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SLiMSuite QSLiMFinder Server

# Output for QSLiMFinder V2.1.1: Wed Dec  9 00:47:09 2015
# 2 warnings; 0 errors: see log output (below) for details.
# JobID: 15120900008

Click here for QSLiMFinder 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 15120900008 (qslimfinder) Finished.
IP:122.150.74.70
No queue.
qslimfinder&query=P03254&uniprotid=P0C7T5,P38398,O00257,Q12873,Q99708,Q13363,P35221,Q92769,Q14526,Q13422,P15884,Q92831,Q8N3X6,Q96JN0,Q13465,Q96MY1,P48552,Q15291,A7XYQ1,Q9P2Y4,Q8IX07,P03254&dismask=T&consmask=F&featuremask=F&ambiguity=T&slimlen=5&maxwild=2
Run Started: 2015-12-09 00:47:09; PID=39396
Run finished: 2015-12-09 00:52:27

 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
qslimfinder 15120900008 FreqDisComp-5-8 Ql5w2o2a3 QSig 00:05:11 22 17 12754 6 1 8.57e-04 P.DLS.[KR] 4.77 6 6 5 0.038 5.85e-08 1 13 9
qslimfinder 15120900008 FreqDisComp-5-8 Ql5w2o2a3 QSig 00:05:11 22 17 12754 6 2 0.003 P[IL]DL 3.77 9 9 7 0.34 6.29e-07 1 13 9
qslimfinder 15120900008 FreqDisComp-5-8 Ql5w2o2a3 QSig 00:05:11 22 17 12754 6 3 0.004 [IL]DLS.[KR] 4.54 8 8 5 0.057 2.76e-07 1 13 9
qslimfinder 15120900008 FreqDisComp-5-8 Ql5w2o2a3 QSig 00:05:11 22 17 12754 6 4 0.018 P.DLS.K 5.00 4 4 4 0.021 1.21e-06 1 13 9
qslimfinder 15120900008 FreqDisComp-5-8 Ql5w2o2a3 QSig 00:05:11 22 17 12754 6 5 0.022 P.DL[ST] 3.77 11 10 7 0.48 4.41e-06 1 13 9
qslimfinder 15120900008 FreqDisComp-5-8 Ql5w2o2a3 QSig 00:05:11 22 17 12754 6 6 0.086 P[IL]DLS 4.77 5 5 4 0.036 6.12e-06 1 13 9
Dataset RunID Rank Pattern Sig Seq Start_Pos End_Pos Prot_Len Match Variant MisMatch Desc PepSeq PepDesign
qslimfinder 15120900008 1 P.DLS.[KR] 8.57e-04 ZN219_HUMAN__Q9P2Y4 626 632 722 PLDLSLR P.DLS.[KR] 0 RecName: Full=Zinc finger protein 219; PLDLSLR OK
qslimfinder 15120900008 1 P.DLS.[KR] 8.57e-04 E1A_ADE02__P03254 279 285 289 PLDLSCK P.DLS.[KR] 0 RecName: Full=Early E1A protein {ECO:0000305}; AltName: Full=Early E1A 32 kDa protein; PLDLSCK OK
qslimfinder 15120900008 1 P.DLS.[KR] 8.57e-04 NOL4L_HUMAN__Q96MY1 365 371 436 PTDLSMK P.DLS.[KR] 0 RecName: Full=Nucleolar protein 4-like; PTDLSMK OK
qslimfinder 15120900008 1 P.DLS.[KR] 8.57e-04 FOG1_HUMAN__Q8IX07 794 800 1006 PIDLSKK P.DLS.[KR] 0 RecName: Full=Zinc finger protein ZFPM1; AltName: Full=Friend of GATA protein 1; Short=FOG-1; Short=Friend of GATA 1; AltName: Full=Zinc finger protein 89A; AltName: Full=Zinc finger protein multitype 1; PIDLSKK OK
qslimfinder 15120900008 1 P.DLS.[KR] 8.57e-04 NRIP1_HUMAN__P48552 440 446 1158 PIDLSCK P.DLS.[KR] 0 RecName: Full=Nuclear receptor-interacting protein 1; AltName: Full=Nuclear factor RIP140; AltName: Full=Receptor-interacting protein 140; PIDLSCK OK
qslimfinder 15120900008 1 P.DLS.[KR] 8.57e-04 COM1_HUMAN__Q99708 490 496 897 PLDLSDR P.DLS.[KR] 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; PLDLSDR OK
qslimfinder 15120900008 2 P[IL]DL 0.003 FOG1_HUMAN__Q8IX07 794 797 1006 PIDL P[IL]DL 0 RecName: Full=Zinc finger protein ZFPM1; AltName: Full=Friend of GATA protein 1; Short=FOG-1; Short=Friend of GATA 1; AltName: Full=Zinc finger protein 89A; AltName: Full=Zinc finger protein multitype 1; PIDL OK
qslimfinder 15120900008 2 P[IL]DL 0.003 E1A_ADE02__P03254 279 282 289 PLDL P[IL]DL 0 RecName: Full=Early E1A protein {ECO:0000305}; AltName: Full=Early E1A 32 kDa protein; PLDL OK
qslimfinder 15120900008 2 P[IL]DL 0.003 ZN219_HUMAN__Q9P2Y4 626 629 722 PLDL P[IL]DL 0 RecName: Full=Zinc finger protein 219; PLDL OK
qslimfinder 15120900008 2 P[IL]DL 0.003 CBX4_HUMAN__O00257 472 475 560 PIDL P[IL]DL 0 RecName: Full=E3 SUMO-protein ligase CBX4; EC=6.3.2.-; AltName: Full=Chromobox protein homolog 4; AltName: Full=Polycomb 2 homolog; Short=Pc2; Short=hPc2; PIDL OK
qslimfinder 15120900008 2 P[IL]DL 0.003 ATX1L_HUMAN__P0C7T5 219 222 689 PLDL P[IL]DL 0 RecName: Full=Ataxin-1-like; AltName: Full=Brother of ataxin-1; Short=Brother of ATXN1; PLDL OK
qslimfinder 15120900008 2 P[IL]DL 0.003 LCORL_HUMAN__Q8N3X6 212 215 602 PLDL P[IL]DL 0 RecName: Full=Ligand-dependent nuclear receptor corepressor-like protein; Short=LCoR-like protein; PLDL OK
qslimfinder 15120900008 2 P[IL]DL 0.003 NRIP1_HUMAN__P48552 440 443 1158 PIDL P[IL]DL 0 RecName: Full=Nuclear receptor-interacting protein 1; AltName: Full=Nuclear factor RIP140; AltName: Full=Receptor-interacting protein 140; PIDL OK
qslimfinder 15120900008 2 P[IL]DL 0.003 LCOR_HUMAN__Q96JN0 64 67 433 PLDL P[IL]DL 0 RecName: Full=Ligand-dependent corepressor; Short=LCoR; AltName: Full=Mblk1-related protein 2; PLDL OK
qslimfinder 15120900008 2 P[IL]DL 0.003 COM1_HUMAN__Q99708 490 493 897 PLDL P[IL]DL 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; PLDL OK
qslimfinder 15120900008 3 [IL]DLS.[KR] 0.004 NRIP1_HUMAN__P48552 441 446 1158 IDLSCK [IL]DLS.[KR] 0 RecName: Full=Nuclear receptor-interacting protein 1; AltName: Full=Nuclear factor RIP140; AltName: Full=Receptor-interacting protein 140; IDLSCK OK
qslimfinder 15120900008 3 [IL]DLS.[KR] 0.004 E1A_ADE02__P03254 280 285 289 LDLSCK [IL]DLS.[KR] 0 RecName: Full=Early E1A protein {ECO:0000305}; AltName: Full=Early E1A 32 kDa protein; LDLSCK OK
qslimfinder 15120900008 3 [IL]DLS.[KR] 0.004 ZN219_HUMAN__Q9P2Y4 627 632 722 LDLSLR [IL]DLS.[KR] 0 RecName: Full=Zinc finger protein 219; LDLSLR OK
qslimfinder 15120900008 3 [IL]DLS.[KR] 0.004 FOG1_HUMAN__Q8IX07 795 800 1006 IDLSKK [IL]DLS.[KR] 0 RecName: Full=Zinc finger protein ZFPM1; AltName: Full=Friend of GATA protein 1; Short=FOG-1; Short=Friend of GATA 1; AltName: Full=Zinc finger protein 89A; AltName: Full=Zinc finger protein multitype 1; IDLSKK OK
qslimfinder 15120900008 3 [IL]DLS.[KR] 0.004 LCORL_HUMAN__Q8N3X6 232 237 602 LDLSTK [IL]DLS.[KR] 0 RecName: Full=Ligand-dependent nuclear receptor corepressor-like protein; Short=LCoR-like protein; LDLSTK OK
qslimfinder 15120900008 3 [IL]DLS.[KR] 0.004 HIC1_HUMAN__Q14526 242 247 733 LDLSKK [IL]DLS.[KR] 0 RecName: Full=Hypermethylated in cancer 1 protein; Short=Hic-1; AltName: Full=Zinc finger and BTB domain-containing protein 29; LDLSKK OK
qslimfinder 15120900008 3 [IL]DLS.[KR] 0.004 LCOR_HUMAN__Q96JN0 83 88 433 LDLSTK [IL]DLS.[KR] 0 RecName: Full=Ligand-dependent corepressor; Short=LCoR; AltName: Full=Mblk1-related protein 2; LDLSTK OK
qslimfinder 15120900008 3 [IL]DLS.[KR] 0.004 COM1_HUMAN__Q99708 491 496 897 LDLSDR [IL]DLS.[KR] 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; LDLSDR OK
qslimfinder 15120900008 4 P.DLS.K 0.018 E1A_ADE02__P03254 279 285 289 PLDLSCK P.DLS.K 0 RecName: Full=Early E1A protein {ECO:0000305}; AltName: Full=Early E1A 32 kDa protein; PLDLSCK OK
qslimfinder 15120900008 4 P.DLS.K 0.018 FOG1_HUMAN__Q8IX07 794 800 1006 PIDLSKK P.DLS.K 0 RecName: Full=Zinc finger protein ZFPM1; AltName: Full=Friend of GATA protein 1; Short=FOG-1; Short=Friend of GATA 1; AltName: Full=Zinc finger protein 89A; AltName: Full=Zinc finger protein multitype 1; PIDLSKK OK
qslimfinder 15120900008 4 P.DLS.K 0.018 NRIP1_HUMAN__P48552 440 446 1158 PIDLSCK P.DLS.K 0 RecName: Full=Nuclear receptor-interacting protein 1; AltName: Full=Nuclear factor RIP140; AltName: Full=Receptor-interacting protein 140; PIDLSCK OK
qslimfinder 15120900008 4 P.DLS.K 0.018 NOL4L_HUMAN__Q96MY1 365 371 436 PTDLSMK P.DLS.K 0 RecName: Full=Nucleolar protein 4-like; PTDLSMK OK
qslimfinder 15120900008 5 P.DL[ST] 0.022 E1A_ADE02__P03254 279 283 289 PLDLS P.DL[ST] 0 RecName: Full=Early E1A protein {ECO:0000305}; AltName: Full=Early E1A 32 kDa protein; PLDLS OK
qslimfinder 15120900008 5 P.DL[ST] 0.022 ZN219_HUMAN__Q9P2Y4 626 630 722 PLDLS P.DL[ST] 0 RecName: Full=Zinc finger protein 219; PLDLS OK
qslimfinder 15120900008 5 P.DL[ST] 0.022 IKZF1_HUMAN__Q13422 34 38 519 PEDLS P.DL[ST] 0 RecName: Full=DNA-binding protein Ikaros; AltName: Full=Ikaros family zinc finger protein 1; AltName: Full=Lymphoid transcription factor LyF-1; PEDLS OK
qslimfinder 15120900008 5 P.DL[ST] 0.022 FOG1_HUMAN__Q8IX07 794 798 1006 PIDLS P.DL[ST] 0 RecName: Full=Zinc finger protein ZFPM1; AltName: Full=Friend of GATA protein 1; Short=FOG-1; Short=Friend of GATA 1; AltName: Full=Zinc finger protein 89A; AltName: Full=Zinc finger protein multitype 1; PIDLS OK
qslimfinder 15120900008 5 P.DL[ST] 0.022 NOL4L_HUMAN__Q96MY1 365 369 436 PTDLS P.DL[ST] 0 RecName: Full=Nucleolar protein 4-like; PTDLS OK
qslimfinder 15120900008 5 P.DL[ST] 0.022 NOL4L_HUMAN__Q96MY1 149 153 436 PEDLT P.DL[ST] 0 RecName: Full=Nucleolar protein 4-like; PEDLT OK
qslimfinder 15120900008 5 P.DL[ST] 0.022 LCORL_HUMAN__Q8N3X6 212 216 602 PLDLT P.DL[ST] 0 RecName: Full=Ligand-dependent nuclear receptor corepressor-like protein; Short=LCoR-like protein; PLDLT OK
qslimfinder 15120900008 5 P.DL[ST] 0.022 NRIP1_HUMAN__P48552 440 444 1158 PIDLS P.DL[ST] 0 RecName: Full=Nuclear receptor-interacting protein 1; AltName: Full=Nuclear factor RIP140; AltName: Full=Receptor-interacting protein 140; PIDLS OK
qslimfinder 15120900008 5 P.DL[ST] 0.022 BRCA1_HUMAN__P38398 1544 1548 1863 PHDLT P.DL[ST] 0 RecName: Full=Breast cancer type 1 susceptibility protein; EC=6.3.2.-; AltName: Full=RING finger protein 53; PHDLT OK
qslimfinder 15120900008 5 P.DL[ST] 0.022 LCOR_HUMAN__Q96JN0 64 68 433 PLDLT P.DL[ST] 0 RecName: Full=Ligand-dependent corepressor; Short=LCoR; AltName: Full=Mblk1-related protein 2; PLDLT OK
qslimfinder 15120900008 5 P.DL[ST] 0.022 COM1_HUMAN__Q99708 490 494 897 PLDLS P.DL[ST] 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
qslimfinder 15120900008 6 P[IL]DLS 0.086 FOG1_HUMAN__Q8IX07 794 798 1006 PIDLS P[IL]DLS 0 RecName: Full=Zinc finger protein ZFPM1; AltName: Full=Friend of GATA protein 1; Short=FOG-1; Short=Friend of GATA 1; AltName: Full=Zinc finger protein 89A; AltName: Full=Zinc finger protein multitype 1; PIDLS OK
qslimfinder 15120900008 6 P[IL]DLS 0.086 NRIP1_HUMAN__P48552 440 444 1158 PIDLS P[IL]DLS 0 RecName: Full=Nuclear receptor-interacting protein 1; AltName: Full=Nuclear factor RIP140; AltName: Full=Receptor-interacting protein 140; PIDLS OK
qslimfinder 15120900008 6 P[IL]DLS 0.086 E1A_ADE02__P03254 279 283 289 PLDLS P[IL]DLS 0 RecName: Full=Early E1A protein {ECO:0000305}; AltName: Full=Early E1A 32 kDa protein; PLDLS OK
qslimfinder 15120900008 6 P[IL]DLS 0.086 ZN219_HUMAN__Q9P2Y4 626 630 722 PLDLS P[IL]DLS 0 RecName: Full=Zinc finger protein 219; PLDLS OK
qslimfinder 15120900008 6 P[IL]DLS 0.086 COM1_HUMAN__Q99708 490 494 897 PLDLS P[IL]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
#qslimfinder# 22 Seq; 17 UPC; 20.594 MST; blaste=1.00e-04, blastcf=F, blastf=T
UP	N	MST	Seqs
1	2	1.909	ATX1L_HUMAN__P0C7T5 SOBP_HUMAN__A7XYQ1
2	1	1.000	BRCA1_HUMAN__P38398
3	1	1.000	CBX4_HUMAN__O00257
4	1	1.000	CHD3_HUMAN__Q12873
5	1	1.000	COM1_HUMAN__Q99708
6	1	1.000	CTBP1_HUMAN__Q13363
7	1	1.000	CTNA1_HUMAN__P35221
8	1	1.000	E1A_ADE02__P03254
9	4	3.035	FOG1_HUMAN__Q8IX07 HIC1_HUMAN__Q14526 IKZF1_HUMAN__Q13422 ZN219_HUMAN__Q9P2Y4
10	1	1.000	HDAC2_HUMAN__Q92769
11	1	1.000	ITF2_HUMAN__P15884
12	1	1.000	KAT2B_HUMAN__Q92831
13	2	1.651	LCORL_HUMAN__Q8N3X6 LCOR_HUMAN__Q96JN0
14	1	1.000	MDS1_HUMAN__Q13465
15	1	1.000	NOL4L_HUMAN__Q96MY1
16	1	1.000	NRIP1_HUMAN__P48552
17	1	1.000	RBBP5_HUMAN__Q15291
qslimfinder: 22 Seq, 17 UPC, 6 Sig SLiMs in 1 Clouds

Cloud 1 (6 SLiMs):	P.DLS.[KR]	P[IL]DL	[IL]DLS.[KR]	P.DLS.K	P.DL[ST]	P[IL]DLS	(p = 8.57e-04)
9 UPC	13 Seq:	ATX1L_HUMAN__P0C7T5	BRCA1_HUMAN__P38398	CBX4_HUMAN__O00257	COM1_HUMAN__Q99708	E1A_ADE02__P03254	FOG1_HUMAN__Q8IX07	HIC1_HUMAN__Q14526	IKZF1_HUMAN__Q13422	LCORL_HUMAN__Q8N3X6	LCOR_HUMAN__Q96JN0	NOL4L_HUMAN__Q96MY1	NRIP1_HUMAN__P48552	ZN219_HUMAN__Q9P2Y4

SLiMMaker Consensus: P[IL]DL[ST]
- SLiM matches 7 of 16 sequences (43.8%).

PLDLSCK
PIDLSKK
PTDLSMK
PIDLSCK
PLDLSDR
PEDLSTT
PLDLSLR
PHDLTET
PLDLTVN
PLDLTVR
PEDLTVG
GLDLSKK
VLDLSTK
VLDLSTK
PIDLRCV
PLDLAPG


#Cloud Seq coverage/overlap
Cloud	Dataset	1
1:P.DLS.[KR]	0.591	1.000


#Cloud UPC coverage/overlap
Cloud	Dataset	1
1:P.DLS.[KR]	0.529	1.000

>ATX1L_HUMAN__P0C7T5 RecName: Full=Ataxin-1-like; AltName: Full=Brother of ataxin-1; Short=Brother of ATXN1;
XKPVHERSQECLPPKKRDLPVTSEDMGRTTSCSTNHTPSSDASEWSRGVVVAGQSQAGARVSLGGDGAEAITXXXXXXXXXXXXXXVXXAXXXPTGLPSVVNMSPLXXXXNVASSLIQHXXIXYPPLHYAXXXSTXXXXXXXPXXXXXXXXXXXXXXXLLSPSANLATXHLPXFVPYASLLAEGATPXXQAXSPAHSFNKAPSATSPSGQLPHHSSTQPLDLAPGRMPIYYQMSRLPAGYTLHETPPAGASPVLTPQESQSALEXXXANGGQRPRERNLVRRESEALDSPNSKGEGQGLVPXXECXVDGQLFSGSQTPRVEVAAPAHRGTPDTDLEVQRVVGALASQDYRVVAAQRKEEPSPLNLSHHTPDHQGEGRGSARNPAELAEKSQARGFYPQSHQEPVKHRPLPKAMVVANGNLVPTGTDSGLLPVGSEILVASSLDVQARATFPDKEPTPPPITSSHLPSHFMKGAIIQLATGELKRVEDLQTQDFVRSAEVSGXXXIDSSTVVDXQXSXXXXXXXLHXXXXXXXSKVSIEVPPEXXXXXYGQGWSXXXXGXXXXXXXLXXXXXXXXXXXXXXXXXSLXXNSVSQASCAPPSQLGPPRERPERTVLGSRELCDSEGKSQPAGEGSRVVEPSQPESGAQACWPAPSFQRYSMQGEEARAALLRPSFIPQEVKLSIEGRSNAGK
>BRCA1_HUMAN__P38398 RecName: Full=Breast cancer type 1 susceptibility protein; EC=6.3.2.-; AltName: Full=RING finger protein 53;
XDLSALRXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXLXXXXXXXXSXXESTXFXXXXXXXXXXXXXXXXXXXXXXXXSYNFAKKENNSPEHLKDEVSIIQSMGYRNRAKRLLQSEPENPSLQETSLSVQLSNLGTVRTLRTKQRIQPQKTSVYIELGSDSSEDTVNKATYCSVGDQELLQITPQGTRDEISLDSAKKAACEFSETDVTNTEHHQPSNNDLNTTEKRAAERHPEKYQGSSVSNLHVEPCGTNTHASSLQHENSSLLLTKDRMNVEKAEFCNKSKQPGLARSQHNRWAGSKETCNDRRTPSTEKKVDLNADPLCERKEWNKQKLPCSENPRDTEDVPWITLNSSIQKVNEWFSRSDELLGSDDSHDGESESNAKVADVLDVLNEVDEYSGSSEKIDLLASDPHEALICKSERVHSKSVESNIEDKIFGKTYRKKASLPNXXHXXXXXIXXXFVTEPQIIQERPLTNKLKRKRRPTSGLHPEDFIKKADLAVQKTPEMINQGTNQTEQNGQVMNITNSGHENKTKGDSIQNEKNPNPIESLEKESAFKTKAEPISSSISNMELELNIHNSKAPKKNRLRRKSSTRHIHALELVVSRNLSPPNCTELQIDSCSSSEEIKKKKYNQMPVRHSRNLQLMEGKEPATGAKKSNKPNEQTSKRHDSDTFPELKLTNAPGSFTKCSNTSELKEFVNPSLPREXKXXKLETVKVSNNAEDPKDLMLSGERVLQTERSVEXXXISLVPGTDYGTQESISLLEVSTLGKAKTEPXKCVSQCAAFXXXKGLIHGCSKDNRNDTEGFKYPLGHEVNHSRETSIEMEESELDAQYLQNTFKVSKRQSFAPFSNPGNAEEECATFSAHSGSLKKQSPKVTFECEQKEENQGKNESNIKPVQTVNITAGFPVVGQKDKPVDNAKCSIKGXSRFCLSSQFRGNETGLITPNKHGLLQNPYRIPPLFPIKSFVKTKCKKNLLEENFEEHSMSPEREMGNENIPSTVSTISRNNIRENVFKEASSSNINEVGSSTNEVGSSINEIGSSDENIQAELGRNRGPKLNAMLRLGVLQPEVYKQSLPGSNCKHPEIKKQEYEEVVQTVNTDFSPYLISDNLEQPMGSSHASQVCSETPDDLLDDGEIKEDTSFAENDIKESSAVFSKSVQKGELSRSPSPFTHTHLAQGYRRGAKKLESSEENLSSEDEELPCFQHLLFGKVNNIPSQSTRHSTVATECLSKNTEENLXSLKNSXXXXXNQVILAKASQEHHLSEETKCSASLFSSQCSELEDLTANTNTQDPFLIGSSKQMRHQSESQGVGLSDKELVSDDEERGTGLEENNQEEQSMDSNLGEAASGCESETSVSEDCSGLSSQSDILTTQQRDTMQHNLIKLQQEMAELEAVLEQHGSQPSNSYPSIISDSSALEDLRNPEQSTSEKAVLTSQKSSEYPISQNPEGLSADKFEVSADSSTSKNKEPGVERSSPSKCPSLDDRWYMHSCSGSLQNRNYPSQEELIKVVDVEEQQLEESGPHDLTETSYLPRQDLEGTPYLESGISLFSDDPESDPSEDRAPESARVGNIPSSTSALKVPQLKVAESAQSPAAAHTTDTAGYNAMEESVSREKPELTASTERVNKRMSMVVSXXXXXXXXXXXXXXXXXXXXXTXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXLNEHDFEVRGDVVNGRNHQGPKRARESQDRKXXRXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXVVQPDXXXXXXGFHXXXQMXXXXXXXXXXXXXXXXXXXXXXXXXXXXPQIPHSHY
>CBX4_HUMAN__O00257 RecName: Full=E3 SUMO-protein ligase CBX4; EC=6.3.2.-; AltName: Full=Chromobox protein homolog 4; AltName: Full=Polycomb 2 homolog; Short=Pc2; Short=hPc2;
XELPAVGEHXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXTWEPEENXXDPRLLIAFQNRERQEQLMGYRKRGPKPKPLVVQVPTFARRSNVLTGLQDSSTDNRAKLDLGAQGKGQGHQYELNSKKHHQYQPHSKERAGKPPPPGKSGKYYYQLNSKKHHPYQPDPKMYDLQYQGGHKEAPSPTCPDLGAKSHPPDKWAQGAGAKGYLGAVKPLAGAAGAPGKGSEKGPPNGMMPAPKEAVTGNGIGGKMKIVKNKNKNGRIVIVMSKYMENGMQAVKIKSGEVAEGEARSPSHKKRAADERHPPADRTFKKAAGAEEKKVEAPPKRREEEVSGVSDPQPQDAGSRKLSPTKEAFGEQPLQLTTKPDLLAWDPARNTHPPSHXPXPXPXXXXXXXXXXXHAVGLNLSHVRKRCLSETHGEREPCKKRLTARSISTPTCLGGSPAAERPADLPPAAALPQPEVILLDSDLDEPIDLRCVKTRSEAGEPPSSLQVKPETPASXXVXVXXXXAPTTTAEKPPAEAQDEPAESLSEFKPXXXXXXXXXXXXXXXXXXXXXYVTV
>CHD3_HUMAN__Q12873 RecName: Full=Chromodomain-helicase-DNA-binding protein 3; Short=CHD-3; EC=3.6.4.12; AltName: Full=ATP-dependent helicase CHD3; AltName: Full=Mi-2 autoantigen 240 kDa protein; AltName: Full=Mi2-alpha; AltName: Full=Zinc finger helicase; Short=hZFH;
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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;
XNISGSSCGSPNSADTSSDFKDLWTKLKECHDXEVQGLQVKVTXXKXXRXXXXXRLXXFXTKNQQLREQQKVLHXXIKXXXXXXXXXXXXRCAVTEEHMRKKQQEFENIRQQNLKLITELMNERNTLQEENKKLSEQLQQKIENDQQHQAAELECEEDVIPDSPITAFSFSGVNRLRRKENPHVRYIEQTHTKLEHSVCANEMRKVSKSSTHPQHNPNENEILVADTYDQSQSPMAKAHGTSSYTPDKSSFNLATVVAETLGLGVQEESETQGPMSPLGDELYHCLEGNHKKQPFEESTRNTEDSLRFSDSTSKTPPQEELPTRVSSPVFGATSSIKSGLDLNTSLSPSLLQPGKKKHLKTLPFSNTCISRLEKTRSKSEDSALFTHHSXGSEVNKIIIQSSNKQILINKNISESLGEQNRTEYGKDSNTDKHLEPLKSLGGRTSKRKKTEXXSXHEVSCPQASFDKENAFPFPMDNQFSMNGDCVMDKPLDLSDRFSAIQRQEKSQGSETSKNKFRQVTLYEALKTIPKGFSSSRKASDGNCTLPKDSPGEPCSQECIILQPLNKCSPDNKPSLQIKEENAVFKIPLRPRESLETENVLDDIKSAGSHEPIKIQTRSDHGGCELASVLQLNXCRTGKIKSLQNNQDVSFENIQWSIDPGADLSQYKMDVTVIDTKDGSQSKLGGETVDMDCTLVSETVLLKMKKQEQKGEKSSNEERKMNDSLEDMFDRTTHEEYESCLADSFSQAADEEEELSTATKKLHTHGDKQDKVKQKAFVEPYFKGDERETSLQNFPHIEVVRKKEERRXXXXXXXXXXXXXYAXXPAXEREKKLASCSRHRFRYIPXNTPENFWEVGFPSTQTCMERGYIKEDLDPCPRPKRRQPYNAIFSPKGKEQKT
>CTBP1_HUMAN__Q13363 RecName: Full=C-terminal-binding protein 1; Short=CtBP1; EC=1.1.1.-;
XGSSHLLNKGLPLGVRPPIMNGPLHPRPXVALLDGXXXXXXXXXXXXXXXXXXXXXXXXXXXXEKXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXREXXXVQSVEQIREVASGAXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXNDFXXXXXXXGAXXXNTAXXXXXXEKALAQALKEGRIRGAALDVHESEPFSFSQGPLKDAPNLICTPHAAWYSEQASIEMREEAAREIRRAITGRIPDSLKNCVNKDHLTAATHWASMDPAVVHXELNGAXXXYPPXVXXXXPXGIPAAVEGIVPSAMSLSHGLPPVAHPPHAPSPGQTVKPEADRDHASDQL
>CTNA1_HUMAN__P35221 RecName: Full=Catenin alpha-1; AltName: Full=Alpha E-catenin; AltName: Full=Cadherin-associated protein; AltName: Full=Renal carcinoma antigen NY-REN-13;
XTAVHAGNINXXXXXXXXXXXXXXXXXXLXXXXTQVTTLVNTNSKGPSNKKRGRSKKAHVLAASVEQATENFLEKGDKIAKESQFLKXXLVAAVEDVRKQGDLMKAAAGEFADDPCSSVKRGXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXLGIQYKALXXXVDKLNIMAAKRQQELKDVGHRDQMAAARGIXXXXXXXXXXXXXXXXXXXDVXXXXXNRXXXXXXLQQAXXXISNAAQATASDDASQHQGXXXGELAYALNNFDXXXIVDPLSFSEERFRPSLEERLESIISGAALMADSSCTRDDRRERIVAECNXVRXXLQDLLSEYMGNAGRKERSDALNSAIDKMTKKTRDLRRQLRKAVMDHVSXXXXXXXXXXXXXXEXXXXXNEXEVKEYAQVFXXXXXXXXXXXXXXXXXXXXXXXXXLXRXXXXXXXXXXXXXXXXXXXXXXXXQSXXAQENMDLFKXQWEXXVXXLXXXXXXXXXXDXXXXXXXXXXXXXXXXXXXXXXXXXXXXLDRTAGXXXXXAAXVIXVVTSXMDNYEPGVYTEKVLEATKLLSNTVMPRFTEQVEAAVEALSSDPAQPMDENEFIDASRLXXXXXXXXXXAVLMIRTPEELDDSDFETEDFDVRSRTSVQTEDDQLIAGQSARAIMAQLPQEQKAKIAEQVASFQEEKSKLDAEVSKWDDSGNDIIVXAKQMXXXXMEMTDFTRGKGPLKNTSDVISAAKKIAEAGSRMDKLGRTIADHXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXTKXQKSQGMASLNLPAVSWKMKAPEKKPLVKREKQDETQTKIKRASQKKHVNPVQALSEFKAMDSI
>E1A_ADE02__P03254 RecName: Full=Early E1A protein {ECO:0000305}; AltName: Full=Early E1A 32 kDa protein;
XRHIICHGGXXXXXXXASXXXQXIEEVLADNLPPPSHFEPPTLHELYDLDVTAPEDPNEEAVSQIFPDSVMLAVQEGIDLLTFPPAPGSPEPPHLSRQPEQPEQRALGPVSMPNLVPEVIDLTCHEAGFPPSDDEDXXGXEFVLDYVEXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXSPVSEPEPEPEPEPEPARPTRRPKLVPAILRRPTSPVSRECNSSTDSCDSGPSNTPPEIHPVVPLCPIKPVAVRXXGRRXXXECIEDLLNXXGQPLDLSCKRPRP
>FOG1_HUMAN__Q8IX07 RecName: Full=Zinc finger protein ZFPM1; AltName: Full=Friend of GATA protein 1; Short=FOG-1; Short=Friend of GATA 1; AltName: Full=Zinc finger protein 89A; AltName: Full=Zinc finger protein multitype 1;
XSRRKQSNPRQIKRSLGDMEAREEVQLVGASHMEQKATAPEAPSPPSADVNSPXXLXXXTSPGGPKELEGQEPEPRPTEEEPGSPWSGPDELEPVVQDGQRRIRARLSLATGLSWGPFHGSVQTRASSPRQAEPSPALTLXXXXXXXXXXXXPQAXXEAEANTEXHRKDDALWCRVTKPVXXGGLLSVLLTAEPHSTPGHPVKKEPAEPTCPAPAHDLQLLPQQAGXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXGTGSPAAAATDEKPKETYPNERVCPFPQCRKXXXSASSLEIHMRSXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXQPGSKGEIYSPGAGHPATKLPPDSLGSFQQQHTALQGPLASADLGLAPTPSPGLDRKALAEATNGEARAEPLAQNGGSSEPPAAPRSIKVEAVEEPEAAPILGPGEPGPQAPSRTPSPRSPAPARVKAELSSPTPGSSPVPGELGLAXXXFXXXYVFGPDAAPPASEILAKMSELVHSRLQQGAXAXAXGAQTGLFPGXXXXXXXXXXXXXXXXXXXXXXXXXXYCSGRRAPEDAPAARRPKAPPGPARAPPGQPAEPDAPRSSPGPGAREEGAGGAATPEDGAGGRGSEGSQSPGSSVDDAEDDPSRTLCEACNIRFSRHEXXTVHKRYYCASRHDPPPRRPAAXXGXXGXAAXPAPSPAAPVRTXXXRKLYELHAAGAPXXXXXGHAPAPESPRPGSGSGSGPGLAPARSPGPAADGPIDLSKKPRRPLPGAPAPALAXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXLLEXFXXXXXXLLGAPLAGPGVEARTPADRGPSPAPAPAASPQPGSRGPRDGLGPEXQEXXXGXXXSPAAAPEAVXXXXAXPSYSDKGVQTPSKGTPAPLPNGNHXXXXXXXXXXXXXXXXXXXXXXXXXXXAAEHVK
>HDAC2_HUMAN__Q92769 RecName: Full=Histone deacetylase 2; Short=HD2; EC=3.5.1.98;
XXYSQGGXXXXXXXXXXXXXXXXXXGQGXXMKXHRIRMXXXXXXXXXXXXXXXXYRPHKATAEEMTKYHSDEYIKFLRSIRPDNMSEYSKQMQRFNVXXDXXXXXXXXXXXXXXXXXXXXGAVKLNRQXTDMAVNWAGGLHXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXYXXXXXXXXXXXXXXXXXXXXGDLRXXXAXXXXXYXXNFPMRDXXDDEXYGQXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXNXYXXXXXXXFKXHISPSNMTNQNTPEYMEKIKQRLFENLRMLPHAPGVQMQAIPEDAVHEDSGDEDGEDPDKRISIRASDKRIACDEEFSDSEDEGEGGRRNVADHKKGAKKARIEEDKKETEDKKTDVKEEDKSKDNSGEKTDTKGTKSEQLSNP
>HIC1_HUMAN__Q14526 RecName: Full=Hypermethylated in cancer 1 protein; Short=Hic-1; AltName: Full=Zinc finger and BTB domain-containing protein 29;
XTFPEADILLKSGECAGQTMLDTMEAPGHSRQLLLQLXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXYCHLRGXXXXXXGYAPYGRPGRGLRAATPVIQACYPSXVGXXXXXAAEXPSGPEAAVNTHCAELYAXXXGPAAXLCXXXXXXXXXCGLDLSKKSPPGSAAPERPLAERELPXRXDSXPSAGPAAYKEPPLALPSLPPLPFQKLEEAAPPSDPFRGGSGSPGPEPPGRPDGPSLLYRWMKHEPGLGSYGDELGRERGSPSERCEERGGDAAVSPGGPPLGLAPPPRYPGSLDGPXAXXDGDDYKSSSEETGSSEDPSPPGGHLEGYPCPHLAYGEPXXFXXXXXXXXXXXXXXXXXEQLNAHVEAHVXXXEALYGRAEXXEVXXGXAGLGPPFXXXGDKVAGAPGGLGEXLRPYRCASCDKSYKDPATLRQHEKTHWXTRPXPCTICGKKFTQRGTMTRHMRSHLXXXXXXXXXXXXXXXXXXRLTEHMRIHSXXKPXXCQVCGXXXXXXRNLISHMKMHAVXXAXXXXXXXAGLGGLPGVPGPDGKGKLDFPEGVFAVXRXTAEXLSLKQXDKAXXXXLLAQXXXXXXXXXXXXXXXXXXXXXXXXXXLXPDKAAEVLSQGAHLAAGPDGRTIDRFSPT
>IKZF1_HUMAN__Q13422 RecName: Full=DNA-binding protein Ikaros; AltName: Full=Ikaros family zinc finger protein 1; AltName: Full=Lymphoid transcription factor LyF-1;
XDADEGQDMSQVSGKESPPVSDTPDEGDEPMPIPEDLSTTSGGQQSSKSDRVVASNVKVETQSDEENGRACEMNGEECAEDLRMLDASGEKMNGSHRDQGSSALSGVGGIRXXXXXXXXXXXXXXXXXXXXXXXXXRSHTXERPFQCNQCGXXXXXXGNXLRHIKLHXXXXXXXXXXXXXXXXXXXXXXXHLRTHSXXKPXXCGYCGRSYKQRSSLEEHKERCHNYLESMGLPGTLYPVIKEETNHSEMAEDLCKIGSERSLVLDRLASNVAKRKSSMPQKFLGDKGLSDTPYDSSASYEKENEMMKSHVMDQAINNAINYLGAESLRPLVQTPPGGSEVVPVISPMYQLHKPLAEGTPRSNHSAQDSAVENLLLLSKAKLVPSEREASPSNSCQDSTDTESNNEEQRSGLIYLTNHIAPHARNGLSLKEEHRAYDLLRAASENSQDALRVVSTXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXFSSHITRGEHRFHMS
>ITF2_HUMAN__P15884 RecName: Full=Transcription factor 4; Short=TCF-4; AltName: Full=Class B basic helix-loop-helix protein 19; Short=bHLHb19; AltName: Full=Immunoglobulin transcription factor 2; Short=ITF-2; AltName: Full=SL3-3 enhancer factor 2; Short=SEF-2;
XHHQQRMAALGTDKELSDLLDFSAMFSPPVSSGKNGPTSLASGHFTGSNVEDRSSSGSWGNGGHPSPSRNYGDGTPYDHMTSRDLGSHDNLSPPFVNSRIQSKTERGSYSSYGRESNLQGCHQQSLLGGDMDMGNPGTLSPTKPGSQYYQYSSNNPRRRPLHSSAMEVQTKKVRKVPPGLPSSVYAPSASTADYNRDSPGYPSSKPATSTFPSSFFMQDGHHSXDPWXXXSGMNQPGYAGMLGNSSHIPQSSSYCSLHPHERLSYPSHSSADINSSLPPMSTFHRSGTNHYSTSSCTPPANGTDSIMANRGSGAAGSSQTGDALGKALASIYSPDHTNNSFSSNPSTPVGSPPSLSAGTAVWSRNGGQASSSPNYEGPLHSLQSRIEDRLERLDDAIHVLRNHAVGPSTAMPGGHGDMHGIIGPSHNGAMGXLXSXYGTGLLSANRHSLMVGTHREDGVALRGSHSLLPNQVPVPQLPVQSATSPDLNPPQDPYRGMPPGLQGQSVXXGXSEIKSDDEGDENLQDTKSSEDKKLDDDKKDIKSITSNNDDEDLTPEQKAEREKERRMANNARERLRVRDINEAXXXXGRMVQLHLKXXXXXXXXXXXXXXXXXXXXXXXXXRXRNLNPKAACLKRREEEKVSSEPPPLSLAGPHPGMGDASNHMGQM
>KAT2B_HUMAN__Q92831 RecName: Full=Histone acetyltransferase KAT2B; EC=2.3.1.48; AltName: Full=Histone acetyltransferase PCAF; Short=Histone acetylase PCAF; AltName: Full=Lysine acetyltransferase 2B; AltName: Full=P300/CBP-associated factor; Short=P/CAF;
XSEAGXAXPXXCXAXAGAGAGPGALPPQPAALPPAPPQGSPCAAAAGGSGXXGPATXVXXXGTAEGPXXXGSARIAVKKAQLRSAPRAKKLEKLGVXXXXXXXXXXKCNGWKNPNXSXTXPRADLQQIIVSLTEXXXXXXXXXXXXVSHLEXXSXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXKPVVEGSLEKKPPFEKPSIEQGVNNFVQYKFSHXXXXEXXXXXXXXXXXXXXXXXXXXXAPSQRRLRSPNDDISGXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXQLLXQARQEKDKLPLEKRXXXXXXXXXXXXXXEEXVXSQNSPIWDQDFLSASSRTSQLGIQTVINPPPVAGTISYNXTXXSLEQPNAGSSSPACKASSGLEANPGEKRKMTDSHVLEEAKKPRVMGDIPMELINEVMSTITDPAAMLGPETNFLSAHSARDEAARLEERRGVXXFHVVGNSXXXXXXXXXXXXXXXXXXXXXXXXPXXXXXYXTXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXIXXXXXXXXXXYPGLXCFKDGVRQIPIESIPGIRETGWKPSGKEKSKEPRDPDQLYSTLKSILQQVKSHQSAWPFMEPVKRXXXXXYXXVXXXXXXXXXXXXXLXXXXXXXXXXXXXXXXXXXXXCKXXXXXXXXXXXXXXXXXXXXXXXXXXAGLIDK
>LCORL_HUMAN__Q8N3X6 RecName: Full=Ligand-dependent nuclear receptor corepressor-like protein; Short=LCoR-like protein;
XDKGRERMAXXXXXXXXXAXXXXCRSPRCAAERXGFRXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXFEXXEPEELTDWSXDEKXXFCXXXRXXXSDCIPSLDSSQSTPTEELSSQGQSNTDKIECQAENYLNALFRKKDLPQNCDPNIPLVAQXLXXXXXXQFAIEYISKSGKTQENRNGSIGPSIVCKSIQMNQAENSLQEEQEGPLDLTVNRMQEQNTQQGDGVLDLSTKKTSIKSEESSICDPSSENSVAGRLHRNREDYVERSAEFADXXLSXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXLEAXXXXKPASFKNKTRDFHDSYSYKDSXEXXXXXXXXXXXXRAQAEXXEKSKLNLLETSEXXXPXASTYXXQXTLQKMVTQFKEKNESLQYETSNPTVQLKIPQLRVSSVSKSQPDGSGLLDVMYQVSKXSSVLEGSALQKLKNILPKQNKIECSGPVTHSSVDSYFXHGDLSPLCLNSKNGTVDGTSENTEDGLDRKDSKQPRKKRGRYRQYDHEIMEEAIAMVMSGKMSVSKAQGIYGVPHSTLEYKVKERSGTLKTPPKKKLRLPDTGLYNMTDSGTGSCKNSSKPV
>LCOR_HUMAN__Q96JN0 RecName: Full=Ligand-dependent corepressor; Short=LCoR; AltName: Full=Mblk1-related protein 2;
XQRMIQQFAAEYTSKNSSTQDPSQPNSTKNQSLPKASPVTTSPTAATTQNPVLSKLLMADQDSPLDLTVRKSQSEPSEQDGVLDLSTKKSPCAGSTSLSHSPGCSSTQGNGRPGRPSQYRPDGLRSGDGVPPRSLQDGTREGFGHSTSLKVPLARSLQISEELLSRNQLSTAASLGPSGLQNHGQHLILSREASXXXXHYEXXLXRMKXXGXGXXXXISDLPFLAENSAFPKMALQAKQDGKKDVSHSSPVDLKIPQVRGMDLSWESRTGDQYSYSSLVMGSQTESALSKKLRAILPKQSRKSMLDAGPDSWGSDAEQSTSGQPYPTSDQEGDPGSKQPRKKRGRYRQYNSEILEEAISVVMSGKXXXSKAQSIYGIPHSTLEYKVKERLGTLKNPPKKKMKLMRSEGPDVSVKIELDPQGEAAQSANESKNE
>MDS1_HUMAN__Q13465 RecName: Full=MDS1 and EVI1 complex locus protein MDS1; AltName: Full=Myelodysplasia syndrome 1 protein; AltName: Full=Myelodysplasia syndrome-associated protein 1;
XRSKGRARKLATNNECVYGNYPEIPLEEMPDADGVASTPSLNIQEPCSPATSSEAFTPKEGSPYKAPIYIPDDIPIPAEFELRESNMPGAGLGIWTKRKIXXGEKFGPYVGEQRSNLKDPSYGWEVHLPXXXXXXXXXWXXXXXXXXXXXXXXXXXXXXXXXXQCAFLS
>NOL4L_HUMAN__Q96MY1 RecName: Full=Nucleolar protein 4-like;
XSDSTWMSADPHLASSLSPSQDERMRSPQNLHSQEDDDSXXEXGSGNGSSTLNPSTSSSTQGDPAFPEMNGNGAVAPMDFTTAAEDQPINLCDKLPPATALGTASYPSDGCGADGLRSRVKYGVKTTPESPPYSSGSYDSIKTEVSGCPEDLTVGRAPTADXXXXXHXXHEDNDKMNDSEGMDPERLKAFNMFVXXXXXXXXDRMVPISKQPKEKIQAIIESCSRQFPEFQERARKRIRTYLKSCRRMKKNGMEMTRPTPPHLTSAMAENILAAACESETRKAAKRMRLEIYQSSQDEPIALDKQHSRDSAAITHSTYSLPASSYSQDPVYANGGLNYSYRGYGALSSNLQPPASLQTGNHSNGPTDLSMKGGASTXSXXPXPTPSSTSTSRPVPTAQLSPTEISAVRQLIXXXXXXXXXXXXXXXXXXXLILQQN
