|
SLiMSuite REST Server |
| |
SLiMSuite SLiMFinder Server
# Output for SLiMFinder V5.2.3: Wed Dec 9 01:11:19 2015
# 2 warnings; 0 errors: see log output (below) for details.
# JobID: 15120900013
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: python PATH/slimparser.py restin=JOBID restout=T [password=X] [restbase=X]
JobID 15120900013 (slimfinder) Finished.
IP:122.150.74.70
No queue.
slimfinder&uniprotid=Q9H6U6,Q96MA1,O15409,Q14526,P09067,Q13422,O94818,Q96MY1,P48552,Q9NQ66,Q99708,Q15583,Q63HK5&dismask=T&consmask=T&featuremask=T&ambiguity=T&slimlen=5&maxwild=2
Run Started: 2015-12-09 01:11:19; PID=39543
Run finished: 2015-12-09 01:11:41
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} ]
Click here and save the page to download this output.
Dataset |
RunID |
Masking |
Build |
Chance |
RunTime |
SeqNum |
UPNum |
AANum |
MotNum |
Rank |
Sig |
Pattern |
IC |
Occ |
Support |
UP |
ExpUP |
Prob |
Cloud |
CloudSeq |
CloudUP |
slimfinder |
15120900013 |
FreqConsDisComp-5-8FT |
l5w2o2a3 |
Sig |
00:00:17 |
13 |
8 |
4021 |
2 |
1 |
0.001 |
P.DLS |
4.00 |
6 |
6 |
5 |
0.043 |
2.37e-10 |
1 |
9 |
7 |
slimfinder |
15120900013 |
FreqConsDisComp-5-8FT |
l5w2o2a3 |
Sig |
00:00:17 |
13 |
8 |
4021 |
2 |
2 |
0.047 |
DLS |
3.00 |
12 |
9 |
7 |
0.79 |
6.63e-07 |
1 |
9 |
7 |
Click here and save the page to download this output.
Dataset |
RunID |
Rank |
Pattern |
Sig |
Seq |
Start_Pos |
End_Pos |
Prot_Len |
Match |
Variant |
MisMatch |
Desc |
PepSeq |
PepDesign |
slimfinder |
15120900013 |
1 |
P.DLS |
0.001 |
IKZF1_HUMAN__Q13422 |
34 |
38 |
519 |
PEDLS |
P.DLS |
0 |
RecName: Full=DNA-binding protein Ikaros; AltName: Full=Ikaros family zinc finger protein 1; AltName: Full=Lymphoid transcription factor LyF-1; |
PEDLS |
OK |
slimfinder |
15120900013 |
1 |
P.DLS |
0.001 |
TGIF1_HUMAN__Q15583 |
153 |
157 |
401 |
PLDLS |
P.DLS |
0 |
RecName: Full=Homeobox protein TGIF1; AltName: Full=5'-TG-3'-interacting factor 1; |
PLDLS |
OK |
slimfinder |
15120900013 |
1 |
P.DLS |
0.001 |
NOL4L_HUMAN__Q96MY1 |
365 |
369 |
436 |
PTDLS |
P.DLS |
0 |
RecName: Full=Nucleolar protein 4-like; |
PTDLS |
OK |
slimfinder |
15120900013 |
1 |
P.DLS |
0.001 |
NRIP1_HUMAN__P48552 |
440 |
444 |
1158 |
PIDLS |
P.DLS |
0 |
RecName: Full=Nuclear receptor-interacting protein 1; AltName: Full=Nuclear factor RIP140; AltName: Full=Receptor-interacting protein 140; |
PIDLS |
OK |
slimfinder |
15120900013 |
1 |
P.DLS |
0.001 |
NOL4_HUMAN__O94818 |
576 |
580 |
638 |
PTDLS |
P.DLS |
0 |
RecName: Full=Nucleolar protein 4; AltName: Full=Nucleolar-localized protein; |
PTDLS |
OK |
slimfinder |
15120900013 |
1 |
P.DLS |
0.001 |
COM1_HUMAN__Q99708 |
490 |
494 |
897 |
PLDLS |
P.DLS |
0 |
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; |
PLDLS |
OK |
slimfinder |
15120900013 |
2 |
DLS |
0.047 |
NRIP1_HUMAN__P48552 |
442 |
444 |
1158 |
DLS |
DLS |
0 |
RecName: Full=Nuclear receptor-interacting protein 1; AltName: Full=Nuclear factor RIP140; AltName: Full=Receptor-interacting protein 140; |
DLS |
OK |
slimfinder |
15120900013 |
2 |
DLS |
0.047 |
NRIP1_HUMAN__P48552 |
948 |
950 |
1158 |
DLS |
DLS |
0 |
RecName: Full=Nuclear receptor-interacting protein 1; AltName: Full=Nuclear factor RIP140; AltName: Full=Receptor-interacting protein 140; |
DLS |
OK |
slimfinder |
15120900013 |
2 |
DLS |
0.047 |
HIC1_HUMAN__Q14526 |
243 |
245 |
733 |
DLS |
DLS |
0 |
RecName: Full=Hypermethylated in cancer 1 protein; Short=Hic-1; AltName: Full=Zinc finger and BTB domain-containing protein 29; |
DLS |
OK |
slimfinder |
15120900013 |
2 |
DLS |
0.047 |
NOL4L_HUMAN__Q96MY1 |
367 |
369 |
436 |
DLS |
DLS |
0 |
RecName: Full=Nucleolar protein 4-like; |
DLS |
OK |
slimfinder |
15120900013 |
2 |
DLS |
0.047 |
TGIF1_HUMAN__Q15583 |
155 |
157 |
401 |
DLS |
DLS |
0 |
RecName: Full=Homeobox protein TGIF1; AltName: Full=5'-TG-3'-interacting factor 1; |
DLS |
OK |
slimfinder |
15120900013 |
2 |
DLS |
0.047 |
TSH3_HUMAN__Q63HK5 |
926 |
928 |
1081 |
DLS |
DLS |
0 |
RecName: Full=Teashirt homolog 3; AltName: Full=Zinc finger protein 537; |
DLS |
OK |
slimfinder |
15120900013 |
2 |
DLS |
0.047 |
HXB5_HUMAN__P09067 |
53 |
55 |
269 |
DLS |
DLS |
0 |
RecName: Full=Homeobox protein Hox-B5; AltName: Full=Homeobox protein HHO.C10; AltName: Full=Homeobox protein Hox-2A; AltName: Full=Homeobox protein Hu-1; |
DLS |
OK |
slimfinder |
15120900013 |
2 |
DLS |
0.047 |
IKZF1_HUMAN__Q13422 |
36 |
38 |
519 |
DLS |
DLS |
0 |
RecName: Full=DNA-binding protein Ikaros; AltName: Full=Ikaros family zinc finger protein 1; AltName: Full=Lymphoid transcription factor LyF-1; |
DLS |
OK |
slimfinder |
15120900013 |
2 |
DLS |
0.047 |
NOL4_HUMAN__O94818 |
375 |
377 |
638 |
DLS |
DLS |
0 |
RecName: Full=Nucleolar protein 4; AltName: Full=Nucleolar-localized protein; |
DLS |
OK |
slimfinder |
15120900013 |
2 |
DLS |
0.047 |
NOL4_HUMAN__O94818 |
578 |
580 |
638 |
DLS |
DLS |
0 |
RecName: Full=Nucleolar protein 4; AltName: Full=Nucleolar-localized protein; |
DLS |
OK |
slimfinder |
15120900013 |
2 |
DLS |
0.047 |
COM1_HUMAN__Q99708 |
492 |
494 |
897 |
DLS |
DLS |
0 |
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; |
DLS |
OK |
slimfinder |
15120900013 |
2 |
DLS |
0.047 |
COM1_HUMAN__Q99708 |
662 |
664 |
897 |
DLS |
DLS |
0 |
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; |
DLS |
OK |
Click here and save the page to download this output.
#slimfinder# 13 Seq; 8 UPC; 12.111 MST; blaste=1.00e-04, blastcf=F, blastf=T
UP N MST Seqs
1 1 1.000 BCAS3_HUMAN__Q9H6U6
2 3 2.916 COM1_HUMAN__Q99708 FOXP2_HUMAN__O15409 PLCB1_HUMAN__Q9NQ66
3 3 2.757 DMRTB_HUMAN__Q96MA1 IKZF1_HUMAN__Q13422 HIC1_HUMAN__Q14526
4 1 1.000 HXB5_HUMAN__P09067
5 2 1.438 NOL4L_HUMAN__Q96MY1 NOL4_HUMAN__O94818
6 1 1.000 NRIP1_HUMAN__P48552
7 1 1.000 TGIF1_HUMAN__Q15583
8 1 1.000 TSH3_HUMAN__Q63HK5
Click here and save the page to download this output.
slimfinder: 13 Seq, 8 UPC, 2 Sig SLiMs in 1 Clouds
Cloud 1 (2 SLiMs): P.DLS DLS (p = 0.001)
7 UPC 9 Seq: COM1_HUMAN__Q99708 HIC1_HUMAN__Q14526 HXB5_HUMAN__P09067 IKZF1_HUMAN__Q13422 NOL4L_HUMAN__Q96MY1 NOL4_HUMAN__O94818 NRIP1_HUMAN__P48552 TGIF1_HUMAN__Q15583 TSH3_HUMAN__Q63HK5
SLiMMaker Consensus: [GP].DLS
- SLiM matches 9 of 12 sequences (75.0%).
PLDLS
GADLS
GLDLS
GMDLS
PEDLS
PTDLS
AEDLS
PTDLS
PIDLS
VRDLS
PLDLS
MSDLS
#Cloud Seq coverage/overlap
Cloud Dataset 1
1:P.DLS 0.692 1.000
#Cloud UPC coverage/overlap
Cloud Dataset 1
1:P.DLS 0.875 1.000
Click here and save the page to download this output.
>BCAS3_HUMAN__Q9H6U6 RecName: Full=Breast carcinoma-amplified sequence 3 {ECO:0000312|HGNC:HGNC:14347, ECO:0000312|MIM:607470}; AltName: Full=GAOB1;
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
>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;
XXXSXSXCGSPXSXXXXXDFKXLWXKLKEXHDXEXQXLXXKXXXXKXXRXXXXXRLXXFXTKNQXLRXQQKXLXXXIKXXXXXXXXXXXXRCXVTEEHMXKKQXEFENIRQQNLXLITELMNXXNXLQXENKKLSEQLXQXXXXXXXXXXXXXXXEEXXIPDSPXXXFSFSGXNRLRRKENXHVRYXEQTXXKLEXXXCXXEXXXXXKXSXXXXXXXXEXEILVADTYDQXXSPXXKXXXXXXYXXXKXSXNLAXVVAETLGLXXQEESEXQXXXSXLXXXLXXCLXXXXKKQXFXEXXXXXEDXXRFSDSXXXTPPXXXXXXRXSSPVFGAXSXXKXXXXLXTSXSPSLLXXGKKXXLKTXXFXNXXXSRXXKXRSKSEDXALXTXXXXGSEXXXIIIQSSXKQXLXXKNXSESXXXXXXXXXXKXXXXDXXXXPLKSLGGRXXKRKXXEEEXEXXXXCXXXSFDKENXXPFXXXXXXXXNGXXXXDKPLDLSDRFXXXXXQEKXXGXEXXKXXXXQXTXYEALKTIPKGFSSXXXXXXGXXXXXXDXXGXXCXQXXXXXQXXXKXSPDXKXXLQIKEEXXXFKXXXXXXXSXETEXXXXDXKXXXXXEPXXXXXRXXHGXCEXASVLQLNXCRXXKXXXXXXXXDXXXENXQWSXDPGADLSQYKMDXTVXDXKXXSXXXXXGEXXDMDXTXVSEXXLLKXKKQEQXXEXSXXXXXKMNDSXXXMFDXTXXEEYESCLAXXFXXXXXEXXELSXXTKKXXXHXXXXDXXKQKAFVEPYFKXXERXXXXXXFPHIEVXRKKXERRXXXXXXXXXXXXXYAXXPXXERXKKLAXCSRHRFRYIPXXTPENFWEVGFPSTQTCXXRGYIKEXXXXXXRPXRRQPYXXXFSXKXKEQXT
>DMRTB_HUMAN__Q96MA1 RecName: Full=Doublesex- and mab-3-related transcription factor B1;
XXXXMVRTPXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXQKXLXXQAXXEXQXXXLXXQGPXXXSXXXAXXXXXXXXPAXSXXPLXPXXXXGXAXPXXXGXXAXCFXEXXPXGRNPGPRALQXVXGGRXXXXXXXXXXXXXXSXXXPXXXXXAXXXGXXXXLXXXXPXXTVPXPLFXXXXXPLXIXPDXXLGXXYPXXXXXXPYXPFPLGXXDAPXGVPXQXGFRHVSXXXYXGXXLXXEPXGDFQPXYYXPPXXXXXXXXXXXXXXPQFLPPGYLSALHXLPXXXPXXXXXXXXLXXXXDTXKEXTXDXXXXXXXXEPSQXSXQEXXX
>FOXP2_HUMAN__O15409 RecName: Full=Forkhead box protein P2; AltName: Full=CAG repeat protein 44; AltName: Full=Trinucleotide repeat-containing gene 10 protein;
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
>HIC1_HUMAN__Q14526 RecName: Full=Hypermethylated in cancer 1 protein; Short=Hic-1; AltName: Full=Zinc finger and BTB domain-containing protein 29;
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
>HXB5_HUMAN__P09067 RecName: Full=Homeobox protein Hox-B5; AltName: Full=Homeobox protein HHO.C10; AltName: Full=Homeobox protein Hox-2A; AltName: Full=Homeobox protein Hu-1;
XSSYFVNSFSGRYPNGXXYXXLNYGXXXXXXXSYRXXXXMHXXXYGYNYNGMDLSXNRXXXSXXHFGAVGXXXRXFXXXXQEXRFRQXXXSCSLSSPESLPCXNXXXXXXXXXXXXPSDXXXXXXSXXXFTEIDEXSASSEPEEXXXXXXXXXXXRAXXXXXXXXXAXXXGQXPQIFPWMRKLHIXHXXXGXXXKRXRTXYTRXXTLEXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXNRRMKWKKXXKXXSMXXXXXXXXXXX
>IKZF1_HUMAN__Q13422 RecName: Full=DNA-binding protein Ikaros; AltName: Full=Ikaros family zinc finger protein 1; AltName: Full=Lymphoid transcription factor LyF-1;
XXXDEXQDXXXXSGXXSPXXXXXXDXXDEPMPIPEDLSTXXXXQQXXXXXXXXXXNXKXEXXSDEENGXXCXXNGEECAEDLRXLDXSGXKXNGSXXXXXXXAXXXXGGXRXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXERPFXCXXCGXXXXXXGNXXRHXKXHXXXXXXXXXXXXXXXXXXXXXXXHXRXHSXXXPXXCXYCGRSYKQRSSLEEHKERCHNYLXXMXXXXXXXXVXKEEXNXXXXXEDXXXXXXXRSLVLDRLAXNVAKRKSSMPQKFXGXKXLXXXXYDXXXXXXXXXEXMXXHVXDQAINNAIXYLGAESLRPLVQTXPXXSXXVXXXXXMYXLHKXXXXXXXXXXXXAXDXAXENLLLLSKXKLXXSEXXXSPSXSXQDSTDTESNXEXXRXGLIYLTNHIXPXXRNGXXXXEEXXXYXXLRAXXXXXXDALRVXSXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXFSSHITRGEHRXXXX
>NOL4L_HUMAN__Q96MY1 RecName: Full=Nucleolar protein 4-like;
XXDXTWXSAXXHXXXXXXPXXXXXMXSPQNXXXXEDDXSSSESXXGNXXXXLXPXXXSXXXGDXXXPEXNGNXXXAPXDFXXXXEDQPXNLXXKLXXXXXLXXXXYXXXXXXXDXLRXRXKYXXKXTXESPPYSSGSYDSXKXEXXXCXEDLXVXRXXXXXXXXXXXXXXXXXXXXXDXEGXDPERLKAFNMFVXXXXXXXXDRMVPISKQPKEKIQAIIESCSRQFPEFQERARKRIRTYLKSCRRMKKNGMEXXRPTPPHLTSAMAENILAAACESEXRKAAKRMRXXXYQXXXXXXXXLXKXXXXXXXXXTXSXYSLPAXXYSQDPVYXNGGLXYSYRGYGXXXXXXQXXASLXTGXHXNGPTDLSMKGXAXXXXXXXXXXXXXXXTXRXXPXXQLSPTEIXAVRQLIXXXXXXXXXXXXXXXXXXXLILQQN
>NOL4_HUMAN__O94818 RecName: Full=Nucleolar protein 4; AltName: Full=Nucleolar-localized protein;
XXXXXXXXXXFQXWCLRTYGDSGKTKTVTRXKYXXIXXXLXGXXXSXXXXAKFKFWVKSKGFQLXXXXXXXXXXXXXXXVLXVXXXXXDXXGVXXXXXXXXXXXXXXXXXXXXXMHVEXXXXXXXXXKHAGQKXTYXAIXEXYAXXPRXAVXXFLMSCXECQKRMHXNXXXXXXKXXXXPXXLVXXXIDYNMPXTXXXXKXMKLQXXXSXXXXDESSXXSXXXDMXDSTXXSAXXXXXSSXXXEXXXXPQXXXGQQDDDSAAEXXXXNXTXGXXSXXXGXXXXXEXXXXXXXXXXXXXQXEQPLNLSDXPXSAXXTXXXRXXXXXXXGXXXXXXXLXXXLKXXXXAXEXXXKSPAHSXXSYXSXKXEXXXXXXEDLSXXRXDXDXDXHXXXXDXXKXNXXXGXXXERLKXXXXXXXXXXXXXXXRMVPISKQPKEKIQAIIXSCXRQFPEXXERXRKRIRTYLKSCRXXXXXXXXXXRPXPXHLTSAXAEXILAXACESEXRNAAKRMRLXXXQDXXXXXDKXXXXXXXXXXYSXSXXXXXQXXXYINGXXXXXXXXYXXLXXXLXNXXXXXXSGPTDLSMKXXXXXXXXXXSXXXXXXQLSPXEXXAVRQLXXXXXXXXXXXXXXXXXXXXLXLQQX
>NRIP1_HUMAN__P48552 RecName: Full=Nuclear receptor-interacting protein 1; AltName: Full=Nuclear factor RIP140; AltName: Full=Receptor-interacting protein 140;
XTXGEXXXXXXHXDSXXLTYXEGLLMHQAXXGXGXAXXXXSXGXXXXDXNFXXSGXXFPXCXXNXPXXXTXXXQGSGMLHLKKARLLQSSEDWNAAXXXRXSXXXXXLNXXXEXXXXGXXXXXPXXKQDSTLLASLLXXXXXXXXXVXXXQQXXXXXXEQXXXLSXXXXXXXKDLXCYXXASSHLKTLLXKSKXKDQXXXXXXPXXXXXXXXXXFXESXXXXXQSGTKXXXEPXSCAXRLXAVASMVXXRXSPXXSPKPSVACSQLALLXXSEAHXQQYSXXHALKXQXXXXXASERLAAMARLQEXXXKXXXXXXXXXXXSXHLNGXARXXXXKXXAXKXXXXXFQXPXXXXXSSPKXXGYKXXXERNXXKXXXXNSLXXHXLKSQXXXXXXXGXXXXEXXXXFXXXSTPTTXDEXSDXNPSFTXDSSXDESSXSXCXPIDLSXKXRXXKXXXXXXXSLDNFTQSLLNXWDPKXXXXXXXXDXDXXXXSXLNSHQKVTLXQXXLGHKXXEXVEKXXXXQXXXXDXXKFXXQXXXRTXVXESPXXXRXTPXXTPPLXXSXXXXSPINLSQHSLXXKXXSPPYXCXXXXXXXXXXAXXHXXDLTKXKXXXXXXXXXXXXXXXXATFSASKLLQNLAQCGXQXXXXXEXXXXXXXLLXXXXXKPXGXIDRLXSPLLXNKXXXXEEXXXXXXXXXXXEXXXXGSEIENLLERRTVLQLLLGXXXKGKXXKKXXXXXXXEXXXEXXXXXXSEQILXVKIKSEPXDDXXXXXXXXXXXXXXXXXXFXGXXPXXXRSXXAXXXXEXXKXEPXSPQDFSXSKNGLLSRLLRQNXXSYXXXXXDXXXXXXEXXXXEXXXXCXVPKKRKLXXEPLENPXKXXKXXXXXXXXXHXXPEXLYGSXLXQXELKXSRXXXEXKXXXXXXSXXXXXXXXWXRESKSFNVLKQLLLSENCVRDLSPXRXXXXXXXXXKGXXXXXXXXKPEFSISSLNGLMXXXXQXXXCXXXRTFXXPXXXXXPXSPTFXEXLGXXGXRXEXGXXNXCXXXXXKGPIXWVIXXXXKXXYXXDSPRLTKTNPILYYMLQKGGXXXXXXEXXDXXXWXEXXXXXSXXQVTXKEEXXPXAETXXXFFXLRXXYXSXXGXXXXXXHXXNGEXYGLLXXXLTIKKEXE
>PLCB1_HUMAN__Q9NQ66 RecName: Full=1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-1; EC=3.1.4.11; AltName: Full=PLC-154; AltName: Full=Phosphoinositide phospholipase C-beta-1; AltName: Full=Phospholipase C-I; Short=PLC-I; AltName: Full=Phospholipase C-beta-1; Short=PLC-beta-1;
XXXXXXGXXXXXXXXVXVXXXXXXGXKFXXWXXXXXXXTPXXXXXXXXXXXXYWXDXXXXXXXLXXXXXXXXRXGXXXXXXXDPKLRELLDVGXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXGXXXXKNIXXXXXXXRXXXEXALXXXXLPSXRXDSIXXXXFXPEXYXXFLXNXXXXXXXDXXFXEXXXXSXXXXXXXXXXXFXNXXQXDPRLNEILYPXXXXXXXXXLXXXYEPNXXXAXXGXXSXXGFXRYLXGEXNXXXXXXKLDXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXKKXHKXXXXXXKKKXXXQXSNXXSDXSSXXEPSSPGXGXXXXXSXDDXXXDXXXKXXXXXXXAGXEXXAXXEXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXRXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXEXXXKQLAALTLEXEXEXXKXXXXGXXPSEXXXXXXXXPAENGXNHXXXXXPKPXSQXXHSXXXXXXVKXPXKXEDLIQSVLTXXXAXTIEXLXXXKXXXKXXXKXXKEMKXLXKXHXKKTXXLIXEHXXXXXXIQXXXXRRRAXLXKXXKKDSKKXXXXXXXXHXXSXXEQXLXXLDXEXXQXLXXLKXXQQQQLLXLRQEXYYXEXXQXXXXXXXXXXXXXXXXXXCQXXQLXKLKXXCEKXKXXXXXXXXXXRXXXXXXXXXKDKXXXEEEKXEXXRSXIXEVXQYIKRLXXAQSKRXEXLXEKHXXIRQQILDEKPKXXXXLXXEXQXXXXXXPXXIXEXVQXXMKGKXSEDXXHGSXXXXXXXDXXKXNXKXPXXEEXXXXXXXXXFDTXL
>TGIF1_HUMAN__Q15583 RecName: Full=Homeobox protein TGIF1; AltName: Full=5'-TG-3'-interacting factor 1;
XXXXXXXXXXXXXXXHCSGSXXXGSDXFPWPASHPGNPQCSFSTAFLAXXXXXXXXXXXXXXAXWSSLAXXXXXXXXSCAPXXXPARCXXXRXLXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXMXGIXAXSGSETEDXDXMDXPLDLSSXXXXGKRXRRGNLPKESVQILRDWLXXHRXNAXXSEQEKXLLSXQTXXXXXXXXXXXXXXXXXXLPXMLRKDGKDPNXFTISRRGXKXXEXXXXXSXXXXXXXXPXXEEXPFXXXXXGXXXXXXXPXXXKXXSPGXXLARPSVICXTXVXXXXXXXXXXXXXXXXXXXXXXXQXXXXXXTDXSXXYXEDXXXXGXXXNXQSGLFNTPXXTXPDLXQDFSGFQXXVXXXXXXXXXXELQAKXXX
>TSH3_HUMAN__Q63HK5 RecName: Full=Teashirt homolog 3; AltName: Full=Zinc finger protein 537;
XXXXXXXXXXXXAAYVSEELKAAALVDEGXDXEEXXXXGEPXXKYXCPXKXXXXXXPXXQXSPAAXFSXHEMDSESHXSETSDRMXDFESXSXKNEXXXKXXXXXXXXXXXSDSLEQMKAXYXXXLXXXXWSXLXLNLXQXXXXXXXXXXSXXXXXXXXXGSXXXDWHQXAMAKTLQXVSQXXXXXEPXLFSTVXLYXXXXXXXXXXXXXXXXXXXXXXXXXXXXXVELTVHMNETGHYRDDNHETDXXXXKRWSKPRKRSLLEMEGKEDAQKVLKCXXXXXXXXXXXXLSVHXIKTKHYQKVPLKEPVTPXXXKIXXXXRKXXXXXLXXPSSPDSXGGTPKXXXXXXXDXLQKXXNPYITPNNRYGHQNGASYAWXFEXXXXXXXKCMECGXXXXTXQXLTXHMMVTGHFIKVTNSAXKKGKXXXEXXXXPXXXXXXXEKVQSVPLAATTFTXPXXXPXSXSPKXXXEXKKEXXKEXXXXXXXXKXXXXXXEXEEKXDXSSKYXYLTEXDLXESPKGGXDILKSLENTVTSAINKAQNGXPSWGGYPSIHAAYQLPNXMKLSLXXXXKXXXLKXXXXXXXXXSPXXXQXXXXPXXXQXSXXPKXNFHAMEELVKKVTEKVAKVEEKXXXPXXXXSPXXRXTPSPCXSEXXEXXKXEXSXXXXXXSQXXSPXXXRDXCKXXXPXXEPXENGKXXXXXXXXXXSXSTAIITDHPPEQPFVNPLSALQXXMNXHLGKAAKPXLPXLDPMSMLFKMSNSLAEKAAVAXXXPXXXKXXXXLDRYFYHXXNDQPIDLTKGKXXXXXSLXSXXXSXXXXXXXXXSXXXXXXXXSAVXSFMSNSPLRENALSDISDMLXNLTEXXXXKSXTPXSXSEXXDIXGXTXEXXEXXXPAQKRKGRQSNWNPQHLLILQAQFAXSLRQTXXGKYXMSDLSPQERMHISRFTGXXXXXXXXXXXXXXXXXXXXXGXKFLKNXXXXXXXXXXXXXXXXXXXXSTYXXHLESHXXXRXRDLXKLSXEQXXXQIXXXXXXSXXXXXXXXXXXXGXXXQCKLCXRXXXXXHAVKLHLSKTHGKSPEDHLXXVXELXKX
Click here and save the page to download this output.
