RN   [21]
RP   VARIANTS FECD6 THR-78; ALA-649; PRO-810; PRO-840 AND THR-905.
RX   PubMed=20036349; DOI=10.1016/j.ajhg.2009.12.001;
RA   Riazuddin S.A., Zaghloul N.A., Al-Saif A., Davey L., Diplas B.H.,
RA   Meadows D.N., Eghrari A.O., Minear M.A., Li Y.J., Klintworth G.K.,
RA   Afshari N., Gregory S.G., Gottsch J.D., Katsanis N.;
RT   "Missense mutations in TCF8 cause late-onset Fuchs corneal dystrophy
RT   and interact with FCD4 on chromosome 9p.";
RL   Am. J. Hum. Genet. 86:45-53(2010).
RN   [22]
RP   INVOLVEMENT IN FECD6 AND PPCD3, VARIANT FECD6 HIS-640,
RP   CHARACTERIZATION OF VARIANTS FECD6 THR-78 AND HIS-640, AND VARIANT
RP   GLU-525.
RX   PubMed=23599324; DOI=10.1167/iovs.13-11781;
RA   Lechner J., Dash D.P., Muszynska D., Hosseini M., Segev F., George S.,
RA   Frazer D.G., Moore J.E., Kaye S.B., Young T., Simpson D.A.,
RA   Churchill A.J., Heon E., Willoughby C.E.;
RT   "Mutational spectrum of the ZEB1 gene in corneal dystrophies supports
RT   a genotype-phenotype correlation.";
RL   Invest. Ophthalmol. Vis. Sci. 54:3215-3223(2013).
RN   [23]
RP   VARIANTS FECD6 THR-78; ALA-649; SER-696; PRO-810; PRO-840 AND GLY-905,
RP   CHARACTERIZATION OF VARIANTS FECD6 THR-78; ALA-649; SER-696; PRO-810;
RP   PRO-840 AND GLY-905, AND SUBCELLULAR LOCATION.
RX   PubMed=25190660; DOI=10.1167/iovs.14-15247;
RA   Chung D.W., Frausto R.F., Ann L.B., Jang M.S., Aldave A.J.;
RT   "Functional impact of ZEB1 mutations associated with posterior
RT   polymorphous and Fuchs' endothelial corneal dystrophies.";
RL   Invest. Ophthalmol. Vis. Sci. 55:6159-6166(2014).
CC   -!- FUNCTION: Acts as a transcriptional repressor. Inhibits
CC       interleukin-2 (IL-2) gene expression. Enhances or represses the
CC       promoter activity of the ATP1A1 gene depending on the quantity of
CC       cDNA and on the cell type. Represses E-cadherin promoter and
CC       induces an epithelial-mesenchymal transition (EMT) by recruiting
CC       SMARCA4/BRG1. Represses BCL6 transcription in the presence of the
CC       corepressor CTBP1. Positively regulates neuronal differentiation.
CC       Represses RCOR1 transcription activation during neurogenesis.
CC       Represses transcription by binding to the E box (5'-CANNTG-3').
CC       Promotes tumorigenicity by repressing stemness-inhibiting
CC       microRNAs. {ECO:0000269|PubMed:19935649,
CC       ECO:0000269|PubMed:20175752, ECO:0000269|PubMed:20418909}.
CC   -!- SUBUNIT: Interacts (via N-terminus) with SMARCA4/BRG1.
CC       {ECO:0000269|PubMed:20418909}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20418909,
CC       ECO:0000269|PubMed:25190660}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=5;
CC       Name=1;
CC         IsoId=P37275-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P37275-2; Sequence=VSP_045184;
CC         Note=No experimental confirmation available.;
CC       Name=3;
CC         IsoId=P37275-3; Sequence=VSP_047280;
CC       Name=4;
CC         IsoId=P37275-4; Sequence=VSP_047281;
CC       Name=5;
CC         IsoId=P37275-5; Sequence=VSP_047279, VSP_045184;
CC   -!- TISSUE SPECIFICITY: Colocalizes with SMARCA4/BRG1 in E-cadherin-
CC       negative cells from established lines, and stroma of normal colon
CC       as well as in de-differentiated epithelial cells at the invasion
CC       front of colorectal carcinomas (at protein level). Expressed in
CC       heart and skeletal muscle, but not in liver, spleen, or pancreas.
CC       {ECO:0000269|PubMed:20418909}.
CC   -!- DISEASE: Corneal dystrophy, posterior polymorphous, 3 (PPCD3)
CC       [MIM:609141]: A subtype of posterior corneal dystrophy, a disease
CC       characterized by alterations of Descemet membrane presenting as
CC       vesicles, opacities or band-like lesions on slit-lamp examination
CC       and specular microscopy. Affected patient typically are
CC       asymptomatic. {ECO:0000269|PubMed:16252232,
CC       ECO:0000269|PubMed:23599324}. Note=The disease is caused by
CC       mutations affecting the gene represented in this entry.
CC   -!- DISEASE: Corneal dystrophy, Fuchs endothelial, 6 (FECD6)
CC       [MIM:613270]: A corneal disease caused by loss of endothelium of
CC       the central cornea. It is characterized by focal wart-like guttata
CC       that arise from Descemet membrane and develop in the central
CC       cornea, epithelial blisters, reduced vision and pain. Descemet
CC       membrane is thickened by abnormal collagenous deposition.
CC       {ECO:0000269|PubMed:20036349, ECO:0000269|PubMed:23599324}.
CC       Note=The disease is caused by mutations affecting the gene
CC       represented in this entry.
CC   -!- SIMILARITY: Belongs to the delta-EF1/ZFH-1 C2H2-type zinc-finger
CC       family. {ECO:0000305}.
CC   -!- SIMILARITY: Contains 7 C2H2-type zinc fingers.
CC       {ECO:0000255|PROSITE-ProRule:PRU00042}.
CC   -!- SIMILARITY: Contains 1 homeobox DNA-binding domain. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAG62481.1; Type=Frameshift; Positions=177; Evidence={ECO:0000305};
CC   -----------------------------------------------------------------------
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CC   -----------------------------------------------------------------------
DR   EMBL; D15050; BAA03646.1; -; mRNA.
DR   EMBL; U12170; AAA20602.1; -; mRNA.
DR   EMBL; AK091478; BAC03673.1; -; mRNA.
DR   EMBL; AK296244; BAG58962.1; -; mRNA.
DR   EMBL; AK300830; BAG62481.1; ALT_FRAME; mRNA.
DR   EMBL; AL158080; CAI17320.1; -; Genomic_DNA.
DR   EMBL; AL117340; CAI17320.1; JOINED; Genomic_DNA.
DR   EMBL; AL161935; CAI17320.1; JOINED; Genomic_DNA.
DR   EMBL; AL355148; CAI17320.1; JOINED; Genomic_DNA.
DR   EMBL; AL161935; CAH74132.1; -; Genomic_DNA.
DR   EMBL; AL117340; CAH74132.1; JOINED; Genomic_DNA.
DR   EMBL; AL158080; CAH74132.1; JOINED; Genomic_DNA.
DR   EMBL; AL355148; CAH74132.1; JOINED; Genomic_DNA.
DR   EMBL; AL117340; CAI12550.1; -; Genomic_DNA.
DR   EMBL; AL158080; CAI12550.1; JOINED; Genomic_DNA.
DR   EMBL; AL161935; CAI12550.1; JOINED; Genomic_DNA.
DR   EMBL; AL355148; CAI12550.1; JOINED; Genomic_DNA.
DR   EMBL; AL355148; CAI15108.1; -; Genomic_DNA.
DR   EMBL; AL117340; CAI15108.1; JOINED; Genomic_DNA.
DR   EMBL; AL158080; CAI15108.1; JOINED; Genomic_DNA.
DR   EMBL; AL161935; CAI15108.1; JOINED; Genomic_DNA.
DR   EMBL; CH471072; EAW85989.1; -; Genomic_DNA.
DR   EMBL; BC112392; AAI12393.1; -; mRNA.
DR   EMBL; M81699; -; NOT_ANNOTATED_CDS; mRNA.
DR   CCDS; CCDS44370.1; -. [P37275-5]
DR   CCDS; CCDS53505.1; -. [P37275-2]
DR   CCDS; CCDS53506.1; -. [P37275-4]
DR   CCDS; CCDS53507.1; -. [P37275-3]
DR   CCDS; CCDS7169.1; -. [P37275-1]
DR   PIR; JX0293; JX0293.
DR   RefSeq; NP_001121600.1; NM_001128128.2. [P37275-5]
DR   RefSeq; NP_001167564.1; NM_001174093.1. [P37275-4]
DR   RefSeq; NP_001167565.1; NM_001174094.1.
DR   RefSeq; NP_001167566.1; NM_001174095.1. [P37275-3]
DR   RefSeq; NP_001167567.1; NM_001174096.1. [P37275-2]
DR   RefSeq; NP_110378.3; NM_030751.5. [P37275-1]
DR   UniGene; Hs.124503; -.
DR   PDB; 2E19; NMR; -; A=586-642.
DR   PDBsum; 2E19; -.
DR   ProteinModelPortal; P37275; -.
DR   SMR; P37275; 583-642.
DR   BioGrid; 112796; 22.
DR   IntAct; P37275; 2.
DR   MINT; MINT-94525; -.
DR   STRING; 9606.ENSP00000354487; -.
DR   PhosphoSite; P37275; -.
DR   BioMuta; ZEB1; -.
DR   DMDM; 6166575; -.
DR   MaxQB; P37275; -.
DR   PaxDb; P37275; -.
DR   PRIDE; P37275; -.
DR   Ensembl; ENST00000320985; ENSP00000319248; ENSG00000148516. [P37275-1]
DR   Ensembl; ENST00000361642; ENSP00000354487; ENSG00000148516. [P37275-2]
DR   Ensembl; ENST00000446923; ENSP00000391612; ENSG00000148516. [P37275-5]
DR   Ensembl; ENST00000542815; ENSP00000444891; ENSG00000148516. [P37275-3]
DR   Ensembl; ENST00000560721; ENSP00000452787; ENSG00000148516. [P37275-4]
DR   GeneID; 6935; -.
DR   KEGG; hsa:6935; -.
DR   UCSC; uc001ivr.4; human. [P37275-1]
DR   UCSC; uc001ivu.4; human.
DR   CTD; 6935; -.
DR   GeneCards; ZEB1; -.
DR   HGNC; HGNC:11642; ZEB1.
DR   HPA; CAB058686; -.
DR   HPA; HPA027524; -.
DR   MIM; 189909; gene.
DR   MIM; 609141; phenotype.
DR   MIM; 613270; phenotype.
DR   neXtProt; NX_P37275; -.
DR   Orphanet; 98974; Fuchs endothelial corneal dystrophy.
DR   Orphanet; 98973; Posterior polymorphous corneal dystrophy.
DR   PharmGKB; PA162409589; -.
DR   eggNOG; KOG3623; Eukaryota.
DR   eggNOG; ENOG410ZFMZ; LUCA.
DR   GeneTree; ENSGT00630000089829; -.
DR   HOGENOM; HOG000264256; -.
DR   HOVERGEN; HBG004697; -.
DR   InParanoid; P37275; -.
DR   KO; K09299; -.
DR   OMA; ECEKPQG; -.
DR   OrthoDB; EOG790G0D; -.
DR   PhylomeDB; P37275; -.
DR   TreeFam; TF331759; -.
DR   SignaLink; P37275; -.
DR   ChiTaRS; ZEB1; human.
DR   EvolutionaryTrace; P37275; -.
DR   GeneWiki; ZEB1; -.
DR   GenomeRNAi; 6935; -.
DR   NextBio; 27137; -.
DR   PRO; PR:P37275; -.
DR   Proteomes; UP000005640; Chromosome 10.
DR   Bgee; P37275; -.
DR   CleanEx; HS_ZEB1; -.
DR   ExpressionAtlas; P37275; baseline and differential.
DR   Genevisible; P37275; HS.
DR   GO; GO:0005737; C:cytoplasm; IDA:HPA.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0005667; C:transcription factor complex; IEA:Ensembl.
DR   GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
DR   GO; GO:0070888; F:E-box binding; ISS:UniProtKB.
DR   GO; GO:0003713; F:transcription coactivator activity; TAS:ProtInc.
DR   GO; GO:0003714; F:transcription corepressor activity; TAS:ProtInc.
DR   GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; TAS:ProtInc.
DR   GO; GO:0001227; F:transcriptional repressor activity, RNA polymerase II transcription regulatory region sequence-specific binding; IDA:HGNC.
DR   GO; GO:0008270; F:zinc ion binding; TAS:ProtInc.
DR   GO; GO:0051216; P:cartilage development; IEA:Ensembl.
DR   GO; GO:0008283; P:cell proliferation; TAS:ProtInc.
DR   GO; GO:0071230; P:cellular response to amino acid stimulus; IEA:Ensembl.
DR   GO; GO:0007417; P:central nervous system development; IEA:Ensembl.
DR   GO; GO:0090103; P:cochlea morphogenesis; IEA:Ensembl.
DR   GO; GO:0048596; P:embryonic camera-type eye morphogenesis; IEA:Ensembl.
DR   GO; GO:0048704; P:embryonic skeletal system morphogenesis; IEA:Ensembl.
DR   GO; GO:0006955; P:immune response; TAS:ProtInc.
DR   GO; GO:0008285; P:negative regulation of cell proliferation; IEA:Ensembl.
DR   GO; GO:0030857; P:negative regulation of epithelial cell differentiation; IEA:Ensembl.
DR   GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:HGNC.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR   GO; GO:0007389; P:pattern specification process; IEA:Ensembl.
DR   GO; GO:0045666; P:positive regulation of neuron differentiation; ISS:UniProtKB.
DR   GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IEA:Ensembl.
DR   GO; GO:0010464; P:regulation of mesenchymal cell proliferation; IEA:Ensembl.
DR   GO; GO:0051150; P:regulation of smooth muscle cell differentiation; IEA:Ensembl.
DR   GO; GO:0033081; P:regulation of T cell differentiation in thymus; IEA:Ensembl.
DR   GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; TAS:ProtInc.
DR   GO; GO:0017015; P:regulation of transforming growth factor beta receptor signaling pathway; IEA:Ensembl.
DR   GO; GO:0048752; P:semicircular canal morphogenesis; IEA:Ensembl.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.10.60; -; 1.
DR   Gene3D; 3.30.160.60; -; 5.
DR   InterPro; IPR008598; Di19_Zn_binding_dom.
DR   InterPro; IPR001356; Homeobox_dom.
DR   InterPro; IPR009057; Homeodomain-like.
DR   InterPro; IPR007087; Znf_C2H2.
DR   InterPro; IPR015880; Znf_C2H2-like.
DR   InterPro; IPR013087; Znf_C2H2/integrase_DNA-bd.
DR   Pfam; PF00046; Homeobox; 1.
DR   Pfam; PF05605; zf-Di19; 1.
DR   SMART; SM00389; HOX; 1.
DR   SMART; SM00355; ZnF_C2H2; 7.
DR   SUPFAM; SSF46689; SSF46689; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 5.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 6.
PE   1: Evidence at protein level;
KW   3D-structure; Activator; Alternative splicing; Complete proteome;
KW   Corneal dystrophy; Differentiation; Disease mutation; DNA-binding;
KW   Homeobox; Isopeptide bond; Metal-binding; Neurogenesis; Nucleus;
KW   Phosphoprotein; Polymorphism; Reference proteome; Repeat; Repressor;
KW   Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW   Zinc-finger.
FT   CHAIN         1   1124       Zinc finger E-box-binding homeobox 1.
FT                                /FTId=PRO_0000047231.
FT   ZN_FING     170    193       C2H2-type 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     200    222       C2H2-type 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     240    262       C2H2-type 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     268    292       C2H2-type 4; atypical.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00042}.
FT   DNA_BIND    581    640       Homeobox; atypical.
FT   ZN_FING     904    926       C2H2-type 5. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     932    954       C2H2-type 6. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     960    981       C2H2-type 7; atypical.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00042}.
FT   COMPBIAS    989   1124       Glu-rich (acidic).
FT   MOD_RES      31     31       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q62947}.
FT   MOD_RES      33     33       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q62947}.
FT   MOD_RES     313    313       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q64318}.
FT   MOD_RES     322    322       Phosphoserine.
FT                                {ECO:0000244|PubMed:18669648}.
FT   MOD_RES     642    642       Phosphoserine.
FT                                {ECO:0000244|PubMed:19690332}.
FT   MOD_RES     679    679       Phosphoserine.
FT                                {ECO:0000244|PubMed:19690332,
FT                                ECO:0000244|PubMed:20068231}.
FT   MOD_RES     686    686       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q64318}.
FT   MOD_RES     693    693       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q64318}.
FT   MOD_RES     700    700       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q64318}.
FT   MOD_RES     702    702       Phosphothreonine.
FT                                {ECO:0000244|PubMed:19690332}.
FT   MOD_RES     704    704       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q64318}.
FT   CROSSLNK    347    347       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO).
FT   CROSSLNK    493    493       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:25218447}.
FT   CROSSLNK    504    504       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:25218447}.
FT   CROSSLNK    515    515       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:25218447}.
FT   CROSSLNK    774    774       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO).
FT   VAR_SEQ       1     19       MADGPRCKRRKQANPRRNN -> MK (in isoform 5).
FT                                {ECO:0000303|PubMed:14702039}.
FT                                /FTId=VSP_047279.
FT   VAR_SEQ      20     87       VTNYNTVVETNSDSDDEDKLHIVEEESVTDAADCEGVPEDD
FT                                LPTDQTVLPGRSSEREGNAKNCWEDDR -> G (in
FT                                isoform 3).
FT                                {ECO:0000303|PubMed:14702039}.
FT                                /FTId=VSP_047280.