>NRIP1_HUMAN__P48552 RecName: Full=Nuclear receptor-interacting protein 1; AltName: Full=Nuclear factor RIP140; AltName: Full=Receptor-interacting protein 140;
XTHGEELGSDVHQDSIXLTYXEGLLMHQAAGGSGTAVDKKSAGHNEEDQNFNISGSAFPTCQSNGPVLNTHTYQGSGMLHLKKARLLQSSEDWNAAKRKRLSDSIMNLNXXKEXXLAGMVDSVPKGKQDSTLLASLLXXXXXXXXXVXXSQQIXXXXKEQGYALSHDSLKXXKDLRCYXVASSHLKTLLKKSKVKDQKPDTNLPDVTKNLIRDRFAESPHHVGQSGTKVMSEPLSCAARLQAVASMVEKRASPATSPKPSVACSQLALLXXSEAHLQQYSREHALKTQNANQAASERLAAMARLQENGQKDVGSYQLPKGMSSHLNGQARTSSSKLMASKSSATVFQNPMGIIPSSPKNAGYKNSLERNNIKQAANNSLXXHXLKSQTIPKPMNGHSHSERGSIFEESSTPTTIDEYSDNNPSFTDDSSGDESSYSNCVPIDLSCKHRTEKSESDQPVSLDNFTQSLLNTWDPKVPDVDIKEDQDTSKNSKLNSHQKVTLXQXXLGHKNEENVEKNTSPQGVHNDVSKFNTQNYARTSVIESPSTNRTTPVSTPPLLTSSKAGSPINLSQHSLVIKWNSPPYVCSTQSEKLTNTASNHSMDLTKSKDPPGEKPAQNEGAQNSATFSASKLLQNLAQCGMQSSMSVEEQRPSKQLLTGNTDKPIGMIDRLNSPLLSNKTNAVEENKAFSSQPTGPEPGLSGSEIENLLERRTVLQLLLGNPNKGKSEKKEKTPLRDESTQEHSERALSEQILMVKIKSEPCDDLQIPNTNVHLSHDAKSAPFLGMAPAVQRSAPALPVSEDFKSEPVSPQDFSFSKNGLLSRLLRQNQDSYLADDSDRSHRNNEMALLESKNLCMVPKKRKLYTEPLENPFKKMKNNIVDAANNHSAPEVLYGSLLNQEELKFSRNDLEFKYPAGHGSASESEHRSWARESKSFNVLKQLLLSENCVRDLSPHRSNSVADSKKKGHKNNVTNSKPEFSISSLNGLMYSSTQPSSCMDNRTFSYPGVVKTPVSPTFPEHLGCAGSRPESGLLNGCSMPSEKGPIKWVITDAEKNEYEKDSPRLTKTNPILYYMLQKGGNSVTSRETQDKDIWREASSAESVSQVTAKEELLPTAETKASFFNLRSPYNSHMGNNASRPHSANGEVYGLLGSVLTIKKESE
>RBBP5_HUMAN__Q15291 RecName: Full=Retinoblastoma-binding protein 5; Short=RBBP-5; AltName: Full=Retinoblastoma-binding protein RBQ-3;
XNLELLESFGQNYPXEAXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXSTXXXXXQWDVLXXXCDXXXXXPSPILKVQYHPRDXNKVLVCPXXXXXXXXXLXDSKHVVLPVDDXXXXNVVXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXSFRVXXXXXXXXAIKSXXXXXXXXXXXXXXXXXXXXXXXXXXILTCGRDGEPEPMQKLQDLVNRTPWKKXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXWXAFAPDFKELDENVEYXXRXSEFDIEDEDKSEPEQTGADAAEDEEVDVTSVDPIAAFCSSDEELEDSKALLYLPIAPEVEDPEENPYGPPPDAVQTSLMDEGASSEKKRQSSADGSQPPKKKPKTTNIELQGVPNDEVHPLLGVKGDGKSKKKQAGRPKGSKGKEKDSPFKPKLYKGDRGLPLEGSAKGKVQAELSQPLTAGGAISELL
>SOBP_HUMAN__A7XYQ1 RecName: Full=Sine oculis-binding protein homolog; AltName: Full=Jackson circler protein 1;
XXEMEKEGRPPENKRSRKPAHPVKREINEEMKNFAENTMNELLXWYGYDKVXXKXGEDIEFRSYPTDGESRQHISVLKENSLPKPKLPEDSVISPYNISTGYSGLATGNGLSDSPAGSKDHGSVPIIVPLIPXXFIKXPAEDDXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXRNKARDEDGHAENFPQQHYAKETPRXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXAGLCSTLHPPMENKAEGTGVQLLTPDSWNIPLTDARRKAPSPVATAGQSQGPGPSASTTVSPSDTANCSVTKIPTPVPKSIPISETPNIPPVSVQPPASIGPPLGVPPRSPPMVMTNRGPVPLPIFMEQQIMQQIRPPFIRGPPHHASNPNSPLSNPMLPGIGPPPGGPRNLGPTSSPMHRPMLSPHIHPPSTPTMPGNPXGLLXXXXXGAXLPSLPFPPVSMMPNGPMPVPQMMXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXPIPHVSDSKPPNGFSSNGENFIPNAPGDSAAAGGKPSGHSLSPRDSKQGSSKSADSPPGCSGQALSLAPTPAEHGRSEVVDLTRRAGSPPGPPGAGGQLGFPGVLQGPQDGVIDLTVGHRARLHNVIHRALHAHVKAEREPSAAERRTCGGCRDGHCSPPAAGDPGPGAPAGPEXXXACNVIVNGTRGAAAEGAKSAEPXXEQXXXXXXXAXPKKLLSPEEPAVSELESVKENNCASNCHLDGEAAKKLMGEEALAGGDKSDPNLNNPADEDHAYALRMLPKTGCVIQPVPKPAXKAAMAPCIISSPMLSAGPEDLEPPLKRRCLRIRNQNK
>ZN219_HUMAN__Q9P2Y4 RecName: Full=Zinc finger protein 219;
XEGSRPRAPSGHLAPSPPAFDGELDLQRYSNGPAVSAGSLGMGAVSWSESRAXXRRXPXXXXXXXXXXXXXXXXXXXXXXXXXAFQCPHCGHRAAQRALLRSHLRTHQPERPRSPAARLLLELEERALLREARLGRARSSGGMQATPATEGLARPQAPSSSAFRCPYCKGKFXTXAXRERHXHXXXXXXXXXXXXXXXXQEEELLHHSLTAHGAPERPLAATSAAPXXQXQXQXXXQXEPRSVPQPEPEPEPEREATPTPAPAAPEEXXAXPEFRCQVCGQSFXXXWFLKGHXRXXXXXXXXXXXXXXXXXXXXXXXKXXMKVHASKLGPLRAPGPASGPARAPQPPDLGLLAYEPLGPALLLAPAPTPAERREPPSLLGYLSLRAGEGRPNGEGAEPGPGRSFGGFRPLSSALPARARRHRAEXPXXXXXVVXAXXETWARGRSLGSLASLHPRPGEGPGHSASXXGXQARSTATQEENGLLVGGTRPEGGRGATGKDCPFCGKSFXSXHHLKVHLRVHTGERPYKCPHCDYAGTQSGSLKYHLQRHHREQRSGAGPGXXXEXXXPSQRGSAPQSGAKPSPQPATWVEGASSPRPPSSGAGPGSRRKPASPGRTLRNGRGGEAEPLDLSLRAGPGXEAXPXGXXXXXXXXXXXXXXXXXMALHLQVHHSRXAXGXRPPQADASPPYARVPSGETPPSPSQEGEEGSGLSRPGEAGLGGQER
>ATX1L_HUMAN__P0C7T5-qslimfinder Motifs
--------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------PLDL-----------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------
>ATX1L_HUMAN__P0C7T5-masked
XKPVHERSQECLPPKKRDLPVTSEDMGRTTSCSTNHTPSSDASEWSRGVVVAGQSQAGARVSLGGDGAEAITXXXXXXXXXXXXXXVXXAXXXPTGLPSVVNMSPLXXXXNVASSLIQHXXIXYPPLHYAXXXSTXXXXXXXPXXXXXXXXXXXXXXXLLSPSANLATXHLPXFVPYASLLAEGATPXXQAXSPAHSFNKAPSATSPSGQLPHHSSTQPLDLAPGRMPIYYQMSRLPAGYTLHETPPAGASPVLTPQESQSALEXXXANGGQRPRERNLVRRESEALDSPNSKGEGQGLVPXXECXVDGQLFSGSQTPRVEVAAPAHRGTPDTDLEVQRVVGALASQDYRVVAAQRKEEPSPLNLSHHTPDHQGEGRGSARNPAELAEKSQARGFYPQSHQEPVKHRPLPKAMVVANGNLVPTGTDSGLLPVGSEILVASSLDVQARATFPDKEPTPPPITSSHLPSHFMKGAIIQLATGELKRVEDLQTQDFVRSAEVSGXXXIDSSTVVDXQXSXXXXXXXLHXXXXXXXSKVSIEVPPEXXXXXYGQGWSXXXXGXXXXXXXLXXXXXXXXXXXXXXXXXSLXXNSVSQASCAPPSQLGPPRERPERTVLGSRELCDSEGKSQPAGEGSRVVEPSQPESGAQACWPAPSFQRYSMQGEEARAALLRPSFIPQEVKLSIEGRSNAGK
>ATX1L_HUMAN__P0C7T5 RecName: Full=Ataxin-1-like; AltName: Full=Brother of ataxin-1; Short=Brother of ATXN1;
MKPVHERSQECLPPKKRDLPVTSEDMGRTTSCSTNHTPSSDASEWSRGVVVAGQSQAGARVSLGGDGAEAITGLTVDQYGMLYKVAVPPATFSPTGLPSVVNMSPLPPTFNVASSLIQHPGIHYPPLHYAQLPSTSLQFIGSPYSLPYAVPPNFLPSPLLSPSANLATSHLPHFVPYASLLAEGATPPPQAPSPAHSFNKAPSATSPSGQLPHHSSTQPLDLAPGRMPIYYQMSRLPAGYTLHETPPAGASPVLTPQESQSALEAAAANGGQRPRERNLVRRESEALDSPNSKGEGQGLVPVVECVVDGQLFSGSQTPRVEVAAPAHRGTPDTDLEVQRVVGALASQDYRVVAAQRKEEPSPLNLSHHTPDHQGEGRGSARNPAELAEKSQARGFYPQSHQEPVKHRPLPKAMVVANGNLVPTGTDSGLLPVGSEILVASSLDVQARATFPDKEPTPPPITSSHLPSHFMKGAIIQLATGELKRVEDLQTQDFVRSAEVSGGLKIDSSTVVDIQESQWPGFVMLHFVVGEQQSKVSIEVPPEHPFFVYGQGWSSCSPGRTTQLFSLPCHRLQVGDVCISISLQSLNSNSVSQASCAPPSQLGPPRERPERTVLGSRELCDSEGKSQPAGEGSRVVEPSQPESGAQACWPAPSFQRYSMQGEEARAALLRPSFIPQEVKLSIEGRSNAGK
>BRCA1_HUMAN__P38398-qslimfinder Motifs
-------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------P-DLT---------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------
>BRCA1_HUMAN__P38398-masked
XDLSALRXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXLXXXXXXXXSXXESTXFXXXXXXXXXXXXXXXXXXXXXXXXSYNFAKKENNSPEHLKDEVSIIQSMGYRNRAKRLLQSEPENPSLQETSLSVQLSNLGTVRTLRTKQRIQPQKTSVYIELGSDSSEDTVNKATYCSVGDQELLQITPQGTRDEISLDSAKKAACEFSETDVTNTEHHQPSNNDLNTTEKRAAERHPEKYQGSSVSNLHVEPCGTNTHASSLQHENSSLLLTKDRMNVEKAEFCNKSKQPGLARSQHNRWAGSKETCNDRRTPSTEKKVDLNADPLCERKEWNKQKLPCSENPRDTEDVPWITLNSSIQKVNEWFSRSDELLGSDDSHDGESESNAKVADVLDVLNEVDEYSGSSEKIDLLASDPHEALICKSERVHSKSVESNIEDKIFGKTYRKKASLPNXXHXXXXXIXXXFVTEPQIIQERPLTNKLKRKRRPTSGLHPEDFIKKADLAVQKTPEMINQGTNQTEQNGQVMNITNSGHENKTKGDSIQNEKNPNPIESLEKESAFKTKAEPISSSISNMELELNIHNSKAPKKNRLRRKSSTRHIHALELVVSRNLSPPNCTELQIDSCSSSEEIKKKKYNQMPVRHSRNLQLMEGKEPATGAKKSNKPNEQTSKRHDSDTFPELKLTNAPGSFTKCSNTSELKEFVNPSLPREXKXXKLETVKVSNNAEDPKDLMLSGERVLQTERSVEXXXISLVPGTDYGTQESISLLEVSTLGKAKTEPXKCVSQCAAFXXXKGLIHGCSKDNRNDTEGFKYPLGHEVNHSRETSIEMEESELDAQYLQNTFKVSKRQSFAPFSNPGNAEEECATFSAHSGSLKKQSPKVTFECEQKEENQGKNESNIKPVQTVNITAGFPVVGQKDKPVDNAKCSIKGXSRFCLSSQFRGNETGLITPNKHGLLQNPYRIPPLFPIKSFVKTKCKKNLLEENFEEHSMSPEREMGNENIPSTVSTISRNNIRENVFKEASSSNINEVGSSTNEVGSSINEIGSSDENIQAELGRNRGPKLNAMLRLGVLQPEVYKQSLPGSNCKHPEIKKQEYEEVVQTVNTDFSPYLISDNLEQPMGSSHASQVCSETPDDLLDDGEIKEDTSFAENDIKESSAVFSKSVQKGELSRSPSPFTHTHLAQGYRRGAKKLESSEENLSSEDEELPCFQHLLFGKVNNIPSQSTRHSTVATECLSKNTEENLXSLKNSXXXXXNQVILAKASQEHHLSEETKCSASLFSSQCSELEDLTANTNTQDPFLIGSSKQMRHQSESQGVGLSDKELVSDDEERGTGLEENNQEEQSMDSNLGEAASGCESETSVSEDCSGLSSQSDILTTQQRDTMQHNLIKLQQEMAELEAVLEQHGSQPSNSYPSIISDSSALEDLRNPEQSTSEKAVLTSQKSSEYPISQNPEGLSADKFEVSADSSTSKNKEPGVERSSPSKCPSLDDRWYMHSCSGSLQNRNYPSQEELIKVVDVEEQQLEESGPHDLTETSYLPRQDLEGTPYLESGISLFSDDPESDPSEDRAPESARVGNIPSSTSALKVPQLKVAESAQSPAAAHTTDTAGYNAMEESVSREKPELTASTERVNKRMSMVVSXXXXXXXXXXXXXXXXXXXXXTXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXLNEHDFEVRGDVVNGRNHQGPKRARESQDRKXXRXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXVVQPDXXXXXXGFHXXXQMXXXXXXXXXXXXXXXXXXXXXXXXXXXXPQIPHSHY
>BRCA1_HUMAN__P38398 RecName: Full=Breast cancer type 1 susceptibility protein; EC=6.3.2.-; AltName: Full=RING finger protein 53;
MDLSALRVEEVQNVINAMQKILECPICLELIKEPVSTKCDHIFCKFCMLKLLNQKKGPSQCPLCKNDITKRSLQESTRFSQLVEELLKIICAFQLDTGLEYANSYNFAKKENNSPEHLKDEVSIIQSMGYRNRAKRLLQSEPENPSLQETSLSVQLSNLGTVRTLRTKQRIQPQKTSVYIELGSDSSEDTVNKATYCSVGDQELLQITPQGTRDEISLDSAKKAACEFSETDVTNTEHHQPSNNDLNTTEKRAAERHPEKYQGSSVSNLHVEPCGTNTHASSLQHENSSLLLTKDRMNVEKAEFCNKSKQPGLARSQHNRWAGSKETCNDRRTPSTEKKVDLNADPLCERKEWNKQKLPCSENPRDTEDVPWITLNSSIQKVNEWFSRSDELLGSDDSHDGESESNAKVADVLDVLNEVDEYSGSSEKIDLLASDPHEALICKSERVHSKSVESNIEDKIFGKTYRKKASLPNLSHVTENLIIGAFVTEPQIIQERPLTNKLKRKRRPTSGLHPEDFIKKADLAVQKTPEMINQGTNQTEQNGQVMNITNSGHENKTKGDSIQNEKNPNPIESLEKESAFKTKAEPISSSISNMELELNIHNSKAPKKNRLRRKSSTRHIHALELVVSRNLSPPNCTELQIDSCSSSEEIKKKKYNQMPVRHSRNLQLMEGKEPATGAKKSNKPNEQTSKRHDSDTFPELKLTNAPGSFTKCSNTSELKEFVNPSLPREEKEEKLETVKVSNNAEDPKDLMLSGERVLQTERSVESSSISLVPGTDYGTQESISLLEVSTLGKAKTEPNKCVSQCAAFENPKGLIHGCSKDNRNDTEGFKYPLGHEVNHSRETSIEMEESELDAQYLQNTFKVSKRQSFAPFSNPGNAEEECATFSAHSGSLKKQSPKVTFECEQKEENQGKNESNIKPVQTVNITAGFPVVGQKDKPVDNAKCSIKGGSRFCLSSQFRGNETGLITPNKHGLLQNPYRIPPLFPIKSFVKTKCKKNLLEENFEEHSMSPEREMGNENIPSTVSTISRNNIRENVFKEASSSNINEVGSSTNEVGSSINEIGSSDENIQAELGRNRGPKLNAMLRLGVLQPEVYKQSLPGSNCKHPEIKKQEYEEVVQTVNTDFSPYLISDNLEQPMGSSHASQVCSETPDDLLDDGEIKEDTSFAENDIKESSAVFSKSVQKGELSRSPSPFTHTHLAQGYRRGAKKLESSEENLSSEDEELPCFQHLLFGKVNNIPSQSTRHSTVATECLSKNTEENLLSLKNSLNDCSNQVILAKASQEHHLSEETKCSASLFSSQCSELEDLTANTNTQDPFLIGSSKQMRHQSESQGVGLSDKELVSDDEERGTGLEENNQEEQSMDSNLGEAASGCESETSVSEDCSGLSSQSDILTTQQRDTMQHNLIKLQQEMAELEAVLEQHGSQPSNSYPSIISDSSALEDLRNPEQSTSEKAVLTSQKSSEYPISQNPEGLSADKFEVSADSSTSKNKEPGVERSSPSKCPSLDDRWYMHSCSGSLQNRNYPSQEELIKVVDVEEQQLEESGPHDLTETSYLPRQDLEGTPYLESGISLFSDDPESDPSEDRAPESARVGNIPSSTSALKVPQLKVAESAQSPAAAHTTDTAGYNAMEESVSREKPELTASTERVNKRMSMVVSGLTPEEFMLVYKFARKHHITLTNLITEETTHVVMKTDAEFVCERTLKYFLGIAGGKWVVSYFWVTQSIKERKMLNEHDFEVRGDVVNGRNHQGPKRARESQDRKIFRGLEICCYGPFTNMPTDQLEWMVQLCGASVVKELSSFTLGTGVHPIVVVQPDAWTEDNGFHAIGQMCEAPVVTREWVLDSVALYQCQELDTYLIPQIPHSHY
>CBX4_HUMAN__O00257-qslimfinder Motifs
---------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------PIDL-------------------------------------------------------------------------------------
>CBX4_HUMAN__O00257-masked
XELPAVGEHXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXTWEPEENXXDPRLLIAFQNRERQEQLMGYRKRGPKPKPLVVQVPTFARRSNVLTGLQDSSTDNRAKLDLGAQGKGQGHQYELNSKKHHQYQPHSKERAGKPPPPGKSGKYYYQLNSKKHHPYQPDPKMYDLQYQGGHKEAPSPTCPDLGAKSHPPDKWAQGAGAKGYLGAVKPLAGAAGAPGKGSEKGPPNGMMPAPKEAVTGNGIGGKMKIVKNKNKNGRIVIVMSKYMENGMQAVKIKSGEVAEGEARSPSHKKRAADERHPPADRTFKKAAGAEEKKVEAPPKRREEEVSGVSDPQPQDAGSRKLSPTKEAFGEQPLQLTTKPDLLAWDPARNTHPPSHXPXPXPXXXXXXXXXXXHAVGLNLSHVRKRCLSETHGEREPCKKRLTARSISTPTCLGGSPAAERPADLPPAAALPQPEVILLDSDLDEPIDLRCVKTRSEAGEPPSSLQVKPETPASXXVXVXXXXAPTTTAEKPPAEAQDEPAESLSEFKPXXXXXXXXXXXXXXXXXXXXXYVTV
>CBX4_HUMAN__O00257 RecName: Full=E3 SUMO-protein ligase CBX4; EC=6.3.2.-; AltName: Full=Chromobox protein homolog 4; AltName: Full=Polycomb 2 homolog; Short=Pc2; Short=hPc2;
MELPAVGEHVFAVESIEKKRIRKGRVEYLVKWRGWSPKYNTWEPEENILDPRLLIAFQNRERQEQLMGYRKRGPKPKPLVVQVPTFARRSNVLTGLQDSSTDNRAKLDLGAQGKGQGHQYELNSKKHHQYQPHSKERAGKPPPPGKSGKYYYQLNSKKHHPYQPDPKMYDLQYQGGHKEAPSPTCPDLGAKSHPPDKWAQGAGAKGYLGAVKPLAGAAGAPGKGSEKGPPNGMMPAPKEAVTGNGIGGKMKIVKNKNKNGRIVIVMSKYMENGMQAVKIKSGEVAEGEARSPSHKKRAADERHPPADRTFKKAAGAEEKKVEAPPKRREEEVSGVSDPQPQDAGSRKLSPTKEAFGEQPLQLTTKPDLLAWDPARNTHPPSHHPHPHPHHHHHHHHHHHHAVGLNLSHVRKRCLSETHGEREPCKKRLTARSISTPTCLGGSPAAERPADLPPAAALPQPEVILLDSDLDEPIDLRCVKTRSEAGEPPSSLQVKPETPASAAVAVAAAAAPTTTAEKPPAEAQDEPAESLSEFKPFFGNIIITDVTANCLTVTFKEYVTV
>CHD3_HUMAN__Q12873-qslimfinder Motifs
--------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------
>CHD3_HUMAN__Q12873-masked
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
>CHD3_HUMAN__Q12873 RecName: Full=Chromodomain-helicase-DNA-binding protein 3; Short=CHD-3; EC=3.6.4.12; AltName: Full=ATP-dependent helicase CHD3; AltName: Full=Mi-2 autoantigen 240 kDa protein; AltName: Full=Mi2-alpha; AltName: Full=Zinc finger helicase; Short=hZFH;
MKAADTVILWARSKNDQLRISFPPGLCWGDRMPDKDDIRLLPSALGVKKRKRGPKKQKENKPGKPRKRKKRDSEEEFGSERDEYREKSESGGSEYGTGPGRKRRRKHREKKEKKTKRRKKGEGDGGQKQVEQKSSATLLLTWGLEDVEHVFSEEDYHTLTNYKAFSQFMRPLIAKKNPKIPMSKMMTILGAKWREFSANNPFKGSAAAVAAAAAAAAAAVAEQVSAAVSSATPIAPSGPPALPPPPAADIQPPPIRRAKTKEGKGPGHKRRSKSPRVPDGRKKLRGKKMAPLKIKLGLLGGKRKKGGSYVFQSDEGPEPEAEESDLDSGSVHSASGRPDGPVRTKKLKRGRPGRKKKKVLGCPAVAGEEEVDGYETDHQDYCEVCQQGGEIILCDTCPRAYHLVCLDPELDRAPEGKWSCPHCEKEGVQWEAKEEEEEYEEEGEEEGEKEEEDDHMEYCRVCKDGGELLCCDACISSYHIHCLNPPLPDIPNGEWLCPRCTCPVLKGRVQKILHWRWGEPPVAVPAPQQADGNPDVPPPRPLQGRSEREFFVKWVGLSYWHCSWAKELQLEIFHLVMYRNYQRKNDMDEPPPLDYGSGEDDGKSDKRKVKDPHYAEMEEKYYRFGIKPEWMTVHRIINHSVDKKGNYHYLVKWRDLPYDQSTWEEDEMNIPEYEEHKQSYWRHRELIMGEDPAQPRKYKKKKKELQGDGPPSSPTNDPTVKYETQPRFITATGGTLHMYQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLYSLYKEGHTKGPFLVSAPLSTIINWEREFQMWAPKFYVVTYTGDKDSRAIIRENEFSFEDNAIKGGKKAFKMKREAQVKFHVLLTSYELITIDQAALGSIRWACLVVDEAHRLKNNQSKFFRVLNGYKIDHKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEFADISKEDQIKKLHDLLGPHMLRRLKADVFKNMPAKTELIVRVELSPMQKKYYKYILTRNFEALNSRGGGNQVSLLNIMMDLKKCCNHPYLFPVAAMESPKLPSGAYEGGALIKSSGKLMLLQKMLRKLKEQGHRVLIFSQMTKMLDLLEDFLDYEGYKYERIDGGITGALRQEAIDRFNAPGAQQFCFLLSTRAGGLGINLATADTVIIFDSDWNPHNDIQAFSRAHRIGQANKVMIYRFVTRASVEERITQVAKRKMMLTHLVVRPGLGSKAGSMSKQELDDILKFGTEELFKDENEGENKEEDSSVIHYDNEAIARLLDRNQDATEDTDVQNMNEYLSSFKVAQYVVREEDKIEEIEREIIKQEENVDPDYWEKLLRHHYEQQQEDLARNLGKGKRVRKQVNYNDAAQEDQDNQSEYSVGSEEEDEDFDERPEGRRQSKRQLRNEKDKPLPPLLARVGGNIEVLGFNTRQRKAFLNAVMRWGMPPQDAFTTQWLVRDLRGKTEKEFKAYVSLFMRHLCEPGADGSETFADGVPREGLSRQQVLTRIGVMSLVKKKVQEFEHINGRWSMPELMPDPSADSKRSSRASSPTKTSPTTPEASATNSPCTSKPATPAPSEKGEGIRTPLEKEEAENQEEKPEKNSRIGEKMETEADAPSPAPSLGERLEPRKIPLEDEVPGVPGEMEPEPGYRGDREKSATESTPGERGEEKPLDGQEHRERPEGETGDLGKREDVKGDRELRPGPRDEPRSNGRREEKTEKPRFMFNIADGGFTELHTLWQNEERAAISSGKLNEIWHRRHDYWLLAGIVLHGYARWQDIQNDAQFAIINEPFKTEANKGNFLEMKNKFLARRFKLLEQALVIEEQLRRAAYLNLSQEPAHPAMALHARFAEAECLAESHQHLSKESLAGNKPANAVLHKVLNQLEELLSDMKADVTRLPATLSRIPPIAARLQMSERSILSRLASKGTEPHPTPAYPPGPYATPPGYGAAFSAAPVGALAAAGANYSQMPAGSFITAATNGPPVLVKKEKEMVGALVSDGLDRKEPRAGEVICIDD
>COM1_HUMAN__Q99708-qslimfinder Motifs
---------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------PLDLS-R-----------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------
>COM1_HUMAN__Q99708-masked
XNISGSSCGSPNSADTSSDFKDLWTKLKECHDXEVQGLQVKVTXXKXXRXXXXXRLXXFXTKNQQLREQQKVLHXXIKXXXXXXXXXXXXRCAVTEEHMRKKQQEFENIRQQNLKLITELMNERNTLQEENKKLSEQLQQKIENDQQHQAAELECEEDVIPDSPITAFSFSGVNRLRRKENPHVRYIEQTHTKLEHSVCANEMRKVSKSSTHPQHNPNENEILVADTYDQSQSPMAKAHGTSSYTPDKSSFNLATVVAETLGLGVQEESETQGPMSPLGDELYHCLEGNHKKQPFEESTRNTEDSLRFSDSTSKTPPQEELPTRVSSPVFGATSSIKSGLDLNTSLSPSLLQPGKKKHLKTLPFSNTCISRLEKTRSKSEDSALFTHHSXGSEVNKIIIQSSNKQILINKNISESLGEQNRTEYGKDSNTDKHLEPLKSLGGRTSKRKKTEXXSXHEVSCPQASFDKENAFPFPMDNQFSMNGDCVMDKPLDLSDRFSAIQRQEKSQGSETSKNKFRQVTLYEALKTIPKGFSSSRKASDGNCTLPKDSPGEPCSQECIILQPLNKCSPDNKPSLQIKEENAVFKIPLRPRESLETENVLDDIKSAGSHEPIKIQTRSDHGGCELASVLQLNXCRTGKIKSLQNNQDVSFENIQWSIDPGADLSQYKMDVTVIDTKDGSQSKLGGETVDMDCTLVSETVLLKMKKQEQKGEKSSNEERKMNDSLEDMFDRTTHEEYESCLADSFSQAADEEEELSTATKKLHTHGDKQDKVKQKAFVEPYFKGDERETSLQNFPHIEVVRKKEERRXXXXXXXXXXXXXYAXXPAXEREKKLASCSRHRFRYIPXNTPENFWEVGFPSTQTCMERGYIKEDLDPCPRPKRRQPYNAIFSPKGKEQKT
>COM1_HUMAN__Q99708 RecName: Full=DNA endonuclease RBBP8; EC=3.1.-.-; AltName: Full=CtBP-interacting protein; Short=CtIP; AltName: Full=Retinoblastoma-binding protein 8; Short=RBBP-8; AltName: Full=Retinoblastoma-interacting protein and myosin-like; Short=RIM; AltName: Full=Sporulation in the absence of SPO11 protein 2 homolog; Short=SAE2;
MNISGSSCGSPNSADTSSDFKDLWTKLKECHDREVQGLQVKVTKLKQERILDAQRLEEFFTKNQQLREQQKVLHETIKVLEDRLRAGLCDRCAVTEEHMRKKQQEFENIRQQNLKLITELMNERNTLQEENKKLSEQLQQKIENDQQHQAAELECEEDVIPDSPITAFSFSGVNRLRRKENPHVRYIEQTHTKLEHSVCANEMRKVSKSSTHPQHNPNENEILVADTYDQSQSPMAKAHGTSSYTPDKSSFNLATVVAETLGLGVQEESETQGPMSPLGDELYHCLEGNHKKQPFEESTRNTEDSLRFSDSTSKTPPQEELPTRVSSPVFGATSSIKSGLDLNTSLSPSLLQPGKKKHLKTLPFSNTCISRLEKTRSKSEDSALFTHHSLGSEVNKIIIQSSNKQILINKNISESLGEQNRTEYGKDSNTDKHLEPLKSLGGRTSKRKKTEEESEHEVSCPQASFDKENAFPFPMDNQFSMNGDCVMDKPLDLSDRFSAIQRQEKSQGSETSKNKFRQVTLYEALKTIPKGFSSSRKASDGNCTLPKDSPGEPCSQECIILQPLNKCSPDNKPSLQIKEENAVFKIPLRPRESLETENVLDDIKSAGSHEPIKIQTRSDHGGCELASVLQLNPCRTGKIKSLQNNQDVSFENIQWSIDPGADLSQYKMDVTVIDTKDGSQSKLGGETVDMDCTLVSETVLLKMKKQEQKGEKSSNEERKMNDSLEDMFDRTTHEEYESCLADSFSQAADEEEELSTATKKLHTHGDKQDKVKQKAFVEPYFKGDERETSLQNFPHIEVVRKKEERRKLLGHTCKECEIYYADMPAEEREKKLASCSRHRFRYIPPNTPENFWEVGFPSTQTCMERGYIKEDLDPCPRPKRRQPYNAIFSPKGKEQKT
>CTBP1_HUMAN__Q13363-qslimfinder Motifs
--------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------
>CTBP1_HUMAN__Q13363-masked
XGSSHLLNKGLPLGVRPPIMNGPLHPRPXVALLDGXXXXXXXXXXXXXXXXXXXXXXXXXXXXEKXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXREXXXVQSVEQIREVASGAXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXNDFXXXXXXXGAXXXNTAXXXXXXEKALAQALKEGRIRGAALDVHESEPFSFSQGPLKDAPNLICTPHAAWYSEQASIEMREEAAREIRRAITGRIPDSLKNCVNKDHLTAATHWASMDPAVVHXELNGAXXXYPPXVXXXXPXGIPAAVEGIVPSAMSLSHGLPPVAHPPHAPSPGQTVKPEADRDHASDQL
>CTBP1_HUMAN__Q13363 RecName: Full=C-terminal-binding protein 1; Short=CtBP1; EC=1.1.1.-;
MGSSHLLNKGLPLGVRPPIMNGPLHPRPLVALLDGRDCTVEMPILKDVATVAFCDAQSTQEIHEKVLNEAVGALMYHTITLTREDLEKFKALRIIVRIGSGFDNIDIKSAGDLGIAVCNVPAASVEETADSTLCHILNLYRRATWLHQALREGTRVQSVEQIREVASGAARIRGETLGIIGLGRVGQAVALRAKAFGFNVLFYDPYLSDGVERALGLQRVSTLQDLLFHSDCVTLHCGLNEHNHHLINDFTVKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHESEPFSFSQGPLKDAPNLICTPHAAWYSEQASIEMREEAAREIRRAITGRIPDSLKNCVNKDHLTAATHWASMDPAVVHPELNGAAYRYPPGVVGVAPTGIPAAVEGIVPSAMSLSHGLPPVAHPPHAPSPGQTVKPEADRDHASDQL
>CTNA1_HUMAN__P35221-qslimfinder Motifs
------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------
>CTNA1_HUMAN__P35221-masked
XTAVHAGNINXXXXXXXXXXXXXXXXXXLXXXXTQVTTLVNTNSKGPSNKKRGRSKKAHVLAASVEQATENFLEKGDKIAKESQFLKXXLVAAVEDVRKQGDLMKAAAGEFADDPCSSVKRGXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXLGIQYKALXXXVDKLNIMAAKRQQELKDVGHRDQMAAARGIXXXXXXXXXXXXXXXXXXXDVXXXXXNRXXXXXXLQQAXXXISNAAQATASDDASQHQGXXXGELAYALNNFDXXXIVDPLSFSEERFRPSLEERLESIISGAALMADSSCTRDDRRERIVAECNXVRXXLQDLLSEYMGNAGRKERSDALNSAIDKMTKKTRDLRRQLRKAVMDHVSXXXXXXXXXXXXXXEXXXXXNEXEVKEYAQVFXXXXXXXXXXXXXXXXXXXXXXXXXLXRXXXXXXXXXXXXXXXXXXXXXXXXQSXXAQENMDLFKXQWEXXVXXLXXXXXXXXXXDXXXXXXXXXXXXXXXXXXXXXXXXXXXXLDRTAGXXXXXAAXVIXVVTSXMDNYEPGVYTEKVLEATKLLSNTVMPRFTEQVEAAVEALSSDPAQPMDENEFIDASRLXXXXXXXXXXAVLMIRTPEELDDSDFETEDFDVRSRTSVQTEDDQLIAGQSARAIMAQLPQEQKAKIAEQVASFQEEKSKLDAEVSKWDDSGNDIIVXAKQMXXXXMEMTDFTRGKGPLKNTSDVISAAKKIAEAGSRMDKLGRTIADHXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXTKXQKSQGMASLNLPAVSWKMKAPEKKPLVKREKQDETQTKIKRASQKKHVNPVQALSEFKAMDSI
>CTNA1_HUMAN__P35221 RecName: Full=Catenin alpha-1; AltName: Full=Alpha E-catenin; AltName: Full=Cadherin-associated protein; AltName: Full=Renal carcinoma antigen NY-REN-13;
MTAVHAGNINFKWDPKSLEIRTLAVERLLEPLVTQVTTLVNTNSKGPSNKKRGRSKKAHVLAASVEQATENFLEKGDKIAKESQFLKEELVAAVEDVRKQGDLMKAAAGEFADDPCSSVKRGNMVRAARALLSAVTRLLILADMADVYKLLVQLKVVEDGILKLRNAGNEQDLGIQYKALKPEVDKLNIMAAKRQQELKDVGHRDQMAAARGILQKNVPILYTASQACLQHPDVAAYKANRDLIYKQLQQAVTGISNAAQATASDDASQHQGGGGGELAYALNNFDKQIIVDPLSFSEERFRPSLEERLESIISGAALMADSSCTRDDRRERIVAECNAVRQALQDLLSEYMGNAGRKERSDALNSAIDKMTKKTRDLRRQLRKAVMDHVSDSFLETNVPLLVLIEAAKNGNEKEVKEYAQVFREHANKLIEVANLACSISNNEEGVKLVRMSASQLEALCPQVINAALALAAKPQSKLAQENMDLFKEQWEKQVRVLTDAVDDITSIDDFLAVSENHILEDVNKCVIALQEKDVDGLDRTAGAIRGRAARVIHVVTSEMDNYEPGVYTEKVLEATKLLSNTVMPRFTEQVEAAVEALSSDPAQPMDENEFIDASRLVYDGIRDIRKAVLMIRTPEELDDSDFETEDFDVRSRTSVQTEDDQLIAGQSARAIMAQLPQEQKAKIAEQVASFQEEKSKLDAEVSKWDDSGNDIIVLAKQMCMIMMEMTDFTRGKGPLKNTSDVISAAKKIAEAGSRMDKLGRTIADHCPDSACKQDLLAYLQRIALYCHQLNICSKVKAEVQNLGGELVVSGVDSAMSLIQAAKNLMNAVVQTVKASYVASTKYQKSQGMASLNLPAVSWKMKAPEKKPLVKREKQDETQTKIKRASQKKHVNPVQALSEFKAMDSI
>E1A_ADE02__P03254-qslimfinder Motifs
--------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------PLDLS-K----
>E1A_ADE02__P03254-masked
XRHIICHGGXXXXXXXASXXXQXIEEVLADNLPPPSHFEPPTLHELYDLDVTAPEDPNEEAVSQIFPDSVMLAVQEGIDLLTFPPAPGSPEPPHLSRQPEQPEQRALGPVSMPNLVPEVIDLTCHEAGFPPSDDEDXXGXEFVLDYVEXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXSPVSEPEPEPEPEPEPARPTRRPKLVPAILRRPTSPVSRECNSSTDSCDSGPSNTPPEIHPVVPLCPIKPVAVRXXGRRXXXECIEDLLNXXGQPLDLSCKRPRP
>E1A_ADE02__P03254 RecName: Full=Early E1A protein {ECO:0000305}; AltName: Full=Early E1A 32 kDa protein;
MRHIICHGGVITEEMAASLLDQLIEEVLADNLPPPSHFEPPTLHELYDLDVTAPEDPNEEAVSQIFPDSVMLAVQEGIDLLTFPPAPGSPEPPHLSRQPEQPEQRALGPVSMPNLVPEVIDLTCHEAGFPPSDDEDEEGEEFVLDYVEHPGHGCRSCHYHRRNTGDPDIMCSLCYMRTCGMFVYSPVSEPEPEPEPEPEPARPTRRPKLVPAILRRPTSPVSRECNSSTDSCDSGPSNTPPEIHPVVPLCPIKPVAVRVGGRRQAVECIEDLLNESGQPLDLSCKRPRP
>FOG1_HUMAN__Q8IX07-qslimfinder Motifs
-------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------PIDLS-K--------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------
>FOG1_HUMAN__Q8IX07-masked
XSRRKQSNPRQIKRSLGDMEAREEVQLVGASHMEQKATAPEAPSPPSADVNSPXXLXXXTSPGGPKELEGQEPEPRPTEEEPGSPWSGPDELEPVVQDGQRRIRARLSLATGLSWGPFHGSVQTRASSPRQAEPSPALTLXXXXXXXXXXXXPQAXXEAEANTEXHRKDDALWCRVTKPVXXGGLLSVLLTAEPHSTPGHPVKKEPAEPTCPAPAHDLQLLPQQAGXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXGTGSPAAAATDEKPKETYPNERVCPFPQCRKXXXSASSLEIHMRSXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXQPGSKGEIYSPGAGHPATKLPPDSLGSFQQQHTALQGPLASADLGLAPTPSPGLDRKALAEATNGEARAEPLAQNGGSSEPPAAPRSIKVEAVEEPEAAPILGPGEPGPQAPSRTPSPRSPAPARVKAELSSPTPGSSPVPGELGLAXXXFXXXYVFGPDAAPPASEILAKMSELVHSRLQQGAXAXAXGAQTGLFPGXXXXXXXXXXXXXXXXXXXXXXXXXXYCSGRRAPEDAPAARRPKAPPGPARAPPGQPAEPDAPRSSPGPGAREEGAGGAATPEDGAGGRGSEGSQSPGSSVDDAEDDPSRTLCEACNIRFSRHEXXTVHKRYYCASRHDPPPRRPAAXXGXXGXAAXPAPSPAAPVRTXXXRKLYELHAAGAPXXXXXGHAPAPESPRPGSGSGSGPGLAPARSPGPAADGPIDLSKKPRRPLPGAPAPALAXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXLLEXFXXXXXXLLGAPLAGPGVEARTPADRGPSPAPAPAASPQPGSRGPRDGLGPEXQEXXXGXXXSPAAAPEAVXXXXAXPSYSDKGVQTPSKGTPAPLPNGNHXXXXXXXXXXXXXXXXXXXXXXXXXXXAAEHVK
>FOG1_HUMAN__Q8IX07 RecName: Full=Zinc finger protein ZFPM1; AltName: Full=Friend of GATA protein 1; Short=FOG-1; Short=Friend of GATA 1; AltName: Full=Zinc finger protein 89A; AltName: Full=Zinc finger protein multitype 1;
MSRRKQSNPRQIKRSLGDMEAREEVQLVGASHMEQKATAPEAPSPPSADVNSPPPLPPPTSPGGPKELEGQEPEPRPTEEEPGSPWSGPDELEPVVQDGQRRIRARLSLATGLSWGPFHGSVQTRASSPRQAEPSPALTLLLVDEACWLRTLPQALTEAEANTEIHRKDDALWCRVTKPVPAGGLLSVLLTAEPHSTPGHPVKKEPAEPTCPAPAHDLQLLPQQAGMASILATAVINKDVFPCKDCGIWYRSERNLQAHLLYYCASRQGTGSPAAAATDEKPKETYPNERVCPFPQCRKSCPSASSLEIHMRSHSGERPFVCLICLSAFTTKANCERHLKVHTDTLSGVCHSCGFISTTRDILYSHLVTNHMVCQPGSKGEIYSPGAGHPATKLPPDSLGSFQQQHTALQGPLASADLGLAPTPSPGLDRKALAEATNGEARAEPLAQNGGSSEPPAAPRSIKVEAVEEPEAAPILGPGEPGPQAPSRTPSPRSPAPARVKAELSSPTPGSSPVPGELGLAGALFLPQYVFGPDAAPPASEILAKMSELVHSRLQQGAGAGAGGAQTGLFPGAPKGATCFECEITFSNVNNYYVHKRLYCSGRRAPEDAPAARRPKAPPGPARAPPGQPAEPDAPRSSPGPGAREEGAGGAATPEDGAGGRGSEGSQSPGSSVDDAEDDPSRTLCEACNIRFSRHETYTVHKRYYCASRHDPPPRRPAAPPGPPGPAAPPAPSPAAPVRTRRRRKLYELHAAGAPPPPPPGHAPAPESPRPGSGSGSGPGLAPARSPGPAADGPIDLSKKPRRPLPGAPAPALADYHECTACRVSFHSLEAYLAHKKYSCPAAPPPGALGLPAAACPYCPPNGPVRGDLLEHFRLAHGLLLGAPLAGPGVEARTPADRGPSPAPAPAASPQPGSRGPRDGLGPEPQEPPPGPPPSPAAAPEAVPPPPAPPSYSDKGVQTPSKGTPAPLPNGNHRYCRLCNIKFSSLSTFIAHKKYYCSSHAAEHVK
>HDAC2_HUMAN__Q92769-qslimfinder Motifs
--------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------
>HDAC2_HUMAN__Q92769-masked
XXYSQGGXXXXXXXXXXXXXXXXXXGQGXXMKXHRIRMXXXXXXXXXXXXXXXXYRPHKATAEEMTKYHSDEYIKFLRSIRPDNMSEYSKQMQRFNVXXDXXXXXXXXXXXXXXXXXXXXGAVKLNRQXTDMAVNWAGGLHXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXYXXXXXXXXXXXXXXXXXXXXGDLRXXXAXXXXXYXXNFPMRDXXDDEXYGQXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXNXYXXXXXXXFKXHISPSNMTNQNTPEYMEKIKQRLFENLRMLPHAPGVQMQAIPEDAVHEDSGDEDGEDPDKRISIRASDKRIACDEEFSDSEDEGEGGRRNVADHKKGAKKARIEEDKKETEDKKTDVKEEDKSKDNSGEKTDTKGTKSEQLSNP
>HDAC2_HUMAN__Q92769 RecName: Full=Histone deacetylase 2; Short=HD2; EC=3.5.1.98;
MAYSQGGGKKKVCYYYDGDIGNYYYGQGHPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKATAEEMTKYHSDEYIKFLRSIRPDNMSEYSKQMQRFNVGEDCPVFDGLFEFCQLSTGGSVAGAVKLNRQQTDMAVNWAGGLHHAKKSEASGFCYVNDIVLAILELLKYHQRVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKYGEYFPGTGDLRDIGAGKGKYYAVNFPMRDGIDDESYGQIFKPIISKVMEMYQPSAVVLQCGADSLSGDRLGCFNLTVKGHAKCVEVVKTFNLPLLMLGGGGYTIRNVARCWTYETAVALDCEIPNELPYNDYFEYFGPDFKLHISPSNMTNQNTPEYMEKIKQRLFENLRMLPHAPGVQMQAIPEDAVHEDSGDEDGEDPDKRISIRASDKRIACDEEFSDSEDEGEGGRRNVADHKKGAKKARIEEDKKETEDKKTDVKEEDKSKDNSGEKTDTKGTKSEQLSNP
>HIC1_HUMAN__Q14526-qslimfinder Motifs
-------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------LDLS-K------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------
>HIC1_HUMAN__Q14526-masked
XTFPEADILLKSGECAGQTMLDTMEAPGHSRQLLLQLXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXYCHLRGXXXXXXGYAPYGRPGRGLRAATPVIQACYPSXVGXXXXXAAEXPSGPEAAVNTHCAELYAXXXGPAAXLCXXXXXXXXXCGLDLSKKSPPGSAAPERPLAERELPXRXDSXPSAGPAAYKEPPLALPSLPPLPFQKLEEAAPPSDPFRGGSGSPGPEPPGRPDGPSLLYRWMKHEPGLGSYGDELGRERGSPSERCEERGGDAAVSPGGPPLGLAPPPRYPGSLDGPXAXXDGDDYKSSSEETGSSEDPSPPGGHLEGYPCPHLAYGEPXXFXXXXXXXXXXXXXXXXXEQLNAHVEAHVXXXEALYGRAEXXEVXXGXAGLGPPFXXXGDKVAGAPGGLGEXLRPYRCASCDKSYKDPATLRQHEKTHWXTRPXPCTICGKKFTQRGTMTRHMRSHLXXXXXXXXXXXXXXXXXXRLTEHMRIHSXXKPXXCQVCGXXXXXXRNLISHMKMHAVXXAXXXXXXXAGLGGLPGVPGPDGKGKLDFPEGVFAVXRXTAEXLSLKQXDKAXXXXLLAQXXXXXXXXXXXXXXXXXXXXXXXXXXLXPDKAAEVLSQGAHLAAGPDGRTIDRFSPT
>HIC1_HUMAN__Q14526 RecName: Full=Hypermethylated in cancer 1 protein; Short=Hic-1; AltName: Full=Zinc finger and BTB domain-containing protein 29;
MTFPEADILLKSGECAGQTMLDTMEAPGHSRQLLLQLNNQRTKGFLCDVIIVVQNALFRAHKNVLAASSAYLKSLVVHDNLLNLDHDMVSPAVFRLVLDFIYTGRLADGAEAAAAAAVAPGAEPSLGAVLAAASYLQIPDLVALCKKRLKRHGKYCHLRGGGGGGGGYAPYGRPGRGLRAATPVIQACYPSPVGPPPPPAAEPPSGPEAAVNTHCAELYASGPGPAAALCASERRCSPLCGLDLSKKSPPGSAAPERPLAERELPPRPDSPPSAGPAAYKEPPLALPSLPPLPFQKLEEAAPPSDPFRGGSGSPGPEPPGRPDGPSLLYRWMKHEPGLGSYGDELGRERGSPSERCEERGGDAAVSPGGPPLGLAPPPRYPGSLDGPGAGGDGDDYKSSSEETGSSEDPSPPGGHLEGYPCPHLAYGEPESFGDNLYVCIPCGKGFPSSEQLNAHVEAHVEEEEALYGRAEAAEVAAGAAGLGPPFGGGGDKVAGAPGGLGELLRPYRCASCDKSYKDPATLRQHEKTHWLTRPYPCTICGKKFTQRGTMTRHMRSHLGLKPFACDACGMRFTRQYRLTEHMRIHSGEKPYECQVCGGKFAQQRNLISHMKMHAVGGAAGAAGALAGLGGLPGVPGPDGKGKLDFPEGVFAVARLTAEQLSLKQQDKAAAAELLAQTTHFLHDPKVALESLYPLAKFTAELGLSPDKAAEVLSQGAHLAAGPDGRTIDRFSPT
>IKZF1_HUMAN__Q13422-qslimfinder Motifs
---------------------------------P-DLS-------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------
>IKZF1_HUMAN__Q13422-masked