>BCAS3_HUMAN__Q9H6U6-slimfinder Motifs
----------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------
>BCAS3_HUMAN__Q9H6U6-masked
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
>BCAS3_HUMAN__Q9H6U6 RecName: Full=Breast carcinoma-amplified sequence 3 {ECO:0000312|HGNC:HGNC:14347, ECO:0000312|MIM:607470}; AltName: Full=GAOB1;
MNEAMATDSPRRPSRCTGGVVVRPQAVTEQSYMESVVTFLQDVVPQAYSGTPLTEEKEKIVWVRFENADLNDTSRNLEFHEIHSTGNEPPLLIMIGYSDGMQVWSIPISGEAQELFSVRHGPIRAARILPAPQFGAQKCDNFAEKRPLLGVCKSIGSSGTSPPYCCVDLYSLRTGEMVKSIQFKTPIYDLHCNKRILVVVLQEKIAAFDSCTFTKKFFVTSCYPCPGPNMNPIALGSRWLAYAENKLIRCHQSRGGACGDNIQSYTATVISAAKTLKSGLTMVGKVVTQLTGTLPSGVTEDDVAIHSNSRRSPLVPGIITVIDTETVGEGQVLVSEDSDSDGIVAHFPAHEKPVCCMAFNTSGMLLVTTDTLGHDFHVFQILTHPWSSSQCAVHHLYTLHRGETEAKVQDICFSHDCRWVVVSTLRGTSHVFPINPYGGQPCVRTHMSPRVVNRMSRFQKSAGLEEIEQELTSKQGGRCSPVPGLSSSPSGSPLHGKLNSQDSYNNFTNNNPGNPRLSPLPSLMVVMPLAQIKQPMTLGTITKRTGPYLFGAGCFSIKAPCKVKPPPQISPSKSMGGEFCVAAIFGTSRSWFANNAGLKREKDQSKQVVVESLYIISCYGTLVEHMMEPRPLSTAPKISDDTPLEMMTSPRASWTLVRTPQWNELQPPFNANHPLLLAADAVQYYQFLLAGLVPPGSPGPITRHGSYDSLASDHSGQEDEEWLSQVEIVTHTGPHRRLWMGPQFQFKTIHPSGQTTVISSSSSVLQSHGPSDTPQPLLDFDTDDLDLNSLRIQPVRSDPVSMPGSSRPVSDRRGVSTVIDAASGTFDRSVTLLEVCGSWPEGFGLRHMSSMEHTEEGLRERLADAMAESPSRDVVGSGTELQREGSIETLSNSSGSTSGSIPRNFDGYRSPLPTNESQPLSLFPTGFP
>COM1_HUMAN__Q99708-slimfinder Motifs
---------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------P-DLS-----------------------------------------------------------------------------------------------------------------------------------------------------------------------DLS-----------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------
>COM1_HUMAN__Q99708-masked
XXXSXSXCGSPXSXXXXXDFKXLWXKLKEXHDXEXQXLXXKXXXXKXXRXXXXXRLXXFXTKNQXLRXQQKXLXXXIKXXXXXXXXXXXXRCXVTEEHMXKKQXEFENIRQQNLXLITELMNXXNXLQXENKKLSEQLXQXXXXXXXXXXXXXXXEEXXIPDSPXXXFSFSGXNRLRRKENXHVRYXEQTXXKLEXXXCXXEXXXXXKXSXXXXXXXXEXEILVADTYDQXXSPXXKXXXXXXYXXXKXSXNLAXVVAETLGLXXQEESEXQXXXSXLXXXLXXCLXXXXKKQXFXEXXXXXEDXXRFSDSXXXTPPXXXXXXRXSSPVFGAXSXXKXXXXLXTSXSPSLLXXGKKXXLKTXXFXNXXXSRXXKXRSKSEDXALXTXXXXGSEXXXIIIQSSXKQXLXXKNXSESXXXXXXXXXXKXXXXDXXXXPLKSLGGRXXKRKXXEEEXEXXXXCXXXSFDKENXXPFXXXXXXXXNGXXXXDKPLDLSDRFXXXXXQEKXXGXEXXKXXXXQXTXYEALKTIPKGFSSXXXXXXGXXXXXXDXXGXXCXQXXXXXQXXXKXSPDXKXXLQIKEEXXXFKXXXXXXXSXETEXXXXDXKXXXXXEPXXXXXRXXHGXCEXASVLQLNXCRXXKXXXXXXXXDXXXENXQWSXDPGADLSQYKMDXTVXDXKXXSXXXXXGEXXDMDXTXVSEXXLLKXKKQEQXXEXSXXXXXKMNDSXXXMFDXTXXEEYESCLAXXFXXXXXEXXELSXXTKKXXXHXXXXDXXKQKAFVEPYFKXXERXXXXXXFPHIEVXRKKXERRXXXXXXXXXXXXXYAXXPXXERXKKLAXCSRHRFRYIPXXTPENFWEVGFPSTQTCXXRGYIKEXXXXXXRPXRRQPYXXXFSXKXKEQXT
>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
>DMRTB_HUMAN__Q96MA1-slimfinder Motifs
------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------
>DMRTB_HUMAN__Q96MA1-masked
XXXXMVRTPXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXQKXLXXQAXXEXQXXXLXXQGPXXXSXXXAXXXXXXXXPAXSXXPLXPXXXXGXAXPXXXGXXAXCFXEXXPXGRNPGPRALQXVXGGRXXXXXXXXXXXXXXSXXXPXXXXXAXXXGXXXXLXXXXPXXTVPXPLFXXXXXPLXIXPDXXLGXXYPXXXXXXPYXPFPLGXXDAPXGVPXQXGFRHVSXXXYXGXXLXXEPXGDFQPXYYXPPXXXXXXXXXXXXXXPQFLPPGYLSALHXLPXXXPXXXXXXXXLXXXXDTXKEXTXDXXXXXXXXEPSQXSXQEXXX
>DMRTB_HUMAN__Q96MA1 RecName: Full=Doublesex- and mab-3-related transcription factor B1;
MADKMVRTPKCSRCRNHGFLVPVKGHAGKCRWKQCLCEKCYLISERQKIMAAQKVLKTQAAEEEQEAALCAQGPKQASGAAAAAPAPVPVPAASLRPLSPGTPSGDADPGPEGRAAACFFEQPPRGRNPGPRALQPVLGGRSHVEPSERAAVAMPSLAGPPFGAEAAGSGYPGPLDLRRPMRTVPGPLFTDFVRPLNINPDRALGPEYPGGSSMHPYCPFPLGYLDAPPGVPLQQGFRHVSRSQYQGGGLVSEPGGDFQPSYYLPPPPPPLPPLPPLPPQPQFLPPGYLSALHFLPPPPPPPPPSSFSLTVLFDTDKENTDDQDAEVLSGEPSQPSSQEQSD
>FOXP2_HUMAN__O15409-slimfinder Motifs
-------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------
>FOXP2_HUMAN__O15409-masked
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
>FOXP2_HUMAN__O15409 RecName: Full=Forkhead box protein P2; AltName: Full=CAG repeat protein 44; AltName: Full=Trinucleotide repeat-containing gene 10 protein;
MMQESATETISNSSMNQNGMSTLSSQLDAGSRDGRSSGDTSSEVSTVELLHLQQQQALQAARQLLLQQQTSGLKSPKSSDKQRPLQVPVSVAMMTPQVITPQQMQQILQQQVLSPQQLQALLQQQQAVMLQQQQLQEFYKKQQEQLHLQLLQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQHPGKQAKEQQQQQQQQQQLAAQQLVFQQQLLQMQQLQQQQHLLSLQRQGLISIPPGQAALPVQSLPQAGLSPAEIQQLWKEVTGVHSMEDNGIKHGGLDLTTNNSSSTTSSNTSKASPPITHHSIVNGQSSVLSARRDSSSHEETGASHTLYGHGVCKWPGCESICEDFGQFLKHLNNEHALDDRSTAQCRVQMQVVQQLEIQLSKERERLQAMMTHLHMRPSEPKPSPKPLNLVSSVTMSKNMLETSPQSLPQTPTTPTAPVTPITQGPSVITPASVPNVGAIRRRHSDKYNIPMSSEIAPNYEFYKNADVRPPFTYATLIRQAIMESSDRQLTLNEIYSWFTRTFAYFRRNAATWKNAVRHNLSLHKCFVRVENVKGAVWTVDEVEYQKRRSQKITGSPTLVKNIPTSLGYGAALNASLQAALAESSLPLLSNPGLINNASSGLLQAVHEDLNGSLDHIDSNGNSSPGCSPQPHIHSIHVKEEPVIAEDEDCPMSLVTTANHSPELEDDREIEEEPLSEDLE
>HIC1_HUMAN__Q14526-slimfinder Motifs
--------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------DLS--------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------
>HIC1_HUMAN__Q14526-masked
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
>HIC1_HUMAN__Q14526 RecName: Full=Hypermethylated in cancer 1 protein; Short=Hic-1; AltName: Full=Zinc finger and BTB domain-containing protein 29;
MTFPEADILLKSGECAGQTMLDTMEAPGHSRQLLLQLNNQRTKGFLCDVIIVVQNALFRAHKNVLAASSAYLKSLVVHDNLLNLDHDMVSPAVFRLVLDFIYTGRLADGAEAAAAAAVAPGAEPSLGAVLAAASYLQIPDLVALCKKRLKRHGKYCHLRGGGGGGGGYAPYGRPGRGLRAATPVIQACYPSPVGPPPPPAAEPPSGPEAAVNTHCAELYASGPGPAAALCASERRCSPLCGLDLSKKSPPGSAAPERPLAERELPPRPDSPPSAGPAAYKEPPLALPSLPPLPFQKLEEAAPPSDPFRGGSGSPGPEPPGRPDGPSLLYRWMKHEPGLGSYGDELGRERGSPSERCEERGGDAAVSPGGPPLGLAPPPRYPGSLDGPGAGGDGDDYKSSSEETGSSEDPSPPGGHLEGYPCPHLAYGEPESFGDNLYVCIPCGKGFPSSEQLNAHVEAHVEEEEALYGRAEAAEVAAGAAGLGPPFGGGGDKVAGAPGGLGELLRPYRCASCDKSYKDPATLRQHEKTHWLTRPYPCTICGKKFTQRGTMTRHMRSHLGLKPFACDACGMRFTRQYRLTEHMRIHSGEKPYECQVCGGKFAQQRNLISHMKMHAVGGAAGAAGALAGLGGLPGVPGPDGKGKLDFPEGVFAVARLTAEQLSLKQQDKAAAAELLAQTTHFLHDPKVALESLYPLAKFTAELGLSPDKAAEVLSQGAHLAAGPDGRTIDRFSPT
>HXB5_HUMAN__P09067-slimfinder Motifs
----------------------------------------------------DLS----------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------
>HXB5_HUMAN__P09067-masked
XSSYFVNSFSGRYPNGXXYXXLNYGXXXXXXXSYRXXXXMHXXXYGYNYNGMDLSXNRXXXSXXHFGAVGXXXRXFXXXXQEXRFRQXXXSCSLSSPESLPCXNXXXXXXXXXXXXPSDXXXXXXSXXXFTEIDEXSASSEPEEXXXXXXXXXXXRAXXXXXXXXXAXXXGQXPQIFPWMRKLHIXHXXXGXXXKRXRTXYTRXXTLEXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXNRRMKWKKXXKXXSMXXXXXXXXXXX
>HXB5_HUMAN__P09067 RecName: Full=Homeobox protein Hox-B5; AltName: Full=Homeobox protein HHO.C10; AltName: Full=Homeobox protein Hox-2A; AltName: Full=Homeobox protein Hu-1;
MSSYFVNSFSGRYPNGPDYQLLNYGSGSSLSGSYRDPAAMHTGSYGYNYNGMDLSVNRSSASSSHFGAVGESSRAFPAPAQEPRFRQAASSCSLSSPESLPCTNGDSHGAKPSASSPSDQATSASSSANFTEIDEASASSEPEEAASQLSSPSLARAQPEPMATSTAAPEGQTPQIFPWMRKLHISHDMTGPDGKRARTAYTRYQTLELEKEFHFNRYLTRRRRIEIAHALCLSERQIKIWFQNRRMKWKKDNKLKSMSLATAGSAFQP
>IKZF1_HUMAN__Q13422-slimfinder Motifs
---------------------------------P-DLS-------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------
>IKZF1_HUMAN__Q13422-masked
XXXDEXQDXXXXSGXXSPXXXXXXDXXDEPMPIPEDLSTXXXXQQXXXXXXXXXXNXKXEXXSDEENGXXCXXNGEECAEDLRXLDXSGXKXNGSXXXXXXXAXXXXGGXRXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXERPFXCXXCGXXXXXXGNXXRHXKXHXXXXXXXXXXXXXXXXXXXXXXXHXRXHSXXXPXXCXYCGRSYKQRSSLEEHKERCHNYLXXMXXXXXXXXVXKEEXNXXXXXEDXXXXXXXRSLVLDRLAXNVAKRKSSMPQKFXGXKXLXXXXYDXXXXXXXXXEXMXXHVXDQAINNAIXYLGAESLRPLVQTXPXXSXXVXXXXXMYXLHKXXXXXXXXXXXXAXDXAXENLLLLSKXKLXXSEXXXSPSXSXQDSTDTESNXEXXRXGLIYLTNHIXPXXRNGXXXXEEXXXYXXLRAXXXXXXDALRVXSXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXFSSHITRGEHRXXXX
>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
>NOL4L_HUMAN__Q96MY1-slimfinder Motifs
----------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------P-DLS-------------------------------------------------------------------
>NOL4L_HUMAN__Q96MY1-masked
XXDXTWXSAXXHXXXXXXPXXXXXMXSPQNXXXXEDDXSSSESXXGNXXXXLXPXXXSXXXGDXXXPEXNGNXXXAPXDFXXXXEDQPXNLXXKLXXXXXLXXXXYXXXXXXXDXLRXRXKYXXKXTXESPPYSSGSYDSXKXEXXXCXEDLXVXRXXXXXXXXXXXXXXXXXXXXXDXEGXDPERLKAFNMFVXXXXXXXXDRMVPISKQPKEKIQAIIESCSRQFPEFQERARKRIRTYLKSCRRMKKNGMEXXRPTPPHLTSAMAENILAAACESEXRKAAKRMRXXXYQXXXXXXXXLXKXXXXXXXXXTXSXYSLPAXXYSQDPVYXNGGLXYSYRGYGXXXXXXQXXASLXTGXHXNGPTDLSMKGXAXXXXXXXXXXXXXXXTXRXXPXXQLSPTEIXAVRQLIXXXXXXXXXXXXXXXXXXXLILQQN
>NOL4L_HUMAN__Q96MY1 RecName: Full=Nucleolar protein 4-like;
MSDSTWMSADPHLASSLSPSQDERMRSPQNLHSQEDDDSSSESGSGNGSSTLNPSTSSSTQGDPAFPEMNGNGAVAPMDFTTAAEDQPINLCDKLPPATALGTASYPSDGCGADGLRSRVKYGVKTTPESPPYSSGSYDSIKTEVSGCPEDLTVGRAPTADDDDDDHDDHEDNDKMNDSEGMDPERLKAFNMFVRLFVDENLDRMVPISKQPKEKIQAIIESCSRQFPEFQERARKRIRTYLKSCRRMKKNGMEMTRPTPPHLTSAMAENILAAACESETRKAAKRMRLEIYQSSQDEPIALDKQHSRDSAAITHSTYSLPASSYSQDPVYANGGLNYSYRGYGALSSNLQPPASLQTGNHSNGPTDLSMKGGASTTSTTPTPTPSSTSTSRPVPTAQLSPTEISAVRQLIAGYRESAAFLLRSADELENLILQQN
>NOL4_HUMAN__O94818-slimfinder Motifs
--------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------DLS------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------P-DLS----------------------------------------------------------
>NOL4_HUMAN__O94818-masked
XXXXXXXXXXFQXWCLRTYGDSGKTKTVTRXKYXXIXXXLXGXXXSXXXXAKFKFWVKSKGFQLXXXXXXXXXXXXXXXVLXVXXXXXDXXGVXXXXXXXXXXXXXXXXXXXXXMHVEXXXXXXXXXKHAGQKXTYXAIXEXYAXXPRXAVXXFLMSCXECQKRMHXNXXXXXXKXXXXPXXLVXXXIDYNMPXTXXXXKXMKLQXXXSXXXXDESSXXSXXXDMXDSTXXSAXXXXXSSXXXEXXXXPQXXXGQQDDDSAAEXXXXNXTXGXXSXXXGXXXXXEXXXXXXXXXXXXXQXEQPLNLSDXPXSAXXTXXXRXXXXXXXGXXXXXXXLXXXLKXXXXAXEXXXKSPAHSXXSYXSXKXEXXXXXXEDLSXXRXDXDXDXHXXXXDXXKXNXXXGXXXERLKXXXXXXXXXXXXXXXRMVPISKQPKEKIQAIIXSCXRQFPEXXERXRKRIRTYLKSCRXXXXXXXXXXRPXPXHLTSAXAEXILAXACESEXRNAAKRMRLXXXQDXXXXXDKXXXXXXXXXXYSXSXXXXXQXXXYINGXXXXXXXXYXXLXXXLXNXXXXXXSGPTDLSMKXXXXXXXXXXSXXXXXXQLSPXEXXAVRQLXXXXXXXXXXXXXXXXXXXXLXLQQX
>NOL4_HUMAN__O94818 RecName: Full=Nucleolar protein 4; AltName: Full=Nucleolar-localized protein;
MESERDMYRQFQDWCLRTYGDSGKTKTVTRKKYERIVQLLNGSESSSTDNAKFKFWVKSKGFQLGQPDEVRGGGGGAKQVLYVPVKTTDGVGVDEKLSLRRVAVVEDFFDIIYSMHVETGPNGEQIRKHAGQKRTYKAISESYAFLPREAVTRFLMSCSECQKRMHLNPDGTDHKDNGKPPTLVTSMIDYNMPITMAYMKHMKLQLLNSQQDEDESSIESDEFDMSDSTRMSAVNSDLSSNLEERMQSPQNLHGQQDDDSAAESFNGNETLGHSSIASGGTHSREMGDSNSDGKTGLEQDEQPLNLSDSPLSAQLTSEYRIDDHNSNGKNKYKNLLISDLKMEREARENGSKSPAHSYSSYDSGKNESVDRGAEDLSLNRGDEDEDDHEDHDDSEKVNETDGVEAERLKAFNMFVRLFVDENLDRMVPISKQPKEKIQAIIDSCRRQFPEYQERARKRIRTYLKSCRRMKRSGFEMSRPIPSHLTSAVAESILASACESESRNAAKRMRLERQQDESAPADKQCKPEATQATYSTSAVPGSQDVLYINGNGTYSYHSYRGLGGGLLNLNDASSSGPTDLSMKRQLATSSGSSSSSNSRPQLSPTEINAVRQLVAGYRESAAFLLRSADELENLILQQN
>NRIP1_HUMAN__P48552-slimfinder Motifs
-------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------P-DLS-----------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------DLS----------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------
>NRIP1_HUMAN__P48552-masked
XTXGEXXXXXXHXDSXXLTYXEGLLMHQAXXGXGXAXXXXSXGXXXXDXNFXXSGXXFPXCXXNXPXXXTXXXQGSGMLHLKKARLLQSSEDWNAAXXXRXSXXXXXLNXXXEXXXXGXXXXXPXXKQDSTLLASLLXXXXXXXXXVXXXQQXXXXXXEQXXXLSXXXXXXXKDLXCYXXASSHLKTLLXKSKXKDQXXXXXXPXXXXXXXXXXFXESXXXXXQSGTKXXXEPXSCAXRLXAVASMVXXRXSPXXSPKPSVACSQLALLXXSEAHXQQYSXXHALKXQXXXXXASERLAAMARLQEXXXKXXXXXXXXXXXSXHLNGXARXXXXKXXAXKXXXXXFQXPXXXXXSSPKXXGYKXXXERNXXKXXXXNSLXXHXLKSQXXXXXXXGXXXXEXXXXFXXXSTPTTXDEXSDXNPSFTXDSSXDESSXSXCXPIDLSXKXRXXKXXXXXXXSLDNFTQSLLNXWDPKXXXXXXXXDXDXXXXSXLNSHQKVTLXQXXLGHKXXEXVEKXXXXQXXXXDXXKFXXQXXXRTXVXESPXXXRXTPXXTPPLXXSXXXXSPINLSQHSLXXKXXSPPYXCXXXXXXXXXXAXXHXXDLTKXKXXXXXXXXXXXXXXXXATFSASKLLQNLAQCGXQXXXXXEXXXXXXXLLXXXXXKPXGXIDRLXSPLLXNKXXXXEEXXXXXXXXXXXEXXXXGSEIENLLERRTVLQLLLGXXXKGKXXKKXXXXXXXEXXXEXXXXXXSEQILXVKIKSEPXDDXXXXXXXXXXXXXXXXXXFXGXXPXXXRSXXAXXXXEXXKXEPXSPQDFSXSKNGLLSRLLRQNXXSYXXXXXDXXXXXXEXXXXEXXXXCXVPKKRKLXXEPLENPXKXXKXXXXXXXXXHXXPEXLYGSXLXQXELKXSRXXXEXKXXXXXXSXXXXXXXXWXRESKSFNVLKQLLLSENCVRDLSPXRXXXXXXXXXKGXXXXXXXXKPEFSISSLNGLMXXXXQXXXCXXXRTFXXPXXXXXPXSPTFXEXLGXXGXRXEXGXXNXCXXXXXKGPIXWVIXXXXKXXYXXDSPRLTKTNPILYYMLQKGGXXXXXXEXXDXXXWXEXXXXXSXXQVTXKEEXXPXAETXXXFFXLRXXYXSXXGXXXXXXHXXNGEXYGLLXXXLTIKKEXE
>NRIP1_HUMAN__P48552 RecName: Full=Nuclear receptor-interacting protein 1; AltName: Full=Nuclear factor RIP140; AltName: Full=Receptor-interacting protein 140;
MTHGEELGSDVHQDSIVLTYLEGLLMHQAAGGSGTAVDKKSAGHNEEDQNFNISGSAFPTCQSNGPVLNTHTYQGSGMLHLKKARLLQSSEDWNAAKRKRLSDSIMNLNVKKEALLAGMVDSVPKGKQDSTLLASLLQSFSSRLQTVALSQQIRQSLKEQGYALSHDSLKVEKDLRCYGVASSHLKTLLKKSKVKDQKPDTNLPDVTKNLIRDRFAESPHHVGQSGTKVMSEPLSCAARLQAVASMVEKRASPATSPKPSVACSQLALLLSSEAHLQQYSREHALKTQNANQAASERLAAMARLQENGQKDVGSYQLPKGMSSHLNGQARTSSSKLMASKSSATVFQNPMGIIPSSPKNAGYKNSLERNNIKQAANNSLLLHLLKSQTIPKPMNGHSHSERGSIFEESSTPTTIDEYSDNNPSFTDDSSGDESSYSNCVPIDLSCKHRTEKSESDQPVSLDNFTQSLLNTWDPKVPDVDIKEDQDTSKNSKLNSHQKVTLLQLLLGHKNEENVEKNTSPQGVHNDVSKFNTQNYARTSVIESPSTNRTTPVSTPPLLTSSKAGSPINLSQHSLVIKWNSPPYVCSTQSEKLTNTASNHSMDLTKSKDPPGEKPAQNEGAQNSATFSASKLLQNLAQCGMQSSMSVEEQRPSKQLLTGNTDKPIGMIDRLNSPLLSNKTNAVEENKAFSSQPTGPEPGLSGSEIENLLERRTVLQLLLGNPNKGKSEKKEKTPLRDESTQEHSERALSEQILMVKIKSEPCDDLQIPNTNVHLSHDAKSAPFLGMAPAVQRSAPALPVSEDFKSEPVSPQDFSFSKNGLLSRLLRQNQDSYLADDSDRSHRNNEMALLESKNLCMVPKKRKLYTEPLENPFKKMKNNIVDAANNHSAPEVLYGSLLNQEELKFSRNDLEFKYPAGHGSASESEHRSWARESKSFNVLKQLLLSENCVRDLSPHRSNSVADSKKKGHKNNVTNSKPEFSISSLNGLMYSSTQPSSCMDNRTFSYPGVVKTPVSPTFPEHLGCAGSRPESGLLNGCSMPSEKGPIKWVITDAEKNEYEKDSPRLTKTNPILYYMLQKGGNSVTSRETQDKDIWREASSAESVSQVTAKEELLPTAETKASFFNLRSPYNSHMGNNASRPHSANGEVYGLLGSVLTIKKESE
>PLCB1_HUMAN__Q9NQ66-slimfinder Motifs
----------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------
>PLCB1_HUMAN__Q9NQ66-masked
XXXXXXGXXXXXXXXVXVXXXXXXGXKFXXWXXXXXXXTPXXXXXXXXXXXXYWXDXXXXXXXLXXXXXXXXRXGXXXXXXXDPKLRELLDVGXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXGXXXXKNIXXXXXXXRXXXEXALXXXXLPSXRXDSIXXXXFXPEXYXXFLXNXXXXXXXDXXFXEXXXXSXXXXXXXXXXXFXNXXQXDPRLNEILYPXXXXXXXXXLXXXYEPNXXXAXXGXXSXXGFXRYLXGEXNXXXXXXKLDXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXKKXHKXXXXXXKKKXXXQXSNXXSDXSSXXEPSSPGXGXXXXXSXDDXXXDXXXKXXXXXXXAGXEXXAXXEXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXRXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXEXXXKQLAALTLEXEXEXXKXXXXGXXPSEXXXXXXXXPAENGXNHXXXXXPKPXSQXXHSXXXXXXVKXPXKXEDLIQSVLTXXXAXTIEXLXXXKXXXKXXXKXXKEMKXLXKXHXKKTXXLIXEHXXXXXXIQXXXXRRRAXLXKXXKKDSKKXXXXXXXXHXXSXXEQXLXXLDXEXXQXLXXLKXXQQQQLLXLRQEXYYXEXXQXXXXXXXXXXXXXXXXXXCQXXQLXKLKXXCEKXKXXXXXXXXXXRXXXXXXXXXKDKXXXEEEKXEXXRSXIXEVXQYIKRLXXAQSKRXEXLXEKHXXIRQQILDEKPKXXXXLXXEXQXXXXXXPXXIXEXVQXXMKGKXSEDXXHGSXXXXXXXDXXKXNXKXPXXEEXXXXXXXXXFDTXL
>PLCB1_HUMAN__Q9NQ66 RecName: Full=1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-1; EC=3.1.4.11; AltName: Full=PLC-154; AltName: Full=Phosphoinositide phospholipase C-beta-1; AltName: Full=Phospholipase C-I; Short=PLC-I; AltName: Full=Phospholipase C-beta-1; Short=PLC-beta-1;
MAGAQPGVHALQLKPVCVSDSLKKGTKFVKWDDDSTIVTPIILRTDPQGFFFYWTDQNKETELLDLSLVKDARCGRHAKAPKDPKLRELLDVGNIGRLEQRMITVVYGPDLVNISHLNLVAFQEEVAKEWTNEVFSLATNLLAQNMSRDAFLEKAYTKLKLQVTPEGRIPLKNIYRLFSADRKRVETALEACSLPSSRNDSIPQEDFTPEVYRVFLNNLCPRPEIDNIFSEFGAKSKPYLTVDQMMDFINLKQRDPRLNEILYPPLKQEQVQVLIEKYEPNNSLARKGQISVDGFMRYLSGEENGVVSPEKLDLNEDMSQPLSHYFINSSHNTYLTAGQLAGNSSVEMYRQVLLSGCRCVELDCWKGRTAEEEPVITHGFTMTTEISFKEVIEAIAECAFKTSPFPILLSFENHVDSPKQQAKMAEYCRLIFGDALLMEPLEKYPLESGVPLPSPMDLMYKILVKNKKKSHKSSEGSGKKKLSEQASNTYSDSSSMFEPSSPGAGEADTESDDDDDDDDCKKSSMDEGTAGSEAMATEEMSNLVNYIQPVKFESFEISKKRNKSFEMSSFVETKGLEQLTKSPVEFVEYNKMQLSRIYPKGTRVDSSNYMPQLFWNAGCQMVALNFQTMDLAMQINMGMYEYNGKSGYRLKPEFMRRPDKHFDPFTEGIVDGIVANTLSVKIISGQFLSDKKVGTYVEVDMFGLPVDTRRKAFKTKTSQGNAVNPVWEEEPIVFKKVVLPTLACLRIAVYEEGGKFIGHRILPVQAIRPGYHYICLRNERNQPLTLPAVFVYIEVKDYVPDTYADVIEALSNPIRYVNLMEQRAKQLAALTLEDEEEVKKEADPGETPSEAPSEARTTPAENGVNHTTTLTPKPPSQALHSQPAPGSVKAPAKTEDLIQSVLTEVEAQTIEELKQQKSFVKLQKKHYKEMKDLVKRHHKKTTDLIKEHTTKYNEIQNDYLRRRAALEKSAKKDSKKKSEPSSPDHGSSTIEQDLAALDAEMTQKLIDLKDKQQQQLLNLRQEQYYSEKYQKREHIKLLIQKLTDVAEECQNNQLKKLKEICEKEKKELKKKMDKKRQEKITEAKSKDKSQMEEEKTEMIRSYIQEVVQYIKRLEEAQSKRQEKLVEKHKEIRQQILDEKPKLQVELEQEYQDKFKRLPLEILEFVQEAMKGKISEDSNHGSAPLSLSSDPGKVNHKTPSSEELGGDIPGKEFDTPL
>TGIF1_HUMAN__Q15583-slimfinder Motifs
--------------------------------------------------------------------------------------------------------------------------------------------------------P-DLS----------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------
>TGIF1_HUMAN__Q15583-masked
XXXXXXXXXXXXXXXHCSGSXXXGSDXFPWPASHPGNPQCSFSTAFLAXXXXXXXXXXXXXXAXWSSLAXXXXXXXXSCAPXXXPARCXXXRXLXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXMXGIXAXSGSETEDXDXMDXPLDLSSXXXXGKRXRRGNLPKESVQILRDWLXXHRXNAXXSEQEKXLLSXQTXXXXXXXXXXXXXXXXXXLPXMLRKDGKDPNXFTISRRGXKXXEXXXXXSXXXXXXXXPXXEEXPFXXXXXGXXXXXXXPXXXKXXSPGXXLARPSVICXTXVXXXXXXXXXXXXXXXXXXXXXXXQXXXXXXTDXSXXYXEDXXXXGXXXNXQSGLFNTPXXTXPDLXQDFSGFQXXVXXXXXXXXXXELQAKXXX
>TGIF1_HUMAN__Q15583 RecName: Full=Homeobox protein TGIF1; AltName: Full=5'-TG-3'-interacting factor 1;
MVLAQSRVSAGVGSPHCSGSGGGGSDSFPWPASHPGNPQCSFSTAFLASPRLSRGTLAYLPPAPWSSLATPSALLGSSCAPPPPPARCPQPRALSPELGTKAGPRRPHRWELPRSPSQGAQGPAPRRRLLETMKGIVAASGSETEDEDSMDIPLDLSSSAGSGKRRRRGNLPKESVQILRDWLYEHRYNAYPSEQEKALLSQQTHLSTLQVCNWFINARRRLLPDMLRKDGKDPNQFTISRRGAKISETSSVESVMGIKNFMPALEETPFHSCTAGPNPTLGRPLSPKPSSPGSVLARPSVICHTTVTALKDVPFSLCQSVGVGQNTDIQQIAAKNFTDTSLMYPEDTCKSGPSTNTQSGLFNTPPPTPPDLNQDFSGFQLLVDVALKRAAEMELQAKLTA
>TSH3_HUMAN__Q63HK5-slimfinder Motifs
-------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------DLS---------------------------------------------------------------------------------------------------------------------------------------------------------
>TSH3_HUMAN__Q63HK5-masked
XXXXXXXXXXXXAAYVSEELKAAALVDEGXDXEEXXXXGEPXXKYXCPXKXXXXXXPXXQXSPAAXFSXHEMDSESHXSETSDRMXDFESXSXKNEXXXKXXXXXXXXXXXSDSLEQMKAXYXXXLXXXXWSXLXLNLXQXXXXXXXXXXSXXXXXXXXXGSXXXDWHQXAMAKTLQXVSQXXXXXEPXLFSTVXLYXXXXXXXXXXXXXXXXXXXXXXXXXXXXXVELTVHMNETGHYRDDNHETDXXXXKRWSKPRKRSLLEMEGKEDAQKVLKCXXXXXXXXXXXXLSVHXIKTKHYQKVPLKEPVTPXXXKIXXXXRKXXXXXLXXPSSPDSXGGTPKXXXXXXXDXLQKXXNPYITPNNRYGHQNGASYAWXFEXXXXXXXKCMECGXXXXTXQXLTXHMMVTGHFIKVTNSAXKKGKXXXEXXXXPXXXXXXXEKVQSVPLAATTFTXPXXXPXSXSPKXXXEXKKEXXKEXXXXXXXXKXXXXXXEXEEKXDXSSKYXYLTEXDLXESPKGGXDILKSLENTVTSAINKAQNGXPSWGGYPSIHAAYQLPNXMKLSLXXXXKXXXLKXXXXXXXXXSPXXXQXXXXPXXXQXSXXPKXNFHAMEELVKKVTEKVAKVEEKXXXPXXXXSPXXRXTPSPCXSEXXEXXKXEXSXXXXXXSQXXSPXXXRDXCKXXXPXXEPXENGKXXXXXXXXXXSXSTAIITDHPPEQPFVNPLSALQXXMNXHLGKAAKPXLPXLDPMSMLFKMSNSLAEKAAVAXXXPXXXKXXXXLDRYFYHXXNDQPIDLTKGKXXXXXSLXSXXXSXXXXXXXXXSXXXXXXXXSAVXSFMSNSPLRENALSDISDMLXNLTEXXXXKSXTPXSXSEXXDIXGXTXEXXEXXXPAQKRKGRQSNWNPQHLLILQAQFAXSLRQTXXGKYXMSDLSPQERMHISRFTGXXXXXXXXXXXXXXXXXXXXXGXKFLKNXXXXXXXXXXXXXXXXXXXXSTYXXHLESHXXXRXRDLXKLSXEQXXXQIXXXXXXSXXXXXXXXXXXXGXXXQCKLCXRXXXXXHAVKLHLSKTHGKSPEDHLXXVXELXKX
>TSH3_HUMAN__Q63HK5 RecName: Full=Teashirt homolog 3; AltName: Full=Zinc finger protein 537;
MPRRKQQAPRRAAAYVSEELKAAALVDEGLDPEEHTADGEPSAKYMCPEKELARACPSYQNSPAAEFSCHEMDSESHISETSDRMADFESGSIKNEEETKEVTVPLEDTTVSDSLEQMKAVYNNFLSNSYWSNLNLNLHQPSSEKNNGSSSSSSSSSSSCGSGSFDWHQSAMAKTLQQVSQSRMLPEPSLFSTVQLYRQSSKLYGSIFTGASKFRCKDCSAAYDTLVELTVHMNETGHYRDDNHETDNNNPKRWSKPRKRSLLEMEGKEDAQKVLKCMYCGHSFESLQDLSVHMIKTKHYQKVPLKEPVTPVAAKIIPATRKKASLELELPSSPDSTGGTPKATISDTNDALQKNSNPYITPNNRYGHQNGASYAWHFEARKSQILKCMECGSSHDTLQELTAHMMVTGHFIKVTNSAMKKGKPIVETPVTPTITTLLDEKVQSVPLAATTFTSPSNTPASISPKLNVEVKKEVDKEKAVTDEKPKQKDKPGEEEEKCDISSKYHYLTENDLEESPKGGLDILKSLENTVTSAINKAQNGTPSWGGYPSIHAAYQLPNMMKLSLGSSGKSTPLKPMFGNSEIVSPTKNQTLVSPPSSQTSPMPKTNFHAMEELVKKVTEKVAKVEEKMKEPDGKLSPPKRATPSPCSSEVGEPIKMEASSDGGFRSQENSPSPPRDGCKDGSPLAEPVENGKELVKPLASSLSGSTAIITDHPPEQPFVNPLSALQSVMNIHLGKAAKPSLPALDPMSMLFKMSNSLAEKAAVATPPPLQSKKADHLDRYFYHVNNDQPIDLTKGKSDKGCSLGSVLLSPTSTAPATSSSTVTTAKTSAVVSFMSNSPLRENALSDISDMLKNLTESHTSKSSTPSSISEKSDIDGATLEEAEESTPAQKRKGRQSNWNPQHLLILQAQFAASLRQTSEGKYIMSDLSPQERMHISRFTGLSMTTISHWLANVKYQLRRTGGTKFLKNLDTGHPVFFCNDCASQIRTPSTYISHLESHLGFRLRDLSKLSTEQINSQIAQTKSPSEKMVTSSPEEDLGTSYQCKLCNRTFASKHAVKLHLSKTHGKSPEDHLLYVSELEKQ
Click here and save the page to download this output.
