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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

Click here for SLiMFinder help/documentation. Click on tabs to see server output. (Mouseover for description.)

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

JobID 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

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

Different sources of input can also be given with:
`slimfinder`&seqin=LIST&dismask=T/F&consmask=T/F

Run with &rest=help for general options. Run with &rest=full to get full server output as plain text. Otherwise,
individual outputs are parsed and presented in different tabs:

### Outputs available:
    main = main results file (extras=-1)
    seqin = Input file (extras=-1)
    occ = occurrence file (extras=0)
    upc = UPC file (extras=0)
    slimdb = Fasta file used for UPC generation etc. (extras=0)
    cloud = cloud.txt (extras=1)
    masked = masked.fas (extras=1)
    mapping = mapping.fas file (extras=1)
    motifaln = motif alignments (extras=1)
    maskaln = masked motif alignments (extras=1)
    motifs = motifs file for CompariMotif (extras=2)
    compare = CM compare.tdt file (extras=2)
    xgmml = XGMML file (extras=2)
    dismatrix = *.dis.tdt file (extras=3)
    rank = optional SLiMDisc output (extras=3)
    dat.rank = optional SLiMDisc output (extras=3)

&rest=OUTFMT can then be used to retrieve individual parts of the output in future.
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
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
#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
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

>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;
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
>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
>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
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
>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
>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-
>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-
>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
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";
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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   -----------------------------------------------------------------------
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DR   EMBL; AF043431; AAC34368.1; -; mRNA.
DR   EMBL; U72066; AAC14371.1; -; mRNA.
DR   EMBL; AK292481; BAF85170.1; -; mRNA.
DR   EMBL; BX648221; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AC091147; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC106033; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471088; EAX01144.1; -; Genomic_DNA.
DR   EMBL; BC030590; AAH30590.1; -; mRNA.
DR   CCDS; CCDS11874.1; -. [Q99708-3]
DR   CCDS; CCDS11875.1; -. [Q99708-1]
DR   RefSeq; NP_002885.1; NM_002894.2. [Q99708-1]
DR   RefSeq; NP_976036.1; NM_203291.1. [Q99708-1]
DR   RefSeq; NP_976037.1; NM_203292.1. [Q99708-3]
DR   RefSeq; XP_006722582.1; XM_006722519.1. [Q99708-1]
DR   RefSeq; XP_006722583.1; XM_006722520.1. [Q99708-1]
DR   RefSeq; XP_006722584.1; XM_006722521.1. [Q99708-1]
DR   RefSeq; XP_011524434.1; XM_011526132.1. [Q99708-1]
DR   UniGene; Hs.546282; -.
DR   PDB; 2L4Z; NMR; -; A=641-685.
DR   PDB; 4D2H; X-ray; 1.90 A; A/B/C/D/E/F/G/H=18-52.
DR   PDBsum; 2L4Z; -.
DR   PDBsum; 4D2H; -.
DR   ProteinModelPortal; Q99708; -.
DR   SMR; Q99708; 18-52, 641-677.
DR   BioGrid; 111867; 43.
DR   DIP; DIP-24244N; -.
DR   IntAct; Q99708; 27.
DR   MINT; MINT-102295; -.
DR   STRING; 9606.ENSP00000323050; -.
DR   PhosphoSite; Q99708; -.
DR   BioMuta; RBBP8; -.
DR   DMDM; 116242745; -.
DR   MaxQB; Q99708; -.
DR   PaxDb; Q99708; -.
DR   PRIDE; Q99708; -.
DR   DNASU; 5932; -.
DR   Ensembl; ENST00000327155; ENSP00000323050; ENSG00000101773. [Q99708-1]
DR   Ensembl; ENST00000399722; ENSP00000382628; ENSG00000101773. [Q99708-1]
DR   Ensembl; ENST00000399725; ENSP00000382630; ENSG00000101773. [Q99708-3]
DR   GeneID; 5932; -.
DR   KEGG; hsa:5932; -.
DR   UCSC; uc002ktw.3; human. [Q99708-1]
DR   UCSC; uc002ktz.3; human.
DR   CTD; 5932; -.
DR   GeneCards; RBBP8; -.
DR   GeneReviews; RBBP8; -.
DR   HGNC; HGNC:9891; RBBP8.
DR   HPA; HPA039890; -.
DR   HPA; HPA052946; -.
DR   MIM; 251255; phenotype.
DR   MIM; 604124; gene.
DR   MIM; 606744; phenotype.
DR   neXtProt; NX_Q99708; -.
DR   Orphanet; 313795; Jawad syndrome.
DR   Orphanet; 808; Seckel syndrome.
DR   PharmGKB; PA34255; -.
DR   eggNOG; ENOG410IJ39; Eukaryota.
DR   eggNOG; ENOG410ZSBE; LUCA.
DR   GeneTree; ENSGT00530000063835; -.
DR   HOGENOM; HOG000293331; -.
DR   HOVERGEN; HBG057046; -.
DR   InParanoid; Q99708; -.
DR   OrthoDB; EOG771274; -.
DR   PhylomeDB; Q99708; -.
DR   TreeFam; TF106469; -.
DR   Reactome; R-HSA-912446; Meiotic recombination.
DR   ChiTaRS; RBBP8; human.
DR   EvolutionaryTrace; Q99708; -.
DR   GeneWiki; RBBP8; -.
DR   GenomeRNAi; 5932; -.
DR   NextBio; 23118; -.
DR   PRO; PR:Q99708; -.
DR   Proteomes; UP000005640; Chromosome 18.
DR   Bgee; Q99708; -.
DR   CleanEx; HS_RBBP8; -.
DR   ExpressionAtlas; Q99708; baseline and differential.
DR   Genevisible; Q99708; HS.
DR   GO; GO:0005730; C:nucleolus; IDA:HPA.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; TAS:ProtInc.
DR   GO; GO:0017053; C:transcriptional repressor complex; IDA:BHF-UCL.
DR   GO; GO:0003684; F:damaged DNA binding; IDA:UniProtKB.
DR   GO; GO:0001103; F:RNA polymerase II repressing transcription factor binding; IPI:BHF-UCL.
DR   GO; GO:0001106; F:RNA polymerase II transcription corepressor activity; IDA:BHF-UCL.
DR   GO; GO:0000014; F:single-stranded DNA endodeoxyribonuclease activity; IMP:UniProtKB.
DR   GO; GO:0001835; P:blastocyst hatching; IEA:Ensembl.
DR   GO; GO:0000075; P:cell cycle checkpoint; TAS:ProtInc.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0010792; P:DNA double-strand break processing involved in repair via single-strand annealing; IMP:UniProtKB.
DR   GO; GO:0006281; P:DNA repair; TAS:ProtInc.
DR   GO; GO:0000724; P:double-strand break repair via homologous recombination; IDA:UniProtKB.
DR   GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IEA:Ensembl.
DR   GO; GO:0031572; P:G2 DNA damage checkpoint; IDA:UniProtKB.
DR   GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0007067; P:mitotic nuclear division; IEA:UniProtKB-KW.
DR   GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:GOC.
DR   GO; GO:0006289; P:nucleotide-excision repair; IMP:CACAO.
DR   GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; TAS:ProtInc.
DR   GO; GO:0032355; P:response to estradiol; IEA:Ensembl.
DR   InterPro; IPR013882; Com1/Ctip_fam.
DR   InterPro; IPR019518; CtIP_N.
DR   Pfam; PF10482; CtIP_N; 1.
DR   Pfam; PF08573; SAE2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative splicing; Cell cycle;
KW   Cell division; Coiled coil; Complete proteome; DNA damage; DNA repair;
KW   DNA-binding; Dwarfism; Endonuclease; Hydrolase; Isopeptide bond;
KW   Meiosis; Mental retardation; Mitosis; Nuclease; Nucleus;
KW   Phosphoprotein; Polymorphism; Reference proteome; Ubl conjugation.
FT   CHAIN         1    897       DNA endonuclease RBBP8.
FT                                /FTId=PRO_0000097179.
FT   REGION       22     45       Essential for binding to the MRN complex
FT                                and for RPA focus formation on DNA
FT                                damage.
FT   REGION      509    557       Damage-recruitment motif.
FT   COILED       28    157       {ECO:0000255}.
FT   MOTIF       490    494       PXDLS motif.
FT   COMPBIAS    750    753       Poly-Glu.
FT   MOD_RES     233    233       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q80YR6}.
FT   MOD_RES     326    326       Phosphoserine.
FT                                {ECO:0000269|PubMed:17965729}.
FT   MOD_RES     327    327       Phosphoserine.
FT                                {ECO:0000269|PubMed:15485915}.
FT   MOD_RES     349    349       Phosphoserine.
FT                                {ECO:0000269|PubMed:17965729}.
FT   MOD_RES     432    432       N6-acetyllysine.
FT                                {ECO:0000269|PubMed:20829486}.
FT   MOD_RES     526    526       N6-acetyllysine.
FT                                {ECO:0000269|PubMed:20829486}.
FT   MOD_RES     604    604       N6-acetyllysine.
FT                                {ECO:0000269|PubMed:20829486}.