XDADEGQDMSQVSGKESPPVSDTPDEGDEPMPIPEDLSTTSGGQQSSKSDRVVASNVKVETQSDEENGRACEMNGEECAEDLRMLDASGEKMNGSHRDQGSSALSGVGGIRXXXXXXXXXXXXXXXXXXXXXXXXXRSHTXERPFQCNQCGXXXXXXGNXLRHIKLHXXXXXXXXXXXXXXXXXXXXXXXHLRTHSXXKPXXCGYCGRSYKQRSSLEEHKERCHNYLESMGLPGTLYPVIKEETNHSEMAEDLCKIGSERSLVLDRLASNVAKRKSSMPQKFLGDKGLSDTPYDSSASYEKENEMMKSHVMDQAINNAINYLGAESLRPLVQTPPGGSEVVPVISPMYQLHKPLAEGTPRSNHSAQDSAVENLLLLSKAKLVPSEREASPSNSCQDSTDTESNNEEQRSGLIYLTNHIAPHARNGLSLKEEHRAYDLLRAASENSQDALRVVSTXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXFSSHITRGEHRFHMS
>IKZF1_HUMAN__Q13422 RecName: Full=DNA-binding protein Ikaros; AltName: Full=Ikaros family zinc finger protein 1; AltName: Full=Lymphoid transcription factor LyF-1;
MDADEGQDMSQVSGKESPPVSDTPDEGDEPMPIPEDLSTTSGGQQSSKSDRVVASNVKVETQSDEENGRACEMNGEECAEDLRMLDASGEKMNGSHRDQGSSALSGVGGIRLPNGKLKCDICGIICIGPNVLMVHKRSHTGERPFQCNQCGASFTQKGNLLRHIKLHSGEKPFKCHLCNYACRRRDALTGHLRTHSVGKPHKCGYCGRSYKQRSSLEEHKERCHNYLESMGLPGTLYPVIKEETNHSEMAEDLCKIGSERSLVLDRLASNVAKRKSSMPQKFLGDKGLSDTPYDSSASYEKENEMMKSHVMDQAINNAINYLGAESLRPLVQTPPGGSEVVPVISPMYQLHKPLAEGTPRSNHSAQDSAVENLLLLSKAKLVPSEREASPSNSCQDSTDTESNNEEQRSGLIYLTNHIAPHARNGLSLKEEHRAYDLLRAASENSQDALRVVSTSGEQMKVYKCEHCRVLFLDHVMYTIHMGCHGFRDPFECNMCGYHSQDRYEFSSHITRGEHRFHMS
>ITF2_HUMAN__P15884-qslimfinder Motifs
-------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------
>ITF2_HUMAN__P15884-masked
XHHQQRMAALGTDKELSDLLDFSAMFSPPVSSGKNGPTSLASGHFTGSNVEDRSSSGSWGNGGHPSPSRNYGDGTPYDHMTSRDLGSHDNLSPPFVNSRIQSKTERGSYSSYGRESNLQGCHQQSLLGGDMDMGNPGTLSPTKPGSQYYQYSSNNPRRRPLHSSAMEVQTKKVRKVPPGLPSSVYAPSASTADYNRDSPGYPSSKPATSTFPSSFFMQDGHHSXDPWXXXSGMNQPGYAGMLGNSSHIPQSSSYCSLHPHERLSYPSHSSADINSSLPPMSTFHRSGTNHYSTSSCTPPANGTDSIMANRGSGAAGSSQTGDALGKALASIYSPDHTNNSFSSNPSTPVGSPPSLSAGTAVWSRNGGQASSSPNYEGPLHSLQSRIEDRLERLDDAIHVLRNHAVGPSTAMPGGHGDMHGIIGPSHNGAMGXLXSXYGTGLLSANRHSLMVGTHREDGVALRGSHSLLPNQVPVPQLPVQSATSPDLNPPQDPYRGMPPGLQGQSVXXGXSEIKSDDEGDENLQDTKSSEDKKLDDDKKDIKSITSNNDDEDLTPEQKAEREKERRMANNARERLRVRDINEAXXXXGRMVQLHLKXXXXXXXXXXXXXXXXXXXXXXXXXRXRNLNPKAACLKRREEEKVSSEPPPLSLAGPHPGMGDASNHMGQM
>ITF2_HUMAN__P15884 RecName: Full=Transcription factor 4; Short=TCF-4; AltName: Full=Class B basic helix-loop-helix protein 19; Short=bHLHb19; AltName: Full=Immunoglobulin transcription factor 2; Short=ITF-2; AltName: Full=SL3-3 enhancer factor 2; Short=SEF-2;
MHHQQRMAALGTDKELSDLLDFSAMFSPPVSSGKNGPTSLASGHFTGSNVEDRSSSGSWGNGGHPSPSRNYGDGTPYDHMTSRDLGSHDNLSPPFVNSRIQSKTERGSYSSYGRESNLQGCHQQSLLGGDMDMGNPGTLSPTKPGSQYYQYSSNNPRRRPLHSSAMEVQTKKVRKVPPGLPSSVYAPSASTADYNRDSPGYPSSKPATSTFPSSFFMQDGHHSSDPWSSSSGMNQPGYAGMLGNSSHIPQSSSYCSLHPHERLSYPSHSSADINSSLPPMSTFHRSGTNHYSTSSCTPPANGTDSIMANRGSGAAGSSQTGDALGKALASIYSPDHTNNSFSSNPSTPVGSPPSLSAGTAVWSRNGGQASSSPNYEGPLHSLQSRIEDRLERLDDAIHVLRNHAVGPSTAMPGGHGDMHGIIGPSHNGAMGGLGSGYGTGLLSANRHSLMVGTHREDGVALRGSHSLLPNQVPVPQLPVQSATSPDLNPPQDPYRGMPPGLQGQSVSSGSSEIKSDDEGDENLQDTKSSEDKKLDDDKKDIKSITSNNDDEDLTPEQKAEREKERRMANNARERLRVRDINEAFKELGRMVQLHLKSDKPQTKLLILHQAVAVILSLEQQVRERNLNPKAACLKRREEEKVSSEPPPLSLAGPHPGMGDASNHMGQM
>KAT2B_HUMAN__Q92831-qslimfinder Motifs
----------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------
>KAT2B_HUMAN__Q92831-masked
XSEAGXAXPXXCXAXAGAGAGPGALPPQPAALPPAPPQGSPCAAAAGGSGXXGPATXVXXXGTAEGPXXXGSARIAVKKAQLRSAPRAKKLEKLGVXXXXXXXXXXKCNGWKNPNXSXTXPRADLQQIIVSLTEXXXXXXXXXXXXVSHLEXXSXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXKPVVEGSLEKKPPFEKPSIEQGVNNFVQYKFSHXXXXEXXXXXXXXXXXXXXXXXXXXXAPSQRRLRSPNDDISGXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXQLLXQARQEKDKLPLEKRXXXXXXXXXXXXXXEEXVXSQNSPIWDQDFLSASSRTSQLGIQTVINPPPVAGTISYNXTXXSLEQPNAGSSSPACKASSGLEANPGEKRKMTDSHVLEEAKKPRVMGDIPMELINEVMSTITDPAAMLGPETNFLSAHSARDEAARLEERRGVXXFHVVGNSXXXXXXXXXXXXXXXXXXXXXXXXPXXXXXYXTXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXIXXXXXXXXXXYPGLXCFKDGVRQIPIESIPGIRETGWKPSGKEKSKEPRDPDQLYSTLKSILQQVKSHQSAWPFMEPVKRXXXXXYXXVXXXXXXXXXXXXXLXXXXXXXXXXXXXXXXXXXXXCKXXXXXXXXXXXXXXXXXXXXXXXXXXAGLIDK
>KAT2B_HUMAN__Q92831 RecName: Full=Histone acetyltransferase KAT2B; EC=2.3.1.48; AltName: Full=Histone acetyltransferase PCAF; Short=Histone acetylase PCAF; AltName: Full=Lysine acetyltransferase 2B; AltName: Full=P300/CBP-associated factor; Short=P/CAF;
MSEAGGAGPGGCGAGAGAGAGPGALPPQPAALPPAPPQGSPCAAAAGGSGACGPATAVAAAGTAEGPGGGGSARIAVKKAQLRSAPRAKKLEKLGVYSACKAEESCKCNGWKNPNPSPTPPRADLQQIIVSLTESCRSCSHALAAHVSHLENVSEEEMNRLLGIVLDVEYLFTCVHKEEDADTKQVYFYLFKLLRKSILQRGKPVVEGSLEKKPPFEKPSIEQGVNNFVQYKFSHLPAKERQTIVELAKMFLNRINYWHLEAPSQRRLRSPNDDISGYKENYTRWLCYCNVPQFCDSLPRYETTQVFGRTLLRSVFTVMRRQLLEQARQEKDKLPLEKRTLILTHFPKFLSMLEEEVYSQNSPIWDQDFLSASSRTSQLGIQTVINPPPVAGTISYNSTSSSLEQPNAGSSSPACKASSGLEANPGEKRKMTDSHVLEEAKKPRVMGDIPMELINEVMSTITDPAAMLGPETNFLSAHSARDEAARLEERRGVIEFHVVGNSLNQKPNKKILMWLVGLQNVFSHQLPRMPKEYITRLVFDPKHKTLALIKDGRVIGGICFRMFPSQGFTEIVFCAVTSNEQVKGYGTHLMNHLKEYHIKHDILNFLTYADEYAIGYFKKQGFSKEIKIPKTKYVGYIKDYEGATLMGCELNPRIPYTEFSVIIKKQKEIIKKLIERKQAQIRKVYPGLSCFKDGVRQIPIESIPGIRETGWKPSGKEKSKEPRDPDQLYSTLKSILQQVKSHQSAWPFMEPVKRTEAPGYYEVIRFPMDLKTMSERLKNRYYVSKKLFMADLQRVFTNCKEYNPPESEYYKCANILEKFFFSKIKEAGLIDK
>LCORL_HUMAN__Q8N3X6-qslimfinder Motifs
-------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------PLDLT---------------LDLS-K-----------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------
>LCORL_HUMAN__Q8N3X6-masked
XDKGRERMAXXXXXXXXXAXXXXCRSPRCAAERXGFRXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXFEXXEPEELTDWSXDEKXXFCXXXRXXXSDCIPSLDSSQSTPTEELSSQGQSNTDKIECQAENYLNALFRKKDLPQNCDPNIPLVAQXLXXXXXXQFAIEYISKSGKTQENRNGSIGPSIVCKSIQMNQAENSLQEEQEGPLDLTVNRMQEQNTQQGDGVLDLSTKKTSIKSEESSICDPSSENSVAGRLHRNREDYVERSAEFADXXLSXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXLEAXXXXKPASFKNKTRDFHDSYSYKDSXEXXXXXXXXXXXXRAQAEXXEKSKLNLLETSEXXXPXASTYXXQXTLQKMVTQFKEKNESLQYETSNPTVQLKIPQLRVSSVSKSQPDGSGLLDVMYQVSKXSSVLEGSALQKLKNILPKQNKIECSGPVTHSSVDSYFXHGDLSPLCLNSKNGTVDGTSENTEDGLDRKDSKQPRKKRGRYRQYDHEIMEEAIAMVMSGKMSVSKAQGIYGVPHSTLEYKVKERSGTLKTPPKKKLRLPDTGLYNMTDSGTGSCKNSSKPV
>LCORL_HUMAN__Q8N3X6 RecName: Full=Ligand-dependent nuclear receptor corepressor-like protein; Short=LCoR-like protein;
MDKGRERMAAAAAAAAAAAAAAQCRSPRCAAERRGFRRELDSWRHRLMHCVGFESILEGLYGPRLRRDLSLFEDCEPEELTDWSMDEKCSFCNLQREAVSDCIPSLDSSQSTPTEELSSQGQSNTDKIECQAENYLNALFRKKDLPQNCDPNIPLVAQELMKKMIRQFAIEYISKSGKTQENRNGSIGPSIVCKSIQMNQAENSLQEEQEGPLDLTVNRMQEQNTQQGDGVLDLSTKKTSIKSEESSICDPSSENSVAGRLHRNREDYVERSAEFADGLLSKALKDIQSGALDINKAGILYGIPQKTLLLHLEALPAGKPASFKNKTRDFHDSYSYKDSKETCAVLQKVALWARAQAERTEKSKLNLLETSEIKFPTASTYLHQLTLQKMVTQFKEKNESLQYETSNPTVQLKIPQLRVSSVSKSQPDGSGLLDVMYQVSKTSSVLEGSALQKLKNILPKQNKIECSGPVTHSSVDSYFLHGDLSPLCLNSKNGTVDGTSENTEDGLDRKDSKQPRKKRGRYRQYDHEIMEEAIAMVMSGKMSVSKAQGIYGVPHSTLEYKVKERSGTLKTPPKKKLRLPDTGLYNMTDSGTGSCKNSSKPV
>LCOR_HUMAN__Q96JN0-qslimfinder Motifs
---------------------------------------------------------------PLDLT--------------LDLS-K---------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------
>LCOR_HUMAN__Q96JN0-masked
XQRMIQQFAAEYTSKNSSTQDPSQPNSTKNQSLPKASPVTTSPTAATTQNPVLSKLLMADQDSPLDLTVRKSQSEPSEQDGVLDLSTKKSPCAGSTSLSHSPGCSSTQGNGRPGRPSQYRPDGLRSGDGVPPRSLQDGTREGFGHSTSLKVPLARSLQISEELLSRNQLSTAASLGPSGLQNHGQHLILSREASXXXXHYEXXLXRMKXXGXGXXXXISDLPFLAENSAFPKMALQAKQDGKKDVSHSSPVDLKIPQVRGMDLSWESRTGDQYSYSSLVMGSQTESALSKKLRAILPKQSRKSMLDAGPDSWGSDAEQSTSGQPYPTSDQEGDPGSKQPRKKRGRYRQYNSEILEEAISVVMSGKXXXSKAQSIYGIPHSTLEYKVKERLGTLKNPPKKKMKLMRSEGPDVSVKIELDPQGEAAQSANESKNE
>LCOR_HUMAN__Q96JN0 RecName: Full=Ligand-dependent corepressor; Short=LCoR; AltName: Full=Mblk1-related protein 2;
MQRMIQQFAAEYTSKNSSTQDPSQPNSTKNQSLPKASPVTTSPTAATTQNPVLSKLLMADQDSPLDLTVRKSQSEPSEQDGVLDLSTKKSPCAGSTSLSHSPGCSSTQGNGRPGRPSQYRPDGLRSGDGVPPRSLQDGTREGFGHSTSLKVPLARSLQISEELLSRNQLSTAASLGPSGLQNHGQHLILSREASWAKPHYEFNLSRMKFRGNGALSNISDLPFLAENSAFPKMALQAKQDGKKDVSHSSPVDLKIPQVRGMDLSWESRTGDQYSYSSLVMGSQTESALSKKLRAILPKQSRKSMLDAGPDSWGSDAEQSTSGQPYPTSDQEGDPGSKQPRKKRGRYRQYNSEILEEAISVVMSGKMSVSKAQSIYGIPHSTLEYKVKERLGTLKNPPKKKMKLMRSEGPDVSVKIELDPQGEAAQSANESKNE
>MDS1_HUMAN__Q13465-qslimfinder Motifs
-------------------------------------------------------------------------------------------------------------------------------------------------------------------------
>MDS1_HUMAN__Q13465-masked
XRSKGRARKLATNNECVYGNYPEIPLEEMPDADGVASTPSLNIQEPCSPATSSEAFTPKEGSPYKAPIYIPDDIPIPAEFELRESNMPGAGLGIWTKRKIXXGEKFGPYVGEQRSNLKDPSYGWEVHLPXXXXXXXXXWXXXXXXXXXXXXXXXXXXXXXXXXQCAFLS
>MDS1_HUMAN__Q13465 RecName: Full=MDS1 and EVI1 complex locus protein MDS1; AltName: Full=Myelodysplasia syndrome 1 protein; AltName: Full=Myelodysplasia syndrome-associated protein 1;
MRSKGRARKLATNNECVYGNYPEIPLEEMPDADGVASTPSLNIQEPCSPATSSEAFTPKEGSPYKAPIYIPDDIPIPAEFELRESNMPGAGLGIWTKRKIEVGEKFGPYVGEQRSNLKDPSYGWEVHLPRSRRVSVHSWLYLGKRSSDVGIAFSQADVYMPGLQCAFLS
>NOL4L_HUMAN__Q96MY1-qslimfinder Motifs
----------------------------------------------------------------------------------------------------------------------------------------------------P-DLT-------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------P-DLS-K-----------------------------------------------------------------
>NOL4L_HUMAN__Q96MY1-masked
XSDSTWMSADPHLASSLSPSQDERMRSPQNLHSQEDDDSXXEXGSGNGSSTLNPSTSSSTQGDPAFPEMNGNGAVAPMDFTTAAEDQPINLCDKLPPATALGTASYPSDGCGADGLRSRVKYGVKTTPESPPYSSGSYDSIKTEVSGCPEDLTVGRAPTADXXXXXHXXHEDNDKMNDSEGMDPERLKAFNMFVXXXXXXXXDRMVPISKQPKEKIQAIIESCSRQFPEFQERARKRIRTYLKSCRRMKKNGMEMTRPTPPHLTSAMAENILAAACESETRKAAKRMRLEIYQSSQDEPIALDKQHSRDSAAITHSTYSLPASSYSQDPVYANGGLNYSYRGYGALSSNLQPPASLQTGNHSNGPTDLSMKGGASTXSXXPXPTPSSTSTSRPVPTAQLSPTEISAVRQLIXXXXXXXXXXXXXXXXXXXLILQQN
>NOL4L_HUMAN__Q96MY1 RecName: Full=Nucleolar protein 4-like;
MSDSTWMSADPHLASSLSPSQDERMRSPQNLHSQEDDDSSSESGSGNGSSTLNPSTSSSTQGDPAFPEMNGNGAVAPMDFTTAAEDQPINLCDKLPPATALGTASYPSDGCGADGLRSRVKYGVKTTPESPPYSSGSYDSIKTEVSGCPEDLTVGRAPTADDDDDDHDDHEDNDKMNDSEGMDPERLKAFNMFVRLFVDENLDRMVPISKQPKEKIQAIIESCSRQFPEFQERARKRIRTYLKSCRRMKKNGMEMTRPTPPHLTSAMAENILAAACESETRKAAKRMRLEIYQSSQDEPIALDKQHSRDSAAITHSTYSLPASSYSQDPVYANGGLNYSYRGYGALSSNLQPPASLQTGNHSNGPTDLSMKGGASTTSTTPTPTPSSTSTSRPVPTAQLSPTEISAVRQLIAGYRESAAFLLRSADELENLILQQN
>NRIP1_HUMAN__P48552-qslimfinder Motifs
-------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------PIDLS-K----------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------
>NRIP1_HUMAN__P48552-masked
XTHGEELGSDVHQDSIXLTYXEGLLMHQAAGGSGTAVDKKSAGHNEEDQNFNISGSAFPTCQSNGPVLNTHTYQGSGMLHLKKARLLQSSEDWNAAKRKRLSDSIMNLNXXKEXXLAGMVDSVPKGKQDSTLLASLLXXXXXXXXXVXXSQQIXXXXKEQGYALSHDSLKXXKDLRCYXVASSHLKTLLKKSKVKDQKPDTNLPDVTKNLIRDRFAESPHHVGQSGTKVMSEPLSCAARLQAVASMVEKRASPATSPKPSVACSQLALLXXSEAHLQQYSREHALKTQNANQAASERLAAMARLQENGQKDVGSYQLPKGMSSHLNGQARTSSSKLMASKSSATVFQNPMGIIPSSPKNAGYKNSLERNNIKQAANNSLXXHXLKSQTIPKPMNGHSHSERGSIFEESSTPTTIDEYSDNNPSFTDDSSGDESSYSNCVPIDLSCKHRTEKSESDQPVSLDNFTQSLLNTWDPKVPDVDIKEDQDTSKNSKLNSHQKVTLXQXXLGHKNEENVEKNTSPQGVHNDVSKFNTQNYARTSVIESPSTNRTTPVSTPPLLTSSKAGSPINLSQHSLVIKWNSPPYVCSTQSEKLTNTASNHSMDLTKSKDPPGEKPAQNEGAQNSATFSASKLLQNLAQCGMQSSMSVEEQRPSKQLLTGNTDKPIGMIDRLNSPLLSNKTNAVEENKAFSSQPTGPEPGLSGSEIENLLERRTVLQLLLGNPNKGKSEKKEKTPLRDESTQEHSERALSEQILMVKIKSEPCDDLQIPNTNVHLSHDAKSAPFLGMAPAVQRSAPALPVSEDFKSEPVSPQDFSFSKNGLLSRLLRQNQDSYLADDSDRSHRNNEMALLESKNLCMVPKKRKLYTEPLENPFKKMKNNIVDAANNHSAPEVLYGSLLNQEELKFSRNDLEFKYPAGHGSASESEHRSWARESKSFNVLKQLLLSENCVRDLSPHRSNSVADSKKKGHKNNVTNSKPEFSISSLNGLMYSSTQPSSCMDNRTFSYPGVVKTPVSPTFPEHLGCAGSRPESGLLNGCSMPSEKGPIKWVITDAEKNEYEKDSPRLTKTNPILYYMLQKGGNSVTSRETQDKDIWREASSAESVSQVTAKEELLPTAETKASFFNLRSPYNSHMGNNASRPHSANGEVYGLLGSVLTIKKESE
>NRIP1_HUMAN__P48552 RecName: Full=Nuclear receptor-interacting protein 1; AltName: Full=Nuclear factor RIP140; AltName: Full=Receptor-interacting protein 140;
MTHGEELGSDVHQDSIVLTYLEGLLMHQAAGGSGTAVDKKSAGHNEEDQNFNISGSAFPTCQSNGPVLNTHTYQGSGMLHLKKARLLQSSEDWNAAKRKRLSDSIMNLNVKKEALLAGMVDSVPKGKQDSTLLASLLQSFSSRLQTVALSQQIRQSLKEQGYALSHDSLKVEKDLRCYGVASSHLKTLLKKSKVKDQKPDTNLPDVTKNLIRDRFAESPHHVGQSGTKVMSEPLSCAARLQAVASMVEKRASPATSPKPSVACSQLALLLSSEAHLQQYSREHALKTQNANQAASERLAAMARLQENGQKDVGSYQLPKGMSSHLNGQARTSSSKLMASKSSATVFQNPMGIIPSSPKNAGYKNSLERNNIKQAANNSLLLHLLKSQTIPKPMNGHSHSERGSIFEESSTPTTIDEYSDNNPSFTDDSSGDESSYSNCVPIDLSCKHRTEKSESDQPVSLDNFTQSLLNTWDPKVPDVDIKEDQDTSKNSKLNSHQKVTLLQLLLGHKNEENVEKNTSPQGVHNDVSKFNTQNYARTSVIESPSTNRTTPVSTPPLLTSSKAGSPINLSQHSLVIKWNSPPYVCSTQSEKLTNTASNHSMDLTKSKDPPGEKPAQNEGAQNSATFSASKLLQNLAQCGMQSSMSVEEQRPSKQLLTGNTDKPIGMIDRLNSPLLSNKTNAVEENKAFSSQPTGPEPGLSGSEIENLLERRTVLQLLLGNPNKGKSEKKEKTPLRDESTQEHSERALSEQILMVKIKSEPCDDLQIPNTNVHLSHDAKSAPFLGMAPAVQRSAPALPVSEDFKSEPVSPQDFSFSKNGLLSRLLRQNQDSYLADDSDRSHRNNEMALLESKNLCMVPKKRKLYTEPLENPFKKMKNNIVDAANNHSAPEVLYGSLLNQEELKFSRNDLEFKYPAGHGSASESEHRSWARESKSFNVLKQLLLSENCVRDLSPHRSNSVADSKKKGHKNNVTNSKPEFSISSLNGLMYSSTQPSSCMDNRTFSYPGVVKTPVSPTFPEHLGCAGSRPESGLLNGCSMPSEKGPIKWVITDAEKNEYEKDSPRLTKTNPILYYMLQKGGNSVTSRETQDKDIWREASSAESVSQVTAKEELLPTAETKASFFNLRSPYNSHMGNNASRPHSANGEVYGLLGSVLTIKKESE
>RBBP5_HUMAN__Q15291-qslimfinder Motifs
----------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------
>RBBP5_HUMAN__Q15291-masked
XNLELLESFGQNYPXEAXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXSTXXXXXQWDVLXXXCDXXXXXPSPILKVQYHPRDXNKVLVCPXXXXXXXXXLXDSKHVVLPVDDXXXXNVVXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXSFRVXXXXXXXXAIKSXXXXXXXXXXXXXXXXXXXXXXXXXXILTCGRDGEPEPMQKLQDLVNRTPWKKXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXWXAFAPDFKELDENVEYXXRXSEFDIEDEDKSEPEQTGADAAEDEEVDVTSVDPIAAFCSSDEELEDSKALLYLPIAPEVEDPEENPYGPPPDAVQTSLMDEGASSEKKRQSSADGSQPPKKKPKTTNIELQGVPNDEVHPLLGVKGDGKSKKKQAGRPKGSKGKEKDSPFKPKLYKGDRGLPLEGSAKGKVQAELSQPLTAGGAISELL
>RBBP5_HUMAN__Q15291 RecName: Full=Retinoblastoma-binding protein 5; Short=RBBP-5; AltName: Full=Retinoblastoma-binding protein RBQ-3;
MNLELLESFGQNYPEEADGTLDCISMALTCTFNRWGTLLAVGCNDGRIVIWDFLTRGIAKIISAHIHPVCSLCWSRDGHKLVSASTDNIVSQWDVLSGDCDQRFRFPSPILKVQYHPRDQNKVLVCPMKSAPVMLTLSDSKHVVLPVDDDSDLNVVASFDRRGEYIYTGNAKGKILVLKTDSQDLVASFRVTTGTSNTTAIKSIEFARKGSCFLINTADRIIRVYDGREILTCGRDGEPEPMQKLQDLVNRTPWKKCCFSGDGEYIVAGSARQHALYIWEKSIGNLVKILHGTRGELLLDVAWHPVRPIIASISSGVVSIWAQNQVENWSAFAPDFKELDENVEYEERESEFDIEDEDKSEPEQTGADAAEDEEVDVTSVDPIAAFCSSDEELEDSKALLYLPIAPEVEDPEENPYGPPPDAVQTSLMDEGASSEKKRQSSADGSQPPKKKPKTTNIELQGVPNDEVHPLLGVKGDGKSKKKQAGRPKGSKGKEKDSPFKPKLYKGDRGLPLEGSAKGKVQAELSQPLTAGGAISELL
>SOBP_HUMAN__A7XYQ1-qslimfinder Motifs
---------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------
>SOBP_HUMAN__A7XYQ1-masked
XXEMEKEGRPPENKRSRKPAHPVKREINEEMKNFAENTMNELLXWYGYDKVXXKXGEDIEFRSYPTDGESRQHISVLKENSLPKPKLPEDSVISPYNISTGYSGLATGNGLSDSPAGSKDHGSVPIIVPLIPXXFIKXPAEDDXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXRNKARDEDGHAENFPQQHYAKETPRXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXAGLCSTLHPPMENKAEGTGVQLLTPDSWNIPLTDARRKAPSPVATAGQSQGPGPSASTTVSPSDTANCSVTKIPTPVPKSIPISETPNIPPVSVQPPASIGPPLGVPPRSPPMVMTNRGPVPLPIFMEQQIMQQIRPPFIRGPPHHASNPNSPLSNPMLPGIGPPPGGPRNLGPTSSPMHRPMLSPHIHPPSTPTMPGNPXGLLXXXXXGAXLPSLPFPPVSMMPNGPMPVPQMMXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXPIPHVSDSKPPNGFSSNGENFIPNAPGDSAAAGGKPSGHSLSPRDSKQGSSKSADSPPGCSGQALSLAPTPAEHGRSEVVDLTRRAGSPPGPPGAGGQLGFPGVLQGPQDGVIDLTVGHRARLHNVIHRALHAHVKAEREPSAAERRTCGGCRDGHCSPPAAGDPGPGAPAGPEXXXACNVIVNGTRGAAAEGAKSAEPXXEQXXXXXXXAXPKKLLSPEEPAVSELESVKENNCASNCHLDGEAAKKLMGEEALAGGDKSDPNLNNPADEDHAYALRMLPKTGCVIQPVPKPAXKAAMAPCIISSPMLSAGPEDLEPPLKRRCLRIRNQNK
>SOBP_HUMAN__A7XYQ1 RecName: Full=Sine oculis-binding protein homolog; AltName: Full=Jackson circler protein 1;
MAEMEKEGRPPENKRSRKPAHPVKREINEEMKNFAENTMNELLGWYGYDKVELKDGEDIEFRSYPTDGESRQHISVLKENSLPKPKLPEDSVISPYNISTGYSGLATGNGLSDSPAGSKDHGSVPIIVPLIPPPFIKPPAEDDVSNVQIMCAWCQKVGIKRYSLSMGSEVKSFCSEKCFAACRRAYFKRNKARDEDGHAENFPQQHYAKETPRLAFKNNCELLVCDWCKHIRHTKEYLDFGDGERRLQFCSAKCLNQYKMDIFYKETQANLPAGLCSTLHPPMENKAEGTGVQLLTPDSWNIPLTDARRKAPSPVATAGQSQGPGPSASTTVSPSDTANCSVTKIPTPVPKSIPISETPNIPPVSVQPPASIGPPLGVPPRSPPMVMTNRGPVPLPIFMEQQIMQQIRPPFIRGPPHHASNPNSPLSNPMLPGIGPPPGGPRNLGPTSSPMHRPMLSPHIHPPSTPTMPGNPPGLLPPPPPGAPLPSLPFPPVSMMPNGPMPVPQMMNFGLPSLAPLVPPPTLLVPYPVIVPLPVPIPIPIPIPHVSDSKPPNGFSSNGENFIPNAPGDSAAAGGKPSGHSLSPRDSKQGSSKSADSPPGCSGQALSLAPTPAEHGRSEVVDLTRRAGSPPGPPGAGGQLGFPGVLQGPQDGVIDLTVGHRARLHNVIHRALHAHVKAEREPSAAERRTCGGCRDGHCSPPAAGDPGPGAPAGPEAAAACNVIVNGTRGAAAEGAKSAEPPPEQPPPPPPPAPPKKLLSPEEPAVSELESVKENNCASNCHLDGEAAKKLMGEEALAGGDKSDPNLNNPADEDHAYALRMLPKTGCVIQPVPKPAEKAAMAPCIISSPMLSAGPEDLEPPLKRRCLRIRNQNK
>ZN219_HUMAN__Q9P2Y4-qslimfinder Motifs
-------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------PLDLS-R------------------------------------------------------------------------------------------
>ZN219_HUMAN__Q9P2Y4-masked
XEGSRPRAPSGHLAPSPPAFDGELDLQRYSNGPAVSAGSLGMGAVSWSESRAXXRRXPXXXXXXXXXXXXXXXXXXXXXXXXXAFQCPHCGHRAAQRALLRSHLRTHQPERPRSPAARLLLELEERALLREARLGRARSSGGMQATPATEGLARPQAPSSSAFRCPYCKGKFXTXAXRERHXHXXXXXXXXXXXXXXXXQEEELLHHSLTAHGAPERPLAATSAAPXXQXQXQXXXQXEPRSVPQPEPEPEPEREATPTPAPAAPEEXXAXPEFRCQVCGQSFXXXWFLKGHXRXXXXXXXXXXXXXXXXXXXXXXXKXXMKVHASKLGPLRAPGPASGPARAPQPPDLGLLAYEPLGPALLLAPAPTPAERREPPSLLGYLSLRAGEGRPNGEGAEPGPGRSFGGFRPLSSALPARARRHRAEXPXXXXXVVXAXXETWARGRSLGSLASLHPRPGEGPGHSASXXGXQARSTATQEENGLLVGGTRPEGGRGATGKDCPFCGKSFXSXHHLKVHLRVHTGERPYKCPHCDYAGTQSGSLKYHLQRHHREQRSGAGPGXXXEXXXPSQRGSAPQSGAKPSPQPATWVEGASSPRPPSSGAGPGSRRKPASPGRTLRNGRGGEAEPLDLSLRAGPGXEAXPXGXXXXXXXXXXXXXXXXXMALHLQVHHSRXAXGXRPPQADASPPYARVPSGETPPSPSQEGEEGSGLSRPGEAGLGGQER
>ZN219_HUMAN__Q9P2Y4 RecName: Full=Zinc finger protein 219;
MEGSRPRAPSGHLAPSPPAFDGELDLQRYSNGPAVSAGSLGMGAVSWSESRAGERRFPCPVCGKRFRFNSILALHLRAHPGAQAFQCPHCGHRAAQRALLRSHLRTHQPERPRSPAARLLLELEERALLREARLGRARSSGGMQATPATEGLARPQAPSSSAFRCPYCKGKFRTSAERERHLHILHRPWKCGLCSFGSSQEEELLHHSLTAHGAPERPLAATSAAPPPQPQPQPPPQPEPRSVPQPEPEPEPEREATPTPAPAAPEEPPAPPEFRCQVCGQSFTQSWFLKGHMRKHKASFDHACPVCGRCFKEPWFLKNHMKVHASKLGPLRAPGPASGPARAPQPPDLGLLAYEPLGPALLLAPAPTPAERREPPSLLGYLSLRAGEGRPNGEGAEPGPGRSFGGFRPLSSALPARARRHRAEEPEEEEEVVEAEEETWARGRSLGSLASLHPRPGEGPGHSASAAGAQARSTATQEENGLLVGGTRPEGGRGATGKDCPFCGKSFRSAHHLKVHLRVHTGERPYKCPHCDYAGTQSGSLKYHLQRHHREQRSGAGPGPPPEPPPPSQRGSAPQSGAKPSPQPATWVEGASSPRPPSSGAGPGSRRKPASPGRTLRNGRGGEAEPLDLSLRAGPGGEAGPGGALHRCLFCPFATGAPELMALHLQVHHSRRARGRRPPQADASPPYARVPSGETPPSPSQEGEEGSGLSRPGEAGLGGQER
>qslimfinder 15120900008 SLiMFinder Motifs motifs
-1----------------------------------P.DLS.[KR]---------------------------XXXXXXXXXX-2----------------------------------P[IL]DL---------------------------XXXXXXXXXX-3----------------------------------[IL]DLS.[KR]------------------------XXXXXXXXXX-4----------------------------------P.DLS.K------------------------------XXXXXXXXXX-5----------------------------------P.DL[ST]---------------------------XXXXXXXXXX-6----------------------------------P[IL]DLS---------------------------
>LCORL_HUMAN__Q8N3X6 RecName: Full=Ligand-dependent nuclear receptor corepressor-like protein; Short=LCoR-like protein;
-------------------------------------------------------------------------XXXXXXXXXX-0212-NRNGSIGPSIVCKSIQMNQAENSLQEEQEGPLDLTVNRMQEQNTQQGDGVLDLSTKKTSIKSE-XXXXXXXXXX-0232-ENSLQEEQEGPLDLTVNRMQEQNTQQGDGVLDLSTKKTSIKSEESSICDPSSENSVAGRLHRNRE-XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX-0212-NRNGSIGPSIVCKSIQMNQAENSLQEEQEGPLDLTVNRMQEQNTQQGDGVLDLSTKKTSIKSEE-XXXXXXXXXX-----------------------------------------------------------------------
>ZN219_HUMAN__Q9P2Y4 RecName: Full=Zinc finger protein 219;
-0626-PPSSGAGPGSRRKPASPGRTLRNGRGGEAEPLDLSLRAGPGGEAGPGGALHRCLFCPFATGAPELM-XXXXXXXXXX-0626-PPSSGAGPGSRRKPASPGRTLRNGRGGEAEPLDLSLRAGPGGEAGPGGALHRCLFCPFATGAP-XXXXXXXXXX-0627-PSSGAGPGSRRKPASPGRTLRNGRGGEAEPLDLSLRAGPGGEAGPGGALHRCLFCPFATGAPELM-XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX-0626-PPSSGAGPGSRRKPASPGRTLRNGRGGEAEPLDLSLRAGPGGEAGPGGALHRCLFCPFATGAPE-XXXXXXXXXX-0626-PPSSGAGPGSRRKPASPGRTLRNGRGGEAEPLDLSLRAGPGGEAGPGGALHRCLFCPFATGAPE-
>E1A_ADE02__P03254 RecName: Full=Early E1A protein {ECO:0000305}; AltName: Full=Early E1A 32 kDa protein;
-0279-LCPIKPVAVRVGGRRQAVECIEDLLNESGQPLDLSCKRPRP--------------------------XXXXXXXXXX-0279-LCPIKPVAVRVGGRRQAVECIEDLLNESGQPLDLSCKRPRP-----------------------XXXXXXXXXX-0280-CPIKPVAVRVGGRRQAVECIEDLLNESGQPLDLSCKRPRP--------------------------XXXXXXXXXX-0279-LCPIKPVAVRVGGRRQAVECIEDLLNESGQPLDLSCKRPRP--------------------------XXXXXXXXXX-0279-LCPIKPVAVRVGGRRQAVECIEDLLNESGQPLDLSCKRPRP------------------------XXXXXXXXXX-0279-LCPIKPVAVRVGGRRQAVECIEDLLNESGQPLDLSCKRPRP------------------------
>IKZF1_HUMAN__Q13422 RecName: Full=DNA-binding protein Ikaros; AltName: Full=Ikaros family zinc finger protein 1; AltName: Full=Lymphoid transcription factor LyF-1;
-------------------------------------------------------------------------XXXXXXXXXX----------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX-0034-DEGQDMSQVSGKESPPVSDTPDEGDEPMPIPEDLSTTSGGQQSSKSDRVVASNVKVETQSDEEN-XXXXXXXXXX-----------------------------------------------------------------------
>CBX4_HUMAN__O00257 RecName: Full=E3 SUMO-protein ligase CBX4; EC=6.3.2.-; AltName: Full=Chromobox protein homolog 4; AltName: Full=Polycomb 2 homolog; Short=Pc2; Short=hPc2;
-------------------------------------------------------------------------XXXXXXXXXX-0472-SPAAERPADLPPAAALPQPEVILLDSDLDEPIDLRCVKTRSEAGEPPSSLQVKPETPASAAVA-XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------
>NOL4L_HUMAN__Q96MY1 RecName: Full=Nucleolar protein 4-like;
-0365-GLNYSYRGYGALSSNLQPPASLQTGNHSNGPTDLSMKGGASTTSTTPTPTPSSTSTSRPVPTAQLS-XXXXXXXXXX----------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX-0365-GLNYSYRGYGALSSNLQPPASLQTGNHSNGPTDLSMKGGASTTSTTPTPTPSSTSTSRPVPTAQLS-XXXXXXXXXX-0365-GLNYSYRGYGALSSNLQPPASLQTGNHSNGPTDLSMKGGASTTSTTPTPTPSSTSTSRPVPTAQ-XXXXXXXXXX-----------------------------------------------------------------------
>NOL4L_HUMAN__Q96MY1 RecName: Full=Nucleolar protein 4-like;
-------------------------------------------------------------------------XXXXXXXXXX----------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX-0149-RVKYGVKTTPESPPYSSGSYDSIKTEVSGCPEDLTVGRAPTADDDDDDHDDHEDNDKMNDSEGM-XXXXXXXXXX-----------------------------------------------------------------------
>FOG1_HUMAN__Q8IX07 RecName: Full=Zinc finger protein ZFPM1; AltName: Full=Friend of GATA protein 1; Short=FOG-1; Short=Friend of GATA 1; AltName: Full=Zinc finger protein 89A; AltName: Full=Zinc finger protein multitype 1;
-0794-PAPESPRPGSGSGSGPGLAPARSPGPAADGPIDLSKKPRRPLPGAPAPALADYHECTACRVSFHSL-XXXXXXXXXX-0794-PAPESPRPGSGSGSGPGLAPARSPGPAADGPIDLSKKPRRPLPGAPAPALADYHECTACRVSF-XXXXXXXXXX-0795-APESPRPGSGSGSGPGLAPARSPGPAADGPIDLSKKPRRPLPGAPAPALADYHECTACRVSFHSL-XXXXXXXXXX-0794-PAPESPRPGSGSGSGPGLAPARSPGPAADGPIDLSKKPRRPLPGAPAPALADYHECTACRVSFHSL-XXXXXXXXXX-0794-PAPESPRPGSGSGSGPGLAPARSPGPAADGPIDLSKKPRRPLPGAPAPALADYHECTACRVSFH-XXXXXXXXXX-0794-PAPESPRPGSGSGSGPGLAPARSPGPAADGPIDLSKKPRRPLPGAPAPALADYHECTACRVSFH-
>HIC1_HUMAN__Q14526 RecName: Full=Hypermethylated in cancer 1 protein; Short=Hic-1; AltName: Full=Zinc finger and BTB domain-containing protein 29;
-------------------------------------------------------------------------XXXXXXXXXX----------------------------------------------------------------------XXXXXXXXXX-0242-NTHCAELYASGPGPAAALCASERRCSPLCGLDLSKKSPPGSAAPERPLAERELPPRPDSPPSAGP-XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------
>NRIP1_HUMAN__P48552 RecName: Full=Nuclear receptor-interacting protein 1; AltName: Full=Nuclear factor RIP140; AltName: Full=Receptor-interacting protein 140;
-0440-TPTTIDEYSDNNPSFTDDSSGDESSYSNCVPIDLSCKHRTEKSESDQPVSLDNFTQSLLNTWDPKV-XXXXXXXXXX-0440-TPTTIDEYSDNNPSFTDDSSGDESSYSNCVPIDLSCKHRTEKSESDQPVSLDNFTQSLLNTWD-XXXXXXXXXX-0441-PTTIDEYSDNNPSFTDDSSGDESSYSNCVPIDLSCKHRTEKSESDQPVSLDNFTQSLLNTWDPKV-XXXXXXXXXX-0440-TPTTIDEYSDNNPSFTDDSSGDESSYSNCVPIDLSCKHRTEKSESDQPVSLDNFTQSLLNTWDPKV-XXXXXXXXXX-0440-TPTTIDEYSDNNPSFTDDSSGDESSYSNCVPIDLSCKHRTEKSESDQPVSLDNFTQSLLNTWDP-XXXXXXXXXX-0440-TPTTIDEYSDNNPSFTDDSSGDESSYSNCVPIDLSCKHRTEKSESDQPVSLDNFTQSLLNTWDP-
>BRCA1_HUMAN__P38398 RecName: Full=Breast cancer type 1 susceptibility protein; EC=6.3.2.-; AltName: Full=RING finger protein 53;
-------------------------------------------------------------------------XXXXXXXXXX----------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX-1544-SGSLQNRNYPSQEELIKVVDVEEQQLEESGPHDLTETSYLPRQDLEGTPYLESGISLFSDDPES-XXXXXXXXXX-----------------------------------------------------------------------
>LCOR_HUMAN__Q96JN0 RecName: Full=Ligand-dependent corepressor; Short=LCoR; AltName: Full=Mblk1-related protein 2;
-------------------------------------------------------------------------XXXXXXXXXX-0064-PKASPVTTSPTAATTQNPVLSKLLMADQDSPLDLTVRKSQSEPSEQDGVLDLSTKKSPCAGST-XXXXXXXXXX-0083-LSKLLMADQDSPLDLTVRKSQSEPSEQDGVLDLSTKKSPCAGSTSLSHSPGCSSTQGNGRPGRPS-XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX-0064-PKASPVTTSPTAATTQNPVLSKLLMADQDSPLDLTVRKSQSEPSEQDGVLDLSTKKSPCAGSTS-XXXXXXXXXX-----------------------------------------------------------------------
>ATX1L_HUMAN__P0C7T5 RecName: Full=Ataxin-1-like; AltName: Full=Brother of ataxin-1; Short=Brother of ATXN1;
-------------------------------------------------------------------------XXXXXXXXXX-0219-PQAPSPAHSFNKAPSATSPSGQLPHHSSTQPLDLAPGRMPIYYQMSRLPAGYTLHETPPAGAS-XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------
>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;
-0490-CPQASFDKENAFPFPMDNQFSMNGDCVMDKPLDLSDRFSAIQRQEKSQGSETSKNKFRQVTLYEAL-XXXXXXXXXX-0490-CPQASFDKENAFPFPMDNQFSMNGDCVMDKPLDLSDRFSAIQRQEKSQGSETSKNKFRQVTLY-XXXXXXXXXX-0491-PQASFDKENAFPFPMDNQFSMNGDCVMDKPLDLSDRFSAIQRQEKSQGSETSKNKFRQVTLYEAL-XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX-0490-CPQASFDKENAFPFPMDNQFSMNGDCVMDKPLDLSDRFSAIQRQEKSQGSETSKNKFRQVTLYE-XXXXXXXXXX-0490-CPQASFDKENAFPFPMDNQFSMNGDCVMDKPLDLSDRFSAIQRQEKSQGSETSKNKFRQVTLYE-
>qslimfinder 15120900008 SLiMFinder Motifs motifs
-1----------------------------------P.DLS.[KR]---------------------------XXXXXXXXXX-2----------------------------------P[IL]DL---------------------------XXXXXXXXXX-3----------------------------------[IL]DLS.[KR]------------------------XXXXXXXXXX-4----------------------------------P.DLS.K------------------------------XXXXXXXXXX-5----------------------------------P.DL[ST]---------------------------XXXXXXXXXX-6----------------------------------P[IL]DLS---------------------------
>LCORL_HUMAN__Q8N3X6 RecName: Full=Ligand-dependent nuclear receptor corepressor-like protein; Short=LCoR-like protein;
-------------------------------------------------------------------------XXXXXXXXXX-0212-NRNGSIGPSIVCKSIQMNQAENSLQEEQEGPLDLTVNRMQEQNTQQGDGVLDLSTKKTSIKSE-XXXXXXXXXX-0232-ENSLQEEQEGPLDLTVNRMQEQNTQQGDGVLDLSTKKTSIKSEESSICDPSSENSVAGRLHRNRE-XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX-0212-NRNGSIGPSIVCKSIQMNQAENSLQEEQEGPLDLTVNRMQEQNTQQGDGVLDLSTKKTSIKSEE-XXXXXXXXXX-----------------------------------------------------------------------