>slimfinder 15120900013 SLiMFinder Motifs motifs
-1---------------------------------P.DLS------------------------------XXXXXXXXXX-2---------------------------------DLS------------------------------
>IKZF1_HUMAN__Q13422 RecName: Full=DNA-binding protein Ikaros; AltName: Full=Ikaros family zinc finger protein 1; AltName: Full=Lymphoid transcription factor LyF-1;
-034-DEGQDMSQVSGKESPPVSDTPDEGDEPMPIPEDLSTTSGGQQSSKSDRVVASNVKVETQSDEEN-XXXXXXXXXX-036-GQDMSQVSGKESPPVSDTPDEGDEPMPIPEDLSTTSGGQQSSKSDRVVASNVKVETQSDEEN-
>TGIF1_HUMAN__Q15583 RecName: Full=Homeobox protein TGIF1; AltName: Full=5'-TG-3'-interacting factor 1;
-153-PAPRRRLLETMKGIVAASGSETEDEDSMDIPLDLSSSAGSGKRRRRGNLPKESVQILRDWLYEH-XXXXXXXXXX-155-PRRRLLETMKGIVAASGSETEDEDSMDIPLDLSSSAGSGKRRRRGNLPKESVQILRDWLYEH-
>NOL4L_HUMAN__Q96MY1 RecName: Full=Nucleolar protein 4-like;
-365-GLNYSYRGYGALSSNLQPPASLQTGNHSNGPTDLSMKGGASTTSTTPTPTPSSTSTSRPVPTAQ-XXXXXXXXXX-367-NYSYRGYGALSSNLQPPASLQTGNHSNGPTDLSMKGGASTTSTTPTPTPSSTSTSRPVPTAQ-
>TSH3_HUMAN__Q63HK5 RecName: Full=Teashirt homolog 3; AltName: Full=Zinc finger protein 537;
----------------------------------------------------------------------XXXXXXXXXX-926-SNWNPQHLLILQAQFAASLRQTSEGKYIMSDLSPQERMHISRFTGLSMTTISHWLANVKYQL-
>HXB5_HUMAN__P09067 RecName: Full=Homeobox protein Hox-B5; AltName: Full=Homeobox protein HHO.C10; AltName: Full=Homeobox protein Hox-2A; AltName: Full=Homeobox protein Hu-1;
----------------------------------------------------------------------XXXXXXXXXX-053-NYGSGSSLSGSYRDPAAMHTGSYGYNYNGMDLSVNRSSASSSHFGAVGESSRAFPAPAQEPR-
>NRIP1_HUMAN__P48552 RecName: Full=Nuclear receptor-interacting protein 1; AltName: Full=Nuclear factor RIP140; AltName: Full=Receptor-interacting protein 140;
-440-TPTTIDEYSDNNPSFTDDSSGDESSYSNCVPIDLSCKHRTEKSESDQPVSLDNFTQSLLNTWDP-XXXXXXXXXX-442-TTIDEYSDNNPSFTDDSSGDESSYSNCVPIDLSCKHRTEKSESDQPVSLDNFTQSLLNTWDP-
>NRIP1_HUMAN__P48552 RecName: Full=Nuclear receptor-interacting protein 1; AltName: Full=Nuclear factor RIP140; AltName: Full=Receptor-interacting protein 140;
----------------------------------------------------------------------XXXXXXXXXX-948-ASESEHRSWARESKSFNVLKQLLLSENCVRDLSPHRSNSVADSKKKGHKNNVTNSKPEFSIS-
>NOL4_HUMAN__O94818 RecName: Full=Nucleolar protein 4; AltName: Full=Nucleolar-localized protein;
-576-YINGNGTYSYHSYRGLGGGLLNLNDASSSGPTDLSMKRQLATSSGSSSSSNSRPQLSPTEINAV-XXXXXXXXXX-375-EARENGSKSPAHSYSSYDSGKNESVDRGAEDLSLNRGDEDEDDHEDHDDSEKVNETDGVEAE-
>NOL4_HUMAN__O94818 RecName: Full=Nucleolar protein 4; AltName: Full=Nucleolar-localized protein;
----------------------------------------------------------------------XXXXXXXXXX-578-NGNGTYSYHSYRGLGGGLLNLNDASSSGPTDLSMKRQLATSSGSSSSSNSRPQLSPTEINAV-
>HIC1_HUMAN__Q14526 RecName: Full=Hypermethylated in cancer 1 protein; Short=Hic-1; AltName: Full=Zinc finger and BTB domain-containing protein 29;
----------------------------------------------------------------------XXXXXXXXXX-243-THCAELYASGPGPAAALCASERRCSPLCGLDLSKKSPPGSAAPERPLAERELPPRPDSPPSA-
>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;
-490-CPQASFDKENAFPFPMDNQFSMNGDCVMDKPLDLSDRFSAIQRQEKSQGSETSKNKFRQVTLYE-XXXXXXXXXX-492-QASFDKENAFPFPMDNQFSMNGDCVMDKPLDLSDRFSAIQRQEKSQGSETSKNKFRQVTLYE-
>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;
----------------------------------------------------------------------XXXXXXXXXX-662-NPCRTGKIKSLQNNQDVSFENIQWSIDPGADLSQYKMDVTVIDTKDGSQSKLGGETVDMDCT-
Click here and save the page to download this output.
>slimfinder 15120900013 SLiMFinder Motifs motifs
-1---------------------------------P.DLS------------------------------XXXXXXXXXX-2---------------------------------DLS------------------------------
>IKZF1_HUMAN__Q13422 RecName: Full=DNA-binding protein Ikaros; AltName: Full=Ikaros family zinc finger protein 1; AltName: Full=Lymphoid transcription factor LyF-1;
-034-DEXQDXXXXSGXXSPXXXXXXDXXDEPMPIPEDLSTXXXXQQXXXXXXXXXXNXKXEXXSDEEN-XXXXXXXXXX-036-XQDXXXXSGXXSPXXXXXXDXXDEPMPIPEDLSTXXXXQQXXXXXXXXXXNXKXEXXSDEEN-
>TGIF1_HUMAN__Q15583 RecName: Full=Homeobox protein TGIF1; AltName: Full=5'-TG-3'-interacting factor 1;
-153-XXXXXXXXXXMXGIXAXSGSETEDXDXMDXPLDLSSXXXXGKRXRRGNLPKESVQILRDWLXXH-XXXXXXXXXX-155-XXXXXXXXMXGIXAXSGSETEDXDXMDXPLDLSSXXXXGKRXRRGNLPKESVQILRDWLXXH-
>NOL4L_HUMAN__Q96MY1 RecName: Full=Nucleolar protein 4-like;
-365-GLXYSYRGYGXXXXXXQXXASLXTGXHXNGPTDLSMKGXAXXXXXXXXXXXXXXXTXRXXPXXQ-XXXXXXXXXX-367-XYSYRGYGXXXXXXQXXASLXTGXHXNGPTDLSMKGXAXXXXXXXXXXXXXXXTXRXXPXXQ-
>TSH3_HUMAN__Q63HK5 RecName: Full=Teashirt homolog 3; AltName: Full=Zinc finger protein 537;
----------------------------------------------------------------------XXXXXXXXXX-926-SNWNPQHLLILQAQFAXSLRQTXXGKYXMSDLSPQERMHISRFTGXXXXXXXXXXXXXXXXX-
>HXB5_HUMAN__P09067 RecName: Full=Homeobox protein Hox-B5; AltName: Full=Homeobox protein HHO.C10; AltName: Full=Homeobox protein Hox-2A; AltName: Full=Homeobox protein Hu-1;
----------------------------------------------------------------------XXXXXXXXXX-053-NYGXXXXXXXSYRXXXXMHXXXYGYNYNGMDLSXNRXXXSXXHFGAVGXXXRXFXXXXQEXR-
>NRIP1_HUMAN__P48552 RecName: Full=Nuclear receptor-interacting protein 1; AltName: Full=Nuclear factor RIP140; AltName: Full=Receptor-interacting protein 140;
-440-TPTTXDEXSDXNPSFTXDSSXDESSXSXCXPIDLSXKXRXXKXXXXXXXSLDNFTQSLLNXWDP-XXXXXXXXXX-442-TTXDEXSDXNPSFTXDSSXDESSXSXCXPIDLSXKXRXXKXXXXXXXSLDNFTQSLLNXWDP-
>NRIP1_HUMAN__P48552 RecName: Full=Nuclear receptor-interacting protein 1; AltName: Full=Nuclear factor RIP140; AltName: Full=Receptor-interacting protein 140;
----------------------------------------------------------------------XXXXXXXXXX-948-XXXXXXXXWXRESKSFNVLKQLLLSENCVRDLSPXRXXXXXXXXXKGXXXXXXXXKPEFSIS-
>NOL4_HUMAN__O94818 RecName: Full=Nucleolar protein 4; AltName: Full=Nucleolar-localized protein;
-576-YINGXXXXXXXXYXXLXXXLXNXXXXXXSGPTDLSMKXXXXXXXXXXSXXXXXXQLSPXEXXAV-XXXXXXXXXX-375-XAXEXXXKSPAHSXXSYXSXKXEXXXXXXEDLSXXRXDXDXDXHXXXXDXXKXNXXXGXXXE-
>NOL4_HUMAN__O94818 RecName: Full=Nucleolar protein 4; AltName: Full=Nucleolar-localized protein;
----------------------------------------------------------------------XXXXXXXXXX-578-NGXXXXXXXXYXXLXXXLXNXXXXXXSGPTDLSMKXXXXXXXXXXSXXXXXXQLSPXEXXAV-
>HIC1_HUMAN__Q14526 RecName: Full=Hypermethylated in cancer 1 protein; Short=Hic-1; AltName: Full=Zinc finger and BTB domain-containing protein 29;
----------------------------------------------------------------------XXXXXXXXXX-243-THCAELYAXXXXXXXXLXXXXXXXXXXCGLDLSKKSPXXXXXXXXXXXEXXLPXRXDSPPXX-
>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;
-490-CXXXSFDKENXXPFXXXXXXXXNGXXXXDKPLDLSDRFXXXXXQEKXXGXEXXKXXXXQXTXYE-XXXXXXXXXX-492-XXSFDKENXXPFXXXXXXXXNGXXXXDKPLDLSDRFXXXXXQEKXXGXEXXKXXXXQXTXYE-
>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;
----------------------------------------------------------------------XXXXXXXXXX-662-NXCRXXKXXXXXXXXDXXXENXQWSXDPGADLSQYKMDXTVXDXKXXSXXXXXGEXXDMDXT-
Click here and save the page to download this output.
>BCAS3_HUMAN__Q9H6U6 RecName: Full=Breast carcinoma-amplified sequence 3 {ECO:0000312|HGNC:HGNC:14347, ECO:0000312|MIM:607470}; AltName: Full=GAOB1;
MNEAMATDSPRRPSRCTGGVVVRPQAVTEQSYMESVVTFLQDVVPQAYSGTPLTEEKEKIVWVRFENADLNDTSRNLEFHEIHSTGNEPPLLIMIGYSDGMQVWSIPISGEAQELFSVRHGPIRAARILPAPQFGAQKCDNFAEKRPLLGVCKSIGSSGTSPPYCCVDLYSLRTGEMVKSIQFKTPIYDLHCNKRILVVVLQEKIAAFDSCTFTKKFFVTSCYPCPGPNMNPIALGSRWLAYAENKLIRCHQSRGGACGDNIQSYTATVISAAKTLKSGLTMVGKVVTQLTGTLPSGVTEDDVAIHSNSRRSPLVPGIITVIDTETVGEGQVLVSEDSDSDGIVAHFPAHEKPVCCMAFNTSGMLLVTTDTLGHDFHVFQILTHPWSSSQCAVHHLYTLHRGETEAKVQDICFSHDCRWVVVSTLRGTSHVFPINPYGGQPCVRTHMSPRVVNRMSRFQKSAGLEEIEQELTSKQGGRCSPVPGLSSSPSGSPLHGKLNSQDSYNNFTNNNPGNPRLSPLPSLMVVMPLAQIKQPMTLGTITKRTGPYLFGAGCFSIKAPCKVKPPPQISPSKSMGGEFCVAAIFGTSRSWFANNAGLKREKDQSKQVVVESLYIISCYGTLVEHMMEPRPLSTAPKISDDTPLEMMTSPRASWTLVRTPQWNELQPPFNANHPLLLAADAVQYYQFLLAGLVPPGSPGPITRHGSYDSLASDHSGQEDEEWLSQVEIVTHTGPHRRLWMGPQFQFKTIHPSGQTTVISSSSSVLQSHGPSDTPQPLLDFDTDDLDLNSLRIQPVRSDPVSMPGSSRPVSDRRGVSTVIDAASGTFDRSVTLLEVCGSWPEGFGLRHMSSMEHTEEGLRERLADAMAESPSRDVVGSGTELQREGSIETLSNSSGSTSGSIPRNFDGYRSPLPTNESQPLSLFPTGFP
>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
>DMRTB_HUMAN__Q96MA1 RecName: Full=Doublesex- and mab-3-related transcription factor B1;
MADKMVRTPKCSRCRNHGFLVPVKGHAGKCRWKQCLCEKCYLISERQKIMAAQKVLKTQAAEEEQEAALCAQGPKQASGAAAAAPAPVPVPAASLRPLSPGTPSGDADPGPEGRAAACFFEQPPRGRNPGPRALQPVLGGRSHVEPSERAAVAMPSLAGPPFGAEAAGSGYPGPLDLRRPMRTVPGPLFTDFVRPLNINPDRALGPEYPGGSSMHPYCPFPLGYLDAPPGVPLQQGFRHVSRSQYQGGGLVSEPGGDFQPSYYLPPPPPPLPPLPPLPPQPQFLPPGYLSALHFLPPPPPPPPPSSFSLTVLFDTDKENTDDQDAEVLSGEPSQPSSQEQSD
>FOXP2_HUMAN__O15409 RecName: Full=Forkhead box protein P2; AltName: Full=CAG repeat protein 44; AltName: Full=Trinucleotide repeat-containing gene 10 protein;
MMQESATETISNSSMNQNGMSTLSSQLDAGSRDGRSSGDTSSEVSTVELLHLQQQQALQAARQLLLQQQTSGLKSPKSSDKQRPLQVPVSVAMMTPQVITPQQMQQILQQQVLSPQQLQALLQQQQAVMLQQQQLQEFYKKQQEQLHLQLLQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQHPGKQAKEQQQQQQQQQQLAAQQLVFQQQLLQMQQLQQQQHLLSLQRQGLISIPPGQAALPVQSLPQAGLSPAEIQQLWKEVTGVHSMEDNGIKHGGLDLTTNNSSSTTSSNTSKASPPITHHSIVNGQSSVLSARRDSSSHEETGASHTLYGHGVCKWPGCESICEDFGQFLKHLNNEHALDDRSTAQCRVQMQVVQQLEIQLSKERERLQAMMTHLHMRPSEPKPSPKPLNLVSSVTMSKNMLETSPQSLPQTPTTPTAPVTPITQGPSVITPASVPNVGAIRRRHSDKYNIPMSSEIAPNYEFYKNADVRPPFTYATLIRQAIMESSDRQLTLNEIYSWFTRTFAYFRRNAATWKNAVRHNLSLHKCFVRVENVKGAVWTVDEVEYQKRRSQKITGSPTLVKNIPTSLGYGAALNASLQAALAESSLPLLSNPGLINNASSGLLQAVHEDLNGSLDHIDSNGNSSPGCSPQPHIHSIHVKEEPVIAEDEDCPMSLVTTANHSPELEDDREIEEEPLSEDLE
>HIC1_HUMAN__Q14526 RecName: Full=Hypermethylated in cancer 1 protein; Short=Hic-1; AltName: Full=Zinc finger and BTB domain-containing protein 29;
MTFPEADILLKSGECAGQTMLDTMEAPGHSRQLLLQLNNQRTKGFLCDVIIVVQNALFRAHKNVLAASSAYLKSLVVHDNLLNLDHDMVSPAVFRLVLDFIYTGRLADGAEAAAAAAVAPGAEPSLGAVLAAASYLQIPDLVALCKKRLKRHGKYCHLRGGGGGGGGYAPYGRPGRGLRAATPVIQACYPSPVGPPPPPAAEPPSGPEAAVNTHCAELYASGPGPAAALCASERRCSPLCGLDLSKKSPPGSAAPERPLAERELPPRPDSPPSAGPAAYKEPPLALPSLPPLPFQKLEEAAPPSDPFRGGSGSPGPEPPGRPDGPSLLYRWMKHEPGLGSYGDELGRERGSPSERCEERGGDAAVSPGGPPLGLAPPPRYPGSLDGPGAGGDGDDYKSSSEETGSSEDPSPPGGHLEGYPCPHLAYGEPESFGDNLYVCIPCGKGFPSSEQLNAHVEAHVEEEEALYGRAEAAEVAAGAAGLGPPFGGGGDKVAGAPGGLGELLRPYRCASCDKSYKDPATLRQHEKTHWLTRPYPCTICGKKFTQRGTMTRHMRSHLGLKPFACDACGMRFTRQYRLTEHMRIHSGEKPYECQVCGGKFAQQRNLISHMKMHAVGGAAGAAGALAGLGGLPGVPGPDGKGKLDFPEGVFAVARLTAEQLSLKQQDKAAAAELLAQTTHFLHDPKVALESLYPLAKFTAELGLSPDKAAEVLSQGAHLAAGPDGRTIDRFSPT
>HXB5_HUMAN__P09067 RecName: Full=Homeobox protein Hox-B5; AltName: Full=Homeobox protein HHO.C10; AltName: Full=Homeobox protein Hox-2A; AltName: Full=Homeobox protein Hu-1;
MSSYFVNSFSGRYPNGPDYQLLNYGSGSSLSGSYRDPAAMHTGSYGYNYNGMDLSVNRSSASSSHFGAVGESSRAFPAPAQEPRFRQAASSCSLSSPESLPCTNGDSHGAKPSASSPSDQATSASSSANFTEIDEASASSEPEEAASQLSSPSLARAQPEPMATSTAAPEGQTPQIFPWMRKLHISHDMTGPDGKRARTAYTRYQTLELEKEFHFNRYLTRRRRIEIAHALCLSERQIKIWFQNRRMKWKKDNKLKSMSLATAGSAFQP
>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
>NOL4L_HUMAN__Q96MY1 RecName: Full=Nucleolar protein 4-like;
MSDSTWMSADPHLASSLSPSQDERMRSPQNLHSQEDDDSSSESGSGNGSSTLNPSTSSSTQGDPAFPEMNGNGAVAPMDFTTAAEDQPINLCDKLPPATALGTASYPSDGCGADGLRSRVKYGVKTTPESPPYSSGSYDSIKTEVSGCPEDLTVGRAPTADDDDDDHDDHEDNDKMNDSEGMDPERLKAFNMFVRLFVDENLDRMVPISKQPKEKIQAIIESCSRQFPEFQERARKRIRTYLKSCRRMKKNGMEMTRPTPPHLTSAMAENILAAACESETRKAAKRMRLEIYQSSQDEPIALDKQHSRDSAAITHSTYSLPASSYSQDPVYANGGLNYSYRGYGALSSNLQPPASLQTGNHSNGPTDLSMKGGASTTSTTPTPTPSSTSTSRPVPTAQLSPTEISAVRQLIAGYRESAAFLLRSADELENLILQQN
>NOL4_HUMAN__O94818 RecName: Full=Nucleolar protein 4; AltName: Full=Nucleolar-localized protein;
MESERDMYRQFQDWCLRTYGDSGKTKTVTRKKYERIVQLLNGSESSSTDNAKFKFWVKSKGFQLGQPDEVRGGGGGAKQVLYVPVKTTDGVGVDEKLSLRRVAVVEDFFDIIYSMHVETGPNGEQIRKHAGQKRTYKAISESYAFLPREAVTRFLMSCSECQKRMHLNPDGTDHKDNGKPPTLVTSMIDYNMPITMAYMKHMKLQLLNSQQDEDESSIESDEFDMSDSTRMSAVNSDLSSNLEERMQSPQNLHGQQDDDSAAESFNGNETLGHSSIASGGTHSREMGDSNSDGKTGLEQDEQPLNLSDSPLSAQLTSEYRIDDHNSNGKNKYKNLLISDLKMEREARENGSKSPAHSYSSYDSGKNESVDRGAEDLSLNRGDEDEDDHEDHDDSEKVNETDGVEAERLKAFNMFVRLFVDENLDRMVPISKQPKEKIQAIIDSCRRQFPEYQERARKRIRTYLKSCRRMKRSGFEMSRPIPSHLTSAVAESILASACESESRNAAKRMRLERQQDESAPADKQCKPEATQATYSTSAVPGSQDVLYINGNGTYSYHSYRGLGGGLLNLNDASSSGPTDLSMKRQLATSSGSSSSSNSRPQLSPTEINAVRQLVAGYRESAAFLLRSADELENLILQQN
>NRIP1_HUMAN__P48552 RecName: Full=Nuclear receptor-interacting protein 1; AltName: Full=Nuclear factor RIP140; AltName: Full=Receptor-interacting protein 140;
MTHGEELGSDVHQDSIVLTYLEGLLMHQAAGGSGTAVDKKSAGHNEEDQNFNISGSAFPTCQSNGPVLNTHTYQGSGMLHLKKARLLQSSEDWNAAKRKRLSDSIMNLNVKKEALLAGMVDSVPKGKQDSTLLASLLQSFSSRLQTVALSQQIRQSLKEQGYALSHDSLKVEKDLRCYGVASSHLKTLLKKSKVKDQKPDTNLPDVTKNLIRDRFAESPHHVGQSGTKVMSEPLSCAARLQAVASMVEKRASPATSPKPSVACSQLALLLSSEAHLQQYSREHALKTQNANQAASERLAAMARLQENGQKDVGSYQLPKGMSSHLNGQARTSSSKLMASKSSATVFQNPMGIIPSSPKNAGYKNSLERNNIKQAANNSLLLHLLKSQTIPKPMNGHSHSERGSIFEESSTPTTIDEYSDNNPSFTDDSSGDESSYSNCVPIDLSCKHRTEKSESDQPVSLDNFTQSLLNTWDPKVPDVDIKEDQDTSKNSKLNSHQKVTLLQLLLGHKNEENVEKNTSPQGVHNDVSKFNTQNYARTSVIESPSTNRTTPVSTPPLLTSSKAGSPINLSQHSLVIKWNSPPYVCSTQSEKLTNTASNHSMDLTKSKDPPGEKPAQNEGAQNSATFSASKLLQNLAQCGMQSSMSVEEQRPSKQLLTGNTDKPIGMIDRLNSPLLSNKTNAVEENKAFSSQPTGPEPGLSGSEIENLLERRTVLQLLLGNPNKGKSEKKEKTPLRDESTQEHSERALSEQILMVKIKSEPCDDLQIPNTNVHLSHDAKSAPFLGMAPAVQRSAPALPVSEDFKSEPVSPQDFSFSKNGLLSRLLRQNQDSYLADDSDRSHRNNEMALLESKNLCMVPKKRKLYTEPLENPFKKMKNNIVDAANNHSAPEVLYGSLLNQEELKFSRNDLEFKYPAGHGSASESEHRSWARESKSFNVLKQLLLSENCVRDLSPHRSNSVADSKKKGHKNNVTNSKPEFSISSLNGLMYSSTQPSSCMDNRTFSYPGVVKTPVSPTFPEHLGCAGSRPESGLLNGCSMPSEKGPIKWVITDAEKNEYEKDSPRLTKTNPILYYMLQKGGNSVTSRETQDKDIWREASSAESVSQVTAKEELLPTAETKASFFNLRSPYNSHMGNNASRPHSANGEVYGLLGSVLTIKKESE
>PLCB1_HUMAN__Q9NQ66 RecName: Full=1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-1; EC=3.1.4.11; AltName: Full=PLC-154; AltName: Full=Phosphoinositide phospholipase C-beta-1; AltName: Full=Phospholipase C-I; Short=PLC-I; AltName: Full=Phospholipase C-beta-1; Short=PLC-beta-1;
MAGAQPGVHALQLKPVCVSDSLKKGTKFVKWDDDSTIVTPIILRTDPQGFFFYWTDQNKETELLDLSLVKDARCGRHAKAPKDPKLRELLDVGNIGRLEQRMITVVYGPDLVNISHLNLVAFQEEVAKEWTNEVFSLATNLLAQNMSRDAFLEKAYTKLKLQVTPEGRIPLKNIYRLFSADRKRVETALEACSLPSSRNDSIPQEDFTPEVYRVFLNNLCPRPEIDNIFSEFGAKSKPYLTVDQMMDFINLKQRDPRLNEILYPPLKQEQVQVLIEKYEPNNSLARKGQISVDGFMRYLSGEENGVVSPEKLDLNEDMSQPLSHYFINSSHNTYLTAGQLAGNSSVEMYRQVLLSGCRCVELDCWKGRTAEEEPVITHGFTMTTEISFKEVIEAIAECAFKTSPFPILLSFENHVDSPKQQAKMAEYCRLIFGDALLMEPLEKYPLESGVPLPSPMDLMYKILVKNKKKSHKSSEGSGKKKLSEQASNTYSDSSSMFEPSSPGAGEADTESDDDDDDDDCKKSSMDEGTAGSEAMATEEMSNLVNYIQPVKFESFEISKKRNKSFEMSSFVETKGLEQLTKSPVEFVEYNKMQLSRIYPKGTRVDSSNYMPQLFWNAGCQMVALNFQTMDLAMQINMGMYEYNGKSGYRLKPEFMRRPDKHFDPFTEGIVDGIVANTLSVKIISGQFLSDKKVGTYVEVDMFGLPVDTRRKAFKTKTSQGNAVNPVWEEEPIVFKKVVLPTLACLRIAVYEEGGKFIGHRILPVQAIRPGYHYICLRNERNQPLTLPAVFVYIEVKDYVPDTYADVIEALSNPIRYVNLMEQRAKQLAALTLEDEEEVKKEADPGETPSEAPSEARTTPAENGVNHTTTLTPKPPSQALHSQPAPGSVKAPAKTEDLIQSVLTEVEAQTIEELKQQKSFVKLQKKHYKEMKDLVKRHHKKTTDLIKEHTTKYNEIQNDYLRRRAALEKSAKKDSKKKSEPSSPDHGSSTIEQDLAALDAEMTQKLIDLKDKQQQQLLNLRQEQYYSEKYQKREHIKLLIQKLTDVAEECQNNQLKKLKEICEKEKKELKKKMDKKRQEKITEAKSKDKSQMEEEKTEMIRSYIQEVVQYIKRLEEAQSKRQEKLVEKHKEIRQQILDEKPKLQVELEQEYQDKFKRLPLEILEFVQEAMKGKISEDSNHGSAPLSLSSDPGKVNHKTPSSEELGGDIPGKEFDTPL
>TGIF1_HUMAN__Q15583 RecName: Full=Homeobox protein TGIF1; AltName: Full=5'-TG-3'-interacting factor 1;
MVLAQSRVSAGVGSPHCSGSGGGGSDSFPWPASHPGNPQCSFSTAFLASPRLSRGTLAYLPPAPWSSLATPSALLGSSCAPPPPPARCPQPRALSPELGTKAGPRRPHRWELPRSPSQGAQGPAPRRRLLETMKGIVAASGSETEDEDSMDIPLDLSSSAGSGKRRRRGNLPKESVQILRDWLYEHRYNAYPSEQEKALLSQQTHLSTLQVCNWFINARRRLLPDMLRKDGKDPNQFTISRRGAKISETSSVESVMGIKNFMPALEETPFHSCTAGPNPTLGRPLSPKPSSPGSVLARPSVICHTTVTALKDVPFSLCQSVGVGQNTDIQQIAAKNFTDTSLMYPEDTCKSGPSTNTQSGLFNTPPPTPPDLNQDFSGFQLLVDVALKRAAEMELQAKLTA
>TSH3_HUMAN__Q63HK5 RecName: Full=Teashirt homolog 3; AltName: Full=Zinc finger protein 537;