FT   MOD_RES     664    664       Phosphoserine; by ATM.
FT                                {ECO:0000269|PubMed:10910365}.
FT   MOD_RES     679    679       Phosphoserine.
FT                                {ECO:0000269|PubMed:17965729}.
FT   MOD_RES     723    723       Phosphoserine.
FT                                {ECO:0000244|PubMed:20068231}.
FT   MOD_RES     745    745       Phosphoserine; by ATM.
FT                                {ECO:0000269|PubMed:10910365}.
FT   MOD_RES     847    847       Phosphothreonine; by CDK1.
FT                                {ECO:0000269|PubMed:19202191}.
FT   CROSSLNK    869    869       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:25218447}.
FT   VAR_SEQ     714    714       S -> SMLFYI (in isoform 2).
FT                                {ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_043220.
FT   VAR_SEQ     786    867       RETSLQNFPHIEVVRKKEERRKLLGHTCKECEIYYADMPAE
FT                                EREKKLASCSRHRFRYIPPNTPENFWEVGFPSTQTCMERGY
FT                                -> SIMQICQQKKEKRNWLPAQDTDSATFHPTHQRIFGKLV
FT                                FLPLRLVWKEVILRKILILVLVQKDVSLTTQYFLQKARSRR
FT                                HRR (in isoform 3).
FT                                {ECO:0000303|PubMed:17974005}.
FT                                /FTId=VSP_045247.
FT   VAR_SEQ     868    897       Missing (in isoform 3).
FT                                {ECO:0000303|PubMed:17974005}.
FT                                /FTId=VSP_045248.
FT   VARIANT     357    357       K -> N (in dbSNP:rs34678569).
FT                                /FTId=VAR_051308.
FT   VARIANT     387    387       H -> Y (in dbSNP:rs1804732).
FT                                /FTId=VAR_028308.
FT   MUTAGEN      31     31       H->A: No effect on RPA focus formation on
FT                                DNA damage.
FT                                {ECO:0000269|PubMed:19759395}.
FT   MUTAGEN      35     35       V->A: No effect on RPA focus formation on
FT                                DNA damage.
FT                                {ECO:0000269|PubMed:19759395}.
FT   MUTAGEN      41     41       K->A: No effect on RPA focus formation on
FT                                DNA damage.
FT                                {ECO:0000269|PubMed:19759395}.
FT   MUTAGEN      45     45       L->A: No effect on RPA focus formation on
FT                                DNA damage.
FT                                {ECO:0000269|PubMed:19759395}.
FT   MUTAGEN     327    327       S->A: Abolishes BRCA1 interaction and
FT                                ubiquitination. No activation of CHEK1
FT                                after DNA damage.
FT                                {ECO:0000269|PubMed:15485915,
FT                                ECO:0000269|PubMed:16818604}.
FT   MUTAGEN     432    432       K->R: Greatly reduced acetylation.
FT                                Alleviates resection defects caused by
FT                                depletion of SIRT6; when associated with
FT                                R-526 and R-604.
FT                                {ECO:0000269|PubMed:20829486}.
FT   MUTAGEN     513    513       K->A: Abolishes damage recruitment
FT                                capability.
FT                                {ECO:0000269|PubMed:20064462}.
FT   MUTAGEN     515    515       K->A: Abolishes damage recruitment
FT                                capability.
FT                                {ECO:0000269|PubMed:20064462}.
FT   MUTAGEN     526    526       K->R: Greatly reduced acetylation.
FT                                Alleviates resection defects caused by
FT                                depletion of SIRT6; when associated with
FT                                R-432 and R-604.
FT                                {ECO:0000269|PubMed:20829486}.
FT   MUTAGEN     604    604       K->R: Greatly reduced acetylation.
FT                                Alleviates resection defects caused by
FT                                depletion of SIRT6; when associated with
FT                                R-432 and R-526.
FT                                {ECO:0000269|PubMed:20829486}.
FT   MUTAGEN     664    664       S->A: Abrogates dissociation of BRCA1.
FT                                {ECO:0000269|PubMed:10910365}.
FT   MUTAGEN     745    745       S->A: Abrogates dissociation of BRCA1.
FT                                {ECO:0000269|PubMed:10910365}.
FT   MUTAGEN     847    847       T->A: Impairs DNA resection.
FT                                {ECO:0000269|PubMed:19202191}.
FT   MUTAGEN     847    847       T->E: Mimics constitutive
FT                                phosphorylation.
FT                                {ECO:0000269|PubMed:19202191}.
FT   CONFLICT      4      4       S -> L (in Ref. 1; AAC14371).
FT                                {ECO:0000305}.
FT   CONFLICT     74     74       H -> Q (in Ref. 4; BX648221).
FT                                {ECO:0000305}.
FT   CONFLICT     92     92       C -> Y (in Ref. 3; BAF85170).
FT                                {ECO:0000305}.
FT   CONFLICT    123    123       E -> G (in Ref. 3; BAF85170).
FT                                {ECO:0000305}.
FT   CONFLICT    341    341       D -> G (in Ref. 4; BX648221).
FT                                {ECO:0000305}.
FT   CONFLICT    515    515       K -> R (in Ref. 4; BX648221).
FT                                {ECO:0000305}.
FT   CONFLICT    521    521       L -> P (in Ref. 3; BAF85170).
FT                                {ECO:0000305}.
FT   CONFLICT    642    642       L -> P (in Ref. 4; BX648221).
FT                                {ECO:0000305}.
FT   HELIX        18     50       {ECO:0000244|PDB:4D2H}.
FT   STRAND      648    650       {ECO:0000244|PDB:2L4Z}.
FT   HELIX       651    653       {ECO:0000244|PDB:2L4Z}.
FT   TURN        662    666       {ECO:0000244|PDB:2L4Z}.
FT   STRAND      677    679       {ECO:0000244|PDB:2L4Z}.
SQ   SEQUENCE   897 AA;  101942 MW;  E028DE56DE55C0F2 CRC64;
     MNISGSSCGS PNSADTSSDF KDLWTKLKEC HDREVQGLQV KVTKLKQERI LDAQRLEEFF
     TKNQQLREQQ KVLHETIKVL EDRLRAGLCD RCAVTEEHMR KKQQEFENIR QQNLKLITEL
     MNERNTLQEE NKKLSEQLQQ KIENDQQHQA AELECEEDVI PDSPITAFSF SGVNRLRRKE
     NPHVRYIEQT HTKLEHSVCA NEMRKVSKSS THPQHNPNEN EILVADTYDQ SQSPMAKAHG
     TSSYTPDKSS FNLATVVAET LGLGVQEESE TQGPMSPLGD ELYHCLEGNH KKQPFEESTR
     NTEDSLRFSD STSKTPPQEE LPTRVSSPVF GATSSIKSGL DLNTSLSPSL LQPGKKKHLK
     TLPFSNTCIS RLEKTRSKSE DSALFTHHSL GSEVNKIIIQ SSNKQILINK NISESLGEQN
     RTEYGKDSNT DKHLEPLKSL GGRTSKRKKT EEESEHEVSC PQASFDKENA FPFPMDNQFS
     MNGDCVMDKP LDLSDRFSAI QRQEKSQGSE TSKNKFRQVT LYEALKTIPK GFSSSRKASD
     GNCTLPKDSP GEPCSQECII LQPLNKCSPD NKPSLQIKEE NAVFKIPLRP RESLETENVL
     DDIKSAGSHE PIKIQTRSDH GGCELASVLQ LNPCRTGKIK SLQNNQDVSF ENIQWSIDPG
     ADLSQYKMDV TVIDTKDGSQ SKLGGETVDM DCTLVSETVL LKMKKQEQKG EKSSNEERKM
     NDSLEDMFDR TTHEEYESCL ADSFSQAADE EEELSTATKK LHTHGDKQDK VKQKAFVEPY
     FKGDERETSL QNFPHIEVVR KKEERRKLLG HTCKECEIYY ADMPAEEREK KLASCSRHRF
     RYIPPNTPEN FWEVGFPSTQ TCMERGYIKE DLDPCPRPKR RQPYNAIFSP KGKEQKT
//
ID   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}.
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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";
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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";
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DR   EMBL; L41919; AAD09201.1; -; Genomic_DNA.
DR   EMBL; AC090617; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471108; EAW90562.1; -; Genomic_DNA.
DR   EMBL; CH471108; EAW90563.1; -; Genomic_DNA.
DR   CCDS; CCDS42229.1; -. [Q14526-1]
DR   CCDS; CCDS42230.1; -. [Q14526-2]
DR   RefSeq; NP_001091672.1; NM_001098202.1. [Q14526-1]
DR   RefSeq; NP_006488.2; NM_006497.3. [Q14526-2]
DR   UniGene; Hs.695682; -.
DR   UniGene; Hs.72956; -.
DR   ProteinModelPortal; Q14526; -.
DR   SMR; Q14526; 25-145, 429-613.
DR   BioGrid; 109337; 26.
DR   IntAct; Q14526; 11.
DR   MINT; MINT-2730619; -.
DR   STRING; 9606.ENSP00000314080; -.
DR   PhosphoSite; Q14526; -.