>ZN219_HUMAN__Q9P2Y4 RecName: Full=Zinc finger protein 219;
-0626-PPSSGAGPGSRRKPASPGRTLRNGRGGEAEPLDLSLRAGPGXEAXPXGXXXXXXXXXXXXXXXXXM-XXXXXXXXXX-0626-PPSSGAGPGSRRKPASPGRTLRNGRGGEAEPLDLSLRAGPGXEAXPXGXXXXXXXXXXXXXXX-XXXXXXXXXX-0627-PSSGAGPGSRRKPASPGRTLRNGRGGEAEPLDLSLRAGPGXEAXPXGXXXXXXXXXXXXXXXXXM-XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX-0626-PPSSGAGPGSRRKPASPGRTLRNGRGGEAEPLDLSLRAGPGXEAXPXGXXXXXXXXXXXXXXXX-XXXXXXXXXX-0626-PPSSGAGPGSRRKPASPGRTLRNGRGGEAEPLDLSLRAGPGXEAXPXGXXXXXXXXXXXXXXXX-
>E1A_ADE02__P03254 RecName: Full=Early E1A protein {ECO:0000305}; AltName: Full=Early E1A 32 kDa protein;
-0279-LCPIKPVAVRXXGRRXXXECIEDLLNXXGQPLDLSCKRPRP--------------------------XXXXXXXXXX-0279-LCPIKPVAVRXXGRRXXXECIEDLLNXXGQPLDLSCKRPRP-----------------------XXXXXXXXXX-0280-CPIKPVAVRXXGRRXXXECIEDLLNXXGQPLDLSCKRPRP--------------------------XXXXXXXXXX-0279-LCPIKPVAVRXXGRRXXXECIEDLLNXXGQPLDLSCKRPRP--------------------------XXXXXXXXXX-0279-LCPIKPVAVRXXGRRXXXECIEDLLNXXGQPLDLSCKRPRP------------------------XXXXXXXXXX-0279-LCPIKPVAVRXXGRRXXXECIEDLLNXXGQPLDLSCKRPRP------------------------
>IKZF1_HUMAN__Q13422 RecName: Full=DNA-binding protein Ikaros; AltName: Full=Ikaros family zinc finger protein 1; AltName: Full=Lymphoid transcription factor LyF-1;
-------------------------------------------------------------------------XXXXXXXXXX----------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX-0034-DEGQDMSQVSGKESPPVSDTPDEGDEPMPIPEDLSTTSGGQQSSKSDRVVASNVKVETQSDEEN-XXXXXXXXXX-----------------------------------------------------------------------
>CBX4_HUMAN__O00257 RecName: Full=E3 SUMO-protein ligase CBX4; EC=6.3.2.-; AltName: Full=Chromobox protein homolog 4; AltName: Full=Polycomb 2 homolog; Short=Pc2; Short=hPc2;
-------------------------------------------------------------------------XXXXXXXXXX-0472-SPAAERPADLPPAAALPQPEVILLDSDLDEPIDLRCVKTRSEAGEPPSSLQVKPETPASXXVX-XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------
>NOL4L_HUMAN__Q96MY1 RecName: Full=Nucleolar protein 4-like;
-0365-GLNYSYRGYGALSSNLQPPASLQTGNHSNGPTDLSMKGGASTXSXXPXPTPSSTSTSRPVPTAQLS-XXXXXXXXXX----------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX-0365-GLNYSYRGYGALSSNLQPPASLQTGNHSNGPTDLSMKGGASTXSXXPXPTPSSTSTSRPVPTAQLS-XXXXXXXXXX-0365-GLNYSYRGYGALSSNLQPPASLQTGNHSNGPTDLSMKGGASTXSXXPXPTPSSTSTSRPVPTAQ-XXXXXXXXXX-----------------------------------------------------------------------
>NOL4L_HUMAN__Q96MY1 RecName: Full=Nucleolar protein 4-like;
-------------------------------------------------------------------------XXXXXXXXXX----------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX-0149-RVKYGVKTTPESPPYSSGSYDSIKTEVSGCPEDLTVGRAPTADXXXXXHXXHEDNDKMNDSEGM-XXXXXXXXXX-----------------------------------------------------------------------
>FOG1_HUMAN__Q8IX07 RecName: Full=Zinc finger protein ZFPM1; AltName: Full=Friend of GATA protein 1; Short=FOG-1; Short=Friend of GATA 1; AltName: Full=Zinc finger protein 89A; AltName: Full=Zinc finger protein multitype 1;
-0794-PAPESPRPGSGSGSGPGLAPARSPGPAADGPIDLSKKPRRPLPGAPAPALAXXXXXXXXXXXXXXX-XXXXXXXXXX-0794-PAPESPRPGSGSGSGPGLAPARSPGPAADGPIDLSKKPRRPLPGAPAPALAXXXXXXXXXXXX-XXXXXXXXXX-0795-APESPRPGSGSGSGPGLAPARSPGPAADGPIDLSKKPRRPLPGAPAPALAXXXXXXXXXXXXXXX-XXXXXXXXXX-0794-PAPESPRPGSGSGSGPGLAPARSPGPAADGPIDLSKKPRRPLPGAPAPALAXXXXXXXXXXXXXXX-XXXXXXXXXX-0794-PAPESPRPGSGSGSGPGLAPARSPGPAADGPIDLSKKPRRPLPGAPAPALAXXXXXXXXXXXXX-XXXXXXXXXX-0794-PAPESPRPGSGSGSGPGLAPARSPGPAADGPIDLSKKPRRPLPGAPAPALAXXXXXXXXXXXXX-
>HIC1_HUMAN__Q14526 RecName: Full=Hypermethylated in cancer 1 protein; Short=Hic-1; AltName: Full=Zinc finger and BTB domain-containing protein 29;
-------------------------------------------------------------------------XXXXXXXXXX----------------------------------------------------------------------XXXXXXXXXX-0242-NTHCAELYAXXXGPAAXLCXXXXXXXXXCGLDLSKKSPPGSAAPERPLAERELPXRXDSXPSAGP-XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------
>NRIP1_HUMAN__P48552 RecName: Full=Nuclear receptor-interacting protein 1; AltName: Full=Nuclear factor RIP140; AltName: Full=Receptor-interacting protein 140;
-0440-TPTTIDEYSDNNPSFTDDSSGDESSYSNCVPIDLSCKHRTEKSESDQPVSLDNFTQSLLNTWDPKV-XXXXXXXXXX-0440-TPTTIDEYSDNNPSFTDDSSGDESSYSNCVPIDLSCKHRTEKSESDQPVSLDNFTQSLLNTWD-XXXXXXXXXX-0441-PTTIDEYSDNNPSFTDDSSGDESSYSNCVPIDLSCKHRTEKSESDQPVSLDNFTQSLLNTWDPKV-XXXXXXXXXX-0440-TPTTIDEYSDNNPSFTDDSSGDESSYSNCVPIDLSCKHRTEKSESDQPVSLDNFTQSLLNTWDPKV-XXXXXXXXXX-0440-TPTTIDEYSDNNPSFTDDSSGDESSYSNCVPIDLSCKHRTEKSESDQPVSLDNFTQSLLNTWDP-XXXXXXXXXX-0440-TPTTIDEYSDNNPSFTDDSSGDESSYSNCVPIDLSCKHRTEKSESDQPVSLDNFTQSLLNTWDP-
>BRCA1_HUMAN__P38398 RecName: Full=Breast cancer type 1 susceptibility protein; EC=6.3.2.-; AltName: Full=RING finger protein 53;
-------------------------------------------------------------------------XXXXXXXXXX----------------------------------------------------------------------XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX-1544-SGSLQNRNYPSQEELIKVVDVEEQQLEESGPHDLTETSYLPRQDLEGTPYLESGISLFSDDPES-XXXXXXXXXX-----------------------------------------------------------------------
>LCOR_HUMAN__Q96JN0 RecName: Full=Ligand-dependent corepressor; Short=LCoR; AltName: Full=Mblk1-related protein 2;
-------------------------------------------------------------------------XXXXXXXXXX-0064-PKASPVTTSPTAATTQNPVLSKLLMADQDSPLDLTVRKSQSEPSEQDGVLDLSTKKSPCAGST-XXXXXXXXXX-0083-LSKLLMADQDSPLDLTVRKSQSEPSEQDGVLDLSTKKSPCAGSTSLSHSPGCSSTQGNGRPGRPS-XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX-0064-PKASPVTTSPTAATTQNPVLSKLLMADQDSPLDLTVRKSQSEPSEQDGVLDLSTKKSPCAGSTS-XXXXXXXXXX-----------------------------------------------------------------------
>ATX1L_HUMAN__P0C7T5 RecName: Full=Ataxin-1-like; AltName: Full=Brother of ataxin-1; Short=Brother of ATXN1;
-------------------------------------------------------------------------XXXXXXXXXX-0219-XQAXSPAHSFNKAPSATSPSGQLPHHSSTQPLDLAPGRMPIYYQMSRLPAGYTLHETPPAGAS-XXXXXXXXXX------------------------------------------------------------------------XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------XXXXXXXXXX-----------------------------------------------------------------------
>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;
-0490-CPQASFDKENAFPFPMDNQFSMNGDCVMDKPLDLSDRFSAIQRQEKSQGSETSKNKFRQVTLYEAL-XXXXXXXXXX-0490-CPQASFDKENAFPFPMDNQFSMNGDCVMDKPLDLSDRFSAIQRQEKSQGSETSKNKFRQVTLY-XXXXXXXXXX-0491-PQASFDKENAFPFPMDNQFSMNGDCVMDKPLDLSDRFSAIQRQEKSQGSETSKNKFRQVTLYEAL-XXXXXXXXXX-------------------------------------------------------------------------XXXXXXXXXX-0490-CPQASFDKENAFPFPMDNQFSMNGDCVMDKPLDLSDRFSAIQRQEKSQGSETSKNKFRQVTLYE-XXXXXXXXXX-0490-CPQASFDKENAFPFPMDNQFSMNGDCVMDKPLDLSDRFSAIQRQEKSQGSETSKNKFRQVTLYE-
>ATX1L_HUMAN__P0C7T5 RecName: Full=Ataxin-1-like; AltName: Full=Brother of ataxin-1; Short=Brother of ATXN1;
MKPVHERSQECLPPKKRDLPVTSEDMGRTTSCSTNHTPSSDASEWSRGVVVAGQSQAGARVSLGGDGAEAITGLTVDQYGMLYKVAVPPATFSPTGLPSVVNMSPLPPTFNVASSLIQHPGIHYPPLHYAQLPSTSLQFIGSPYSLPYAVPPNFLPSPLLSPSANLATSHLPHFVPYASLLAEGATPPPQAPSPAHSFNKAPSATSPSGQLPHHSSTQPLDLAPGRMPIYYQMSRLPAGYTLHETPPAGASPVLTPQESQSALEAAAANGGQRPRERNLVRRESEALDSPNSKGEGQGLVPVVECVVDGQLFSGSQTPRVEVAAPAHRGTPDTDLEVQRVVGALASQDYRVVAAQRKEEPSPLNLSHHTPDHQGEGRGSARNPAELAEKSQARGFYPQSHQEPVKHRPLPKAMVVANGNLVPTGTDSGLLPVGSEILVASSLDVQARATFPDKEPTPPPITSSHLPSHFMKGAIIQLATGELKRVEDLQTQDFVRSAEVSGGLKIDSSTVVDIQESQWPGFVMLHFVVGEQQSKVSIEVPPEHPFFVYGQGWSSCSPGRTTQLFSLPCHRLQVGDVCISISLQSLNSNSVSQASCAPPSQLGPPRERPERTVLGSRELCDSEGKSQPAGEGSRVVEPSQPESGAQACWPAPSFQRYSMQGEEARAALLRPSFIPQEVKLSIEGRSNAGK
>BRCA1_HUMAN__P38398 RecName: Full=Breast cancer type 1 susceptibility protein; EC=6.3.2.-; AltName: Full=RING finger protein 53;
MDLSALRVEEVQNVINAMQKILECPICLELIKEPVSTKCDHIFCKFCMLKLLNQKKGPSQCPLCKNDITKRSLQESTRFSQLVEELLKIICAFQLDTGLEYANSYNFAKKENNSPEHLKDEVSIIQSMGYRNRAKRLLQSEPENPSLQETSLSVQLSNLGTVRTLRTKQRIQPQKTSVYIELGSDSSEDTVNKATYCSVGDQELLQITPQGTRDEISLDSAKKAACEFSETDVTNTEHHQPSNNDLNTTEKRAAERHPEKYQGSSVSNLHVEPCGTNTHASSLQHENSSLLLTKDRMNVEKAEFCNKSKQPGLARSQHNRWAGSKETCNDRRTPSTEKKVDLNADPLCERKEWNKQKLPCSENPRDTEDVPWITLNSSIQKVNEWFSRSDELLGSDDSHDGESESNAKVADVLDVLNEVDEYSGSSEKIDLLASDPHEALICKSERVHSKSVESNIEDKIFGKTYRKKASLPNLSHVTENLIIGAFVTEPQIIQERPLTNKLKRKRRPTSGLHPEDFIKKADLAVQKTPEMINQGTNQTEQNGQVMNITNSGHENKTKGDSIQNEKNPNPIESLEKESAFKTKAEPISSSISNMELELNIHNSKAPKKNRLRRKSSTRHIHALELVVSRNLSPPNCTELQIDSCSSSEEIKKKKYNQMPVRHSRNLQLMEGKEPATGAKKSNKPNEQTSKRHDSDTFPELKLTNAPGSFTKCSNTSELKEFVNPSLPREEKEEKLETVKVSNNAEDPKDLMLSGERVLQTERSVESSSISLVPGTDYGTQESISLLEVSTLGKAKTEPNKCVSQCAAFENPKGLIHGCSKDNRNDTEGFKYPLGHEVNHSRETSIEMEESELDAQYLQNTFKVSKRQSFAPFSNPGNAEEECATFSAHSGSLKKQSPKVTFECEQKEENQGKNESNIKPVQTVNITAGFPVVGQKDKPVDNAKCSIKGGSRFCLSSQFRGNETGLITPNKHGLLQNPYRIPPLFPIKSFVKTKCKKNLLEENFEEHSMSPEREMGNENIPSTVSTISRNNIRENVFKEASSSNINEVGSSTNEVGSSINEIGSSDENIQAELGRNRGPKLNAMLRLGVLQPEVYKQSLPGSNCKHPEIKKQEYEEVVQTVNTDFSPYLISDNLEQPMGSSHASQVCSETPDDLLDDGEIKEDTSFAENDIKESSAVFSKSVQKGELSRSPSPFTHTHLAQGYRRGAKKLESSEENLSSEDEELPCFQHLLFGKVNNIPSQSTRHSTVATECLSKNTEENLLSLKNSLNDCSNQVILAKASQEHHLSEETKCSASLFSSQCSELEDLTANTNTQDPFLIGSSKQMRHQSESQGVGLSDKELVSDDEERGTGLEENNQEEQSMDSNLGEAASGCESETSVSEDCSGLSSQSDILTTQQRDTMQHNLIKLQQEMAELEAVLEQHGSQPSNSYPSIISDSSALEDLRNPEQSTSEKAVLTSQKSSEYPISQNPEGLSADKFEVSADSSTSKNKEPGVERSSPSKCPSLDDRWYMHSCSGSLQNRNYPSQEELIKVVDVEEQQLEESGPHDLTETSYLPRQDLEGTPYLESGISLFSDDPESDPSEDRAPESARVGNIPSSTSALKVPQLKVAESAQSPAAAHTTDTAGYNAMEESVSREKPELTASTERVNKRMSMVVSGLTPEEFMLVYKFARKHHITLTNLITEETTHVVMKTDAEFVCERTLKYFLGIAGGKWVVSYFWVTQSIKERKMLNEHDFEVRGDVVNGRNHQGPKRARESQDRKIFRGLEICCYGPFTNMPTDQLEWMVQLCGASVVKELSSFTLGTGVHPIVVVQPDAWTEDNGFHAIGQMCEAPVVTREWVLDSVALYQCQELDTYLIPQIPHSHY
>CBX4_HUMAN__O00257 RecName: Full=E3 SUMO-protein ligase CBX4; EC=6.3.2.-; AltName: Full=Chromobox protein homolog 4; AltName: Full=Polycomb 2 homolog; Short=Pc2; Short=hPc2;
MELPAVGEHVFAVESIEKKRIRKGRVEYLVKWRGWSPKYNTWEPEENILDPRLLIAFQNRERQEQLMGYRKRGPKPKPLVVQVPTFARRSNVLTGLQDSSTDNRAKLDLGAQGKGQGHQYELNSKKHHQYQPHSKERAGKPPPPGKSGKYYYQLNSKKHHPYQPDPKMYDLQYQGGHKEAPSPTCPDLGAKSHPPDKWAQGAGAKGYLGAVKPLAGAAGAPGKGSEKGPPNGMMPAPKEAVTGNGIGGKMKIVKNKNKNGRIVIVMSKYMENGMQAVKIKSGEVAEGEARSPSHKKRAADERHPPADRTFKKAAGAEEKKVEAPPKRREEEVSGVSDPQPQDAGSRKLSPTKEAFGEQPLQLTTKPDLLAWDPARNTHPPSHHPHPHPHHHHHHHHHHHHAVGLNLSHVRKRCLSETHGEREPCKKRLTARSISTPTCLGGSPAAERPADLPPAAALPQPEVILLDSDLDEPIDLRCVKTRSEAGEPPSSLQVKPETPASAAVAVAAAAAPTTTAEKPPAEAQDEPAESLSEFKPFFGNIIITDVTANCLTVTFKEYVTV
>CHD3_HUMAN__Q12873 RecName: Full=Chromodomain-helicase-DNA-binding protein 3; Short=CHD-3; EC=3.6.4.12; AltName: Full=ATP-dependent helicase CHD3; AltName: Full=Mi-2 autoantigen 240 kDa protein; AltName: Full=Mi2-alpha; AltName: Full=Zinc finger helicase; Short=hZFH;
MKAADTVILWARSKNDQLRISFPPGLCWGDRMPDKDDIRLLPSALGVKKRKRGPKKQKENKPGKPRKRKKRDSEEEFGSERDEYREKSESGGSEYGTGPGRKRRRKHREKKEKKTKRRKKGEGDGGQKQVEQKSSATLLLTWGLEDVEHVFSEEDYHTLTNYKAFSQFMRPLIAKKNPKIPMSKMMTILGAKWREFSANNPFKGSAAAVAAAAAAAAAAVAEQVSAAVSSATPIAPSGPPALPPPPAADIQPPPIRRAKTKEGKGPGHKRRSKSPRVPDGRKKLRGKKMAPLKIKLGLLGGKRKKGGSYVFQSDEGPEPEAEESDLDSGSVHSASGRPDGPVRTKKLKRGRPGRKKKKVLGCPAVAGEEEVDGYETDHQDYCEVCQQGGEIILCDTCPRAYHLVCLDPELDRAPEGKWSCPHCEKEGVQWEAKEEEEEYEEEGEEEGEKEEEDDHMEYCRVCKDGGELLCCDACISSYHIHCLNPPLPDIPNGEWLCPRCTCPVLKGRVQKILHWRWGEPPVAVPAPQQADGNPDVPPPRPLQGRSEREFFVKWVGLSYWHCSWAKELQLEIFHLVMYRNYQRKNDMDEPPPLDYGSGEDDGKSDKRKVKDPHYAEMEEKYYRFGIKPEWMTVHRIINHSVDKKGNYHYLVKWRDLPYDQSTWEEDEMNIPEYEEHKQSYWRHRELIMGEDPAQPRKYKKKKKELQGDGPPSSPTNDPTVKYETQPRFITATGGTLHMYQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLYSLYKEGHTKGPFLVSAPLSTIINWEREFQMWAPKFYVVTYTGDKDSRAIIRENEFSFEDNAIKGGKKAFKMKREAQVKFHVLLTSYELITIDQAALGSIRWACLVVDEAHRLKNNQSKFFRVLNGYKIDHKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEFADISKEDQIKKLHDLLGPHMLRRLKADVFKNMPAKTELIVRVELSPMQKKYYKYILTRNFEALNSRGGGNQVSLLNIMMDLKKCCNHPYLFPVAAMESPKLPSGAYEGGALIKSSGKLMLLQKMLRKLKEQGHRVLIFSQMTKMLDLLEDFLDYEGYKYERIDGGITGALRQEAIDRFNAPGAQQFCFLLSTRAGGLGINLATADTVIIFDSDWNPHNDIQAFSRAHRIGQANKVMIYRFVTRASVEERITQVAKRKMMLTHLVVRPGLGSKAGSMSKQELDDILKFGTEELFKDENEGENKEEDSSVIHYDNEAIARLLDRNQDATEDTDVQNMNEYLSSFKVAQYVVREEDKIEEIEREIIKQEENVDPDYWEKLLRHHYEQQQEDLARNLGKGKRVRKQVNYNDAAQEDQDNQSEYSVGSEEEDEDFDERPEGRRQSKRQLRNEKDKPLPPLLARVGGNIEVLGFNTRQRKAFLNAVMRWGMPPQDAFTTQWLVRDLRGKTEKEFKAYVSLFMRHLCEPGADGSETFADGVPREGLSRQQVLTRIGVMSLVKKKVQEFEHINGRWSMPELMPDPSADSKRSSRASSPTKTSPTTPEASATNSPCTSKPATPAPSEKGEGIRTPLEKEEAENQEEKPEKNSRIGEKMETEADAPSPAPSLGERLEPRKIPLEDEVPGVPGEMEPEPGYRGDREKSATESTPGERGEEKPLDGQEHRERPEGETGDLGKREDVKGDRELRPGPRDEPRSNGRREEKTEKPRFMFNIADGGFTELHTLWQNEERAAISSGKLNEIWHRRHDYWLLAGIVLHGYARWQDIQNDAQFAIINEPFKTEANKGNFLEMKNKFLARRFKLLEQALVIEEQLRRAAYLNLSQEPAHPAMALHARFAEAECLAESHQHLSKESLAGNKPANAVLHKVLNQLEELLSDMKADVTRLPATLSRIPPIAARLQMSERSILSRLASKGTEPHPTPAYPPGPYATPPGYGAAFSAAPVGALAAAGANYSQMPAGSFITAATNGPPVLVKKEKEMVGALVSDGLDRKEPRAGEVICIDD
>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
>CTBP1_HUMAN__Q13363 RecName: Full=C-terminal-binding protein 1; Short=CtBP1; EC=1.1.1.-;
MGSSHLLNKGLPLGVRPPIMNGPLHPRPLVALLDGRDCTVEMPILKDVATVAFCDAQSTQEIHEKVLNEAVGALMYHTITLTREDLEKFKALRIIVRIGSGFDNIDIKSAGDLGIAVCNVPAASVEETADSTLCHILNLYRRATWLHQALREGTRVQSVEQIREVASGAARIRGETLGIIGLGRVGQAVALRAKAFGFNVLFYDPYLSDGVERALGLQRVSTLQDLLFHSDCVTLHCGLNEHNHHLINDFTVKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHESEPFSFSQGPLKDAPNLICTPHAAWYSEQASIEMREEAAREIRRAITGRIPDSLKNCVNKDHLTAATHWASMDPAVVHPELNGAAYRYPPGVVGVAPTGIPAAVEGIVPSAMSLSHGLPPVAHPPHAPSPGQTVKPEADRDHASDQL
>CTNA1_HUMAN__P35221 RecName: Full=Catenin alpha-1; AltName: Full=Alpha E-catenin; AltName: Full=Cadherin-associated protein; AltName: Full=Renal carcinoma antigen NY-REN-13;
MTAVHAGNINFKWDPKSLEIRTLAVERLLEPLVTQVTTLVNTNSKGPSNKKRGRSKKAHVLAASVEQATENFLEKGDKIAKESQFLKEELVAAVEDVRKQGDLMKAAAGEFADDPCSSVKRGNMVRAARALLSAVTRLLILADMADVYKLLVQLKVVEDGILKLRNAGNEQDLGIQYKALKPEVDKLNIMAAKRQQELKDVGHRDQMAAARGILQKNVPILYTASQACLQHPDVAAYKANRDLIYKQLQQAVTGISNAAQATASDDASQHQGGGGGELAYALNNFDKQIIVDPLSFSEERFRPSLEERLESIISGAALMADSSCTRDDRRERIVAECNAVRQALQDLLSEYMGNAGRKERSDALNSAIDKMTKKTRDLRRQLRKAVMDHVSDSFLETNVPLLVLIEAAKNGNEKEVKEYAQVFREHANKLIEVANLACSISNNEEGVKLVRMSASQLEALCPQVINAALALAAKPQSKLAQENMDLFKEQWEKQVRVLTDAVDDITSIDDFLAVSENHILEDVNKCVIALQEKDVDGLDRTAGAIRGRAARVIHVVTSEMDNYEPGVYTEKVLEATKLLSNTVMPRFTEQVEAAVEALSSDPAQPMDENEFIDASRLVYDGIRDIRKAVLMIRTPEELDDSDFETEDFDVRSRTSVQTEDDQLIAGQSARAIMAQLPQEQKAKIAEQVASFQEEKSKLDAEVSKWDDSGNDIIVLAKQMCMIMMEMTDFTRGKGPLKNTSDVISAAKKIAEAGSRMDKLGRTIADHCPDSACKQDLLAYLQRIALYCHQLNICSKVKAEVQNLGGELVVSGVDSAMSLIQAAKNLMNAVVQTVKASYVASTKYQKSQGMASLNLPAVSWKMKAPEKKPLVKREKQDETQTKIKRASQKKHVNPVQALSEFKAMDSI
>E1A_ADE02__P03254 RecName: Full=Early E1A protein {ECO:0000305}; AltName: Full=Early E1A 32 kDa protein;
MRHIICHGGVITEEMAASLLDQLIEEVLADNLPPPSHFEPPTLHELYDLDVTAPEDPNEEAVSQIFPDSVMLAVQEGIDLLTFPPAPGSPEPPHLSRQPEQPEQRALGPVSMPNLVPEVIDLTCHEAGFPPSDDEDEEGEEFVLDYVEHPGHGCRSCHYHRRNTGDPDIMCSLCYMRTCGMFVYSPVSEPEPEPEPEPEPARPTRRPKLVPAILRRPTSPVSRECNSSTDSCDSGPSNTPPEIHPVVPLCPIKPVAVRVGGRRQAVECIEDLLNESGQPLDLSCKRPRP
>FOG1_HUMAN__Q8IX07 RecName: Full=Zinc finger protein ZFPM1; AltName: Full=Friend of GATA protein 1; Short=FOG-1; Short=Friend of GATA 1; AltName: Full=Zinc finger protein 89A; AltName: Full=Zinc finger protein multitype 1;
MSRRKQSNPRQIKRSLGDMEAREEVQLVGASHMEQKATAPEAPSPPSADVNSPPPLPPPTSPGGPKELEGQEPEPRPTEEEPGSPWSGPDELEPVVQDGQRRIRARLSLATGLSWGPFHGSVQTRASSPRQAEPSPALTLLLVDEACWLRTLPQALTEAEANTEIHRKDDALWCRVTKPVPAGGLLSVLLTAEPHSTPGHPVKKEPAEPTCPAPAHDLQLLPQQAGMASILATAVINKDVFPCKDCGIWYRSERNLQAHLLYYCASRQGTGSPAAAATDEKPKETYPNERVCPFPQCRKSCPSASSLEIHMRSHSGERPFVCLICLSAFTTKANCERHLKVHTDTLSGVCHSCGFISTTRDILYSHLVTNHMVCQPGSKGEIYSPGAGHPATKLPPDSLGSFQQQHTALQGPLASADLGLAPTPSPGLDRKALAEATNGEARAEPLAQNGGSSEPPAAPRSIKVEAVEEPEAAPILGPGEPGPQAPSRTPSPRSPAPARVKAELSSPTPGSSPVPGELGLAGALFLPQYVFGPDAAPPASEILAKMSELVHSRLQQGAGAGAGGAQTGLFPGAPKGATCFECEITFSNVNNYYVHKRLYCSGRRAPEDAPAARRPKAPPGPARAPPGQPAEPDAPRSSPGPGAREEGAGGAATPEDGAGGRGSEGSQSPGSSVDDAEDDPSRTLCEACNIRFSRHETYTVHKRYYCASRHDPPPRRPAAPPGPPGPAAPPAPSPAAPVRTRRRRKLYELHAAGAPPPPPPGHAPAPESPRPGSGSGSGPGLAPARSPGPAADGPIDLSKKPRRPLPGAPAPALADYHECTACRVSFHSLEAYLAHKKYSCPAAPPPGALGLPAAACPYCPPNGPVRGDLLEHFRLAHGLLLGAPLAGPGVEARTPADRGPSPAPAPAASPQPGSRGPRDGLGPEPQEPPPGPPPSPAAAPEAVPPPPAPPSYSDKGVQTPSKGTPAPLPNGNHRYCRLCNIKFSSLSTFIAHKKYYCSSHAAEHVK
>HDAC2_HUMAN__Q92769 RecName: Full=Histone deacetylase 2; Short=HD2; EC=3.5.1.98;
MAYSQGGGKKKVCYYYDGDIGNYYYGQGHPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKATAEEMTKYHSDEYIKFLRSIRPDNMSEYSKQMQRFNVGEDCPVFDGLFEFCQLSTGGSVAGAVKLNRQQTDMAVNWAGGLHHAKKSEASGFCYVNDIVLAILELLKYHQRVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKYGEYFPGTGDLRDIGAGKGKYYAVNFPMRDGIDDESYGQIFKPIISKVMEMYQPSAVVLQCGADSLSGDRLGCFNLTVKGHAKCVEVVKTFNLPLLMLGGGGYTIRNVARCWTYETAVALDCEIPNELPYNDYFEYFGPDFKLHISPSNMTNQNTPEYMEKIKQRLFENLRMLPHAPGVQMQAIPEDAVHEDSGDEDGEDPDKRISIRASDKRIACDEEFSDSEDEGEGGRRNVADHKKGAKKARIEEDKKETEDKKTDVKEEDKSKDNSGEKTDTKGTKSEQLSNP
>HIC1_HUMAN__Q14526 RecName: Full=Hypermethylated in cancer 1 protein; Short=Hic-1; AltName: Full=Zinc finger and BTB domain-containing protein 29;
MTFPEADILLKSGECAGQTMLDTMEAPGHSRQLLLQLNNQRTKGFLCDVIIVVQNALFRAHKNVLAASSAYLKSLVVHDNLLNLDHDMVSPAVFRLVLDFIYTGRLADGAEAAAAAAVAPGAEPSLGAVLAAASYLQIPDLVALCKKRLKRHGKYCHLRGGGGGGGGYAPYGRPGRGLRAATPVIQACYPSPVGPPPPPAAEPPSGPEAAVNTHCAELYASGPGPAAALCASERRCSPLCGLDLSKKSPPGSAAPERPLAERELPPRPDSPPSAGPAAYKEPPLALPSLPPLPFQKLEEAAPPSDPFRGGSGSPGPEPPGRPDGPSLLYRWMKHEPGLGSYGDELGRERGSPSERCEERGGDAAVSPGGPPLGLAPPPRYPGSLDGPGAGGDGDDYKSSSEETGSSEDPSPPGGHLEGYPCPHLAYGEPESFGDNLYVCIPCGKGFPSSEQLNAHVEAHVEEEEALYGRAEAAEVAAGAAGLGPPFGGGGDKVAGAPGGLGELLRPYRCASCDKSYKDPATLRQHEKTHWLTRPYPCTICGKKFTQRGTMTRHMRSHLGLKPFACDACGMRFTRQYRLTEHMRIHSGEKPYECQVCGGKFAQQRNLISHMKMHAVGGAAGAAGALAGLGGLPGVPGPDGKGKLDFPEGVFAVARLTAEQLSLKQQDKAAAAELLAQTTHFLHDPKVALESLYPLAKFTAELGLSPDKAAEVLSQGAHLAAGPDGRTIDRFSPT
>IKZF1_HUMAN__Q13422 RecName: Full=DNA-binding protein Ikaros; AltName: Full=Ikaros family zinc finger protein 1; AltName: Full=Lymphoid transcription factor LyF-1;
MDADEGQDMSQVSGKESPPVSDTPDEGDEPMPIPEDLSTTSGGQQSSKSDRVVASNVKVETQSDEENGRACEMNGEECAEDLRMLDASGEKMNGSHRDQGSSALSGVGGIRLPNGKLKCDICGIICIGPNVLMVHKRSHTGERPFQCNQCGASFTQKGNLLRHIKLHSGEKPFKCHLCNYACRRRDALTGHLRTHSVGKPHKCGYCGRSYKQRSSLEEHKERCHNYLESMGLPGTLYPVIKEETNHSEMAEDLCKIGSERSLVLDRLASNVAKRKSSMPQKFLGDKGLSDTPYDSSASYEKENEMMKSHVMDQAINNAINYLGAESLRPLVQTPPGGSEVVPVISPMYQLHKPLAEGTPRSNHSAQDSAVENLLLLSKAKLVPSEREASPSNSCQDSTDTESNNEEQRSGLIYLTNHIAPHARNGLSLKEEHRAYDLLRAASENSQDALRVVSTSGEQMKVYKCEHCRVLFLDHVMYTIHMGCHGFRDPFECNMCGYHSQDRYEFSSHITRGEHRFHMS
>ITF2_HUMAN__P15884 RecName: Full=Transcription factor 4; Short=TCF-4; AltName: Full=Class B basic helix-loop-helix protein 19; Short=bHLHb19; AltName: Full=Immunoglobulin transcription factor 2; Short=ITF-2; AltName: Full=SL3-3 enhancer factor 2; Short=SEF-2;
MHHQQRMAALGTDKELSDLLDFSAMFSPPVSSGKNGPTSLASGHFTGSNVEDRSSSGSWGNGGHPSPSRNYGDGTPYDHMTSRDLGSHDNLSPPFVNSRIQSKTERGSYSSYGRESNLQGCHQQSLLGGDMDMGNPGTLSPTKPGSQYYQYSSNNPRRRPLHSSAMEVQTKKVRKVPPGLPSSVYAPSASTADYNRDSPGYPSSKPATSTFPSSFFMQDGHHSSDPWSSSSGMNQPGYAGMLGNSSHIPQSSSYCSLHPHERLSYPSHSSADINSSLPPMSTFHRSGTNHYSTSSCTPPANGTDSIMANRGSGAAGSSQTGDALGKALASIYSPDHTNNSFSSNPSTPVGSPPSLSAGTAVWSRNGGQASSSPNYEGPLHSLQSRIEDRLERLDDAIHVLRNHAVGPSTAMPGGHGDMHGIIGPSHNGAMGGLGSGYGTGLLSANRHSLMVGTHREDGVALRGSHSLLPNQVPVPQLPVQSATSPDLNPPQDPYRGMPPGLQGQSVSSGSSEIKSDDEGDENLQDTKSSEDKKLDDDKKDIKSITSNNDDEDLTPEQKAEREKERRMANNARERLRVRDINEAFKELGRMVQLHLKSDKPQTKLLILHQAVAVILSLEQQVRERNLNPKAACLKRREEEKVSSEPPPLSLAGPHPGMGDASNHMGQM
>KAT2B_HUMAN__Q92831 RecName: Full=Histone acetyltransferase KAT2B; EC=2.3.1.48; AltName: Full=Histone acetyltransferase PCAF; Short=Histone acetylase PCAF; AltName: Full=Lysine acetyltransferase 2B; AltName: Full=P300/CBP-associated factor; Short=P/CAF;
MSEAGGAGPGGCGAGAGAGAGPGALPPQPAALPPAPPQGSPCAAAAGGSGACGPATAVAAAGTAEGPGGGGSARIAVKKAQLRSAPRAKKLEKLGVYSACKAEESCKCNGWKNPNPSPTPPRADLQQIIVSLTESCRSCSHALAAHVSHLENVSEEEMNRLLGIVLDVEYLFTCVHKEEDADTKQVYFYLFKLLRKSILQRGKPVVEGSLEKKPPFEKPSIEQGVNNFVQYKFSHLPAKERQTIVELAKMFLNRINYWHLEAPSQRRLRSPNDDISGYKENYTRWLCYCNVPQFCDSLPRYETTQVFGRTLLRSVFTVMRRQLLEQARQEKDKLPLEKRTLILTHFPKFLSMLEEEVYSQNSPIWDQDFLSASSRTSQLGIQTVINPPPVAGTISYNSTSSSLEQPNAGSSSPACKASSGLEANPGEKRKMTDSHVLEEAKKPRVMGDIPMELINEVMSTITDPAAMLGPETNFLSAHSARDEAARLEERRGVIEFHVVGNSLNQKPNKKILMWLVGLQNVFSHQLPRMPKEYITRLVFDPKHKTLALIKDGRVIGGICFRMFPSQGFTEIVFCAVTSNEQVKGYGTHLMNHLKEYHIKHDILNFLTYADEYAIGYFKKQGFSKEIKIPKTKYVGYIKDYEGATLMGCELNPRIPYTEFSVIIKKQKEIIKKLIERKQAQIRKVYPGLSCFKDGVRQIPIESIPGIRETGWKPSGKEKSKEPRDPDQLYSTLKSILQQVKSHQSAWPFMEPVKRTEAPGYYEVIRFPMDLKTMSERLKNRYYVSKKLFMADLQRVFTNCKEYNPPESEYYKCANILEKFFFSKIKEAGLIDK
>LCORL_HUMAN__Q8N3X6 RecName: Full=Ligand-dependent nuclear receptor corepressor-like protein; Short=LCoR-like protein;
MDKGRERMAAAAAAAAAAAAAAQCRSPRCAAERRGFRRELDSWRHRLMHCVGFESILEGLYGPRLRRDLSLFEDCEPEELTDWSMDEKCSFCNLQREAVSDCIPSLDSSQSTPTEELSSQGQSNTDKIECQAENYLNALFRKKDLPQNCDPNIPLVAQELMKKMIRQFAIEYISKSGKTQENRNGSIGPSIVCKSIQMNQAENSLQEEQEGPLDLTVNRMQEQNTQQGDGVLDLSTKKTSIKSEESSICDPSSENSVAGRLHRNREDYVERSAEFADGLLSKALKDIQSGALDINKAGILYGIPQKTLLLHLEALPAGKPASFKNKTRDFHDSYSYKDSKETCAVLQKVALWARAQAERTEKSKLNLLETSEIKFPTASTYLHQLTLQKMVTQFKEKNESLQYETSNPTVQLKIPQLRVSSVSKSQPDGSGLLDVMYQVSKTSSVLEGSALQKLKNILPKQNKIECSGPVTHSSVDSYFLHGDLSPLCLNSKNGTVDGTSENTEDGLDRKDSKQPRKKRGRYRQYDHEIMEEAIAMVMSGKMSVSKAQGIYGVPHSTLEYKVKERSGTLKTPPKKKLRLPDTGLYNMTDSGTGSCKNSSKPV
>LCOR_HUMAN__Q96JN0 RecName: Full=Ligand-dependent corepressor; Short=LCoR; AltName: Full=Mblk1-related protein 2;
MQRMIQQFAAEYTSKNSSTQDPSQPNSTKNQSLPKASPVTTSPTAATTQNPVLSKLLMADQDSPLDLTVRKSQSEPSEQDGVLDLSTKKSPCAGSTSLSHSPGCSSTQGNGRPGRPSQYRPDGLRSGDGVPPRSLQDGTREGFGHSTSLKVPLARSLQISEELLSRNQLSTAASLGPSGLQNHGQHLILSREASWAKPHYEFNLSRMKFRGNGALSNISDLPFLAENSAFPKMALQAKQDGKKDVSHSSPVDLKIPQVRGMDLSWESRTGDQYSYSSLVMGSQTESALSKKLRAILPKQSRKSMLDAGPDSWGSDAEQSTSGQPYPTSDQEGDPGSKQPRKKRGRYRQYNSEILEEAISVVMSGKMSVSKAQSIYGIPHSTLEYKVKERLGTLKNPPKKKMKLMRSEGPDVSVKIELDPQGEAAQSANESKNE
>MDS1_HUMAN__Q13465 RecName: Full=MDS1 and EVI1 complex locus protein MDS1; AltName: Full=Myelodysplasia syndrome 1 protein; AltName: Full=Myelodysplasia syndrome-associated protein 1;
MRSKGRARKLATNNECVYGNYPEIPLEEMPDADGVASTPSLNIQEPCSPATSSEAFTPKEGSPYKAPIYIPDDIPIPAEFELRESNMPGAGLGIWTKRKIEVGEKFGPYVGEQRSNLKDPSYGWEVHLPRSRRVSVHSWLYLGKRSSDVGIAFSQADVYMPGLQCAFLS
>NOL4L_HUMAN__Q96MY1 RecName: Full=Nucleolar protein 4-like;
MSDSTWMSADPHLASSLSPSQDERMRSPQNLHSQEDDDSSSESGSGNGSSTLNPSTSSSTQGDPAFPEMNGNGAVAPMDFTTAAEDQPINLCDKLPPATALGTASYPSDGCGADGLRSRVKYGVKTTPESPPYSSGSYDSIKTEVSGCPEDLTVGRAPTADDDDDDHDDHEDNDKMNDSEGMDPERLKAFNMFVRLFVDENLDRMVPISKQPKEKIQAIIESCSRQFPEFQERARKRIRTYLKSCRRMKKNGMEMTRPTPPHLTSAMAENILAAACESETRKAAKRMRLEIYQSSQDEPIALDKQHSRDSAAITHSTYSLPASSYSQDPVYANGGLNYSYRGYGALSSNLQPPASLQTGNHSNGPTDLSMKGGASTTSTTPTPTPSSTSTSRPVPTAQLSPTEISAVRQLIAGYRESAAFLLRSADELENLILQQN
>NRIP1_HUMAN__P48552 RecName: Full=Nuclear receptor-interacting protein 1; AltName: Full=Nuclear factor RIP140; AltName: Full=Receptor-interacting protein 140;
MTHGEELGSDVHQDSIVLTYLEGLLMHQAAGGSGTAVDKKSAGHNEEDQNFNISGSAFPTCQSNGPVLNTHTYQGSGMLHLKKARLLQSSEDWNAAKRKRLSDSIMNLNVKKEALLAGMVDSVPKGKQDSTLLASLLQSFSSRLQTVALSQQIRQSLKEQGYALSHDSLKVEKDLRCYGVASSHLKTLLKKSKVKDQKPDTNLPDVTKNLIRDRFAESPHHVGQSGTKVMSEPLSCAARLQAVASMVEKRASPATSPKPSVACSQLALLLSSEAHLQQYSREHALKTQNANQAASERLAAMARLQENGQKDVGSYQLPKGMSSHLNGQARTSSSKLMASKSSATVFQNPMGIIPSSPKNAGYKNSLERNNIKQAANNSLLLHLLKSQTIPKPMNGHSHSERGSIFEESSTPTTIDEYSDNNPSFTDDSSGDESSYSNCVPIDLSCKHRTEKSESDQPVSLDNFTQSLLNTWDPKVPDVDIKEDQDTSKNSKLNSHQKVTLLQLLLGHKNEENVEKNTSPQGVHNDVSKFNTQNYARTSVIESPSTNRTTPVSTPPLLTSSKAGSPINLSQHSLVIKWNSPPYVCSTQSEKLTNTASNHSMDLTKSKDPPGEKPAQNEGAQNSATFSASKLLQNLAQCGMQSSMSVEEQRPSKQLLTGNTDKPIGMIDRLNSPLLSNKTNAVEENKAFSSQPTGPEPGLSGSEIENLLERRTVLQLLLGNPNKGKSEKKEKTPLRDESTQEHSERALSEQILMVKIKSEPCDDLQIPNTNVHLSHDAKSAPFLGMAPAVQRSAPALPVSEDFKSEPVSPQDFSFSKNGLLSRLLRQNQDSYLADDSDRSHRNNEMALLESKNLCMVPKKRKLYTEPLENPFKKMKNNIVDAANNHSAPEVLYGSLLNQEELKFSRNDLEFKYPAGHGSASESEHRSWARESKSFNVLKQLLLSENCVRDLSPHRSNSVADSKKKGHKNNVTNSKPEFSISSLNGLMYSSTQPSSCMDNRTFSYPGVVKTPVSPTFPEHLGCAGSRPESGLLNGCSMPSEKGPIKWVITDAEKNEYEKDSPRLTKTNPILYYMLQKGGNSVTSRETQDKDIWREASSAESVSQVTAKEELLPTAETKASFFNLRSPYNSHMGNNASRPHSANGEVYGLLGSVLTIKKESE
>RBBP5_HUMAN__Q15291 RecName: Full=Retinoblastoma-binding protein 5; Short=RBBP-5; AltName: Full=Retinoblastoma-binding protein RBQ-3;
MNLELLESFGQNYPEEADGTLDCISMALTCTFNRWGTLLAVGCNDGRIVIWDFLTRGIAKIISAHIHPVCSLCWSRDGHKLVSASTDNIVSQWDVLSGDCDQRFRFPSPILKVQYHPRDQNKVLVCPMKSAPVMLTLSDSKHVVLPVDDDSDLNVVASFDRRGEYIYTGNAKGKILVLKTDSQDLVASFRVTTGTSNTTAIKSIEFARKGSCFLINTADRIIRVYDGREILTCGRDGEPEPMQKLQDLVNRTPWKKCCFSGDGEYIVAGSARQHALYIWEKSIGNLVKILHGTRGELLLDVAWHPVRPIIASISSGVVSIWAQNQVENWSAFAPDFKELDENVEYEERESEFDIEDEDKSEPEQTGADAAEDEEVDVTSVDPIAAFCSSDEELEDSKALLYLPIAPEVEDPEENPYGPPPDAVQTSLMDEGASSEKKRQSSADGSQPPKKKPKTTNIELQGVPNDEVHPLLGVKGDGKSKKKQAGRPKGSKGKEKDSPFKPKLYKGDRGLPLEGSAKGKVQAELSQPLTAGGAISELL
>SOBP_HUMAN__A7XYQ1 RecName: Full=Sine oculis-binding protein homolog; AltName: Full=Jackson circler protein 1;
MAEMEKEGRPPENKRSRKPAHPVKREINEEMKNFAENTMNELLGWYGYDKVELKDGEDIEFRSYPTDGESRQHISVLKENSLPKPKLPEDSVISPYNISTGYSGLATGNGLSDSPAGSKDHGSVPIIVPLIPPPFIKPPAEDDVSNVQIMCAWCQKVGIKRYSLSMGSEVKSFCSEKCFAACRRAYFKRNKARDEDGHAENFPQQHYAKETPRLAFKNNCELLVCDWCKHIRHTKEYLDFGDGERRLQFCSAKCLNQYKMDIFYKETQANLPAGLCSTLHPPMENKAEGTGVQLLTPDSWNIPLTDARRKAPSPVATAGQSQGPGPSASTTVSPSDTANCSVTKIPTPVPKSIPISETPNIPPVSVQPPASIGPPLGVPPRSPPMVMTNRGPVPLPIFMEQQIMQQIRPPFIRGPPHHASNPNSPLSNPMLPGIGPPPGGPRNLGPTSSPMHRPMLSPHIHPPSTPTMPGNPPGLLPPPPPGAPLPSLPFPPVSMMPNGPMPVPQMMNFGLPSLAPLVPPPTLLVPYPVIVPLPVPIPIPIPIPHVSDSKPPNGFSSNGENFIPNAPGDSAAAGGKPSGHSLSPRDSKQGSSKSADSPPGCSGQALSLAPTPAEHGRSEVVDLTRRAGSPPGPPGAGGQLGFPGVLQGPQDGVIDLTVGHRARLHNVIHRALHAHVKAEREPSAAERRTCGGCRDGHCSPPAAGDPGPGAPAGPEAAAACNVIVNGTRGAAAEGAKSAEPPPEQPPPPPPPAPPKKLLSPEEPAVSELESVKENNCASNCHLDGEAAKKLMGEEALAGGDKSDPNLNNPADEDHAYALRMLPKTGCVIQPVPKPAEKAAMAPCIISSPMLSAGPEDLEPPLKRRCLRIRNQNK
>ZN219_HUMAN__Q9P2Y4 RecName: Full=Zinc finger protein 219;
MEGSRPRAPSGHLAPSPPAFDGELDLQRYSNGPAVSAGSLGMGAVSWSESRAGERRFPCPVCGKRFRFNSILALHLRAHPGAQAFQCPHCGHRAAQRALLRSHLRTHQPERPRSPAARLLLELEERALLREARLGRARSSGGMQATPATEGLARPQAPSSSAFRCPYCKGKFRTSAERERHLHILHRPWKCGLCSFGSSQEEELLHHSLTAHGAPERPLAATSAAPPPQPQPQPPPQPEPRSVPQPEPEPEPEREATPTPAPAAPEEPPAPPEFRCQVCGQSFTQSWFLKGHMRKHKASFDHACPVCGRCFKEPWFLKNHMKVHASKLGPLRAPGPASGPARAPQPPDLGLLAYEPLGPALLLAPAPTPAERREPPSLLGYLSLRAGEGRPNGEGAEPGPGRSFGGFRPLSSALPARARRHRAEEPEEEEEVVEAEEETWARGRSLGSLASLHPRPGEGPGHSASAAGAQARSTATQEENGLLVGGTRPEGGRGATGKDCPFCGKSFRSAHHLKVHLRVHTGERPYKCPHCDYAGTQSGSLKYHLQRHHREQRSGAGPGPPPEPPPPSQRGSAPQSGAKPSPQPATWVEGASSPRPPSSGAGPGSRRKPASPGRTLRNGRGGEAEPLDLSLRAGPGGEAGPGGALHRCLFCPFATGAPELMALHLQVHHSRRARGRRPPQADASPPYARVPSGETPPSPSQEGEEGSGLSRPGEAGLGGQER
ID   ATX1L_HUMAN             Reviewed;         689 AA.