FT   VAR_SEQ      87    107       RKEGQEILGPEAQADEAGCTV -> I (in isoform
FT                                4). {ECO:0000303|PubMed:14702039}.
FT                                /FTId=VSP_047281.
FT   VAR_SEQ      87     87       R -> TG (in isoform 2 and isoform 5).
FT                                {ECO:0000303|PubMed:14702039,
FT                                ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_045184.
FT   VARIANT      78     78       N -> T (in FECD6; no effect on protein
FT                                expression; no effect on nuclear
FT                                localization; dbSNP:rs80194531).
FT                                {ECO:0000269|PubMed:20036349,
FT                                ECO:0000269|PubMed:23599324,
FT                                ECO:0000269|PubMed:25190660}.
FT                                /FTId=VAR_063759.
FT   VARIANT      90     90       G -> R (in dbSNP:rs12217419).
FT                                /FTId=VAR_052731.
FT   VARIANT     525    525       G -> E (found in a patient with FECD6).
FT                                {ECO:0000269|PubMed:23599324}.
FT                                /FTId=VAR_072897.
FT   VARIANT     553    553       K -> R (in dbSNP:rs35753967).
FT                                /FTId=VAR_031824.
FT   VARIANT     640    640       Q -> H (in FECD6; down-regulation of
FT                                several collagen genes expression).
FT                                {ECO:0000269|PubMed:23599324}.
FT                                /FTId=VAR_072898.
FT   VARIANT     649    649       P -> A (in FECD6; no effect on protein
FT                                expression; no effect on nuclear
FT                                localization).
FT                                {ECO:0000269|PubMed:20036349,
FT                                ECO:0000269|PubMed:25190660}.
FT                                /FTId=VAR_063760.
FT   VARIANT     696    696       N -> S (in FECD6; no effect on protein
FT                                expression; no effect on nuclear
FT                                localization).
FT                                {ECO:0000269|PubMed:25190660}.
FT                                /FTId=VAR_072899.
FT   VARIANT     810    810       Q -> P (in FECD6; no effect on protein
FT                                expression; no effect on nuclear
FT                                localization).
FT                                {ECO:0000269|PubMed:20036349,
FT                                ECO:0000269|PubMed:25190660}.
FT                                /FTId=VAR_063761.
FT   VARIANT     840    840       Q -> P (in FECD6; no effect on protein
FT                                expression; no effect on nuclear
FT                                localization; dbSNP:rs118020901).
FT                                {ECO:0000269|PubMed:20036349,
FT                                ECO:0000269|PubMed:25190660}.
FT                                /FTId=VAR_063762.
FT   VARIANT     905    905       A -> G (in FECD6; no effect on protein
FT                                expression; no effect on nuclear
FT                                localization).
FT                                {ECO:0000269|PubMed:25190660}.
FT                                /FTId=VAR_072900.
FT   VARIANT     905    905       A -> T (in FECD6).
FT                                {ECO:0000269|PubMed:20036349}.
FT                                /FTId=VAR_063763.
FT   CONFLICT     12     12       Q -> R (in Ref. 3; BAC03673).
FT                                {ECO:0000305}.
FT   CONFLICT     81     81       N -> S (in Ref. 3; BAC03673).
FT                                {ECO:0000305}.
FT   CONFLICT     84     84       E -> K (in Ref. 3; BAC03673).
FT                                {ECO:0000305}.
FT   CONFLICT    220    220       T -> A (in Ref. 3; BAG62481).
FT                                {ECO:0000305}.
FT   CONFLICT    390    390       M -> T (in Ref. 3; BAG62481).
FT                                {ECO:0000305}.
FT   CONFLICT    420    420       V -> I (in Ref. 2; AAA20602).
FT                                {ECO:0000305}.
FT   CONFLICT    472    472       K -> R (in Ref. 3; BAG58962).
FT                                {ECO:0000305}.
FT   CONFLICT    609    609       E -> Q (in Ref. 7; M81699).
FT                                {ECO:0000305}.
FT   CONFLICT    654    654       I -> T (in Ref. 2; AAA20602).
FT                                {ECO:0000305}.
FT   CONFLICT    672    672       D -> H (in Ref. 7; M81699).
FT                                {ECO:0000305}.
FT   CONFLICT    681    681       L -> S (in Ref. 7; M81699).
FT                                {ECO:0000305}.
FT   CONFLICT    775    775       K -> T (in Ref. 3; BAG62481).
FT                                {ECO:0000305}.
FT   CONFLICT    793    794       IP -> KY (in Ref. 3; BAG58962).
FT                                {ECO:0000305}.
FT   CONFLICT    797    797       A -> N (in Ref. 3; BAG58962).
FT                                {ECO:0000305}.
FT   CONFLICT    818    818       A -> V (in Ref. 3; BAG62481).
FT                                {ECO:0000305}.
FT   CONFLICT    838    838       I -> T (in Ref. 3; BAC03673).
FT                                {ECO:0000305}.
FT   CONFLICT   1066   1066       E -> G (in Ref. 3; BAC03673).
FT                                {ECO:0000305}.
FT   HELIX       590    600       {ECO:0000244|PDB:2E19}.
FT   HELIX       608    618       {ECO:0000244|PDB:2E19}.
FT   HELIX       622    634       {ECO:0000244|PDB:2E19}.
SQ   SEQUENCE   1124 AA;  124074 MW;  0A2714CC37C848D1 CRC64;
     MADGPRCKRR KQANPRRNNV TNYNTVVETN SDSDDEDKLH IVEEESVTDA ADCEGVPEDD
     LPTDQTVLPG RSSEREGNAK NCWEDDRKEG QEILGPEAQA DEAGCTVKDD ECESDAENEQ
     NHDPNVEEFL QQQDTAVIFP EAPEEDQRQG TPEASGHDEN GTPDAFSQLL TCPYCDRGYK
     RFTSLKEHIK YRHEKNEDNF SCSLCSYTFA YRTQLERHMT SHKSGRDQRH VTQSGCNRKF
     KCTECGKAFK YKHHLKEHLR IHSGEKPYEC PNCKKRFSHS GSYSSHISSK KCISLIPVNG
     RPRTGLKTSQ CSSPSLSASP GSPTRPQIRQ KIENKPLQEQ LSVNQIKTEP VDYEFKPIVV
     ASGINCSTPL QNGVFTGGGP LQATSSPQGM VQAVVLPTVG LVSPISINLS DIQNVLKVAV
     DGNVIRQVLE NNQANLASKE QETINASPIQ QGGHSVISAI SLPLVDQDGT TKIIINYSLE
     QPSQLQVVPQ NLKKENPVAT NSCKSEKLPE DLTVKSEKDK SFEGGVNDST CLLCDDCPGD
     INALPELKHY DLKQPTQPPP LPAAEAEKPE SSVSSATGDG NLSPSQPPLK NLLSLLKAYY
     ALNAQPSAEE LSKIADSVNL PLDVVKKWFE KMQAGQISVQ SSEPSSPEPG KVNIPAKNND
     QPQSANANEP QDSTVNLQSP LKMTNSPVLP VGSTTNGSRS STPSPSPLNL SSSRNTQGYL
     YTAEGAQEEP QVEPLDLSLP KQQGELLERS TITSVYQNSV YSVQEEPLNL SCAKKEPQKD
     SCVTDSEPVV NVIPPSANPI NIAIPTVTAQ LPTIVAIADQ NSVPCLRALA ANKQTILIPQ
     VAYTYSTTVS PAVQEPPLKV IQPNGNQDER QDTSSEGVSN VEDQNDSDST PPKKKMRKTE
     NGMYACDLCD KIFQKSSSLL RHKYEHTGKR PHECGICKKA FKHKHHLIEH MRLHSGEKPY
     QCDKCGKRFS HSGSYSQHMN HRYSYCKREA EERDSTEQEE AGPEILSNEH VGARASPSQG
     DSDERESLTR EEDEDSEKEE EEEDKEMEEL QEEKECEKPQ GDEEEEEEEE EVEEEEVEEA
     ENEGEEAKTE GLMKDDRAES QASSLGQKVG ESSEQVSEEK TNEA
//
ID   ZEB2_HUMAN              Reviewed;        1214 AA.
AC   O60315; A0JP09; B7Z2P2; F5H814; Q9UED1;
DT   21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   11-NOV-2015, entry version 167.
DE   RecName: Full=Zinc finger E-box-binding homeobox 2;
DE   AltName: Full=Smad-interacting protein 1;
DE            Short=SMADIP1;
DE   AltName: Full=Zinc finger homeobox protein 1b;
GN   Name=ZEB2; Synonyms=KIAA0569, SIP1, ZFHX1B, ZFX1B;
GN   ORFNames=HRIHFB2411;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INVOLVEMENT IN MOWS.
RX   PubMed=11448942; DOI=10.1093/hmg/10.14.1503;
RA   Cacheux V., Dastot-Le Moal F., Kaeaeriaeinen H., Bondurand N.,
RA   Rintala R., Boissier B., Wilson M., Mowat D., Goossens M.;
RT   "Loss-of-function mutations in SIP1 Smad interacting protein 1 result
RT   in a syndromic Hirschsprung disease.";
RL   Hum. Mol. Genet. 10:1503-1510(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   PubMed=11279515; DOI=10.1038/86860;
RA   Wakamatsu N., Yamada Y., Yamada K., Ono T., Nomura N., Taniguchi H.,
RA   Kitoh H., Mutoh N., Yamanaka T., Mushiake K., Kato K., Sonta S.,
RA   Nagaya M.;
RT   "Mutations in SIP1, encoding Smad interacting protein 1, cause a form
RT   of Hirschsprung disease.";
RL   Nat. Genet. 27:369-370(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
RX   PubMed=9628581; DOI=10.1093/dnares/5.1.31;
RA   Nagase T., Ishikawa K., Miyajima N., Tanaka A., Kotani H., Nomura N.,
RA   Ohara O.;
RT   "Prediction of the coding sequences of unidentified human genes. IX.
RT   The complete sequences of 100 new cDNA clones from brain which can
RT   code for large proteins in vitro.";
RL   DNA Res. 5:31-39(1998).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Brain;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15815621; DOI=10.1038/nature03466;
RA   Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
RA   Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA   Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA   Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA   Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA   Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA   Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA   Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA   Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA   Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA   McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA   Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
RA   Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA   Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA   Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA   Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA   Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA   Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA   Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA   Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA   McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA   Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA   Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
RA   Waterston R.H., Wilson R.K.;
RT   "Generation and annotation of the DNA sequences of human chromosomes 2
RT   and 4.";
RL   Nature 434:724-731(2005).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1161-1214 (ISOFORM 1), AND
RP   SUBCELLULAR LOCATION.
RC   TISSUE=Fetal brain;
RX   PubMed=9853615; DOI=10.1038/4315;
RA   Ueki N., Oda T., Kondo M., Yano K., Noguchi T., Muramatsu M.-A.;
RT   "Selection system for genes encoding nuclear-targeted proteins.";
RL   Nat. Biotechnol. 16:1338-1342(1998).
RN   [8]
RP   FUNCTION, SUMOYLATION AT LYS-391 AND LYS-866, INTERACTION WITH CBX4
RP   AND CTBP1, AND SUBCELLULAR LOCATION.
RX   PubMed=16061479; DOI=10.1074/jbc.M504477200;
RA   Long J., Zuo D., Park M.;
RT   "Pc2-mediated sumoylation of Smad-interacting protein 1 attenuates
RT   transcriptional repression of E-cadherin.";
RL   J. Biol. Chem. 280:35477-35489(2005).
RN   [9]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-377, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19608861; DOI=10.1126/science.1175371;
RA   Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA   Walther T.C., Olsen J.V., Mann M.;
RT   "Lysine acetylation targets protein complexes and co-regulates major
RT   cellular functions.";
RL   Science 325:834-840(2009).
RN   [10]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
RA   Wang L., Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human
RT   liver phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [11]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-391 AND LYS-866, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25218447; DOI=10.1038/nsmb.2890;
RA   Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA   Vertegaal A.C.;
RT   "Uncovering global SUMOylation signaling networks in a site-specific
RT   manner.";
RL   Nat. Struct. Mol. Biol. 21:927-936(2014).
RN   [12]
RP   STRUCTURE BY NMR OF 647-705.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of the homeobox domain of zinc finger homeobox
RT   protein 1B (SMAD interacting protein 1).";
RL   Submitted (DEC-2006) to the PDB data bank.
RN   [13]
RP   VARIANT MOWS ASN-99 DEL.
RX   PubMed=12451214; DOI=10.1212/01.WNL.0000034842.78350.4E;
RA   Yoneda M., Fujita T., Yamada Y., Yamada K., Fujii A., Inagaki T.,
RA   Nakagawa H., Shimada A., Kishikawa M., Nagaya M., Azuma T.,
RA   Kuriyama M., Wakamatsu N.;
RT   "Late infantile Hirschsprung disease-mental retardation syndrome with
RT   a 3-bp deletion in ZFHX1B.";
RL   Neurology 59:1637-1640(2002).
RN   [14]
RP   VARIANT MOWS GLY-953.
RX   PubMed=15384097; DOI=10.1002/ajmg.a.30312;
RA   Gregory-Evans C.Y., Vieira H., Dalton R., Adams G.G.W., Salt A.,
RA   Gregory-Evans K.;
RT   "Ocular coloboma and high myopia with Hirschsprung disease associated
RT   with a novel ZFHX1B missense mutation and trisomy 21.";
RL   Am. J. Med. Genet. A 131:86-90(2004).
RN   [15]
RP   VARIANT MOWS ARG-1119.
RX   PubMed=16688751; DOI=10.1002/ajmg.a.31267;
RA   Heinritz W., Zweier C., Froster U.G., Strenge S., Kujat A., Syrbe S.,
RA   Rauch A., Schuster V.;
RT   "A missense mutation in the ZFHX1B gene associated with an atypical
RT   Mowat-Wilson syndrome phenotype.";
RL   Am. J. Med. Genet. A 140:1223-1227(2006).
RN   [16]
RP   VARIANT [LARGE SCALE ANALYSIS] ASN-983.
RX   PubMed=16959974; DOI=10.1126/science.1133427;
RA   Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA   Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
RA   Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
RA   Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
RA   Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
RA   Vogelstein B., Kinzler K.W., Velculescu V.E.;
RT   "The consensus coding sequences of human breast and colorectal
RT   cancers.";
RL   Science 314:268-274(2006).
CC   -!- FUNCTION: Transcriptional inhibitor that binds to DNA sequence 5'-
CC       CACCT-3' in different promoters. Represses transcription of E-
CC       cadherin. {ECO:0000269|PubMed:16061479}.
CC   -!- SUBUNIT: Binds activated SMAD1, activated SMAD2 and activated
CC       SMAD3; binding with SMAD4 is not detected (By similarity).
CC       Interacts with CBX4 and CTBP1. {ECO:0000250,
CC       ECO:0000269|PubMed:16061479}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16061479,
CC       ECO:0000269|PubMed:9853615}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=O60315-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=O60315-2; Sequence=VSP_044797;
CC         Note=No experimental confirmation available.;
CC   -!- PTM: Sumoylation on Lys-391 and Lys-866 is promoted by the E3
CC       SUMO-protein ligase CBX4, and impairs interaction with CTBP1 and
CC       transcription repression activity. {ECO:0000269|PubMed:16061479}.
CC   -!- DISEASE: Mowat-Wilson syndrome (MOWS) [MIM:235730]: A complex
CC       developmental disorder characterized by mental retardation,
CC       delayed motor development, epilepsy, microcephaly and a wide
CC       spectrum of clinically heterogeneous features suggestive of
CC       neurocristopathies at the cephalic, cardiac, and vagal levels.
CC       Affected patients show an easily recognizable facial appearance
CC       with deep set eyes and hypertelorism, medially divergent, broad
CC       eyebrows, prominent columella, pointed chin and uplifted, notched
CC       ear lobes. Some patients manifest Hirschsprung disease.
CC       {ECO:0000269|PubMed:11448942, ECO:0000269|PubMed:12451214,
CC       ECO:0000269|PubMed:15384097, ECO:0000269|PubMed:16688751}.
CC       Note=The disease is caused by mutations affecting the gene
CC       represented in this entry.
CC   -!- SIMILARITY: Belongs to the delta-EF1/ZFH-1 C2H2-type zinc-finger
CC       family. {ECO:0000305}.
CC   -!- SIMILARITY: Contains 8 C2H2-type zinc fingers.
CC       {ECO:0000255|PROSITE-ProRule:PRU00042}.
CC   -!- SIMILARITY: Contains 1 homeobox DNA-binding domain. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA25495.2; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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DR   EMBL; AY029472; AAK52081.1; -; Genomic_DNA.
DR   EMBL; AB056507; BAB40819.1; -; mRNA.
DR   EMBL; AB011141; BAA25495.2; ALT_INIT; mRNA.
DR   EMBL; AK294928; BAH11928.1; -; mRNA.
DR   EMBL; AC009951; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC010130; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC127102; AAI27103.1; -; mRNA.
DR   EMBL; AB015341; BAA34798.1; -; mRNA.
DR   CCDS; CCDS2186.1; -. [O60315-1]
DR   CCDS; CCDS54403.1; -. [O60315-2]
DR   RefSeq; NP_001165124.1; NM_001171653.1. [O60315-2]
DR   RefSeq; NP_055610.1; NM_014795.3. [O60315-1]
DR   RefSeq; XP_006712944.1; XM_006712881.2. [O60315-1]
DR   RefSeq; XP_006712945.1; XM_006712882.2. [O60315-1]
DR   UniGene; Hs.34871; -.
DR   PDB; 2DA7; NMR; -; A=647-704.
DR   PDBsum; 2DA7; -.
DR   ProteinModelPortal; O60315; -.
DR   SMR; O60315; 648-705.
DR   BioGrid; 115175; 20.
DR   IntAct; O60315; 11.