DR   BioMuta; HIC1; -.
DR   DMDM; 296439502; -.
DR   PaxDb; Q14526; -.
DR   PRIDE; Q14526; -.
DR   DNASU; 3090; -.
DR   Ensembl; ENST00000322941; ENSP00000314080; ENSG00000177374. [Q14526-1]
DR   Ensembl; ENST00000399849; ENSP00000382742; ENSG00000177374. [Q14526-2]
DR   Ensembl; ENST00000619757; ENSP00000477858; ENSG00000177374. [Q14526-2]
DR   GeneID; 3090; -.
DR   KEGG; hsa:3090; -.
DR   UCSC; uc002fty.4; human. [Q14526-1]
DR   CTD; 3090; -.
DR   GeneCards; HIC1; -.
DR   H-InvDB; HIX0039113; -.
DR   HGNC; HGNC:4909; HIC1.
DR   HPA; HPA043372; -.
DR   MIM; 603825; gene.
DR   neXtProt; NX_Q14526; -.
DR   Orphanet; 531; Miller-Dieker syndrome.
DR   PharmGKB; PA29282; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   eggNOG; COG5048; LUCA.
DR   GeneTree; ENSGT00800000124025; -.
DR   HOGENOM; HOG000026793; -.
DR   HOVERGEN; HBG031606; -.
DR   InParanoid; Q14526; -.
DR   OMA; PPDPFRG; -.
DR   OrthoDB; EOG74J97F; -.
DR   PhylomeDB; Q14526; -.
DR   TreeFam; TF333488; -.
DR   SignaLink; Q14526; -.
DR   GeneWiki; HIC1; -.
DR   GenomeRNAi; 3090; -.
DR   NextBio; 12259; -.
DR   PRO; PR:Q14526; -.
DR   Proteomes; UP000005640; Chromosome 17.
DR   Bgee; Q14526; -.
DR   CleanEx; HS_HIC1; -.
DR   ExpressionAtlas; Q14526; baseline and differential.
DR   Genevisible; Q14526; HS.
DR   GO; GO:0000785; C:chromatin; ISS:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; IDA:HPA.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0042826; F:histone deacetylase binding; IDA:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
DR   GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IDA:UniProtKB.
DR   GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; IDA:UniProtKB.
DR   GO; GO:0007275; P:multicellular organismal development; IEA:UniProtKB-KW.
DR   GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
DR   GO; GO:0030178; P:negative regulation of Wnt signaling pathway; IDA:UniProtKB.
DR   GO; GO:0043517; P:positive regulation of DNA damage response, signal transduction by p53 class mediator; ISS:UniProtKB.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; TAS:UniProtKB.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
DR   GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.160.60; -; 4.
DR   InterPro; IPR000210; BTB/POZ_dom.
DR   InterPro; IPR028424; HIC1.
DR   InterPro; IPR011333; POZ_dom.
DR   InterPro; IPR007087; Znf_C2H2.
DR   InterPro; IPR015880; Znf_C2H2-like.
DR   InterPro; IPR013087; Znf_C2H2/integrase_DNA-bd.
DR   PANTHER; PTHR24409:SF69; PTHR24409:SF69; 1.
DR   Pfam; PF00651; BTB; 1.
DR   Pfam; PF00096; zf-C2H2; 1.
DR   SMART; SM00225; BTB; 1.
DR   SMART; SM00355; ZnF_C2H2; 5.
DR   SUPFAM; SSF54695; SSF54695; 1.
DR   PROSITE; PS50097; BTB; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 5.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 5.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Complete proteome;
KW   Developmental protein; DNA-binding; Isopeptide bond; Metal-binding;
KW   Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repeat;
KW   Repressor; Transcription; Transcription regulation; Tumor suppressor;
KW   Ubl conjugation; Wnt signaling pathway; Zinc; Zinc-finger.
FT   CHAIN         1    733       Hypermethylated in cancer 1 protein.
FT                                /FTId=PRO_0000046942.
FT   DOMAIN       47    110       BTB. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00037}.
FT   ZN_FING     439    459       C2H2-type 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     509    529       C2H2-type 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     537    557       C2H2-type 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     565    585       C2H2-type 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     593    613       C2H2-type 5. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   REGION      154    315       Mediates HDAC-dependent transcriptional
FT                                repression.
FT   REGION      241    247       Interaction with CTBP1.
FT   COMPBIAS    110    119       Poly-Ala.
FT   COMPBIAS    160    167       Poly-Gly.
FT   COMPBIAS    195    199       Poly-Pro.
FT   MOD_RES     237    237       Phosphoserine.
FT                                {ECO:0000244|PubMed:24275569}.
FT   MOD_RES     248    248       Phosphoserine.
FT                                {ECO:0000244|PubMed:24275569}.
FT   MOD_RES     333    333       N6-acetyllysine; alternate.
FT                                {ECO:0000269|PubMed:17283066}.
FT   MOD_RES     366    366       Phosphoserine.
FT                                {ECO:0000244|PubMed:24275569}.
FT   MOD_RES     704    704       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9R1Y5}.
FT   CROSSLNK    333    333       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO);
FT                                alternate.
FT   VAR_SEQ       1     19       Missing (in isoform 2). {ECO:0000305}.
FT                                /FTId=VSP_006826.
FT   VARIANT     725    725       R -> G (in dbSNP:rs1063317).
FT                                {ECO:0000269|PubMed:7585125}.
FT                                /FTId=VAR_063109.
FT   MUTAGEN     244    244       L->A: Abolishes interaction with CTBP1
FT                                and CTBP2. Impairs transcriptional
FT                                repression.
FT                                {ECO:0000269|PubMed:16762039}.
FT   MUTAGEN     333    333       K->Q: Mimicks acetylation. Impairs
FT                                interaction with RBBP4 and MTA1 and no
FT                                effect on interaction with CTBP2. Reduces
FT                                transcriptional repression.
FT                                {ECO:0000269|PubMed:17283066,
FT                                ECO:0000269|PubMed:20547755}.
FT   MUTAGEN     333    333       K->R: Abolishes sumoylation; impairs
FT                                transcriptional repression activity.
FT                                {ECO:0000269|PubMed:17283066,
FT                                ECO:0000269|PubMed:20547755}.
FT   MUTAGEN     335    335       E->A: Impairs transcriptional repression
FT                                activity. Decreases interaction with
FT                                MTA1. {ECO:0000269|PubMed:17283066,
FT                                ECO:0000269|PubMed:20547755}.
FT   MUTAGEN     336    336       P->A: Impairs K-333 acetylation; no
FT                                effect on sumoylation. Decreases
FT                                interaction with MTA1.
FT                                {ECO:0000269|PubMed:17283066,
FT                                ECO:0000269|PubMed:20547755}.
FT   MUTAGEN     540    540       C->S: Abolishes repression activity.
FT                                {ECO:0000269|PubMed:15231840}.
FT   CONFLICT    190    190       P -> R (in Ref. 1; AAD09201).
FT                                {ECO:0000305}.
SQ   SEQUENCE   733 AA;  76508 MW;  6DDD0F49C4E490D3 CRC64;
     MTFPEADILL KSGECAGQTM LDTMEAPGHS RQLLLQLNNQ RTKGFLCDVI IVVQNALFRA
     HKNVLAASSA YLKSLVVHDN LLNLDHDMVS PAVFRLVLDF IYTGRLADGA EAAAAAAVAP
     GAEPSLGAVL AAASYLQIPD LVALCKKRLK RHGKYCHLRG GGGGGGGYAP YGRPGRGLRA
     ATPVIQACYP SPVGPPPPPA AEPPSGPEAA VNTHCAELYA SGPGPAAALC ASERRCSPLC
     GLDLSKKSPP GSAAPERPLA ERELPPRPDS PPSAGPAAYK EPPLALPSLP PLPFQKLEEA
     APPSDPFRGG SGSPGPEPPG RPDGPSLLYR WMKHEPGLGS YGDELGRERG SPSERCEERG
     GDAAVSPGGP PLGLAPPPRY PGSLDGPGAG GDGDDYKSSS EETGSSEDPS PPGGHLEGYP
     CPHLAYGEPE SFGDNLYVCI PCGKGFPSSE QLNAHVEAHV EEEEALYGRA EAAEVAAGAA
     GLGPPFGGGG DKVAGAPGGL GELLRPYRCA SCDKSYKDPA TLRQHEKTHW LTRPYPCTIC
     GKKFTQRGTM TRHMRSHLGL KPFACDACGM RFTRQYRLTE HMRIHSGEKP YECQVCGGKF
     AQQRNLISHM KMHAVGGAAG AAGALAGLGG LPGVPGPDGK GKLDFPEGVF AVARLTAEQL
     SLKQQDKAAA AELLAQTTHF LHDPKVALES LYPLAKFTAE LGLSPDKAAE VLSQGAHLAA
     GPDGRTIDRF SPT
//
ID   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};
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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";
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DR   EMBL; U40462; AAC50459.1; -; mRNA.
DR   EMBL; S80876; AAB50683.1; -; mRNA.
DR   EMBL; AY377974; AAR84585.1; -; mRNA.