AC   P0C7T5;
DT   22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-JUL-2008, sequence version 1.
DT   11-NOV-2015, entry version 66.
DE   RecName: Full=Ataxin-1-like;
DE   AltName: Full=Brother of ataxin-1;
DE            Short=Brother of ATXN1;
GN   Name=ATXN1L; Synonyms=BOAT, BOAT1;
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 GENOMIC DNA].
RX   PubMed=15616553; DOI=10.1038/nature03187;
RA   Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X.,
RA   Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A.,
RA   Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.,
RA   Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L.,
RA   Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A.,
RA   Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D.,
RA   Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J.,
RA   Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA   Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I.,
RA   Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W.,
RA   Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A.,
RA   Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S.,
RA   Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA   Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA   Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L.,
RA   Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A.,
RA   Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L.,
RA   Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N.,
RA   Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M.,
RA   Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L.,
RA   Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D.,
RA   Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P.,
RA   Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M.,
RA   Rubin E.M., Pennacchio L.A.;
RT   "The sequence and analysis of duplication-rich human chromosome 16.";
RL   Nature 432:988-994(2004).
RN   [2]
RP   INTERACTION WITH NCOR2 AND ATXN1, SUBCELLULAR LOCATION, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=16121196; DOI=10.1038/sj.emboj.7600785;
RA   Mizutani A., Wang L., Rajan H., Vig P.J.S., Alaynick W.A.,
RA   Thaler J.P., Tsai C.-C.;
RT   "Boat, an AXH domain protein, suppresses the cytotoxicity of mutant
RT   ataxin-1.";
RL   EMBO J. 24:3339-3351(2005).
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-284, 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   [5]
RP   FUNCTION, AND INTERACTION WITH RBPJ.
RX   PubMed=21475249; DOI=10.1038/embor.2011.49;
RA   Tong X., Gui H., Jin F., Heck B.W., Lin P., Ma J., Fondell J.D.,
RA   Tsai C.C.;
RT   "Ataxin-1 and Brother of ataxin-1 are components of the Notch
RT   signalling pathway.";
RL   EMBO Rep. 12:428-435(2011).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-361, 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: Chromatin-binding factor that repress Notch signaling in
CC       the absence of Notch intracellular domain by acting as a CBF1
CC       corepressor. Binds to the HEY promoter and might assist, along
CC       with NCOR2, RBPJ-mediated repression. Can suppress ATXN1
CC       cytotoxicity in spinocerebellar ataxia type 1 (SCA1) (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer. Interacts with CIC (By similarity). Interacts
CC       (via AXH domain) with NCOR2. Interacts with ATXN1. Directly
CC       interacts with RBPJ; this interaction is disrupted in the presence
CC       of Notch intracellular domain. Competes with ATXN1 for RBPJ-
CC       binding. {ECO:0000250, ECO:0000269|PubMed:16121196,
CC       ECO:0000269|PubMed:21475249}.
CC   -!- INTERACTION:
CC       Q06330:RBPJ; NbExp=7; IntAct=EBI-8624731, EBI-632552;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16121196}. Cell
CC       projection, dendrite {ECO:0000269|PubMed:16121196}. Note=Forms
CC       nuclear foci. Colocalizes with NCOR2 and HDAC3. Distributed beyond
CC       the nucleus into the cell body and dendrites in Purkinje cells and
CC       in inferior olive cells.
CC   -!- TISSUE SPECIFICITY: Expressed in cerebellum and cerebral cortex.
CC       {ECO:0000269|PubMed:16121196}.
CC   -!- SIMILARITY: Belongs to the ATXN1 family. {ECO:0000305}.
CC   -!- SIMILARITY: Contains 1 AXH domain. {ECO:0000255|PROSITE-
CC       ProRule:PRU00496}.
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DR   EMBL; AC010653; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BX537575; -; NOT_ANNOTATED_CDS; mRNA.
DR   CCDS; CCDS45523.1; -.
DR   RefSeq; NP_001131147.1; NM_001137675.3.
DR   UniGene; Hs.743239; -.
DR   ProteinModelPortal; P0C7T5; -.
DR   SMR; P0C7T5; 468-582.
DR   BioGrid; 131172; 67.
DR   IntAct; P0C7T5; 4.
DR   MINT; MINT-8176805; -.
DR   STRING; 9606.ENSP00000415822; -.
DR   PhosphoSite; P0C7T5; -.
DR   DMDM; 206557834; -.
DR   MaxQB; P0C7T5; -.
DR   PaxDb; P0C7T5; -.
DR   PRIDE; P0C7T5; -.
DR   Ensembl; ENST00000427980; ENSP00000415822; ENSG00000224470.
DR   GeneID; 342371; -.
DR   KEGG; hsa:342371; -.
DR   UCSC; uc002fbd.3; human.
DR   CTD; 342371; -.
DR   GeneCards; ATXN1L; -.
DR   H-InvDB; HIX0013220; -.
DR   HGNC; HGNC:33279; ATXN1L.
DR   MIM; 614301; gene.
DR   neXtProt; NX_P0C7T5; -.
DR   PharmGKB; PA162377321; -.
DR   eggNOG; KOG4053; Eukaryota.
DR   eggNOG; ENOG410XSNX; LUCA.
DR   GeneTree; ENSGT00390000005939; -.
DR   HOGENOM; HOG000034225; -.
DR   HOVERGEN; HBG100955; -.
DR   InParanoid; P0C7T5; -.
DR   OMA; TSCSTNH; -.
DR   OrthoDB; EOG7PGDQ2; -.
DR   PhylomeDB; P0C7T5; -.
DR   TreeFam; TF350643; -.
DR   ChiTaRS; ATXN1L; human.
DR   GenomeRNAi; 342371; -.
DR   NextBio; 98271; -.
DR   PRO; PR:P0C7T5; -.
DR   Proteomes; UP000005640; Chromosome 16.
DR   Bgee; P0C7T5; -.
DR   CleanEx; HS_ATXN1L; -.
DR   Genevisible; P0C7T5; HS.
DR   GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR   GO; GO:0005730; C:nucleolus; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; IDA:HPA.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0030198; P:extracellular matrix organization; IEA:Ensembl.
DR   GO; GO:0048286; P:lung alveolus development; IEA:Ensembl.
DR   GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IEA:Ensembl.
DR   GO; GO:1902035; P:positive regulation of hematopoietic stem cell proliferation; IEA:Ensembl.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
DR   Gene3D; 2.170.16.10; -; 1.
DR   InterPro; IPR013723; Ataxin-1_HBP1.
DR   InterPro; IPR028992; Hedgehog/Intein_dom.
DR   Pfam; PF08517; AXH; 1.
DR   SUPFAM; SSF102031; SSF102031; 1.
DR   PROSITE; PS51148; AXH; 1.
PE   1: Evidence at protein level;
KW   Cell projection; Complete proteome; DNA-binding; Nucleus;
KW   Phosphoprotein; Polymorphism; Reference proteome; Repressor;
KW   Transcription; Transcription regulation.
FT   CHAIN         1    689       Ataxin-1-like.
FT                                /FTId=PRO_0000343709.
FT   DOMAIN      457    588       AXH. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00496}.
FT   REGION       20    197       Interaction with NCOR2 and ATXN1.
FT   REGION       20    197       Self-association.
FT   COMPBIAS     88    256       Pro-rich.
FT   MOD_RES     284    284       Phosphoserine.
FT                                {ECO:0000244|PubMed:20068231}.
FT   MOD_RES     361    361       Phosphoserine.
FT                                {ECO:0000244|PubMed:24275569}.
FT   VARIANT     313    313       S -> P (in dbSNP:rs7194407).
FT                                /FTId=VAR_044496.
SQ   SEQUENCE   689 AA;  73306 MW;  9C5D3938EF91F2C7 CRC64;
     MKPVHERSQE CLPPKKRDLP VTSEDMGRTT SCSTNHTPSS DASEWSRGVV VAGQSQAGAR
     VSLGGDGAEA ITGLTVDQYG MLYKVAVPPA TFSPTGLPSV VNMSPLPPTF NVASSLIQHP
     GIHYPPLHYA QLPSTSLQFI GSPYSLPYAV PPNFLPSPLL SPSANLATSH LPHFVPYASL
     LAEGATPPPQ APSPAHSFNK APSATSPSGQ LPHHSSTQPL DLAPGRMPIY YQMSRLPAGY
     TLHETPPAGA SPVLTPQESQ SALEAAAANG GQRPRERNLV RRESEALDSP NSKGEGQGLV
     PVVECVVDGQ LFSGSQTPRV EVAAPAHRGT PDTDLEVQRV VGALASQDYR VVAAQRKEEP
     SPLNLSHHTP DHQGEGRGSA RNPAELAEKS QARGFYPQSH QEPVKHRPLP KAMVVANGNL
     VPTGTDSGLL PVGSEILVAS SLDVQARATF PDKEPTPPPI TSSHLPSHFM KGAIIQLATG
     ELKRVEDLQT QDFVRSAEVS GGLKIDSSTV VDIQESQWPG FVMLHFVVGE QQSKVSIEVP
     PEHPFFVYGQ GWSSCSPGRT TQLFSLPCHR LQVGDVCISI SLQSLNSNSV SQASCAPPSQ
     LGPPRERPER TVLGSRELCD SEGKSQPAGE GSRVVEPSQP ESGAQACWPA PSFQRYSMQG
     EEARAALLRP SFIPQEVKLS IEGRSNAGK
//
ID   BRCA1_HUMAN             Reviewed;        1863 AA.
AC   P38398; E9PFZ0; O15129; Q1RMC1; Q3LRJ0; Q3LRJ6; Q6IN79; Q7KYU9;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 2.
DT   11-NOV-2015, entry version 209.
DE   RecName: Full=Breast cancer type 1 susceptibility protein;
DE            EC=6.3.2.-;
DE   AltName: Full=RING finger protein 53;
GN   Name=BRCA1; Synonyms=RNF53;
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 VARIANT BC ARG-1775.
RX   PubMed=7545954; DOI=10.1126/science.7545954;
RA   Miki Y., Swensen J., Shattuck-Eidens D., Futreal P.A., Harshman K.,
RA   Tavtigian S., Liu Q., Cochran C., Bennett L.M., Ding W., Bell R.,
RA   Rosenthal J., Hussey C., Tran T., McClure M., Frye C., Hattier T.,
RA   Phelps R., Haugen-Strano A., Katcher H., Yakumo K., Gholami Z.,
RA   Shaffer D., Stone S., Bayer S., Wray C., Bogden R., Dayananth P.,
RA   Ward J., Tonin P., Narod S., Bristow P.K., Norris F.H., Helvering L.,
RA   Morrison P., Rosteck P., Lai M., Barrett J.C., Lewis C., Neuhausen S.,
RA   Cannon-Albright L., Godlgar D., Wiseman R., Kamb A., Skolnick M.H.;
RT   "A strong candidate for the breast and ovarian cancer susceptibility
RT   gene BRCA1.";
RL   Science 266:66-71(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8938427; DOI=10.1101/gr.6.11.1029;
RA   Smith T.M., Lee M.K., Szabo C.I., Jerome N., McEuen M., Taylor M.,
RA   Hood L., King M.-C.;
RT   "Complete genomic sequence and analysis of 117 kb of human DNA
RT   containing the gene BRCA1.";
RL   Genome Res. 6:1029-1049(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), SUBCELLULAR LOCATION (ISOFORM
RP   2), VARIANTS ARG-239 AND GLY-1613, AND TISSUE SPECIFICITY (ISOFORMS 1
RP   AND 3).
RC   TISSUE=Mammary gland;
RX   PubMed=9010228; DOI=10.1038/sj.onc.1200924;
RA   Wilson C.A., Payton M.N., Elliott G.S., Buaas F.W., Cajulis E.E.,
RA   Grosshans D., Ramos L., Reese D.M., Slamon D.J., Calzone F.J.;
RT   "Differential subcellular localization, expression and biological
RT   toxicity of BRCA1 and the splice variant BRCA1-delta11b.";
RL   Oncogene 14:1-16(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC   TISSUE=Testis;
RA   Holt J.T., Robinson-Benion C.;
RL   Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ARG-356.
RA   Raymond C.K., Paddock M., Subramanian S., Deodato C., Zhou Y.,
RA   Haugen E., Kaul R., Olson M.V.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS SER-275; ARG-356;
RP   ASN-693; LEU-871; GLY-1038; ASN-1040; GLY-1140; ARG-1183; GLY-1613 AND
RP   ALA-1620.
RG   NIEHS SNPs program;
RL   Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
RN   [7]
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   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 6 AND 7), AND
RP   VARIANTS LEU-871; GLY-1038; ARG-1183; GLY-1613 AND ILE-1652.
RC   TISSUE=PNS;
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   [9]
RP   PROTEIN SEQUENCE OF 6-18 (ISOFORM 1), PROTEIN SEQUENCE OF 18-26
RP   (ISOFORM 4), AND ALTERNATIVE INITIATION (ISOFORM 4).
RX   PubMed=10851077; DOI=10.1038/sj.onc.1203599;
RA   Liu J., Prolla G., Rostagno A., Chiarle R., Feiner H., Inghirami G.;
RT   "Initiation of translation from a downstream in-frame AUG codon on
RT   BRCA1 can generate the novel isoform protein DeltaBRCA1(17aa).";
RL   Oncogene 19:2767-2773(2000).
RN   [10]
RP   ALTERNATIVE SPLICING (ISOFORM 5), AND SUBCELLULAR LOCATION (ISOFORM
RP   5).
RX   PubMed=8972225;
RA   Thakur S., Zhang H.B., Peng Y., Le H., Carroll B., Ward T., Yao J.,
RA   Farid L.M., Couch F.J., Wilson R.B., Weber B.L.;
RT   "Localization of BRCA1 and a splice variant identifies the nuclear
RT   localization signal.";
RL   Mol. Cell. Biol. 17:444-452(1997).
RN   [11]
RP   INTERACTION WITH BAP1, SUBCELLULAR LOCATION, VARIANTS GLY-61 AND
RP   GLY-64, AND MUTAGENESIS OF ARG-71.
RX   PubMed=9528852; DOI=10.1038/sj.onc.1201861;
RA   Jensen D.E., Proctor M., Marquis S.T., Gardner H.P., Ha S.I.,
RA   Chodosh L.A., Ishov A.M., Tommerup N., Vissing H., Sekido Y.,
RA   Minna J., Borodovsky A., Schultz D.C., Wilkinson K.D., Maul G.G.,
RA   Barlev N., Berger S., Prendergast G.C., Rauscher F.J. III;
RT   "BAP1: a novel ubiquitin hydrolase which binds to the BRCA1 RING
RT   finger and enhances BRCA1-mediated cell growth suppression.";
RL   Oncogene 16:1097-1112(1998).
RN   [12]
RP   INTERACTION WITH RBBP8.
RX   PubMed=9811458; DOI=10.1038/sj.onc.1202150;
RA   Wong A.K., Ormonde P.A., Pero R., Chen Y., Lian L., Salada G.,
RA   Berry S., Lawrence Q., Dayananth P., Ha P., Tavtigian S.V., Teng D.H.,
RA   Bartel P.L.;
RT   "Characterization of a carboxy-terminal BRCA1 interacting protein.";
RL   Oncogene 17:2279-2285(1998).
RN   [13]
RP   FUNCTION AS AN E2-DEPENDENT UBIQUITIN-PROTEIN LIGASE.
RX   PubMed=10500182; DOI=10.1073/pnas.96.20.11364;
RA   Lorick K.L., Jensen J.P., Fang S., Ong A.M., Hatakeyama S.,
RA   Weissman A.M.;
RT   "RING fingers mediate ubiquitin-conjugating enzyme (E2)-dependent
RT   ubiquitination.";
RL   Proc. Natl. Acad. Sci. U.S.A. 96:11364-11369(1999).
RN   [14]
RP   IDENTIFICATION IN THE BASC COMPLEX.
RX   PubMed=10783165; DOI=10.1101/gad.827000;
RA   Wang Y., Cortez D., Yazdi P., Neff N., Elledge S.J., Qin J.;
RT   "BASC, a super complex of BRCA1-associated proteins involved in the
RT   recognition and repair of aberrant DNA structures.";
RL   Genes Dev. 14:927-939(2000).
RN   [15]
RP   PHOSPHORYLATION AT SER-1143; SER-1280; SER-1387; THR-1394; SER-1423
RP   AND SER-1457, MUTAGENESIS OF SER-1143; SER-1239; SER-1280; SER-1298;
RP   SER-1330; SER-1387; THR-1394; SER-1423; SER-1457; SER-1466; SER-1524
RP   AND SER-1755, AND CHARACTERIZATION OF VARIANT BC ALA-1720.
RX   PubMed=11114888; DOI=10.1101/gad.851000;
RA   Tibbetts R.S., Cortez D., Brumbaugh K.M., Scully R., Livingston D.,
RA   Elledge S.J., Abraham R.T.;
RT   "Functional interactions between BRCA1 and the checkpoint kinase ATR
RT   during genotoxic stress.";
RL   Genes Dev. 14:2989-3002(2000).
RN   [16]
RP   FUNCTION IN DNA DAMAGE RESPONSE, PHOSPHORYLATION AT SER-988 BY CHEK2,
RP   AND INTERACTION WITH CHEK2.
RX   PubMed=10724175; DOI=10.1038/35004614;
RA   Lee J.S., Collins K.M., Brown A.L., Lee C.H., Chung J.H.;
RT   "hCds1-mediated phosphorylation of BRCA1 regulates the DNA damage
RT   response.";
RL   Nature 404:201-204(2000).
RN   [17]
RP   INTERACTION WITH BRIP1, CHARACTERIZATION OF VARIANT OVARIAN CANCER
RP   ARG-1749, AND CHARACTERIZATION OF VARIANT BC ARG-1775.
RX   PubMed=11301010; DOI=10.1016/S0092-8674(01)00304-X;
RA   Cantor S.B., Bell D.W., Ganesan S., Kass E.M., Drapkin R.,
RA   Grossman S., Wahrer D.C.R., Sgroi D.C., Lane W.S., Haber D.A.,
RA   Livingston D.M.;
RT   "BACH1, a novel helicase-like protein, interacts directly with BRCA1
RT   and contributes to its DNA repair function.";
RL   Cell 105:149-160(2001).
RN   [18]
RP   INTERACTION WITH NELFB.
RX   PubMed=11739404; DOI=10.1083/jcb.200108049;
RA   Ye Q., Hu Y.-F., Zhong H., Nye A.C., Belmont A.S., Li R.;
RT   "BRCA1-induced large-scale chromatin unfolding and allele-specific
RT   effects of cancer-predisposing mutations.";
RL   J. Cell Biol. 155:911-921(2001).
RN   [19]
RP   INTERACTION WITH FANCD2.
RX   PubMed=11239454; DOI=10.1016/S1097-2765(01)00173-3;
RA   Garcia-Higuera I., Taniguchi T., Ganesan S., Meyn M.S., Timmers C.,
RA   Hejna J., Grompe M., D'Andrea A.D.;
RT   "Interaction of the Fanconi anemia proteins and BRCA1 in a common
RT   pathway.";
RL   Mol. Cell 7:249-262(2001).
RN   [20]
RP   PHOSPHORYLATION BY ATM, AND MUTAGENESIS OF SER-1387; SER-1423 AND
RP   SER-1524.
RX   PubMed=12183412;
RA   Xu B., O'Donnell A.H., Kim S.-T., Kastan M.B.;
RT   "Phosphorylation of serine 1387 in BRCA1 is specifically required for
RT   the Atm-mediated S-phase checkpoint after ionizing irradiation.";
RL   Cancer Res. 62:4588-4591(2002).
RN   [21]
RP   INTERACTION WITH H2AFX.
RX   PubMed=12419185; DOI=10.1016/S0960-9822(02)01259-9;
RA   Kobayashi J., Tauchi H., Sakamoto S., Nakamura A., Morishima K.,
RA   Matsuura S., Kobayashi T., Tamai K., Tanimoto K., Komatsu K.;
RT   "NBS1 localizes to gamma-H2AX foci through interaction with the
RT   FHA/BRCT domain.";
RL   Curr. Biol. 12:1846-1851(2002).
RN   [22]
RP   INTERACTION WITH SMC1A.
RX   PubMed=11877377; DOI=10.1101/gad.970702;
RA   Yazdi P.T., Wang Y., Zhao S., Patel N., Lee E.Y.-H.P., Qin J.;
RT   "SMC1 is a downstream effector in the ATM/NBS1 branch of the human S-
RT   phase checkpoint.";
RL   Genes Dev. 16:571-582(2002).
RN   [23]
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   [24]
RP   FUNCTION, AND INTERACTION WITH CHEK1.
RX   PubMed=11836499; DOI=10.1038/ng837;
RA   Yarden R.I., Pardo-Reoyo S., Sgagias M., Cowan K.H., Brody L.C.;
RT   "BRCA1 regulates the G2/M checkpoint by activating Chk1 kinase upon
RT   DNA damage.";
RL   Nat. Genet. 30:285-289(2002).
RN   [25]
RP   INTERACTION WITH ACACA.
RX   PubMed=12360400; DOI=10.1038/sj.onc.1205915;
RA   Magnard C., Bachelier R., Vincent A., Jaquinod M., Kieffer S.,
RA   Lenoir G.M., Venezia N.D.;
RT   "BRCA1 interacts with acetyl-CoA carboxylase through its tandem of
RT   BRCT domains.";
RL   Oncogene 21:6729-6739(2002).
RN   [26]
RP   FUNCTION, UBIQUITINATION, AND INTERACTION WITH BARD1.
RX   PubMed=12890688; DOI=10.1074/jbc.C300249200;
RA   Wu-Baer F., Lagrazon K., Yuan W., Baer R.;
RT   "The BRCA1/BARD1 heterodimer assembles polyubiquitin chains through an
RT   unconventional linkage involving lysine residue K6 of ubiquitin.";
RL   J. Biol. Chem. 278:34743-34746(2003).
RN   [27]
RP   FUNCTION.
RX   PubMed=12887909; DOI=10.1016/S1097-2765(03)00281-8;
RA   Vandenberg C.J., Gergely F., Ong C.Y., Pace P., Mallery D.L., Hiom K.,
RA   Patel K.J.;
RT   "BRCA1-independent ubiquitination of FANCD2.";
RL   Mol. Cell 12:247-254(2003).
RN   [28]
RP   INTERACTION WITH BRCC3.
RX   PubMed=14636569; DOI=10.1016/S1097-2765(03)00424-6;
RA   Dong Y., Hakimi M.-A., Chen X., Kumaraswamy E., Cooch N.S.,
RA   Godwin A.K., Shiekhattar R.;
RT   "Regulation of BRCC, a holoenzyme complex containing BRCA1 and BRCA2,
RT   by a signalosome-like subunit and its role in DNA repair.";
RL   Mol. Cell 12:1087-1099(2003).
RN   [29]
RP   FUNCTION, AND INTERACTION WITH BARD1.
RX   PubMed=14976165; DOI=10.1093/hmg/ddh095;
RA   Morris J.R., Solomon E.;
RT   "BRCA1:BARD1 induces the formation of conjugated ubiquitin structures,
RT   dependent on K6 of ubiquitin, in cells during DNA replication and
RT   repair.";
RL   Hum. Mol. Genet. 13:807-817(2004).
RN   [30]
RP   INTERACTION WITH AURKA, FUNCTION, MUTAGENESIS OF SER-308, AND
RP   PHOSPHORYLATION AT SER-308.
RX   PubMed=14990569; DOI=10.1074/jbc.M311780200;
RA   Ouchi M., Fujiuchi N., Sasai K., Katayama H., Minamishima Y.A.,
RA   Ongusaha P.P., Deng C., Sen S., Lee S.W., Ouchi T.;
RT   "BRCA1 phosphorylation by Aurora-A in the regulation of G2 to M
RT   transition.";
RL   J. Biol. Chem. 279:19643-19648(2004).
RN   [31]
RP   INTERACTION WITH DCLRE1C.
RX   PubMed=15456891; DOI=10.1128/MCB.24.20.9207-9220.2004;
RA   Zhang X., Succi J., Feng Z., Prithivirajsingh S., Story M.D.,
RA   Legerski R.J.;
RT   "Artemis is a phosphorylation target of ATM and ATR and is involved in
RT   the G2/M DNA damage checkpoint response.";
RL   Mol. Cell. Biol. 24:9207-9220(2004).
RN   [32]
RP   INTERACTION WITH CLSPN.
RX   PubMed=15096610; DOI=10.1073/pnas.0401847101;
RA   Lin S.-Y., Li K., Stewart G.S., Elledge S.J.;
RT   "Human claspin works with BRCA1 to both positively and negatively
RT   regulate cell proliferation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:6484-6489(2004).
RN   [33]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1336, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA   Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA   Mann M.;
RT   "Global, in vivo, and site-specific phosphorylation dynamics in
RT   signaling networks.";
RL   Cell 127:635-648(2006).
RN   [34]
RP   FUNCTION, INTERACTION WITH RBBP8, AND MUTAGENESIS OF ILE-26.
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   [35]
RP   FUNCTION, AND INTERACTION WITH ACACA.
RX   PubMed=16326698; DOI=10.1074/jbc.M504652200;
RA   Moreau K., Dizin E., Ray H., Luquain C., Lefai E., Foufelle F.,
RA   Billaud M., Lenoir G.M., Venezia N.D.;
RT   "BRCA1 affects lipid synthesis through its interaction with acetyl-CoA
RT   carboxylase.";
RL   J. Biol. Chem. 281:3172-3181(2006).
RN   [36]
RP   INTERACTION WITH ACACA.
RX   PubMed=16698035; DOI=10.1016/j.jmb.2006.04.010;
RA   Ray H., Moreau K., Dizin E., Callebaut I., Venezia N.D.;
RT   "ACCA phosphopeptide recognition by the BRCT repeats of BRCA1.";
RL   J. Mol. Biol. 359:973-982(2006).
RN   [37]
RP   FUNCTION, PHOSPHORYLATION BY AURKA, AND ENZYME REGULATION.
RX   PubMed=18056443; DOI=10.1158/0008-5472.CAN-07-2578;
RA   Sankaran S., Crone D.E., Palazzo R.E., Parvin J.D.;
RT   "Aurora-A kinase regulates breast cancer associated gene 1 inhibition
RT   of centrosome-dependent microtubule nucleation.";
RL   Cancer Res. 67:11186-11194(2007).
RN   [38]
RP   INTERACTION WITH FAM175A.
RX   PubMed=17643122; DOI=10.1038/nsmb1277;
RA   Kim H., Huang J., Chen J.;
RT   "CCDC98 is a BRCA1-BRCT domain-binding protein involved in the DNA
RT   damage response.";
RL   Nat. Struct. Mol. Biol. 14:710-715(2007).
RN   [39]
RP   INTERACTION WITH FAM175A.
RX   PubMed=17643121; DOI=10.1038/nsmb1279;
RA   Liu Z., Wu J., Yu X.;
RT   "CCDC98 targets BRCA1 to DNA damage sites.";
RL   Nat. Struct. Mol. Biol. 14:716-720(2007).
RN   [40]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic kidney;
RX   PubMed=17525332; DOI=10.1126/science.1140321;
RA   Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
RA   Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
RA   Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
RT   "ATM and ATR substrate analysis reveals extensive protein networks
RT   responsive to DNA damage.";
RL   Science 316:1160-1166(2007).
RN   [41]
RP   FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH FAM175A.
RX   PubMed=17525340; DOI=10.1126/science.1139476;
RA   Wang B., Matsuoka S., Ballif B.A., Zhang D., Smogorzewska A., Giyi S.,
RA   Elledge S.J.;
RT   "Abraxas and RAP80 form a BRCA1 protein complex required for the DNA
RT   damage response.";
RL   Science 316:1194-1198(2007).
RN   [42]
RP   INVOLVEMENT IN PNCA4.
RX   PubMed=18762988; DOI=10.1007/s00439-008-0554-0;
RA   Al-Sukhni W., Rothenmund H., Borgida A.E., Zogopoulos G., O'Shea A.M.,
RA   Pollett A., Gallinger S.;
RT   "Germline BRCA1 mutations predispose to pancreatic adenocarcinoma.";
RL   Hum. Genet. 124:271-278(2008).
RN   [43]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-395; SER-398; SER-753;
RP   SER-1211; SER-1217 AND SER-1218, AND IDENTIFICATION BY MASS
RP   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   [44]
RP   FUNCTION, AND IDENTIFICATION IN THE BRCA1-A COMPLEX.
RX   PubMed=19261748; DOI=10.1101/gad.1770609;
RA   Feng L., Huang J., Chen J.;
RT   "MERIT40 facilitates BRCA1 localization and DNA damage repair.";
RL   Genes Dev. 23:719-728(2009).
RN   [45]
RP   IDENTIFICATION IN THE BRCA1-A COMPLEX.
RX   PubMed=19261749; DOI=10.1101/gad.1770309;
RA   Wang B., Hurov K., Hofmann K., Elledge S.J.;
RT   "NBA1, a new player in the Brca1 A complex, is required for DNA damage
RT   resistance and checkpoint control.";
RL   Genes Dev. 23:729-739(2009).
RN   [46]
RP   IDENTIFICATION IN THE BRCA1-A COMPLEX.
RX   PubMed=19261746; DOI=10.1101/gad.1739609;
RA   Shao G., Patterson-Fortin J., Messick T.E., Feng D., Shanbhag N.,
RA   Wang Y., Greenberg R.A.;
RT   "MERIT40 controls BRCA1-Rap80 complex integrity and recruitment to DNA
RT   double-strand breaks.";
RL   Genes Dev. 23:740-754(2009).
RN   [47]
RP   IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, INTERACTION WITH PALB2,
RP   IDENTIFICATION IN A BRCA COMPLEX WITH BRCA1 AND PALB2, AND
RP   CHARACTERIZATION OF VARIANT OVARIAN CANCER 1411-THR.
RX   PubMed=19369211; DOI=10.1073/pnas.0811159106;
RA   Sy S.M., Huen M.S., Chen J.;
RT   "PALB2 is an integral component of the BRCA complex required for
RT   homologous recombination repair.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:7155-7160(2009).
RN   [48]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-395 AND SER-398, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA   Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA   Rodionov V., Han D.K.;
RT   "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT   reveals system-wide modulation of protein-protein interactions.";
RL   Sci. Signal. 2:RA46-RA46(2009).
RN   [49]
RP   FUNCTION, INTERACTION WITH CCAR2, AND SUBCELLULAR LOCATION.
RX   PubMed=20160719; DOI=10.1038/sj.bjc.6605577;
RA   Hiraike H., Wada-Hiraike O., Nakagawa S., Koyama S., Miyamoto Y.,
RA   Sone K., Tanikawa M., Tsuruga T., Nagasaka K., Matsumoto Y., Oda K.,
RA   Shoji K., Fukuhara H., Saji S., Nakagawa K., Kato S., Yano T.,
RA   Taketani Y.;
RT   "Identification of DBC1 as a transcriptional repressor for BRCA1.";
RL   Br. J. Cancer 102:1061-1067(2010).
RN   [50]
RP   FUNCTION, INTERACTION WITH BARD1 AND UBXN1, UBIQUITINATION, AND
RP   MUTAGENESIS OF ILE-26.
RX   PubMed=20351172; DOI=10.1128/MCB.01056-09;
RA   Wu-Baer F., Ludwig T., Baer R.;
RT   "The UBXN1 protein associates with autoubiquitinated forms of the
RT   BRCA1 tumor suppressor and inhibits its enzymatic function.";
RL   Mol. Cell. Biol. 30:2787-2798(2010).
RN   [51]
RP   FUNCTION IN CHROMOSOMAL STABILITY, AND PHOSPHORYLATION AT SER-988 BY
RP   CHEK2.
RX   PubMed=20364141; DOI=10.1038/ncb2051;
RA   Stolz A., Ertych N., Kienitz A., Vogel C., Schneider V., Fritz B.,
RA   Jacob R., Dittmar G., Weichert W., Petersen I., Bastians H.;
RT   "The CHK2-BRCA1 tumour suppressor pathway ensures chromosomal
RT   stability in human somatic cells.";
RL   Nat. Cell Biol. 12:492-499(2010).
RN   [52]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114; SER-423; SER-694;
RP   SER-1328; SER-1336 AND SER-1342, AND IDENTIFICATION BY MASS
RP   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   [53]
RP   PHOSPHORYLATION AT SER-1524, AND SUBCELLULAR LOCATION.
RX   PubMed=21144835; DOI=10.1016/j.bbrc.2010.12.005;
RA   Kang Y., Cheong H.M., Lee J.H., Song P.I., Lee K.H., Kim S.Y.,
RA   Jun J.Y., You H.J.;
RT   "Protein phosphatase 5 is necessary for ATR-mediated DNA repair.";
RL   Biochem. Biophys. Res. Commun. 404:476-481(2011).
RN   [54]
RP   INTERACTION WITH KIAA0101.
RX   PubMed=21673012; DOI=10.1158/1541-7786.MCR-10-0503;
RA   Kais Z., Barsky S.H., Mathsyaraja H., Zha A., Ransburgh D.J., He G.,
RA   Pilarski R.T., Shapiro C.L., Huang K., Parvin J.D.;
RT   "KIAA0101 interacts with BRCA1 and regulates centrosome number.";
RL   Mol. Cancer Res. 9:1091-1099(2011).
RN   [55]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114; SER-1218; SER-1336
RP   AND SER-1342, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   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   [56]
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   [57]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-339; LYS-459; LYS-583;
RP   LYS-654; LYS-734 AND LYS-739, AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=25218447; DOI=10.1038/nsmb.2890;
RA   Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA   Vertegaal A.C.;
RT   "Uncovering global SUMOylation signaling networks in a site-specific
RT   manner.";
RL   Nat. Struct. Mol. Biol. 21:927-936(2014).
RN   [58]
RP   STRUCTURE BY NMR OF 1-110 IN COMPLEX WITH ZINC IONS AND BARD1, AND
RP   SUBUNIT.
RX   PubMed=11573085; DOI=10.1038/nsb1001-833;
RA   Brzovic P.S., Rajagopal P., Hoyt D.W., King M.C., Klevit R.E.;
RT   "Structure of a BRCA1-BARD1 heterodimeric RING-RING complex.";
RL   Nat. Struct. Biol. 8:833-837(2001).
RN   [59]
RP   X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1646-1859, PARTIAL PROTEIN
RP   SEQUENCE, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=11573086; DOI=10.1038/nsb1001-838;
RA   Williams R.S., Green R., Glover J.N.;
RT   "Crystal structure of the BRCT repeat region from the breast cancer-
RT   associated protein BRCA1.";
RL   Nat. Struct. Biol. 8:838-842(2001).
RN   [60]
RP   X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 1646-1859 OF VARIANT BC
RP   ARG-1775, CHARACTERIZATION OF VARIANT BC ARG-1775, AND CIRCULAR
RP   DICHROISM.
RX   PubMed=12427738; DOI=10.1074/jbc.M210019200;
RA   Williams R.S., Glover J.N.;
RT   "Structural consequences of a cancer-causing BRCA1-BRCT missense
RT   mutation.";
RL   J. Biol. Chem. 278:2630-2635(2003).
RN   [61]
RP   STRUCTURE BY NMR OF 1755-1863.
RX   PubMed=15609993; DOI=10.1021/bi049550q;
RA   Gaiser O.J., Ball L.J., Schmieder P., Leitner D., Strauss H., Wahl M.,
RA   Kuhne R., Oschkinat H., Heinemann U.;
RT   "Solution structure, backbone dynamics, and association behavior of
RT   the C-terminal BRCT domain from the breast cancer-associated protein
RT   BRCA1.";
RL   Biochemistry 43:15983-15995(2004).
RN   [62]
RP   X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 1649-1859 IN COMPLEX WITH
RP   WITH PHOSPHORYLATED BRIP1 PEPTIDE, MUTAGENESIS OF SER-1655; LYS-1702
RP   AND GLY-1738, CHARACTERIZATION OF VARIANT OVARIAN CANCER ARG-1749,
RP   CHARACTERIZATION OF VARIANT BC ARG-1775, SUBCELLULAR LOCATION, AND
RP   INTERACTION WITH PHOSPHORYLATED BRIP1.
RX   PubMed=15133502; DOI=10.1038/nsmb775;
RA   Clapperton J.A., Manke I.A., Lowery D.M., Ho T., Haire L.F.,
RA   Yaffe M.B., Smerdon S.J.;
RT   "Structure and mechanism of BRCA1 BRCT domain recognition of
RT   phosphorylated BACH1 with implications for cancer.";
RL   Nat. Struct. Mol. Biol. 11:512-518(2004).
RN   [63]
RP   X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1646-1859 IN COMPLEX WITH
RP   PHOSPHORYLATED RBBP8 PEPTIDE, AND SUBUNIT.
RX   PubMed=16101277; DOI=10.1021/bi0509651;
RA   Varma A.K., Brown R.S., Birrane G., Ladias J.A.;
RT   "Structural basis for cell cycle checkpoint control by the BRCA1-CtIP
RT   complex.";
RL   Biochemistry 44:10941-10946(2005).
RN   [64]
RP   X-RAY CRYSTALLOGRAPHY (3.21 ANGSTROMS) OF 1646-1859 IN COMPLEX WITH
RP   PHOSPHORYLATED ACACA PEPTIDE, AND SUBUNIT.
RX   PubMed=18452305; DOI=10.1021/bi800314m;
RA   Shen Y., Tong L.;
RT   "Structural evidence for direct interactions between the BRCT domains
RT   of human BRCA1 and a phospho-peptide from human ACC1.";
RL   Biochemistry 47:5767-5773(2008).
RN   [65]
RP   X-RAY CRYSTALLOGRAPHY (3.6 ANGSTROMS) OF 1649-1859 OF VARIANT BC
RP   LYS-1775, VARIANT BC LYS-1775, AND CHARACTERIZATION OF VARIANT BC
RP   LYS-1775.
RX   PubMed=18285836; DOI=10.1038/ejhg.2008.13;
RA   Tischkowitz M., Hamel N., Carvalho M.A., Birrane G., Soni A.,
RA   van Beers E.H., Joosse S.A., Wong N., Novak D., Quenneville L.A.,
RA   Grist S.A., Nederlof P.M., Goldgar D.E., Tavtigian S.V.,
RA   Monteiro A.N., Ladias J.A., Foulkes W.D.;
RT   "Pathogenicity of the BRCA1 missense variant M1775K is determined by
RT   the disruption of the BRCT phosphopeptide-binding pocket: a multi-
RT   modal approach.";
RL   Eur. J. Hum. Genet. 16:820-832(2008).
RN   [66]
RP   X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 1646-1859 IN COMPLEX WITH
RP   PHOSPHORYLATED PEPTIDES, AND DOMAIN.
RX   PubMed=20159462; DOI=10.1016/j.str.2009.12.008;
RA   Campbell S.J., Edwards R.A., Glover J.N.;
RT   "Comparison of the structures and peptide binding specificities of the
RT   BRCT domains of MDC1 and BRCA1.";
RL   Structure 18:167-176(2010).
RN   [67]
RP   REVIEW ON VARIANTS.
RX   PubMed=8807330; DOI=10.1002/humu.1380080102;
RA   Couch F.J., Weber B.L.;
RT   "Mutations and polymorphisms in the familial early-onset breast cancer
RT   (BRCA1) gene.";
RL   Hum. Mutat. 8:8-18(1996).
RN   [68]
RP   VARIANT BC ARG-1775, AND VARIANTS LEU-1637 AND GLU-1708.
RX   PubMed=7939630; DOI=10.1126/science.7939630;
RA   Futreal P.A., Liu Q., Shattuck-Eidens D., Cochran C., Harshman K.,
RA   Tavtigian S., Bennett L.M., Haugen-Strano A., Swensen J., Miki Y.,
RA   Eddington K., McClure M., Frye C., Weaver-Felhaus J., Ding W.,
RA   Gholami Z., Soederkvist P., Terry L., Jhanwar S., Berchuk A.,
RA   Iglehart J.D., Marks J., Ballinger D.G., Barrett J.C., Skolnick M.H.,
RA   Kamb A., Wiseman R.;
RT   "BRCA1 mutations in primary breast and ovarian carcinomas.";
RL   Science 266:120-122(1994).
RN   [69]
RP   VARIANT BC GLY-64, AND VARIANTS ALA-772; ASN-1040 AND GLY-1443.
RX   PubMed=7894491; DOI=10.1038/ng1294-387;
RA   Castilla L.H., Couch F.J., Erdos M.R., Hoskins K.F., Calzone K.,
RA   Garber J.E., Boyd J., Lubin M.B., Deshano M.L., Brody L.C.,
RA   Collins F.S., Weber B.L.;
RT   "Mutations in the BRCA1 gene in families with early-onset breast and
RT   ovarian cancer.";
RL   Nat. Genet. 8:387-391(1994).
RN   [70]
RP   VARIANT BC GLY-61, AND VARIANTS ARG-356; GLY-1038; ASN-1040; ARG-1183
RP   AND GLY-1613.
RX   PubMed=7894493; DOI=10.1038/ng1294-399;
RA   Friedman L.S., Ostermeyer E.A., Szabo C.I., Dowd P., Lynch E.D.,
RA   Rowell S.E., King M.-C.;
RT   "Confirmation of BRCA1 by analysis of germline mutations linked to
RT   breast and ovarian cancer in ten families.";
RL   Nat. Genet. 8:399-404(1994).
RN   [71]
RP   VARIANT BC GLY-61.
RX   PubMed=8554067;
RA   Serova O., Montagna M., Torchard D., Narod S.A., Tonin P., Sylla B.,
RA   Lynch H.T., Feunteun J., Lenoir G.M.;
RT   "A high incidence of BRCA1 mutations in 20 breast-ovarian cancer
RT   families.";
RL   Am. J. Hum. Genet. 58:42-51(1996).
RN   [72]
RP   VARIANT BROVCA1 TRP-841.
RX   PubMed=8968716;
RX   DOI=10.1002/(SICI)1098-2272(1996)13:6<595::AID-GEPI5>3.3.CO;2-0;
RA   Barker D.F., Almeida E.F.A., Casey G., Fain P.R., Liao S.-Y.,
RA   Masunaka I., Noble B., Kurosaki T., Anton-Culver H.;
RT   "BRCA1 R841W: a strong candidate for a common mutation with moderate
RT   phenotype.";
RL   Genet. Epidemiol. 13:595-604(1996).
RN   [73]
RP   VARIANTS BC AND BROVCA1.
RX   PubMed=8776600; DOI=10.1093/hmg/5.6.835;
RA   Durocher F., Shattuck-Eidens D., McClure M., Labrie F., Skolnick M.H.,
RA   Goldgar D.E., Simard J.;
RT   "Comparison of BRCA1 polymorphisms, rare sequence variants and/or
RT   missense mutations in unaffected and breast/ovarian cancer
RT   populations.";
RL   Hum. Mol. Genet. 5:835-842(1996).
RN   [74]
RP   VARIANTS BC MET-271 AND SER-1150.
RX   PubMed=8723683;
RX   DOI=10.1002/(SICI)1098-1004(1996)7:4<334::AID-HUMU7>3.3.CO;2-K;
RA   Katagiri T., Emi M., Ito I., Kobayashi K., Yoshimoto M., Iwase T.,
RA   Kasumi F., Miki Y., Skolnick M.H., Nakamura Y.;
RT   "Mutations in the BRCA1 gene in Japanese breast cancer patients.";
RL   Hum. Mutat. 7:334-339(1996).
RN   [75]
RP   VARIANT BC GLY-61, AND VARIANTS ARG-239; TRP-841 AND ILE-1512.
RX   PubMed=9760198; DOI=10.1007/s004390050799;
RA   Dong J., Chang-Claude J., Wu Y., Schumacher V., Debatin I., Tonin P.,
RA   Royer-Pokora B.;
RT   "A high proportion of mutations in the BRCA1 gene in German
RT   breast/ovarian cancer families with clustering of mutations in the 3'
RT   third of the gene.";
RL   Hum. Genet. 103:154-161(1998).
RN   [76]
RP   VARIANT BC GLY-64, AND VARIANTS ALA-772; GLU-820; ASN-1040; GLY-1443;
RP   ILE-1512; LEU-1637 AND ILE-1652.
RX   PubMed=9482581;
RX   DOI=10.1002/(SICI)1098-1004(1998)11:2<166::AID-HUMU10>3.0.CO;2-X;
RA   Andersen T.I., Eiken H.G., Couch F., Kaada G., Skrede M., Johnsen H.,
RA   Aloysius T.A., Tveit K.M., Tranebjaerg L., Doerum A., Moeller P.,
RA   Weber B.L., Boerresen-Dale A.-L.;
RT   "Constant denaturant gel electrophoresis (CDGE) in BRCA1 mutation
RT   screening.";
RL   Hum. Mutat. 11:166-174(1998).
RN   [77]
RP   VARIANTS BC SER-22; LEU-461; ASP-465; VAL-552; SER-892; ASP-960;
RP   ILE-1025 AND ALA-1047.
RX   PubMed=9609997; DOI=10.1007/s100380050035;
RA   Katagiri T., Kasumi F., Yoshimoto M., Nomizu T., Asaishi K., Abe R.,
RA   Tsuchiya A., Sugano M., Takai S., Yoneda M., Fukutomi T., Nanba K.,
RA   Makita M., Okazaki H., Hirata K., Okazaki M., Furutsuma Y.,
RA   Morishita Y., Iino Y., Karino T., Ayabe H., Hara S., Kajiwara T.,
RA   Houga S., Shimizu T., Toda M., Yamazaki Y., Uchida T., Kunitomo K.,
RA   Sonoo H., Kurebayashi J., Shimotsuma K., Nakamura Y., Miki Y.;
RT   "High proportion of missense mutations of the BRCA1 and BRCA2 genes in
RT   Japanese breast cancer families.";
RL   J. Hum. Genet. 43:42-48(1998).
RN   [78]
RP   VARIANT OVARIAN CANCER ARG-1749.
RX   PubMed=10486320; DOI=10.1086/302583;
RA   Gayther S.A., Russell P., Harrington P., Antoniou A.C., Easton D.F.,
RA   Ponder B.A.J.;
RT   "The contribution of germline BRCA1 and BRCA2 mutations to familial
RT   ovarian cancer: no evidence for other ovarian cancer-susceptibility
RT   genes.";
RL   Am. J. Hum. Genet. 65:1021-1029(1999).
RN   [79]
RP   VARIANT BC SER-346, AND VARIANTS LEU-871; GLY-1038; ARG-1183 AND
RP   GLY-1613.
RX   PubMed=10323242; DOI=10.1007/s004390050936;
RA   Li S.S.-L., Tseng H.-M., Yang T.-P., Liu C.-H., Teng S.-J.,
RA   Huang H.-W., Chen L.-M., Kao H.-W., Chen J.H., Tseng J.-N., Chen A.,
RA   Hou M.-F., Huang T.-J., Chang H.-T., Mok K.-T., Tsai J.-H.;
RT   "Molecular characterization of germline mutations in the BRCA1 and
RT   BRCA2 genes from breast cancer families in Taiwan.";
RL   Hum. Genet. 104:201-204(1999).
RN   [80]
RP   VARIANTS OVARIAN CANCER, AND VARIANTS.
RX   PubMed=10196379; DOI=10.1093/hmg/8.5.889;
RA   Janezic S.A., Ziogas A., Krumroy L.M., Krasner M., Plummer S.J.,
RA   Cohen P., Gildea M., Barker D., Haile R., Casey G., Anton-Culver H.;
RT   "Germline BRCA1 alterations in a population-based series of ovarian
RT   cancer cases.";
RL   Hum. Mol. Genet. 8:889-897(1999).