MPRRKQQAPRRAAAYVSEELKAAALVDEGLDPEEHTADGEPSAKYMCPEKELARACPSYQNSPAAEFSCHEMDSESHISETSDRMADFESGSIKNEEETKEVTVPLEDTTVSDSLEQMKAVYNNFLSNSYWSNLNLNLHQPSSEKNNGSSSSSSSSSSSCGSGSFDWHQSAMAKTLQQVSQSRMLPEPSLFSTVQLYRQSSKLYGSIFTGASKFRCKDCSAAYDTLVELTVHMNETGHYRDDNHETDNNNPKRWSKPRKRSLLEMEGKEDAQKVLKCMYCGHSFESLQDLSVHMIKTKHYQKVPLKEPVTPVAAKIIPATRKKASLELELPSSPDSTGGTPKATISDTNDALQKNSNPYITPNNRYGHQNGASYAWHFEARKSQILKCMECGSSHDTLQELTAHMMVTGHFIKVTNSAMKKGKPIVETPVTPTITTLLDEKVQSVPLAATTFTSPSNTPASISPKLNVEVKKEVDKEKAVTDEKPKQKDKPGEEEEKCDISSKYHYLTENDLEESPKGGLDILKSLENTVTSAINKAQNGTPSWGGYPSIHAAYQLPNMMKLSLGSSGKSTPLKPMFGNSEIVSPTKNQTLVSPPSSQTSPMPKTNFHAMEELVKKVTEKVAKVEEKMKEPDGKLSPPKRATPSPCSSEVGEPIKMEASSDGGFRSQENSPSPPRDGCKDGSPLAEPVENGKELVKPLASSLSGSTAIITDHPPEQPFVNPLSALQSVMNIHLGKAAKPSLPALDPMSMLFKMSNSLAEKAAVATPPPLQSKKADHLDRYFYHVNNDQPIDLTKGKSDKGCSLGSVLLSPTSTAPATSSSTVTTAKTSAVVSFMSNSPLRENALSDISDMLKNLTESHTSKSSTPSSISEKSDIDGATLEEAEESTPAQKRKGRQSNWNPQHLLILQAQFAASLRQTSEGKYIMSDLSPQERMHISRFTGLSMTTISHWLANVKYQLRRTGGTKFLKNLDTGHPVFFCNDCASQIRTPSTYISHLESHLGFRLRDLSKLSTEQINSQIAQTKSPSEKMVTSSPEEDLGTSYQCKLCNRTFASKHAVKLHLSKTHGKSPEDHLLYVSELEKQ
Click here and save the page to download this output.
ID BCAS3_HUMAN Reviewed; 928 AA.
AC Q9H6U6; Q17RM0; Q6KF21; Q8IXI6; Q8NDR8; Q8TDL9; Q8TDM1; Q8WY55;
AC Q9BVF0; Q9H957; Q9H9Y9; Q9NXP4;
DT 25-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 3.
DT 11-NOV-2015, entry version 130.
DE RecName: Full=Breast carcinoma-amplified sequence 3 {ECO:0000312|HGNC:HGNC:14347, ECO:0000312|MIM:607470};
DE AltName: Full=GAOB1;
GN Name=BCAS3 {ECO:0000312|HGNC:HGNC:14347, ECO:0000312|MIM:607470};
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), TISSUE SPECIFICITY,
RP CHROMOSOMAL TRANSLOCATION WITH BCAS4, AND VARIANT SER-87.
RC TISSUE=Liver;
RX PubMed=12378525; DOI=10.1002/gcc.10121;
RA Baerlund M., Monni O., Weaver J.D., Kauraniemi P., Sauter G.,
RA Heiskanen M., Kallioniemi O.-P., Kallioniemi A.;
RT "Cloning of BCAS3 (17q23) and BCAS4 (20q13) genes that undergo
RT amplification, overexpression, and fusion in breast cancer.";
RL Genes Chromosomes Cancer 35:311-317(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 5 AND 6),
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 478-928 (ISOFORM 3), AND
RP VARIANT SER-87.
RC TISSUE=Colon;
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT SER-87.
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 1), AND VARIANT
RP SER-87.
RC TISSUE=Brain, and Cervix;
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 1-433 (ISOFORM 6), AND PARTIAL
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
RA Bauer M.;
RT "Cloning and sequencing of a new isoform similar to FLJ20128 and
RT BCAS3.";
RL Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 475-928 (ISOFORM 4).
RC TISSUE=Brain;
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 [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 510-928 (ISOFORMS 1/6).
RA Wu G., Couch F.J.;
RT "Five novel genes from 17q23 amplicon have different amplification and
RT overexpression frequency in breast cancer.";
RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=16617102; DOI=10.1073/pnas.0601989103;
RA Gururaj A.E., Singh R.R., Rayala S.K., Holm C., den Hollander P.,
RA Zhang H., Balasenthil S., Talukder A.H., Landberg G., Kumar R.;
RT "MTA1, a transcriptional activator of breast cancer amplified sequence
RT 3.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:6670-6675(2006).
RN [10]
RP ERRATUM.
RA Gururaj A.E., Singh R.R., Rayala S.K., Holm C., den Hollander P.,
RA Zhang H., Balasenthil S., Talukder A.H., Landberg G., Kumar R.;
RL Proc. Natl. Acad. Sci. U.S.A. 110:4147-4148(2013).
RN [11]
RP FUNCTION, INTERACTION WITH HISTONE H3; ESR1; KAT2B AND PELP1,
RP SUBCELLULAR LOCATION, AND CHROMATIN-BINDING.
RX PubMed=17505058; DOI=10.1210/me.2006-0514;
RA Gururaj A.E., Peng S., Vadlamudi R.K., Kumar R.;
RT "Estrogen induces expression of BCAS3, a novel estrogen receptor-alpha
RT coactivator, through proline-, glutamic acid-, and leucine-rich
RT protein-1 (PELP1).";
RL Mol. Endocrinol. 21:1847-1860(2007).
RN [12]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=18030336; DOI=10.1371/journal.pone.0001202;
RA Siva K., Venu P., Mahadevan A., Shankar S.K., Inamdar M.S.;
RT "Human BCAS3 expression in embryonic stem cells and vascular
RT precursors suggests a role in human embryogenesis and tumor
RT angiogenesis.";
RL PLoS ONE 2:E1202-E1202(2007).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-480, 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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-886, 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 [15]
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 [16]
RP INTERACTION WITH BETA-TUBULIN AND VIM.
RX PubMed=22300583; DOI=10.1016/j.yexcr.2012.01.016;
RA Jain M., Bhat G.P., Vijayra havan K., Inamdar M.S.;
RT "Rudhira/BCAS3 is a cytoskeletal protein that controls Cdc42
RT activation and directional cell migration during angiogenesis.";
RL Exp. Cell Res. 318:753-767(2012).
RN [17]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [18]
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: Plays a role in angiogenesis. Participates in the
CC regulation of cell polarity and directional endothelial cell
CC migration by mediating both the activation and recruitment of
CC CDC42 and the reorganization of the actin cytoskeleton at the cell
CC leading edge. Promotes filipodia formation (By similarity).
CC Functions synergistically with PELP1 as a transcriptional
CC coactivator of estrogen receptor-responsive genes. Stimulates
CC histone acetyltransferase activity. Binds to chromatin.
CC {ECO:0000250|UniProtKB:Q8CCN5, ECO:0000269|PubMed:17505058}.
CC -!- SUBUNIT: Interacts with histone H3, ESR1, KAT2B and PELP1; the
CC interactions occur in a estrogen-dependent manner. Interacts with
CC beta-tubulin and VIM. {ECO:0000269|PubMed:17505058,
CC ECO:0000269|PubMed:22300583}.
CC -!- INTERACTION:
CC Q9BSU1:C16orf70; NbExp=3; IntAct=EBI-10307911, EBI-946080;
CC Q9UJX2:CDC23; NbExp=3; IntAct=EBI-6083685, EBI-396137;
CC Q13363-2:CTBP1; NbExp=3; IntAct=EBI-6083685, EBI-10171858;
CC Q8IY44:CTBP2; NbExp=3; IntAct=EBI-6083685, EBI-10171902;
CC P08670:VIM; NbExp=3; IntAct=EBI-6083685, EBI-353844;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16617102,
CC ECO:0000269|PubMed:17505058}. Cytoplasm
CC {ECO:0000269|PubMed:16617102, ECO:0000269|PubMed:17505058,
CC ECO:0000269|PubMed:18030336}. Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q8CCN5}. Note=Localizes in the cytoplasm in
CC stationary cells. Translocates from the cytoplasm to the leading
CC edge in motile cells. Colocalizes with microtubules and
CC intermediate filaments in both stationary and motile cells (By
CC similarity). Associates with chromatin. Recruited to estrogen
CC receptor-induced promoters in a PELP1-dependent manner.
CC {ECO:0000250|UniProtKB:Q8CCN5, ECO:0000269|PubMed:17505058}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=2;
CC IsoId=Q9H6U6-1; Sequence=Displayed;
CC Name=1;
CC IsoId=Q9H6U6-2; Sequence=VSP_007858;
CC Name=3;
CC IsoId=Q9H6U6-3; Sequence=VSP_007858, VSP_007860;
CC Name=4;
CC IsoId=Q9H6U6-8; Sequence=VSP_007860;
CC Name=5; Synonyms=Maaab1;
CC IsoId=Q9H6U6-7; Sequence=VSP_007858, VSP_040113;
CC Note=No experimental confirmation available. Ref.2 (AK225757)
CC sequence differs from that shown due to a frameshift in position
CC 895. Ref.4 (CAD54076) sequence differs from that shown due to a
CC frameshift in position 894. Ref.4 (CAD54076) sequence is in
CC conflict in position: 891:G->R. {ECO:0000305};
CC Name=6; Synonyms=Maaab2;
CC IsoId=Q9H6U6-6; Sequence=VSP_040112, VSP_007858;
CC -!- TISSUE SPECIFICITY: Expressed in stomach, liver, lung, kidney,
CC prostate, testis, thyroid gland, adrenal gland, brain, heart,
CC skeletal muscle, colon, spleen, small intestine, placenta, blood
CC leukocyte and mammary epithelial cells. Expressed in
CC undifferentiated ES cells. Expressed in blood islands and nascent
CC blood vessels derived from differentiated ES cells into embryoid
CC bodies (BD). Expressed in endothelial cells. Not detected in
CC brain. Expressed in brain tumors (at protein level). Expressed in
CC brain. Highly expressed in breast cancers and in glioma cell
CC lines. {ECO:0000269|PubMed:12378525, ECO:0000269|PubMed:16617102,
CC ECO:0000269|PubMed:18030336}.
CC -!- DEVELOPMENTAL STAGE: Fetal.
CC -!- INDUCTION: By estrogen. {ECO:0000269|PubMed:16617102}.
CC -!- DISEASE: Note=A chromosomal aberration involving BCAS3 has been
CC found in some breast carcinoma cell lines. Translocation
CC t(17;20)(q23;q13) with BCAS4.
CC -!- SIMILARITY: Belongs to the WD repeat BCAS3 family. {ECO:0000305}.
CC -!- SIMILARITY: Contains 7 WD repeats. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF70324.1; Type=Frameshift; Positions=693; Evidence={ECO:0000305};
CC Sequence=AAL99634.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAA90966.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
CC Sequence=BAB14078.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC and Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/BCAS3ID766.html";
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AF361219; AAL99632.1; -; mRNA.
DR EMBL; AF361221; AAL99634.1; ALT_INIT; mRNA.
DR EMBL; AK000135; BAA90966.1; ALT_INIT; mRNA.
DR EMBL; AK022526; BAB14078.1; ALT_INIT; mRNA.
DR EMBL; AK023054; BAB14380.1; -; mRNA.
DR EMBL; AK025510; BAB15156.1; -; mRNA.
DR EMBL; AK225757; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AC005746; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC005856; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC005884; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC015876; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC079005; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC110602; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471179; EAW51414.1; -; Genomic_DNA.
DR EMBL; BC001250; AAH01250.2; -; mRNA.
DR EMBL; BC117275; AAI17276.1; -; mRNA.
DR EMBL; BC143386; AAI43387.1; -; mRNA.
DR EMBL; AJ511332; CAD54076.1; ALT_FRAME; mRNA.
DR EMBL; AJ518105; CAD57723.1; -; mRNA.
DR EMBL; AL831895; CAD38568.1; -; mRNA.
DR EMBL; AF260268; AAF70324.1; ALT_FRAME; mRNA.
DR CCDS; CCDS11626.1; -. [Q9H6U6-2]
DR CCDS; CCDS45749.1; -. [Q9H6U6-1]
DR RefSeq; NP_001092902.1; NM_001099432.1. [Q9H6U6-1]
DR RefSeq; NP_060149.3; NM_017679.3. [Q9H6U6-2]
DR RefSeq; XP_005257529.1; XM_005257472.1. [Q9H6U6-8]
DR RefSeq; XP_005257532.1; XM_005257475.1. [Q9H6U6-7]
DR RefSeq; XP_011523254.1; XM_011524952.1. [Q9H6U6-6]
DR UniGene; Hs.655028; -.
DR ProteinModelPortal; Q9H6U6; -.
DR SMR; Q9H6U6; 348-381.
DR BioGrid; 120182; 15.
DR IntAct; Q9H6U6; 19.
DR STRING; 9606.ENSP00000375067; -.
DR PhosphoSite; Q9H6U6; -.
DR BioMuta; BCAS3; -.
DR DMDM; 313104248; -.
DR MaxQB; Q9H6U6; -.
DR PaxDb; Q9H6U6; -.
DR PRIDE; Q9H6U6; -.
DR Ensembl; ENST00000390652; ENSP00000375067; ENSG00000141376. [Q9H6U6-1]
DR Ensembl; ENST00000407086; ENSP00000385323; ENSG00000141376. [Q9H6U6-2]
DR Ensembl; ENST00000408905; ENSP00000386173; ENSG00000141376. [Q9H6U6-3]
DR Ensembl; ENST00000588462; ENSP00000468592; ENSG00000141376. [Q9H6U6-8]
DR Ensembl; ENST00000588874; ENSP00000464825; ENSG00000141376. [Q9H6U6-6]
DR Ensembl; ENST00000589222; ENSP00000466078; ENSG00000141376. [Q9H6U6-7]
DR GeneID; 54828; -.
DR KEGG; hsa:54828; -.
DR UCSC; uc002iyu.4; human. [Q9H6U6-2]
DR UCSC; uc002iyv.4; human. [Q9H6U6-1]
DR UCSC; uc002iyw.4; human. [Q9H6U6-7]
DR UCSC; uc002iyy.4; human. [Q9H6U6-6]
DR UCSC; uc002iyz.4; human. [Q9H6U6-8]
DR UCSC; uc002iza.4; human. [Q9H6U6-3]
DR CTD; 54828; -.
DR GeneCards; BCAS3; -.
DR H-InvDB; HIX0021877; -.
DR HGNC; HGNC:14347; BCAS3.
DR HPA; HPA052409; -.
DR MIM; 607470; gene.
DR neXtProt; NX_Q9H6U6; -.
DR PharmGKB; PA25286; -.
DR eggNOG; KOG2109; Eukaryota.
DR eggNOG; KOG4415; Eukaryota.
DR eggNOG; ENOG410XSW7; LUCA.
DR GeneTree; ENSGT00390000006454; -.
DR HOVERGEN; HBG050676; -.
DR InParanoid; Q9H6U6; -.
DR OMA; TSRNMEF; -.
DR OrthoDB; EOG75MVVN; -.
DR PhylomeDB; Q9H6U6; -.
DR TreeFam; TF105856; -.
DR SignaLink; Q9H6U6; -.
DR ChiTaRS; BCAS3; human.
DR GeneWiki; BCAS3; -.
DR GenomeRNAi; 54828; -.
DR NextBio; 57598; -.
DR PRO; PR:Q9H6U6; -.
DR Proteomes; UP000005640; Chromosome 17.
DR Bgee; Q9H6U6; -.
DR ExpressionAtlas; Q9H6U6; baseline and differential.
DR Genevisible; Q9H6U6; HS.
DR GO; GO:0031252; C:cell leading edge; ISS:UniProtKB.
DR GO; GO:0071944; C:cell periphery; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005881; C:cytoplasmic microtubule; ISS:UniProtKB.
DR GO; GO:0045111; C:intermediate filament cytoskeleton; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0035327; C:transcriptionally active chromatin; IDA:UniProtKB.
DR GO; GO:0010698; F:acetyltransferase activator activity; IDA:UniProtKB.
DR GO; GO:0048487; F:beta-tubulin binding; IDA:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
DR GO; GO:0035035; F:histone acetyltransferase binding; IPI:UniProtKB.
DR GO; GO:0042393; F:histone binding; IDA:UniProtKB.
DR GO; GO:0035257; F:nuclear hormone receptor binding; IPI:UniProtKB.
DR GO; GO:0008134; F:transcription factor binding; IPI:UniProtKB.
DR GO; GO:0090630; P:activation of GTPase activity; ISS:UniProtKB.
DR GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR GO; GO:0071391; P:cellular response to estrogen stimulus; IDA:UniProtKB.
DR GO; GO:0007030; P:Golgi organization; ISS:UniProtKB.
DR GO; GO:0031023; P:microtubule organizing center organization; ISS:UniProtKB.
DR GO; GO:0051895; P:negative regulation of focal adhesion assembly; ISS:UniProtKB.
DR GO; GO:0034260; P:negative regulation of GTPase activity; ISS:UniProtKB.
DR GO; GO:2000251; P:positive regulation of actin cytoskeleton reorganization; ISS:UniProtKB.
DR GO; GO:0043085; P:positive regulation of catalytic activity; IDA:UniProtKB.
DR GO; GO:0010595; P:positive regulation of endothelial cell migration; ISS:UniProtKB.
DR GO; GO:0051491; P:positive regulation of filopodium assembly; ISS:UniProtKB.
DR GO; GO:0043547; P:positive regulation of GTPase activity; ISS:UniProtKB.
DR GO; GO:0090316; P:positive regulation of intracellular protein transport; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
DR GO; GO:2000114; P:regulation of establishment of cell polarity; ISS:UniProtKB.
DR GO; GO:0042594; P:response to starvation; IBA:GO_Central.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
DR GO; GO:0035148; P:tube formation; ISS:UniProtKB.
DR Gene3D; 2.130.10.10; -; 2.
DR InterPro; IPR022175; BCAS3.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR017986; WD40_repeat_dom.
DR Pfam; PF12490; BCAS3; 1.
DR SMART; SM00320; WD40; 2.
DR SUPFAM; SSF50978; SSF50978; 2.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Angiogenesis;
KW Chromosomal rearrangement; Complete proteome; Cytoplasm; Cytoskeleton;
KW Nucleus; Phosphoprotein; Polymorphism; Proto-oncogene;
KW Reference proteome; Repeat; Transcription; Transcription regulation;
KW WD repeat.
FT CHAIN 1 928 Breast carcinoma-amplified sequence 3.
FT /FTId=PRO_0000050883.
FT REPEAT 69 110 WD 1.
FT REPEAT 111 175 WD 2.
FT REPEAT 176 234 WD 3.
FT REPEAT 235 288 WD 4.
FT REPEAT 289 341 WD 5.
FT REPEAT 342 394 WD 6.
FT REPEAT 395 433 WD 7.
FT SITE 824 825 Breakpoint for translocation to form
FT BCAS4-BCAS3.
FT MOD_RES 1 1 N-acetylmethionine.
FT {ECO:0000244|PubMed:22814378}.
FT MOD_RES 461 461 Phosphoserine.
FT {ECO:0000250|UniProtKB:Q8CCN5}.
FT MOD_RES 480 480 Phosphoserine.
FT {ECO:0000244|PubMed:18669648}.
FT MOD_RES 488 488 Phosphoserine.
FT {ECO:0000250|UniProtKB:Q8CCN5}.
FT MOD_RES 838 838 Phosphoserine.
FT {ECO:0000250|UniProtKB:Q8CCN5}.
FT MOD_RES 886 886 Phosphoserine.
FT {ECO:0000244|PubMed:19690332}.
FT MOD_RES 898 898 Phosphoserine.
FT {ECO:0000250|UniProtKB:Q8CCN5}.
FT VAR_SEQ 1 229 Missing (in isoform 6).
FT {ECO:0000303|PubMed:14702039,
FT ECO:0000303|Ref.6}.
FT /FTId=VSP_040112.
FT VAR_SEQ 547 561 Missing (in isoform 1, isoform 3, isoform
FT 5 and isoform 6).
FT {ECO:0000303|PubMed:12378525,
FT ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334,
FT ECO:0000303|Ref.6}.
FT /FTId=VSP_007858.
FT VAR_SEQ 879 879 T -> TDTALDVAVKTFPPERHVAVKCF (in isoform
FT 3 and isoform 4).
FT {ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:17974005}.
FT /FTId=VSP_007860.