DR   EMBL; AK303586; BAG64603.1; -; mRNA.
DR   EMBL; BT009836; AAP88838.1; -; mRNA.
DR   EMBL; AC124014; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC233268; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471128; EAW60977.1; -; Genomic_DNA.
DR   EMBL; CH471128; EAW60978.1; -; Genomic_DNA.
DR   EMBL; CH471128; EAW60981.1; -; Genomic_DNA.
DR   EMBL; CH236955; EAL23900.1; -; Genomic_DNA.
DR   EMBL; CH471128; EAW60979.1; -; Genomic_DNA.
DR   EMBL; BC018349; AAH18349.1; -; mRNA.
DR   CCDS; CCDS59055.1; -. [Q13422-7]
DR   CCDS; CCDS69299.1; -. [Q13422-5]
DR   CCDS; CCDS75596.1; -. [Q13422-1]
DR   CCDS; CCDS75597.1; -. [Q13422-3]
DR   CCDS; CCDS78233.1; -. [Q13422-2]
DR   RefSeq; NP_001207694.1; NM_001220765.2. [Q13422-7]
DR   RefSeq; NP_001207696.1; NM_001220767.2.
DR   RefSeq; NP_001207697.1; NM_001220768.2. [Q13422-3]
DR   RefSeq; NP_001207699.1; NM_001220770.2.
DR   RefSeq; NP_001207700.1; NM_001220771.2. [Q13422-5]
DR   RefSeq; NP_001278766.1; NM_001291837.1. [Q13422-7]
DR   RefSeq; NP_001278767.1; NM_001291838.1. [Q13422-2]
DR   RefSeq; NP_001278768.1; NM_001291839.1.
DR   RefSeq; NP_001278769.1; NM_001291840.1. [Q13422-6]
DR   RefSeq; NP_001278770.1; NM_001291841.1.
DR   RefSeq; NP_001278771.1; NM_001291842.1.
DR   RefSeq; NP_001278772.1; NM_001291843.1.
DR   RefSeq; NP_001278773.1; NM_001291844.1.
DR   RefSeq; NP_006051.1; NM_006060.5. [Q13422-1]
DR   RefSeq; XP_011513370.1; XM_011515068.1. [Q13422-1]
DR   RefSeq; XP_011513371.1; XM_011515069.1. [Q13422-1]
DR   RefSeq; XP_011513377.1; XM_011515075.1. [Q13422-2]
DR   RefSeq; XP_011513378.1; XM_011515076.1. [Q13422-2]
DR   UniGene; Hs.435949; -.
DR   UniGene; Hs.488251; -.
DR   UniGene; Hs.646004; -.
DR   UniGene; Hs.731495; -.
DR   ProteinModelPortal; Q13422; -.
DR   SMR; Q13422; 112-220, 460-509.
DR   BioGrid; 115604; 118.
DR   DIP; DIP-41110N; -.
DR   IntAct; Q13422; 68.
DR   MINT; MINT-129252; -.
DR   STRING; 9606.ENSP00000331614; -.
DR   PhosphoSite; Q13422; -.
DR   BioMuta; IKZF1; -.
DR   DMDM; 3913926; -.
DR   MaxQB; Q13422; -.
DR   PaxDb; Q13422; -.
DR   PRIDE; Q13422; -.
DR   DNASU; 10320; -.
DR   Ensembl; ENST00000331340; ENSP00000331614; ENSG00000185811. [Q13422-1]
DR   Ensembl; ENST00000343574; ENSP00000342750; ENSG00000185811. [Q13422-2]
DR   Ensembl; ENST00000349824; ENSP00000342485; ENSG00000185811. [Q13422-5]
DR   Ensembl; ENST00000357364; ENSP00000349928; ENSG00000185811. [Q13422-3]
DR   Ensembl; ENST00000359197; ENSP00000352123; ENSG00000185811. [Q13422-7]
DR   Ensembl; ENST00000438033; ENSP00000396554; ENSG00000185811. [Q13422-2]
DR   Ensembl; ENST00000439701; ENSP00000413025; ENSG00000185811. [Q13422-7]
DR   GeneID; 10320; -.
DR   KEGG; hsa:10320; -.
DR   UCSC; uc003tow.4; human. [Q13422-1]
DR   UCSC; uc003tox.4; human. [Q13422-7]
DR   UCSC; uc003tpa.4; human. [Q13422-6]
DR   UCSC; uc011kck.2; human. [Q13422-2]
DR   UCSC; uc022acq.1; human. [Q13422-5]
DR   UCSC; uc022acs.1; human. [Q13422-4]
DR   UCSC; uc022acx.1; human. [Q13422-3]
DR   CTD; 10320; -.
DR   GeneCards; IKZF1; -.
DR   HGNC; HGNC:13176; IKZF1.
DR   HPA; CAB009247; -.
DR   HPA; HPA035221; -.
DR   HPA; HPA035222; -.
DR   MIM; 603023; gene.
DR   neXtProt; NX_Q13422; -.
DR   Orphanet; 317473; Pancytopenia due to IKZF1 mutations.
DR   Orphanet; 99860; Precursor B-cell acute lymphoblastic leukemia.
DR   PharmGKB; PA37748; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   eggNOG; COG5048; LUCA.
DR   GeneTree; ENSGT00550000074392; -.
DR   HOVERGEN; HBG004752; -.
DR   InParanoid; Q13422; -.
DR   KO; K09220; -.
DR   OMA; GDKCLSD; -.
DR   PhylomeDB; Q13422; -.
DR   TreeFam; TF331189; -.
DR   SignaLink; Q13422; -.
DR   ChiTaRS; IKZF1; human.
DR   GeneWiki; IKZF1; -.
DR   GenomeRNAi; 10320; -.
DR   NextBio; 39123; -.
DR   PRO; PR:Q13422; -.
DR   Proteomes; UP000005640; Chromosome 7.
DR   Bgee; Q13422; -.
DR   CleanEx; HS_IKZF1; -.
DR   ExpressionAtlas; Q13422; baseline and differential.
DR   Genevisible; Q13422; HS.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0005721; C:pericentric heterochromatin; IEA:Ensembl.
DR   GO; GO:0043234; C:protein complex; IDA:MGI.
DR   GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IEA:Ensembl.
DR   GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0044212; F:transcription regulatory region DNA binding; IBA:GO_Central.
DR   GO; GO:0035881; P:amacrine cell differentiation; IEA:Ensembl.
DR   GO; GO:0030183; P:B cell differentiation; IEA:Ensembl.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0016568; P:chromatin modification; IEA:UniProtKB-KW.
DR   GO; GO:0030218; P:erythrocyte differentiation; IMP:UniProtKB.
DR   GO; GO:0030900; P:forebrain development; IEA:Ensembl.
DR   GO; GO:0048535; P:lymph node development; IEA:Ensembl.
DR   GO; GO:0030098; P:lymphocyte differentiation; IMP:UniProtKB.
DR   GO; GO:0007498; P:mesoderm development; TAS:ProtInc.
DR   GO; GO:0001779; P:natural killer cell differentiation; IEA:Ensembl.
DR   GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IBA:GO_Central.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR   GO; GO:0048541; P:Peyer's patch development; IEA:Ensembl.
DR   GO; GO:0045579; P:positive regulation of B cell differentiation; IEA:Ensembl.
DR   GO; GO:0040018; P:positive regulation of multicellular organism growth; IEA:Ensembl.
DR   GO; GO:0045660; P:positive regulation of neutrophil differentiation; IEA:Ensembl.
DR   GO; GO:0051138; P:positive regulation of NK T cell differentiation; IEA:Ensembl.
DR   GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IBA:GO_Central.
DR   GO; GO:0060040; P:retinal bipolar neuron differentiation; IEA:Ensembl.
DR   GO; GO:0030217; P:T cell differentiation; IEA:Ensembl.
DR   GO; GO:0048538; P:thymus development; IEA:Ensembl.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.160.60; -; 4.
DR   InterPro; IPR007087; Znf_C2H2.
DR   InterPro; IPR015880; Znf_C2H2-like.
DR   InterPro; IPR013087; Znf_C2H2/integrase_DNA-bd.
DR   Pfam; PF00096; zf-C2H2; 1.
DR   SMART; SM00355; ZnF_C2H2; 6.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 5.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 4.
PE   1: Evidence at protein level;
KW   Activator; Alternative splicing; Cell cycle; Chromatin regulator;
KW   Chromosomal rearrangement; Complete proteome; Cytoplasm;
KW   Developmental protein; DNA-binding; Isopeptide bond; Metal-binding;
KW   Nucleus; Phosphoprotein; Reference proteome; Repeat; Repressor;
KW   Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW   Zinc-finger.
FT   CHAIN         1    519       DNA-binding protein Ikaros.
FT                                /FTId=PRO_0000047094.
FT   ZN_FING     117    139       C2H2-type 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     145    167       C2H2-type 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     173    195       C2H2-type 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     201    224       C2H2-type 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     462    484       C2H2-type 5. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     490    514       C2H2-type 6. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   REGION      154    163       Required for both high-affinity DNA
FT                                binding and pericentromeric
FT                                heterochromatin localization.