RN   [81]
RP   VARIANTS GLY-1347; ILE-1512 AND ILE-1652.
RX   PubMed=12215251; DOI=10.1089/10906570260199375;
RA   Deffenbaugh A.M., Frank T.S., Hoffman M., Cannon-Albright L.,
RA   Neuhausen S.L.;
RT   "Characterization of common BRCA1 and BRCA2 variants.";
RL   Genet. Test. 6:119-121(2002).
RN   [82]
RP   VARIANTS ILE-656; LEU-871 AND GLY-1613.
RX   PubMed=12442274; DOI=10.1002/humu.9083;
RA   Zhi X., Szabo C., Chopin S., Suter N., Wang Q.-S., Ostrander E.A.,
RA   Sinilnikova O.M., Lenoir G.M., Goldgar D., Shi Y.-R.;
RT   "BRCA1 and BRCA2 sequence variants in Chinese breast cancer
RT   families.";
RL   Hum. Mutat. 20:474-474(2002).
RN   [83]
RP   VARIANT BC TYR-749.
RX   PubMed=12442275; DOI=10.1002/humu.9084;
RA   Ruiz-Flores P., Sinilnikova O.M., Badzioch M.,
RA   Calderon-Garciduenas A.L., Chopin S., Fabrice O.,
RA   Gonzalez-Guerrero J.F., Szabo C., Lenoir G., Goldgar D.E.,
RA   Barrera-Saldana H.A.;
RT   "BRCA1 and BRCA2 mutation analysis of early-onset and familial breast
RT   cancer cases in Mexico.";
RL   Hum. Mutat. 20:474-475(2002).
RN   [84]
RP   VARIANTS BC GLY-61; LYS-71; GLN-866; TYR-888; ILE-1139; GLY-1210 AND
RP   PRO-1297, AND VARIANTS BROVCA1 TYR-835 AND PRO-1786.
RX   PubMed=12938098; DOI=10.1002/humu.9174;
RA   Meyer P., Voigtlaender T., Bartram C.R., Klaes R.;
RT   "Twenty-three novel BRCA1 and BRCA2 sequence alterations in breast
RT   and/or ovarian cancer families in Southern Germany.";
RL   Hum. Mutat. 22:259-259(2003).
RN   [85]
RP   VARIANTS ASN-693; ASN-1040; ALA-1060 AND MET-1665.
RX   PubMed=15026808; DOI=10.1038/sj.bjc.6601656;
RA   Claes K., Poppe B., Coene I., De Paepe A., Messiaen L.;
RT   "BRCA1 and BRCA2 germline mutation spectrum and frequencies in Belgian
RT   breast/ovarian cancer families.";
RL   Br. J. Cancer 90:1244-1251(2004).
RN   [86]
RP   VARIANTS OVARIAN CANCER GLY-61; THR-1411; ARG-1697 AND TRP-1699.
RX   PubMed=14746861; DOI=10.1016/j.ejca.2003.09.016;
RA   Malander S., Ridderheim M., Masbaeck A., Loman N., Kristoffersson U.,
RA   Olsson H., Nilbert M., Borg A.;
RT   "One in 10 ovarian cancer patients carry germ line BRCA1 or BRCA2
RT   mutations: results of a prospective study in Southern Sweden.";
RL   Eur. J. Cancer 40:422-428(2004).
RN   [87]
RP   VARIANTS BC/BROVCA1 LYS-10; LYS-23; ILE-1187; HIS-1200 AND TYR-1217,
RP   VARIANTS BC ILE-1204 AND ASN-1207, VARIANTS BROVCA1 LEU-1226 AND
RP   GLY-1243, AND VARIANT ARG-1183.
RX   PubMed=14722926; DOI=10.1002/humu.9213;
RA   Valarmathi M.T., Sawhney M., Deo S.S.V., Shukla N.K., Das S.N.;
RT   "Novel germline mutations in the BRCA1 and BRCA2 genes in Indian
RT   breast and breast-ovarian cancer families.";
RL   Hum. Mutat. 23:205-205(2004).
RN   [88]
RP   VARIANTS HIS-856; LEU-871; GLY-1038; ARG-1183; THR-1628; GLN-1690 AND
RP   GLY-1713.
RX   PubMed=15365993; DOI=10.1002/humu.9275;
RA   Seo J.H., Cho D.-Y., Ahn S.-H., Yoon K.-S., Kang C.-S., Cho H.M.,
RA   Lee H.S., Choe J.J., Choi C.W., Kim B.S., Shin S.W., Kim Y.H.,
RA   Kim J.S., Son G.-S., Lee J.-B., Koo B.H.;
RT   "BRCA1 and BRCA2 germline mutations in Korean patients with sporadic
RT   breast cancer.";
RL   Hum. Mutat. 24:350-350(2004).
RN   [89]
RP   VARIANTS [LARGE SCALE ANALYSIS] PHE-30; PHE-758 AND CYS-778.
RX   PubMed=16959974; DOI=10.1126/science.1133427;
RA   Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA   Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
RA   Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
RA   Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
RA   Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
RA   Vogelstein B., Kinzler K.W., Velculescu V.E.;
RT   "The consensus coding sequences of human breast and colorectal
RT   cancers.";
RL   Science 314:268-274(2006).
RN   [90]
RP   VARIANTS THR-18; MET-1495; GLY-1623; ILE-1685; ALA-1685; ARG-1689;
RP   TRP-1699; GLU-1706; GLU-1708; ARG-1715; ARG-1738; PRO-1764; SER-1766
RP   AND VAL-1788.
RX   PubMed=17924331; DOI=10.1086/521032;
RA   Easton D.F., Deffenbaugh A.M., Pruss D., Frye C., Wenstrup R.J.,
RA   Allen-Brady K., Tavtigian S.V., Monteiro A.N.A., Iversen E.S.,
RA   Couch F.J., Goldgar D.E.;
RT   "A systematic genetic assessment of 1,433 sequence variants of unknown
RT   clinical significance in the BRCA1 and BRCA2 breast cancer-
RT   predisposition genes.";
RL   Am. J. Hum. Genet. 81:873-883(2007).
RN   [91]
RP   CHARACTERIZATION OF VARIANTS GLY-1623 AND ILE-1685.
RX   PubMed=20513136; DOI=10.1002/humu.21267;
RA   Walker L.C., Whiley P.J., Couch F.J., Farrugia D.J., Healey S.,
RA   Eccles D.M., Lin F., Butler S.A., Goff S.A., Thompson B.A.,
RA   Lakhani S.R., Da Silva L.M., Tavtigian S.V., Goldgar D.E., Brown M.A.,
RA   Spurdle A.B.;
RT   "Detection of splicing aberrations caused by BRCA1 and BRCA2 sequence
RT   variants encoding missense substitutions: implications for prediction
RT   of pathogenicity.";
RL   Hum. Mutat. 31:E1484-E1505(2010).
RN   [92]
RP   CHARACTERIZATION OF VARIANTS BC PHE-4; THR-18; GLN-45; GLY-61; GLY-64;
RP   TYR-67; LYS-132; HIS-142; PHE-147; PRO-165; TRP-170; TYR-186; ILE-191;
RP   MET-231; VAL-245; VAL-246; LEU-271; PHE-668; ASN-695; LEU-798;
RP   TYR-810; LYS-826; GLN-841; HIS-856; ASN-1101; ASN-1140; GLY-1140;
RP   LYS-1214; LYS-1236; SER-1267; VAL-1282; SER-1297 DEL; ARG-1301;
RP   LYS-1346; ILE-1378; VAL-1400; PRO-1407; THR-1411; GLY-1443; GLY-1448;
RP   CYS-1486; MET-1534; PRO-1589; THR-1628; PRO-1651; PHE-1651; PHE-1655;
RP   ARG-1686; GLN-1686; VAL-1688 DEL; ILE-1691; TRP-1699; GLN-1699;
RP   GLU-1706; ALA-1706; GLU-1708; CYS-1718; ALA-1720; LYS-1735; ALA-1736;
RP   GLY-1739; VAL-1739; GLN-1746; THR-1753; PRO-1764; SER-1767; VAL-1770;
RP   CYS-1782; THR-1789; ASP-1794; ASP-1804; ARG-1812; ARG-1837 AND
RP   LEU-1862, AND VARIANTS CYS-105; CYS-866; ALA-1060; LYS-1250 AND
RP   ILE-1652.
RX   PubMed=23867111; DOI=10.1158/2159-8290.CD-13-0094;
RA   Bouwman P., van der Gulden H., van der Heijden I., Drost R.,
RA   Klijn C.N., Prasetyanti P., Pieterse M., Wientjens E., Seibler J.,
RA   Hogervorst F.B., Jonkers J.;
RT   "A high-throughput functional complementation assay for classification
RT   of BRCA1 missense variants.";
RL   Cancer Discov. 3:1142-1155(2013).
CC   -!- FUNCTION: E3 ubiquitin-protein ligase that specifically mediates
CC       the formation of 'Lys-6'-linked polyubiquitin chains and plays a
CC       central role in DNA repair by facilitating cellular responses to
CC       DNA damage. It is unclear whether it also mediates the formation
CC       of other types of polyubiquitin chains. The E3 ubiquitin-protein
CC       ligase activity is required for its tumor suppressor function. The
CC       BRCA1-BARD1 heterodimer coordinates a diverse range of cellular
CC       pathways such as DNA damage repair, ubiquitination and
CC       transcriptional regulation to maintain genomic stability.
CC       Regulates centrosomal microtubule nucleation. Required for normal
CC       cell cycle progression from G2 to mitosis. Required for
CC       appropriate cell cycle arrests after ionizing irradiation in both
CC       the S-phase and the G2 phase of the cell cycle. Involved in
CC       transcriptional regulation of P21 in response to DNA damage.
CC       Required for FANCD2 targeting to sites of DNA damage. May function
CC       as a transcriptional regulator. Inhibits lipid synthesis by
CC       binding to inactive phosphorylated ACACA and preventing its
CC       dephosphorylation. Contributes to homologous recombination repair
CC       (HRR) via its direct interaction with PALB2, fine-tunes
CC       recombinational repair partly through its modulatory role in the
CC       PALB2-dependent loading of BRCA2-RAD51 repair machinery at DNA
CC       breaks. Component of the BRCA1-RBBP8 complex which regulates CHEK1
CC       activation and controls cell cycle G2/M checkpoints on DNA damage
CC       via BRCA1-mediated ubiquitination of RBBP8. Acts as a
CC       transcriptional activator (PubMed:20160719).
CC       {ECO:0000269|PubMed:10500182, ECO:0000269|PubMed:10724175,
CC       ECO:0000269|PubMed:11836499, ECO:0000269|PubMed:12887909,
CC       ECO:0000269|PubMed:12890688, ECO:0000269|PubMed:14976165,
CC       ECO:0000269|PubMed:14990569, ECO:0000269|PubMed:16326698,
CC       ECO:0000269|PubMed:16818604, ECO:0000269|PubMed:17525340,
CC       ECO:0000269|PubMed:18056443, ECO:0000269|PubMed:19261748,
CC       ECO:0000269|PubMed:19369211, ECO:0000269|PubMed:20160719,
CC       ECO:0000269|PubMed:20351172, ECO:0000269|PubMed:20364141}.
CC   -!- ENZYME REGULATION: The E3 ubiquitin-protein ligase activity is
CC       inhibited by phosphorylation by AURKA. Activity is increased by
CC       phosphatase treatment. {ECO:0000269|PubMed:18056443}.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: Heterodimer with BARD1. Part of the BRCA1-associated
CC       genome surveillance complex (BASC), which contains BRCA1, MSH2,
CC       MSH6, MLH1, ATM, BLM, PMS2 and the MRE11-RAD50-NBN protein (MRN)
CC       complex. This association could be a dynamic process changing
CC       throughout the cell cycle and within subnuclear domains. Component
CC       of the BRCA1-A complex, at least composed of the BRCA1, BARD1,
CC       UIMC1, BRCC3, BRE and BABAM1. Interacts (via the BRCT domains)
CC       with FAM175A. Component of the BRCA1-RBBP8 complex. Interacts (via
CC       the BRCT domains) with RBBP8 ('Ser-327' phosphorylated form); the
CC       interaction ubiquitinates RBBP8, regulates CHEK1 activation, and
CC       involves RBBP8 in BRCA1-dependent G2/M checkpoint control on DNA
CC       damage. Associates with RNA polymerase II holoenzyme. Interacts
CC       with SMC1A, COBRA1, DCLRE1C, CLSPN. CHEK1, CHEK2, BAP1, BRCC3,
CC       AURKA, UBXN1 and KIAA0101/PAF15. Interacts (via BRCT domains) with
CC       BRIP1 (phosphorylated form). Interacts with FANCD2 (ubiquitinated
CC       form). Interacts with H2AFX (phosphorylated on 'Ser-140').
CC       Interacts (via the BRCT domains) with ACACA (phosphorylated form);
CC       the interaction prevents dephosphorylation of ACACA. Part of a
CC       BRCA complex containing BRCA1, BRCA2 and PALB2. Interacts directly
CC       with PALB2; the interaction is essential for its function in HRR.
CC       Interacts directly with BRCA2; the interaction occurs only in the
CC       presence of PALB2 which serves as the bridging protein. Interacts
CC       (via the BRCT domains) with LMO4; the interaction represses the
CC       transcriptional activity of BRCA1. Interacts (via the BRCT
CC       domains) with CCAR2 (via N-terminus); the interaction represses
CC       the transcriptional activator activity of BRCA1.
CC       {ECO:0000269|PubMed:10724175, ECO:0000269|PubMed:10783165,
CC       ECO:0000269|PubMed:11239454, ECO:0000269|PubMed:11301010,
CC       ECO:0000269|PubMed:11573085, ECO:0000269|PubMed:11739404,
CC       ECO:0000269|PubMed:11751867, ECO:0000269|PubMed:11836499,
CC       ECO:0000269|PubMed:11877377, ECO:0000269|PubMed:12360400,
CC       ECO:0000269|PubMed:12419185, ECO:0000269|PubMed:12890688,
CC       ECO:0000269|PubMed:14636569, ECO:0000269|PubMed:14976165,
CC       ECO:0000269|PubMed:14990569, ECO:0000269|PubMed:15096610,
CC       ECO:0000269|PubMed:15133502, ECO:0000269|PubMed:15456891,
CC       ECO:0000269|PubMed:16101277, ECO:0000269|PubMed:16326698,
CC       ECO:0000269|PubMed:16698035, ECO:0000269|PubMed:16818604,
CC       ECO:0000269|PubMed:17525340, ECO:0000269|PubMed:17643121,
CC       ECO:0000269|PubMed:17643122, ECO:0000269|PubMed:18452305,
CC       ECO:0000269|PubMed:19261746, ECO:0000269|PubMed:19261748,
CC       ECO:0000269|PubMed:19261749, ECO:0000269|PubMed:19369211,
CC       ECO:0000269|PubMed:20159462, ECO:0000269|PubMed:20160719,
CC       ECO:0000269|PubMed:20351172, ECO:0000269|PubMed:21673012,
CC       ECO:0000269|PubMed:9528852, ECO:0000269|PubMed:9811458}.
CC   -!- INTERACTION:
CC       Q13085:ACACA; NbExp=2; IntAct=EBI-349905, EBI-717681;
CC       Q92560:BAP1; NbExp=3; IntAct=EBI-349905, EBI-1791447;
CC       Q99728:BARD1; NbExp=9; IntAct=EBI-349905, EBI-473181;
CC       P10415:BCL2; NbExp=6; IntAct=EBI-349905, EBI-77694;
CC       Q7Z569:BRAP; NbExp=3; IntAct=EBI-349905, EBI-349900;
CC       Q6PJG6:BRAT1; NbExp=6; IntAct=EBI-349905, EBI-10826195;
CC       Q9BX63:BRIP1; NbExp=12; IntAct=EBI-349905, EBI-3509650;
CC       P24385:CCND1; NbExp=3; IntAct=EBI-349905, EBI-375001;
CC       P24864:CCNE1; NbExp=2; IntAct=EBI-349905, EBI-519526;
CC       O14757:CHEK1; NbExp=3; IntAct=EBI-349905, EBI-974488;
CC       P03372:ESR1; NbExp=12; IntAct=EBI-349905, EBI-78473;
CC       Q61188:Ezh2 (xeno); NbExp=5; IntAct=EBI-349905, EBI-904311;
CC       Q6UWZ7:FAM175A; NbExp=10; IntAct=EBI-349905, EBI-1263451;
CC       Q14192:FHL2; NbExp=6; IntAct=EBI-349905, EBI-701903;
CC       P78347:GTF2I; NbExp=5; IntAct=EBI-349905, EBI-359622;
CC       P16104:H2AFX; NbExp=4; IntAct=EBI-349905, EBI-494830;
CC       P10809:HSPD1; NbExp=2; IntAct=EBI-349905, EBI-352528;
CC       Q16666:IFI16; NbExp=9; IntAct=EBI-349905, EBI-2867186;
CC       P52292:KPNA2; NbExp=3; IntAct=EBI-349905, EBI-349938;
CC       Q8WX92:NELFB; NbExp=5; IntAct=EBI-349905, EBI-347721;
CC       P62136:PPP1CA; NbExp=2; IntAct=EBI-349905, EBI-357253;
CC       P62140:PPP1CB; NbExp=3; IntAct=EBI-349905, EBI-352350;
CC       P36873:PPP1CC; NbExp=2; IntAct=EBI-349905, EBI-356283;
CC       Q99708:RBBP8; NbExp=9; IntAct=EBI-349905, EBI-745715;
CC       Q9Y4A5:TRRAP; NbExp=8; IntAct=EBI-349905, EBI-399128;
CC       Q96RL1:UIMC1; NbExp=9; IntAct=EBI-349905, EBI-725300;
CC       Q6NZY4:ZCCHC8; NbExp=2; IntAct=EBI-349905, EBI-1263058;
CC       Q9GZX5:ZNF350; NbExp=3; IntAct=EBI-349905, EBI-396421;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15133502,
CC       ECO:0000269|PubMed:17525340, ECO:0000269|PubMed:20160719,
CC       ECO:0000269|PubMed:21144835, ECO:0000269|PubMed:9528852}.
CC       Chromosome {ECO:0000250|UniProtKB:P48754}. Cytoplasm
CC       {ECO:0000269|PubMed:20160719}. Note=Localizes at sites of DNA
CC       damage at double-strand breaks (DSBs); recruitment to DNA damage
CC       sites is mediated by the BRCA1-A complex. Translocated to the
CC       cytoplasm during UV-induced apoptosis.
CC       {ECO:0000269|PubMed:20160719}.
CC   -!- SUBCELLULAR LOCATION: Isoform 3: Cytoplasm.
CC   -!- SUBCELLULAR LOCATION: Isoform 5: Cytoplasm
CC       {ECO:0000269|PubMed:8972225}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing, Alternative initiation; Named isoforms=8;
CC       Name=1;
CC         IsoId=P38398-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P38398-2; Sequence=VSP_047891;
CC         Note=May be produced at very low levels due to a premature stop
CC         codon in the mRNA, leading to nonsense-mediated mRNA decay.;
CC       Name=3; Synonyms=Delta11b;
CC         IsoId=P38398-3; Sequence=VSP_035399, VSP_043797;
CC       Name=4; Synonyms=DeltaBRCA1(17aa);
CC         IsoId=P38398-4; Sequence=VSP_035396;
CC         Note=Produced by alternative initiation at Met-18 of isoform 1.;
CC       Name=5; Synonyms=Delta11, Delta772-3095;
CC         IsoId=P38398-5; Sequence=VSP_035398;
CC       Name=6;
CC         IsoId=P38398-6; Sequence=VSP_035399, VSP_043797, VSP_043798;
CC         Note=No experimental confirmation available.;
CC       Name=7;
CC         IsoId=P38398-7; Sequence=VSP_055404;
CC         Note=No experimental confirmation available. Ref.8 (AAI15038)
CC         sequence is in conflict in position: 1461:N->D. {ECO:0000305};
CC       Name=8;
CC         IsoId=P38398-8; Sequence=VSP_057569;
CC         Note=No experimental confirmation available. The N-terminus is
CC         confirmed by several cDNAs. {ECO:0000305};
CC   -!- TISSUE SPECIFICITY: Isoform 1 and isoform 3 are widely expressed.
CC       Isoform 3 is reduced or absent in several breast and ovarian
CC       cancer cell lines.
CC   -!- DOMAIN: The BRCT domains recognize and bind phosphorylated pSXXF
CC       motif on proteins. The interaction with the phosphorylated pSXXF
CC       motif of FAM175A/Abraxas, recruits BRCA1 at DNA damage sites.
CC       {ECO:0000269|PubMed:20159462}.
CC   -!- DOMAIN: The RING-type zinc finger domain interacts with BAP1.
CC       {ECO:0000269|PubMed:20159462}.
CC   -!- PTM: Phosphorylation at Ser-308 by AURKA is required for normal
CC       cell cycle progression from G2 to mitosis. Phosphorylated in
CC       response to IR, UV, and various stimuli that cause checkpoint
CC       activation, probably by ATM or ATR. Phosphorylation at Ser-988 by
CC       CHEK2 regulates mitotic spindle assembly.
CC       {ECO:0000269|PubMed:10724175, ECO:0000269|PubMed:11114888,
CC       ECO:0000269|PubMed:12183412, ECO:0000269|PubMed:14990569,
CC       ECO:0000269|PubMed:18056443, ECO:0000269|PubMed:20364141,
CC       ECO:0000269|PubMed:21144835}.
CC   -!- PTM: Autoubiquitinated, undergoes 'Lys-6'-linked
CC       polyubiquitination. 'Lys-6'-linked polyubiquitination does not
CC       promote degradation. {ECO:0000269|PubMed:12890688,
CC       ECO:0000269|PubMed:20351172}.
CC   -!- POLYMORPHISM: There is evidence that the presence of the rare form
CC       of Gln-356-Arg and Leu-871-Pro polymorphisms may be associated
CC       with an increased risk for developing ovarian cancer.
CC   -!- DISEASE: Breast cancer (BC) [MIM:114480]: A common malignancy
CC       originating from breast epithelial tissue. Breast neoplasms can be
CC       distinguished by their histologic pattern. Invasive ductal
CC       carcinoma is by far the most common type. Breast cancer is
CC       etiologically and genetically heterogeneous. Important genetic
CC       factors have been indicated by familial occurrence and bilateral
CC       involvement. Mutations at more than one locus can be involved in
CC       different families or even in the same case.
CC       {ECO:0000269|PubMed:10323242, ECO:0000269|PubMed:12442275,
CC       ECO:0000269|PubMed:12938098, ECO:0000269|PubMed:14722926,
CC       ECO:0000269|PubMed:18285836, ECO:0000269|PubMed:7545954,
CC       ECO:0000269|PubMed:7894491, ECO:0000269|PubMed:7894493,
CC       ECO:0000269|PubMed:7939630, ECO:0000269|PubMed:8554067,
CC       ECO:0000269|PubMed:8723683, ECO:0000269|PubMed:8776600,
CC       ECO:0000269|PubMed:9482581, ECO:0000269|PubMed:9609997,
CC       ECO:0000269|PubMed:9760198}. Note=Disease susceptibility is
CC       associated with variations affecting the gene represented in this
CC       entry. Mutations in BRCA1 are thought to be responsible for 45% of
CC       inherited breast cancer. Moreover, BRCA1 carriers have a 4-fold
CC       increased risk of colon cancer, whereas male carriers face a 3-
CC       fold increased risk of prostate cancer. Cells lacking BRCA1 show
CC       defects in DNA repair by homologous recombination.
CC   -!- DISEASE: Breast-ovarian cancer, familial, 1 (BROVCA1)
CC       [MIM:604370]: A condition associated with familial predisposition
CC       to cancer of the breast and ovaries. Characteristic features in
CC       affected families are an early age of onset of breast cancer
CC       (often before age 50), increased chance of bilateral cancers
CC       (cancer that develop in both breasts, or both ovaries,
CC       independently), frequent occurrence of breast cancer among men,
CC       increased incidence of tumors of other specific organs, such as
CC       the prostate. {ECO:0000269|PubMed:12938098,
CC       ECO:0000269|PubMed:14722926, ECO:0000269|PubMed:8968716}.
CC       Note=Disease susceptibility is associated with variations
CC       affecting the gene represented in this entry. Mutations in BRCA1
CC       are thought to be responsible for more than 80% of inherited
CC       breast-ovarian cancer.
CC   -!- DISEASE: Ovarian cancer (OC) [MIM:167000]: The term ovarian cancer
CC       defines malignancies originating from ovarian tissue. Although
CC       many histologic types of ovarian tumors have been described,
CC       epithelial ovarian carcinoma is the most common form. Ovarian
CC       cancers are often asymptomatic and the recognized signs and
CC       symptoms, even of late-stage disease, are vague. Consequently,
CC       most patients are diagnosed with advanced disease.
CC       {ECO:0000269|PubMed:10196379, ECO:0000269|PubMed:10486320,
CC       ECO:0000269|PubMed:14746861}. Note=Disease susceptibility is
CC       associated with variations affecting the gene represented in this
CC       entry.
CC   -!- DISEASE: Pancreatic cancer 4 (PNCA4) [MIM:614320]: A malignant
CC       neoplasm of the pancreas. Tumors can arise from both the exocrine
CC       and endocrine portions of the pancreas, but 95% of them develop
CC       from the exocrine portion, including the ductal epithelium, acinar
CC       cells, connective tissue, and lymphatic tissue.
CC       {ECO:0000269|PubMed:18762988}. Note=Disease susceptibility is
CC       associated with variations affecting the gene represented in this
CC       entry.
CC   -!- SIMILARITY: Contains 2 BRCT domains. {ECO:0000255|PROSITE-
CC       ProRule:PRU00033}.
CC   -!- SIMILARITY: Contains 1 RING-type zinc finger.
CC       {ECO:0000255|PROSITE-ProRule:PRU00175}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB61673.1; Type=Erroneous translation; Note=Wrong choice of CDS.; Evidence={ECO:0000305};
CC       Sequence=AAI15038.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
CC       Sequence=AAI15038.1; Type=Erroneous termination; Positions=526; Note=Translated as Gln.; Evidence={ECO:0000305};
CC   -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC       and Haematology;
CC       URL="http://atlasgeneticsoncology.org/Genes/BRCA1ID163ch17q21.html";
CC   -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC       URL="http://egp.gs.washington.edu/data/brca1/";
CC   -!- WEB RESOURCE: Name=SHMPD; Note=The Singapore human mutation and
CC       polymorphism database;
CC       URL="http://shmpd.bii.a-star.edu.sg/gene.php?genestart=A&genename=BRCA1";
CC   -!- WEB RESOURCE: Name=Wikipedia; Note=BRCA1 entry;
CC       URL="https://en.wikipedia.org/wiki/BRCA1";
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DR   EMBL; U14680; AAA73985.1; -; mRNA.
DR   EMBL; L78833; AAC37594.1; -; Genomic_DNA.
DR   EMBL; U64805; AAC00049.1; -; mRNA.
DR   EMBL; AF005068; AAB61673.1; ALT_SEQ; mRNA.
DR   EMBL; DQ190450; ABA29208.1; -; Genomic_DNA.
DR   EMBL; DQ190451; ABA29211.1; -; Genomic_DNA.
DR   EMBL; DQ190452; ABA29214.1; -; Genomic_DNA.
DR   EMBL; DQ190453; ABA29217.1; -; Genomic_DNA.
DR   EMBL; DQ190454; ABA29220.1; -; Genomic_DNA.
DR   EMBL; DQ190455; ABA29223.1; -; Genomic_DNA.
DR   EMBL; DQ190456; ABA29226.1; -; Genomic_DNA.
DR   EMBL; AY273801; AAP12647.1; -; Genomic_DNA.
DR   EMBL; AC060780; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC135721; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC072418; AAH72418.1; -; mRNA.
DR   EMBL; BC115037; AAI15038.1; ALT_SEQ; mRNA.
DR   CCDS; CCDS11453.1; -. [P38398-1]
DR   CCDS; CCDS11454.2; -. [P38398-3]
DR   CCDS; CCDS11455.2; -. [P38398-6]
DR   CCDS; CCDS11456.2; -. [P38398-7]
DR   CCDS; CCDS11459.2; -. [P38398-8]
DR   PIR; A58881; A58881.
DR   RefSeq; NP_009225.1; NM_007294.3. [P38398-1]
DR   RefSeq; NP_009228.2; NM_007297.3. [P38398-8]
DR   RefSeq; NP_009229.2; NM_007298.3. [P38398-3]
DR   RefSeq; NP_009230.2; NM_007299.3. [P38398-6]
DR   RefSeq; NP_009231.2; NM_007300.3. [P38398-7]
DR   UniGene; Hs.194143; -.
DR   PDB; 1JM7; NMR; -; A=1-110.
DR   PDB; 1JNX; X-ray; 2.50 A; X=1646-1859.
DR   PDB; 1N5O; X-ray; 2.80 A; X=1646-1859.
DR   PDB; 1OQA; NMR; -; A=1755-1863.
DR   PDB; 1T15; X-ray; 1.85 A; A=1646-1859.
DR   PDB; 1T29; X-ray; 2.30 A; A=1646-1859.
DR   PDB; 1T2U; X-ray; 2.80 A; A=1646-1859.
DR   PDB; 1T2V; X-ray; 3.30 A; A/B/C/D/E=1646-1859.
DR   PDB; 1Y98; X-ray; 2.50 A; A=1646-1859.
DR   PDB; 2ING; X-ray; 3.60 A; X=1649-1859.
DR   PDB; 3COJ; X-ray; 3.21 A; A/B/C/D/E/F/G/X=1646-1859.
DR   PDB; 3K0H; X-ray; 2.70 A; A=1646-1859.
DR   PDB; 3K0K; X-ray; 2.70 A; A=1646-1859.
DR   PDB; 3K15; X-ray; 2.80 A; A=1646-1859.
DR   PDB; 3K16; X-ray; 3.00 A; A=1646-1859.
DR   PDB; 3PXA; X-ray; 2.55 A; A=1646-1859.
DR   PDB; 3PXB; X-ray; 2.50 A; A=1646-1859.
DR   PDB; 3PXC; X-ray; 2.80 A; X=1646-1859.
DR   PDB; 3PXD; X-ray; 2.80 A; A=1646-1859.
DR   PDB; 3PXE; X-ray; 2.85 A; A/B/C/D=1646-1859.
DR   PDB; 4IFI; X-ray; 2.20 A; A=1646-1859.
DR   PDB; 4IGK; X-ray; 1.75 A; A/B=1646-1859.
DR   PDB; 4JLU; X-ray; 3.50 A; A=1649-1859.
DR   PDB; 4OFB; X-ray; 3.05 A; A=1646-1859.
DR   PDB; 4U4A; X-ray; 3.51 A; A/B/C=1646-1859.
DR   PDBsum; 1JM7; -.
DR   PDBsum; 1JNX; -.
DR   PDBsum; 1N5O; -.
DR   PDBsum; 1OQA; -.
DR   PDBsum; 1T15; -.
DR   PDBsum; 1T29; -.
DR   PDBsum; 1T2U; -.
DR   PDBsum; 1T2V; -.
DR   PDBsum; 1Y98; -.
DR   PDBsum; 2ING; -.
DR   PDBsum; 3COJ; -.
DR   PDBsum; 3K0H; -.
DR   PDBsum; 3K0K; -.
DR   PDBsum; 3K15; -.
DR   PDBsum; 3K16; -.
DR   PDBsum; 3PXA; -.
DR   PDBsum; 3PXB; -.
DR   PDBsum; 3PXC; -.
DR   PDBsum; 3PXD; -.
DR   PDBsum; 3PXE; -.
DR   PDBsum; 4IFI; -.
DR   PDBsum; 4IGK; -.
DR   PDBsum; 4JLU; -.
DR   PDBsum; 4OFB; -.
DR   PDBsum; 4U4A; -.
DR   DisProt; DP00238; -.
DR   ProteinModelPortal; P38398; -.
DR   SMR; P38398; 1-103, 1649-1859.
DR   BioGrid; 107140; 561.
DR   DIP; DIP-5971N; -.
DR   IntAct; P38398; 74.
DR   MINT; MINT-90433; -.
DR   STRING; 9606.ENSP00000418960; -.
DR   BindingDB; P38398; -.
DR   ChEMBL; CHEMBL5990; -.
DR   PhosphoSite; P38398; -.
DR   BioMuta; BRCA1; -.
DR   DMDM; 728984; -.
DR   MaxQB; P38398; -.
DR   PaxDb; P38398; -.
DR   PRIDE; P38398; -.
DR   DNASU; 672; -.
DR   Ensembl; ENST00000352993; ENSP00000312236; ENSG00000012048. [P38398-5]
DR   Ensembl; ENST00000357654; ENSP00000350283; ENSG00000012048. [P38398-1]
DR   Ensembl; ENST00000461221; ENSP00000418548; ENSG00000012048. [P38398-2]
DR   Ensembl; ENST00000461798; ENSP00000417988; ENSG00000012048. [P38398-2]
DR   Ensembl; ENST00000468300; ENSP00000417148; ENSG00000012048. [P38398-6]
DR   Ensembl; ENST00000471181; ENSP00000418960; ENSG00000012048. [P38398-7]
DR   Ensembl; ENST00000491747; ENSP00000420705; ENSG00000012048. [P38398-3]
DR   Ensembl; ENST00000493795; ENSP00000418775; ENSG00000012048. [P38398-8]
DR   GeneID; 672; -.
DR   KEGG; hsa:672; -.
DR   UCSC; uc002icp.4; human. [P38398-2]
DR   UCSC; uc002icq.3; human. [P38398-1]
DR   UCSC; uc002icu.3; human. [P38398-6]
DR   UCSC; uc010whq.1; human. [P38398-3]
DR   CTD; 672; -.
DR   GeneCards; BRCA1; -.
DR   GeneReviews; BRCA1; -.
DR   HGNC; HGNC:1100; BRCA1.
DR   HPA; CAB001946; -.
DR   HPA; CAB018369; -.
DR   HPA; HPA034966; -.
DR   MIM; 113705; gene.
DR   MIM; 114480; phenotype.
DR   MIM; 167000; phenotype.
DR   MIM; 604370; phenotype.
DR   MIM; 614320; phenotype.
DR   neXtProt; NX_P38398; -.
DR   Orphanet; 1333; Familial pancreatic carcinoma.
DR   Orphanet; 1331; Familial prostate cancer.
DR   Orphanet; 145; Hereditary breast and ovarian cancer syndrome.
DR   Orphanet; 227535; Hereditary breast cancer.
DR   Orphanet; 213524; Hereditary site-specific ovarian cancer syndrome.
DR   Orphanet; 168829; Primary peritoneal carcinoma.
DR   PharmGKB; PA25411; -.
DR   eggNOG; ENOG410ITQ4; Eukaryota.
DR   eggNOG; ENOG4112BIH; LUCA.
DR   GeneTree; ENSGT00440000034289; -.
DR   HOGENOM; HOG000230969; -.
DR   HOVERGEN; HBG050730; -.
DR   InParanoid; P38398; -.
DR   KO; K10605; -.
DR   OMA; FQHLLFG; -.
DR   OrthoDB; EOG79CXXK; -.
DR   PhylomeDB; P38398; -.
DR   BRENDA; 6.3.2.19; 2681.
DR   Reactome; R-HSA-1221632; Meiotic synapsis.
DR   Reactome; R-HSA-3108214; SUMOylation of DNA damage response and repair proteins.
DR   Reactome; R-HSA-419524; Fanconi Anemia pathway.
DR   Reactome; R-HSA-69473; G2/M DNA damage checkpoint.
DR   Reactome; R-HSA-75148; ATM mediated phosphorylation of repair proteins.
DR   Reactome; R-HSA-75154; Recruitment of repair and signaling proteins to double-strand breaks.
DR   Reactome; R-HSA-912446; Meiotic recombination.
DR   SignaLink; P38398; -.
DR   UniPathway; UPA00143; -.
DR   ChiTaRS; BRCA1; human.
DR   EvolutionaryTrace; P38398; -.
DR   GeneWiki; BRCA1; -.
DR   GenomeRNAi; 672; -.
DR   NextBio; 2752; -.
DR   PMAP-CutDB; P38398; -.
DR   PRO; PR:P38398; -.
DR   Proteomes; UP000005640; Chromosome 17.
DR   Bgee; P38398; -.
DR   CleanEx; HS_BRCA1; -.
DR   ExpressionAtlas; P38398; baseline and differential.
DR   Genevisible; P38398; HS.
DR   GO; GO:0070531; C:BRCA1-A complex; IDA:UniProtKB.
DR   GO; GO:0031436; C:BRCA1-BARD1 complex; IDA:UniProtKB.
DR   GO; GO:0005694; C:chromosome; ISS:UniProtKB.
DR   GO; GO:0000794; C:condensed nuclear chromosome; IEA:Ensembl.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0008274; C:gamma-tubulin ring complex; NAS:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IDA:BHF-UCL.
DR   GO; GO:0043234; C:protein complex; IDA:UniProtKB.
DR   GO; GO:0030529; C:ribonucleoprotein complex; IDA:MGI.
DR   GO; GO:0000151; C:ubiquitin ligase complex; NAS:UniProtKB.
DR   GO; GO:0050681; F:androgen receptor binding; NAS:UniProtKB.
DR   GO; GO:0003684; F:damaged DNA binding; IEA:Ensembl.
DR   GO; GO:0003677; F:DNA binding; TAS:ProtInc.
DR   GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IDA:MGI.
DR   GO; GO:0003713; F:transcription coactivator activity; NAS:UniProtKB.
DR   GO; GO:0044212; F:transcription regulatory region DNA binding; IDA:BHF-UCL.
DR   GO; GO:0015631; F:tubulin binding; NAS:UniProtKB.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; TAS:ProtInc.
DR   GO; GO:0030521; P:androgen receptor signaling pathway; NAS:UniProtKB.
DR   GO; GO:0006915; P:apoptotic process; TAS:UniProtKB.
DR   GO; GO:0044267; P:cellular protein metabolic process; TAS:Reactome.
DR   GO; GO:0006974; P:cellular response to DNA damage stimulus; TAS:ProtInc.
DR   GO; GO:0071681; P:cellular response to indole-3-methanol; IDA:UniProtKB.
DR   GO; GO:0071356; P:cellular response to tumor necrosis factor; IMP:BHF-UCL.
DR   GO; GO:0007098; P:centrosome cycle; IEA:Ensembl.
DR   GO; GO:0043009; P:chordate embryonic development; IBA:GO_Central.
DR   GO; GO:0031052; P:chromosome breakage; IEA:Ensembl.
DR   GO; GO:0007059; P:chromosome segregation; IMP:UniProtKB.
DR   GO; GO:0006978; P:DNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator; TAS:UniProtKB.
DR   GO; GO:0006281; P:DNA repair; TAS:Reactome.
DR   GO; GO:0006260; P:DNA replication; IEA:Ensembl.
DR   GO; GO:0009048; P:dosage compensation by inactivation of X chromosome; IBA:GO_Central.
DR   GO; GO:0006302; P:double-strand break repair; IMP:UniProtKB.
DR   GO; GO:0000724; P:double-strand break repair via homologous recombination; IDA:HGNC.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0031572; P:G2 DNA damage checkpoint; IMP:UniProtKB.
DR   GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; IDA:MGI.
DR   GO; GO:0046600; P:negative regulation of centriole replication; NAS:UniProtKB.
DR   GO; GO:1902042; P:negative regulation of extrinsic apoptotic signaling pathway via death domain receptors; IMP:BHF-UCL.
DR   GO; GO:0045717; P:negative regulation of fatty acid biosynthetic process; IMP:UniProtKB.
DR   GO; GO:0035067; P:negative regulation of histone acetylation; IBA:GO_Central.
DR   GO; GO:0051572; P:negative regulation of histone H3-K4 methylation; IEA:Ensembl.
DR   GO; GO:0051573; P:negative regulation of histone H3-K9 methylation; IDA:BHF-UCL.
DR   GO; GO:0033147; P:negative regulation of intracellular estrogen receptor signaling pathway; IMP:CACAO.
DR   GO; GO:2000378; P:negative regulation of reactive oxygen species metabolic process; IMP:BHF-UCL.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR   GO; GO:0045766; P:positive regulation of angiogenesis; IMP:BHF-UCL.
DR   GO; GO:0071158; P:positive regulation of cell cycle arrest; IDA:BHF-UCL.
DR   GO; GO:0045739; P:positive regulation of DNA repair; IMP:UniProtKB.
DR   GO; GO:0010628; P:positive regulation of gene expression; IMP:BHF-UCL.
DR   GO; GO:0035066; P:positive regulation of histone acetylation; IDA:BHF-UCL.
DR   GO; GO:0051571; P:positive regulation of histone H3-K4 methylation; IDA:BHF-UCL.
DR   GO; GO:2000617; P:positive regulation of histone H3-K9 acetylation; IDA:BHF-UCL.
DR   GO; GO:0051574; P:positive regulation of histone H3-K9 methylation; IEA:Ensembl.
DR   GO; GO:2000620; P:positive regulation of histone H4-K16 acetylation; IDA:BHF-UCL.
DR   GO; GO:0070512; P:positive regulation of histone H4-K20 methylation; IDA:BHF-UCL.
DR   GO; GO:0031398; P:positive regulation of protein ubiquitination; IDA:UniProtKB.
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; IDA:UniProtKB.
DR   GO; GO:0010575; P:positive regulation of vascular endothelial growth factor production; IMP:BHF-UCL.
DR   GO; GO:0043687; P:post-translational protein modification; TAS:Reactome.
DR   GO; GO:0006301; P:postreplication repair; IDA:HGNC.
DR   GO; GO:0051865; P:protein autoubiquitination; IDA:UniProtKB.
DR   GO; GO:0085020; P:protein K6-linked ubiquitination; IDA:UniProtKB.
DR   GO; GO:0016925; P:protein sumoylation; TAS:Reactome.
DR   GO; GO:0016567; P:protein ubiquitination; IDA:HGNC.
DR   GO; GO:0042981; P:regulation of apoptotic process; TAS:UniProtKB.
DR   GO; GO:0042127; P:regulation of cell proliferation; TAS:UniProtKB.
DR   GO; GO:0044030; P:regulation of DNA methylation; IEA:Ensembl.
DR   GO; GO:0006349; P:regulation of gene expression by genetic imprinting; IEA:Ensembl.
DR   GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; TAS:ProtInc.
DR   GO; GO:0006359; P:regulation of transcription from RNA polymerase III promoter; TAS:UniProtKB.
DR   GO; GO:0043627; P:response to estrogen; IDA:UniProtKB.
DR   GO; GO:0010212; P:response to ionizing radiation; IMP:UniProtKB.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.40.10; -; 1.
DR   Gene3D; 3.40.50.10190; -; 2.
DR   InterPro; IPR011364; BRCA1.
DR   InterPro; IPR031099; BRCA1-associated.
DR   InterPro; IPR025994; BRCA1_serine_dom.
DR   InterPro; IPR001357; BRCT_dom.
DR   InterPro; IPR018957; Znf_C3HC4_RING-type.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   PANTHER; PTHR13763; PTHR13763; 1.
DR   PANTHER; PTHR13763:SF0; PTHR13763:SF0; 1.
DR   Pfam; PF00533; BRCT; 2.
DR   Pfam; PF12820; BRCT_assoc; 1.
DR   Pfam; PF00097; zf-C3HC4; 1.
DR   PIRSF; PIRSF001734; BRCA1; 1.
DR   PRINTS; PR00493; BRSTCANCERI.
DR   SMART; SM00292; BRCT; 2.
DR   SMART; SM00184; RING; 1.
DR   SUPFAM; SSF52113; SSF52113; 2.
DR   PROSITE; PS50172; BRCT; 2.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Activator; Alternative initiation;
KW   Alternative splicing; Cell cycle; Chromosome; Complete proteome;
KW   Cytoplasm; Direct protein sequencing; Disease mutation; DNA damage;
KW   DNA recombination; DNA repair; DNA-binding; Fatty acid biosynthesis;
KW   Fatty acid metabolism; Isopeptide bond; Ligase; Lipid biosynthesis;
KW   Lipid metabolism; Metal-binding; Nucleus; Phosphoprotein;
KW   Polymorphism; Reference proteome; Repeat; Transcription;
KW   Transcription regulation; Tumor suppressor; Ubl conjugation;
KW   Ubl conjugation pathway; Zinc; Zinc-finger.
FT   CHAIN         1   1863       Breast cancer type 1 susceptibility
FT                                protein.
FT                                /FTId=PRO_0000055830.
FT   DOMAIN     1642   1736       BRCT 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00033}.
FT   DOMAIN     1756   1855       BRCT 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00033}.
FT   ZN_FING      24     65       RING-type. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00175}.
FT   REGION     1397   1424       Interaction with PALB2.
FT   COMPBIAS    651    654       Poly-Lys.
FT   MOD_RES       1      1       N-acetylmethionine.
FT                                {ECO:0000244|PubMed:22814378}.
FT   MOD_RES     114    114       Phosphoserine.
FT                                {ECO:0000244|PubMed:20068231,
FT                                ECO:0000244|PubMed:21406692}.
FT   MOD_RES     308    308       Phosphoserine; by AURKA.
FT                                {ECO:0000269|PubMed:14990569}.
FT   MOD_RES     395    395       Phosphoserine.
FT                                {ECO:0000244|PubMed:18669648,
FT                                ECO:0000244|PubMed:19690332}.
FT   MOD_RES     398    398       Phosphoserine.
FT                                {ECO:0000244|PubMed:18669648,
FT                                ECO:0000244|PubMed:19690332}.
FT   MOD_RES     423    423       Phosphoserine.
FT                                {ECO:0000244|PubMed:20068231}.
FT   MOD_RES     694    694       Phosphoserine.
FT                                {ECO:0000244|PubMed:20068231}.
FT   MOD_RES     725    725       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P48754}.
FT   MOD_RES     753    753       Phosphoserine.
FT                                {ECO:0000244|PubMed:18669648}.
FT   MOD_RES     840    840       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P48754}.
FT   MOD_RES     988    988       Phosphoserine; by CHEK2.
FT                                {ECO:0000269|PubMed:10724175,
FT                                ECO:0000269|PubMed:20364141}.
FT   MOD_RES    1143   1143       Phosphoserine; by ATR; in vitro.
FT                                {ECO:0000269|PubMed:11114888}.
FT   MOD_RES    1211   1211       Phosphoserine.
FT                                {ECO:0000244|PubMed:18669648}.
FT   MOD_RES    1217   1217       Phosphoserine.
FT                                {ECO:0000244|PubMed:18669648}.
FT   MOD_RES    1218   1218       Phosphoserine.
FT                                {ECO:0000244|PubMed:18669648,
FT                                ECO:0000244|PubMed:21406692}.
FT   MOD_RES    1280   1280       Phosphoserine; by ATR; in vitro.
FT                                {ECO:0000269|PubMed:11114888}.
FT   MOD_RES    1328   1328       Phosphoserine.
FT                                {ECO:0000244|PubMed:20068231}.
FT   MOD_RES    1336   1336       Phosphoserine.
FT                                {ECO:0000244|PubMed:17081983,
FT                                ECO:0000244|PubMed:20068231,
FT                                ECO:0000244|PubMed:21406692}.
FT   MOD_RES    1342   1342       Phosphoserine.
FT                                {ECO:0000244|PubMed:20068231,
FT                                ECO:0000244|PubMed:21406692}.
FT   MOD_RES    1387   1387       Phosphoserine; by ATM and ATR.
FT                                {ECO:0000269|PubMed:11114888}.
FT   MOD_RES    1394   1394       Phosphothreonine; by ATR; in vitro.