FT VAR_SEQ 880 928 ELQREGSIETLSNSSGSTSGSIPRNFDGYRSPLPTNESQPL
FT SLFPTGFP -> DTALDVAVKTFPPERHVAVKCFGKKKGKK
FT KQCQQPSVREQPNSNKACVRDGGRTSARGKHRDSE (in
FT isoform 5).
FT {ECO:0000303|PubMed:14702039}.
FT /FTId=VSP_040113.
FT VARIANT 87 87 N -> S (in dbSNP:rs2643103).
FT {ECO:0000269|PubMed:12378525,
FT ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334,
FT ECO:0000269|Ref.4}.
FT /FTId=VAR_065093.
FT VARIANT 106 106 I -> V (in dbSNP:rs34712615).
FT /FTId=VAR_057583.
FT CONFLICT 29 29 E -> K (in Ref. 1; AAL99632).
FT {ECO:0000305}.
FT CONFLICT 127 127 R -> K (in Ref. 1; AAL99632).
FT {ECO:0000305}.
FT CONFLICT 199 200 VV -> II (in Ref. 2; BAB15156).
FT {ECO:0000305}.
FT CONFLICT 533 533 K -> E (in Ref. 2; BAB14078/BAB14380).
FT {ECO:0000305}.
FT CONFLICT 640 640 D -> G (in Ref. 2; BAB15156).
FT {ECO:0000305}.
FT CONFLICT 666 666 Q -> R (in Ref. 2; BAB14078).
FT {ECO:0000305}.
FT CONFLICT 806 806 S -> P (in Ref. 2; BAB15156).
FT {ECO:0000305}.
SQ SEQUENCE 928 AA; 101237 MW; 00D82E2EDCD1E8D7 CRC64;
MNEAMATDSP RRPSRCTGGV VVRPQAVTEQ SYMESVVTFL QDVVPQAYSG TPLTEEKEKI
VWVRFENADL NDTSRNLEFH EIHSTGNEPP LLIMIGYSDG MQVWSIPISG EAQELFSVRH
GPIRAARILP APQFGAQKCD NFAEKRPLLG VCKSIGSSGT SPPYCCVDLY SLRTGEMVKS
IQFKTPIYDL HCNKRILVVV LQEKIAAFDS CTFTKKFFVT SCYPCPGPNM NPIALGSRWL
AYAENKLIRC HQSRGGACGD NIQSYTATVI SAAKTLKSGL TMVGKVVTQL TGTLPSGVTE
DDVAIHSNSR RSPLVPGIIT VIDTETVGEG QVLVSEDSDS DGIVAHFPAH EKPVCCMAFN
TSGMLLVTTD TLGHDFHVFQ ILTHPWSSSQ CAVHHLYTLH RGETEAKVQD ICFSHDCRWV
VVSTLRGTSH VFPINPYGGQ PCVRTHMSPR VVNRMSRFQK SAGLEEIEQE LTSKQGGRCS
PVPGLSSSPS GSPLHGKLNS QDSYNNFTNN NPGNPRLSPL PSLMVVMPLA QIKQPMTLGT
ITKRTGPYLF GAGCFSIKAP CKVKPPPQIS PSKSMGGEFC VAAIFGTSRS WFANNAGLKR
EKDQSKQVVV ESLYIISCYG TLVEHMMEPR PLSTAPKISD DTPLEMMTSP RASWTLVRTP
QWNELQPPFN ANHPLLLAAD AVQYYQFLLA GLVPPGSPGP ITRHGSYDSL ASDHSGQEDE
EWLSQVEIVT HTGPHRRLWM GPQFQFKTIH PSGQTTVISS SSSVLQSHGP SDTPQPLLDF
DTDDLDLNSL RIQPVRSDPV SMPGSSRPVS DRRGVSTVID AASGTFDRSV TLLEVCGSWP
EGFGLRHMSS MEHTEEGLRE RLADAMAESP SRDVVGSGTE LQREGSIETL SNSSGSTSGS
IPRNFDGYRS PLPTNESQPL SLFPTGFP
//
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";
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
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 DMRTB_HUMAN Reviewed; 342 AA.
AC Q96MA1; Q96SD2;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 11-NOV-2015, entry version 111.
DE RecName: Full=Doublesex- and mab-3-related transcription factor B1;
GN Name=DMRTB1;
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].
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(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 NUCLEOTIDE SEQUENCE [MRNA] OF 7-342, AND TISSUE SPECIFICITY.
RC TISSUE=Testis;
RX PubMed=11863363; DOI=10.1006/geno.2002.6711;
RA Ottolenghi C., Fellous M., Barbieri M., McElreavey K.;
RT "Novel paralogy relations among human chromosomes support a link
RT between the phylogeny of doublesex-related genes and the evolution of
RT sex determination.";
RL Genomics 79:333-343(2002).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-
CC ProRule:PRU00070}.
CC -!- TISSUE SPECIFICITY: Testis. {ECO:0000269|PubMed:11863363}.
CC -!- SIMILARITY: Belongs to the DMRT family. {ECO:0000305}.
CC -!- SIMILARITY: Contains 1 DM DNA-binding domain.
CC {ECO:0000255|PROSITE-ProRule:PRU00070}.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AK057273; BAB71407.1; -; mRNA.
DR EMBL; AL365445; CAI22836.1; -; Genomic_DNA.
DR EMBL; CH471059; EAX06736.1; -; Genomic_DNA.
DR EMBL; AJ291671; CAC40654.1; -; mRNA.
DR CCDS; CCDS581.1; -.
DR RefSeq; NP_149056.1; NM_033067.2.
DR UniGene; Hs.131654; -.
DR ProteinModelPortal; Q96MA1; -.
DR SMR; Q96MA1; 7-65.
DR BioGrid; 122012; 15.
DR IntAct; Q96MA1; 8.
DR MINT; MINT-1437877; -.
DR STRING; 9606.ENSP00000360500; -.
DR PhosphoSite; Q96MA1; -.
DR BioMuta; DMRTB1; -.
DR DMDM; 74752030; -.
DR PaxDb; Q96MA1; -.
DR PRIDE; Q96MA1; -.
DR Ensembl; ENST00000371445; ENSP00000360500; ENSG00000143006.
DR GeneID; 63948; -.
DR KEGG; hsa:63948; -.
DR UCSC; uc001cvq.1; human.
DR CTD; 63948; -.
DR GeneCards; DMRTB1; -.
DR HGNC; HGNC:13913; DMRTB1.
DR HPA; HPA036490; -.
DR HPA; HPA058553; -.
DR MIM; 614805; gene.
DR neXtProt; NX_Q96MA1; -.
DR PharmGKB; PA27386; -.
DR eggNOG; KOG3815; Eukaryota.
DR eggNOG; ENOG410XSK9; LUCA.
DR GeneTree; ENSGT00550000074486; -.
DR HOGENOM; HOG000112231; -.
DR HOVERGEN; HBG095592; -.
DR InParanoid; Q96MA1; -.
DR KO; K19492; -.
DR OMA; CYLISER; -.
DR OrthoDB; EOG741Z32; -.
DR PhylomeDB; Q96MA1; -.
DR TreeFam; TF317837; -.
DR GenomeRNAi; 63948; -.
DR NextBio; 65732; -.
DR PRO; PR:Q96MA1; -.
DR Proteomes; UP000005640; Chromosome 1.
DR Bgee; Q96MA1; -.
DR CleanEx; HS_DMRTB1; -.
DR Genevisible; Q96MA1; HS.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042803; F:protein homodimerization activity; IBA:GO_Central.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
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; 4.10.1040.10; -; 1.
DR InterPro; IPR001275; DM_DNA-bd.
DR InterPro; IPR026607; DMRT/dsx/mab-3.
DR PANTHER; PTHR12322; PTHR12322; 1.
DR Pfam; PF00751; DM; 1.
DR SMART; SM00301; DM; 1.
DR SUPFAM; SSF82927; SSF82927; 1.
DR PROSITE; PS40000; DM_1; 1.
DR PROSITE; PS50809; DM_2; 1.
PE 2: Evidence at transcript level;
KW Complete proteome; DNA-binding; Metal-binding; Nucleus;
KW Reference proteome; Transcription; Transcription regulation; Zinc.
FT CHAIN 1 342 Doublesex- and mab-3-related
FT transcription factor B1.
FT /FTId=PRO_0000316012.
FT DNA_BIND 11 58 DM. {ECO:0000255|PROSITE-
FT ProRule:PRU00070}.
FT COMPBIAS 80 84 Poly-Ala.
FT COMPBIAS 85 304 Pro-rich.
SQ SEQUENCE 342 AA; 36205 MW; 18B0D5B0A6DB03EB CRC64;
MADKMVRTPK CSRCRNHGFL VPVKGHAGKC RWKQCLCEKC YLISERQKIM AAQKVLKTQA
AEEEQEAALC AQGPKQASGA AAAAPAPVPV PAASLRPLSP GTPSGDADPG PEGRAAACFF
EQPPRGRNPG PRALQPVLGG RSHVEPSERA AVAMPSLAGP PFGAEAAGSG YPGPLDLRRP
MRTVPGPLFT DFVRPLNINP DRALGPEYPG GSSMHPYCPF PLGYLDAPPG VPLQQGFRHV
SRSQYQGGGL VSEPGGDFQP SYYLPPPPPP LPPLPPLPPQ PQFLPPGYLS ALHFLPPPPP
PPPPSSFSLT VLFDTDKENT DDQDAEVLSG EPSQPSSQEQ SD
//
ID FOXP2_HUMAN Reviewed; 715 AA.
AC O15409; A0AUV6; A4D0U8; A6NNW4; B4DLD9; Q6ZND1; Q75MJ3; Q8IZE0;
AC Q8N0W2; Q8N6B7; Q8N6B8; Q8NFQ1; Q8NFQ2; Q8NFQ3; Q8NFQ4; Q8TD74;
DT 05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT 05-DEC-2001, sequence version 2.
DT 11-NOV-2015, entry version 157.
DE RecName: Full=Forkhead box protein P2;
DE AltName: Full=CAG repeat protein 44;
DE AltName: Full=Trinucleotide repeat-containing gene 10 protein;
GN Name=FOXP2; Synonyms=CAGH44, TNRC10;
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), ALTERNATIVE SPLICING, AND
RP VARIANT SPCH1 HIS-553.
RX PubMed=11586359; DOI=10.1038/35097076;
RA Lai C.S.L., Fisher S.E., Hurst J.A., Vargha-Khadem F., Monaco A.P.;
RT "A forkhead-domain gene is mutated in a severe speech and language
RT disorder.";
RL Nature 413:519-523(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 7), NUCLEOTIDE SEQUENCE [MRNA] OF
RP 1-415 (ISOFORM 1), NUCLEOTIDE SEQUENCE [MRNA] OF 259-715 (ISOFORM 6),
RP AND TISSUE SPECIFICITY.
RC TISSUE=Brain, Corpus striatum, Fetal brain, and Frontal cortex;
RX PubMed=12189486; DOI=10.1007/s00439-002-0768-5;
RA Bruce H.A., Margolis R.L.;
RT "FOXP2: novel exons, splice variants, and CAG repeat length
RT stability.";
RL Hum. Genet. 111:136-144(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
RA Vincent J.B., Scherer S.W.;
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Brain;
RA Guo J.H., Chen L., Yu L.;
RL Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 8 AND 9).
RC TISSUE=Tongue;
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 [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 3).
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 [10]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-304 (ISOFORM 1).
RC TISSUE=Brain cortex;
RX PubMed=9225980; DOI=10.1007/s004390050476;
RA Margolis R.L., Abraham M.R., Gatchell S.B., Li S.-H., Kidwai A.S.,
RA Breschel T.S., Stine O.C., Callahan C., McInnis M.G., Ross C.A.;
RT "cDNAs with long CAG trinucleotide repeats from human brain.";
RL Hum. Genet. 100:114-122(1997).
RN [11]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 113-329.
RX PubMed=12192408; DOI=10.1038/nature01025;
RA Enard W., Przeworski M., Fisher S.E., Lai C.S.L., Wiebe V., Kitano T.,
RA Monaco A.P., Paeaebo S.;
RT "Molecular evolution of FOXP2, a gene involved in speech and
RT language.";
RL Nature 418:869-872(2002).
RN [12]
RP DEVELOPMENTAL STAGE.
RX PubMed=15056695; DOI=10.1523/JNEUROSCI.5589-03.2004;
RA Teramitsu I., Kudo L.C., London S.E., Geschwind D.H., White S.A.;
RT "Parallel FoxP1 and FoxP2 expression in songbird and human brain
RT predicts functional interaction.";
RL J. Neurosci. 24:3152-3163(2004).
CC -!- FUNCTION: Transcriptional repressor that may play a role in the
CC specification and differentiation of lung epithelium. May also
CC play a role in developing neural, gastrointestinal and
CC cardiovascular tissues. Can act with CTBP1 to synergistically
CC repress transcription but CTPBP1 is not essential. Plays a role in
CC synapse formation by regulating SRPX2 levels. Involved in neural
CC mechanisms mediating the development of speech and language.
CC -!- SUBUNIT: Forms homodimers and heterodimers with FOXP1 and FOXP4.
CC Dimerization is required for DNA-binding. Interacts with CTBP1 (By
CC similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC Q08117:AES; NbExp=3; IntAct=EBI-983612, EBI-717810;
CC P24863:CCNC; NbExp=3; IntAct=EBI-983612, EBI-395261;
CC Q13363-2:CTBP1; NbExp=3; IntAct=EBI-983612, EBI-10171858;
CC P56545:CTBP2; NbExp=3; IntAct=EBI-983612, EBI-741533;
CC Q86V42:FAM124A; NbExp=3; IntAct=EBI-983612, EBI-744506;
CC Q13526:PIN1; NbExp=3; IntAct=EBI-983612, EBI-714158;
CC O00560:SDCBP; NbExp=3; IntAct=EBI-983612, EBI-727004;
CC Q96A04:TSACC; NbExp=3; IntAct=EBI-983612, EBI-740411;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=9;
CC Name=1; Synonyms=I;
CC IsoId=O15409-1; Sequence=Displayed;
CC Name=2; Synonyms=II;
CC IsoId=O15409-3; Sequence=Not described;
CC Name=3; Synonyms=III, IV;
CC IsoId=O15409-2; Sequence=VSP_001558;
CC Name=4;
CC IsoId=O15409-4; Sequence=VSP_011532;
CC Name=5;
CC IsoId=O15409-5; Sequence=VSP_011532, VSP_011535, VSP_011536;
CC Name=6; Synonyms=FOXP2-S;
CC IsoId=O15409-6; Sequence=VSP_011538, VSP_011539;
CC Name=7;
CC IsoId=O15409-7; Sequence=VSP_011537;
CC Name=8;
CC IsoId=O15409-8; Sequence=VSP_011533, VSP_011534;
CC Note=No experimental confirmation available.;
CC Name=9;
CC IsoId=O15409-9; Sequence=VSP_043464;
CC Note=No experimental confirmation available.;
CC -!- TISSUE SPECIFICITY: Isoform 1 and isoform 6 are expressed in adult
CC and fetal brain, caudate nucleus and lung.
CC {ECO:0000269|PubMed:12189486}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the brain at 15 and 22 weeks of
CC gestation, with a pattern of strong cortical, basal ganglia,
CC thalamic and cerebellar expression. Highly expressed in the head
CC and tail of nucleus caudatus and putamen. Restricted expression
CC within the globus pallidus, with high levels in the pars interna,
CC which provides the principal source of output from the basal
CC ganglia to the nucleus centrum medianum thalami (CM) and the major
CC motor relay nuclei of the thalamus. In the thalamus, present in
CC the CM and nucleus medialis dorsalis thalami. Lower levels are
CC observed in the nuclei anterior thalami, dorsal and ventral, and
CC the nucleus parafascicularis thalami. Expressed in the ventrobasal
CC complex comprising the nucleus ventralis posterior
CC lateralis/medialis. The ventral tier of the thalamus exhibits
CC strong expression, including nuclei ventralis anterior, lateralis
CC and posterior lateralis pars oralis. Also expressed in the nucleus
CC subthalamicus bilaterally and in the nucleus ruber.
CC {ECO:0000269|PubMed:15056695}.
CC -!- DOMAIN: The leucine-zipper is required for dimerization and
CC transcriptional repression. {ECO:0000250}.
CC -!- DISEASE: Speech-language disorder 1 (SPCH1) [MIM:602081]: A
CC disorder characterized by severe orofacial dyspraxia resulting in
CC largely incomprehensible speech. Affected individuals have severe
CC impairment in the selection and sequencing of fine orofacial
CC movements which are necessary for articulation, and deficits in
CC several facets of grammatical skills and language processing, such
CC as the ability to break up words into their constituent phonemes.
CC {ECO:0000269|PubMed:11586359}. Note=The disease is caused by
CC mutations affecting the gene represented in this entry.
CC -!- DISEASE: Note=A chromosomal aberration involving FOXP2 is a cause
CC of severe speech and language impairment. Translocation
CC t(5;7)(q22;q31.2).
CC -!- SIMILARITY: Contains 1 C2H2-type zinc finger. {ECO:0000305}.
CC -!- SIMILARITY: Contains 1 fork-head DNA-binding domain.
CC {ECO:0000255|PROSITE-ProRule:PRU00089}.
CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=Talking heads - Issue
CC 51 of October 2004;
CC URL="http://web.expasy.org/spotlight/back_issues/051";
CC -!- WEB RESOURCE: Name=Wikipedia; Note=FOXP2 entry;
CC URL="https://en.wikipedia.org/wiki/FOXP2";
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AF337817; AAL10762.1; -; mRNA.
DR EMBL; AF467252; AAM60762.1; -; mRNA.
DR EMBL; AF467253; AAM60763.1; -; mRNA.
DR EMBL; AF467254; AAM60764.1; -; mRNA.
DR EMBL; AF467255; AAM60765.1; -; mRNA.
DR EMBL; AF467256; AAM60766.1; -; mRNA.
DR EMBL; AF467257; AAM60767.1; -; mRNA.
DR EMBL; AF493430; AAM13672.1; -; mRNA.
DR EMBL; AY144615; AAN60016.1; -; mRNA.
DR EMBL; AK131266; BAD18444.1; ALT_SEQ; mRNA.
DR EMBL; AK296957; BAG59501.1; -; mRNA.
DR EMBL; AC003992; AAS07399.1; -; Genomic_DNA.
DR EMBL; AC020606; AAS07502.1; -; Genomic_DNA.
DR EMBL; AC073626; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC074000; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC092148; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC092606; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH236947; EAL24367.1; -; Genomic_DNA.
DR EMBL; CH236947; EAL24369.1; -; Genomic_DNA.
DR EMBL; CH471070; EAW83484.1; -; Genomic_DNA.
DR EMBL; CH471070; EAW83486.1; -; Genomic_DNA.
DR EMBL; BC126104; AAI26105.1; -; mRNA.
DR EMBL; BC143866; AAI43867.1; -; mRNA.
DR EMBL; U80741; AAB91439.1; -; mRNA.
DR EMBL; AF515031; AAN03389.1; -; Genomic_DNA.
DR EMBL; AF515032; AAN03390.1; -; Genomic_DNA.
DR EMBL; AF515033; AAN03391.1; -; Genomic_DNA.
DR EMBL; AF515034; AAN03392.1; -; Genomic_DNA.
DR EMBL; AF515035; AAN03393.1; -; Genomic_DNA.
DR EMBL; AF515036; AAN03394.1; -; Genomic_DNA.
DR EMBL; AF515037; AAN03395.1; -; Genomic_DNA.
DR EMBL; AF515038; AAN03396.1; -; Genomic_DNA.
DR EMBL; AF515039; AAN03397.1; -; Genomic_DNA.
DR EMBL; AF515040; AAN03398.1; -; Genomic_DNA.
DR EMBL; AF515041; AAN03399.1; -; Genomic_DNA.
DR EMBL; AF515042; AAN03400.1; -; Genomic_DNA.
DR EMBL; AF515043; AAN03401.1; -; Genomic_DNA.
DR EMBL; AF515044; AAN03402.1; -; Genomic_DNA.
DR EMBL; AF515045; AAN03403.1; -; Genomic_DNA.
DR EMBL; AF515046; AAN03404.1; -; Genomic_DNA.
DR EMBL; AF515047; AAN03405.1; -; Genomic_DNA.
DR EMBL; AF515048; AAN03406.1; -; Genomic_DNA.
DR EMBL; AF515049; AAN03407.1; -; Genomic_DNA.
DR EMBL; AF515050; AAN03408.1; -; Genomic_DNA.
DR CCDS; CCDS43635.1; -. [O15409-4]
DR CCDS; CCDS55154.1; -. [O15409-9]
DR CCDS; CCDS5760.1; -. [O15409-1]
DR CCDS; CCDS5761.2; -. [O15409-6]
DR RefSeq; NP_001166237.1; NM_001172766.2.
DR RefSeq; NP_001166238.1; NM_001172767.2.
DR RefSeq; NP_055306.1; NM_014491.3. [O15409-1]
DR RefSeq; NP_683696.2; NM_148898.3. [O15409-4]
DR RefSeq; NP_683697.2; NM_148899.3. [O15409-6]
DR RefSeq; NP_683698.2; NM_148900.3. [O15409-9]
DR UniGene; Hs.282787; -.
DR PDB; 2A07; X-ray; 1.90 A; F/G/H/I/J/K=502-594.
DR PDB; 2AS5; X-ray; 2.70 A; F/G=502-594.
DR PDBsum; 2A07; -.
DR PDBsum; 2AS5; -.
DR ProteinModelPortal; O15409; -.
DR SMR; O15409; 351-409, 503-584.
DR BioGrid; 125073; 28.
DR DIP; DIP-29004N; -.
DR IntAct; O15409; 9.
DR STRING; 9606.ENSP00000386200; -.
DR PhosphoSite; O15409; -.
DR BioMuta; FOXP2; -.
DR MaxQB; O15409; -.
DR PaxDb; O15409; -.
DR PRIDE; O15409; -.
DR Ensembl; ENST00000350908; ENSP00000265436; ENSG00000128573. [O15409-1]
DR Ensembl; ENST00000360232; ENSP00000353367; ENSG00000128573. [O15409-6]
DR Ensembl; ENST00000378237; ENSP00000367482; ENSG00000128573. [O15409-7]
DR Ensembl; ENST00000393489; ENSP00000377129; ENSG00000128573. [O15409-2]
DR Ensembl; ENST00000393494; ENSP00000377132; ENSG00000128573. [O15409-1]
DR Ensembl; ENST00000403559; ENSP00000385069; ENSG00000128573. [O15409-9]
DR Ensembl; ENST00000408937; ENSP00000386200; ENSG00000128573. [O15409-4]
DR Ensembl; ENST00000412402; ENSP00000405470; ENSG00000128573. [O15409-8]
DR Ensembl; ENST00000441290; ENSP00000416825; ENSG00000128573. [O15409-8]
DR GeneID; 93986; -.
DR KEGG; hsa:93986; -.
DR UCSC; uc003vgv.1; human. [O15409-7]
DR UCSC; uc003vgw.3; human. [O15409-5]
DR UCSC; uc003vgx.2; human. [O15409-1]
DR UCSC; uc003vgz.3; human. [O15409-4]
DR UCSC; uc003vhd.3; human. [O15409-6]
DR UCSC; uc011kmu.2; human. [O15409-9]
DR CTD; 93986; -.
DR GeneCards; FOXP2; -.
DR HGNC; HGNC:13875; FOXP2.
DR HPA; CAB011488; -.
DR HPA; HPA000382; -.
DR HPA; HPA000383; -.
DR MIM; 602081; phenotype.
DR MIM; 605317; gene.
DR neXtProt; NX_O15409; -.
DR Orphanet; 251061; 7q31 microdeletion syndrome.
DR Orphanet; 209908; Childhood apraxia of speech.
DR PharmGKB; PA28242; -.
DR eggNOG; KOG4385; Eukaryota.
DR eggNOG; COG5025; LUCA.
DR GeneTree; ENSGT00800000124075; -.
DR HOGENOM; HOG000092089; -.
DR HOVERGEN; HBG051657; -.
DR InParanoid; O15409; -.
DR KO; K09409; -.
DR OMA; PETKLCV; -.
DR OrthoDB; EOG7M6D7G; -.
DR PhylomeDB; O15409; -.
DR TreeFam; TF326978; -.
DR ChiTaRS; FOXP2; human.
DR EvolutionaryTrace; O15409; -.
DR GeneWiki; FOXP2; -.
DR GenomeRNAi; 93986; -.
DR NextBio; 78260; -.
DR PRO; PR:O15409; -.
DR Proteomes; UP000005640; Chromosome 7.
DR Bgee; O15409; -.
DR ExpressionAtlas; O15409; baseline and differential.
DR Genevisible; O15409; HS.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IDA: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:0000978; F:RNA polymerase II core promoter proximal region sequence-specific DNA binding; IEA:Ensembl.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:BHF-UCL.
DR GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IDA:BHF-UCL.
DR GO; GO:0001078; F:transcriptional repressor activity, RNA polymerase II core promoter proximal region sequence-specific binding; IEA:Ensembl.
DR GO; GO:0043010; P:camera-type eye development; IEA:Ensembl.
DR GO; GO:0021757; P:caudate nucleus development; IMP:UniProtKB.
DR GO; GO:0021549; P:cerebellum development; IEA:Ensembl.
DR GO; GO:0021987; P:cerebral cortex development; IEP:BHF-UCL.
DR GO; GO:0040007; P:growth; IEA:Ensembl.
DR GO; GO:0048286; P:lung alveolus development; IEA:Ensembl.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:BHF-UCL.
DR GO; GO:0060501; P:positive regulation of epithelial cell proliferation involved in lung morphogenesis; IEA:Ensembl.
DR GO; GO:0002053; P:positive regulation of mesenchymal cell proliferation; IEA:Ensembl.
DR GO; GO:0009791; P:post-embryonic development; IEA:Ensembl.
DR GO; GO:0021758; P:putamen development; IMP:UniProtKB.
DR GO; GO:0060013; P:righting reflex; IEA:Ensembl.
DR GO; GO:0007519; P:skeletal muscle tissue development; IEA:Ensembl.
DR GO; GO:0048745; P:smooth muscle tissue development; IEA:Ensembl.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
DR GO; GO:0042297; P:vocal learning; IEA:Ensembl.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR001766; Fork_head_dom.
DR InterPro; IPR032354; FOXP-CC.
DR InterPro; IPR011991; WHTH_DNA-bd_dom.
DR InterPro; IPR015880; Znf_C2H2-like.
DR Pfam; PF00250; Forkhead; 1.
DR Pfam; PF16159; FOXP-CC; 1.
DR PRINTS; PR00053; FORKHEAD.
DR SMART; SM00339; FH; 1.
DR SMART; SM00355; ZnF_C2H2; 1.
DR PROSITE; PS00658; FORK_HEAD_2; 1.
DR PROSITE; PS50039; FORK_HEAD_3; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Chromosomal rearrangement;
KW Complete proteome; Disease mutation; DNA-binding; Metal-binding;
KW Nucleus; Reference proteome; Repressor; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1 715 Forkhead box protein P2.
FT /FTId=PRO_0000091879.
FT ZN_FING 346 371 C2H2-type.
FT DNA_BIND 504 594 Fork-head. {ECO:0000255|PROSITE-
FT ProRule:PRU00089}.
FT REGION 388 409 Leucine-zipper.
FT REGION 422 426 CTBP1-binding. {ECO:0000250}.
FT COMPBIAS 53 268 Gln-rich.
FT VAR_SEQ 1 92 Missing (in isoform 3).
FT {ECO:0000303|PubMed:15489334}.
FT /FTId=VSP_001558.
FT VAR_SEQ 86 86 Q -> QELLPETKLCICGHSSGDGHPHNTFA (in
FT isoform 4 and isoform 5).
FT {ECO:0000303|Ref.3, ECO:0000303|Ref.4}.
FT /FTId=VSP_011532.
FT VAR_SEQ 87 87 V -> P (in isoform 8).
FT {ECO:0000303|PubMed:14702039}.
FT /FTId=VSP_011533.
FT VAR_SEQ 88 715 Missing (in isoform 8).
FT {ECO:0000303|PubMed:14702039}.
FT /FTId=VSP_011534.