DR   MINT; MINT-1181379; -.
DR   STRING; 9606.ENSP00000302501; -.
DR   PhosphoSite; O60315; -.
DR   BioMuta; ZEB2; -.
DR   MaxQB; O60315; -.
DR   PaxDb; O60315; -.
DR   PRIDE; O60315; -.
DR   Ensembl; ENST00000409487; ENSP00000386854; ENSG00000169554. [O60315-1]
DR   Ensembl; ENST00000539609; ENSP00000443792; ENSG00000169554. [O60315-2]
DR   Ensembl; ENST00000558170; ENSP00000454157; ENSG00000169554. [O60315-1]
DR   Ensembl; ENST00000627532; ENSP00000487174; ENSG00000169554. [O60315-1]
DR   GeneID; 9839; -.
DR   KEGG; hsa:9839; -.
DR   UCSC; uc002tvu.3; human. [O60315-1]
DR   CTD; 9839; -.
DR   GeneCards; ZEB2; -.
DR   GeneReviews; ZEB2; -.
DR   HGNC; HGNC:14881; ZEB2.
DR   HPA; HPA003456; -.
DR   MIM; 235730; phenotype.
DR   MIM; 605802; gene.
DR   neXtProt; NX_O60315; -.
DR   Orphanet; 261552; Mowat-Wilson syndrome due to a ZEB2 point mutation.
DR   Orphanet; 261537; Mowat-Wilson syndrome due to monosomy 2q22.
DR   PharmGKB; PA162409612; -.
DR   eggNOG; ENOG410IMF7; Eukaryota.
DR   eggNOG; ENOG410ZQ40; LUCA.
DR   GeneTree; ENSGT00630000089829; -.
DR   HOGENOM; HOG000264256; -.
DR   HOVERGEN; HBG004697; -.
DR   InParanoid; O60315; -.
DR   KO; K09299; -.
DR   OMA; LDHSRSN; -.
DR   OrthoDB; EOG790G0D; -.
DR   PhylomeDB; O60315; -.
DR   TreeFam; TF331759; -.
DR   SignaLink; O60315; -.
DR   ChiTaRS; ZEB2; human.
DR   EvolutionaryTrace; O60315; -.
DR   GeneWiki; ZEB2; -.
DR   GenomeRNAi; 9839; -.
DR   NextBio; 37070; -.
DR   PRO; PR:O60315; -.
DR   Proteomes; UP000005640; Chromosome 2.
DR   Bgee; O60315; -.
DR   CleanEx; HS_SIP1; -.
DR   CleanEx; HS_ZEB2; -.
DR   ExpressionAtlas; O60315; baseline and differential.
DR   Genevisible; O60315; HS.
DR   GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0019208; F:phosphatase regulator activity; NAS:UniProtKB.
DR   GO; GO:0048066; P:developmental pigmentation; ISS:BHF-UCL.
DR   GO; GO:0097324; P:melanocyte migration; ISS:BHF-UCL.
DR   GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IMP:BHF-UCL.
DR   GO; GO:0007399; P:nervous system development; NAS:UniProtKB.
DR   GO; GO:0048023; P:positive regulation of melanin biosynthetic process; IC:BHF-UCL.
DR   GO; GO:0045636; P:positive regulation of melanocyte differentiation; ISS:BHF-UCL.
DR   GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IMP:BHF-UCL.
DR   GO; GO:0050790; P:regulation of catalytic activity; NAS:GOC.
DR   GO; GO:1903056; P:regulation of melanosome organization; ISS:BHF-UCL.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.160.60; -; 5.
DR   InterPro; IPR008598; Di19_Zn_binding_dom.
DR   InterPro; IPR001356; Homeobox_dom.
DR   InterPro; IPR009057; Homeodomain-like.
DR   InterPro; IPR007087; Znf_C2H2.
DR   InterPro; IPR015880; Znf_C2H2-like.
DR   InterPro; IPR013087; Znf_C2H2/integrase_DNA-bd.
DR   Pfam; PF05605; zf-Di19; 1.
DR   SMART; SM00389; HOX; 1.
DR   SMART; SM00355; ZnF_C2H2; 8.
DR   SUPFAM; SSF46689; SSF46689; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 5.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 6.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative splicing; Complete proteome;
KW   Disease mutation; DNA-binding; Epilepsy; Hirschsprung disease;
KW   Homeobox; Isopeptide bond; Mental retardation; Metal-binding; Nucleus;
KW   Phosphoprotein; Polymorphism; Reference proteome; Repeat; Repressor;
KW   Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW   Zinc-finger.
FT   CHAIN         1   1214       Zinc finger E-box-binding homeobox 2.
FT                                /FTId=PRO_0000047236.
FT   ZN_FING     211    234       C2H2-type 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     241    263       C2H2-type 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     282    304       C2H2-type 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     310    334       C2H2-type 4; atypical.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00042}.
FT   ZN_FING     581    605       C2H2-type 5; atypical.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00042}.
FT   DNA_BIND    644    703       Homeobox; atypical.
FT   ZN_FING     999   1021       C2H2-type 6. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING    1027   1049       C2H2-type 7. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING    1055   1076       C2H2-type 8; atypical.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00042}.
FT   REGION      437    487       SMAD-MH2 binding domain. {ECO:0000250}.
FT   COMPBIAS   1084   1214       Glu-rich (acidic).
FT   MOD_RES     356    356       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9R0G7}.
FT   MOD_RES     360    360       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9R0G7}.
FT   MOD_RES     364    364       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9R0G7}.
FT   MOD_RES     377    377       N6-acetyllysine.
FT                                {ECO:0000244|PubMed:19608861}.
FT   MOD_RES     731    731       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9R0G7}.
FT   MOD_RES     780    780       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9R0G7}.
FT   MOD_RES     784    784       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9R0G7}.
FT   MOD_RES    1124   1124       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9R0G7}.
FT   MOD_RES    1203   1203       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9R0G7}.
FT   CROSSLNK    391    391       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO);
FT                                alternate.
FT   CROSSLNK    391    391       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2);
FT                                alternate. {ECO:0000244|PubMed:25218447}.
FT   CROSSLNK    866    866       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO);
FT                                alternate.
FT   CROSSLNK    866    866       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2);
FT                                alternate. {ECO:0000244|PubMed:25218447}.
FT   VAR_SEQ     111    134       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:14702039}.
FT                                /FTId=VSP_044797.
FT   VARIANT      99     99       Missing (in MOWS).
FT                                {ECO:0000269|PubMed:12451214}.
FT                                /FTId=VAR_027016.
FT   VARIANT     953    953       R -> G (in MOWS).
FT                                {ECO:0000269|PubMed:15384097}.
FT                                /FTId=VAR_027017.
FT   VARIANT     983    983       D -> N (in a colorectal cancer sample;
FT                                somatic mutation).
FT                                {ECO:0000269|PubMed:16959974}.
FT                                /FTId=VAR_035563.
FT   VARIANT    1119   1119       Q -> R (in MOWS).
FT                                {ECO:0000269|PubMed:16688751}.
FT                                /FTId=VAR_027018.
FT   CONFLICT   1155   1155       D -> G (in Ref. 4; BAH11928).
FT                                {ECO:0000305}.
FT   HELIX       654    665
FT   HELIX       671    681
FT   HELIX       685    700
SQ   SEQUENCE   1214 AA;  136447 MW;  B578FD91339C3FDD CRC64;
     MKQPIMADGP RCKRRKQANP RRKNVVNYDN VVDTGSETDE EDKLHIAEDD GIANPLDQET
     SPASVPNHES SPHVSQALLP REEEEDEIRE GGVEHPWHNN EILQASVDGP EEMKEDYDTM
     GPEATIQTAI NNGTVKNANC TSDFEEYFAK RKLEERDGHA VSIEEYLQRS DTAIIYPEAP
     EELSRLGTPE ANGQEENDLP PGTPDAFAQL LTCPYCDRGY KRLTSLKEHI KYRHEKNEEN
     FSCPLCSYTF AYRTQLERHM VTHKPGTDQH QMLTQGAGNR KFKCTECGKA FKYKHHLKEH
     LRIHSGEKPY ECPNCKKRFS HSGSYSSHIS SKKCIGLISV NGRMRNNIKT GSSPNSVSSS
     PTNSAITQLR NKLENGKPLS MSEQTGLLKI KTEPLDFNDY KVLMATHGFS GTSPFMNGGL
     GATSPLGVHP SAQSPMQHLG VGMEAPLLGF PTMNSNLSEV QKVLQIVDNT VSRQKMDCKA
     EEISKLKGYH MKDPCSQPEE QGVTSPNIPP VGLPVVSHNG ATKSIIDYTL EKVNEAKACL
     QSLTTDSRRQ ISNIKKEKLR TLIDLVTDDK MIENHNISTP FSCQFCKESF PGPIPLHQHE
     RYLCKMNEEI KAVLQPHENI VPNKAGVFVD NKALLLSSVL SEKGMTSPIN PYKDHMSVLK
     AYYAMNMEPN SDELLKISIA VGLPQEFVKE WFEQRKVYQY SNSRSPSLER SSKPLAPNSN
     PPTKDSLLPR SPVKPMDSIT SPSIAELHNS VTNCDPPLRL TKPSHFTNIK PVEKLDHSRS
     NTPSPLNLSS TSSKNSHSSS YTPNSFSSEE LQAEPLDLSL PKQMKEPKSI IATKNKTKAS
     SISLDHNSVS SSSENSDEPL NLTFIKKEFS NSNNLDNKST NPVFSMNPFS AKPLYTALPP
     QSAFPPATFM PPVQTSIPGL RPYPGLDQMS FLPHMAYTYP TGAATFADMQ QRRKYQRKQG
     FQGELLDGAQ DYMSGLDDMT DSDSCLSRKK IKKTESGMYA CDLCDKTFQK SSSLLRHKYE
     HTGKRPHQCQ ICKKAFKHKH HLIEHSRLHS GEKPYQCDKC GKRFSHSGSY SQHMNHRYSY
     CKREAEEREA AEREAREKGH LEPTELLMNR AYLQSITPQG YSDSEERESM PRDGESEKEH
     EKEGEDGYGK LGRQDGDEEF EEEEEESENK SMDTDPETIR DEEETGDHSM DDSSEDGKME
     TKSDHEEDNM EDGM
//
ID   ZFH1_DROME              Reviewed;        1054 AA.
AC   P28166; Q59DT3; Q6NP51; Q8MSQ8; Q9VA39; Q9VA40;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2004, sequence version 2.
DT   11-NOV-2015, entry version 148.
DE   RecName: Full=Zinc finger protein 1;
DE   AltName: Full=Zinc finger homeodomain protein 1;
GN   Name=zfh1; Synonyms=zfh-1; ORFNames=CG1322;
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
OC   Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha;
OC   Ephydroidea; Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=1680376; DOI=10.1016/0925-4773(91)90048-B;
RA   Fortini M.E., Lai Z., Rubin G.M.;
RT   "The Drosophila zfh-1 and zfh-2 genes encode novel proteins containing
RT   both zinc-finger and homeodomain motifs.";
RL   Mech. Dev. 34:113-122(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley;
RX   PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA   Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA   Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA   George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA   Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
RA   Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
RA   Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
RA   Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
RA   Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
RA   Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
RA   Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
RA   Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
RA   Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
RA   de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
RA   Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
RA   Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
RA   Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
RA   Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
RA   Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
RA   Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
RA   Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
RA   Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
RA   Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
RA   Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
RA   Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
RA   Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
RA   Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
RA   Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
RA   Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA   Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
RA   Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
RA   Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
RA   Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
RA   Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
RA   Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
RA   Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [3]
RP   GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
RC   STRAIN=Berkeley;
RX   PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
RA   Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
RA   Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a
RT   systematic review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 30-1054 (ISOFORM B).
RC   STRAIN=Berkeley; TISSUE=Embryo;
RA   Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W.,
RA   Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E.,
RA   George R.A., Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G.,
RA   Miranda A., Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S.,
RA   Patel S., Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M.,
RA   Celniker S.E.;
RL   Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 540-1054.
RC   STRAIN=Berkeley; TISSUE=Embryo;
RX   PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA   Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M.,
RA   George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H.,
RA   Rubin G.M., Celniker S.E.;
RT   "A Drosophila full-length cDNA resource.";
RL   Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-582; SER-586 AND
RP   SER-934, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Embryo;
RX   PubMed=18327897; DOI=10.1021/pr700696a;
RA   Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT   "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL   J. Proteome Res. 7:1675-1682(2008).
CC   -!- FUNCTION: Involved in the development of the embryonic central
CC       nervous system, embryonic mesoderm and adult musculature.
CC       {ECO:0000269|PubMed:1680376}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=B;
CC         IsoId=P28166-1; Sequence=Displayed;
CC       Name=A;
CC         IsoId=P28166-2; Sequence=VSP_009670, VSP_009671;
CC         Note=No experimental confirmation available.;
CC   -!- TISSUE SPECIFICITY: Mesoderm and mesodermally-derived structures
CC       in the embryo including the dorsal vessel, support cells of the
CC       gonads, and segment-specific arrays of adult muscle precursor.
CC       Also identified in motor neurons of developing CNS.
CC       {ECO:0000269|PubMed:1680376}.
CC   -!- SIMILARITY: Belongs to the delta-EF1/ZFH-1 C2H2-type zinc-finger
CC       family. {ECO:0000305}.
CC   -!- SIMILARITY: Contains 9 C2H2-type zinc fingers.
CC       {ECO:0000255|PROSITE-ProRule:PRU00042}.
CC   -!- SIMILARITY: Contains 1 homeobox DNA-binding domain.
CC       {ECO:0000255|PROSITE-ProRule:PRU00108}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAM50023.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence.; Evidence={ECO:0000305};
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; M63449; AAA29050.1; -; Genomic_DNA.
DR   EMBL; AE014297; AAF57083.1; -; Genomic_DNA.
DR   EMBL; AE014297; AAF57084.1; -; Genomic_DNA.
DR   EMBL; BT003277; AAO25034.1; -; mRNA.
DR   EMBL; BT011080; AAR82746.1; -; mRNA.
DR   EMBL; AY118654; AAM50023.1; ALT_SEQ; mRNA.
DR   PIR; S33641; S33641.
DR   RefSeq; NP_476850.1; NM_057502.5. [P28166-1]
DR   RefSeq; NP_733402.1; NM_170523.3. [P28166-2]
DR   UniGene; Dm.4708; -.
DR   ProteinModelPortal; P28166; -.
DR   SMR; P28166; 289-404, 694-756, 920-1053.
DR   BioGrid; 68501; 14.
DR   IntAct; P28166; 5.
DR   MINT; MINT-94472; -.
DR   STRING; 7227.FBpp0303607; -.
DR   PaxDb; P28166; -.
DR   GeneID; 43650; -.
DR   KEGG; dme:Dmel_CG1322; -.
DR   CTD; 43650; -.
DR   FlyBase; FBgn0004606; zfh1.
DR   eggNOG; KOG3623; Eukaryota.
DR   eggNOG; ENOG410ZFMZ; LUCA.
DR   InParanoid; P28166; -.
DR   KO; K09299; -.
DR   OrthoDB; EOG7C5M7G; -.
DR   PhylomeDB; P28166; -.
DR   SignaLink; P28166; -.
DR   GenomeRNAi; 43650; -.
DR   NextBio; 835065; -.
DR   PRO; PR:P28166; -.
DR   Proteomes; UP000000803; Chromosome 3R.
DR   Bgee; P28166; -.
DR   Genevisible; P28166; DM.
DR   GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR   GO; GO:0003677; F:DNA binding; TAS:FlyBase.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000977; F:RNA polymerase II regulatory region sequence-specific DNA binding; IDA:FlyBase.
DR   GO; GO:0003705; F:transcription factor activity, RNA polymerase II distal enhancer sequence-specific binding; IDA:FlyBase.
DR   GO; GO:0019730; P:antimicrobial humoral response; IMP:FlyBase.
DR   GO; GO:0061321; P:garland nephrocyte differentiation; IMP:FlyBase.
DR   GO; GO:0008354; P:germ cell migration; IMP:FlyBase.
DR   GO; GO:0008406; P:gonad development; TAS:FlyBase.
DR   GO; GO:0007507; P:heart development; NAS:FlyBase.
DR   GO; GO:0007516; P:hemocyte development; IMP:FlyBase.
DR   GO; GO:0048542; P:lymph gland development; IMP:FlyBase.
DR   GO; GO:0007498; P:mesoderm development; IGI:FlyBase.
DR   GO; GO:0008045; P:motor neuron axon guidance; IMP:FlyBase.
DR   GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:FlyBase.
DR   GO; GO:0007399; P:nervous system development; IEP:FlyBase.
DR   GO; GO:0007280; P:pole cell migration; TAS:FlyBase.
DR   GO; GO:0048103; P:somatic stem cell division; IMP:FlyBase.
DR   Gene3D; 1.10.10.60; -; 1.
DR   Gene3D; 3.30.160.60; -; 5.
DR   InterPro; IPR017970; Homeobox_CS.
DR   InterPro; IPR001356; Homeobox_dom.
DR   InterPro; IPR009057; Homeodomain-like.
DR   InterPro; IPR007087; Znf_C2H2.
DR   InterPro; IPR015880; Znf_C2H2-like.
DR   InterPro; IPR013087; Znf_C2H2/integrase_DNA-bd.
DR   Pfam; PF00046; Homeobox; 1.
DR   SMART; SM00389; HOX; 1.
DR   SMART; SM00355; ZnF_C2H2; 9.
DR   SUPFAM; SSF46689; SSF46689; 1.
DR   PROSITE; PS00027; HOMEOBOX_1; 1.
DR   PROSITE; PS50071; HOMEOBOX_2; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 6.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 9.
PE   1: Evidence at protein level;
KW   Alternative splicing; Complete proteome; DNA-binding; Homeobox;
KW   Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW   Zinc; Zinc-finger.