FT                                {ECO:0000250}.
FT   REGION      180    195       Required for both high-affinity DNA
FT                                binding and pericentromeric
FT                                heterochromatin localization.
FT                                {ECO:0000250}.
FT   REGION      468    471       Required for binding PP1CC.
FT                                {ECO:0000250}.
FT   COMPBIAS    373    376       Poly-Leu.
FT   SITE        159    159       Required for both pericentromeric
FT                                heterochromatin localization and complete
FT                                DNA binding. {ECO:0000250}.
FT   SITE        162    162       Required for both pericentromeric
FT                                heterochromatin localization and complete
FT                                DNA binding. {ECO:0000250}.
FT   SITE        188    188       Required for both pericentromeric
FT                                heterochromatin localization and DNA
FT                                binding. {ECO:0000250}.
FT   MOD_RES      13     13       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q03267}.
FT   MOD_RES      23     23       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:Q03267}.
FT   MOD_RES      63     63       Phosphoserine.
FT                                {ECO:0000244|PubMed:19690332}.
FT   MOD_RES     101    101       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q03267}.
FT   MOD_RES     140    140       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:Q03267}.
FT   MOD_RES     168    168       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q03267}.
FT   MOD_RES     196    196       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q03267}.
FT   MOD_RES     258    258       Phosphoserine.
FT                                {ECO:0000244|PubMed:19690332}.
FT   MOD_RES     295    295       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q03267}.
FT   MOD_RES     361    361       Phosphoserine.
FT                                {ECO:0000244|PubMed:19690332,
FT                                ECO:0000269|PubMed:23071339}.
FT   MOD_RES     364    364       Phosphoserine.
FT                                {ECO:0000244|PubMed:19690332,
FT                                ECO:0000269|PubMed:23071339}.
FT   MOD_RES     389    389       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q03267}.
FT   MOD_RES     391    391       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q03267}.
FT   MOD_RES     393    393       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q03267}.
FT   MOD_RES     397    397       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q03267}.
FT   MOD_RES     398    398       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:Q03267}.
FT   MOD_RES     402    402       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q03267}.
FT   MOD_RES     445    445       Phosphoserine.
FT                                {ECO:0000244|PubMed:24275569}.
FT   CROSSLNK     58     58       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO).
FT                                {ECO:0000250}.
FT   CROSSLNK    241    241       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO).
FT                                {ECO:0000250}.
FT   VAR_SEQ      10     53       Missing (in isoform Ik4). {ECO:0000305}.
FT                                /FTId=VSP_006847.
FT   VAR_SEQ      54    283       Missing (in isoform Ik6). {ECO:0000305}.
FT                                /FTId=VSP_006849.
FT   VAR_SEQ      54    140       Missing (in isoform Ik2).
FT                                {ECO:0000303|PubMed:14702039}.
FT                                /FTId=VSP_006848.
FT   VAR_SEQ     141    283       Missing (in isoform Ik5). {ECO:0000305}.
FT                                /FTId=VSP_006852.
FT   VAR_SEQ     197    283       Missing (in isoform Ik3 and isoform Ik4).
FT                                {ECO:0000305}.
FT                                /FTId=VSP_006850.
FT   VAR_SEQ     197    238       Missing (in isoform Ik7 and isoform Ikx).
FT                                {ECO:0000303|PubMed:15489334,
FT                                ECO:0000303|Ref.3, ECO:0000303|Ref.5}.
FT                                /FTId=VSP_006851.
FT   VAR_SEQ     260    268       RSLVLDRLA -> ISRAGQTSK (in isoform Ikx).
FT                                {ECO:0000303|Ref.3}.
FT                                /FTId=VSP_053404.
FT   VAR_SEQ     269    519       Missing (in isoform Ikx).
FT                                {ECO:0000303|Ref.3}.
FT                                /FTId=VSP_053405.
FT   CONFLICT     11     12       QV -> FS (in Ref. 2; AAB50683).
FT                                {ECO:0000305}.
FT   CONFLICT    214    214       S -> T (in Ref. 2; AAB50683).
FT                                {ECO:0000305}.
FT   CONFLICT    245    245       N -> K (in Ref. 2; AAB50683).
FT                                {ECO:0000305}.
FT   CONFLICT    296    296       Missing (in Ref. 2; AAB50683).
FT                                {ECO:0000305}.
FT   CONFLICT    298    298       S -> T (in Ref. 2; AAB50683).
FT                                {ECO:0000305}.
FT   CONFLICT    352    355       KPLA -> RRS (in Ref. 2; AAB50683).
FT                                {ECO:0000305}.
FT   CONFLICT    372    372       N -> Y (in Ref. 2; AAB50683).
FT                                {ECO:0000305}.
FT   CONFLICT    420    426       PHARNGL -> RRAQRV (in Ref. 2; AAB50683).
FT                                {ECO:0000305}.
SQ   SEQUENCE   519 AA;  57528 MW;  7B0129C4E3FE41A8 CRC64;
     MDADEGQDMS QVSGKESPPV SDTPDEGDEP MPIPEDLSTT SGGQQSSKSD RVVASNVKVE
     TQSDEENGRA CEMNGEECAE DLRMLDASGE KMNGSHRDQG SSALSGVGGI RLPNGKLKCD
     ICGIICIGPN VLMVHKRSHT GERPFQCNQC GASFTQKGNL LRHIKLHSGE KPFKCHLCNY
     ACRRRDALTG HLRTHSVGKP HKCGYCGRSY KQRSSLEEHK ERCHNYLESM GLPGTLYPVI
     KEETNHSEMA EDLCKIGSER SLVLDRLASN VAKRKSSMPQ KFLGDKGLSD TPYDSSASYE
     KENEMMKSHV MDQAINNAIN YLGAESLRPL VQTPPGGSEV VPVISPMYQL HKPLAEGTPR
     SNHSAQDSAV ENLLLLSKAK LVPSEREASP SNSCQDSTDT ESNNEEQRSG LIYLTNHIAP
     HARNGLSLKE EHRAYDLLRA ASENSQDALR VVSTSGEQMK VYKCEHCRVL FLDHVMYTIH
     MGCHGFRDPF ECNMCGYHSQ DRYEFSSHIT RGEHRFHMS
//
ID   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.;
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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};
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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";
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DR   EMBL; X84373; CAA59108.1; -; mRNA.
DR   EMBL; AF248484; AAF62185.1; -; Genomic_DNA.
DR   EMBL; AF127577; AAF35255.1; -; Genomic_DNA.
DR   EMBL; AL163207; CAB90396.1; -; Genomic_DNA.
DR   EMBL; BC040361; AAH40361.1; -; mRNA.
DR   CCDS; CCDS13568.1; -.
DR   PIR; S57348; S57348.
DR   RefSeq; NP_003480.2; NM_003489.3.
DR   RefSeq; XP_005261120.1; XM_005261063.2.
DR   RefSeq; XP_005261122.1; XM_005261065.2.
DR   RefSeq; XP_011528049.1; XM_011529747.1.
DR   RefSeq; XP_011528050.1; XM_011529748.1.
DR   RefSeq; XP_011528051.1; XM_011529749.1.
DR   RefSeq; XP_011528052.1; XM_011529750.1.
DR   RefSeq; XP_011528053.1; XM_011529751.1.
DR   RefSeq; XP_011528054.1; XM_011529752.1.
DR   UniGene; Hs.155017; -.
DR   PDB; 2GPO; X-ray; 1.95 A; C=366-390.
DR   PDB; 2GPP; X-ray; 2.60 A; C/D=366-390.
DR   PDB; 4S14; X-ray; 3.54 A; C=499-510.
DR   PDB; 4S15; X-ray; 1.90 A; C/D=499-510.
DR   PDBsum; 2GPO; -.
DR   PDBsum; 2GPP; -.
DR   PDBsum; 4S14; -.
DR   PDBsum; 4S15; -.
DR   ProteinModelPortal; P48552; -.
DR   BioGrid; 113843; 56.
DR   DIP; DIP-5964N; -.
DR   IntAct; P48552; 22.
DR   MINT; MINT-192711; -.
DR   STRING; 9606.ENSP00000327213; -.
DR   PhosphoSite; P48552; -.
DR   BioMuta; NRIP1; -.
DR   DMDM; 9988061; -.
DR   MaxQB; P48552; -.
DR   PaxDb; P48552; -.
DR   PRIDE; P48552; -.
DR   DNASU; 8204; -.
DR   Ensembl; ENST00000318948; ENSP00000327213; ENSG00000180530.
DR   Ensembl; ENST00000400199; ENSP00000383060; ENSG00000180530.
DR   Ensembl; ENST00000400202; ENSP00000383063; ENSG00000180530.
DR   GeneID; 8204; -.
DR   KEGG; hsa:8204; -.
DR   UCSC; uc002yjx.2; human.
DR   CTD; 8204; -.
DR   GeneCards; NRIP1; -.
DR   H-InvDB; HIX0027827; -.
DR   HGNC; HGNC:8001; NRIP1.
DR   HPA; HPA046571; -.
DR   HPA; HPA060036; -.
DR   MIM; 602490; gene.
DR   neXtProt; NX_P48552; -.