FT VAR_SEQ 132 132 Q -> QDFLDSGLENFRAALEKN (in isoform 9).
FT {ECO:0000303|PubMed:14702039}.
FT /FTId=VSP_043464.
FT VAR_SEQ 133 143 QQLQEFYKKQQ -> VMWVTCFGVLA (in isoform
FT 5). {ECO:0000303|Ref.3}.
FT /FTId=VSP_011535.
FT VAR_SEQ 144 715 Missing (in isoform 5).
FT {ECO:0000303|Ref.3}.
FT /FTId=VSP_011536.
FT VAR_SEQ 366 715 Missing (in isoform 7).
FT {ECO:0000303|PubMed:12189486}.
FT /FTId=VSP_011537.
FT VAR_SEQ 423 432 LNLVSSVTMS -> VSAYCFINSK (in isoform 6).
FT {ECO:0000303|PubMed:12189486}.
FT /FTId=VSP_011538.
FT VAR_SEQ 433 715 Missing (in isoform 6).
FT {ECO:0000303|PubMed:12189486}.
FT /FTId=VSP_011539.
FT VARIANT 553 553 R -> H (in SPCH1).
FT {ECO:0000269|PubMed:11586359}.
FT /FTId=VAR_012278.
FT CONFLICT 29 29 A -> V (in Ref. 2; AAM60762).
FT {ECO:0000305}.
FT CONFLICT 134 134 Q -> H (in Ref. 10; AAB91439).
FT {ECO:0000305}.
FT CONFLICT 290 304 DLTTNNSSSTTSSNT -> EEFPVQGPAAVCAGL (in
FT Ref. 10; AAB91439). {ECO:0000305}.
FT CONFLICT 414 414 S -> L (in Ref. 2; AAM60766).
FT {ECO:0000305}.
FT HELIX 509 519 {ECO:0000244|PDB:2A07}.
FT HELIX 527 541 {ECO:0000244|PDB:2A07}.
FT HELIX 545 558 {ECO:0000244|PDB:2A07}.
FT STRAND 562 567 {ECO:0000244|PDB:2AS5}.
FT STRAND 568 572 {ECO:0000244|PDB:2A07}.
FT HELIX 577 583 {ECO:0000244|PDB:2A07}.
SQ SEQUENCE 715 AA; 79919 MW; 4F9FBDB6D90516E0 CRC64;
MMQESATETI SNSSMNQNGM STLSSQLDAG SRDGRSSGDT SSEVSTVELL HLQQQQALQA
ARQLLLQQQT SGLKSPKSSD KQRPLQVPVS VAMMTPQVIT PQQMQQILQQ QVLSPQQLQA
LLQQQQAVML QQQQLQEFYK KQQEQLHLQL LQQQQQQQQQ QQQQQQQQQQ QQQQQQQQQQ
QQQQQQQQQQ QHPGKQAKEQ QQQQQQQQQL AAQQLVFQQQ LLQMQQLQQQ QHLLSLQRQG
LISIPPGQAA LPVQSLPQAG LSPAEIQQLW KEVTGVHSME DNGIKHGGLD LTTNNSSSTT
SSNTSKASPP ITHHSIVNGQ SSVLSARRDS SSHEETGASH TLYGHGVCKW PGCESICEDF
GQFLKHLNNE HALDDRSTAQ CRVQMQVVQQ LEIQLSKERE RLQAMMTHLH MRPSEPKPSP
KPLNLVSSVT MSKNMLETSP QSLPQTPTTP TAPVTPITQG PSVITPASVP NVGAIRRRHS
DKYNIPMSSE IAPNYEFYKN ADVRPPFTYA TLIRQAIMES SDRQLTLNEI YSWFTRTFAY
FRRNAATWKN AVRHNLSLHK CFVRVENVKG AVWTVDEVEY QKRRSQKITG SPTLVKNIPT
SLGYGAALNA SLQAALAESS LPLLSNPGLI NNASSGLLQA VHEDLNGSLD HIDSNGNSSP
GCSPQPHIHS IHVKEEPVIA EDEDCPMSLV TTANHSPELE DDREIEEEPL SEDLE
//
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";
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
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 HXB5_HUMAN Reviewed; 269 AA.
AC P09067; B2RC69; P09069; Q17RP4;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 3.
DT 11-NOV-2015, entry version 156.
DE RecName: Full=Homeobox protein Hox-B5;
DE AltName: Full=Homeobox protein HHO.C10;
DE AltName: Full=Homeobox protein Hox-2A;
DE AltName: Full=Homeobox protein Hu-1;
GN Name=HOXB5; Synonyms=HOX2A;
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=1355360;
RA Galang C.K., Hauser C.A.;
RT "Cooperative DNA binding of the highly conserved human Hox 2.1
RT homeodomain gene product.";
RL New Biol. 4:558-568(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Kidd K.K., Busygina V., DeMille M.M.C., Speed W.C., Ruggeri V.,
RA Kidd J.R., Pakstis A.J.;
RT "Overall linkage disequilibrium in 33 populations for highly
RT informative multisite haplotypes spanning the HOXB gene cluster.";
RL Am. J. Hum. Genet. 67:235-235(2000).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 188-269.
RX PubMed=4075393; DOI=10.1016/0092-8674(85)90008-X;
RA Hauser C.A., Joyner A.L., Klein R.D., Learned T.K., Martin G.R.,
RA Tjian R.;
RT "Expression of homologous homeo-box-containing genes in differentiated
RT human teratocarcinoma cells and mouse embryos.";
RL Cell 43:19-28(1985).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 191-269.
RX PubMed=6091895; DOI=10.1016/0092-8674(84)90261-7;
RA Levine M., Rubin G.M., Tjian R.;
RT "Human DNA sequences homologous to a protein coding region conserved
RT between homeotic genes of Drosophila.";
RL Cell 38:667-673(1984).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 200-269.
RX PubMed=3453105; DOI=10.1038/320763a0;
RA Simeone A., Mavilio F., Bottero L., Giampaolo A., Russo G.,
RA Faiella A., Boncinelli E., Peschle C.;
RT "A human homoeo box gene specifically expressed in spinal cord during
RT embryonic development.";
RL Nature 320:763-765(1986).
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 199-269.
RX PubMed=2576652;
RA Boncinelli E., Acampora D., Pannese M., D'Esposito M., Somma R.,
RA Gaudino G., Stornaiuolo A., Cafiero M., Faiella A., Simeone A.;
RT "Organization of human class I homeobox genes.";
RL Genome 31:745-756(1989).
RN [9]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 217-269.
RC TISSUE=Osteosarcoma;
RA Waye M.M.Y.;
RT "Cloning of a homeobox-containing cDNA (HHO.c10 or Hu-1) from a gt11
RT cDNA library of human osteosarcoma cell MG-63.";
RL Submitted (FEB-1993) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Sequence-specific transcription factor which is part of
CC a developmental regulatory system that provides cells with
CC specific positional identities on the anterior-posterior axis.
CC -!- INTERACTION:
CC Q13363-2:CTBP1; NbExp=3; IntAct=EBI-3893317, EBI-10171858;
CC Q8IY44:CTBP2; NbExp=3; IntAct=EBI-3893317, EBI-10171902;
CC P43364-2:MAGEA11; NbExp=3; IntAct=EBI-3893317, EBI-10178634;
CC P36406:TRIM23; NbExp=3; IntAct=EBI-3893317, EBI-740098;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- TISSUE SPECIFICITY: Spinal cord.
CC -!- DEVELOPMENTAL STAGE: Embryo.
CC -!- SIMILARITY: Belongs to the Antp homeobox family. {ECO:0000305}.
CC -!- SIMILARITY: Contains 1 homeobox DNA-binding domain.
CC {ECO:0000255|PROSITE-ProRule:PRU00108}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA52681.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; M92299; AAA52682.1; -; mRNA.
DR EMBL; AF287967; AAG31553.1; -; Genomic_DNA.
DR EMBL; AK314964; BAG37466.1; -; mRNA.
DR EMBL; BC117247; AAI17248.1; -; mRNA.
DR EMBL; X03794; CAA27420.1; -; mRNA.
DR EMBL; K02572; AAA52681.1; ALT_INIT; Genomic_DNA.
DR EMBL; M86726; AAB59430.1; -; mRNA.
DR CCDS; CCDS11530.1; -.
DR PIR; A24777; A24777.
DR PIR; A45578; A45578.
DR RefSeq; NP_002138.1; NM_002147.3.
DR UniGene; Hs.654456; -.
DR ProteinModelPortal; P09067; -.
DR SMR; P09067; 201-256.
DR BioGrid; 109455; 50.
DR IntAct; P09067; 5.
DR STRING; 9606.ENSP00000239151; -.
DR PhosphoSite; P09067; -.
DR BioMuta; HOXB5; -.
DR DMDM; 400000; -.
DR PaxDb; P09067; -.
DR PRIDE; P09067; -.
DR Ensembl; ENST00000239151; ENSP00000239151; ENSG00000120075.
DR GeneID; 3215; -.
DR KEGG; hsa:3215; -.
DR UCSC; uc002inr.3; human.
DR CTD; 3215; -.
DR GeneCards; HOXB5; -.
DR HGNC; HGNC:5116; HOXB5.
DR MIM; 142960; gene.
DR neXtProt; NX_P09067; -.
DR PharmGKB; PA29392; -.
DR eggNOG; KOG0489; Eukaryota.
DR eggNOG; ENOG410ZTBY; LUCA.
DR GeneTree; ENSGT00760000118945; -.
DR HOGENOM; HOG000231178; -.
DR HOVERGEN; HBG016849; -.
DR InParanoid; P09067; -.
DR KO; K09305; -.
DR OMA; TNGESHG; -.
DR OrthoDB; EOG780RP4; -.
DR PhylomeDB; P09067; -.
DR TreeFam; TF316310; -.
DR GeneWiki; HOXB5; -.
DR GenomeRNAi; 3215; -.
DR NextBio; 12792; -.
DR PRO; PR:P09067; -.
DR Proteomes; UP000005640; Chromosome 17.
DR Bgee; P09067; -.
DR CleanEx; HS_HOXB5; -.
DR Genevisible; P09067; HS.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0000980; F:RNA polymerase II distal enhancer sequence-specific DNA binding; IEA:Ensembl.
DR GO; GO:0001205; F:transcriptional activator activity, RNA polymerase II distal enhancer sequence-specific binding; IEA:Ensembl.
DR GO; GO:0009653; P:anatomical structure morphogenesis; TAS:ProtInc.
DR GO; GO:0009952; P:anterior/posterior pattern specification; IEA:Ensembl.
DR GO; GO:0048704; P:embryonic skeletal system morphogenesis; IEA:Ensembl.
DR GO; GO:0045446; P:endothelial cell differentiation; IEA:Ensembl.
DR Gene3D; 1.10.10.60; -; 1.
DR InterPro; IPR017995; Homeobox_antennapedia.
DR InterPro; IPR001827; Homeobox_Antennapedia_CS.
DR InterPro; IPR017970; Homeobox_CS.
DR InterPro; IPR001356; Homeobox_dom.
DR InterPro; IPR020479; Homeobox_metazoa.
DR InterPro; IPR009057; Homeodomain-like.
DR Pfam; PF00046; Homeobox; 1.
DR PRINTS; PR00025; ANTENNAPEDIA.
DR PRINTS; PR00024; HOMEOBOX.
DR SMART; SM00389; HOX; 1.
DR SUPFAM; SSF46689; SSF46689; 1.
DR PROSITE; PS00032; ANTENNAPEDIA; 1.
DR PROSITE; PS00027; HOMEOBOX_1; 1.
DR PROSITE; PS50071; HOMEOBOX_2; 1.
PE 1: Evidence at protein level;
KW Complete proteome; Developmental protein; DNA-binding; Homeobox;
KW Nucleus; Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1 269 Homeobox protein Hox-B5.
FT /FTId=PRO_0000200128.
FT DNA_BIND 194 253 Homeobox. {ECO:0000255|PROSITE-
FT ProRule:PRU00108}.
FT MOTIF 176 181 Antp-type hexapeptide.
SQ SEQUENCE 269 AA; 29434 MW; 58197F105DB0F8C4 CRC64;
MSSYFVNSFS GRYPNGPDYQ LLNYGSGSSL SGSYRDPAAM HTGSYGYNYN GMDLSVNRSS
ASSSHFGAVG ESSRAFPAPA QEPRFRQAAS SCSLSSPESL PCTNGDSHGA KPSASSPSDQ
ATSASSSANF TEIDEASASS EPEEAASQLS SPSLARAQPE PMATSTAAPE GQTPQIFPWM
RKLHISHDMT GPDGKRARTA YTRYQTLELE KEFHFNRYLT RRRRIEIAHA LCLSERQIKI
WFQNRRMKWK KDNKLKSMSL ATAGSAFQP
//
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";
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
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 NOL4L_HUMAN Reviewed; 436 AA.
AC Q96MY1; Q5JYB7; Q6P0Y4; Q9BR34; Q9NQF6;
DT 01-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2003, sequence version 2.
DT 11-NOV-2015, entry version 111.
DE RecName: Full=Nucleolar protein 4-like;
GN Name=NOL4L; Synonyms=C20orf112, C20orf113;
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=Neuron;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M.,
RA Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J.,
RA Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M.,
RA Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R.,
RA Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M.,
RA Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H.,
RA Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S.,
RA Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E.,
RA Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A.,
RA Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M.,
RA Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A.,
RA Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S.,
RA Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-130, 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).
CC -!- INTERACTION:
CC Q13363-2:CTBP1; NbExp=3; IntAct=EBI-6660790, EBI-10171858;
CC P56545:CTBP2; NbExp=3; IntAct=EBI-6660790, EBI-741533;
CC Q8IY44:CTBP2; NbExp=3; IntAct=EBI-6660790, EBI-10171902;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q96MY1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96MY1-2; Sequence=VSP_014667, VSP_014668;
CC Note=No experimental confirmation available.;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AK056286; BAB71138.1; -; mRNA.
DR EMBL; AL034550; CAI42261.1; -; Genomic_DNA.
DR EMBL; BC065370; AAH65370.1; -; mRNA.
DR CCDS; CCDS13202.1; -. [Q96MY1-1]
DR RefSeq; NP_001243727.1; NM_001256798.1.
DR RefSeq; NP_542183.2; NM_080616.4. [Q96MY1-1]
DR RefSeq; XP_005260345.1; XM_005260288.1. [Q96MY1-1]
DR RefSeq; XP_005260346.1; XM_005260289.3. [Q96MY1-1]
DR UniGene; Hs.516978; -.
DR UniGene; Hs.729596; -.
DR ProteinModelPortal; Q96MY1; -.
DR BioGrid; 126651; 5.
DR IntAct; Q96MY1; 4.
DR STRING; 9606.ENSP00000352704; -.
DR PhosphoSite; Q96MY1; -.
DR BioMuta; C20orf112; -.
DR DMDM; 28212212; -.
DR MaxQB; Q96MY1; -.
DR PaxDb; Q96MY1; -.
DR PRIDE; Q96MY1; -.
DR DNASU; 140688; -.
DR Ensembl; ENST00000359676; ENSP00000352704; ENSG00000197183. [Q96MY1-1]
DR GeneID; 140688; -.
DR KEGG; hsa:140688; -.
DR UCSC; uc002wxu.5; human. [Q96MY1-1]
DR CTD; 140688; -.
DR GeneCards; NOL4L; -.
DR H-InvDB; HIX0015727; -.
DR H-InvDB; HIX0015728; -.
DR HGNC; HGNC:16106; NOL4L.
DR HPA; HPA041768; -.
DR HPA; HPA043600; -.
DR neXtProt; NX_Q96MY1; -.
DR PharmGKB; PA25652; -.
DR eggNOG; ENOG410IHZD; Eukaryota.
DR eggNOG; ENOG410YIBB; LUCA.
DR GeneTree; ENSGT00390000017363; -.
DR HOGENOM; HOG000220856; -.
DR HOVERGEN; HBG031438; -.
DR InParanoid; Q96MY1; -.
DR PhylomeDB; Q96MY1; -.
DR TreeFam; TF325594; -.
DR ChiTaRS; C20orf112; human.
DR GenomeRNAi; 140688; -.
DR NextBio; 84231; -.
DR PRO; PR:Q96MY1; -.
DR Proteomes; UP000005640; Chromosome 20.
DR Bgee; Q96MY1; -.
DR CleanEx; HS_C20orf112; -.
DR ExpressionAtlas; Q96MY1; baseline and differential.
DR Genevisible; Q96MY1; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR InterPro; IPR026746; NOL4L.
DR PANTHER; PTHR12449:SF19; PTHR12449:SF19; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Complete proteome; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1 436 Nucleolar protein 4-like.
FT /FTId=PRO_0000079456.
FT COMPBIAS 161 169 Poly-Asp.
FT MOD_RES 130 130 Phosphoserine.
FT {ECO:0000244|PubMed:18669648}.
FT VAR_SEQ 382 398 TPTPSSTSTSRPVPTAQ -> SALSGEPPTRRWGCSSV
FT (in isoform 2).
FT {ECO:0000303|PubMed:15489334}.
FT /FTId=VSP_014667.
FT VAR_SEQ 399 436 Missing (in isoform 2).
FT {ECO:0000303|PubMed:15489334}.
FT /FTId=VSP_014668.
FT CONFLICT 215 215 K -> E (in Ref. 1; BAB71138).
FT {ECO:0000305}.
SQ SEQUENCE 436 AA; 47215 MW; 139A07537D875DF8 CRC64;
MSDSTWMSAD PHLASSLSPS QDERMRSPQN LHSQEDDDSS SESGSGNGSS TLNPSTSSST
QGDPAFPEMN GNGAVAPMDF TTAAEDQPIN LCDKLPPATA LGTASYPSDG CGADGLRSRV
KYGVKTTPES PPYSSGSYDS IKTEVSGCPE DLTVGRAPTA DDDDDDHDDH EDNDKMNDSE
GMDPERLKAF NMFVRLFVDE NLDRMVPISK QPKEKIQAII ESCSRQFPEF QERARKRIRT
YLKSCRRMKK NGMEMTRPTP PHLTSAMAEN ILAAACESET RKAAKRMRLE IYQSSQDEPI
ALDKQHSRDS AAITHSTYSL PASSYSQDPV YANGGLNYSY RGYGALSSNL QPPASLQTGN
HSNGPTDLSM KGGASTTSTT PTPTPSSTST SRPVPTAQLS PTEISAVRQL IAGYRESAAF
LLRSADELEN LILQQN
//
ID NOL4_HUMAN Reviewed; 638 AA.
AC O94818; B4DSQ0; B7Z3Z7; F5H1E3; Q6IBS2; Q9BWF1;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 2.
DT 11-NOV-2015, entry version 108.
DE RecName: Full=Nucleolar protein 4;
DE AltName: Full=Nucleolar-localized protein;
GN Name=NOL4; Synonyms=NOLP; ORFNames=HRIHFB2255;
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), SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RC TISSUE=Fetal brain;
RX PubMed=9813152; DOI=10.1006/bbrc.1998.9606;
RA Ueki N., Kondo M., Seki N., Yano K., Oda T., Masuho Y.,
RA Muramatsu M.-A.;
RT "NOLP: identification of a novel human nucleolar protein and
RT determination of sequence requirements for its nucleolar
RT localization.";
RL Biochem. Biophys. Res. Commun. 252:97-102(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4).
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 9-638 (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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 115-638 (ISOFORM 2).
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 (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 115-638 (ISOFORM 2).
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 336-638 (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).
CC -!- INTERACTION:
CC Q13363-2:CTBP1; NbExp=3; IntAct=EBI-10190763, EBI-10171858;
CC P56545:CTBP2; NbExp=3; IntAct=EBI-10190763, EBI-741533;
CC Q8IY44:CTBP2; NbExp=3; IntAct=EBI-10190763, EBI-10171902;
CC Q8IZU0:FAM9B; NbExp=3; IntAct=EBI-10190763, EBI-10175124;
CC O75971:SNAPC5; NbExp=3; IntAct=EBI-10190763, EBI-749483;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC {ECO:0000269|PubMed:9813152, ECO:0000269|PubMed:9853615}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=O94818-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O94818-2; Sequence=VSP_010080;
CC Name=3;
CC IsoId=O94818-3; Sequence=VSP_043344;
CC Note=No experimental confirmation available.;
CC Name=4;
CC IsoId=O94818-4; Sequence=VSP_045836;
CC Note=No experimental confirmation available.;
CC -!- TISSUE SPECIFICITY: Expressed predominantly in fetal brain, adult
CC brain and testis. {ECO:0000269|PubMed:9813152}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH00313.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Sequence of unknown origin in the N-terminal part.; Evidence={ECO:0000305};
CC Sequence=BAA34576.1; Type=Erroneous termination; Positions=38; Note=Translated as Gln.; Evidence={ECO:0000305};
CC Sequence=BAA34576.1; Type=Frameshift; Positions=82; Evidence={ECO:0000305};
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AB017800; BAA34576.1; ALT_SEQ; mRNA.
DR EMBL; AK296539; BAH12383.1; -; mRNA.
DR EMBL; AK299850; BAG61712.1; -; mRNA.
DR EMBL; AC010798; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC018972; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC087397; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC104985; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC000313; AAH00313.1; ALT_SEQ; mRNA.
DR EMBL; BT006763; AAP35409.1; -; mRNA.
DR EMBL; CR456730; CAG33011.1; -; mRNA.
DR EMBL; AB015339; BAA34797.1; -; mRNA.
DR CCDS; CCDS11907.2; -. [O94818-1]
DR CCDS; CCDS56058.1; -. [O94818-4]
DR CCDS; CCDS56059.1; -. [O94818-3]
DR CCDS; CCDS59308.1; -. [O94818-2]
DR PIR; JE0335; JE0335.
DR RefSeq; NP_001185475.1; NM_001198546.1.
DR RefSeq; NP_001185476.1; NM_001198547.1. [O94818-3]
DR RefSeq; NP_001185477.1; NM_001198548.1. [O94818-2]
DR RefSeq; NP_001185478.1; NM_001198549.1. [O94818-4]
DR RefSeq; NP_001269456.1; NM_001282527.1.
DR RefSeq; NP_003778.2; NM_003787.4. [O94818-1]
DR RefSeq; XP_006722626.1; XM_006722563.2. [O94818-1]
DR RefSeq; XP_011524539.1; XM_011526237.1. [O94818-1]
DR RefSeq; XP_011524540.1; XM_011526238.1.
DR UniGene; Hs.514795; -.
DR ProteinModelPortal; O94818; -.
DR BioGrid; 114256; 9.
DR IntAct; O94818; 8.
DR MINT; MINT-1429799; -.
DR STRING; 9606.ENSP00000261592; -.
DR PhosphoSite; O94818; -.
DR BioMuta; NOL4; -.
DR PaxDb; O94818; -.
DR PRIDE; O94818; -.
DR DNASU; 8715; -.
DR Ensembl; ENST00000261592; ENSP00000261592; ENSG00000101746. [O94818-1]
DR Ensembl; ENST00000535384; ENSP00000445733; ENSG00000101746. [O94818-4]
DR Ensembl; ENST00000538587; ENSP00000443472; ENSG00000101746. [O94818-3]
DR Ensembl; ENST00000589544; ENSP00000465450; ENSG00000101746. [O94818-2]
DR GeneID; 8715; -.
DR KEGG; hsa:8715; -.
DR UCSC; uc002kxt.4; human. [O94818-2]
DR UCSC; uc010dmh.3; human. [O94818-3]
DR UCSC; uc010dmi.3; human. [O94818-1]
DR CTD; 8715; -.
DR GeneCards; NOL4; -.
DR HGNC; HGNC:7870; NOL4.
DR HPA; HPA046740; -.
DR MIM; 603577; gene.
DR neXtProt; NX_O94818; -.
DR PharmGKB; PA31674; -.
DR eggNOG; ENOG410IEBQ; Eukaryota.
DR eggNOG; ENOG411245F; LUCA.
DR GeneTree; ENSGT00390000017363; -.
DR HOGENOM; HOG000220856; -.
DR HOVERGEN; HBG031438; -.
DR InParanoid; O94818; -.
DR OMA; SEYRIED; -.
DR OrthoDB; EOG7JDR0F; -.
DR PhylomeDB; O94818; -.
DR TreeFam; TF325594; -.
DR ChiTaRS; NOL4; human.
DR GenomeRNAi; 8715; -.
DR NextBio; 32683; -.
DR PRO; PR:O94818; -.
DR Proteomes; UP000005640; Chromosome 18.
DR Bgee; O94818; -.
DR CleanEx; HS_NOL4; -.
DR ExpressionAtlas; O94818; baseline and differential.
DR Genevisible; O94818; HS.
DR GO; GO:0005730; C:nucleolus; TAS:ProtInc.
DR GO; GO:0005634; C:nucleus; IDA:HPA.
DR GO; GO:0003723; F:RNA binding; TAS:ProtInc.
DR InterPro; IPR026747; NOL4.
DR PANTHER; PTHR12449:SF17; PTHR12449:SF17; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Complete proteome; Nucleus; Reference proteome.
FT CHAIN 1 638 Nucleolar protein 4.
FT /FTId=PRO_0000096935.
FT VAR_SEQ 1 285 Missing (in isoform 4).
FT {ECO:0000303|PubMed:14702039}.
FT /FTId=VSP_045836.
FT VAR_SEQ 1 87 MESERDMYRQFQDWCLRTYGDSGKTKTVTRKKYERIVQLLN
FT GSESSSTDNAKFKFWVKSKGFQLGQPDEVRGGGGGAKQVLY
FT VPVKT -> MADLMQETFLHHA (in isoform 3).
FT {ECO:0000303|PubMed:14702039}.
FT /FTId=VSP_043344.
FT VAR_SEQ 413 514 Missing (in isoform 2).
FT {ECO:0000303|PubMed:15489334,
FT ECO:0000303|Ref.5, ECO:0000303|Ref.6}.
FT /FTId=VSP_010080.
FT CONFLICT 637 637 Q -> H (in Ref. 2; BAH12383).
FT {ECO:0000305}.
SQ SEQUENCE 638 AA; 71357 MW; 02DF0130F10E0B3F CRC64;
MESERDMYRQ FQDWCLRTYG DSGKTKTVTR KKYERIVQLL NGSESSSTDN AKFKFWVKSK
GFQLGQPDEV RGGGGGAKQV LYVPVKTTDG VGVDEKLSLR RVAVVEDFFD IIYSMHVETG
PNGEQIRKHA GQKRTYKAIS ESYAFLPREA VTRFLMSCSE CQKRMHLNPD GTDHKDNGKP
PTLVTSMIDY NMPITMAYMK HMKLQLLNSQ QDEDESSIES DEFDMSDSTR MSAVNSDLSS
NLEERMQSPQ NLHGQQDDDS AAESFNGNET LGHSSIASGG THSREMGDSN SDGKTGLEQD
EQPLNLSDSP LSAQLTSEYR IDDHNSNGKN KYKNLLISDL KMEREARENG SKSPAHSYSS
YDSGKNESVD RGAEDLSLNR GDEDEDDHED HDDSEKVNET DGVEAERLKA FNMFVRLFVD
ENLDRMVPIS KQPKEKIQAI IDSCRRQFPE YQERARKRIR TYLKSCRRMK RSGFEMSRPI
PSHLTSAVAE SILASACESE SRNAAKRMRL ERQQDESAPA DKQCKPEATQ ATYSTSAVPG
SQDVLYINGN GTYSYHSYRG LGGGLLNLND ASSSGPTDLS MKRQLATSSG SSSSSNSRPQ
LSPTEINAVR QLVAGYRESA AFLLRSADEL ENLILQQN
//
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";
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
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 PLCB1_HUMAN Reviewed; 1216 AA.
AC Q9NQ66; D3DW12; D3DW13; O60325; Q17RQ6; Q5TFF7; Q5TGC9; Q8IV93;
AC Q9BQW2; Q9H4H2; Q9H8H5; Q9NQ65; Q9NQH9; Q9NTH4; Q9UJP6; Q9UM26;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 11-NOV-2015, entry version 164.
DE RecName: Full=1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-1;
DE EC=3.1.4.11;
DE AltName: Full=PLC-154;
DE AltName: Full=Phosphoinositide phospholipase C-beta-1;
DE AltName: Full=Phospholipase C-I;
DE Short=PLC-I;
DE AltName: Full=Phospholipase C-beta-1;
DE Short=PLC-beta-1;
GN Name=PLCB1; Synonyms=KIAA0581;
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] (ISOFORMS A AND B).