FT   CHAIN         1   1054       Zinc finger protein 1.
FT                                /FTId=PRO_0000047241.
FT   ZN_FING      74     97       C2H2-type 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     289    311       C2H2-type 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     324    346       C2H2-type 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     355    377       C2H2-type 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     383    407       C2H2-type 5. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     628    651       C2H2-type 6. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   DNA_BIND    699    758       Homeobox. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00108}.
FT   ZN_FING     967    989       C2H2-type 7. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     995   1017       C2H2-type 8. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING    1023   1044       C2H2-type 9. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   COMPBIAS    222    246       Gln-rich (OPA repeat).
FT   MOD_RES     582    582       Phosphoserine.
FT                                {ECO:0000269|PubMed:18327897}.
FT   MOD_RES     586    586       Phosphoserine.
FT                                {ECO:0000269|PubMed:18327897}.
FT   MOD_RES     934    934       Phosphoserine.
FT                                {ECO:0000269|PubMed:18327897}.
FT   VAR_SEQ       1    307       Missing (in isoform A).
FT                                {ECO:0000303|Ref.4}.
FT                                /FTId=VSP_009670.
FT   VAR_SEQ     308    324       EQLHSPCGPAAVSNVSQ -> MSAAACLLSSSTSSFEK
FT                                (in isoform A). {ECO:0000303|Ref.4}.
FT                                /FTId=VSP_009671.
FT   CONFLICT     78     78       Q -> K (in Ref. 4; AAR82746).
FT                                {ECO:0000305}.
FT   CONFLICT    147    147       S -> T (in Ref. 4; AAR82746).
FT                                {ECO:0000305}.
FT   CONFLICT    239    239       Q -> QMQQQQQ (in Ref. 1; AAA29050).
FT                                {ECO:0000305}.
FT   CONFLICT    625    625       A -> S (in Ref. 1; AAA29050, 4; AAR82746
FT                                and 5; AAM50023). {ECO:0000305}.
FT   CONFLICT    954    954       A -> V (in Ref. 1; AAA29050).
FT                                {ECO:0000305}.
SQ   SEQUENCE   1054 AA;  116598 MW;  5189AB2214AB5B8B CRC64;
     MLSCLAPSSS RFGQEDTIIQ QSMPSTSPFA MQFPSLASTL LHHNQSPKHS NPGSSGIQDA
     HPNQPGAAAD AFLVKCTQCH KRFPEYQSLS EHIASEHPHD KLNCGAAQPE SDAEDEQSNM
     SGSSRRYAKS PLASNNNSST ANANNNSTSS QSMNNNSELA KNHNSANKMS PMCSPGSLTP
     GDLFAQLQHP PPQLPPHLHA QFMAAAASLA MQSARTASSP SQQQQQQLQQ QQQLQQQQQH
     QMAMQQLLPP QLPGSNSSVG SNSAYDLDLS APRSTSSPGS TTGDLSGAYP CMQCTASFAS
     REQLEQHEQL HSPCGPAAVS NVSQTCRICH KAFANVYRLQ RHMISHDESA LLRKFKCKEC
     DKAFKFKHHL KEHVRIHSGE KPFGCDNCGK RFSHSGSFSS HMTSKKCISM GLKLNNNRAL
     LKRLEKSPGS ASSASRRSPS DHGKGKLPEQ PSLPGLPHPM SYFASDAQVQ GGSAAPAPFP
     PFHPNYMNAA LLAFPHNFMA AAAGLDPRVH PYSIQRLLQL SAAGQQQREE EREEQQKQQQ
     HDEEETPDEP KLVMDIEEPE TKEMAPTPEA TEAATPIKRE ESREASPDPE SYRSSSQAIK
     QEQEPLNVAE ERQTPVEEHA PVEHAADLRC SRCSKQFNHP TELVQHEKVL CGLIKEELEQ
     HFQQQQATSF ALASASEEDE EDEEMDVEEE PRQESGERKV RVRTAINEEQ QQQLKQHYSL
     NARPSRDEFR MIAARLQLDP RVVQVWFQNN RSRERKMQSF QNNQAAGAAP PMPIDSQASL
     TREDQPLDLS VKRDPLTPKS ESSPPYIAPP SGEALNPEAI NLSRKFSTSA SMSPASISPS
     SAAALYFGAA PPPSPPNSQL DSTPRSGQAF PGLPPYMLPM SLPMEALFKM RPGGDFASNH
     ALMNSIKLPD YRGTSLSPGG SEKRSWRDDD SRISHEDEFG AGVLMPPKPR RGKAETHGHA
     GDPDLPYVCD QCDKAFAKQS SLARHKYEHS GQRPYQCIEC PKAFKHKHHL TEHKRLHSGE
     KPFQCSKCLK RFSHSGSYSQ HMNHRYSYCK PYRE
//
ID   Q91647_XENLA            Unreviewed;       521 AA.
AC   Q91647;
DT   01-NOV-1996, integrated into UniProtKB/TrEMBL.
DT   01-NOV-1996, sequence version 1.
DT   11-NOV-2015, entry version 75.
DE   SubName: Full=XPolycomb {ECO:0000313|EMBL:AAC59728.1};
GN   Name=cbx4 {ECO:0000313|Xenbase:XB-GENE-986722};
GN   Synonyms=XPolycomb {ECO:0000313|EMBL:AAC59728.1};
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Amphibia; Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus;
OC   Xenopus.
OX   NCBI_TaxID=8355 {ECO:0000313|EMBL:AAC59728.1};
RN   [1] {ECO:0000313|EMBL:AAC59728.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=8555110; DOI=10.1016/0925-4773(95)00422-X;
RA   Reijnen M.J., Hamer K.M., den Blaauwen J.L., Lambrechts C.,
RA   Schoneveld I., van Driel R., Otte A.P.;
RT   "Polycomb and bmi-1 homologs are expressed in overlapping patterns in
RT   Xenopus embryos and are able to interact with each other.";
RL   Mech. Dev. 53:35-46(1995).
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; U39929; AAC59728.1; -; mRNA.
DR   PIR; I51693; I51693.
DR   RefSeq; NP_001080949.1; NM_001087480.1.
DR   UniGene; Xl.338; -.
DR   ProteinModelPortal; Q91647; -.
DR   SMR; Q91647; 8-65.
DR   GeneID; 394294; -.
DR   KEGG; xla:394294; -.
DR   CTD; 8535; -.
DR   Xenbase; XB-GENE-986722; cbx4.
DR   HOVERGEN; HBG005257; -.
DR   KO; K11452; -.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR   InterPro; IPR000953; Chromo/shadow_dom.
DR   InterPro; IPR017984; Chromo_dom_subgr.
DR   InterPro; IPR023780; Chromo_domain.
DR   InterPro; IPR016197; Chromodomain-like.
DR   InterPro; IPR023779; Chromodomain_CS.
DR   Pfam; PF00385; Chromo; 1.
DR   PRINTS; PR00504; CHROMODOMAIN.
DR   SMART; SM00298; CHROMO; 1.
DR   SUPFAM; SSF54160; SSF54160; 1.
DR   PROSITE; PS00598; CHROMO_1; 1.
DR   PROSITE; PS50013; CHROMO_2; 1.
PE   2: Evidence at transcript level;
KW   Nucleus {ECO:0000256|SAAS:SAAS00010661}.
SQ   SEQUENCE   521 AA;  58804 MW;  1AC11753EEF79B56 CRC64;
     MELPAVGEHV FAVESIEKKR IRKGRVEYLV KWRGWSSKYN TWEPEENILD PRLLVAFQNR
     ERQEQIMGYR KRGPKPKNNL VSMPSFARRS NVLSGLHDSS GENRTKLDLG PIPKSHQYQL
     NSKKHHQYQP SGKDHNEKHH SSNKKKYYYQ LNSKKHHHYQ PDPKLYEQYT IEKESQISTD
     VRNRHRDSLT HTQAADMGTQ LKNGTDSVIS GPERNGICNG VSSSPSTEMS SSPSTELSSS
     PSTELPSSGV GGKMKIVKNK NKNGRIVIVM SKYMENGMQS VKIKSSEEDC DMGDVRRRFD
     SPGTLNGDKT CTAQEEKTEH WKKRVESRVK IHEGSKSVDK GSVHLAGLRR TYSTASETLN
     DQPLQLTTKS SHVPMPNRTR SPVYAGEPYN DLVYTNPRKR CLSEANGNKE LCKKTLTSRS
     VSAPGIVECK GGLTPLNVPL QEPDIILLDS DLDEPIDLRC VKSRCDSDQE VDKPEIQVTQ
     NPQSVDVDVC ESQFKPFFGN IVITDVTANC LTVTFKEYIT V
//
#~~# #~+~~+~# #~~#
#LOG 00:00:00 Activity Log for SLiMSuite V1.5.2: Tue Dec 8 23:27:22 2015
#DIR 00:00:00 Run from directory: /srv/slimsuite/logs/prod
#ARG 00:00:00 Commandline arguments: run ip=129.94.133.155 slimfinder&uniprotid=LIG_CtBP_PxDLS_1&dismask=T&runid=CtBP-NoEFilter&efilter=F&jobid=15120800036
#VIO 00:00:00 Verbosity: -1; Interactivity: -1.
#PROG 00:00:00 SLiMFinder V5.2.3: Short Linear Motif Finder
#CMD 00:00:00 Full SLiMFinder CmdList: proglog=F iucut=0.2 usegopher=T protscores=T megablam=F orthdb=qfo_ref.2015-04.Eukaryota.fas sourcedate=2015-04-15 walltime=0 maxgapx=3 rest=format uniprotid=LIG_CtBP_PxDLS_1.acc dismask=T runid=CtBP-NoEFilter efilter=F jobid=15120800036 resfile=slimfinder.csv savespace=0 targz=F megaslim=seqin basefile=slimfinder
#DB 00:00:00 /srv/slimsuite/data/orthdb/qfo_ref.2015-04/qfo_ref.2015-04.Eukaryota.fas already formatted. (Force = False).
#DB 00:00:00 /srv/slimsuite/data/orthdb/qfo_ref.2015-04/qfo_ref.2015-04.Eukaryota.fas already formatted. (Force = False).
#ALPH 00:00:00 Alphabet: A C D E F G H I K L M N P Q R S T V W Y
#WARN 00:00:00 NOTE: cloudfix=F. Be wary of ambiguity over-predictions.
#URL 00:00:03 Extracting 29 AccNum from http://www.uniprot.org/uniprot/: 29 read & extracted; 0 failed; 0 duplicates.
#DAT 00:00:04 Extracting entries from slimfinder.dat: 29 read, 29 extracted.
#SEQ 00:00:04 29 sequences loaded from /srv/slimsuite/scratch/prod/slimfinder/15120800036/slimfinder.dat (Format: uniprot).
#FAS 00:00:04 29 Sequences output to /srv/slimsuite/scratch/prod/slimfinder/15120800036/slimfinder.fas.
#EVOL 00:00:04 WARNING! No evolutionary filtering (efilter=F)
#MIN 00:00:04 AmbOcc 0.05 & 29 UP => AmbOcc 2 UPC.
#MIN 00:00:04 MinOcc 0.05 & 29 UP => MinOcc 3 UPC.
#DIS 00:00:04 Disorder score file: /srv/slimsuite/scratch/prod/slimfinder/15120800036/slimfinder.iupred.txt
#MASK 00:00:04 CBX4_HUMAN__O00257 masked 3 ordered regions. (54 X added.)
#MASK 00:00:04 COM1_HUMAN__Q99708 masked 14 ordered regions. (46 X added.)
#MASK 00:00:04 E1A_ADE02__P03254 masked 7 ordered regions. (54 X added.)
#MASK 00:00:04 ELK3_HUMAN__P41970 masked 9 ordered regions. (139 X added.)
#MASK 00:00:04 EVI1_HUMAN__Q03112 masked 14 ordered regions. (136 X added.)
#MASK 00:00:04 FOG1_HUMAN__Q8IX07 masked 15 ordered regions. (245 X added.)
#MASK 00:00:04 FOG2_HUMAN__Q8WW38 masked 25 ordered regions. (324 X added.)
#MASK 00:00:04 HAIR_DROME__P14003 masked 6 ordered regions. (11 X added.)
#MASK 00:00:04 HDAC4_HUMAN__P56524 masked 23 ordered regions. (213 X added.)
#MASK 00:00:04 HDAC5_HUMAN__Q9UQL6 masked 26 ordered regions. (269 X added.)
#MASK 00:00:04 HDAC9_MOUSE__Q99N13 masked 5 ordered regions. (42 X added.)
#MASK 00:00:04 HDAC7_MOUSE__Q8C2B3 masked 21 ordered regions. (232 X added.)
#MASK 00:00:04 HIC1_HUMAN__Q14526 masked 22 ordered regions. (221 X added.)
#MASK 00:00:04 IKZF1_HUMAN__Q13422 masked 8 ordered regions. (110 X added.)
#MASK 00:00:04 IKZF4_HUMAN__Q9H2S9 masked 12 ordered regions. (109 X added.)
#MASK 00:00:04 KLF3_HUMAN__P57682 masked 9 ordered regions. (48 X added.)
#MASK 00:00:04 KLF8_HUMAN__O95600 masked 15 ordered regions. (49 X added.)
#MASK 00:00:04 KNIR_DROME__P10734 masked 12 ordered regions. (107 X added.)
#MASK 00:00:04 LCOR_HUMAN__Q96JN0 masked 7 ordered regions. (17 X added.)
#MASK 00:00:04 NRIP1_HUMAN__P48552 masked 10 ordered regions. (26 X added.)
#MASK 00:00:04 SOX6_HUMAN__P35712 masked 10 ordered regions. (17 X added.)
#MASK 00:00:04 T7L1A_XENLA__P70062 masked 7 ordered regions. (66 X added.)
#MASK 00:00:04 TGIF1_HUMAN__Q15583 masked 10 ordered regions. (57 X added.)
#MASK 00:00:04 TRPS1_HUMAN__Q9UHF7 masked 23 ordered regions. (365 X added.)
#MASK 00:00:04 TTKB_DROME__P17789 masked 11 ordered regions. (185 X added.)
#MASK 00:00:04 ZEB1_HUMAN__P37275 masked 25 ordered regions. (184 X added.)
#MASK 00:00:04 ZEB2_HUMAN__O60315 masked 30 ordered regions. (145 X added.)
#MASK 00:00:04 ZFH1_DROME__P28166 masked 17 ordered regions. (104 X added.)
#MASK 00:00:04 cbx4_XENLA__Q91647 masked 6 ordered regions. (65 X added.)
#FTMASK 00:00:04 FTMask: None
#MASK 00:00:04 Masked CBX4_HUMAN__O00257 "low complexity" regions. (21 X added.)
#MASK 00:00:04 Masked COM1_HUMAN__Q99708 "low complexity" regions. (3 X added.)
#MASK 00:00:04 Masked E1A_ADE02__P03254 "low complexity" regions. (3 X added.)
#MASK 00:00:04 Masked ELK3_HUMAN__P41970 "low complexity" regions. (6 X added.)
#MASK 00:00:04 Masked EVI1_HUMAN__Q03112 "low complexity" regions. (3 X added.)
#MASK 00:00:04 Masked FOG1_HUMAN__Q8IX07 "low complexity" regions. (34 X added.)
#MASK 00:00:04 Masked FOG2_HUMAN__Q8WW38 "low complexity" regions. (5 X added.)
#MASK 00:00:04 Masked HAIR_DROME__P14003 "low complexity" regions. (30 X added.)
#MASK 00:00:04 Masked HDAC4_HUMAN__P56524 "low complexity" regions. (18 X added.)
#MASK 00:00:04 Masked HDAC5_HUMAN__Q9UQL6 "low complexity" regions. (37 X added.)
#MASK 00:00:04 Masked HDAC9_MOUSE__Q99N13 "low complexity" regions. (20 X added.)
#MASK 00:00:04 Masked HDAC7_MOUSE__Q8C2B3 "low complexity" regions. (8 X added.)
#MASK 00:00:04 Masked HIC1_HUMAN__Q14526 "low complexity" regions. (33 X added.)
#MASK 00:00:04 Masked IKZF4_HUMAN__Q9H2S9 "low complexity" regions. (8 X added.)
#MASK 00:00:04 Masked KNIR_DROME__P10734 "low complexity" regions. (21 X added.)
#MASK 00:00:04 Masked NRIP1_HUMAN__P48552 "low complexity" regions. (6 X added.)
#MASK 00:00:04 Masked SOX6_HUMAN__P35712 "low complexity" regions. (20 X added.)
#MASK 00:00:04 Masked T7L1A_XENLA__P70062 "low complexity" regions. (13 X added.)
#MASK 00:00:04 Masked TGIF1_HUMAN__Q15583 "low complexity" regions. (10 X added.)
#MASK 00:00:04 Masked TRPS1_HUMAN__Q9UHF7 "low complexity" regions. (3 X added.)
#MASK 00:00:04 Masked TTKB_DROME__P17789 "low complexity" regions. (21 X added.)
#MASK 00:00:04 Masked ZEB1_HUMAN__P37275 "low complexity" regions. (39 X added.)
#MASK 00:00:04 Masked ZEB2_HUMAN__O60315 "low complexity" regions. (30 X added.)
#MASK 00:00:04 Masked ZFH1_DROME__P28166 "low complexity" regions. (44 X added.)
#MASK 00:00:04 MetMask: 29 N-terminal Ms masked
#MASK 00:00:04 Masked ZEB1_HUMAN__P37275 position-specific AAs. (1 X added.)
#MASK 00:00:04 slimfinder: Masking of input sequences complete.