FT                                {ECO:0000269|PubMed:11114888}.
FT   MOD_RES    1423   1423       Phosphoserine; by ATM and ATR.
FT                                {ECO:0000269|PubMed:11114888}.
FT   MOD_RES    1457   1457       Phosphoserine; by ATR; in vitro.
FT                                {ECO:0000269|PubMed:11114888}.
FT   MOD_RES    1524   1524       Phosphoserine; by ATM.
FT                                {ECO:0000269|PubMed:21144835}.
FT   CROSSLNK    339    339       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:25218447}.
FT   CROSSLNK    459    459       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:25218447}.
FT   CROSSLNK    583    583       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:25218447}.
FT   CROSSLNK    654    654       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:25218447}.
FT   CROSSLNK    734    734       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:25218447}.
FT   CROSSLNK    739    739       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:25218447}.
FT   VAR_SEQ       1     47       Missing (in isoform 8).
FT                                /FTId=VSP_057569.
FT   VAR_SEQ       1     17       Missing (in isoform 4). {ECO:0000305}.
FT                                /FTId=VSP_035396.
FT   VAR_SEQ      64   1863       Missing (in isoform 2).
FT                                {ECO:0000303|Ref.4}.
FT                                /FTId=VSP_047891.
FT   VAR_SEQ     224   1365       Missing (in isoform 5). {ECO:0000305}.
FT                                /FTId=VSP_035398.
FT   VAR_SEQ     264   1366       Missing (in isoform 3 and isoform 6).
FT                                {ECO:0000303|PubMed:15489334,
FT                                ECO:0000303|PubMed:9010228}.
FT                                /FTId=VSP_035399.
FT   VAR_SEQ    1453   1453       Missing (in isoform 3 and isoform 6).
FT                                {ECO:0000303|PubMed:15489334,
FT                                ECO:0000303|PubMed:9010228}.
FT                                /FTId=VSP_043797.
FT   VAR_SEQ    1453   1453       A -> DSHIHGQRNNSMFSKRPREHIS (in isoform
FT                                7). {ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_055404.
FT   VAR_SEQ    1778   1863       DQLEWMVQLCGASVVKELSSFTLGTGVHPIVVVQPDAWTED
FT                                NGFHAIGQMCEAPVVTREWVLDSVALYQCQELDTYLIPQIP
FT                                HSHY -> GCPPNCGCAARCLDRGQWLPCNWADV (in
FT                                isoform 6).
FT                                {ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_043798.
FT   VARIANT       4      4       S -> F (in BC; unknown pathological
FT                                significance).
FT                                {ECO:0000269|PubMed:23867111}.
FT                                /FTId=VAR_070458.
FT   VARIANT      10     10       E -> K (in BC and BROVCA1).
FT                                {ECO:0000269|PubMed:14722926}.
FT                                /FTId=VAR_020679.
FT   VARIANT      11     11       V -> A (found in breast-ovarian cancer
FT                                patients; unknown pathological
FT                                significance; dbSNP:rs80357017).
FT                                /FTId=VAR_007754.
FT   VARIANT      18     18       M -> T (in BC; unknown pathological
FT                                significance).
FT                                {ECO:0000269|PubMed:17924331,
FT                                ECO:0000269|PubMed:23867111}.
FT                                /FTId=VAR_063899.
FT   VARIANT      21     21       I -> V (found in breast-ovarian cancer
FT                                patients; unknown pathological
FT                                significance; dbSNP:rs80357406).
FT                                /FTId=VAR_007755.
FT   VARIANT      22     22       L -> S (in BC).
FT                                {ECO:0000269|PubMed:9609997}.
FT                                /FTId=VAR_007756.
FT   VARIANT      23     23       E -> K (in BC and BROVCA1).
FT                                {ECO:0000269|PubMed:14722926}.
FT                                /FTId=VAR_020680.
FT   VARIANT      30     30       L -> F (in a breast cancer sample;
FT                                somatic mutation).
FT                                {ECO:0000269|PubMed:16959974}.
FT                                /FTId=VAR_035947.
FT   VARIANT      45     45       K -> Q (in BC; unknown pathological
FT                                significance; functionally neutral in
FT                                vitro). {ECO:0000269|PubMed:23867111}.
FT                                /FTId=VAR_070459.
FT   VARIANT      61     61       C -> G (in BC and ovarian cancer; no
FT                                interaction with BAP1; dbSNP:rs28897672).
FT                                {ECO:0000269|PubMed:12938098,
FT                                ECO:0000269|PubMed:14746861,
FT                                ECO:0000269|PubMed:23867111,
FT                                ECO:0000269|PubMed:7894493,
FT                                ECO:0000269|PubMed:8554067,
FT                                ECO:0000269|PubMed:9528852,
FT                                ECO:0000269|PubMed:9760198}.
FT                                /FTId=VAR_007757.
FT   VARIANT      64     64       C -> G (in BC; no interaction with BAP1).
FT                                {ECO:0000269|PubMed:23867111,
FT                                ECO:0000269|PubMed:7894491,
FT                                ECO:0000269|PubMed:9482581,
FT                                ECO:0000269|PubMed:9528852}.
FT                                /FTId=VAR_007758.
FT   VARIANT      64     64       C -> Y (in dbSNP:rs55851803).
FT                                /FTId=VAR_007759.
FT   VARIANT      67     67       D -> Y (in BC; unknown pathological
FT                                significance; functionally neutral in
FT                                vitro). {ECO:0000269|PubMed:23867111}.
FT                                /FTId=VAR_070460.
FT   VARIANT      71     71       R -> K (in BC; unknown pathological
FT                                significance).
FT                                {ECO:0000269|PubMed:12938098}.
FT                                /FTId=VAR_020681.
FT   VARIANT     105    105       Y -> C. {ECO:0000269|PubMed:23867111}.
FT                                /FTId=VAR_070461.
FT   VARIANT     132    132       N -> K (in BC; unknown pathological
FT                                significance; functionally neutral in
FT                                vitro). {ECO:0000269|PubMed:23867111}.
FT                                /FTId=VAR_070462.
FT   VARIANT     142    142       P -> H (in BC; unknown pathological
FT                                significance; functionally neutral in
FT                                vitro). {ECO:0000269|PubMed:23867111}.
FT                                /FTId=VAR_070463.
FT   VARIANT     147    147       L -> F (in BC; unknown pathological
FT                                significance; functionally neutral in
FT                                vitro). {ECO:0000269|PubMed:23867111}.
FT                                /FTId=VAR_070464.
FT   VARIANT     153    153       S -> R (in dbSNP:rs28897674).
FT                                /FTId=VAR_052077.
FT   VARIANT     165    165       L -> P (in BC; unknown pathological
FT                                significance; functionally neutral in
FT                                vitro). {ECO:0000269|PubMed:23867111}.
FT                                /FTId=VAR_070465.
FT   VARIANT     170    170       R -> W (in BC; unknown pathological
FT                                significance; functionally neutral in
FT                                vitro). {ECO:0000269|PubMed:23867111}.
FT                                /FTId=VAR_070466.
FT   VARIANT     186    186       S -> Y (in BC; unknown pathological
FT                                significance; functionally neutral in
FT                                vitro). {ECO:0000269|PubMed:23867111}.
FT                                /FTId=VAR_070467.
FT   VARIANT     191    191       V -> I (in BC; unknown pathological
FT                                significance; functionally neutral in
FT                                vitro). {ECO:0000269|PubMed:23867111}.
FT                                /FTId=VAR_070468.
FT   VARIANT     227    227       E -> K (in ovarian cancer; unknown
FT                                pathological significance).
FT                                /FTId=VAR_008759.
FT   VARIANT     231    231       T -> M (in BC; unknown pathological
FT                                significance; functionally neutral in
FT                                vitro). {ECO:0000269|PubMed:23867111}.
FT                                /FTId=VAR_070469.
FT   VARIANT     239    239       H -> R. {ECO:0000269|PubMed:9010228,
FT                                ECO:0000269|PubMed:9760198}.
FT                                /FTId=VAR_007760.
FT   VARIANT     245    245       D -> V (in BC; unknown pathological
FT                                significance; functionally neutral in
FT                                vitro). {ECO:0000269|PubMed:23867111}.
FT                                /FTId=VAR_070470.
FT   VARIANT     246    246       L -> V (in BC; unknown pathological
FT                                significance; functionally neutral in
FT                                vitro). {ECO:0000269|PubMed:23867111}.
FT                                /FTId=VAR_070471.
FT   VARIANT     271    271       V -> L (in BC; unknown pathological
FT                                significance; functionally neutral in
FT                                vitro). {ECO:0000269|PubMed:23867111}.
FT                                /FTId=VAR_070472.
FT   VARIANT     271    271       V -> M (in BC; dbSNP:rs80357244).
FT                                {ECO:0000269|PubMed:8723683}.
FT                                /FTId=VAR_007761.
FT   VARIANT     275    275       G -> S (in dbSNP:rs8176153).
FT                                {ECO:0000269|Ref.6}.
FT                                /FTId=VAR_019944.
FT   VARIANT     346    346       P -> S (in BC; unknown pathological
FT                                significance).
FT                                {ECO:0000269|PubMed:10323242}.
FT                                /FTId=VAR_008760.
FT   VARIANT     356    356       Q -> R (common polymorphism;
FT                                dbSNP:rs1799950).
FT                                {ECO:0000269|PubMed:7894493,
FT                                ECO:0000269|Ref.5, ECO:0000269|Ref.6}.
FT                                /FTId=VAR_007762.
FT   VARIANT     369    369       Missing (in BC).
FT                                /FTId=VAR_007763.
FT   VARIANT     379    379       I -> M (in dbSNP:rs56128296).
FT                                /FTId=VAR_007764.
FT   VARIANT     461    461       F -> L (in BC; dbSNP:rs56046357).
FT                                {ECO:0000269|PubMed:9609997}.
FT                                /FTId=VAR_007765.
FT   VARIANT     465    465       Y -> D (in BC).
FT                                {ECO:0000269|PubMed:9609997}.
FT                                /FTId=VAR_007766.
FT   VARIANT     507    507       R -> I (found in breast-ovarian cancer
FT                                patients; unknown pathological
FT                                significance; dbSNP:rs80357224).
FT                                /FTId=VAR_007767.
FT   VARIANT     552    552       G -> V (in BC).
FT                                {ECO:0000269|PubMed:9609997}.
FT                                /FTId=VAR_007768.
FT   VARIANT     656    656       N -> I. {ECO:0000269|PubMed:12442274}.
FT                                /FTId=VAR_020682.
FT   VARIANT     668    668       L -> F (in BC; unknown pathological
FT                                significance; functionally neutral in
FT                                vitro). {ECO:0000269|PubMed:23867111}.
FT                                /FTId=VAR_070473.
FT   VARIANT     693    693       D -> N (rare polymorphism;
FT                                dbSNP:rs4986850).
FT                                {ECO:0000269|PubMed:15026808,
FT                                ECO:0000269|Ref.6}.
FT                                /FTId=VAR_007769.
FT   VARIANT     695    695       D -> N (in BC; unknown pathological
FT                                significance; functionally neutral in
FT                                vitro). {ECO:0000269|PubMed:23867111}.
FT                                /FTId=VAR_070474.
FT   VARIANT     723    723       N -> D (in dbSNP:rs4986845).
FT                                /FTId=VAR_020110.
FT   VARIANT     749    749       D -> Y (in BC).
FT                                {ECO:0000269|PubMed:12442275}.
FT                                /FTId=VAR_020683.
FT   VARIANT     758    758       L -> F (in a breast cancer sample;
FT                                somatic mutation).
FT                                {ECO:0000269|PubMed:16959974}.
FT                                /FTId=VAR_035948.
FT   VARIANT     772    772       V -> A (rare polymorphism).
FT                                {ECO:0000269|PubMed:7894491,
FT                                ECO:0000269|PubMed:9482581}.
FT                                /FTId=VAR_007770.
FT   VARIANT     778    778       G -> C (in a breast cancer sample;
FT                                somatic mutation).
FT                                {ECO:0000269|PubMed:16959974}.
FT                                /FTId=VAR_035949.
FT   VARIANT     798    798       P -> L (in BC; unknown pathological
FT                                significance; functionally neutral in
FT                                vitro). {ECO:0000269|PubMed:23867111}.
FT                                /FTId=VAR_070475.
FT   VARIANT     810    810       N -> Y (in BC; unknown pathological
FT                                significance; functionally neutral in
FT                                vitro). {ECO:0000269|PubMed:23867111}.
FT                                /FTId=VAR_070476.
FT   VARIANT     820    820       K -> E (rare polymorphism;
FT                                dbSNP:rs56082113).
FT                                {ECO:0000269|PubMed:9482581}.
FT                                /FTId=VAR_007771.
FT   VARIANT     826    826       T -> K (in BC; unknown pathological
FT                                significance; functionally neutral in
FT                                vitro; dbSNP:rs28897683).
FT                                {ECO:0000269|PubMed:23867111}.
FT                                /FTId=VAR_007772.
FT   VARIANT     835    835       H -> Y (in BROVCA1; unknown pathological
FT                                significance).
FT                                {ECO:0000269|PubMed:12938098}.
FT                                /FTId=VAR_020684.
FT   VARIANT     841    841       R -> Q (in BC; unknown pathological
FT                                significance; functionally neutral in
FT                                vitro). {ECO:0000269|PubMed:23867111}.
FT                                /FTId=VAR_070477.
FT   VARIANT     841    841       R -> W (in BROVCA1; unknown pathological
FT                                significance; dbSNP:rs1800709).
FT                                {ECO:0000269|PubMed:8968716,
FT                                ECO:0000269|PubMed:9760198}.
FT                                /FTId=VAR_007773.
FT   VARIANT     856    856       Y -> H (in a patient with sporadic breast
FT                                cancer; unknown pathological
FT                                significance; dbSNP:rs80356892).
FT                                {ECO:0000269|PubMed:15365993,
FT                                ECO:0000269|PubMed:23867111}.
FT                                /FTId=VAR_020685.
FT   VARIANT     866    866       R -> C. {ECO:0000269|PubMed:23867111}.
FT                                /FTId=VAR_070478.
FT   VARIANT     866    866       R -> Q (in BC; unknown pathological
FT                                significance).
FT                                {ECO:0000269|PubMed:12938098}.
FT                                /FTId=VAR_020686.
FT   VARIANT     871    871       P -> L (common polymorphism;
FT                                dbSNP:rs799917).
FT                                {ECO:0000269|PubMed:10323242,
FT                                ECO:0000269|PubMed:12442274,
FT                                ECO:0000269|PubMed:15365993,
FT                                ECO:0000269|PubMed:15489334,
FT                                ECO:0000269|Ref.6}.
FT                                /FTId=VAR_007774.
FT   VARIANT     888    888       H -> Y (in BC; unknown pathological
FT                                significance).
FT                                {ECO:0000269|PubMed:12938098}.
FT                                /FTId=VAR_020687.
FT   VARIANT     892    892       L -> S (in BC).
FT                                {ECO:0000269|PubMed:9609997}.
FT                                /FTId=VAR_007775.
FT   VARIANT     925    925       I -> L (in dbSNP:rs4986847).
FT                                /FTId=VAR_021913.
FT   VARIANT     960    960       G -> D (in BC).
FT                                {ECO:0000269|PubMed:9609997}.
FT                                /FTId=VAR_007776.
FT   VARIANT     989    989       F -> S (in dbSNP:rs4986848).
FT                                /FTId=VAR_020111.
FT   VARIANT    1008   1008       M -> I (common polymorphism;
FT                                dbSNP:rs1800704).
FT                                /FTId=VAR_007777.
FT   VARIANT    1025   1025       T -> I (in BC).
FT                                {ECO:0000269|PubMed:9609997}.
FT                                /FTId=VAR_007778.
FT   VARIANT    1038   1038       E -> G (common polymorphism;
FT                                dbSNP:rs16941).
FT                                {ECO:0000269|PubMed:10323242,
FT                                ECO:0000269|PubMed:15365993,
FT                                ECO:0000269|PubMed:15489334,
FT                                ECO:0000269|PubMed:7894493,
FT                                ECO:0000269|Ref.6}.
FT                                /FTId=VAR_007779.
FT   VARIANT    1040   1040       S -> N (rare polymorphism;
FT                                dbSNP:rs4986852).
FT                                {ECO:0000269|PubMed:15026808,
FT                                ECO:0000269|PubMed:7894491,
FT                                ECO:0000269|PubMed:7894493,
FT                                ECO:0000269|PubMed:9482581,
FT                                ECO:0000269|Ref.6}.
FT                                /FTId=VAR_007780.
FT   VARIANT    1047   1047       V -> A (in BC).
FT                                {ECO:0000269|PubMed:9609997}.
FT                                /FTId=VAR_007781.
FT   VARIANT    1060   1060       E -> A. {ECO:0000269|PubMed:15026808,
FT                                ECO:0000269|PubMed:23867111}.
FT                                /FTId=VAR_020688.
FT   VARIANT    1101   1101       S -> N (in BC; unknown pathological
FT                                significance; functionally neutral in
FT                                vitro). {ECO:0000269|PubMed:23867111}.
FT                                /FTId=VAR_070479.
FT   VARIANT    1139   1139       S -> I (in BC; unknown pathological
FT                                significance).
FT                                {ECO:0000269|PubMed:12938098}.
FT                                /FTId=VAR_020689.
FT   VARIANT    1140   1140       S -> G (in BC; unknown pathological
FT                                significance; functionally neutral in
FT                                vitro; dbSNP:rs2227945).
FT                                {ECO:0000269|PubMed:23867111,
FT                                ECO:0000269|Ref.6}.
FT                                /FTId=VAR_019945.
FT   VARIANT    1140   1140       S -> N (in BC; unknown pathological
FT                                significance; functionally neutral in
FT                                vitro). {ECO:0000269|PubMed:23867111}.
FT                                /FTId=VAR_070480.
FT   VARIANT    1150   1150       P -> S (in BC; dbSNP:rs80357272).
FT                                {ECO:0000269|PubMed:8723683}.
FT                                /FTId=VAR_007782.
FT   VARIANT    1183   1183       K -> R (common polymorphism;
FT                                dbSNP:rs16942).
FT                                {ECO:0000269|PubMed:10323242,
FT                                ECO:0000269|PubMed:14722926,
FT                                ECO:0000269|PubMed:15365993,
FT                                ECO:0000269|PubMed:15489334,
FT                                ECO:0000269|PubMed:7894493,
FT                                ECO:0000269|Ref.6}.
FT                                /FTId=VAR_007783.
FT   VARIANT    1187   1187       S -> I (in BC and BROVCA1).
FT                                {ECO:0000269|PubMed:14722926}.
FT                                /FTId=VAR_020690.
FT   VARIANT    1200   1200       Q -> H (in BC and BROVCA1;
FT                                dbSNP:rs56214134).
FT                                {ECO:0000269|PubMed:14722926}.
FT                                /FTId=VAR_020691.
FT   VARIANT    1204   1204       R -> I (in BC).
FT                                {ECO:0000269|PubMed:14722926}.
FT                                /FTId=VAR_020692.
FT   VARIANT    1207   1207       K -> N (in BC).
FT                                {ECO:0000269|PubMed:14722926}.
FT                                /FTId=VAR_020693.
FT   VARIANT    1210   1210       E -> G (in BC; unknown pathological
FT                                significance).
FT                                {ECO:0000269|PubMed:12938098}.
FT                                /FTId=VAR_020694.
FT   VARIANT    1214   1214       E -> K (in BC; unknown pathological
FT                                significance; functionally neutral in
FT                                vitro). {ECO:0000269|PubMed:23867111}.
FT                                /FTId=VAR_070481.
FT   VARIANT    1217   1217       S -> Y (in BC and BROVCA1).
FT                                {ECO:0000269|PubMed:14722926}.
FT                                /FTId=VAR_020695.
FT   VARIANT    1219   1219       E -> D (found in breast-ovarian cancer
FT                                patients; unknown pathological
FT                                significance; dbSNP:rs80356876).
FT                                /FTId=VAR_007784.
FT   VARIANT    1226   1226       F -> L (in BROVCA1).
FT                                {ECO:0000269|PubMed:14722926}.
FT                                /FTId=VAR_020696.
FT   VARIANT    1236   1236       N -> K (in BC; unknown pathological
FT                                significance; functionally neutral in
FT                                vitro; dbSNP:rs28897687).
FT                                {ECO:0000269|PubMed:23867111}.
FT                                /FTId=VAR_052078.
FT   VARIANT    1243   1243       R -> G (in BROVCA1).
FT                                {ECO:0000269|PubMed:14722926}.
FT                                /FTId=VAR_020697.
FT   VARIANT    1250   1250       E -> K (in dbSNP:rs28897686).
FT                                {ECO:0000269|PubMed:23867111}.
FT                                /FTId=VAR_052079.
FT   VARIANT    1267   1267       L -> S (in BC; unknown pathological
FT                                significance; functionally neutral in
FT                                vitro). {ECO:0000269|PubMed:23867111}.
FT                                /FTId=VAR_070482.
FT   VARIANT    1282   1282       E -> V (in BC; unknown pathological
FT                                significance; functionally neutral in
FT                                vitro). {ECO:0000269|PubMed:23867111}.
FT                                /FTId=VAR_070483.
FT   VARIANT    1297   1297       S -> P (in BC; unknown pathological
FT                                significance).
FT                                {ECO:0000269|PubMed:12938098}.
FT                                /FTId=VAR_020698.
FT   VARIANT    1297   1297       Missing (in BC; unknown pathological
FT                                significance; functionally neutral in
FT                                vitro). {ECO:0000269|PubMed:23867111}.
FT                                /FTId=VAR_070484.
FT   VARIANT    1301   1301       S -> R (in BC; unknown pathological
FT                                significance; functionally neutral in
FT                                vitro). {ECO:0000269|PubMed:23867111}.
FT                                /FTId=VAR_070485.
FT   VARIANT    1346   1346       E -> K (in BC; unknown pathological
FT                                significance; functionally neutral in
FT                                vitro). {ECO:0000269|PubMed:23867111}.
FT                                /FTId=VAR_070486.
FT   VARIANT    1347   1347       R -> G (in dbSNP:rs28897689).
FT                                {ECO:0000269|PubMed:12215251}.
FT                                /FTId=VAR_007785.
FT   VARIANT    1378   1378       V -> I (in BC; unknown pathological
FT                                significance; functionally neutral in
FT                                vitro). {ECO:0000269|PubMed:23867111}.
FT                                /FTId=VAR_070487.
FT   VARIANT    1400   1400       M -> V (in BC; unknown pathological
FT                                significance; functionally neutral in
FT                                vitro). {ECO:0000269|PubMed:23867111}.
FT                                /FTId=VAR_070488.
FT   VARIANT    1406   1406       K -> N (polymorphism; dbSNP:rs1800707).
FT                                /FTId=VAR_008761.
FT   VARIANT    1407   1407       L -> P (in BC; unknown pathological
FT                                significance; functionally neutral in
FT                                vitro). {ECO:0000269|PubMed:23867111}.
FT                                /FTId=VAR_070489.
FT   VARIANT    1411   1411       M -> T (in BC and ovarian cancer; unknown
FT                                pathological significance; decreased
FT                                interaction with PALB2).
FT                                {ECO:0000269|PubMed:14746861,
FT                                ECO:0000269|PubMed:23867111}.
FT                                /FTId=VAR_020699.
FT   VARIANT    1431   1431       S -> P.
FT                                /FTId=VAR_007786.
FT   VARIANT    1443   1443       R -> G (in BC; unknown pathological
FT                                significance; functionally neutral in
FT                                vitro). {ECO:0000269|PubMed:23867111,
FT                                ECO:0000269|PubMed:7894491,
FT                                ECO:0000269|PubMed:9482581}.
FT                                /FTId=VAR_007787.
FT   VARIANT    1443   1443       R -> Q (in dbSNP:rs4986849).
FT                                /FTId=VAR_020112.
FT   VARIANT    1448   1448       S -> G (in BC; unknown pathological
FT                                significance; functionally neutral in
FT                                vitro). {ECO:0000269|PubMed:23867111}.
FT                                /FTId=VAR_070490.
FT   VARIANT    1486   1486       S -> C (in BC; unknown pathological
FT                                significance; functionally neutral in
FT                                vitro). {ECO:0000269|PubMed:23867111}.
FT                                /FTId=VAR_070491.
FT   VARIANT    1495   1495       R -> M (in BC; unknown pathological
FT                                significance).
FT                                {ECO:0000269|PubMed:17924331}.
FT                                /FTId=VAR_063900.
FT   VARIANT    1512   1512       S -> I (in dbSNP:rs1800744).
FT                                {ECO:0000269|PubMed:12215251,
FT                                ECO:0000269|PubMed:9482581,
FT                                ECO:0000269|PubMed:9760198}.
FT                                /FTId=VAR_007788.
FT   VARIANT    1534   1534       V -> M (in BC; unknown pathological
FT                                significance; functionally neutral in
FT                                vitro). {ECO:0000269|PubMed:23867111}.
FT                                /FTId=VAR_070492.
FT   VARIANT    1561   1561       T -> I (found in breast cancer; unknown
FT                                pathological significance;
FT                                dbSNP:rs56158747).
FT                                /FTId=VAR_007789.
FT   VARIANT    1589   1589       R -> P (in BC; unknown pathological
FT                                significance; functionally neutral in
FT                                vitro). {ECO:0000269|PubMed:23867111}.
FT                                /FTId=VAR_070493.
FT   VARIANT    1606   1606       K -> E (found in breast cancer; unknown
FT                                pathological significance).
FT                                /FTId=VAR_007790.
FT   VARIANT    1613   1613       S -> G (common polymorphism;
FT                                dbSNP:rs1799966).
FT                                {ECO:0000269|PubMed:10323242,
FT                                ECO:0000269|PubMed:12442274,
FT                                ECO:0000269|PubMed:15489334,
FT                                ECO:0000269|PubMed:7894493,
FT                                ECO:0000269|PubMed:9010228,
FT                                ECO:0000269|Ref.6}.
FT                                /FTId=VAR_007791.
FT   VARIANT    1620   1620       T -> A (in dbSNP:rs8176219).
FT                                {ECO:0000269|Ref.6}.
FT                                /FTId=VAR_019946.
FT   VARIANT    1623   1623       A -> G (could be associated with cancer
FT                                susceptibility; major splicing aberration
FT                                identified with this mutant).
FT                                {ECO:0000269|PubMed:17924331,
FT                                ECO:0000269|PubMed:20513136}.
FT                                /FTId=VAR_063901.
FT   VARIANT    1628   1628       M -> T (in some patients with sporadic
FT                                breast cancer; unknown pathological
FT                                significance; dbSNP:rs4986854).
FT                                {ECO:0000269|PubMed:15365993,
FT                                ECO:0000269|PubMed:23867111}.
FT                                /FTId=VAR_007793.
FT   VARIANT    1628   1628       M -> V (found in breast and ovarian
FT                                cancer patients; unknown pathological
FT                                significance; dbSNP:rs80357465).
FT                                /FTId=VAR_007792.
FT   VARIANT    1637   1637       P -> L (rare polymorphism).
FT                                {ECO:0000269|PubMed:7939630,
FT                                ECO:0000269|PubMed:9482581}.
FT                                /FTId=VAR_007794.
FT   VARIANT    1641   1641       A -> P (in ovarian cancer; unknown
FT                                pathological significance;
FT                                dbSNP:rs1800726).
FT                                /FTId=VAR_008762.
FT   VARIANT    1651   1651       S -> F (in BC; unknown pathological
FT                                significance).
FT                                {ECO:0000269|PubMed:23867111}.
FT                                /FTId=VAR_070494.
FT   VARIANT    1651   1651       S -> P (in BC; unknown pathological
FT                                significance).
FT                                {ECO:0000269|PubMed:23867111}.
FT                                /FTId=VAR_070495.
FT   VARIANT    1652   1652       M -> I (rare polymorphism;
FT                                dbSNP:rs1799967).
FT                                {ECO:0000269|PubMed:12215251,
FT                                ECO:0000269|PubMed:15489334,
FT                                ECO:0000269|PubMed:23867111,
FT                                ECO:0000269|PubMed:9482581}.
FT                                /FTId=VAR_007795.
FT   VARIANT    1655   1655       S -> F (in BC; unknown pathological
FT                                significance; functionally impaired in
FT                                vitro). {ECO:0000269|PubMed:23867111}.
FT                                /FTId=VAR_070496.
FT   VARIANT    1662   1662       F -> C (in dbSNP:rs28897695).
FT                                /FTId=VAR_052080.
FT   VARIANT    1665   1665       V -> M. {ECO:0000269|PubMed:15026808}.
FT                                /FTId=VAR_020700.
FT   VARIANT    1685   1685       T -> A (in BC; unknown pathological
FT                                significance).
FT                                {ECO:0000269|PubMed:17924331}.
FT                                /FTId=VAR_063902.
FT   VARIANT    1685   1685       T -> I (could be associated with cancer
FT                                susceptibility; multifactorial likelihood
FT                                analysis provides evidence for
FT                                pathogenicity).
FT                                {ECO:0000269|PubMed:17924331,
FT                                ECO:0000269|PubMed:20513136}.
FT                                /FTId=VAR_063903.
FT   VARIANT    1686   1686       H -> Q (in BC; unknown pathological
FT                                significance; functionally impaired in
FT                                vitro). {ECO:0000269|PubMed:23867111}.
FT                                /FTId=VAR_070497.
FT   VARIANT    1686   1686       H -> R (in BC; unknown pathological
FT                                significance; functionally impaired in
FT                                vitro). {ECO:0000269|PubMed:23867111}.
FT                                /FTId=VAR_070498.
FT   VARIANT    1688   1688       Missing (in BC; unknown pathological
FT                                significance; functionally impaired in
FT                                vitro). {ECO:0000269|PubMed:23867111}.
FT                                /FTId=VAR_070499.
FT   VARIANT    1689   1689       M -> R (in BC; unknown pathological
FT                                significance).
FT                                {ECO:0000269|PubMed:17924331}.
FT                                /FTId=VAR_063904.
FT   VARIANT    1690   1690       K -> Q (in some patients with sporadic
FT                                breast cancer; unknown pathological
FT                                significance).
FT                                {ECO:0000269|PubMed:15365993}.
FT                                /FTId=VAR_020701.
FT   VARIANT    1691   1691       T -> I (in BC; unknown pathological
FT                                significance; functionally impaired in
FT                                vitro). {ECO:0000269|PubMed:23867111}.
FT                                /FTId=VAR_070500.
FT   VARIANT    1692   1692       D -> N (in ovarian cancer; unknown
FT                                pathological significance).
FT                                /FTId=VAR_008763.
FT   VARIANT    1697   1697       C -> R (in ovarian cancer).
FT                                {ECO:0000269|PubMed:14746861}.
FT                                /FTId=VAR_020702.
FT   VARIANT    1699   1699       R -> Q (in BC; unknown pathological
FT                                significance; functionally impaired in
FT                                vitro). {ECO:0000269|PubMed:23867111}.
FT                                /FTId=VAR_070501.
FT   VARIANT    1699   1699       R -> W (in BC and ovarian cancer;
FT                                functionally impaired in vitro).
FT                                {ECO:0000269|PubMed:14746861,
FT                                ECO:0000269|PubMed:17924331,
FT                                ECO:0000269|PubMed:23867111}.
FT                                /FTId=VAR_020703.
FT   VARIANT    1706   1706       G -> A (in BC; unknown pathological
FT                                significance).
FT                                {ECO:0000269|PubMed:23867111}.
FT                                /FTId=VAR_070502.
FT   VARIANT    1706   1706       G -> E (in BC; unknown pathological
FT                                significance; dbSNP:rs80356860).
FT                                {ECO:0000269|PubMed:17924331,
FT                                ECO:0000269|PubMed:23867111}.
FT                                /FTId=VAR_063905.
FT   VARIANT    1708   1708       A -> E (in BC; abolishes ACACA binding;
FT                                dbSNP:rs28897696).
FT                                {ECO:0000269|PubMed:17924331,
FT                                ECO:0000269|PubMed:23867111,
FT                                ECO:0000269|PubMed:7939630}.
FT                                /FTId=VAR_007796.
FT   VARIANT    1713   1713       V -> G. {ECO:0000269|PubMed:15365993}.
FT                                /FTId=VAR_007797.
FT   VARIANT    1715   1715       S -> R (in BC; unknown pathological
FT                                significance).
FT                                {ECO:0000269|PubMed:17924331}.
FT                                /FTId=VAR_063906.
FT   VARIANT    1718   1718       W -> C (in BC; unknown pathological
FT                                significance; functionally impaired in
FT                                vitro). {ECO:0000269|PubMed:23867111}.
FT                                /FTId=VAR_070503.
FT   VARIANT    1720   1720       T -> A (in BC; unknown pathological
FT                                significance; functionally neutral in
FT                                vitro; no effect on in vitro
FT                                phosphorylation by ATR).
FT                                {ECO:0000269|PubMed:11114888,
FT                                ECO:0000269|PubMed:23867111}.
FT                                /FTId=VAR_070504.
FT   VARIANT    1735   1735       E -> K (in BC; unknown pathological
FT                                significance).
FT                                {ECO:0000269|PubMed:23867111}.
FT                                /FTId=VAR_070505.
FT   VARIANT    1736   1736       V -> A (in BC; unknown pathological
FT                                significance).
FT                                {ECO:0000269|PubMed:23867111}.
FT                                /FTId=VAR_070506.
FT   VARIANT    1738   1738       G -> R (in BC; unknown pathological
FT                                significance).
FT                                {ECO:0000269|PubMed:17924331}.
FT                                /FTId=VAR_063907.
FT   VARIANT    1739   1739       D -> G (in BC; unknown pathological
FT                                significance; functionally impaired in
FT                                vitro). {ECO:0000269|PubMed:23867111}.
FT                                /FTId=VAR_070507.
FT   VARIANT    1739   1739       D -> V (in BC; unknown pathological
FT                                significance; functionally impaired in
FT                                vitro). {ECO:0000269|PubMed:23867111}.
FT                                /FTId=VAR_070508.
FT   VARIANT    1746   1746       H -> Q (in BC; unknown pathological
FT                                significance).
FT                                {ECO:0000269|PubMed:23867111}.
FT                                /FTId=VAR_070509.
FT   VARIANT    1749   1749       P -> R (in ovarian cancer; unknown
FT                                pathological significance; abolishes
FT                                ACACA binding and strongly reduces BRIP1
FT                                binding). {ECO:0000269|PubMed:10486320,
FT                                ECO:0000269|PubMed:11301010,
FT                                ECO:0000269|PubMed:15133502}.
FT                                /FTId=VAR_007798.
FT   VARIANT    1753   1753       R -> T (in BC; unknown pathological
FT                                significance).
FT                                {ECO:0000269|PubMed:23867111}.
FT                                /FTId=VAR_070510.
FT   VARIANT    1764   1764       L -> P (in BC; unknown pathological
FT                                significance; functionally impaired in
FT                                vitro). {ECO:0000269|PubMed:17924331,
FT                                ECO:0000269|PubMed:23867111}.
FT                                /FTId=VAR_063908.
FT   VARIANT    1766   1766       I -> S (in BC; unknown pathological
FT                                significance).
FT                                {ECO:0000269|PubMed:17924331}.
FT                                /FTId=VAR_063909.
FT   VARIANT    1767   1767       C -> S (in BC; unknown pathological
FT                                significance; functionally neutral in
FT                                vitro). {ECO:0000269|PubMed:23867111}.
FT                                /FTId=VAR_070511.
FT   VARIANT    1770   1770       G -> V (in BC; unknown pathological
FT                                significance; functionally impaired in
FT                                vitro). {ECO:0000269|PubMed:23867111}.
FT                                /FTId=VAR_070512.
FT   VARIANT    1775   1775       M -> K (in BC; strongly reduced
FT                                transcription transactivation; abolishes
FT                                interaction with BRIP1 and RBBP8).
FT                                {ECO:0000269|PubMed:18285836}.
FT                                /FTId=VAR_063212.
FT   VARIANT    1775   1775       M -> R (in BC; alters protein stability
FT                                and abolishes ACACA and BRIP1 binding).
FT                                {ECO:0000269|PubMed:11301010,
FT                                ECO:0000269|PubMed:12427738,
FT                                ECO:0000269|PubMed:15133502,
FT                                ECO:0000269|PubMed:7545954,
FT                                ECO:0000269|PubMed:7939630}.
FT                                /FTId=VAR_007799.
FT   VARIANT    1776   1776       P -> S (in ovarian cancer; unknown
FT                                pathological significance;
FT                                dbSNP:rs1800757).
FT                                /FTId=VAR_008764.
FT   VARIANT    1782   1782       W -> C (in BC; unknown pathological
FT                                significance; functionally neutral in
FT                                vitro). {ECO:0000269|PubMed:23867111}.
FT                                /FTId=VAR_070513.
FT   VARIANT    1786   1786       L -> P (in BROVCA1; unknown pathological
FT                                significance).
FT                                {ECO:0000269|PubMed:12938098}.
FT                                /FTId=VAR_020704.
FT   VARIANT    1788   1788       G -> V (in BC; unknown pathological
FT                                significance).
FT                                {ECO:0000269|PubMed:17924331}.
FT                                /FTId=VAR_063910.
FT   VARIANT    1789   1789       A -> T (in BC; unknown pathological
FT                                significance; functionally impaired in
FT                                vitro). {ECO:0000269|PubMed:23867111}.
FT                                /FTId=VAR_070514.
FT   VARIANT    1794   1794       E -> D (in BC; unknown pathological
FT                                significance; functionally neutral in
FT                                vitro). {ECO:0000269|PubMed:23867111}.
FT                                /FTId=VAR_070515.
FT   VARIANT    1804   1804       V -> D (in BC; unknown pathological
FT                                significance; functionally neutral in
FT                                vitro). {ECO:0000269|PubMed:23867111}.
FT                                /FTId=VAR_070516.
FT   VARIANT    1812   1812       P -> R (in BC; unknown pathological
FT                                significance; functionally neutral in
FT                                vitro). {ECO:0000269|PubMed:23867111}.
FT                                /FTId=VAR_070517.
FT   VARIANT    1812   1812       P -> S (in ovarian cancer; unknown
FT                                pathological significance;
FT                                dbSNP:rs1800751).
FT                                /FTId=VAR_008765.
FT   VARIANT    1837   1837       W -> R (in BC; unknown pathological
FT                                significance; functionally impaired in
FT                                vitro). {ECO:0000269|PubMed:23867111}.
FT                                /FTId=VAR_070518.
FT   VARIANT    1862   1862       H -> L (in BC; unknown pathological
FT                                significance; functionally neutral in
FT                                vitro). {ECO:0000269|PubMed:23867111}.
FT                                /FTId=VAR_070519.
FT   MUTAGEN      26     26       I->A: Disrupts the interaction with E2
FT                                enzymes, thereby abolishing the E3
FT                                ubiquitin-protein ligase activity.
FT                                {ECO:0000269|PubMed:16818604,
FT                                ECO:0000269|PubMed:20351172}.
FT   MUTAGEN      26     26       I->E: No ubiquitination of RBBP8. No
FT                                restoration RBBP8-mediated focus
FT                                formation or G2/M checkpoint control upon
FT                                DNA damage. {ECO:0000269|PubMed:16818604,
FT                                ECO:0000269|PubMed:20351172}.
FT   MUTAGEN      71     71       R->G: No effect on interaction with BAP1.
FT                                {ECO:0000269|PubMed:9528852}.
FT   MUTAGEN     308    308       S->N: Abolishes phosphorylation by AURKA
FT                                and interferes with cell cycle
FT                                progression from G2 to mitosis.
FT                                {ECO:0000269|PubMed:14990569}.
FT   MUTAGEN    1143   1143       S->A: Reduces in vitro phosphorylation by
FT                                ATR. {ECO:0000269|PubMed:11114888}.
FT   MUTAGEN    1239   1239       S->A: No effect on in vitro
FT                                phosphorylation by ATR.
FT                                {ECO:0000269|PubMed:11114888}.
FT   MUTAGEN    1280   1280       S->A: Reduces in vitro phosphorylation by
FT                                ATR. {ECO:0000269|PubMed:11114888}.
FT   MUTAGEN    1298   1298       S->A: No effect on in vitro
FT                                phosphorylation by ATR.
FT                                {ECO:0000269|PubMed:11114888}.
FT   MUTAGEN    1330   1330       S->A: No effect on in vitro
FT                                phosphorylation by ATR.
FT                                {ECO:0000269|PubMed:11114888}.
FT   MUTAGEN    1387   1387       S->A: Loss of IR-induced S-phase
FT                                checkpoint. Reduces in vitro
FT                                phosphorylation by ATR.
FT                                {ECO:0000269|PubMed:11114888,
FT                                ECO:0000269|PubMed:12183412}.
FT   MUTAGEN    1394   1394       T->A: Reduces in vitro phosphorylation by
FT                                ATR. {ECO:0000269|PubMed:11114888}.
FT   MUTAGEN    1423   1423       S->A: Inhibition of the infrared-induced
FT                                G2 arrest. Reduces phosphorylation by
FT                                ATR. {ECO:0000269|PubMed:11114888,
FT                                ECO:0000269|PubMed:12183412}.
FT   MUTAGEN    1457   1457       S->A: Reduces in vitro phosphorylation by
FT                                ATR. {ECO:0000269|PubMed:11114888}.
FT   MUTAGEN    1466   1466       S->A: No effect on in vitro
FT                                phosphorylation by ATR.
FT                                {ECO:0000269|PubMed:11114888}.
FT   MUTAGEN    1524   1524       S->A: No change in infrared S-phase
FT                                delay; when associated with A-1387. No
FT                                effect on in vitro phosphorylation by
FT                                ATR. {ECO:0000269|PubMed:11114888,
FT                                ECO:0000269|PubMed:12183412}.
FT   MUTAGEN    1655   1655       S->A: Abolishes interaction with BRIP1.
FT                                {ECO:0000269|PubMed:15133502}.
FT   MUTAGEN    1702   1702       K->M: Abolishes interaction with BRIP1.
FT                                {ECO:0000269|PubMed:15133502}.
FT   MUTAGEN    1738   1738       G->E: Abolishes interaction with BRIP1.
FT                                {ECO:0000269|PubMed:15133502}.
FT   MUTAGEN    1755   1755       S->A: No effect on in vitro
FT                                phosphorylation by ATR.
FT                                {ECO:0000269|PubMed:11114888}.
FT   CONFLICT     89     89       I -> T (in Ref. 4; AAB61673).
FT                                {ECO:0000305}.
FT   CONFLICT    148    148       Missing (in Ref. 4; AAB61673).
FT                                {ECO:0000305}.
FT   CONFLICT    253    253       A -> V (in Ref. 3; AAC00049).
FT                                {ECO:0000305}.
FT   CONFLICT    713    713       S -> P (in Ref. 8; AAI15038).
FT                                {ECO:0000305}.
FT   CONFLICT   1077   1077       G -> R (in Ref. 4; AAB61673).
FT                                {ECO:0000305}.
FT   CONFLICT   1426   1426       S -> P (in Ref. 3; AAC00049).
FT                                {ECO:0000305}.
FT   CONFLICT   1527   1527       E -> G (in Ref. 8; AAI15038).
FT                                {ECO:0000305}.
FT   HELIX         3      5       {ECO:0000244|PDB:1JM7}.
FT   HELIX         8     21       {ECO:0000244|PDB:1JM7}.
FT   STRAND       25     27       {ECO:0000244|PDB:1JM7}.
FT   HELIX        46     53       {ECO:0000244|PDB:1JM7}.
FT   STRAND       54     58       {ECO:0000244|PDB:1JM7}.
FT   TURN         62     64       {ECO:0000244|PDB:1JM7}.
FT   TURN         70     72       {ECO:0000244|PDB:1JM7}.
FT   STRAND       78     80       {ECO:0000244|PDB:1JM7}.
FT   HELIX        81     96       {ECO:0000244|PDB:1JM7}.
FT   STRAND     1651   1656       {ECO:0000244|PDB:4IGK}.
FT   HELIX      1659   1671       {ECO:0000244|PDB:4IGK}.
FT   STRAND     1675   1679       {ECO:0000244|PDB:1T29}.
FT   STRAND     1686   1689       {ECO:0000244|PDB:4IGK}.
FT   STRAND     1695   1697       {ECO:0000244|PDB:4IGK}.
FT   HELIX      1701   1708       {ECO:0000244|PDB:4IGK}.
FT   STRAND     1712   1715       {ECO:0000244|PDB:4IGK}.
FT   HELIX      1717   1725       {ECO:0000244|PDB:4IGK}.
FT   HELIX      1731   1734       {ECO:0000244|PDB:4IGK}.
FT   TURN       1740   1742       {ECO:0000244|PDB:4IGK}.
FT   STRAND     1743   1745       {ECO:0000244|PDB:1T29}.
FT   HELIX      1748   1754       {ECO:0000244|PDB:4IGK}.
FT   TURN       1755   1757       {ECO:0000244|PDB:1T29}.
FT   TURN       1760   1763       {ECO:0000244|PDB:4IGK}.
FT   STRAND     1765   1768       {ECO:0000244|PDB:4IGK}.
FT   STRAND     1770   1772       {ECO:0000244|PDB:1T2V}.
FT   STRAND     1773   1775       {ECO:0000244|PDB:4IGK}.
FT   HELIX      1777   1786       {ECO:0000244|PDB:4IGK}.
FT   STRAND     1790   1794       {ECO:0000244|PDB:4IGK}.
FT   HELIX      1795   1797       {ECO:0000244|PDB:4IGK}.
FT   STRAND     1801   1803       {ECO:0000244|PDB:4IGK}.
FT   STRAND     1806   1810       {ECO:0000244|PDB:4IGK}.
FT   HELIX      1812   1814       {ECO:0000244|PDB:4IGK}.
FT   STRAND     1817   1819       {ECO:0000244|PDB:1OQA}.
FT   HELIX      1820   1822       {ECO:0000244|PDB:4IGK}.
FT   HELIX      1824   1827       {ECO:0000244|PDB:4IGK}.
FT   STRAND     1828   1830       {ECO:0000244|PDB:3PXE}.
FT   STRAND     1832   1834       {ECO:0000244|PDB:4IGK}.
FT   HELIX      1835   1844       {ECO:0000244|PDB:4IGK}.
FT   HELIX      1851   1853       {ECO:0000244|PDB:4IGK}.