DR   PharmGKB; PA31780; -.
DR   eggNOG; ENOG410IFW7; Eukaryota.
DR   eggNOG; ENOG410XPVS; LUCA.
DR   GeneTree; ENSGT00390000007999; -.
DR   HOGENOM; HOG000236277; -.
DR   HOVERGEN; HBG052667; -.
DR   InParanoid; P48552; -.
DR   KO; K17965; -.
DR   OMA; VEKDLRC; -.
DR   OrthoDB; EOG7H1JJQ; -.
DR   PhylomeDB; P48552; -.
DR   TreeFam; TF332210; -.
DR   Reactome; R-HSA-1368082; RORA activates gene expression.
DR   Reactome; R-HSA-1368108; BMAL1:CLOCK,NPAS2 activates circadian gene expression.
DR   Reactome; R-HSA-400253; Circadian Clock.
DR   SignaLink; P48552; -.
DR   ChiTaRS; NRIP1; human.
DR   EvolutionaryTrace; P48552; -.
DR   GeneWiki; NRIP1; -.
DR   GenomeRNAi; 8204; -.
DR   NextBio; 30914; -.
DR   PRO; PR:P48552; -.
DR   Proteomes; UP000005640; Chromosome 21.
DR   Bgee; P48552; -.
DR   CleanEx; HS_NRIP1; -.
DR   ExpressionAtlas; P48552; baseline and differential.
DR   Genevisible; P48552; HS.
DR   GO; GO:0030054; C:cell junction; IDA:HPA.
DR   GO; GO:0000118; C:histone deacetylase complex; IEA:Ensembl.
DR   GO; GO:0000790; C:nuclear chromatin; IDA:BHF-UCL.
DR   GO; GO:0016607; C:nuclear speck; IEA:Ensembl.
DR   GO; GO:0005730; C:nucleolus; IDA:HPA.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0050681; F:androgen receptor binding; NAS:UniProtKB.
DR   GO; GO:0001046; F:core promoter sequence-specific DNA binding; IDA:UniProtKB.
DR   GO; GO:0030331; F:estrogen receptor binding; IPI:UniProtKB.
DR   GO; GO:0035259; F:glucocorticoid receptor binding; IPI:UniProtKB.
DR   GO; GO:0035257; F:nuclear hormone receptor binding; IPI:UniProtKB.
DR   GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB.
DR   GO; GO:0003714; F:transcription corepressor activity; IDA:UniProtKB.
DR   GO; GO:0030521; P:androgen receptor signaling pathway; NAS:UniProtKB.
DR   GO; GO:0071392; P:cellular response to estradiol stimulus; IDA:BHF-UCL.
DR   GO; GO:0032922; P:circadian regulation of gene expression; IMP:UniProtKB.
DR   GO; GO:0007623; P:circadian rhythm; IEP:UniProtKB.
DR   GO; GO:0019915; P:lipid storage; IEA:Ensembl.
DR   GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
DR   GO; GO:0001543; P:ovarian follicle rupture; IEA:Ensembl.
DR   GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; NAS:UniProtKB.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
DR   InterPro; IPR026649; NRIP1.
DR   InterPro; IPR031405; NRIP1_RD1.
DR   InterPro; IPR031406; NRIP1_RD2.
DR   InterPro; IPR031407; NRIP1_RD3.
DR   InterPro; IPR031408; NRIP1_RD4.
DR   PANTHER; PTHR15088; PTHR15088; 1.
DR   Pfam; PF15687; NRIP1_repr_1; 1.
DR   Pfam; PF15688; NRIP1_repr_2; 1.
DR   Pfam; PF15689; NRIP1_repr_3; 1.
DR   Pfam; PF15690; NRIP1_repr_4; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Activator; Biological rhythms;
KW   Complete proteome; Isopeptide bond; Nucleus; Phosphoprotein;
KW   Polymorphism; Reference proteome; Repeat; Transcription;
KW   Transcription regulation; Ubl conjugation.
FT   CHAIN         1   1158       Nuclear receptor-interacting protein 1.
FT                                /FTId=PRO_0000057951.
FT   REGION        1    415       Interaction with ZNF366.
FT   REGION       78    333       Repression domain 1.
FT   REGION      410    700       Repression domain 2.
FT   REGION      431    472       Required for targeting to small nuclear
FT                                foci.
FT   REGION      735    885       Repression domain 3.
FT   REGION      753   1158       Interaction with ZNF366.
FT   REGION     1118   1158       Repression domain 4.
FT   MOTIF        21     25       LXXLL motif 1.
FT   MOTIF       133    137       LXXLL motif 2.
FT   MOTIF       185    189       LXXLL motif 3.
FT   MOTIF       266    270       LXXLL motif 4.
FT   MOTIF       380    384       LXXLL motif 5.
FT   MOTIF       440    446       CTBP-binding; principal site.
FT   MOTIF       500    504       LXXLL motif 6.
FT   MOTIF       565    569       CTBP-binding.
FT   MOTIF       599    603       CTBP-binding. {ECO:0000255}.
FT   MOTIF       713    717       LXXLL motif 7.
FT   MOTIF       819    823       LXXLL motif 8.
FT   MOTIF       936    940       LXXLL motif 9.
FT   MOTIF       946    950       CTBP-binding.
FT   MOTIF      1061   1074       Ligand-dependent nuclear receptor
FT                                binding. {ECO:0000250}.
FT   MOD_RES     104    104       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q8CBD1}.
FT   MOD_RES     111    111       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q8CBD1}.
FT   MOD_RES     158    158       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q8CBD1}.
FT   MOD_RES     207    207       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:Q8CBD1}.
FT   MOD_RES     218    218       Phosphoserine.
FT                                {ECO:0000244|PubMed:24275569}.
FT   MOD_RES     286    286       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q8CBD1}.
FT   MOD_RES     310    310       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q8CBD1}.
FT   MOD_RES     356    356       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q8CBD1}.
FT   MOD_RES     378    378       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q8CBD1}.
FT   MOD_RES     446    446       N6-acetyllysine.
FT                                {ECO:0000269|PubMed:11509661}.
FT   MOD_RES     481    481       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q8CBD1}.
FT   MOD_RES     487    487       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q8CBD1}.
FT   MOD_RES     518    518       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q8CBD1}.
FT   MOD_RES     528    528       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q8CBD1}.
FT   MOD_RES     542    542       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q8CBD1}.
FT   MOD_RES     606    606       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q8CBD1}.
FT   MOD_RES     671    671       Phosphoserine.
FT                                {ECO:0000244|PubMed:24275569}.
FT   MOD_RES     807    807       Phosphoserine.
FT                                {ECO:0000244|PubMed:24275569}.
FT   MOD_RES     931    931       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q8CBD1}.
FT   MOD_RES    1001   1001       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q8CBD1}.
FT   CROSSLNK    756    756       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:25218447}.
FT   CROSSLNK   1105   1105       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:25218447}.
FT   VARIANT      37     37       V -> I (in dbSNP:rs9941840).
FT                                /FTId=VAR_051241.
FT   VARIANT     221    221       H -> R (in dbSNP:rs139263261).
FT                                {ECO:0000269|PubMed:16131398}.
FT                                /FTId=VAR_023706.
FT   VARIANT     315    315       Y -> F (in dbSNP:rs2228507).
FT                                /FTId=VAR_034142.
FT   VARIANT     441    441       I -> V (in dbSNP:rs150468995).
FT                                {ECO:0000269|PubMed:16131398}.
FT                                /FTId=VAR_023707.
FT   VARIANT     448    448       R -> G (common polymorphism;
FT                                dbSNP:rs2229742).
FT                                {ECO:0000269|PubMed:16131398,
FT                                ECO:0000269|PubMed:7641693}.
FT                                /FTId=VAR_023708.
FT   VARIANT     567    567       N -> S (in dbSNP:rs9975169).
FT                                /FTId=VAR_051242.
FT   VARIANT     803    803       S -> L (in dbSNP:rs61750208).
FT                                {ECO:0000269|PubMed:16131398}.
FT                                /FTId=VAR_023709.
FT   VARIANT    1079   1079       V -> F. {ECO:0000269|PubMed:16131398}.
FT                                /FTId=VAR_023710.
FT   MUTAGEN     440    443       PIDL->AAAA: Abolishes interaction with
FT                                CTBP1. {ECO:0000269|PubMed:11509661}.
FT   MUTAGEN     440    442       PID->AIA: Abolishes interaction with
FT                                CTBP1 and attenuates nuclear hormone
FT                                receptor-dependent transcription
FT                                repression.
FT   MUTAGEN     442    443       DL->AA: Reduces, but does not completely
FT                                abolish, interaction with CTBP. Reduces
FT                                transcriptional repression.
FT                                {ECO:0000269|PubMed:14736873,
FT                                ECO:0000269|PubMed:15060175}.
FT   MUTAGEN     442    443       DL->AS: Disrupts interaction with CTBP1,
FT                                and CTBP2 to a lesser extent. Disrupts
FT                                transcriptional repression; when
FT                                associated with 567-AS-568.
FT                                {ECO:0000269|PubMed:14736873,
FT                                ECO:0000269|PubMed:15060175}.