#SPACE 00:00:04 Motif Space, 2 positions: 1,200 motifs
#SPACE 00:00:04 Motif Space, 3 positions: 72,000 motifs
#SPACE 00:00:04 Motif Space, 4 positions: 4,320,000 motifs
#SPACE 00:00:04 Motif Space, 5 positions: 259,200,000 motifs
#DIM 00:00:04 Read dimers from 29 seq: 1,247 dimers
#DIM 00:00:04 Reducing dimers: 1,201 >= 2 of 29 UPC
#SLIM 00:00:04 Selecting 2aa SLiMs: 1,201 >= 2 of 29 UPC
#AMB 00:00:04 Adding Wildcard ambiguity: 100.0% (0 amb motifs)
#AMB 00:00:04 Adding Degeneracy ambiguity: 100.0% (0 amb motifs)
#SLIM 00:01:05 Extending 3aa SLiMs >= 2 of 29 UPC: 29,000 SLiMs
#AMB 00:01:24 Adding Wildcard ambiguity: 100.0% (6,009 amb motifs)
#AMB 00:03:04 Adding Degeneracy ambiguity: 100.0% (11,606 amb motifs)
#SLIM 00:06:32 Extending 4aa SLiMs >= 2 of 29 UPC: 51,312 SLiMs
#AMB 00:07:00 Adding Wildcard ambiguity: 100.0% (11,977 amb motifs)
#AMB 00:07:48 Adding Degeneracy ambiguity: 100.0% (21,111 amb motifs)
#SLIM 00:11:51 Extending 5aa SLiMs >= 2 of 29 UPC: 38,668 SLiMs
#AMB 00:12:11 Adding Wildcard ambiguity: 100.0% (2,949 amb motifs)
#AMB 00:13:31 Adding Degeneracy ambiguity: 100.0% (2,439 amb motifs)
#SLIM 00:13:31 176,272 SLiMs >= 2 of 29 UPC
#SAVE 00:13:50 SLiMFinder Intermediate saved as /srv/slimsuite/scratch/prod/slimfinder/15120800036/slimfinder.l5w2o2a3.FreqDisComp-5-8.pickle (Python pickle).
#GZIP 00:13:53 /srv/slimsuite/scratch/prod/slimfinder/15120800036/slimfinder.l5w2o2a3.FreqDisComp-5-8.pickle zipped.
#SLIM 00:13:55 Filtering 176,272 SLiMs: 87,767 retained.
#PROB 00:15:06 Calculating [Sig] SLiM Probabilities (Sig<=0.10) complete: 1,000 ranked SLiMs.
#COMB 00:15:15 Combined Occurrence Attributes complete.
#CLOUD 00:26:09 Making "Motif Clouds" for 1000 Sig Motifs: 4 Clouds
#WARN 00:26:14 Multiple motif offsets for [ST]..KP..C..C vs H.{1,2}K.H.R.H
#WARN 00:26:17 Multiple motif offsets for [KR]P..C..C.[KR] vs H.{1,2}K.H.R.H
#WARN 00:26:22 Multiple motif offsets for KP..C..C.{1,2}R vs H.{1,2}K.H.R.H
#WARN 00:26:24 Multiple motif offsets for [ST]..[KR]P..C..C vs H.{1,2}K.H.R.H
#WARN 00:26:27 Multiple motif offsets for PY.C..C.[KR] vs H.{1,2}K.H.R.H
#WARN 00:26:31 Multiple motif offsets for E.P[FY].C..C vs H.{1,2}K.H.R.H
#WARN 00:26:39 Multiple motif offsets for KP..C..C vs H.{1,2}K.H.R.H
#WARN 00:26:42 Multiple motif offsets for [KR]P[FY].C..C vs H.{1,2}K.H.R.H
#WARN 00:26:50 Multiple motif offsets for P[HY].C..C.[KR] vs H.{1,2}K.H.R.H
#WARN 00:26:56 Multiple motif offsets for P[FY].C..C vs H.{1,2}K.H.R.H
#WARN 00:27:03 Multiple motif offsets for [KR]P..C..C vs H.{1,2}K.H.R.H
#WARN 00:27:07 Multiple motif offsets for K.{0,1}P..C..C vs G.{0,1}K.Y.C..C
#WARN 00:27:09 Multiple motif offsets for PY.C..C vs H.{1,2}K.H.R.H
#WARN 00:27:13 Multiple motif offsets for P..C..CG..[FY] vs G.{0,1}K.Y.C..C
#WARN 00:27:19 Multiple motif offsets for KP..C..CG vs G.{0,1}K.Y.C..C
#WARN 00:27:21 Multiple motif offsets for P[FHY].C..C vs H.{1,2}K.H.R.H
#WARN 00:27:36 Multiple motif offsets for S..KP..C..C vs H.{1,2}K.H.R.H
#WARN 00:27:40 Multiple motif offsets for P..C..CG[KR] vs G.{0,1}K.Y.C..C
#WARN 00:27:41 Multiple motif offsets for [KR]P..C..CG vs G.{0,1}K.Y.C..C
#WARN 00:27:48 Multiple motif offsets for PY.C..C.K vs H.{1,2}K.H.R.H
#WARN 00:27:53 Multiple motif offsets for G..PY.C..C vs H.{1,2}K.H.R.H
#WARN 00:27:54 Multiple motif offsets for E[KR]P..C..C vs H.{1,2}K.H.R.H
#WARN 00:27:59 Multiple motif offsets for G.{0,1}K.Y.C..C vs P[FY].C..CG
#WARN 00:27:59 Multiple motif offsets for G.{0,1}K.Y.C..C vs P..C..CG
#WARN 00:27:59 Multiple motif offsets for G.{0,1}K.Y.C..C vs P..C..CG.{0,1}R
#WARN 00:27:59 Multiple motif offsets for G.{0,1}K.Y.C..C vs PY.C..CG
#WARN 00:28:05 Multiple motif offsets for PY.C..C.{1,2}R vs H.{1,2}K.H.R.H
#WARN 00:28:13 Multiple motif offsets for PY.C..C.{0,1}K vs H.{1,2}K.H.R.H
#WARN 00:28:23 Multiple motif offsets for H.{0,1}R.{1,2}H.GE vs R.{1,2}H.GEK
#WARN 00:28:24 Multiple motif offsets for H.{0,1}R.{1,2}H.GE vs R.{1,2}H..EKP
#WARN 00:28:24 Multiple motif offsets for H.{0,1}R.{1,2}H.GE vs R.{1,2}HT.E.P
#WARN 00:28:31 Multiple motif offsets for G..P[HY].C..C vs H.{1,2}K.H.R.H
#WARN 00:28:35 Multiple motif offsets for L..H.{0,1}R.{1,2}H.G vs H[ILM][KR].H
#WARN 00:28:35 Multiple motif offsets for L..H.{0,1}R.{1,2}H.G vs R.{1,2}HT.E.P
#WARN 00:28:38 Multiple motif offsets for H.{0,1}R.{1,2}H.G..P vs R.{1,2}HT.E.P
#WARN 00:28:40 Multiple motif offsets for R.{1,2}H.GE.P vs H.{0,1}R.{1,2}H.G.K
#WARN 00:28:40 Multiple motif offsets for R.{1,2}H.GE.P vs R.{1,2}H.GEK
#WARN 00:28:40 Multiple motif offsets for R.{1,2}H.GE.P vs R.{1,2}H.G.KP
#WARN 00:28:40 Multiple motif offsets for R.{1,2}H.GE.P vs R.{1,2}H..EKP
#WARN 00:28:41 Multiple motif offsets for R.{1,2}H.GE.P vs R.{1,2}HT.E.P
#WARN 00:29:19 Multiple motif offsets for KA[FH][KR]..H vs K..H.{0,1}L..H.R
#WARN 00:29:24 Multiple motif offsets for H.{0,1}R.{1,2}H.G.K vs R.{1,2}H..EKP
#WARN 00:29:25 Multiple motif offsets for H.{0,1}R.{1,2}H.G.K vs R.{1,2}HT.E.P
#WARN 00:29:25 Multiple motif offsets for H.{0,1}R.{1,2}H.G.K vs R.{1,2}H..E.P
#WARN 00:29:28 Multiple motif offsets for YEC.NC vs H.{1,2}K.H.R.H
#WARN 00:29:33 Multiple motif offsets for R.{1,2}H.GEK vs R.{1,2}H.G.KP
#WARN 00:29:33 Multiple motif offsets for R.{1,2}H.GEK vs R.{1,2}H..EKP
#WARN 00:29:34 Multiple motif offsets for R.{1,2}H.GEK vs R.{1,2}HT.E.P
#WARN 00:29:34 Multiple motif offsets for R.{1,2}H.GEK vs R.{1,2}H..E.P
#WARN 00:29:44 Multiple motif offsets for R.{1,2}H.G.KP vs H.{0,1}R.{1,2}H..EK
#WARN 00:29:44 Multiple motif offsets for R.{1,2}H.G.KP vs R.{1,2}H..EKP
#WARN 00:29:44 Multiple motif offsets for R.{1,2}H.G.KP vs R.{1,2}HT.E.P
#WARN 00:29:45 Multiple motif offsets for R.{1,2}H.G.KP vs R.{1,2}H..E.P
#WARN 00:29:45 Multiple motif offsets for KPY.C..C vs H.{1,2}K.H.R.H
#WARN 00:29:49 Multiple motif offsets for K.YEC..C vs H.{1,2}K.H.R.H
#WARN 00:29:50 Multiple motif offsets for YEC..C.K vs H.{1,2}K.H.R.H
#WARN 00:29:53 Multiple motif offsets for H.{0,1}R.{1,2}H..EK vs R.{1,2}H..EKP
#WARN 00:29:54 Multiple motif offsets for H.{0,1}R.{1,2}H..EK vs R.{1,2}HT.E.P
#WARN 00:30:02 Multiple motif offsets for H.{1,2}K.H.R.H vs E.PY.C..C
#WARN 00:30:02 Multiple motif offsets for H.{1,2}K.H.R.H vs P..C.NC..R
#WARN 00:30:06 Multiple motif offsets for K.[FH][KR][HR].H vs [HK][HR][HKR].[HY]..[DE]
#WARN 00:30:06 Multiple motif offsets for K.[FH][KR][HR].H vs K..H.{0,1}L..H.R
#WARN 00:30:11 Multiple motif offsets for R.{1,2}H..EKP vs R.{1,2}HT.E.P
#WARN 00:30:40 Multiple motif offsets for A[FH][KR][HR].H vs [HK][HR][HKR].[HY]..[DE]
#WARN 00:30:45 Multiple motif offsets for H[FLM]..H[ST]..K vs H.{0,1}L..H.R.H
#WARN 00:30:47 Multiple motif offsets for L..H.R..[ST]..K vs H[ILM][KR].H
#WARN 00:30:49 Multiple motif offsets for [FLM][KR].[HR][ST]..K vs [KR].[HR].[KR].[HK]..E
#WARN 00:30:49 Multiple motif offsets for [FLM][KR].[HR][ST]..K vs L..[HR].R[IL][HK]
#WARN 00:30:49 Multiple motif offsets for [FLM][KR].[HR][ST]..K vs LK.[HR].R.[HK]
#WARN 00:30:49 Multiple motif offsets for [FLM][KR].[HR][ST]..K vs K.[HR].R[IL][HK]
#WARN 00:30:49 Multiple motif offsets for [FLM][KR].[HR][ST]..K vs H.{0,1}L..H.R.H
#WARN 00:30:49 Multiple motif offsets for [FLM][KR].[HR][ST]..K vs K.[HR].R.[HKR]
#WARN 00:30:52 Multiple motif offsets for H[FLM]R..[ST]..K vs H.{0,1}L..H.R.H
#WARN 00:30:52 Multiple motif offsets for [FLM]R.H[ST]..K vs H.{0,1}L..H.R.H
#WARN 00:30:53 Multiple motif offsets for H.GEKP vs K.{1,2}HL..H.R
#WARN 00:30:53 Multiple motif offsets for H.GEKP vs K.{1,2}HL..H.{0,1}R
#WARN 00:30:54 Multiple motif offsets for H[LM]..HS..K vs H.{0,1}L..H.R.H
#WARN 00:30:58 Multiple motif offsets for H..IHS..K vs H.{0,1}L..H.R.H
#WARN 00:30:58 Multiple motif offsets for K.H.R..[ST]..K vs H.{0,1}L..H.R.H
#WARN 00:30:58 Multiple motif offsets for K.H.R..[ST]..K vs H[ILM][KR].H
#WARN 00:31:00 Multiple motif offsets for [LM][KR].[HR]S..K vs [KR].[HR].[KR].[HK]..E
#WARN 00:31:00 Multiple motif offsets for [LM][KR].[HR]S..K vs L..[HR].R[IL][HK]
#WARN 00:31:00 Multiple motif offsets for [LM][KR].[HR]S..K vs LK.[HR].R.[HK]
#WARN 00:31:00 Multiple motif offsets for [LM][KR].[HR]S..K vs K.[HR].R[IL][HK]
#WARN 00:31:00 Multiple motif offsets for [LM][KR].[HR]S..K vs H.{0,1}L..H.R.H
#WARN 00:31:00 Multiple motif offsets for [LM][KR].[HR]S..K vs K.[HR].R.[HKR]
#WARN 00:31:01 Multiple motif offsets for H.RI.S..K vs H.{0,1}L..H.R.H
#WARN 00:31:02 Multiple motif offsets for RIHS..K vs H.{0,1}L..H.R.H
#WARN 00:31:03 Multiple motif offsets for H[ST]GEK vs K.{1,2}HL..H.R
#WARN 00:31:03 Multiple motif offsets for H[ST]GEK vs K.{1,2}HL..H.{0,1}R
#WARN 00:31:05 Multiple motif offsets for KA.[KR][HR].H vs [HK][HR][HKR].[HY]..[DE]
#WARN 00:31:05 Multiple motif offsets for KA.[KR][HR].H vs K..H.{0,1}L..H.R
#WARN 00:31:09 Multiple motif offsets for L..H.R.H..E vs H[ILM][KR].H
#WARN 00:31:13 Multiple motif offsets for [HR].[KR].[HK].[AG]E vs L..[HR].R[IL][HK]
#WARN 00:31:13 Multiple motif offsets for [HR].[KR].[HK].[AG]E vs LK.[HR].R.[HK]
#WARN 00:31:13 Multiple motif offsets for [HR].[KR].[HK].[AG]E vs K.[HR].R[IL][HK]
#WARN 00:31:13 Multiple motif offsets for [HR].[KR].[HK].[AG]E vs K.[HR].R.[HKR]
#WARN 00:31:14 Multiple motif offsets for [LV]..[HR].[KR].[HK]..E vs L..[HR].R[IL][HK]
#WARN 00:31:14 Multiple motif offsets for [LV]..[HR].[KR].[HK]..E vs LK.[HR].R.[HK]
#WARN 00:31:14 Multiple motif offsets for [LV]..[HR].[KR].[HK]..E vs K.[HR].R[IL][HK]
#WARN 00:31:14 Multiple motif offsets for [LV]..[HR].[KR].[HK]..E vs K.[HR].R.[HKR]
#WARN 00:31:14 Multiple motif offsets for [LV]..[HR].[KR].[HK]..E vs H[ILM][KR].H
#WARN 00:31:16 Multiple motif offsets for R.H.GEK vs K.{1,2}HL..H.R
#WARN 00:31:16 Multiple motif offsets for R.H.GEK vs K.{1,2}HL..H.{0,1}R
#WARN 00:31:17 Multiple motif offsets for [HR].[KR].[HK]..E[KR] vs L..[HR].R[IL][HK]
#WARN 00:31:17 Multiple motif offsets for [HR].[KR].[HK]..E[KR] vs LK.[HR].R.[HK]
#WARN 00:31:17 Multiple motif offsets for [HR].[KR].[HK]..E[KR] vs K.[HR].R[IL][HK]
#WARN 00:31:17 Multiple motif offsets for [HR].[KR].[HK]..E[KR] vs K.[HR].R.[HKR]
#WARN 00:31:19 Multiple motif offsets for [KR].[HK].[AG]E[KR] vs K.{1,2}HL..H.R
#WARN 00:31:19 Multiple motif offsets for [KR].[HK].[AG]E[KR] vs K.{1,2}HL..H.{0,1}R
#WARN 00:31:20 Multiple motif offsets for K.H.R.H..E vs H[ILM][KR].H
#WARN 00:31:24 Multiple motif offsets for [KR].[HR].[KR].[HK]..E vs L..[HR].R[IL][HK]
#WARN 00:31:24 Multiple motif offsets for [KR].[HR].[KR].[HK]..E vs LK.[HR].R.[HK]
#WARN 00:31:24 Multiple motif offsets for [KR].[HR].[KR].[HK]..E vs K.[HR].R[IL][HK]
#WARN 00:31:24 Multiple motif offsets for [KR].[HR].[KR].[HK]..E vs K.[HR].R.[HKR]
#WARN 00:31:24 Multiple motif offsets for [KR].[HR].[KR].[HK]..E vs H[ILM][KR].H
#WARN 00:31:24 Multiple motif offsets for [KR].[HR].[KR].[HK]..E vs LK.[HR]..[IL][HK]
#WARN 00:31:27 Multiple motif offsets for L..H.R.H[ST] vs H[ILM][KR].H