RC TISSUE=Brain;
RX PubMed=11118617; DOI=10.1016/S0167-4781(00)00260-8;
RA Caricasole A., Sala C., Roncarati R., Formenti E., Terstappen G.C.;
RT "Cloning and characterization of the human phosphoinositide-specific
RT phospholipase C-beta 1 (PLCbeta1).";
RL Biochim. Biophys. Acta 1517:63-72(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
RC TISSUE=Brain;
RX PubMed=10760467; DOI=10.1016/S1388-1981(00)00012-3;
RA Peruzzi D., Calabrese G., Faenza I., Manzoli L., Matteucci A.,
RA Gianfrancesco F., Billi A.M., Stuppia L., Palka G., Cocco L.;
RT "Identification and chromosomal localisation by fluorescence in situ
RT hybridisation of human gene of phosphoinositide-specific phospholipase
RT C beta 1.";
RL Biochim. Biophys. Acta 1484:175-182(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
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 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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M.,
RA Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J.,
RA Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M.,
RA Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R.,
RA Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M.,
RA Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H.,
RA Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S.,
RA Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E.,
RA Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A.,
RA Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M.,
RA Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A.,
RA Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S.,
RA Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
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 A AND B).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 261-1216 (ISOFORM B).
RC TISSUE=Testis;
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 [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 417-1062 (ISOFORMS A AND B).
RC TISSUE=Placenta;
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 [10]
RP INTERACTION WITH DGKQ.
RX PubMed=12799190; DOI=10.1016/S0014-4827(03)00115-0;
RA Tabellini G., Bortul R., Santi S., Riccio M., Baldini G.,
RA Cappellini A., Billi A.M., Berezney R., Ruggeri A., Cocco L.,
RA Martelli A.M.;
RT "Diacylglycerol kinase-theta is localized in the speckle domains of
RT the nucleus.";
RL Exp. Cell Res. 287:143-154(2003).
RN [11]
RP INVOLVEMENT IN EIEE12.
RX PubMed=20833646; DOI=10.1093/brain/awq238;
RA Kurian M.A., Meyer E., Vassallo G., Morgan N.V., Prakash N., Pasha S.,
RA Hai N.A., Shuib S., Rahman F., Wassmer E., Cross J.H.,
RA O'Callaghan F.J., Osborne J.P., Scheffer I.E., Gissen P., Maher E.R.;
RT "Phospholipase C beta 1 deficiency is associated with early-onset
RT epileptic encephalopathy.";
RL Brain 133:2964-2970(2010).
RN [12]
RP VARIANT [LARGE SCALE ANALYSIS] PRO-907.
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: The production of the second messenger molecules
CC diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is
CC mediated by activated phosphatidylinositol-specific phospholipase
CC C enzymes.
CC -!- CATALYTIC ACTIVITY: 1-phosphatidyl-1D-myo-inositol 4,5-
CC bisphosphate + H(2)O = 1D-myo-inositol 1,4,5-trisphosphate +
CC diacylglycerol.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC -!- SUBUNIT: Interacts with DGKQ. {ECO:0000269|PubMed:12799190}.
CC -!- INTERACTION:
CC Q8TAP6:CEP76; NbExp=3; IntAct=EBI-3396023, EBI-742887;
CC Q13363-2:CTBP1; NbExp=3; IntAct=EBI-3396023, EBI-10171858;
CC P56545:CTBP2; NbExp=3; IntAct=EBI-3396023, EBI-741533;
CC Q8IY44:CTBP2; NbExp=3; IntAct=EBI-3396023, EBI-10171902;
CC Q12800:TFCP2; NbExp=3; IntAct=EBI-3396023, EBI-717422;
CC -!- SUBCELLULAR LOCATION: Nucleus membrane {ECO:0000250}. Cytoplasm
CC {ECO:0000250}. Note=Colocalizes with the adrenergic receptors,
CC ADREN1A and ADREN1B, at the nuclear membrane of cardiac myocytes.
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=A;
CC IsoId=Q9NQ66-1; Sequence=Displayed;
CC Name=B;
CC IsoId=Q9NQ66-2; Sequence=VSP_004718;
CC -!- DISEASE: Epileptic encephalopathy, early infantile, 12 (EIEE12)
CC [MIM:613722]: A form of epilepsy characterized by frequent tonic
CC seizures or spasms beginning in infancy with a specific EEG
CC finding of suppression-burst patterns, characterized by high-
CC voltage bursts alternating with almost flat suppression phases.
CC Patients may progress to West syndrome, which is characterized by
CC tonic spasms with clustering, arrest of psychomotor development,
CC and hypsarrhythmia on EEG. {ECO:0000269|PubMed:20833646}. Note=The
CC disease is caused by mutations affecting the gene represented in
CC this entry.
CC -!- MISCELLANEOUS: The receptor-mediated activation of PLC-beta-1 is
CC mediated by two G-protein alpha subunits, alpha-Q and alpha-11.
CC -!- SIMILARITY: Contains 1 C2 domain. {ECO:0000255|PROSITE-
CC ProRule:PRU00041}.
CC -!- SIMILARITY: Contains 1 PI-PLC X-box domain. {ECO:0000255|PROSITE-
CC ProRule:PRU00270}.
CC -!- SIMILARITY: Contains 1 PI-PLC Y-box domain. {ECO:0000255|PROSITE-
CC ProRule:PRU00271}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA25507.3; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
CC Sequence=BAB14641.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC and Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/PLCB1ID41742ch20p12.html";
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AJ278313; CAB98142.1; -; mRNA.
DR EMBL; AJ278314; CAB98143.1; -; mRNA.
DR EMBL; AY004175; AAF86613.1; -; mRNA.
DR EMBL; AB011153; BAA25507.3; ALT_INIT; mRNA.
DR EMBL; AL031683; CAI43121.1; -; Genomic_DNA.
DR EMBL; AL034551; CAI43121.1; JOINED; Genomic_DNA.
DR EMBL; AL049593; CAI43121.1; JOINED; Genomic_DNA.
DR EMBL; AL049632; CAI43121.1; JOINED; Genomic_DNA.
DR EMBL; AL050315; CAI43121.1; JOINED; Genomic_DNA.
DR EMBL; AL050323; CAI43121.1; JOINED; Genomic_DNA.
DR EMBL; AL031683; CAI43122.1; -; Genomic_DNA.
DR EMBL; AL034551; CAI43122.1; JOINED; Genomic_DNA.
DR EMBL; AL050315; CAI43122.1; JOINED; Genomic_DNA.
DR EMBL; AL049632; CAI43122.1; JOINED; Genomic_DNA.
DR EMBL; AL050323; CAI43122.1; JOINED; Genomic_DNA.
DR EMBL; AL034551; CAI21973.1; -; Genomic_DNA.
DR EMBL; AL031683; CAI21973.1; JOINED; Genomic_DNA.
DR EMBL; AL049593; CAI21973.1; JOINED; Genomic_DNA.
DR EMBL; AL049632; CAI21973.1; JOINED; Genomic_DNA.
DR EMBL; AL050315; CAI21973.1; JOINED; Genomic_DNA.
DR EMBL; AL050323; CAI21973.1; JOINED; Genomic_DNA.
DR EMBL; AL034551; CAI21974.1; -; Genomic_DNA.
DR EMBL; AL031683; CAI21974.1; JOINED; Genomic_DNA.
DR EMBL; AL050315; CAI21974.1; JOINED; Genomic_DNA.
DR EMBL; AL049632; CAI21974.1; JOINED; Genomic_DNA.
DR EMBL; AL050323; CAI21974.1; JOINED; Genomic_DNA.
DR EMBL; AL049593; CAI22175.1; -; Genomic_DNA.
DR EMBL; AL031683; CAI22175.1; JOINED; Genomic_DNA.
DR EMBL; AL034551; CAI22175.1; JOINED; Genomic_DNA.
DR EMBL; AL049632; CAI22175.1; JOINED; Genomic_DNA.
DR EMBL; AL050315; CAI22175.1; JOINED; Genomic_DNA.
DR EMBL; AL050323; CAI22175.1; JOINED; Genomic_DNA.
DR EMBL; AL049632; CAI43151.1; -; Genomic_DNA.
DR EMBL; AL031683; CAI43151.1; JOINED; Genomic_DNA.
DR EMBL; AL034551; CAI43151.1; JOINED; Genomic_DNA.
DR EMBL; AL049593; CAI43151.1; JOINED; Genomic_DNA.
DR EMBL; AL050315; CAI43151.1; JOINED; Genomic_DNA.
DR EMBL; AL050323; CAI43151.1; JOINED; Genomic_DNA.
DR EMBL; AL049632; CAI43152.1; -; Genomic_DNA.
DR EMBL; AL031683; CAI43152.1; JOINED; Genomic_DNA.
DR EMBL; AL034551; CAI43152.1; JOINED; Genomic_DNA.
DR EMBL; AL050315; CAI43152.1; JOINED; Genomic_DNA.
DR EMBL; AL050323; CAI43152.1; JOINED; Genomic_DNA.
DR EMBL; AL050315; CAI42238.1; -; Genomic_DNA.
DR EMBL; AL031683; CAI42238.1; JOINED; Genomic_DNA.
DR EMBL; AL034551; CAI42238.1; JOINED; Genomic_DNA.
DR EMBL; AL049593; CAI42238.1; JOINED; Genomic_DNA.
DR EMBL; AL049632; CAI42238.1; JOINED; Genomic_DNA.
DR EMBL; AL050323; CAI42238.1; JOINED; Genomic_DNA.
DR EMBL; AL050315; CAI42239.1; -; Genomic_DNA.
DR EMBL; AL031683; CAI42239.1; JOINED; Genomic_DNA.
DR EMBL; AL034551; CAI42239.1; JOINED; Genomic_DNA.
DR EMBL; AL049632; CAI42239.1; JOINED; Genomic_DNA.
DR EMBL; AL050323; CAI42239.1; JOINED; Genomic_DNA.
DR EMBL; AL050323; CAI22830.1; -; Genomic_DNA.
DR EMBL; AL031683; CAI22830.1; JOINED; Genomic_DNA.
DR EMBL; AL034551; CAI22830.1; JOINED; Genomic_DNA.
DR EMBL; AL049593; CAI22830.1; JOINED; Genomic_DNA.
DR EMBL; AL049632; CAI22830.1; JOINED; Genomic_DNA.
DR EMBL; AL050315; CAI22830.1; JOINED; Genomic_DNA.
DR EMBL; AL050323; CAI22831.1; -; Genomic_DNA.
DR EMBL; AL031683; CAI22831.1; JOINED; Genomic_DNA.
DR EMBL; AL034551; CAI22831.1; JOINED; Genomic_DNA.
DR EMBL; AL050315; CAI22831.1; JOINED; Genomic_DNA.
DR EMBL; AL049632; CAI22831.1; JOINED; Genomic_DNA.
DR EMBL; CH471133; EAX10372.1; -; Genomic_DNA.
DR EMBL; CH471133; EAX10373.1; -; Genomic_DNA.
DR EMBL; CH471133; EAX10374.1; -; Genomic_DNA.
DR EMBL; CH471133; EAX10376.1; -; Genomic_DNA.
DR EMBL; BC069420; AAH69420.1; -; mRNA.
DR EMBL; BC117231; AAI17232.1; -; mRNA.
DR EMBL; AL137267; CAB70666.1; -; mRNA.
DR EMBL; AK023689; BAB14641.1; ALT_INIT; mRNA.
DR CCDS; CCDS13102.1; -. [Q9NQ66-1]
DR CCDS; CCDS13103.1; -. [Q9NQ66-2]
DR RefSeq; NP_056007.1; NM_015192.3. [Q9NQ66-1]
DR RefSeq; NP_877398.1; NM_182734.2. [Q9NQ66-2]
DR UniGene; Hs.431173; -.
DR ProteinModelPortal; Q9NQ66; -.
DR SMR; Q9NQ66; 11-833.
DR BioGrid; 116841; 15.
DR IntAct; Q9NQ66; 6.
DR MINT; MINT-5005654; -.
DR STRING; 9606.ENSP00000338185; -.
DR BindingDB; Q9NQ66; -.
DR ChEMBL; CHEMBL4034; -.
DR PhosphoSite; Q9NQ66; -.
DR DMDM; 12643814; -.
DR MaxQB; Q9NQ66; -.
DR PaxDb; Q9NQ66; -.
DR PRIDE; Q9NQ66; -.
DR Ensembl; ENST00000338037; ENSP00000338185; ENSG00000182621. [Q9NQ66-1]
DR Ensembl; ENST00000378637; ENSP00000367904; ENSG00000182621. [Q9NQ66-2]
DR Ensembl; ENST00000378641; ENSP00000367908; ENSG00000182621. [Q9NQ66-2]
DR GeneID; 23236; -.
DR KEGG; hsa:23236; -.
DR UCSC; uc002wna.4; human. [Q9NQ66-2]
DR UCSC; uc002wnb.4; human. [Q9NQ66-1]
DR CTD; 23236; -.
DR GeneCards; PLCB1; -.
DR HGNC; HGNC:15917; PLCB1.
DR HPA; CAB004275; -.
DR HPA; CAB005334; -.
DR HPA; HPA034743; -.
DR HPA; HPA057910; -.
DR MIM; 607120; gene.
DR MIM; 613722; phenotype.
DR neXtProt; NX_Q9NQ66; -.
DR Orphanet; 293181; Malignant migrating partial seizures of infancy.
DR Orphanet; 3451; West syndrome.
DR PharmGKB; PA33384; -.
DR eggNOG; KOG0169; Eukaryota.
DR eggNOG; ENOG410XPSW; LUCA.
DR GeneTree; ENSGT00760000118936; -.
DR HOVERGEN; HBG053609; -.
DR InParanoid; Q9NQ66; -.
DR KO; K05858; -.
DR OMA; MMDFINL; -.
DR OrthoDB; EOG7WDN1N; -.
DR PhylomeDB; Q9NQ66; -.
DR TreeFam; TF313216; -.
DR BRENDA; 3.1.4.11; 2681.
DR Reactome; R-HSA-112043; PLC beta mediated events.
DR Reactome; R-HSA-1855204; Synthesis of IP3 and IP4 in the cytosol.
DR Reactome; R-HSA-399997; Acetylcholine regulates insulin secretion.
DR Reactome; R-HSA-4086398; Ca2+ pathway.
DR Reactome; R-HSA-416476; G alpha (q) signalling events.
DR Reactome; R-HSA-418217; G beta:gamma signalling through PLC beta.
DR Reactome; R-HSA-434316; Fatty Acids bound to GPR40 (FFAR1) regulate insulin secretion.
DR Reactome; R-HSA-500657; Presynaptic function of Kainate receptors.
DR SignaLink; Q9NQ66; -.
DR ChiTaRS; PLCB1; human.
DR GeneWiki; PLCB1; -.
DR GenomeRNAi; 23236; -.
DR NextBio; 44882; -.
DR PRO; PR:Q9NQ66; -.
DR Proteomes; UP000005640; Chromosome 20.
DR Bgee; Q9NQ66; -.
DR ExpressionAtlas; Q9NQ66; baseline and differential.
DR Genevisible; Q9NQ66; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
DR GO; GO:0043209; C:myelin sheath; IEA:Ensembl.
DR GO; GO:0000790; C:nuclear chromatin; ISS:BHF-UCL.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016607; C:nuclear speck; IDA:BHF-UCL.
DR GO; GO:0005634; C:nucleus; NAS:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005516; F:calmodulin binding; IPI:BHF-UCL.
DR GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
DR GO; GO:0005096; F:GTPase activator activity; IDA:BHF-UCL.
DR GO; GO:0004435; F:phosphatidylinositol phospholipase C activity; ISS:AgBase.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IDA:BHF-UCL.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:BHF-UCL.
DR GO; GO:0004871; F:signal transducer activity; IEA:UniProtKB-KW.
DR GO; GO:0060466; P:activation of meiosis involved in egg activation; ISS:BHF-UCL.
DR GO; GO:0021987; P:cerebral cortex development; ISS:BHF-UCL.
DR GO; GO:0045444; P:fat cell differentiation; IEA:Ensembl.
DR GO; GO:0007213; P:G-protein coupled acetylcholine receptor signaling pathway; ISS:BHF-UCL.
DR GO; GO:0000086; P:G2/M transition of mitotic cell cycle; ISS:BHF-UCL.
DR GO; GO:0007215; P:glutamate receptor signaling pathway; ISS:BHF-UCL.
DR GO; GO:0043647; P:inositol phosphate metabolic process; TAS:Reactome.
DR GO; GO:0048009; P:insulin-like growth factor receptor signaling pathway; ISS:BHF-UCL.
DR GO; GO:0070498; P:interleukin-1-mediated signaling pathway; IDA:BHF-UCL.
DR GO; GO:0035722; P:interleukin-12-mediated signaling pathway; IDA:BHF-UCL.
DR GO; GO:0035723; P:interleukin-15-mediated signaling pathway; IDA:BHF-UCL.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0007613; P:memory; ISS:BHF-UCL.
DR GO; GO:2000438; P:negative regulation of monocyte extravasation; ISS:BHF-UCL.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:BHF-UCL.
DR GO; GO:0046488; P:phosphatidylinositol metabolic process; ISS:BHF-UCL.
DR GO; GO:2000344; P:positive regulation of acrosome reaction; ISS:BHF-UCL.
DR GO; GO:2000560; P:positive regulation of CD24 biosynthetic process; ISS:BHF-UCL.
DR GO; GO:0048639; P:positive regulation of developmental growth; ISS:BHF-UCL.
DR GO; GO:0040019; P:positive regulation of embryonic development; ISS:BHF-UCL.
DR GO; GO:1900087; P:positive regulation of G1/S transition of mitotic cell cycle; ISS:BHF-UCL.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IDA:GOC.
DR GO; GO:0032735; P:positive regulation of interleukin-12 production; ISS:BHF-UCL.
DR GO; GO:0046330; P:positive regulation of JNK cascade; IDA:BHF-UCL.
DR GO; GO:0045663; P:positive regulation of myoblast differentiation; ISS:BHF-UCL.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:BHF-UCL.
DR GO; GO:0080154; P:regulation of fertilization; ISS:BHF-UCL.
DR GO; GO:0008277; P:regulation of G-protein coupled receptor protein signaling pathway; ISS:BHF-UCL.
DR GO; GO:0007165; P:signal transduction; NAS:UniProtKB.
DR GO; GO:0044281; P:small molecule metabolic process; TAS:Reactome.
DR GO; GO:0007268; P:synaptic transmission; TAS:Reactome.
DR Gene3D; 1.10.238.10; -; 1.
DR Gene3D; 2.60.40.150; -; 1.
DR Gene3D; 3.20.20.190; -; 2.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR001192; PI-PLC_fam.
DR InterPro; IPR016280; PLC-beta.
DR InterPro; IPR028400; PLC-beta1.
DR InterPro; IPR014815; PLC-beta_C.
DR InterPro; IPR009535; PLC-beta_CS.
DR InterPro; IPR017946; PLC-like_Pdiesterase_TIM-brl.
DR InterPro; IPR015359; PLC_EF-hand-like.
DR InterPro; IPR000909; PLipase_C_PInositol-sp_X_dom.
DR InterPro; IPR001711; PLipase_C_Pinositol-sp_Y.
DR PANTHER; PTHR10336; PTHR10336; 1.
DR PANTHER; PTHR10336:SF12; PTHR10336:SF12; 1.
DR Pfam; PF06631; DUF1154; 1.
DR Pfam; PF09279; EF-hand_like; 1.
DR Pfam; PF00388; PI-PLC-X; 1.
DR Pfam; PF00387; PI-PLC-Y; 1.
DR Pfam; PF08703; PLC-beta_C; 1.
DR PIRSF; PIRSF000956; PLC-beta; 1.
DR PRINTS; PR00390; PHPHLIPASEC.
DR SMART; SM00239; C2; 1.
DR SMART; SM00148; PLCXc; 1.
DR SMART; SM00149; PLCYc; 1.
DR SUPFAM; SSF49562; SSF49562; 1.
DR SUPFAM; SSF51695; SSF51695; 1.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS50007; PIPLC_X_DOMAIN; 1.
DR PROSITE; PS50008; PIPLC_Y_DOMAIN; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Complete proteome; Cytoplasm; Epilepsy;
KW Hydrolase; Lipid degradation; Lipid metabolism; Membrane; Nucleus;
KW Phosphoprotein; Polymorphism; Reference proteome; Transducer.
FT CHAIN 1 1216 1-phosphatidylinositol 4,5-bisphosphate
FT phosphodiesterase beta-1.
FT /FTId=PRO_0000088486.
FT DOMAIN 316 467 PI-PLC X-box. {ECO:0000255|PROSITE-
FT ProRule:PRU00270}.
FT DOMAIN 540 656 PI-PLC Y-box. {ECO:0000255|PROSITE-
FT ProRule:PRU00271}.
FT DOMAIN 663 761 C2. {ECO:0000255|PROSITE-
FT ProRule:PRU00041}.
FT ACT_SITE 331 331 {ECO:0000255|PROSITE-ProRule:PRU00270}.
FT ACT_SITE 378 378 {ECO:0000255|PROSITE-ProRule:PRU00270}.
FT MOD_RES 236 236 Phosphoserine.
FT {ECO:0000250|UniProtKB:Q9Z1B3}.
FT MOD_RES 417 417 Phosphoserine.
FT {ECO:0000250|UniProtKB:Q9Z1B3}.
FT MOD_RES 509 509 Phosphothreonine.
FT {ECO:0000250|UniProtKB:Q9Z1B3}.
FT MOD_RES 511 511 Phosphoserine.
FT {ECO:0000250|UniProtKB:Q9Z1B3}.
FT MOD_RES 582 582 Phosphoserine.
FT {ECO:0000250|UniProtKB:Q9Z1B3}.
FT MOD_RES 887 887 Phosphoserine; by PKC. {ECO:0000250}.
FT MOD_RES 978 978 Phosphoserine.
FT {ECO:0000250|UniProtKB:Q9Z1B3}.
FT MOD_RES 987 987 Phosphoserine.
FT {ECO:0000250|UniProtKB:Q9Z1B3}.
FT MOD_RES 1199 1199 Phosphoserine.
FT {ECO:0000250|UniProtKB:Q9Z1B3}.
FT MOD_RES 1200 1200 Phosphoserine.
FT {ECO:0000250|UniProtKB:Q9Z1B3}.
FT VAR_SEQ 1142 1216 LQVELEQEYQDKFKRLPLEILEFVQEAMKGKISEDSNHGSA
FT PLSLSSDPGKVNHKTPSSEELGGDIPGKEFDTPL -> GEG
FT SSSFLSETCHEDPSVSPNFTPPNPQALKW (in isoform
FT B). {ECO:0000303|PubMed:11118617,
FT ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:17974005}.
FT /FTId=VSP_004718.
FT VARIANT 854 854 E -> K (in dbSNP:rs2076413).
FT /FTId=VAR_050541.
FT VARIANT 907 907 A -> P (in a breast cancer sample;
FT somatic mutation).
FT {ECO:0000269|PubMed:16959974}.
FT /FTId=VAR_036547.
FT CONFLICT 1 34 MAGAQPGVHALQLKPVCVSDSLKKGTKFVKWDDD -> MGS
FT LQGIATKILIRILSDALIRKETDLKS (in Ref. 2;
FT AAF86613). {ECO:0000305}.
FT CONFLICT 189 189 L -> M (in Ref. 2; AAF86613).
FT {ECO:0000305}.
FT CONFLICT 203 203 P -> L (in Ref. 2; AAF86613).
FT {ECO:0000305}.
FT CONFLICT 216 216 L -> F (in Ref. 2; AAF86613).
FT {ECO:0000305}.
FT CONFLICT 221 221 P -> L (in Ref. 2; AAF86613).
FT {ECO:0000305}.
FT CONFLICT 266 266 L -> P (in Ref. 2; AAF86613).
FT {ECO:0000305}.
FT CONFLICT 309 309 P -> T (in Ref. 2; AAF86613).
FT {ECO:0000305}.
FT CONFLICT 320 320 Q -> R (in Ref. 2; AAF86613).
FT {ECO:0000305}.
FT CONFLICT 352 352 V -> A (in Ref. 2; AAF86613).
FT {ECO:0000305}.
FT CONFLICT 366 366 K -> R (in Ref. 2; AAF86613).
FT {ECO:0000305}.
FT CONFLICT 393 393 E -> K (in Ref. 2; AAF86613).
FT {ECO:0000305}.
FT CONFLICT 983 983 P -> S (in Ref. 1; CAB98143).
FT {ECO:0000305}.
SQ SEQUENCE 1216 AA; 138567 MW; 6F4263D1A50C6FD1 CRC64;
MAGAQPGVHA LQLKPVCVSD SLKKGTKFVK WDDDSTIVTP IILRTDPQGF FFYWTDQNKE
TELLDLSLVK DARCGRHAKA PKDPKLRELL DVGNIGRLEQ RMITVVYGPD LVNISHLNLV
AFQEEVAKEW TNEVFSLATN LLAQNMSRDA FLEKAYTKLK LQVTPEGRIP LKNIYRLFSA
DRKRVETALE ACSLPSSRND SIPQEDFTPE VYRVFLNNLC PRPEIDNIFS EFGAKSKPYL
TVDQMMDFIN LKQRDPRLNE ILYPPLKQEQ VQVLIEKYEP NNSLARKGQI SVDGFMRYLS
GEENGVVSPE KLDLNEDMSQ PLSHYFINSS HNTYLTAGQL AGNSSVEMYR QVLLSGCRCV
ELDCWKGRTA EEEPVITHGF TMTTEISFKE VIEAIAECAF KTSPFPILLS FENHVDSPKQ
QAKMAEYCRL IFGDALLMEP LEKYPLESGV PLPSPMDLMY KILVKNKKKS HKSSEGSGKK
KLSEQASNTY SDSSSMFEPS SPGAGEADTE SDDDDDDDDC KKSSMDEGTA GSEAMATEEM
SNLVNYIQPV KFESFEISKK RNKSFEMSSF VETKGLEQLT KSPVEFVEYN KMQLSRIYPK
GTRVDSSNYM PQLFWNAGCQ MVALNFQTMD LAMQINMGMY EYNGKSGYRL KPEFMRRPDK
HFDPFTEGIV DGIVANTLSV KIISGQFLSD KKVGTYVEVD MFGLPVDTRR KAFKTKTSQG
NAVNPVWEEE PIVFKKVVLP TLACLRIAVY EEGGKFIGHR ILPVQAIRPG YHYICLRNER
NQPLTLPAVF VYIEVKDYVP DTYADVIEAL SNPIRYVNLM EQRAKQLAAL TLEDEEEVKK
EADPGETPSE APSEARTTPA ENGVNHTTTL TPKPPSQALH SQPAPGSVKA PAKTEDLIQS
VLTEVEAQTI EELKQQKSFV KLQKKHYKEM KDLVKRHHKK TTDLIKEHTT KYNEIQNDYL
RRRAALEKSA KKDSKKKSEP SSPDHGSSTI EQDLAALDAE MTQKLIDLKD KQQQQLLNLR
QEQYYSEKYQ KREHIKLLIQ KLTDVAEECQ NNQLKKLKEI CEKEKKELKK KMDKKRQEKI
TEAKSKDKSQ MEEEKTEMIR SYIQEVVQYI KRLEEAQSKR QEKLVEKHKE IRQQILDEKP
KLQVELEQEY QDKFKRLPLE ILEFVQEAMK GKISEDSNHG SAPLSLSSDP GKVNHKTPSS
EELGGDIPGK EFDTPL
//
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}.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
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 TSH3_HUMAN Reviewed; 1081 AA.
AC Q63HK5; Q9H0G6; Q9P254;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2006, sequence version 2.
DT 11-NOV-2015, entry version 121.
DE RecName: Full=Teashirt homolog 3;
DE AltName: Full=Zinc finger protein 537;
GN Name=TSHZ3; Synonyms=KIAA1474, TSH3, ZNF537;
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], AND VARIANT GLY-469.
RC TISSUE=Endometrial tumor;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3-1081.