FT   MUTAGEN     446    446       K->Q: Disrupts interaction with CTBP1.
FT                                Decreases lysine acetylation. Disrupts
FT                                nuclear hormone receptor-dependent
FT                                transcription repression.
FT                                {ECO:0000269|PubMed:11509661}.
FT   MUTAGEN     446    446       K->R: Does not disrupt nuclear hormone
FT                                receptor-dependent transcription
FT                                repression.
FT                                {ECO:0000269|PubMed:11509661}.
FT   MUTAGEN     567    568       NL->AA: Disrupts transcriptional
FT                                repression. {ECO:0000269|PubMed:14736873,
FT                                ECO:0000269|PubMed:15060175}.
FT   MUTAGEN     567    568       NL->AS: Disrupts interaction with CTBP1
FT                                and CTBP2. Disrupts transcriptional
FT                                repression; when associated with 442-AS-
FT                                443. {ECO:0000269|PubMed:14736873,
FT                                ECO:0000269|PubMed:15060175}.
FT   MUTAGEN     599    603       SMDLT->PIAAS: Does not further disrupt
FT                                transcriptional repression; when
FT                                associated with 442-AA-443 and 567-AA-
FT                                568.
FT   MUTAGEN     948    949       DL->AA: Abolishes CTBP binding but
FT                                retains transcriptional repressor
FT                                activity. {ECO:0000269|PubMed:14736873}.
FT   CONFLICT    124    124       P -> R (in Ref. 1; CAA59108).
FT                                {ECO:0000305}.
FT   CONFLICT    721    726       NKGKSE -> TKGRVK (in Ref. 1; CAA59108).
FT                                {ECO:0000305}.
FT   CONFLICT    954    954       S -> I (in Ref. 3; AAH40361).
FT                                {ECO:0000305}.
FT   CONFLICT   1080   1080       T -> A (in Ref. 1; CAA59108).
FT                                {ECO:0000305}.
FT   HELIX       379    385       {ECO:0000244|PDB:2GPO}.
FT   HELIX       500    505       {ECO:0000244|PDB:4S15}.
SQ   SEQUENCE   1158 AA;  126942 MW;  81FC424968E9A5F6 CRC64;
     MTHGEELGSD VHQDSIVLTY LEGLLMHQAA GGSGTAVDKK SAGHNEEDQN FNISGSAFPT
     CQSNGPVLNT HTYQGSGMLH LKKARLLQSS EDWNAAKRKR LSDSIMNLNV KKEALLAGMV
     DSVPKGKQDS TLLASLLQSF SSRLQTVALS QQIRQSLKEQ GYALSHDSLK VEKDLRCYGV
     ASSHLKTLLK KSKVKDQKPD TNLPDVTKNL IRDRFAESPH HVGQSGTKVM SEPLSCAARL
     QAVASMVEKR ASPATSPKPS VACSQLALLL SSEAHLQQYS REHALKTQNA NQAASERLAA
     MARLQENGQK DVGSYQLPKG MSSHLNGQAR TSSSKLMASK SSATVFQNPM GIIPSSPKNA
     GYKNSLERNN IKQAANNSLL LHLLKSQTIP KPMNGHSHSE RGSIFEESST PTTIDEYSDN
     NPSFTDDSSG DESSYSNCVP IDLSCKHRTE KSESDQPVSL DNFTQSLLNT WDPKVPDVDI
     KEDQDTSKNS KLNSHQKVTL LQLLLGHKNE ENVEKNTSPQ GVHNDVSKFN TQNYARTSVI
     ESPSTNRTTP VSTPPLLTSS KAGSPINLSQ HSLVIKWNSP PYVCSTQSEK LTNTASNHSM
     DLTKSKDPPG EKPAQNEGAQ NSATFSASKL LQNLAQCGMQ SSMSVEEQRP SKQLLTGNTD
     KPIGMIDRLN SPLLSNKTNA VEENKAFSSQ PTGPEPGLSG SEIENLLERR TVLQLLLGNP
     NKGKSEKKEK TPLRDESTQE HSERALSEQI LMVKIKSEPC DDLQIPNTNV HLSHDAKSAP
     FLGMAPAVQR SAPALPVSED FKSEPVSPQD FSFSKNGLLS RLLRQNQDSY LADDSDRSHR
     NNEMALLESK NLCMVPKKRK LYTEPLENPF KKMKNNIVDA ANNHSAPEVL YGSLLNQEEL
     KFSRNDLEFK YPAGHGSASE SEHRSWARES KSFNVLKQLL LSENCVRDLS PHRSNSVADS
     KKKGHKNNVT NSKPEFSISS LNGLMYSSTQ PSSCMDNRTF SYPGVVKTPV SPTFPEHLGC
     AGSRPESGLL NGCSMPSEKG PIKWVITDAE KNEYEKDSPR LTKTNPILYY MLQKGGNSVT
     SRETQDKDIW REASSAESVS QVTAKEELLP TAETKASFFN LRSPYNSHMG NNASRPHSAN
     GEVYGLLGSV LTIKKESE
//
ID   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   -----------------------------------------------------------------------
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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}.
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DR   EMBL; X89750; CAA61897.1; -; mRNA.
DR   EMBL; AF179900; AAF81643.1; -; mRNA.
DR   EMBL; CR450333; CAG29329.1; -; mRNA.
DR   EMBL; AK291112; BAF83801.1; -; mRNA.
DR   EMBL; AP001025; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471113; EAX01672.1; -; Genomic_DNA.
DR   EMBL; BC000814; AAH00814.1; -; mRNA.
DR   EMBL; BC031268; AAH31268.1; -; mRNA.
DR   EMBL; BE296707; -; NOT_ANNOTATED_CDS; mRNA.
DR   CCDS; CCDS11832.1; -. [Q15583-3]
DR   CCDS; CCDS11833.1; -. [Q15583-2]
DR   CCDS; CCDS11834.1; -. [Q15583-1]
DR   CCDS; CCDS11835.1; -. [Q15583-4]
DR   RefSeq; NP_001265611.1; NM_001278682.1.
DR   RefSeq; NP_001265613.1; NM_001278684.1. [Q15583-2]
DR   RefSeq; NP_001265615.1; NM_001278686.1. [Q15583-4]
DR   RefSeq; NP_003235.1; NM_003244.3. [Q15583-2]
DR   RefSeq; NP_733796.2; NM_170695.3. [Q15583-1]
DR   RefSeq; NP_775299.1; NM_173207.2. [Q15583-3]
DR   RefSeq; NP_775300.1; NM_173208.2. [Q15583-2]
DR   RefSeq; NP_775301.1; NM_173209.2. [Q15583-4]
DR   RefSeq; NP_775302.1; NM_173210.2. [Q15583-4]
DR   RefSeq; NP_775303.1; NM_173211.1. [Q15583-4]
DR   RefSeq; NP_777480.1; NM_174886.2. [Q15583-4]
DR   RefSeq; XP_011524037.1; XM_011525735.1. [Q15583-4]
DR   UniGene; Hs.373550; -.
DR   PDB; 2LK2; NMR; -; A=171-248.
DR   PDBsum; 2LK2; -.
DR   ProteinModelPortal; Q15583; -.
DR   SMR; Q15583; 171-248.
DR   BioGrid; 112908; 21.
DR   IntAct; Q15583; 9.
DR   MINT; MINT-145985; -.
DR   STRING; 9606.ENSP00000327959; -.
DR   PhosphoSite; Q15583; -.
DR   BioMuta; TGIF1; -.
DR   DMDM; 215274200; -.
DR   MaxQB; Q15583; -.
DR   PaxDb; Q15583; -.
DR   PRIDE; Q15583; -.
DR   Ensembl; ENST00000330513; ENSP00000327959; ENSG00000177426. [Q15583-1]
DR   Ensembl; ENST00000343820; ENSP00000339631; ENSG00000177426. [Q15583-2]
DR   Ensembl; ENST00000345133; ENSP00000343969; ENSG00000177426. [Q15583-4]
DR   Ensembl; ENST00000400167; ENSP00000383031; ENSG00000177426. [Q15583-4]
DR   Ensembl; ENST00000401449; ENSP00000385206; ENSG00000177426. [Q15583-4]
DR   Ensembl; ENST00000405385; ENSP00000384970; ENSG00000177426. [Q15583-4]
DR   Ensembl; ENST00000407501; ENSP00000384133; ENSG00000177426. [Q15583-2]
DR   Ensembl; ENST00000472042; ENSP00000449501; ENSG00000177426. [Q15583-4]
DR   Ensembl; ENST00000548489; ENSP00000447747; ENSG00000177426. [Q15583-4]
DR   Ensembl; ENST00000551541; ENSP00000450025; ENSG00000177426. [Q15583-4]
DR   Ensembl; ENST00000618001; ENSP00000483499; ENSG00000177426. [Q15583-3]
DR   GeneID; 7050; -.
DR   KEGG; hsa:7050; -.
DR   UCSC; uc002klu.3; human. [Q15583-1]
DR   UCSC; uc002klv.3; human. [Q15583-3]
DR   UCSC; uc002klw.3; human. [Q15583-2]
DR   CTD; 7050; -.