#WARN 00:31:27 Multiple motif offsets for T.H.R.H[ST] vs H.{0,1}L..H.R.H
#WARN 00:31:27 Multiple motif offsets for H[FLM]R.H[ST] vs H.{0,1}L..H.R.H
#WARN 00:31:30 Multiple motif offsets for K.H.R.H[ST] vs H.{0,1}L..H.R.H
#WARN 00:31:30 Multiple motif offsets for K.H.R.H[ST] vs H[ILM][KR].H
#WARN 00:31:30 Multiple motif offsets for H[LM]R.HS vs H.{0,1}L..H.R.H
#WARN 00:31:31 Multiple motif offsets for H.RIHS vs H.{0,1}L..H.R.H
#WARN 00:31:31 Multiple motif offsets for EH..IHS vs H.{0,1}L..H.R.H
#WARN 00:31:32 Multiple motif offsets for [HR].[KR].[HK].[AG].[KR] vs L..[HR].R[IL][HK]
#WARN 00:31:32 Multiple motif offsets for [HR].[KR].[HK].[AG].[KR] vs LK.[HR].R.[HK]
#WARN 00:31:32 Multiple motif offsets for [HR].[KR].[HK].[AG].[KR] vs K.[HR].R[IL][HK]
#WARN 00:31:32 Multiple motif offsets for [HR].[KR].[HK].[AG].[KR] vs K.[HR].R.[HKR]
#WARN 00:31:33 Multiple motif offsets for E..RIHS vs H.{0,1}L..H.R.H
#WARN 00:31:34 Multiple motif offsets for L..H.R..[ST]G vs H[ILM][KR].H
#WARN 00:31:35 Multiple motif offsets for L..H.R..[ST].E vs H[ILM][KR].H
#WARN 00:31:35 Multiple motif offsets for HL..H.R..[ST] vs H.{0,1}L..H.R.H
#WARN 00:31:35 Multiple motif offsets for HL..H.R..[ST] vs H[ILM][KR].H
#WARN 00:31:36 Multiple motif offsets for EH.RI.S vs H.{0,1}L..H.R.H
#WARN 00:31:36 Multiple motif offsets for [HR][IL]..GE[HK] vs K.{1,2}HL..H.R
#WARN 00:31:36 Multiple motif offsets for [HR][IL]..GE[HK] vs K.{1,2}HL..H.{0,1}R
#WARN 00:31:38 Multiple motif offsets for HL..H.{0,1}R.{1,2}H vs H[ILM][KR].H
#WARN 00:31:41 Multiple motif offsets for L..H.[KR].H vs H[ILM][KR].H
#WARN 00:31:46 Multiple motif offsets for L..H.R.H.G vs H[ILM][KR].H
#WARN 00:31:46 Multiple motif offsets for L..[HR].R[IL][HK] vs H[ILM][KR].H
#WARN 00:31:47 Multiple motif offsets for HL..H.R.H vs H[ILM][KR].H
#WARN 00:31:47 Multiple motif offsets for HL..H.R.H vs H..[IL][HY]
#WARN 00:31:47 Multiple motif offsets for HL..H.R.H vs H..[ILM][HY]
#WARN 00:31:47 Multiple motif offsets for LK.[HR].R.[HK] vs H[ILM][KR].H
#WARN 00:31:48 Multiple motif offsets for K.[HR].R[IL][HK] vs H.{0,1}L..H.R.H
#WARN 00:31:48 Multiple motif offsets for K.[HR].R[IL][HK] vs H[ILM][KR].H
#WARN 00:31:48 Multiple motif offsets for L..H.R.H vs H[ILM][KR].H
#WARN 00:31:49 Multiple motif offsets for H.{0,1}L..H.R.H vs K.H.RIH
#WARN 00:31:49 Multiple motif offsets for H.{0,1}L..H.R.H vs H.K.H.R.H
#WARN 00:31:49 Multiple motif offsets for H.{0,1}L..H.R.H vs H[ILM][KR].H
#WARN 00:31:49 Multiple motif offsets for H.{0,1}L..H.R.H vs HLK.H.R
#WARN 00:31:49 Multiple motif offsets for H.{0,1}L..H.R.H vs [HR]H[FIL][KR].H
#WARN 00:31:49 Multiple motif offsets for H.{0,1}L..H.R.H vs LK.[HR]..[IL][HK]
#WARN 00:31:49 Multiple motif offsets for H.{0,1}L..H.R.H vs LK.H..IH
#WARN 00:31:49 Multiple motif offsets for H.{0,1}L..H.R.H vs H[HK]L..H..L
#WARN 00:31:49 Multiple motif offsets for H.{0,1}L..H.R.H vs H[HK]L..H..[IL]
#WARN 00:31:49 Multiple motif offsets for H.{0,1}L..H.R.H vs [HR]H.[KR].H
#WARN 00:31:49 Multiple motif offsets for H.{0,1}L..H.R.H vs K.H..IH
#WARN 00:31:49 Multiple motif offsets for H.{0,1}L..H.R.H vs H[HK].[KR].H..[IL]
#WARN 00:31:49 Multiple motif offsets for K.H.RIH vs H[ILM][KR].H
#WARN 00:31:50 Multiple motif offsets for L..H.R[IL]H vs H[ILM][KR].H
#WARN 00:31:51 Multiple motif offsets for L..H.RIH vs H[ILM][KR].H
#WARN 00:31:51 Multiple motif offsets for H.K.H.R.H vs H[ILM][KR].H
#WARN 00:31:51 Multiple motif offsets for K.H.R.H.G vs H[ILM][KR].H
#WARN 00:31:51 Multiple motif offsets for K.[HR].R.[HKR] vs H[ILM][KR].H
#WARN 00:31:52 Multiple motif offsets for H[ILM][KR].H vs LK.H.R.H
#WARN 00:31:52 Multiple motif offsets for H[ILM][KR].H vs L.EH.R.H
#WARN 00:31:52 Multiple motif offsets for H[ILM][KR].H vs [HK]..HL..H.R
#WARN 00:31:52 Multiple motif offsets for H[ILM][KR].H vs L..H.{0,1}R.{1,2}H..E
#WARN 00:31:52 Multiple motif offsets for H[ILM][KR].H vs K..H.{0,1}L..H.R
#WARN 00:31:52 Multiple motif offsets for H[ILM][KR].H vs HLK.H.R
#WARN 00:31:52 Multiple motif offsets for H[ILM][KR].H vs L..H..[ILM]H
#WARN 00:31:52 Multiple motif offsets for H[ILM][KR].H vs LK.[HR]..[IL][HK]
#WARN 00:31:52 Multiple motif offsets for H[ILM][KR].H vs LK.H..IH
#WARN 00:31:52 Multiple motif offsets for H[ILM][KR].H vs L..H..IH
#WARN 00:31:52 Multiple motif offsets for H[ILM][KR].H vs K.H..IH
#WARN 00:31:58 Multiple motif offsets for [HK]..HL..H.R vs [HK][HR][HKR].[HY]..[DE]
#WARN 00:31:58 Multiple motif offsets for [HK]..HL..H.R vs K..H.{0,1}L..H.R
#ALN 00:32:50 Unaligned peptides: aligning with PeptCluster
#AAPROP 00:32:50 Reading AA Properties from aaprop.txt... ...I L V C A G M F Y W H K R E Q D N S T P ...Hydrophobic ...Polar ...Small ...Proline ...Positive ...Negative ...Charged ...Tiny ...Aliphatic ...Aromatic ...Done!
#GAPX 00:32:50 PeptLen: 55; MaxLen: 56; Termini: True => 53 x 1 gap variants.
#GAPX 00:32:50 PeptLen: 54; MaxLen: 56; Termini: True => 1,378 x 2 gap variants.
#GAPX 00:33:53 PeptLen: 53; MaxLen: 56; Termini: True => 23,426 x 3 gap variants.
#WARN 00:33:53 Peptide WEGCTWKFARSDELTRHFRKHTGIKPFQCPDCDRSFSRSDHLALHRKRHMLV exceeds MapGapX=3; rejected.
#WARN 00:33:53 Peptide WDGCSWKFARSDELTRHFRKHTGIKPFRCTDCNRSFSRSDHLSLHRRRHDTM exceeds MapGapX=3; rejected.
#WARN 00:33:53 Peptide TWKFARSDELTRHFRKHTGIKPFQCPDCDRSFSRSDHLALHRKRHMLV exceeds MapGapX=3; rejected.
#WARN 00:33:53 Peptide SWKFARSDELTRHFRKHTGIKPFRCTDCNRSFSRSDHLSLHRRRHDTM exceeds MapGapX=3; rejected.
#WARN 00:33:53 Peptide GGRRQAVECIEDLLNESGQPLDLSCKRPRP exceeds MapGapX=3; rejected.
#WARN 00:33:53 Peptide YEPMDIKPSVIQRVPMEQQPLSLVIKKQIKEEEQPWRPW exceeds MapGapX=3; rejected.
#WARN 00:33:53 Peptide EGCTWKFARSDELTRHFRKHTGIKPFQCPDCDRSFSRSDHLALHRKRHMLV exceeds MapGapX=3; rejected.
#WARN 00:33:53 Peptide DGCSWKFARSDELTRHFRKHTGIKPFRCTDCNRSFSRSDHLSLHRRRHDTM exceeds MapGapX=3; rejected.
#WARN 00:33:53 Peptide SGEKPFQCSKCLKRFSHSGSYSQHMNHRYSYCKPYRE exceeds MapGapX=3; rejected.
#WARN 00:33:53 Peptide KPFQCSKCLKRFSHSGSYSQHMNHRYSYCKPYRE exceeds MapGapX=3; rejected.
#WARN 00:33:53 Peptide CPDCDRSFSRSDHLALHRKRHMLV exceeds MapGapX=3; rejected.
#WARN 00:33:53 Peptide CTDCNRSFSRSDHLSLHRRRHDTM exceeds MapGapX=3; rejected.
#WARN 00:33:53 Peptide WKFARSDELTRHFRKHTGIKPFQCPDCDRSFSRSDHLALHRKRHMLV exceeds MapGapX=3; rejected.
#WARN 00:33:53 Peptide WKFARSDELTRHFRKHTGIKPFRCTDCNRSFSRSDHLSLHRRRHDTM exceeds MapGapX=3; rejected.
#WARN 00:33:53 Peptide TDCNRSFSRSDHLSLHRRRHDTM exceeds MapGapX=3; rejected.
#WARN 00:33:53 Peptide TLLNGHMPVPIPSLDRAASPVLLSSNSQKS exceeds MapGapX=3; rejected.
#WARN 00:33:53 Peptide FECNMCGYHSQDRYEFSSHITRGEHRFHMS exceeds MapGapX=3; rejected.
#WARN 00:33:53 Peptide FECNICGYHSQDRYEFSSHIVRGEHKVG exceeds MapGapX=3; rejected.
#WARN 00:33:53 Peptide KTEGLMKDDRAESQASSLGQKVGESSEQVSEEKTNEA exceeds MapGapX=3; rejected.
#WARN 00:33:53 Peptide TCMERGYIKEDLDPCPRPKRRQPYNAIFSPKGKEQKT exceeds MapGapX=3; rejected.
#WARN 00:33:53 Peptide ECIEDLLNESGQPLDLSCKRPRP exceeds MapGapX=3; rejected.
#VAR 00:33:53 359 peptides: 358 singletons; 22 with possible variants.
#ERR 00:33:53 .peptAlign error: (peptAlign line 476) list index out of range
#ERR 00:33:53 Problem during setup.: (peptAlign line 476) list index out of range
#SLIM 00:33:53 Cloud 1 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Q..W.R|A.R.Q.IW|A.RIQ..W|IQ..W.R.Q|IQ.IWS|Q.IW.R.Q|IQSIW|G.I..[IV]..[KR]..E|I..[IV]..[KR]..E.G|IW.R..E.G|IQ..W.R..E|Q.IW.R..E|H.G..Q..W.R|IW.R.QE|AG.IQ..W|AG..Q.IW|HA.R.Q..W|R.Q.IW..L|IQ..W.RL|Q.IW.RL|[HK]..RI..[IV]..[KR]|R..SIW.R|IW.RLQ|HAG..Q..W|[HK].G.I..[IV].S|G.IQ..W..L|G..Q.IW..L|IW.RL.E|G.I.S.W.R|RI..[IV].S[KR]|A..IQ..W..L|A..I.S.W.R|R.Q.IWS|SIW.R.Q|IQS.W.R|IQ..WSR|P..A..IQ..W|IWSR.Q|Q.IWSR|QSIW.R|R.QSIW|A.R..SIW|[HK].G.I..[IV]..[KR]|Q.IW..LQ|Q.IW..L.E|H.G..Q..W..L|G.IQ..WS|G..Q.IWS|SIW.R..E|R.Q..W.R.Q|G.IQS.W|I..IW.R|G..QSIW|IWSR..E|P.H.G..Q..W|A..IQ..WS|G.I..[IV].S[KR]|A..IQS.W|AG.I.S.W|A.R.Q..W.R|Q.IWS..Q|R.Q..W.R..E|H.G..Q..WS|H.G..QS.W|G..Q..W.R.Q|Q..W.R.Q..G|G.I..IW|A..I..IW|SIW.RL|IWSRL|G..Q..W.R..E|AG..Q..W.R|Q..W.R..E.G|IQ.IW|Q..W.R.QE|H..RI..IW|RI..IW..L|I..IW..LQ|RI..IWS|RI.SIW|H..R..SIW|I..IW..L.E|I..IWS..Q|I..IWS.L|I.SIW..L|RI.S.W.R|IW..LQ..G|I.S.W.R.Q|H..R..S.W.R|IW..L.E.G|I.SIWS|IQ..W..L.E|I.S.W.R..E|IWS..Q..G|IW..LQE|RI..IW|R..SIW..L|I.S.W.RL|IWS..QE|W.R.QE.G|F.L..T.S..N|[ST]..D.PL..[ST]|C.{0,2}P.C.K|H..RIQ..W|H..RI.S.W|H.G.I.S.W|HA..I.S.W|[HK]..RI..[IV].S|RIQ..W..L|H..R.Q..W..L|RIQ..WS|RIQS.W|P.H..R.Q..W|A.RI.S.W|H..R.Q..WS|H..R.QS.W|K.K.K.[GS].[IV]|HA.R..S.W|RI.S.W..L|IQ..W..LQ|IQ..WS..Q|HRP..RT|H.P..RTQ|D.P[IL]DL|P[IL]DLS|P.DLS|P[ILMV][DE]L|QPL.[LV][ST]|D.PLDL|PLDLS|P[IL]D.[ST]|[ILM]DL[GS]|PLDL|P.[DE]L[ST]|P[ILMV].[LV][ST]|D.PL.L[ST]|QPL.L..K|P[IL].L[ST].[KR]|D.P.DL|P[IL]D.S|[DE].P[ILMV].L|[DE].P.[DE]L|QP[LV].[LV]|D..[IL]DL|[ILM]D[LV][ST]|P[ILMV].[LV][AS]|PLD.S|LDLS|D.P.DLS|D..LDLS|[ST]..DQP[LV]|Q..P[LMV]DL|P.DLS.{1,2}K|Q..P.DL.[LMV]|P.DL|Q..P.DL[ST]|P.DL..K.{0,2}R|P.DL[ST].K|P[IL]DL..[KR]|[DE].P.DL..[KR]|P.DL..[KR]|P.DL[ST]..[KR]|Q..P.DL|[IL]DLS.K|P.DL..K|P.DL..K[HR]|Q.L.{1,2}L..K|A..S..V[HK]..L|L..L.{1,2}N..K.K|A..S..V..[KR]L|Q.{0,2}P.DLS|A[IV].S..VK) SLiMMaker:
#FREQ 00:33:53 SLiMMaker Unable to make a SLiM with these settings and peptides
#ALN 00:33:53 Unaligned peptides: aligning with PeptCluster
#AAPROP 00:33:53 Reading AA Properties from aaprop.txt... ...I L V C A G M F Y W H K R E Q D N S T P ...Hydrophobic ...Polar ...Small ...Proline ...Positive ...Negative ...Charged ...Tiny ...Aliphatic ...Aromatic ...Done!
#GAPX 00:33:53 PeptLen: 6; MaxLen: 7; Termini: True => 4 x 1 gap variants.
#VAR 00:33:53 29 peptides: 28 singletons; 1 with possible variants.
#PDIS 00:33:53 id distances: 4 => 0 variants.
#VAR 00:33:53 29 peptides tidied: 29 singletons; 0 with variants.
#SLIM 00:33:53 Cloud 2 (IK.E|[IV]K.[DE]P|[IV]K.E..[DE]) SLiMMaker: [IV]K.E[EKP]{0,1}
#FREQ 00:33:53 SLiMMaker SLiM matches 27 of 29 sequences (93.1%).
#SLIM 00:33:53 Cloud 3 (G.{1,2}Y.C..C) SLiMMaker: G
#FREQ 00:33:53 SLiMMaker SLiM matches 4 of 4 sequences (100.0%).
#SLIM 00:33:53 Cloud 4 (D.{1,2}RC.{0,1}K.R) SLiMMaker: D....K.R
#FREQ 00:33:53 SLiMMaker SLiM matches 4 of 4 sequences (100.0%).
#RANK 00:33:53 Rank calculations complete
#CLOUD 00:33:54 Motif cloud data output to /srv/slimsuite/scratch/prod/slimfinder/15120800036/slimfinder.l5w2o2a3.CtBP-NoEFilter.cloud.txt for 4 clouds.
#FAS 00:33:54 29 Sequences output to /srv/slimsuite/scratch/prod/slimfinder/15120800036/slimfinder.l5w2o2a3.CtBP-NoEFilter.masked.fas.
#ERR 00:33:54 EVI1_HUMAN__Q03112 in alignment differs from input: Fudged QPLDLS by 2 aa!
#ERR 00:33:54 EVI1_HUMAN__Q03112 in alignment differs from input: Fudged QPLDLS by 2 aa!
#ERR 00:33:55 HDAC5_HUMAN__Q9UQL6 in alignment differs from input: Fudged QLLILRNK by 1 aa!
#ERR 00:33:55 HDAC5_HUMAN__Q9UQL6 in alignment differs from input: Fudged QLLILRNK by 1 aa!
#ERR 00:33:56 KLF3_HUMAN__P57682 in alignment differs from input: Fudged RTHTGEKP by 1 aa!