RC TISSUE=Brain;
RX PubMed=10819331; DOI=10.1093/dnares/7.2.143;
RA Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVII.
RT The complete sequences of 100 new cDNA clones from brain which code
RT for large proteins in vitro.";
RL DNA Res. 7:143-150(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 176-1081.
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 [4]
RP TISSUE SPECIFICITY.
RX PubMed=18776146; DOI=10.1242/dev.022442;
RA Caubit X., Lye C.M., Martin E., Core N., Long D.A., Vola C.,
RA Jenkins D., Garratt A.N., Skaer H., Woolf A.S., Fasano L.;
RT "Teashirt 3 is necessary for ureteral smooth muscle differentiation
RT downstream of SHH and BMP4.";
RL Development 135:3301-3310(2008).
RN [5]
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 [6]
RP FUNCTION, INTERACTION WITH APBB1; HDAC1 AND HDAC2, IDENTIFICATION IN A
RP TRIMERIC COMPLEX WITH APBB1 AND HDAC1, CHROMATIN-BINDING, MUTAGENESIS
RP OF 953-VAL--TYR-955, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=19343227; DOI=10.1371/journal.pone.0005071;
RA Kajiwara Y., Akram A., Katsel P., Haroutunian V., Schmeidler J.,
RA Beecham G., Haines J.L., Pericak-Vance M.A., Buxbaum J.D.;
RT "FE65 binds Teashirt, inhibiting expression of the primate-specific
RT caspase-4.";
RL PLoS ONE 4:E5071-E5071(2009).
RN [7]
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-682, AND IDENTIFICATION
RP 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 [9]
RP VARIANT GLY-469, AND DEVELOPMENTAL STAGE.
RX PubMed=19745106; DOI=10.1093/ndt/gfp453;
RA Jenkins D., Caubit X., Dimovski A., Matevska N., Lye C.M., Cabuk F.,
RA Gucev Z., Tasic V., Fasano L., Woolf A.S.;
RT "Analysis of TSHZ2 and TSHZ3 genes in congenital pelvi-ureteric
RT junction obstruction.";
RL Nephrol. Dial. Transplant. 25:54-60(2010).
RN [10]
RP STRUCTURE BY NMR OF 200-303.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the first and the second ZF-C2H2-like domains
RT of human teashirt homolog 3.";
RL Submitted (OCT-2006) to the PDB data bank.
CC -!- FUNCTION: Transcriptional regulator involved in developmental
CC processes. Function in association with APBB1, SET and HDAC
CC factors as a transcriptional repressor, that inhibits the
CC expression of CASP4. TSHZ3-mediated transcription repression
CC involves the recruitment of histone deacetylases HDAC1 and HDAC2.
CC Associates with chromatin in a region surrounding the CASP4
CC transcriptional start site(s). Regulates the development of
CC neurons involved in both respiratory rhythm and airflow control.
CC Promotes maintenance of nucleus ambiguus (nA) motoneurons, which
CC govern upper airway function, and establishes a respiratory rhythm
CC generator (RRG) activity compatible with survival at birth.
CC Involved in the differentiation of the proximal uretic smooth
CC muscle cells during developmental processes. Involved in the up-
CC regulation of myocardin, that directs the expression of smooth
CC muscle cells in the proximal ureter.
CC {ECO:0000269|PubMed:19343227}.
CC -!- SUBUNIT: Interacts (via homeobox domain) with APBB1 (via PID
CC domain 1). Interacts (via N-terminus) with HDAC1 and HDAC2; the
CC interaction is direct. Found in a trimeric complex with APBB1 and
CC HDAC1; the interaction between HDAC1 and APBB1 is mediated by
CC TSHZ3. {ECO:0000269|PubMed:19343227}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-
CC ProRule:PRU00108, ECO:0000269|PubMed:19343227}. Cell projection,
CC growth cone {ECO:0000250}. Note=Colocalizes with APBB1 in axonal
CC growth cone (By similarity). Colocalizes with APBB1 in the
CC nucleus. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in brain; strongly reduced in post-
CC mortem elderly subjects with Alzheimer disease.
CC {ECO:0000269|PubMed:18776146, ECO:0000269|PubMed:19343227}.
CC -!- DEVELOPMENTAL STAGE: Expressed in peri-urothelial cells of the
CC proximal ureter and renal pelvis at 9 weeks of gestation.
CC {ECO:0000269|PubMed:19745106}.
CC -!- SIMILARITY: Belongs to the teashirt C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
CC -!- SIMILARITY: Contains 5 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=CAB66739.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=Life's first breath -
CC Issue 122 of October 2010;
CC URL="http://web.expasy.org/spotlight/back_issues/122";
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; BX648745; CAH56184.1; -; mRNA.
DR EMBL; AB040907; BAA95998.1; -; mRNA.
DR EMBL; AL136805; CAB66739.1; ALT_INIT; mRNA.
DR CCDS; CCDS12421.2; -.
DR RefSeq; NP_065907.2; NM_020856.2.
DR UniGene; Hs.278436; -.
DR PDB; 2DMI; NMR; -; A=202-303.
DR PDBsum; 2DMI; -.
DR ProteinModelPortal; Q63HK5; -.
DR SMR; Q63HK5; 200-303.
DR BioGrid; 121663; 21.
DR IntAct; Q63HK5; 1.
DR MINT; MINT-4725267; -.
DR STRING; 9606.ENSP00000240587; -.
DR PhosphoSite; Q63HK5; -.
DR BioMuta; TSHZ3; -.
DR DMDM; 85541971; -.
DR MaxQB; Q63HK5; -.
DR PaxDb; Q63HK5; -.
DR PRIDE; Q63HK5; -.
DR DNASU; 57616; -.
DR Ensembl; ENST00000240587; ENSP00000240587; ENSG00000121297.
DR GeneID; 57616; -.
DR KEGG; hsa:57616; -.
DR UCSC; uc002nsy.4; human.
DR CTD; 57616; -.
DR GeneCards; TSHZ3; -.
DR HGNC; HGNC:30700; TSHZ3.
DR HPA; HPA008834; -.
DR MIM; 614119; gene.
DR neXtProt; NX_Q63HK5; -.
DR PharmGKB; PA134887020; -.
DR eggNOG; ENOG410IFDT; Eukaryota.
DR eggNOG; ENOG410XQQR; LUCA.
DR GeneTree; ENSGT00390000014977; -.
DR HOGENOM; HOG000231480; -.
DR HOVERGEN; HBG079626; -.
DR InParanoid; Q63HK5; -.
DR KO; K09236; -.
DR OMA; YIMSDLS; -.
DR OrthoDB; EOG7NPFSF; -.
DR PhylomeDB; Q63HK5; -.
DR TreeFam; TF328447; -.
DR ChiTaRS; TSHZ3; human.
DR EvolutionaryTrace; Q63HK5; -.
DR GeneWiki; TSHZ3; -.
DR GenomeRNAi; 57616; -.
DR NextBio; 64282; -.
DR PRO; PR:Q63HK5; -.
DR Proteomes; UP000005640; Chromosome 19.
DR Bgee; Q63HK5; -.
DR CleanEx; HS_TSHZ3; -.
DR ExpressionAtlas; Q63HK5; baseline and differential.
DR Genevisible; Q63HK5; HS.
DR GO; GO:0030426; C:growth cone; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007275; P:multicellular organismal development; IEA:UniProtKB-KW.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0002087; P:regulation of respiratory gaseous exchange by neurological system process; ISS:UniProtKB.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
DR InterPro; IPR001356; Homeobox_dom.
DR InterPro; IPR027008; Teashirt_fam.
DR InterPro; IPR026810; Tshz3.
DR InterPro; IPR007087; Znf_C2H2.
DR InterPro; IPR015880; Znf_C2H2-like.
DR PANTHER; PTHR12487; PTHR12487; 1.
DR PANTHER; PTHR12487:SF5; PTHR12487:SF5; 1.
DR SMART; SM00389; HOX; 1.
DR SMART; SM00355; ZnF_C2H2; 5.
DR PROSITE; PS50071; HOMEOBOX_2; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 4.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Cell projection; Coiled coil; Complete proteome;
KW Developmental protein; DNA-binding; Homeobox; Metal-binding; Nucleus;
KW Phosphoprotein; Polymorphism; Reference proteome; Repeat; Repressor;
KW Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1 1081 Teashirt homolog 3.
FT /FTId=PRO_0000047066.
FT ZN_FING 214 238 C2H2-type 1. {ECO:0000255|PROSITE-
FT ProRule:PRU00042}.
FT ZN_FING 275 299 C2H2-type 2. {ECO:0000255|PROSITE-
FT ProRule:PRU00042}.
FT ZN_FING 386 404 C2H2-type 3; atypical.
FT {ECO:0000255|PROSITE-ProRule:PRU00042}.
FT DNA_BIND 891 961 Homeobox; atypical. {ECO:0000255|PROSITE-
FT ProRule:PRU00108}.
FT ZN_FING 976 998 C2H2-type 4. {ECO:0000255|PROSITE-
FT ProRule:PRU00042}.
FT ZN_FING 1041 1064 C2H2-type 5. {ECO:0000255|PROSITE-
FT ProRule:PRU00042}.
FT COILED 606 630 {ECO:0000255}.
FT COMPBIAS 142 164 Ser-rich.
FT COMPBIAS 493 496 Poly-Glu.
FT MOD_RES 682 682 Phosphoserine.
FT {ECO:0000244|PubMed:21406692}.
FT VARIANT 469 469 E -> G (in dbSNP:rs143453460).
FT {ECO:0000269|PubMed:17974005,
FT ECO:0000269|PubMed:19745106}.
FT /FTId=VAR_063635.
FT VARIANT 687 687 P -> L (in dbSNP:rs4805664).
FT /FTId=VAR_052708.
FT MUTAGEN 953 955 VKY->ATA: Does not inhibit interaction
FT with APBB1.
FT {ECO:0000269|PubMed:19343227}.
FT STRAND 213 220 {ECO:0000244|PDB:2DMI}.
FT STRAND 222 225 {ECO:0000244|PDB:2DMI}.
FT HELIX 226 235 {ECO:0000244|PDB:2DMI}.
FT STRAND 278 280 {ECO:0000244|PDB:2DMI}.
FT HELIX 287 296 {ECO:0000244|PDB:2DMI}.
FT TURN 297 301 {ECO:0000244|PDB:2DMI}.
SQ SEQUENCE 1081 AA; 118566 MW; B4E0A4347B04E74A CRC64;
MPRRKQQAPR RAAAYVSEEL KAAALVDEGL DPEEHTADGE PSAKYMCPEK ELARACPSYQ
NSPAAEFSCH EMDSESHISE TSDRMADFES GSIKNEEETK EVTVPLEDTT VSDSLEQMKA
VYNNFLSNSY WSNLNLNLHQ PSSEKNNGSS SSSSSSSSSC GSGSFDWHQS AMAKTLQQVS
QSRMLPEPSL FSTVQLYRQS SKLYGSIFTG ASKFRCKDCS AAYDTLVELT VHMNETGHYR
DDNHETDNNN PKRWSKPRKR SLLEMEGKED AQKVLKCMYC GHSFESLQDL SVHMIKTKHY
QKVPLKEPVT PVAAKIIPAT RKKASLELEL PSSPDSTGGT PKATISDTND ALQKNSNPYI
TPNNRYGHQN GASYAWHFEA RKSQILKCME CGSSHDTLQE LTAHMMVTGH FIKVTNSAMK
KGKPIVETPV TPTITTLLDE KVQSVPLAAT TFTSPSNTPA SISPKLNVEV KKEVDKEKAV
TDEKPKQKDK PGEEEEKCDI SSKYHYLTEN DLEESPKGGL DILKSLENTV TSAINKAQNG
TPSWGGYPSI HAAYQLPNMM KLSLGSSGKS TPLKPMFGNS EIVSPTKNQT LVSPPSSQTS
PMPKTNFHAM EELVKKVTEK VAKVEEKMKE PDGKLSPPKR ATPSPCSSEV GEPIKMEASS
DGGFRSQENS PSPPRDGCKD GSPLAEPVEN GKELVKPLAS SLSGSTAIIT DHPPEQPFVN
PLSALQSVMN IHLGKAAKPS LPALDPMSML FKMSNSLAEK AAVATPPPLQ SKKADHLDRY
FYHVNNDQPI DLTKGKSDKG CSLGSVLLSP TSTAPATSSS TVTTAKTSAV VSFMSNSPLR
ENALSDISDM LKNLTESHTS KSSTPSSISE KSDIDGATLE EAEESTPAQK RKGRQSNWNP
QHLLILQAQF AASLRQTSEG KYIMSDLSPQ ERMHISRFTG LSMTTISHWL ANVKYQLRRT
GGTKFLKNLD TGHPVFFCND CASQIRTPST YISHLESHLG FRLRDLSKLS TEQINSQIAQ
TKSPSEKMVT SSPEEDLGTS YQCKLCNRTF ASKHAVKLHL SKTHGKSPED HLLYVSELEK
Q
//
Click here and save the page to download this output.
#~~# |
#~+~~+~# |
#~~# |
#LOG |
00:00:00 |
Activity Log for SLiMSuite V1.5.2: Wed Dec 9 01:11:19 2015 |
#DIR |
00:00:00 |
Run from directory: /srv/slimsuite/logs/prod |
#ARG |
00:00:00 |
Commandline arguments: run ip=122.150.74.70 slimfinder&uniprotid=Q9H6U6,Q96MA1,O15409,Q14526,P09067,Q13422,O94818,Q96MY1,P48552,Q9NQ66,Q99708,Q15583,Q63HK5&dismask=T&consmask=T&featuremask=T&ambiguity=T&slimlen=5&maxwild=2&jobid=15120900013 |
#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 runid=15120900013 rest=format uniprotid=Q9H6U6,Q96MA1,O15409,Q14526,P09067,Q13422,O94818,Q96MY1,P48552,Q9NQ66,Q99708,Q15583,Q63HK5 dismask=T consmask=T featuremask=T ambiguity=T slimlen=5 maxwild=2 jobid=15120900013 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 |
Command ftmask=T converted to default ftmask=EM,DOMAIN,TRANSMEM. |
#WARN |
00:00:00 |
NOTE: cloudfix=F. Be wary of ambiguity over-predictions. |
#URL |
00:00:03 |
Extracting 13 AccNum from http://www.uniprot.org/uniprot/: 13 read & extracted; 0 failed; 0 duplicates. |
#DAT |
00:00:04 |
Extracting entries from slimfinder.dat: 13 read, 13 extracted. |
#SEQ |
00:00:04 |
13 sequences loaded from /srv/slimsuite/scratch/prod/slimfinder/15120900013/slimfinder.dat (Format: uniprot). |
#FAS |
00:00:04 |
13 Sequences output to /srv/slimsuite/scratch/prod/slimfinder/15120900013/slimfinder.fas. |
#UPC |
00:00:04 |
No UPC file found. |
#FAS |
00:00:04 |
13 Sequences output to /srv/slimsuite/scratch/prod/slimfinder/15120900013/slimfinder.slimdb. |
#DICT |
00:00:04 |
Made "short" seqName dictionary: 13 seq; 13 keys. |
#DB |
00:00:04 |
/share/apps/blast+/2.2.29/bin/makeblastdb -in "/srv/slimsuite/scratch/prod/slimfinder/15120900013/slimfinder.slimdb" -out "/srv/slimsuite/scratch/prod/slimfinder/15120900013/slimfinder.slimdb" -title "/srv/slimsuite/scratch/prod/slimfinder/15120900013/slimfinder.slimdb" -parse_seqids -dbtype prot |
#SYS |
00:00:04 |
/share/apps/blast+/2.2.29/bin/blastp -query /srv/slimsuite/scratch/prod/slimfinder/15120900013/slimfinder.slimdb -db /srv/slimsuite/scratch/prod/slimfinder/15120900013/slimfinder.slimdb -out /srv/slimsuite/scratch/prod/slimfinder/15120900013/slimfinder.self.blast -seg yes -comp_based_stats F -soft_masking true -evalue 1.000000e-04 -num_descriptions 13 -num_alignments 13 |
#INDEX |
00:00:04 |
Indexed "Search" on "Query": 13 unique; 0 missing entries |
#CLUST |
00:00:04 |
8 clusters generated from 13 keys (maxdis=1.00) |
#DICT |
00:00:04 |
Made "short" seqName dictionary: 13 seq; 13 keys. |
#MST |
00:00:04 |
MST for 13 sequences = 12.111. |
#UP |
00:00:04 |
slimfinder: 13 Seq; 8 UPC; 12.111 MST; blaste=1.00e-04, blastcf=F, blastf=T |
#MAT |
00:00:04 |
slimfinder GABLAM Distance matrix out to /srv/slimsuite/scratch/prod/slimfinder/15120900013/slimfinder.dis.tdt (text format). |
#MIN |
00:00:04 |
AmbOcc 0.05 & 8 UP => AmbOcc 2 UPC. |
#MIN |
00:00:04 |
MinOcc 0.05 & 8 UP => MinOcc 3 UPC. |
#DIS |
00:00:04 |
Disorder score file: /srv/slimsuite/scratch/prod/slimfinder/15120900013/slimfinder.iupred.txt |
#MASK |
00:00:04 |
BCAS3_HUMAN__Q9H6U6 masked 28 ordered regions. (308 X added.) |
#MASK |
00:00:04 |
COM1_HUMAN__Q99708 masked 14 ordered regions. (46 X added.) |
#MASK |
00:00:04 |
DMRTB_HUMAN__Q96MA1 masked 1 ordered regions. (43 X added.) |
#MASK |
00:00:04 |
FOXP2_HUMAN__O15409 masked 14 ordered regions. (234 X added.) |
#MASK |
00:00:04 |
HIC1_HUMAN__Q14526 masked 22 ordered regions. (221 X added.) |
#MASK |
00:00:04 |
HXB5_HUMAN__P09067 masked 1 ordered regions. (35 X added.) |
#MASK |
00:00:04 |
IKZF1_HUMAN__Q13422 masked 8 ordered regions. (110 X added.) |
#MASK |
00:00:04 |
NOL4L_HUMAN__Q96MY1 masked 2 ordered regions. (27 X added.) |
#MASK |
00:00:04 |
NOL4_HUMAN__O94818 masked 11 ordered regions. (71 X added.) |
#MASK |
00:00:04 |
NRIP1_HUMAN__P48552 masked 10 ordered regions. (26 X added.) |
#MASK |
00:00:04 |
PLCB1_HUMAN__Q9NQ66 masked 47 ordered regions. (436 X added.) |
#MASK |
00:00:04 |
TGIF1_HUMAN__Q15583 masked 10 ordered regions. (57 X added.) |
#MASK |
00:00:04 |
TSH3_HUMAN__Q63HK5 masked 16 ordered regions. (113 X added.) |
#DB |
00:00:04 |
/srv/slimsuite/data/orthdb/qfo_ref.2015-04/qfo_ref.2015-04.Eukaryota.fas already formatted. (Force = False). |
#MASK |
00:00:04 |
Masked BCAS3_HUMAN__Q9H6U6 low relative conservation. (326 X added to 928aa seq.) |
#MASK |
00:00:04 |
Masked COM1_HUMAN__Q99708 low relative conservation. (377 X added to 897aa seq.) |
#MASK |
00:00:04 |
Masked DMRTB_HUMAN__Q96MA1 low relative conservation. (164 X added to 342aa seq.) |
#MASK |
00:00:04 |
Masked FOXP2_HUMAN__O15409 low relative conservation. (190 X added to 715aa seq.) |
#MASK |
00:00:04 |
Masked HIC1_HUMAN__Q14526 low relative conservation. (238 X added to 733aa seq.) |
#MASK |
00:00:04 |
Masked HXB5_HUMAN__P09067 low relative conservation. (109 X added to 269aa seq.) |
#MASK |
00:00:04 |
Masked IKZF1_HUMAN__Q13422 low relative conservation. (177 X added to 519aa seq.) |
#MASK |
00:00:04 |
Masked NOL4L_HUMAN__Q96MY1 low relative conservation. (167 X added to 436aa seq.) |
#MASK |
00:00:04 |
Masked NOL4_HUMAN__O94818 low relative conservation. (285 X added to 638aa seq.) |
#MASK |
00:00:04 |
Masked NRIP1_HUMAN__P48552 low relative conservation. (544 X added to 1158aa seq.) |
#MASK |
00:00:04 |
Masked PLCB1_HUMAN__Q9NQ66 low relative conservation. (383 X added to 1216aa seq.) |
#MASK |
00:00:04 |
Masked TGIF1_HUMAN__Q15583 low relative conservation. (159 X added to 401aa seq.) |
#MASK |
00:00:04 |
Masked TSH3_HUMAN__Q63HK5 low relative conservation. (336 X added to 1081aa seq.) |
#REL |
00:00:04 |
3,455 aa masked using relative conservation |
#FTMASK |
00:00:04 |
FTMask: EM,DOMAIN,TRANSMEM |
#MASK |
00:00:04 |
BCAS3_HUMAN__Q9H6U6 masked 0 features. (0 X added.) |
#MASK |
00:00:04 |
COM1_HUMAN__Q99708 masked 0 features. (0 X added.) |
#MASK |
00:00:04 |
DMRTB_HUMAN__Q96MA1 masked 0 features. (0 X added.) |
#MASK |
00:00:04 |
FOXP2_HUMAN__O15409 masked 0 features. (0 X added.) |
#MASK |
00:00:04 |
HIC1_HUMAN__Q14526 masked 1 features. (0 X added.) |
#MASK |
00:00:04 |
HXB5_HUMAN__P09067 masked 0 features. (0 X added.) |
#MASK |
00:00:04 |
IKZF1_HUMAN__Q13422 masked 0 features. (0 X added.) |
#MASK |
00:00:04 |
NOL4L_HUMAN__Q96MY1 masked 0 features. (0 X added.) |
#MASK |
00:00:04 |
NOL4_HUMAN__O94818 masked 0 features. (0 X added.) |
#MASK |
00:00:04 |
NRIP1_HUMAN__P48552 masked 0 features. (0 X added.) |
#MASK |
00:00:04 |
PLCB1_HUMAN__Q9NQ66 masked 3 features. (93 X added.) |
#MASK |
00:00:04 |
TGIF1_HUMAN__Q15583 masked 0 features. (0 X added.) |
#MASK |
00:00:04 |
TSH3_HUMAN__Q63HK5 masked 0 features. (0 X added.) |
#MASK |
00:00:04 |
Masked DMRTB_HUMAN__Q96MA1 "low complexity" regions. (3 X added.) |
#MASK |
00:00:04 |
Masked FOXP2_HUMAN__O15409 "low complexity" regions. (3 X added.) |
#MASK |
00:00:04 |
Masked HIC1_HUMAN__Q14526 "low complexity" regions. (3 X added.) |
#MASK |
00:00:04 |
Masked NRIP1_HUMAN__P48552 "low complexity" regions. (6 X added.) |
#MASK |
00:00:04 |
Masked TGIF1_HUMAN__Q15583 "low complexity" regions. (9 X added.) |
#MASK |
00:00:04 |
Masked TSH3_HUMAN__Q63HK5 "low complexity" regions. (7 X added.) |
#MASK |
00:00:04 |
MetMask: 5 N-terminal Ms masked |
#MASK |
00:00:04 |
Masked PLCB1_HUMAN__Q9NQ66 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 13 seq: 1,142 dimers |
#DIM |
00:00:04 |
Reducing dimers: 967 >= 2 of 8 UPC |
#SLIM |
00:00:04 |
Selecting 2aa SLiMs: 967 >= 2 of 8 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 |
00:00:11 |
Extending 3aa SLiMs >= 2 of 8 UPC: 1,952 SLiMs |
#AMB |
00:00:12 |
Adding Wildcard ambiguity: 100.0% (523 amb motifs) |
#AMB |
00:00:12 |
Adding Degeneracy ambiguity: 100.0% (739 amb motifs) |
#SLIM |
00:00:18 |
Extending 4aa SLiMs >= 2 of 8 UPC: 309 SLiMs |
#AMB |
00:00:19 |
Adding Wildcard ambiguity: 100.0% (15 amb motifs) |
#AMB |
00:00:19 |
Adding Degeneracy ambiguity: 100.0% (6 amb motifs) |
#SLIM |
00:00:20 |
Extending 5aa SLiMs >= 2 of 8 UPC: 36 SLiMs |
#AMB |
00:00:20 |
Adding Wildcard ambiguity: 100.0% (0 amb motifs) |
#AMB |
00:00:20 |
Adding Degeneracy ambiguity: 100.0% (0 amb motifs) |
#SLIM |
00:00:20 |
4,547 SLiMs >= 2 of 8 UPC |
#SAVE |
00:00:20 |
SLiMFinder Intermediate saved as /srv/slimsuite/scratch/prod/slimfinder/15120900013/slimfinder.l5w2o2a3.FreqConsDisComp-5-8FT.pickle (Python pickle). |
#GZIP |
00:00:20 |
/srv/slimsuite/scratch/prod/slimfinder/15120900013/slimfinder.l5w2o2a3.FreqConsDisComp-5-8FT.pickle zipped. |
#SLIM |
00:00:20 |
Filtering 4,547 SLiMs: 1,595 retained. |
#PROB |
00:00:21 |
Calculating [Sig] SLiM Probabilities (Sig<=0.10) complete: 2 ranked SLiMs. |
#COMB |
00:00:21 |
Combined Occurrence Attributes complete. |
#CLOUD |
00:00:21 |
Making "Motif Clouds" for 2 Sig Motifs: 1 Clouds |
#SLIM |
00:00:21 |
Cloud 1 (P.DLS|DLS) SLiMMaker: [GP].DLS |
#FREQ |
00:00:21 |
SLiMMaker SLiM matches 9 of 12 sequences (75.0%). |
#RANK |
00:00:21 |
Rank calculations complete |
#CLOUD |
00:00:21 |
Motif cloud data output to /srv/slimsuite/scratch/prod/slimfinder/15120900013/slimfinder.l5w2o2a3.15120900013.cloud.txt for 1 clouds. |
#FAS |
00:00:21 |
13 Sequences output to /srv/slimsuite/scratch/prod/slimfinder/15120900013/slimfinder.l5w2o2a3.15120900013.masked.fas. |
#FAS |
00:00:21 |
39 Sequences output to /srv/slimsuite/scratch/prod/slimfinder/15120900013/slimfinder.l5w2o2a3.15120900013.mapping.fas. |
#ALN |
00:00:21 |
Constructing motif alignments: 2 motifs & 9 seqs.: 100.0%. |
#FAS |
00:00:22 |
13 Sequences output to /srv/slimsuite/scratch/prod/slimfinder/15120900013/slimfinder.l5w2o2a3.15120900013.motifaln.fas. |
#ALN |
00:00:22 |
Constructing motif alignments: 2 motifs & 9 seqs.: 100.0%. |
#FAS |
00:00:22 |
13 Sequences output to /srv/slimsuite/scratch/prod/slimfinder/15120900013/slimfinder.l5w2o2a3.15120900013.maskaln.fas. |
#OCC |
00:00:22 |
Occurrence data output for 18 motif occurrences. |
#RES |
00:00:22 |
SLiMFinder results output to /srv/slimsuite/scratch/prod/slimfinder/15120900013/slimfinder.csv and /srv/slimsuite/scratch/prod/slimfinder/15120900013/slimfinder.occ.csv. |
#RES |
00:00:22 |
Additional dataset results output to /srv/slimsuite/scratch/prod/slimfinder/15120900013/slimfinder.* |
#END |
00:00:22 |
SLiMFinder server run ended (Finished!): see log file for details. |
#WARN |
00:00:22 |
2 warning messages: check log for details. |
#LOG |
00:00:22 |
SLiMFinder V5.2.3 End: Wed Dec 9 01:11:41 2015 |
#JOBID |
00:00:22 |
15120900013 |
#REST |
00:00:22 |
URL for future retrieval: http://rest.slimsuite.unsw.edu.au/retrieve&jobid=15120900013&rest=format&password=None |
Click here and save the page to download this output.
#WARN 00:00:00 Command ftmask=T converted to default ftmask=EM,DOMAIN,TRANSMEM.
#WARN 00:00:00 NOTE: cloudfix=F. Be wary of ambiguity over-predictions.
© 2015 RJ Edwards. Contact: richard.edwards@unsw.edu.au.
|