DR   GeneCards; TGIF1; -.
DR   GeneReviews; TGIF1; -.
DR   H-InvDB; HIX0174209; -.
DR   HGNC; HGNC:11776; TGIF1.
DR   HPA; CAB004596; -.
DR   HPA; HPA062160; -.
DR   MIM; 142946; phenotype.
DR   MIM; 602630; gene.
DR   neXtProt; NX_Q15583; -.
DR   Orphanet; 93925; Alobar holoprosencephaly.
DR   Orphanet; 93924; Lobar holoprosencephaly.
DR   Orphanet; 280200; Microform holoprosencephaly.
DR   Orphanet; 93926; Midline interhemispheric variant of holoprosencephaly.
DR   Orphanet; 220386; Semilobar holoprosencephaly.
DR   Orphanet; 280195; Septopreoptic holoprosencephaly.
DR   PharmGKB; PA36489; -.
DR   eggNOG; KOG0773; Eukaryota.
DR   eggNOG; ENOG410XPMQ; LUCA.
DR   GeneTree; ENSGT00550000074260; -.
DR   HOGENOM; HOG000232039; -.
DR   HOVERGEN; HBG001143; -.
DR   InParanoid; Q15583; -.
DR   KO; K19383; -.
DR   OMA; IAANNFT; -.
DR   PhylomeDB; Q15583; -.
DR   TreeFam; TF318093; -.
DR   Reactome; R-HSA-2173795; Downregulation of SMAD2/3:SMAD4 transcriptional activity.
DR   Reactome; R-HSA-2173796; SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription.
DR   SignaLink; Q15583; -.
DR   EvolutionaryTrace; Q15583; -.
DR   GeneWiki; Homeobox_protein_TGIF1; -.
DR   GenomeRNAi; 7050; -.
DR   NextBio; 27551; -.
DR   PRO; PR:Q15583; -.
DR   Proteomes; UP000005640; Chromosome 18.
DR   Bgee; Q15583; -.
DR   CleanEx; HS_TGIF1; -.
DR   ExpressionAtlas; Q15583; baseline and differential.
DR   Genevisible; Q15583; HS.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
DR   GO; GO:0000978; F:RNA polymerase II core promoter proximal region sequence-specific DNA binding; IDA:NTNU_SB.
DR   GO; GO:0003714; F:transcription corepressor activity; TAS:ProtInc.
DR   GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; TAS:ProtInc.
DR   GO; GO:0001078; F:transcriptional repressor activity, RNA polymerase II core promoter proximal region sequence-specific binding; IDA:NTNU_SB.
DR   GO; GO:0007368; P:determination of left/right symmetry; IEA:Ensembl.
DR   GO; GO:0009953; P:dorsal/ventral pattern formation; IEA:Ensembl.
DR   GO; GO:0010467; P:gene expression; TAS:Reactome.
DR   GO; GO:0007275; P:multicellular organismal development; TAS:ProtInc.
DR   GO; GO:0008285; P:negative regulation of cell proliferation; IEA:Ensembl.
DR   GO; GO:0048387; P:negative regulation of retinoic acid receptor signaling pathway; IEA:Ensembl.
DR   GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:NTNU_SB.
DR   GO; GO:0001843; P:neural tube closure; IEA:Ensembl.
DR   GO; GO:0038092; P:nodal signaling pathway; IEA:Ensembl.
DR   GO; GO:0048146; P:positive regulation of fibroblast proliferation; IEA:Ensembl.
DR   GO; GO:0045666; P:positive regulation of neuron differentiation; IEA:Ensembl.
DR   GO; GO:0010470; P:regulation of gastrulation; IEA:Ensembl.
DR   GO; GO:0042493; P:response to drug; IEA:Ensembl.
DR   GO; GO:0060041; P:retina development in camera-type eye; IEA:Ensembl.
DR   GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; TAS:Reactome.
DR   GO; GO:0006351; P:transcription, DNA-templated; TAS:Reactome.
DR   GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; TAS:Reactome.
DR   Gene3D; 1.10.10.60; -; 1.
DR   InterPro; IPR001356; Homeobox_dom.
DR   InterPro; IPR008422; Homeobox_KN_domain.
DR   InterPro; IPR009057; Homeodomain-like.
DR   Pfam; PF05920; Homeobox_KN; 1.
DR   SMART; SM00389; HOX; 1.
DR   SUPFAM; SSF46689; SSF46689; 1.
DR   PROSITE; PS50071; HOMEOBOX_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Complete proteome;
KW   Disease mutation; DNA-binding; Holoprosencephaly; Homeobox; Nucleus;
KW   Polymorphism; Reference proteome; Repressor; Transcription;
KW   Transcription regulation.
FT   CHAIN         1    401       Homeobox protein TGIF1.
FT                                /FTId=PRO_0000049318.
FT   DNA_BIND    164    226       Homeobox; TALE-type.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00108}.
FT   MOTIF       153    157       CTBP-binding motif.
FT   COMPBIAS    165    168       Poly-Arg.
FT   VAR_SEQ       1    149       Missing (in isoform 4).
FT                                {ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_046848.
FT   VAR_SEQ       1    129       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:10764806,
FT                                ECO:0000303|PubMed:15489334,
FT                                ECO:0000303|PubMed:8537382,
FT                                ECO:0000303|Ref.3}.
FT                                /FTId=VSP_013020.
FT   VAR_SEQ       1    115       Missing (in isoform 3).
FT                                {ECO:0000303|PubMed:14702039}.
FT                                /FTId=VSP_043108.
FT   VAR_SEQ     116    134       PSQGAQGPAPRRRLLETMK -> MTCSGKSCALARSSLTSS
FT                                Q (in isoform 3).
FT                                {ECO:0000303|PubMed:14702039}.
FT                                /FTId=VSP_043109.
FT   VAR_SEQ     130    133       LETM -> MKGK (in isoform 2).
FT                                {ECO:0000303|PubMed:10764806,
FT                                ECO:0000303|PubMed:15489334,
FT                                ECO:0000303|PubMed:8537382,
FT                                ECO:0000303|Ref.3}.
FT                                /FTId=VSP_013021.
FT   VARIANT     157    157       S -> C (in HPE4).
FT                                {ECO:0000269|PubMed:10835638}.
FT                                /FTId=VAR_009961.
FT   VARIANT     192    192       P -> R (in HPE4).
FT                                {ECO:0000269|PubMed:10835638}.
FT                                /FTId=VAR_009962.
FT   VARIANT     236    236       Q -> L (in HPE4).
FT                                {ECO:0000269|PubMed:15221788}.
FT                                /FTId=VAR_023803.
FT   VARIANT     280    280       T -> A (in HPE4).
FT                                {ECO:0000269|PubMed:10835638}.
FT                                /FTId=VAR_009963.
FT   VARIANT     289    289       P -> S (in dbSNP:rs11571512).
FT                                /FTId=VAR_047363.
FT   VARIANT     291    291       S -> F (in HPE4).
FT                                {ECO:0000269|PubMed:10835638}.
FT                                /FTId=VAR_009964.
FT   VARIANT     292    292       P -> L (in dbSNP:rs2229333).
FT                                /FTId=VAR_020151.
FT   VARIANT     292    292       P -> S (in dbSNP:rs4468717).
FT                                {ECO:0000269|PubMed:10764806,
FT                                ECO:0000269|Ref.3}.
FT                                /FTId=VAR_061268.
FT   CONFLICT     96     96       P -> Q (in Ref. 7; AAH31268).
FT                                {ECO:0000305}.
FT   HELIX       173    185       {ECO:0000244|PDB:2LK2}.
FT   HELIX       188    190       {ECO:0000244|PDB:2LK2}.
FT   HELIX       194    203       {ECO:0000244|PDB:2LK2}.
FT   STRAND      204    206       {ECO:0000244|PDB:2LK2}.
FT   HELIX       208    230       {ECO:0000244|PDB:2LK2}.
SQ   SEQUENCE   401 AA;  43013 MW;  4D9C76AFB37A29F0 CRC64;
     MVLAQSRVSA GVGSPHCSGS GGGGSDSFPW PASHPGNPQC SFSTAFLASP RLSRGTLAYL
     PPAPWSSLAT PSALLGSSCA PPPPPARCPQ PRALSPELGT KAGPRRPHRW ELPRSPSQGA
     QGPAPRRRLL ETMKGIVAAS GSETEDEDSM DIPLDLSSSA GSGKRRRRGN LPKESVQILR
     DWLYEHRYNA YPSEQEKALL SQQTHLSTLQ VCNWFINARR RLLPDMLRKD GKDPNQFTIS
     RRGAKISETS SVESVMGIKN FMPALEETPF HSCTAGPNPT LGRPLSPKPS SPGSVLARPS
     VICHTTVTAL KDVPFSLCQS VGVGQNTDIQ QIAAKNFTDT SLMYPEDTCK SGPSTNTQSG
     LFNTPPPTPP DLNQDFSGFQ LLVDVALKRA AEMELQAKLT A
//
ID   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";
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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
//
#~~# #~+~~+~# #~~#
#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
#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.