#ERR 00:33:56 KLF3_HUMAN__P57682 in alignment differs from input: Fudged RTHTGEKP by 1 aa!
#ERR 00:33:56 KLF3_HUMAN__P57682 in alignment differs from input: Fudged RTHTGEKP by 1 aa!
#ERR 00:33:56 KLF3_HUMAN__P57682 in alignment differs from input: Fudged RTHTGEKP by 1 aa!
#ERR 00:33:56 KLF3_HUMAN__P57682 in alignment differs from input: Fudged RTHTGEKP by 1 aa!
#ERR 00:33:56 KLF3_HUMAN__P57682 in alignment differs from input: Fudged RTHTGEKP by 1 aa!
#ERR 00:33:56 KLF3_HUMAN__P57682 in alignment differs from input: Fudged RTHTGEKP by 1 aa!
#ERR 00:33:56 KLF3_HUMAN__P57682 in alignment differs from input: Fudged RTHTGEKP by 1 aa!
#ERR 00:33:56 KLF3_HUMAN__P57682 in alignment differs from input: Fudged RTHTGEKP by 1 aa!
#ERR 00:33:56 KLF3_HUMAN__P57682 in alignment differs from input: Fudged RTHTGEKP by 1 aa!
#ERR 00:33:57 KLF3_HUMAN__P57682 in alignment differs from input: Fudged RTHTGEK by 1 aa!
#ERR 00:33:57 KLF3_HUMAN__P57682 in alignment differs from input: Fudged RTHTGEK by 1 aa!
#ERR 00:33:57 KLF8_HUMAN__O95600 in alignment differs from input: Fudged RIHTGEKP by 1 aa!
#ERR 00:33:57 KLF8_HUMAN__O95600 in alignment differs from input: Fudged RIHTGEKP by 1 aa!
#ERR 00:33:57 KLF8_HUMAN__O95600 in alignment differs from input: Fudged RIHTGEKP by 1 aa!
#ERR 00:33:57 KLF8_HUMAN__O95600 in alignment differs from input: Fudged RIHTGEKP by 1 aa!
#ERR 00:33:57 KLF8_HUMAN__O95600 in alignment differs from input: Fudged RIHTGEKP by 1 aa!
#ERR 00:33:57 KLF8_HUMAN__O95600 in alignment differs from input: Fudged RIHTGEKP by 1 aa!
#ERR 00:33:57 KLF8_HUMAN__O95600 in alignment differs from input: Fudged RIHTGEKP by 1 aa!
#ERR 00:33:57 KLF8_HUMAN__O95600 in alignment differs from input: Fudged RIHTGEKP by 1 aa!
#ERR 00:33:57 KLF8_HUMAN__O95600 in alignment differs from input: Fudged RIHTGEKP by 1 aa!
#ERR 00:33:57 KLF8_HUMAN__O95600 in alignment differs from input: Fudged RIHTGEKP by 1 aa!
#ERR 00:33:57 KLF8_HUMAN__O95600 in alignment differs from input: Fudged RIHTGEK by 1 aa!
#ERR 00:33:57 KLF8_HUMAN__O95600 in alignment differs from input: Fudged RIHTGEK by 1 aa!
#ERR 00:33:57 LCOR_HUMAN__Q96JN0 in alignment differs from input: Fudged KRGR by 1 aa!
#ERR 00:33:57 LCOR_HUMAN__Q96JN0 in alignment differs from input: Fudged KRGR by 1 aa!
#ERR 00:33:57 T7L1A_XENLA__P70062 in alignment differs from input: Fudged KRKR by 1 aa!
#ERR 00:33:57 T7L1A_XENLA__P70062 in alignment differs from input: Fudged KRKR by 1 aa!
#ERR 00:33:57 TGIF1_HUMAN__Q15583 in alignment differs from input: Fudged RPHRWELP by 1 aa!
#ERR 00:33:57 TGIF1_HUMAN__Q15583 in alignment differs from input: Fudged RPHRWELP by 1 aa!
#ERR 00:33:58 ZEB1_HUMAN__P37275 in alignment differs from input: Fudged HLKEHLRIH by 1 aa!
#ERR 00:33:58 ZEB1_HUMAN__P37275 in alignment differs from input: Fudged HLKEHLRIH by 1 aa!
#ERR 00:33:58 ZEB1_HUMAN__P37275 in alignment differs from input: Fudged HLKEHLRIH by 1 aa!
#ERR 00:33:58 ZEB1_HUMAN__P37275 in alignment differs from input: Fudged HLIEHMRLH by 1 aa!
#ERR 00:33:58 ZEB1_HUMAN__P37275 in alignment differs from input: Fudged HLKEHLRIH by 1 aa!
#ERR 00:33:58 ZEB1_HUMAN__P37275 in alignment differs from input: Fudged HLIEHMRLH by 1 aa!
#ERR 00:34:00 ZEB2_HUMAN__O60315 in alignment differs from input: Fudged HLKEHLRIH by 1 aa!
#ERR 00:34:00 ZEB2_HUMAN__O60315 in alignment differs from input: Fudged HLKEHLRIH by 1 aa!
#ERR 00:34:00 ZEB2_HUMAN__O60315 in alignment differs from input: Fudged HLKEHLRIH by 1 aa!
#ERR 00:34:00 ZEB2_HUMAN__O60315 in alignment differs from input: Fudged HLIEHSRLH by 1 aa!
#ERR 00:34:00 ZEB2_HUMAN__O60315 in alignment differs from input: Fudged HLKEHLRIH by 1 aa!
#ERR 00:34:00 ZEB2_HUMAN__O60315 in alignment differs from input: Fudged HLIEHSRLH by 1 aa!
#ERR 00:34:02 ZFH1_DROME__P28166 in alignment differs from input: Fudged HLTEHKRLH by 1 aa!
#ERR 00:34:02 ZFH1_DROME__P28166 in alignment differs from input: Fudged HLTEHKRLH by 1 aa!
#FAS 00:34:02 87 Sequences output to /srv/slimsuite/scratch/prod/slimfinder/15120800036/slimfinder.l5w2o2a3.CtBP-NoEFilter.mapping.fas.
#ALN 00:34:44 Constructing motif alignments: 1,000 motifs & 29 seqs.: 100.0%.
#FAS 00:34:45 80 Sequences output to /srv/slimsuite/scratch/prod/slimfinder/15120800036/slimfinder.l5w2o2a3.CtBP-NoEFilter.motifaln.fas.
#ALN 00:34:46 Constructing motif alignments: 1,000 motifs & 29 seqs.: 100.0%.
#FAS 00:34:47 80 Sequences output to /srv/slimsuite/scratch/prod/slimfinder/15120800036/slimfinder.l5w2o2a3.CtBP-NoEFilter.maskaln.fas.
#OCC 00:34:48 Occurrence data output for 5,628 motif occurrences.
#RES 00:34:48 SLiMFinder results output to /srv/slimsuite/scratch/prod/slimfinder/15120800036/slimfinder.csv and /srv/slimsuite/scratch/prod/slimfinder/15120800036/slimfinder.occ.csv.
#RES 00:34:48 Additional dataset results output to /srv/slimsuite/scratch/prod/slimfinder/15120800036/slimfinder.*
#END 00:34:48 SLiMFinder server run ended (Finished!): see log file for details.
#WARN 00:34:48 201 warning messages: check log for details.
#WARN 00:34:48 20 error messages! Check log for details.
#LOG 00:34:48 SLiMFinder V5.2.3 End: Wed Dec 9 00:02:11 2015
#JOBID 00:34:48 15120800036
#REST 00:34:48 URL for future retrieval: http://rest.slimsuite.unsw.edu.au/retrieve&jobid=15120800036&rest=format&password=None
#WARN	00:00:00	NOTE: cloudfix=F. Be wary of ambiguity over-predictions.
#WARN	00:26:14	Multiple motif offsets for [ST]..KP..C..C vs H.{1,2}K.H.R.H
#WARN	00:26:17	Multiple motif offsets for [KR]P..C..C.[KR] vs H.{1,2}K.H.R.H
#WARN	00:26:22	Multiple motif offsets for KP..C..C.{1,2}R vs H.{1,2}K.H.R.H
#WARN	00:26:24	Multiple motif offsets for [ST]..[KR]P..C..C vs H.{1,2}K.H.R.H
#WARN	00:26:27	Multiple motif offsets for PY.C..C.[KR] vs H.{1,2}K.H.R.H
#WARN	00:26:31	Multiple motif offsets for E.P[FY].C..C vs H.{1,2}K.H.R.H
#WARN	00:26:39	Multiple motif offsets for KP..C..C vs H.{1,2}K.H.R.H
#WARN	00:26:42	Multiple motif offsets for [KR]P[FY].C..C vs H.{1,2}K.H.R.H
#WARN	00:26:50	Multiple motif offsets for P[HY].C..C.[KR] vs H.{1,2}K.H.R.H
#WARN	00:26:56	Multiple motif offsets for P[FY].C..C vs H.{1,2}K.H.R.H
#WARN	00:27:03	Multiple motif offsets for [KR]P..C..C vs H.{1,2}K.H.R.H
#WARN	00:27:07	Multiple motif offsets for K.{0,1}P..C..C vs G.{0,1}K.Y.C..C
#WARN	00:27:09	Multiple motif offsets for PY.C..C vs H.{1,2}K.H.R.H
#WARN	00:27:13	Multiple motif offsets for P..C..CG..[FY] vs G.{0,1}K.Y.C..C
#WARN	00:27:19	Multiple motif offsets for KP..C..CG vs G.{0,1}K.Y.C..C
#WARN	00:27:21	Multiple motif offsets for P[FHY].C..C vs H.{1,2}K.H.R.H
#WARN	00:27:36	Multiple motif offsets for S..KP..C..C vs H.{1,2}K.H.R.H
#WARN	00:27:40	Multiple motif offsets for P..C..CG[KR] vs G.{0,1}K.Y.C..C
#WARN	00:27:41	Multiple motif offsets for [KR]P..C..CG vs G.{0,1}K.Y.C..C
#WARN	00:27:48	Multiple motif offsets for PY.C..C.K vs H.{1,2}K.H.R.H
#WARN	00:27:53	Multiple motif offsets for G..PY.C..C vs H.{1,2}K.H.R.H
#WARN	00:27:54	Multiple motif offsets for E[KR]P..C..C vs H.{1,2}K.H.R.H
#WARN	00:27:59	Multiple motif offsets for G.{0,1}K.Y.C..C vs P[FY].C..CG
#WARN	00:27:59	Multiple motif offsets for G.{0,1}K.Y.C..C vs P..C..CG
#WARN	00:27:59	Multiple motif offsets for G.{0,1}K.Y.C..C vs P..C..CG.{0,1}R
#WARN	00:27:59	Multiple motif offsets for G.{0,1}K.Y.C..C vs PY.C..CG
#WARN	00:28:05	Multiple motif offsets for PY.C..C.{1,2}R vs H.{1,2}K.H.R.H
#WARN	00:28:13	Multiple motif offsets for PY.C..C.{0,1}K vs H.{1,2}K.H.R.H
#WARN	00:28:23	Multiple motif offsets for H.{0,1}R.{1,2}H.GE vs R.{1,2}H.GEK
#WARN	00:28:24	Multiple motif offsets for H.{0,1}R.{1,2}H.GE vs R.{1,2}H..EKP
#WARN	00:28:24	Multiple motif offsets for H.{0,1}R.{1,2}H.GE vs R.{1,2}HT.E.P
#WARN	00:28:31	Multiple motif offsets for G..P[HY].C..C vs H.{1,2}K.H.R.H
#WARN	00:28:35	Multiple motif offsets for L..H.{0,1}R.{1,2}H.G vs H[ILM][KR].H
#WARN	00:28:35	Multiple motif offsets for L..H.{0,1}R.{1,2}H.G vs R.{1,2}HT.E.P
#WARN	00:28:38	Multiple motif offsets for H.{0,1}R.{1,2}H.G..P vs R.{1,2}HT.E.P
#WARN	00:28:40	Multiple motif offsets for R.{1,2}H.GE.P vs H.{0,1}R.{1,2}H.G.K
#WARN	00:28:40	Multiple motif offsets for R.{1,2}H.GE.P vs R.{1,2}H.GEK
#WARN	00:28:40	Multiple motif offsets for R.{1,2}H.GE.P vs R.{1,2}H.G.KP
#WARN	00:28:40	Multiple motif offsets for R.{1,2}H.GE.P vs R.{1,2}H..EKP
#WARN	00:28:41	Multiple motif offsets for R.{1,2}H.GE.P vs R.{1,2}HT.E.P
#WARN	00:29:19	Multiple motif offsets for KA[FH][KR]..H vs K..H.{0,1}L..H.R
#WARN	00:29:24	Multiple motif offsets for H.{0,1}R.{1,2}H.G.K vs R.{1,2}H..EKP
#WARN	00:29:25	Multiple motif offsets for H.{0,1}R.{1,2}H.G.K vs R.{1,2}HT.E.P
#WARN	00:29:25	Multiple motif offsets for H.{0,1}R.{1,2}H.G.K vs R.{1,2}H..E.P
#WARN	00:29:28	Multiple motif offsets for YEC.NC vs H.{1,2}K.H.R.H
#WARN	00:29:33	Multiple motif offsets for R.{1,2}H.GEK vs R.{1,2}H.G.KP
#WARN	00:29:33	Multiple motif offsets for R.{1,2}H.GEK vs R.{1,2}H..EKP
#WARN	00:29:34	Multiple motif offsets for R.{1,2}H.GEK vs R.{1,2}HT.E.P
#WARN	00:29:34	Multiple motif offsets for R.{1,2}H.GEK vs R.{1,2}H..E.P
#WARN	00:29:44	Multiple motif offsets for R.{1,2}H.G.KP vs H.{0,1}R.{1,2}H..EK
#WARN	00:29:44	Multiple motif offsets for R.{1,2}H.G.KP vs R.{1,2}H..EKP
#WARN	00:29:44	Multiple motif offsets for R.{1,2}H.G.KP vs R.{1,2}HT.E.P
#WARN	00:29:45	Multiple motif offsets for R.{1,2}H.G.KP vs R.{1,2}H..E.P
#WARN	00:29:45	Multiple motif offsets for KPY.C..C vs H.{1,2}K.H.R.H
#WARN	00:29:49	Multiple motif offsets for K.YEC..C vs H.{1,2}K.H.R.H
#WARN	00:29:50	Multiple motif offsets for YEC..C.K vs H.{1,2}K.H.R.H
#WARN	00:29:53	Multiple motif offsets for H.{0,1}R.{1,2}H..EK vs R.{1,2}H..EKP
#WARN	00:29:54	Multiple motif offsets for H.{0,1}R.{1,2}H..EK vs R.{1,2}HT.E.P
#WARN	00:30:02	Multiple motif offsets for H.{1,2}K.H.R.H vs E.PY.C..C
#WARN	00:30:02	Multiple motif offsets for H.{1,2}K.H.R.H vs P..C.NC..R
#WARN	00:30:06	Multiple motif offsets for K.[FH][KR][HR].H vs [HK][HR][HKR].[HY]..[DE]
#WARN	00:30:06	Multiple motif offsets for K.[FH][KR][HR].H vs K..H.{0,1}L..H.R
#WARN	00:30:11	Multiple motif offsets for R.{1,2}H..EKP vs R.{1,2}HT.E.P
#WARN	00:30:40	Multiple motif offsets for A[FH][KR][HR].H vs [HK][HR][HKR].[HY]..[DE]
#WARN	00:30:45	Multiple motif offsets for H[FLM]..H[ST]..K vs H.{0,1}L..H.R.H
#WARN	00:30:47	Multiple motif offsets for L..H.R..[ST]..K vs H[ILM][KR].H
#WARN	00:30:49	Multiple motif offsets for [FLM][KR].[HR][ST]..K vs [KR].[HR].[KR].[HK]..E
#WARN	00:30:49	Multiple motif offsets for [FLM][KR].[HR][ST]..K vs L..[HR].R[IL][HK]
#WARN	00:30:49	Multiple motif offsets for [FLM][KR].[HR][ST]..K vs LK.[HR].R.[HK]
#WARN	00:30:49	Multiple motif offsets for [FLM][KR].[HR][ST]..K vs K.[HR].R[IL][HK]
#WARN	00:30:49	Multiple motif offsets for [FLM][KR].[HR][ST]..K vs H.{0,1}L..H.R.H
#WARN	00:30:49	Multiple motif offsets for [FLM][KR].[HR][ST]..K vs K.[HR].R.[HKR]
#WARN	00:30:52	Multiple motif offsets for H[FLM]R..[ST]..K vs H.{0,1}L..H.R.H
#WARN	00:30:52	Multiple motif offsets for [FLM]R.H[ST]..K vs H.{0,1}L..H.R.H
#WARN	00:30:53	Multiple motif offsets for H.GEKP vs K.{1,2}HL..H.R
#WARN	00:30:53	Multiple motif offsets for H.GEKP vs K.{1,2}HL..H.{0,1}R
#WARN	00:30:54	Multiple motif offsets for H[LM]..HS..K vs H.{0,1}L..H.R.H
#WARN	00:30:58	Multiple motif offsets for H..IHS..K vs H.{0,1}L..H.R.H
#WARN	00:30:58	Multiple motif offsets for K.H.R..[ST]..K vs H.{0,1}L..H.R.H
#WARN	00:30:58	Multiple motif offsets for K.H.R..[ST]..K vs H[ILM][KR].H
#WARN	00:31:00	Multiple motif offsets for [LM][KR].[HR]S..K vs [KR].[HR].[KR].[HK]..E
#WARN	00:31:00	Multiple motif offsets for [LM][KR].[HR]S..K vs L..[HR].R[IL][HK]
#WARN	00:31:00	Multiple motif offsets for [LM][KR].[HR]S..K vs LK.[HR].R.[HK]
#WARN	00:31:00	Multiple motif offsets for [LM][KR].[HR]S..K vs K.[HR].R[IL][HK]
#WARN	00:31:00	Multiple motif offsets for [LM][KR].[HR]S..K vs H.{0,1}L..H.R.H
#WARN	00:31:00	Multiple motif offsets for [LM][KR].[HR]S..K vs K.[HR].R.[HKR]
#WARN	00:31:01	Multiple motif offsets for H.RI.S..K vs H.{0,1}L..H.R.H
#WARN	00:31:02	Multiple motif offsets for RIHS..K vs H.{0,1}L..H.R.H
#WARN	00:31:03	Multiple motif offsets for H[ST]GEK vs K.{1,2}HL..H.R
#WARN	00:31:03	Multiple motif offsets for H[ST]GEK vs K.{1,2}HL..H.{0,1}R
#WARN	00:31:05	Multiple motif offsets for KA.[KR][HR].H vs [HK][HR][HKR].[HY]..[DE]
#WARN	00:31:05	Multiple motif offsets for KA.[KR][HR].H vs K..H.{0,1}L..H.R
#WARN	00:31:09	Multiple motif offsets for L..H.R.H..E vs H[ILM][KR].H
#WARN	00:31:13	Multiple motif offsets for [HR].[KR].[HK].[AG]E vs L..[HR].R[IL][HK]
#WARN	00:31:13	Multiple motif offsets for [HR].[KR].[HK].[AG]E vs LK.[HR].R.[HK]
#WARN	00:31:13	Multiple motif offsets for [HR].[KR].[HK].[AG]E vs K.[HR].R[IL][HK]
#WARN	00:31:13	Multiple motif offsets for [HR].[KR].[HK].[AG]E vs K.[HR].R.[HKR]
#WARN	00:31:14	Multiple motif offsets for [LV]..[HR].[KR].[HK]..E vs L..[HR].R[IL][HK]
#WARN	00:31:14	Multiple motif offsets for [LV]..[HR].[KR].[HK]..E vs LK.[HR].R.[HK]
#WARN	00:31:14	Multiple motif offsets for [LV]..[HR].[KR].[HK]..E vs K.[HR].R[IL][HK]
#WARN	00:31:14	Multiple motif offsets for [LV]..[HR].[KR].[HK]..E vs K.[HR].R.[HKR]
#WARN	00:31:14	Multiple motif offsets for [LV]..[HR].[KR].[HK]..E vs H[ILM][KR].H
#WARN	00:31:16	Multiple motif offsets for R.H.GEK vs K.{1,2}HL..H.R
#WARN	00:31:16	Multiple motif offsets for R.H.GEK vs K.{1,2}HL..H.{0,1}R
#WARN	00:31:17	Multiple motif offsets for [HR].[KR].[HK]..E[KR] vs L..[HR].R[IL][HK]
#WARN	00:31:17	Multiple motif offsets for [HR].[KR].[HK]..E[KR] vs LK.[HR].R.[HK]
#WARN	00:31:17	Multiple motif offsets for [HR].[KR].[HK]..E[KR] vs K.[HR].R[IL][HK]
#WARN	00:31:17	Multiple motif offsets for [HR].[KR].[HK]..E[KR] vs K.[HR].R.[HKR]
#WARN	00:31:19	Multiple motif offsets for [KR].[HK].[AG]E[KR] vs K.{1,2}HL..H.R
#WARN	00:31:19	Multiple motif offsets for [KR].[HK].[AG]E[KR] vs K.{1,2}HL..H.{0,1}R
#WARN	00:31:20	Multiple motif offsets for K.H.R.H..E vs H[ILM][KR].H
#WARN	00:31:24	Multiple motif offsets for [KR].[HR].[KR].[HK]..E vs L..[HR].R[IL][HK]
#WARN	00:31:24	Multiple motif offsets for [KR].[HR].[KR].[HK]..E vs LK.[HR].R.[HK]
#WARN	00:31:24	Multiple motif offsets for [KR].[HR].[KR].[HK]..E vs K.[HR].R[IL][HK]
#WARN	00:31:24	Multiple motif offsets for [KR].[HR].[KR].[HK]..E vs K.[HR].R.[HKR]
#WARN	00:31:24	Multiple motif offsets for [KR].[HR].[KR].[HK]..E vs H[ILM][KR].H
#WARN	00:31:24	Multiple motif offsets for [KR].[HR].[KR].[HK]..E vs LK.[HR]..[IL][HK]
#WARN	00:31:27	Multiple motif offsets for L..H.R.H[ST] vs H[ILM][KR].H
#WARN	00:31:27	Multiple motif offsets for T.H.R.H[ST] vs H.{0,1}L..H.R.H
#WARN	00:31:27	Multiple motif offsets for H[FLM]R.H[ST] vs H.{0,1}L..H.R.H
#WARN	00:31:30	Multiple motif offsets for K.H.R.H[ST] vs H.{0,1}L..H.R.H
#WARN	00:31:30	Multiple motif offsets for K.H.R.H[ST] vs H[ILM][KR].H
#WARN	00:31:30	Multiple motif offsets for H[LM]R.HS vs H.{0,1}L..H.R.H
#WARN	00:31:31	Multiple motif offsets for H.RIHS vs H.{0,1}L..H.R.H
#WARN	00:31:31	Multiple motif offsets for EH..IHS vs H.{0,1}L..H.R.H
#WARN	00:31:32	Multiple motif offsets for [HR].[KR].[HK].[AG].[KR] vs L..[HR].R[IL][HK]
#WARN	00:31:32	Multiple motif offsets for [HR].[KR].[HK].[AG].[KR] vs LK.[HR].R.[HK]
#WARN	00:31:32	Multiple motif offsets for [HR].[KR].[HK].[AG].[KR] vs K.[HR].R[IL][HK]
#WARN	00:31:32	Multiple motif offsets for [HR].[KR].[HK].[AG].[KR] vs K.[HR].R.[HKR]
#WARN	00:31:33	Multiple motif offsets for E..RIHS vs H.{0,1}L..H.R.H
#WARN	00:31:34	Multiple motif offsets for L..H.R..[ST]G vs H[ILM][KR].H
#WARN	00:31:35	Multiple motif offsets for L..H.R..[ST].E vs H[ILM][KR].H
#WARN	00:31:35	Multiple motif offsets for HL..H.R..[ST] vs H.{0,1}L..H.R.H
#WARN	00:31:35	Multiple motif offsets for HL..H.R..[ST] vs H[ILM][KR].H
#WARN	00:31:36	Multiple motif offsets for EH.RI.S vs H.{0,1}L..H.R.H
#WARN	00:31:36	Multiple motif offsets for [HR][IL]..GE[HK] vs K.{1,2}HL..H.R
#WARN	00:31:36	Multiple motif offsets for [HR][IL]..GE[HK] vs K.{1,2}HL..H.{0,1}R
#WARN	00:31:38	Multiple motif offsets for HL..H.{0,1}R.{1,2}H vs H[ILM][KR].H
#WARN	00:31:41	Multiple motif offsets for L..H.[KR].H vs H[ILM][KR].H
#WARN	00:31:46	Multiple motif offsets for L..H.R.H.G vs H[ILM][KR].H
#WARN	00:31:46	Multiple motif offsets for L..[HR].R[IL][HK] vs H[ILM][KR].H
#WARN	00:31:47	Multiple motif offsets for HL..H.R.H vs H[ILM][KR].H
#WARN	00:31:47	Multiple motif offsets for HL..H.R.H vs H..[IL][HY]
#WARN	00:31:47	Multiple motif offsets for HL..H.R.H vs H..[ILM][HY]
#WARN	00:31:47	Multiple motif offsets for LK.[HR].R.[HK] vs H[ILM][KR].H
#WARN	00:31:48	Multiple motif offsets for K.[HR].R[IL][HK] vs H.{0,1}L..H.R.H
#WARN	00:31:48	Multiple motif offsets for K.[HR].R[IL][HK] vs H[ILM][KR].H
#WARN	00:31:48	Multiple motif offsets for L..H.R.H vs H[ILM][KR].H
#WARN	00:31:49	Multiple motif offsets for H.{0,1}L..H.R.H vs K.H.RIH
#WARN	00:31:49	Multiple motif offsets for H.{0,1}L..H.R.H vs H.K.H.R.H
#WARN	00:31:49	Multiple motif offsets for H.{0,1}L..H.R.H vs H[ILM][KR].H
#WARN	00:31:49	Multiple motif offsets for H.{0,1}L..H.R.H vs HLK.H.R
#WARN	00:31:49	Multiple motif offsets for H.{0,1}L..H.R.H vs [HR]H[FIL][KR].H
#WARN	00:31:49	Multiple motif offsets for H.{0,1}L..H.R.H vs LK.[HR]..[IL][HK]
#WARN	00:31:49	Multiple motif offsets for H.{0,1}L..H.R.H vs LK.H..IH
#WARN	00:31:49	Multiple motif offsets for H.{0,1}L..H.R.H vs H[HK]L..H..L
#WARN	00:31:49	Multiple motif offsets for H.{0,1}L..H.R.H vs H[HK]L..H..[IL]
#WARN	00:31:49	Multiple motif offsets for H.{0,1}L..H.R.H vs [HR]H.[KR].H
#WARN	00:31:49	Multiple motif offsets for H.{0,1}L..H.R.H vs K.H..IH
#WARN	00:31:49	Multiple motif offsets for H.{0,1}L..H.R.H vs H[HK].[KR].H..[IL]
#WARN	00:31:49	Multiple motif offsets for K.H.RIH vs H[ILM][KR].H
#WARN	00:31:50	Multiple motif offsets for L..H.R[IL]H vs H[ILM][KR].H
#WARN	00:31:51	Multiple motif offsets for L..H.RIH vs H[ILM][KR].H
#WARN	00:31:51	Multiple motif offsets for H.K.H.R.H vs H[ILM][KR].H
#WARN	00:31:51	Multiple motif offsets for K.H.R.H.G vs H[ILM][KR].H
#WARN	00:31:51	Multiple motif offsets for K.[HR].R.[HKR] vs H[ILM][KR].H
#WARN	00:31:52	Multiple motif offsets for H[ILM][KR].H vs LK.H.R.H
#WARN	00:31:52	Multiple motif offsets for H[ILM][KR].H vs L.EH.R.H
#WARN	00:31:52	Multiple motif offsets for H[ILM][KR].H vs [HK]..HL..H.R
#WARN	00:31:52	Multiple motif offsets for H[ILM][KR].H vs L..H.{0,1}R.{1,2}H..E
#WARN	00:31:52	Multiple motif offsets for H[ILM][KR].H vs K..H.{0,1}L..H.R
#WARN	00:31:52	Multiple motif offsets for H[ILM][KR].H vs HLK.H.R
#WARN	00:31:52	Multiple motif offsets for H[ILM][KR].H vs L..H..[ILM]H
#WARN	00:31:52	Multiple motif offsets for H[ILM][KR].H vs LK.[HR]..[IL][HK]
#WARN	00:31:52	Multiple motif offsets for H[ILM][KR].H vs LK.H..IH
#WARN	00:31:52	Multiple motif offsets for H[ILM][KR].H vs L..H..IH
#WARN	00:31:52	Multiple motif offsets for H[ILM][KR].H vs K.H..IH
#WARN	00:31:58	Multiple motif offsets for [HK]..HL..H.R vs [HK][HR][HKR].[HY]..[DE]
#WARN	00:31:58	Multiple motif offsets for [HK]..HL..H.R vs K..H.{0,1}L..H.R
#WARN	00:33:53	Peptide WEGCTWKFARSDELTRHFRKHTGIKPFQCPDCDRSFSRSDHLALHRKRHMLV exceeds MapGapX=3; rejected.
#WARN	00:33:53	Peptide WDGCSWKFARSDELTRHFRKHTGIKPFRCTDCNRSFSRSDHLSLHRRRHDTM exceeds MapGapX=3; rejected.
#WARN	00:33:53	Peptide TWKFARSDELTRHFRKHTGIKPFQCPDCDRSFSRSDHLALHRKRHMLV exceeds MapGapX=3; rejected.
#WARN	00:33:53	Peptide SWKFARSDELTRHFRKHTGIKPFRCTDCNRSFSRSDHLSLHRRRHDTM exceeds MapGapX=3; rejected.
#WARN	00:33:53	Peptide GGRRQAVECIEDLLNESGQPLDLSCKRPRP exceeds MapGapX=3; rejected.
#WARN	00:33:53	Peptide YEPMDIKPSVIQRVPMEQQPLSLVIKKQIKEEEQPWRPW exceeds MapGapX=3; rejected.
#WARN	00:33:53	Peptide EGCTWKFARSDELTRHFRKHTGIKPFQCPDCDRSFSRSDHLALHRKRHMLV exceeds MapGapX=3; rejected.
#WARN	00:33:53	Peptide DGCSWKFARSDELTRHFRKHTGIKPFRCTDCNRSFSRSDHLSLHRRRHDTM exceeds MapGapX=3; rejected.
#WARN	00:33:53	Peptide SGEKPFQCSKCLKRFSHSGSYSQHMNHRYSYCKPYRE exceeds MapGapX=3; rejected.
#WARN	00:33:53	Peptide KPFQCSKCLKRFSHSGSYSQHMNHRYSYCKPYRE exceeds MapGapX=3; rejected.
#WARN	00:33:53	Peptide CPDCDRSFSRSDHLALHRKRHMLV exceeds MapGapX=3; rejected.
#WARN	00:33:53	Peptide CTDCNRSFSRSDHLSLHRRRHDTM exceeds MapGapX=3; rejected.
#WARN	00:33:53	Peptide WKFARSDELTRHFRKHTGIKPFQCPDCDRSFSRSDHLALHRKRHMLV exceeds MapGapX=3; rejected.
#WARN	00:33:53	Peptide WKFARSDELTRHFRKHTGIKPFRCTDCNRSFSRSDHLSLHRRRHDTM exceeds MapGapX=3; rejected.
#WARN	00:33:53	Peptide TDCNRSFSRSDHLSLHRRRHDTM exceeds MapGapX=3; rejected.
#WARN	00:33:53	Peptide TLLNGHMPVPIPSLDRAASPVLLSSNSQKS exceeds MapGapX=3; rejected.
#WARN	00:33:53	Peptide FECNMCGYHSQDRYEFSSHITRGEHRFHMS exceeds MapGapX=3; rejected.
#WARN	00:33:53	Peptide FECNICGYHSQDRYEFSSHIVRGEHKVG exceeds MapGapX=3; rejected.
#WARN	00:33:53	Peptide KTEGLMKDDRAESQASSLGQKVGESSEQVSEEKTNEA exceeds MapGapX=3; rejected.
#WARN	00:33:53	Peptide TCMERGYIKEDLDPCPRPKRRQPYNAIFSPKGKEQKT exceeds MapGapX=3; rejected.
#WARN	00:33:53	Peptide ECIEDLLNESGQPLDLSCKRPRP exceeds MapGapX=3; rejected.
#ERR	00:33:53	.peptAlign error:  (peptAlign line 476) list index out of range  
#ERR	00:33:53	Problem during  setup.:  (peptAlign line 476) list index out of range  
#ERR	00:33:54	EVI1_HUMAN__Q03112 in alignment differs from input: Fudged QPLDLS by 2 aa!
#ERR	00:33:55	HDAC5_HUMAN__Q9UQL6 in alignment differs from input: Fudged QLLILRNK by 1 aa!
#ERR	00:33:56	KLF3_HUMAN__P57682 in alignment differs from input: Fudged RTHTGEKP by 1 aa!
#ERR	00:33:57	KLF3_HUMAN__P57682 in alignment differs from input: Fudged RTHTGEK by 1 aa!
#ERR	00:33:57	KLF8_HUMAN__O95600 in alignment differs from input: Fudged RIHTGEKP by 1 aa!
#ERR	00:33:57	KLF8_HUMAN__O95600 in alignment differs from input: Fudged RIHTGEK by 1 aa!
#ERR	00:33:57	LCOR_HUMAN__Q96JN0 in alignment differs from input: Fudged KRGR by 1 aa!
#ERR	00:33:57	T7L1A_XENLA__P70062 in alignment differs from input: Fudged KRKR by 1 aa!
#ERR	00:33:57	TGIF1_HUMAN__Q15583 in alignment differs from input: Fudged RPHRWELP by 1 aa!
#ERR	00:33:58	ZEB1_HUMAN__P37275 in alignment differs from input: Fudged HLKEHLRIH by 1 aa!
#ERR	00:33:58	ZEB1_HUMAN__P37275 in alignment differs from input: Fudged HLIEHMRLH by 1 aa!
#ERR	00:33:58	ZEB1_HUMAN__P37275 in alignment differs from input: Fudged HLKEHLRIH by 1 aa!
#ERR	00:33:58	ZEB1_HUMAN__P37275 in alignment differs from input: Fudged HLIEHMRLH by 1 aa!
#ERR	00:34:00	ZEB2_HUMAN__O60315 in alignment differs from input: Fudged HLKEHLRIH by 1 aa!
#ERR	00:34:00	ZEB2_HUMAN__O60315 in alignment differs from input: Fudged HLIEHSRLH by 1 aa!
#ERR	00:34:00	ZEB2_HUMAN__O60315 in alignment differs from input: Fudged HLKEHLRIH by 1 aa!
#ERR	00:34:00	ZEB2_HUMAN__O60315 in alignment differs from input: Fudged HLIEHSRLH by 1 aa!
#ERR	00:34:02	ZFH1_DROME__P28166 in alignment differs from input: Fudged HLTEHKRLH by 1 aa!

© 2015 RJ Edwards. Contact: richard.edwards@unsw.edu.au.