SQ   SEQUENCE   1863 AA;  207721 MW;  89C6D83FF56312AF CRC64;
     MDLSALRVEE VQNVINAMQK ILECPICLEL IKEPVSTKCD HIFCKFCMLK LLNQKKGPSQ
     CPLCKNDITK RSLQESTRFS QLVEELLKII CAFQLDTGLE YANSYNFAKK ENNSPEHLKD
     EVSIIQSMGY RNRAKRLLQS EPENPSLQET SLSVQLSNLG TVRTLRTKQR IQPQKTSVYI
     ELGSDSSEDT VNKATYCSVG DQELLQITPQ GTRDEISLDS AKKAACEFSE TDVTNTEHHQ
     PSNNDLNTTE KRAAERHPEK YQGSSVSNLH VEPCGTNTHA SSLQHENSSL LLTKDRMNVE
     KAEFCNKSKQ PGLARSQHNR WAGSKETCND RRTPSTEKKV DLNADPLCER KEWNKQKLPC
     SENPRDTEDV PWITLNSSIQ KVNEWFSRSD ELLGSDDSHD GESESNAKVA DVLDVLNEVD
     EYSGSSEKID LLASDPHEAL ICKSERVHSK SVESNIEDKI FGKTYRKKAS LPNLSHVTEN
     LIIGAFVTEP QIIQERPLTN KLKRKRRPTS GLHPEDFIKK ADLAVQKTPE MINQGTNQTE
     QNGQVMNITN SGHENKTKGD SIQNEKNPNP IESLEKESAF KTKAEPISSS ISNMELELNI
     HNSKAPKKNR LRRKSSTRHI HALELVVSRN LSPPNCTELQ IDSCSSSEEI KKKKYNQMPV
     RHSRNLQLME GKEPATGAKK SNKPNEQTSK RHDSDTFPEL KLTNAPGSFT KCSNTSELKE
     FVNPSLPREE KEEKLETVKV SNNAEDPKDL MLSGERVLQT ERSVESSSIS LVPGTDYGTQ
     ESISLLEVST LGKAKTEPNK CVSQCAAFEN PKGLIHGCSK DNRNDTEGFK YPLGHEVNHS
     RETSIEMEES ELDAQYLQNT FKVSKRQSFA PFSNPGNAEE ECATFSAHSG SLKKQSPKVT
     FECEQKEENQ GKNESNIKPV QTVNITAGFP VVGQKDKPVD NAKCSIKGGS RFCLSSQFRG
     NETGLITPNK HGLLQNPYRI PPLFPIKSFV KTKCKKNLLE ENFEEHSMSP EREMGNENIP
     STVSTISRNN IRENVFKEAS SSNINEVGSS TNEVGSSINE IGSSDENIQA ELGRNRGPKL
     NAMLRLGVLQ PEVYKQSLPG SNCKHPEIKK QEYEEVVQTV NTDFSPYLIS DNLEQPMGSS
     HASQVCSETP DDLLDDGEIK EDTSFAENDI KESSAVFSKS VQKGELSRSP SPFTHTHLAQ
     GYRRGAKKLE SSEENLSSED EELPCFQHLL FGKVNNIPSQ STRHSTVATE CLSKNTEENL
     LSLKNSLNDC SNQVILAKAS QEHHLSEETK CSASLFSSQC SELEDLTANT NTQDPFLIGS
     SKQMRHQSES QGVGLSDKEL VSDDEERGTG LEENNQEEQS MDSNLGEAAS GCESETSVSE
     DCSGLSSQSD ILTTQQRDTM QHNLIKLQQE MAELEAVLEQ HGSQPSNSYP SIISDSSALE
     DLRNPEQSTS EKAVLTSQKS SEYPISQNPE GLSADKFEVS ADSSTSKNKE PGVERSSPSK
     CPSLDDRWYM HSCSGSLQNR NYPSQEELIK VVDVEEQQLE ESGPHDLTET SYLPRQDLEG
     TPYLESGISL FSDDPESDPS EDRAPESARV GNIPSSTSAL KVPQLKVAES AQSPAAAHTT
     DTAGYNAMEE SVSREKPELT ASTERVNKRM SMVVSGLTPE EFMLVYKFAR KHHITLTNLI
     TEETTHVVMK TDAEFVCERT LKYFLGIAGG KWVVSYFWVT QSIKERKMLN EHDFEVRGDV
     VNGRNHQGPK RARESQDRKI FRGLEICCYG PFTNMPTDQL EWMVQLCGAS VVKELSSFTL
     GTGVHPIVVV QPDAWTEDNG FHAIGQMCEA PVVTREWVLD SVALYQCQEL DTYLIPQIPH
     SHY
//
ID   CBX4_HUMAN              Reviewed;         560 AA.
AC   O00257; B1PJR7; Q6TPI8; Q96C04;
DT   24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 3.
DT   11-NOV-2015, entry version 153.
DE   RecName: Full=E3 SUMO-protein ligase CBX4;
DE            EC=6.3.2.-;
DE   AltName: Full=Chromobox protein homolog 4;
DE   AltName: Full=Polycomb 2 homolog;
DE            Short=Pc2;
DE            Short=hPc2;
GN   Name=CBX4;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Fetal brain;
RX   PubMed=9315667;
RA   Satijn D.P.E., Olson D.J., van der Vlag J., Hamer K.M., Lambrechts C.,
RA   Masselink H., Gunster M.J., Sewalt R.G.A.B., van Driel R., Otte A.P.;
RT   "Interference with the expression of a novel human polycomb protein,
RT   hPc2, results in cellular transformation and apoptosis.";
RL   Mol. Cell. Biol. 17:6076-6086(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND SUBCELLULAR LOCATION.
RX   PubMed=19266028; DOI=10.1371/journal.pgen.1000397;
RA   Salichs E., Ledda A., Mularoni L., Alba M.M., de la Luna S.;
RT   "Genome-wide analysis of histidine repeats reveals their role in the
RT   localization of human proteins to the nuclear speckles compartment.";
RL   PLoS Genet. 5:E1000397-E1000397(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RA   Liu M., Cheng J., Wang L.;
RT   "Cloning and identification of NS5ATP1-binding protein 16.";
RL   Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16625196; DOI=10.1038/nature04689;
RA   Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA   Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA   Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA   Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA   DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R.,
RA   Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
RA   Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
RA   Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
RA   Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
RA   Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
RA   Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
RA   Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA   Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA   Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT   "DNA sequence of human chromosome 17 and analysis of rearrangement in
RT   the human lineage.";
RL   Nature 440:1045-1049(2006).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Colon;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 457-560 (ISOFORM 1).
RX   PubMed=9199346;
RA   Satijn D.P.E., Gunster M.J., van der Vlag J., Hamer K.M., Schul W.,
RA   Alkema M.J., Saurin A.J., Freemont P.S., van Driel R., Otte A.P.;
RT   "RING1 is associated with the polycomb group protein complex and acts
RT   as a transcriptional repressor.";
RL   Mol. Cell. Biol. 17:4105-4113(1997).
RN   [7]
RP   INTERACTION WITH SUV39H1.
RX   PubMed=12101246; DOI=10.1128/MCB.22.15.5539-5553.2002;
RA   Sewalt R.G.A.B., Lachner M., Vargas M., Hamer K.M., den Blaauwen J.L.,
RA   Hendrix T., Melcher M., Schweizer D., Jenuwein T., Otte A.P.;
RT   "Selective interactions between vertebrate polycomb homologs and the
RT   SUV39H1 histone lysine methyltransferase suggest that histone H3-K9
RT   methylation contributes to chromosomal targeting of Polycomb group
RT   proteins.";
RL   Mol. Cell. Biol. 22:5539-5553(2002).
RN   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN A PRC1-LIKE
RP   HPRC-H COMPLEX WITH BMI1; CBX2; CBX8; PHC1; PHC2; PHC3; RING1 AND
RP   RNF2.
RX   PubMed=12167701; DOI=10.1128/MCB.22.17.6070-6078.2002;
RA   Levine S.S., Weiss A., Erdjument-Bromage H., Shao Z., Tempst P.,
RA   Kingston R.E.;
RT   "The core of the polycomb repressive complex is compositionally and
RT   functionally conserved in flies and humans.";
RL   Mol. Cell. Biol. 22:6070-6078(2002).
RN   [9]
RP   FUNCTION, SUMOYLATION, AND SUBCELLULAR LOCATION.
RX   PubMed=12679040; DOI=10.1016/S0092-8674(03)00159-4;
RA   Kagey M.H., Melhuish T.A., Wotton D.;
RT   "The polycomb protein Pc2 is a SUMO E3.";
RL   Cell 113:127-137(2003).
RN   [10]
RP   SUMOYLATION AT LYS-494.
RX   PubMed=15592428; DOI=10.1038/sj.emboj.7600506;
RA   Kagey M.H., Melhuish T.A., Powers S.E., Wotton D.;
RT   "Multiple activities contribute to Pc2 E3 function.";
RL   EMBO J. 24:108-119(2005).
RN   [11]
RP   FUNCTION.
RX   PubMed=16061479; DOI=10.1074/jbc.M504477200;
RA   Long J., Zuo D., Park M.;
RT   "Pc2-mediated sumoylation of Smad-interacting protein 1 attenuates
RT   transcriptional repression of E-cadherin.";
RL   J. Biol. Chem. 280:35477-35489(2005).
RN   [12]
RP   FUNCTION, INTERACTION WITH HIPK2, SUMOYLATION, SUBCELLULAR LOCATION,
RP   AND PHOSPHORYLATION AT THR-497.
RX   PubMed=17018294; DOI=10.1016/j.molcel.2006.08.004;
RA   Roscic A., Moeller A., Calzado M.A., Renner F., Wimmer V.C.,
RA   Gresko E., Luedi K.S., Schmitz M.L.;
RT   "Phosphorylation-dependent control of Pc2 SUMO E3 ligase activity by
RT   its substrate protein HIPK2.";
RL   Mol. Cell 24:77-89(2006).
RN   [13]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [14]
RP   IDENTIFICATION IN A PRC1-LIKE COMPLEX.
RX   PubMed=19636380; DOI=10.1371/journal.pone.0006380;
RA   Maertens G.N., El Messaoudi-Aubert S., Racek T., Stock J.K.,
RA   Nicholls J., Rodriguez-Niedenfuhr M., Gil J., Peters G.;
RT   "Several distinct polycomb complexes regulate and co-localize on the
RT   INK4a tumor suppressor locus.";
RL   PLoS ONE 4:E6380-E6380(2009).
RN   [15]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-149, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19608861; DOI=10.1126/science.1175371;
RA   Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA   Walther T.C., Olsen J.V., Mann M.;
RT   "Lysine acetylation targets protein complexes and co-regulates major
RT   cellular functions.";
RL   Science 325:834-840(2009).
RN   [16]
RP   FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY (ISOFORM 2),
RP   IDENTIFICATION IN A PRC1-LIKE COMPLEX, SELF-ASSOCIATION, SUBCELLULAR
RP   LOCATION, AND MUTAGENESIS OF SER-434.
RX   PubMed=21282530; DOI=10.1074/mcp.M110.002642;
RA   Vandamme J., Volkel P., Rosnoblet C., Le Faou P., Angrand P.O.;
RT   "Interaction proteomics analysis of polycomb proteins defines distinct
RT   PRC1 Complexes in mammalian cells.";
RL   Mol. Cell. Proteomics 0:0-0(2011).
RN   [17]
RP   FUNCTION IN ZNF131 SUMOYLATION, SUBCELLULAR LOCATION, AND MUTAGENESIS
RP   OF LYS-494 AND THR-497.
RX   PubMed=22467880; DOI=10.1074/jbc.M111.336354;
RA   Oh Y., Chung K.C.;
RT   "Small ubiquitin-like modifier (SUMO) modification of zinc finger
RT   protein 131 potentiates its negative effect on estrogen signaling.";
RL   J. Biol. Chem. 287:17517-17529(2012).
RN   [18]
RP   FUNCTION.
RX   PubMed=22825850; DOI=10.1074/jbc.M112.390120;
RA   Pelisch F., Pozzi B., Risso G., Munoz M.J., Srebrow A.;
RT   "DNA damage-induced heterogeneous nuclear ribonucleoprotein K
RT   SUMOylation regulates p53 transcriptional activation.";
RL   J. Biol. Chem. 287:30789-30799(2012).
RN   [19]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-467, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
RA   Wang L., Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human
RT   liver phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [20]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-106; LYS-114; LYS-149;
RP   LYS-205; LYS-212 AND LYS-280, AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=25218447; DOI=10.1038/nsmb.2890;
RA   Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA   Vertegaal A.C.;
RT   "Uncovering global SUMOylation signaling networks in a site-specific
RT   manner.";
RL   Nat. Struct. Mol. Biol. 21:927-936(2014).
RN   [21]
RP   STRUCTURE BY NMR OF 8-65.
RG   Structural genomics consortium (SGC);
RT   "Solution NMR structure of the chromo domain of the chromobox protein
RT   homolog 4.";
RL   Submitted (FEB-2009) to the PDB data bank.
RN   [22]
RP   X-RAY CRYSTALLOGRAPHY (1.51 ANGSTROMS) OF 8-62.
RG   Structural genomics consortium (SGC);
RT   "Crystal structure of human chromobox homolog 4 (cbx4).";
RL   Submitted (SEP-2009) to the PDB data bank.
CC   -!- FUNCTION: E3 SUMO-protein ligase which facilitates SUMO1
CC       conjugation by UBE2I. Involved in the sumoylation of HNRNPK, a
CC       p53/TP53 transcriptional coactivator, hence indirectly regulates
CC       p53/TP53 transcriptional activation resulting in p21/CDKN1A
CC       expression. Monosumoylates ZNF131.
CC   -!- FUNCTION: Component of a Polycomb group (PcG) multiprotein PRC1-
CC       like complex, a complex class required to maintain the
CC       transcriptionally repressive state of many genes, including Hox
CC       genes, throughout development. PcG PRC1 complex acts via chromatin
CC       remodeling and modification of histones; it mediates
CC       monoubiquitination of histone H2A 'Lys-119', rendering chromatin
CC       heritably changed in its expressibility.
CC   -!- PATHWAY: Protein modification; protein sumoylation.
CC   -!- SUBUNIT: Interacts with histone H3-K9Me3. Interacts with CHTOP (By
CC       similarity). Component of a PRC1-like complex. Self-associates.
CC       Interacts with SUV39H1 and HIPK2. Interacts with CSNK2B.
CC       {ECO:0000250, ECO:0000269|PubMed:12101246,
CC       ECO:0000269|PubMed:12167701, ECO:0000269|PubMed:17018294,
CC       ECO:0000269|PubMed:19636380, ECO:0000269|PubMed:21282530}.
CC   -!- INTERACTION:
CC       P35226:BMI1; NbExp=4; IntAct=EBI-722425, EBI-2341576;
CC       P68400:CSNK2A1; NbExp=2; IntAct=EBI-4392727, EBI-347804;
CC       P67870:CSNK2B; NbExp=2; IntAct=EBI-4392727, EBI-348169;
CC       Q16665:HIF1A; NbExp=15; IntAct=EBI-722425, EBI-447269;
CC       Q9BYE7:PCGF6; NbExp=2; IntAct=EBI-4392727, EBI-1048026;
CC       Q99496:RNF2; NbExp=2; IntAct=EBI-4392727, EBI-722416;
CC       P31946:YWHAB; NbExp=2; IntAct=EBI-722425, EBI-359815;
CC       P62258:YWHAE; NbExp=2; IntAct=EBI-4392727, EBI-356498;
CC       P63104:YWHAZ; NbExp=2; IntAct=EBI-4392727, EBI-347088;
CC   -!- SUBCELLULAR LOCATION: Nucleus. Nucleus speckle. Note=Localization
CC       to nuclear polycomb bodies is required for ZNF131 sumoylation.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=O00257-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=O00257-3; Sequence=VSP_041599;
CC   -!- TISSUE SPECIFICITY: Ubiquitous.
CC   -!- DOMAIN: The polyhistidine repeat may act as a targeting signal to
CC       nuclear speckles. {ECO:0000269|PubMed:19266028}.
CC   -!- PTM: Phosphorylated on Thr-497 by HIPK2 upon DNA damage. This
CC       phosphorylation stimulates E3 SUMO-protein ligase activity and
CC       promotes sumoylation on Lys-494, as well as sumoylation of other
CC       target proteins, such as HNRNPK. {ECO:0000269|PubMed:12679040,
CC       ECO:0000269|PubMed:15592428, ECO:0000269|PubMed:17018294}.
CC   -!- MISCELLANEOUS: The human orthologs of the Drosophila Polycomb
CC       group protein Pc are CBX2, CBX4, CBX6, CBX7 and CBX8. These show
CC       distinct nuclear localizations, contribute differently to
CC       transcriptional repression, and appear to be part of distinct
CC       PRC1-like protein complexes. The hPRC-H complex purified in
CC       PubMed:12167701 probably presents a mixture of different complexes
CC       containing different Polycomb group proteins.
CC   -!- SIMILARITY: Contains 1 chromo domain. {ECO:0000255|PROSITE-
CC       ProRule:PRU00053}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH14967.1; Type=Miscellaneous discrepancy; Note=Aberrant splicing.; Evidence={ECO:0000305};
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DR   EMBL; AF013956; AAB80718.1; -; mRNA.
DR   EMBL; EU439707; ACA49234.1; -; mRNA.
DR   EMBL; AY390430; AAQ97596.1; -; mRNA.
DR   EMBL; AC100791; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC014967; AAH14967.1; ALT_SEQ; mRNA.
DR   EMBL; U94344; AAB62734.1; -; mRNA.
DR   CCDS; CCDS32758.1; -. [O00257-1]
DR   RefSeq; NP_003646.2; NM_003655.2. [O00257-1]
DR   UniGene; Hs.405046; -.
DR   PDB; 2K28; NMR; -; A=8-65.
DR   PDB; 3I8Z; X-ray; 1.51 A; A=8-62.
DR   PDBsum; 2K28; -.
DR   PDBsum; 3I8Z; -.
DR   ProteinModelPortal; O00257; -.
DR   SMR; O00257; 11-60.
DR   BioGrid; 114105; 75.
DR   DIP; DIP-42042N; -.
DR   IntAct; O00257; 47.
DR   MINT; MINT-1196265; -.
DR   STRING; 9606.ENSP00000269397; -.
DR   BindingDB; O00257; -.
DR   ChEMBL; CHEMBL3232685; -.
DR   PhosphoSite; O00257; -.
DR   BioMuta; CBX4; -.
DR   MaxQB; O00257; -.
DR   PaxDb; O00257; -.
DR   PRIDE; O00257; -.
DR   Ensembl; ENST00000269397; ENSP00000269397; ENSG00000141582. [O00257-1]
DR   GeneID; 8535; -.
DR   KEGG; hsa:8535; -.
DR   UCSC; uc002jxe.3; human. [O00257-1]
DR   CTD; 8535; -.
DR   GeneCards; CBX4; -.
DR   H-InvDB; HIX0014237; -.
DR   HGNC; HGNC:1554; CBX4.
DR   HPA; HPA008228; -.
DR   MIM; 603079; gene.
DR   neXtProt; NX_O00257; -.
DR   PharmGKB; PA26129; -.
DR   eggNOG; ENOG410IPQ6; Eukaryota.
DR   eggNOG; ENOG410ZQCR; LUCA.
DR   GeneTree; ENSGT00530000063056; -.
DR   HOGENOM; HOG000206923; -.
DR   HOVERGEN; HBG005257; -.
DR   InParanoid; O00257; -.
DR   KO; K11452; -.
DR   OMA; HHHHAVD; -.
DR   OrthoDB; EOG7PCJGP; -.
DR   PhylomeDB; O00257; -.
DR   TreeFam; TF106456; -.
DR   Reactome; R-HSA-2559580; Oxidative Stress Induced Senescence.
DR   Reactome; R-HSA-3108214; SUMOylation of DNA damage response and repair proteins.
DR   UniPathway; UPA00886; -.
DR   ChiTaRS; CBX4; human.
DR   EvolutionaryTrace; O00257; -.
DR   GenomeRNAi; 8535; -.
DR   NextBio; 31968; -.
DR   PRO; PR:O00257; -.
DR   Proteomes; UP000005640; Chromosome 17.
DR   Bgee; O00257; -.
DR   CleanEx; HS_CBX4; -.
DR   ExpressionAtlas; O00257; baseline and differential.
DR   Genevisible; O00257; HS.
DR   GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0031519; C:PcG protein complex; IDA:UniProtKB.
DR   GO; GO:0035102; C:PRC1 complex; IDA:UniProtKB.
DR   GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
DR   GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003727; F:single-stranded RNA binding; IEA:Ensembl.
DR   GO; GO:0032183; F:SUMO binding; IDA:MGI.
DR   GO; GO:0019789; F:SUMO transferase activity; EXP:Reactome.
DR   GO; GO:0003714; F:transcription corepressor activity; TAS:ProtInc.
DR   GO; GO:0044212; F:transcription regulatory region DNA binding; IEA:Ensembl.
DR   GO; GO:0044267; P:cellular protein metabolic process; TAS:Reactome.
DR   GO; GO:0016568; P:chromatin modification; IEA:UniProtKB-KW.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; TAS:ProtInc.
DR   GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IMP:UniProtKB.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR   GO; GO:0043687; P:post-translational protein modification; TAS:Reactome.
DR   GO; GO:0016925; P:protein sumoylation; TAS:Reactome.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
DR   InterPro; IPR000953; Chromo/shadow_dom.
DR   InterPro; IPR017984; Chromo_dom_subgr.
DR   InterPro; IPR023780; Chromo_domain.
DR   InterPro; IPR016197; Chromodomain-like.
DR   InterPro; IPR023779; Chromodomain_CS.
DR   Pfam; PF00385; Chromo; 1.
DR   PRINTS; PR00504; CHROMODOMAIN.
DR   SMART; SM00298; CHROMO; 1.
DR   SUPFAM; SSF54160; SSF54160; 1.
DR   PROSITE; PS00598; CHROMO_1; 1.
DR   PROSITE; PS50013; CHROMO_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative splicing; Chromatin regulator;
KW   Complete proteome; Isopeptide bond; Ligase; Nucleus; Phosphoprotein;
KW   Reference proteome; Repressor; Transcription;
KW   Transcription regulation; Ubl conjugation; Ubl conjugation pathway.
FT   CHAIN         1    560       E3 SUMO-protein ligase CBX4.
FT                                /FTId=PRO_0000080206.
FT   DOMAIN       11     69       Chromo. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00053}.
FT   REGION        1    539       Interaction with BMI1.
FT   REGION      540    560       Interaction with RNF2.
FT   COMPBIAS    378    400       His-rich.
FT   COMPBIAS    389    400       Poly-His.
FT   COMPBIAS    499    510       Poly-Ala.
FT   MOD_RES     149    149       N6-acetyllysine; alternate.
FT                                {ECO:0000244|PubMed:19608861}.
FT   MOD_RES     467    467       Phosphoserine.
FT                                {ECO:0000244|PubMed:24275569}.
FT   MOD_RES     497    497       Phosphothreonine; by HIPK2.
FT                                {ECO:0000269|PubMed:17018294}.
FT   CROSSLNK    106    106       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:25218447}.
FT   CROSSLNK    114    114       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:25218447}.
FT   CROSSLNK    149    149       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2);
FT                                alternate. {ECO:0000244|PubMed:25218447}.
FT   CROSSLNK    205    205       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:25218447}.
FT   CROSSLNK    212    212       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:25218447}.
FT   CROSSLNK    280    280       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:25218447}.
FT   CROSSLNK    494    494       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO).
FT   VAR_SEQ     127    396       Missing (in isoform 2).
FT                                {ECO:0000303|Ref.3}.
FT                                /FTId=VSP_041599.
FT   MUTAGEN     434    434       S->A: Abolishes interaction with YWHAZ
FT                                and YWHAE; impairs interaction with PCGF6
FT                                and BMI1; no effect on interaction with
FT                                RNF2. {ECO:0000269|PubMed:21282530}.
FT   MUTAGEN     494    494       K->R: No effect on ZNF131 sumoylation.
FT                                {ECO:0000269|PubMed:22467880}.
FT   MUTAGEN     497    497       T->A: Small decrease in ZNF131
FT                                sumoylation.
FT                                {ECO:0000269|PubMed:22467880}.
FT   CONFLICT    137    138       Missing (in Ref. 1; AAB80718).
FT                                {ECO:0000305}.
FT   CONFLICT    142    142       P -> R (in Ref. 1; AAB80718).
FT                                {ECO:0000305}.
FT   CONFLICT    458    458       P -> R (in Ref. 1; AAB80718 and 5;
FT                                AAB62734). {ECO:0000305}.
FT   CONFLICT    477    477       C -> S (in Ref. 1; AAB80718 and 5;
FT                                AAB62734). {ECO:0000305}.
FT   CONFLICT    480    480       T -> S (in Ref. 1; AAB80718 and 5;
FT                                AAB62734). {ECO:0000305}.
FT   CONFLICT    505    505       V -> VAA (in Ref. 3; ACA49234).
FT                                {ECO:0000305}.
FT   STRAND       13     22       {ECO:0000244|PDB:3I8Z}.
FT   STRAND       25     32       {ECO:0000244|PDB:3I8Z}.
FT   HELIX        37     39       {ECO:0000244|PDB:3I8Z}.
FT   STRAND       41     44       {ECO:0000244|PDB:3I8Z}.
FT   HELIX        45     48       {ECO:0000244|PDB:3I8Z}.
FT   HELIX        51     53       {ECO:0000244|PDB:3I8Z}.
SQ   SEQUENCE   560 AA;  61368 MW;  DF5C8C4C0CCB1F31 CRC64;
     MELPAVGEHV FAVESIEKKR IRKGRVEYLV KWRGWSPKYN TWEPEENILD PRLLIAFQNR
     ERQEQLMGYR KRGPKPKPLV VQVPTFARRS NVLTGLQDSS TDNRAKLDLG AQGKGQGHQY
     ELNSKKHHQY QPHSKERAGK PPPPGKSGKY YYQLNSKKHH PYQPDPKMYD LQYQGGHKEA
     PSPTCPDLGA KSHPPDKWAQ GAGAKGYLGA VKPLAGAAGA PGKGSEKGPP NGMMPAPKEA
     VTGNGIGGKM KIVKNKNKNG RIVIVMSKYM ENGMQAVKIK SGEVAEGEAR SPSHKKRAAD
     ERHPPADRTF KKAAGAEEKK VEAPPKRREE EVSGVSDPQP QDAGSRKLSP TKEAFGEQPL
     QLTTKPDLLA WDPARNTHPP SHHPHPHPHH HHHHHHHHHH AVGLNLSHVR KRCLSETHGE
     REPCKKRLTA RSISTPTCLG GSPAAERPAD LPPAAALPQP EVILLDSDLD EPIDLRCVKT
     RSEAGEPPSS LQVKPETPAS AAVAVAAAAA PTTTAEKPPA EAQDEPAESL SEFKPFFGNI
     IITDVTANCL TVTFKEYVTV
//
ID   CHD3_HUMAN              Reviewed;        2000 AA.
AC   Q12873; D3DTQ9; E9PG89; Q9Y4I0;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-2006, sequence version 3.
DT   11-NOV-2015, entry version 169.
DE   RecName: Full=Chromodomain-helicase-DNA-binding protein 3;
DE            Short=CHD-3;
DE            EC=3.6.4.12;
DE   AltName: Full=ATP-dependent helicase CHD3;
DE   AltName: Full=Mi-2 autoantigen 240 kDa protein;
DE   AltName: Full=Mi2-alpha;
DE   AltName: Full=Zinc finger helicase;
DE            Short=hZFH;
GN   Name=CHD3;
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 1 AND 2), AND TISSUE SPECIFICITY.
RX   PubMed=9688266; DOI=10.1046/j.1432-1327.1998.2540558.x;
RA   Aubry F., Mattei M.-G., Galibert F.;
RT   "Identification of a human 17p-located cDNA encoding a protein of the
RT   Snf2-like helicase family.";
RL   Eur. J. Biochem. 254:558-564(1998).
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   NUCLEOTIDE SEQUENCE [MRNA] OF 1-1966 (ISOFORM 2).
RC   TISSUE=Fetus;
RX   PubMed=9326634; DOI=10.1073/pnas.94.21.11472;
RA   Woodage T., Basrai M.A., Baxevanis A.D., Hieter P., Collins F.S.;
RT   "Characterization of the CHD family of proteins.";
RL   Proc. Natl. Acad. Sci. U.S.A. 94:11472-11477(1997).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 121-654.
RC   TISSUE=Thymus;
RX   PubMed=7560064; DOI=10.1172/JCI118218;
RA   Ge Q., Nilasena D.S., O'Brien C.A., Frank M.B., Targoff I.N.;
RT   "Molecular analysis of a major antigenic region of the 240 kD protein
RT   of Mi-2 autoantigen.";
RL   J. Clin. Invest. 96:1730-1737(1995).
RN   [6]
RP   IDENTIFICATION AS A COMPONENT OF THE NURD COMPLEX, AND FUNCTION.
RX   PubMed=9804427; DOI=10.1038/27699;
RA   Tong J.K., Hassig C.A., Schnitzler G.R., Kingston R.E.,
RA   Schreiber S.L.;
RT   "Chromatin deacetylation by an ATP-dependent nucleosome remodelling
RT   complex.";
RL   Nature 395:917-921(1998).
RN   [7]
RP   INTERACTION WITH TRIM28.
RX   PubMed=11230151; DOI=10.1101/gad.869501;
RA   Schultz D.C., Friedman J.R., Rauscher F.J. III;
RT   "Targeting histone deacetylase complexes via KRAB-zinc finger
RT   proteins: the PHD and bromodomains of KAP-1 form a cooperative unit
RT   that recruits a novel isoform of the Mi-2alpha subunit of NuRD.";
RL   Genes Dev. 15:428-443(2001).
RN   [8]
RP   INTERACTION WITH HABP4 AND SERBP1.
RX   PubMed=12505151; DOI=10.1016/S0014-5793(02)03737-7;
RA   Lemos T.A., Passos D.O., Nery F.C., Kobarg J.;
RT   "Characterization of a new family of proteins that interact with the
RT   C-terminal region of the chromatin-remodeling factor CHD-3.";
RL   FEBS Lett. 533:14-20(2003).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-324; SER-1601 AND
RP   SER-1605, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA   Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA   Mann M.;
RT   "Global, in vivo, and site-specific phosphorylation dynamics in
RT   signaling networks.";
RL   Cell 127:635-648(2006).
RN   [10]
RP   INTERACTION WITH PCNT, SUBCELLULAR LOCATION, AND FUNCTION.
RX   PubMed=17626165; DOI=10.1091/mbc.E06-07-0604;
RA   Sillibourne J.E., Delaval B., Redick S., Sinha M., Doxsey S.J.;
RT   "Chromatin remodeling proteins interact with pericentrin to regulate
RT   centrosome integrity.";
RL   Mol. Biol. Cell 18:3667-3680(2007).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1601, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA   Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA   Greff Z., Keri G., Stemmann O., Mann M.;
RT   "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT   the kinome across the cell cycle.";
RL   Mol. Cell 31:438-448(2008).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-713; SER-1367; SER-1601
RP   AND SER-1605, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   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   [13]
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   [14]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-713; SER-1601 AND
RP   SER-1605, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA   Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA   Rodionov V., Han D.K.;
RT   "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT   reveals system-wide modulation of protein-protein interactions.";
RL   Sci. Signal. 2:RA46-RA46(2009).
RN   [15]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1601 AND SER-1605, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA   Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full
RT   phosphorylation site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [16]
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   [17]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1601, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
RA   Wang L., Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human
RT   liver phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [18]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-1308, 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: Component of the histone deacetylase NuRD complex which
CC       participates in the remodeling of chromatin by deacetylating
CC       histones. Required for anchoring centrosomal pericentrin in both
CC       interphase and mitosis, for spindle organization and centrosome
CC       integrity. {ECO:0000269|PubMed:17626165,
CC       ECO:0000269|PubMed:9804427}.
CC   -!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
CC   -!- SUBUNIT: Central component of the nucleosome remodeling and
CC       histone deacetylase (NuRD) repressive complex. Interacts with
CC       TRIM28 and SERBP1. Interacts (via its C-terminal) with HABP4.
CC       Interacts with PCNT; the interaction regulates centrosome
CC       integrity. {ECO:0000269|PubMed:11230151,
CC       ECO:0000269|PubMed:12505151, ECO:0000269|PubMed:17626165}.
CC   -!- INTERACTION:
CC       Q99728:BARD1; NbExp=2; IntAct=EBI-523590, EBI-473181;
CC       P17844:DDX5; NbExp=4; IntAct=EBI-523590, EBI-351962;
CC       Q9Y2X7:GIT1; NbExp=2; IntAct=EBI-523590, EBI-466061;
CC       P42858:HTT; NbExp=3; IntAct=EBI-523590, EBI-466029;
CC       O60341:KDM1A; NbExp=4; IntAct=EBI-523590, EBI-710124;
CC       O75400:PRPF40A; NbExp=2; IntAct=EBI-523590, EBI-473291;
CC       Q8NC51:SERBP1; NbExp=5; IntAct=EBI-523590, EBI-523558;
CC       P61956:SUMO2; NbExp=3; IntAct=EBI-523590, EBI-473220;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17626165}.
CC       Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
CC       {ECO:0000269|PubMed:17626165}. Note=Associates with centrosomes in
CC       interphase and mitosis.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q12873-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q12873-2; Sequence=VSP_017231;
CC       Name=3;
CC         IsoId=Q12873-3; Sequence=VSP_047097;
CC         Note=No experimental confirmation available. Gene prediction
CC         based on EST data.;
CC   -!- TISSUE SPECIFICITY: Widely expressed.
CC       {ECO:0000269|PubMed:9688266}.
CC   -!- MISCELLANEOUS: One of the main antigens reacting with anti-MI-2
CC       positive sera of dermatomyositis.
CC   -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Contains 2 chromo domains. {ECO:0000255|PROSITE-
CC       ProRule:PRU00053}.
CC   -!- SIMILARITY: Contains 1 helicase ATP-binding domain.
CC       {ECO:0000255|PROSITE-ProRule:PRU00541}.
CC   -!- SIMILARITY: Contains 1 helicase C-terminal domain.
CC       {ECO:0000255|PROSITE-ProRule:PRU00542}.
CC   -!- SIMILARITY: Contains 2 PHD-type zinc fingers.
CC       {ECO:0000255|PROSITE-ProRule:PRU00146}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB87383.1; Type=Miscellaneous discrepancy; Note=Differs from position 1967 onward for unknown reasons.; Evidence={ECO:0000305};
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DR   EMBL; U91543; AAC39923.1; -; mRNA.
DR   EMBL; AC104581; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471108; EAW90114.1; -; Genomic_DNA.
DR   EMBL; CH471108; EAW90116.1; -; Genomic_DNA.
DR   EMBL; AF006515; AAB87383.1; ALT_TERM; mRNA.
DR   EMBL; U08379; AAC50228.1; -; mRNA.
DR   CCDS; CCDS32553.2; -. [Q12873-3]
DR   CCDS; CCDS32554.1; -. [Q12873-1]
DR   CCDS; CCDS32555.1; -. [Q12873-2]
DR   RefSeq; NP_001005271.2; NM_001005271.2. [Q12873-3]
DR   RefSeq; NP_001005273.1; NM_001005273.2. [Q12873-1]
DR   RefSeq; NP_005843.2; NM_005852.3. [Q12873-2]
DR   UniGene; Hs.25601; -.
DR   ProteinModelPortal; Q12873; -.
DR   SMR; Q12873; 374-429, 453-686.
DR   BioGrid; 107532; 135.
DR   DIP; DIP-32496N; -.
DR   IntAct; Q12873; 97.
DR   MINT; MINT-1185641; -.
DR   STRING; 9606.ENSP00000369716; -.
DR   PhosphoSite; Q12873; -.
DR   BioMuta; CHD3; -.
DR   DMDM; 88911273; -.
DR   MaxQB; Q12873; -.
DR   PaxDb; Q12873; -.
DR   PRIDE; Q12873; -.
DR   Ensembl; ENST00000330494; ENSP00000332628; ENSG00000170004. [Q12873-1]
DR   Ensembl; ENST00000358181; ENSP00000350907; ENSG00000170004. [Q12873-2]
DR   Ensembl; ENST00000380358; ENSP00000369716; ENSG00000170004. [Q12873-3]
DR   GeneID; 1107; -.
DR   KEGG; hsa:1107; -.
DR   UCSC; uc002gje.2; human. [Q12873-1]
DR   UCSC; uc002gjf.2; human. [Q12873-2]
DR   CTD; 1107; -.
DR   GeneCards; CHD3; -.
DR   H-InvDB; HIX0013516; -.
DR   HGNC; HGNC:1918; CHD3.
DR   HPA; HPA043368; -.
DR   MIM; 602120; gene.
DR   neXtProt; NX_Q12873; -.
DR   PharmGKB; PA26454; -.
DR   eggNOG; KOG0383; Eukaryota.
DR   eggNOG; COG0553; LUCA.
DR   GeneTree; ENSGT00760000119067; -.
DR   HOGENOM; HOG000231124; -.
DR   HOVERGEN; HBG005326; -.
DR   InParanoid; Q12873; -.
DR   KO; K11642; -.
DR   OMA; GKGPGYK; -.
DR   OrthoDB; EOG7C8GG7; -.
DR   PhylomeDB; Q12873; -.
DR   TreeFam; TF106448; -.
DR   Reactome; R-HSA-3214815; HDACs deacetylate histones.
DR   Reactome; R-HSA-73762; RNA Polymerase I Transcription Initiation.
DR   ChiTaRS; CHD3; human.
DR   GeneWiki; CHD3; -.
DR   GenomeRNAi; 1107; -.
DR   NextBio; 4590; -.
DR   PRO; PR:Q12873; -.
DR   Proteomes; UP000005640; Chromosome 17.
DR   Bgee; Q12873; -.
DR   CleanEx; HS_CHD3; -.
DR   ExpressionAtlas; Q12873; baseline and differential.
DR   Genevisible; Q12873; HS.
DR   GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0045111; C:intermediate filament cytoskeleton; IDA:HPA.
DR   GO; GO:0005730; C:nucleolus; IDA:HPA.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0016581; C:NuRD complex; IDA:BHF-UCL.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004003; F:ATP-dependent DNA helicase activity; TAS:ProtInc.
DR   GO; GO:0003677; F:DNA binding; TAS:ProtInc.
DR   GO; GO:0004386; F:helicase activity; NAS:UniProtKB.
DR   GO; GO:0044822; F:poly(A) RNA binding; IDA:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; NAS:UniProtKB.
DR   GO; GO:0051297; P:centrosome organization; IDA:UniProtKB.
DR   GO; GO:0006333; P:chromatin assembly or disassembly; IEA:Ensembl.
DR   GO; GO:0016568; P:chromatin modification; IEA:UniProtKB-KW.
DR   GO; GO:0006325; P:chromatin organization; TAS:Reactome.
DR   GO; GO:0032508; P:DNA duplex unwinding; TAS:GOC.
DR   GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; TAS:ProtInc.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; NAS:UniProtKB.
DR   GO; GO:0007051; P:spindle organization; IDA:UniProtKB.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.30.10; -; 1.
DR   Gene3D; 3.30.40.10; -; 2.
DR   Gene3D; 3.40.50.300; -; 2.
DR   InterPro; IPR028722; CHD3.
DR   InterPro; IPR012957; CHD_C2.
DR   InterPro; IPR012958; CHD_N.
DR   InterPro; IPR000953; Chromo/shadow_dom.
DR   InterPro; IPR023780; Chromo_domain.
DR   InterPro; IPR016197; Chromodomain-like.
DR   InterPro; IPR023779; Chromodomain_CS.
DR   InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR   InterPro; IPR009462; DUF1086.
DR   InterPro; IPR009463; DUF1087.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR009071; HMG_box_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR000330; SNF2_N.
DR   InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR001965; Znf_PHD.
DR   InterPro; IPR019787; Znf_PHD-finger.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR10799:SF544; PTHR10799:SF544; 4.
DR   Pfam; PF08074; CHDCT2; 1.
DR   Pfam; PF08073; CHDNT; 1.
DR   Pfam; PF00385; Chromo; 1.
DR   Pfam; PF06461; DUF1086; 1.
DR   Pfam; PF06465; DUF1087; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF00628; PHD; 2.
DR   Pfam; PF00176; SNF2_N; 1.
DR   SMART; SM00298; CHROMO; 2.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SMART; SM00249; PHD; 2.
DR   SMART; SM00184; RING; 2.
DR   SUPFAM; SSF47095; SSF47095; 1.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   SUPFAM; SSF54160; SSF54160; 3.
DR   SUPFAM; SSF57903; SSF57903; 1.
DR   PROSITE; PS00598; CHROMO_1; 1.
DR   PROSITE; PS50013; CHROMO_2; 2.
DR   PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS01359; ZF_PHD_1; 2.
DR   PROSITE; PS50016; ZF_PHD_2; 2.
PE   1: Evidence at protein level;
KW   Alternative splicing; ATP-binding; Chromatin regulator;
KW   Complete proteome; Cytoplasm; Cytoskeleton; DNA-binding; Helicase;
KW   Hydrolase; Isopeptide bond; Metal-binding; Nucleotide-binding;
KW   Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repeat;
KW   Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW   Zinc-finger.
FT   CHAIN         1   2000       Chromodomain-helicase-DNA-binding protein
FT                                3.
FT                                /FTId=PRO_0000080227.
FT   DOMAIN      494    594       Chromo 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00053}.
FT   DOMAIN      631    673       Chromo 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00053}.
FT   DOMAIN      748    932       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN     1064   1229       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   ZN_FING     379    426       PHD-type 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00146}.
FT   ZN_FING     456    503       PHD-type 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00146}.
FT   NP_BIND     761    768       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   REGION     1566   1966       Required for interaction with PCNT.
FT   MOTIF       883    886       DEAH box.
FT   COMPBIAS    206    221       Poly-Ala.
FT   COMPBIAS    243    246       Poly-Pro.
FT   COMPBIAS    355    358       Poly-Lys.
FT   COMPBIAS    434    446       Poly-Glu.
FT   COMPBIAS    697    703       Poly-Lys.
FT   MOD_RES     308    308       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q14839}.
FT   MOD_RES     324    324       Phosphoserine.
FT                                {ECO:0000244|PubMed:17081983}.
FT   MOD_RES     376    376       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:Q14839}.
FT   MOD_RES     713    713       Phosphoserine.
FT                                {ECO:0000244|PubMed:18669648,
FT                                ECO:0000244|PubMed:19690332}.
FT   MOD_RES    1219   1219       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q6PDQ2}.
FT   MOD_RES    1367   1367       Phosphoserine.
FT                                {ECO:0000244|PubMed:18669648}.
FT   MOD_RES    1532   1532       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q14839}.
FT   MOD_RES    1538   1538       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q14839}.
FT   MOD_RES    1601   1601       Phosphoserine.
FT                                {ECO:0000244|PubMed:17081983,
FT                                ECO:0000244|PubMed:18669648,
FT                                ECO:0000244|PubMed:18691976,
FT                                ECO:0000244|PubMed:19690332,
FT                                ECO:0000244|PubMed:20068231,
FT                                ECO:0000244|PubMed:24275569}.
FT   MOD_RES    1605   1605       Phosphoserine.
FT                                {ECO:0000244|PubMed:17081983,
FT                                ECO:0000244|PubMed:18669648,
FT                                ECO:0000244|PubMed:19690332,
FT                                ECO:0000244|PubMed:20068231}.
FT   CROSSLNK   1308   1308       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:25218447}.
FT   CROSSLNK   1573   1573       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:Q14839}.
FT   VAR_SEQ       1     32       MKAADTVILWARSKNDQLRISFPPGLCWGDRM -> MASPL
FT                                RDEEEEEEEMVVSEEEEEEEEEGDEEEEEEVEAADEDDEED
FT                                DDEGVLGRGPGHDRGRDRHSPPGCHLFPPPPPPPPPLPPPP
FT                                PPPP (in isoform 3). {ECO:0000305}.
FT                                /FTId=VSP_047097.
FT   VAR_SEQ    1642   1675       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:9326634,
FT                                ECO:0000303|PubMed:9688266}.
FT                                /FTId=VSP_017231.
FT   VARIANT       3      3       A -> V (in dbSNP:rs931543).
FT                                /FTId=VAR_048728.
FT   CONFLICT    121    126       GEGDGG -> PHFQQK (in Ref. 5; AAC50228).
FT                                {ECO:0000305}.
FT   CONFLICT    309    312       Missing (in Ref. 5; AAC50228).
FT                                {ECO:0000305}.
FT   CONFLICT    653    653       W -> G (in Ref. 5; AAC50228).
FT                                {ECO:0000305}.
FT   CONFLICT   1704   1704       K -> N (in Ref. 1; AAC39923).
FT                                {ECO:0000305}.
SQ   SEQUENCE   2000 AA;  226592 MW;  4494F56E5D0E7083 CRC64;
     MKAADTVILW ARSKNDQLRI SFPPGLCWGD RMPDKDDIRL LPSALGVKKR KRGPKKQKEN
     KPGKPRKRKK RDSEEEFGSE RDEYREKSES GGSEYGTGPG RKRRRKHREK KEKKTKRRKK
     GEGDGGQKQV EQKSSATLLL TWGLEDVEHV FSEEDYHTLT NYKAFSQFMR PLIAKKNPKI
     PMSKMMTILG AKWREFSANN PFKGSAAAVA AAAAAAAAAV AEQVSAAVSS ATPIAPSGPP
     ALPPPPAADI QPPPIRRAKT KEGKGPGHKR RSKSPRVPDG RKKLRGKKMA PLKIKLGLLG
     GKRKKGGSYV FQSDEGPEPE AEESDLDSGS VHSASGRPDG PVRTKKLKRG RPGRKKKKVL
     GCPAVAGEEE VDGYETDHQD YCEVCQQGGE IILCDTCPRA YHLVCLDPEL DRAPEGKWSC
     PHCEKEGVQW EAKEEEEEYE EEGEEEGEKE EEDDHMEYCR VCKDGGELLC CDACISSYHI
     HCLNPPLPDI PNGEWLCPRC TCPVLKGRVQ KILHWRWGEP PVAVPAPQQA DGNPDVPPPR
     PLQGRSEREF FVKWVGLSYW HCSWAKELQL EIFHLVMYRN YQRKNDMDEP PPLDYGSGED
     DGKSDKRKVK DPHYAEMEEK YYRFGIKPEW MTVHRIINHS VDKKGNYHYL VKWRDLPYDQ
     STWEEDEMNI PEYEEHKQSY WRHRELIMGE DPAQPRKYKK KKKELQGDGP PSSPTNDPTV
     KYETQPRFIT ATGGTLHMYQ LEGLNWLRFS WAQGTDTILA DEMGLGKTIQ TIVFLYSLYK
     EGHTKGPFLV SAPLSTIINW EREFQMWAPK FYVVTYTGDK DSRAIIRENE FSFEDNAIKG
     GKKAFKMKRE AQVKFHVLLT SYELITIDQA ALGSIRWACL VVDEAHRLKN NQSKFFRVLN
     GYKIDHKLLL TGTPLQNNLE ELFHLLNFLT PERFNNLEGF LEEFADISKE DQIKKLHDLL
     GPHMLRRLKA DVFKNMPAKT ELIVRVELSP MQKKYYKYIL TRNFEALNSR GGGNQVSLLN
     IMMDLKKCCN HPYLFPVAAM ESPKLPSGAY EGGALIKSSG KLMLLQKMLR KLKEQGHRVL
     IFSQMTKMLD LLEDFLDYEG YKYERIDGGI TGALRQEAID RFNAPGAQQF CFLLSTRAGG
     LGINLATADT VIIFDSDWNP HNDIQAFSRA HRIGQANKVM IYRFVTRASV EERITQVAKR
     KMMLTHLVVR PGLGSKAGSM SKQELDDILK FGTEELFKDE NEGENKEEDS SVIHYDNEAI
     ARLLDRNQDA TEDTDVQNMN EYLSSFKVAQ YVVREEDKIE EIEREIIKQE ENVDPDYWEK
     LLRHHYEQQQ EDLARNLGKG KRVRKQVNYN DAAQEDQDNQ SEYSVGSEEE DEDFDERPEG
     RRQSKRQLRN EKDKPLPPLL ARVGGNIEVL GFNTRQRKAF LNAVMRWGMP PQDAFTTQWL
     VRDLRGKTEK EFKAYVSLFM RHLCEPGADG SETFADGVPR EGLSRQQVLT RIGVMSLVKK
     KVQEFEHING RWSMPELMPD PSADSKRSSR ASSPTKTSPT TPEASATNSP CTSKPATPAP
     SEKGEGIRTP LEKEEAENQE EKPEKNSRIG EKMETEADAP SPAPSLGERL EPRKIPLEDE
     VPGVPGEMEP EPGYRGDREK SATESTPGER GEEKPLDGQE HRERPEGETG DLGKREDVKG
     DRELRPGPRD EPRSNGRREE KTEKPRFMFN IADGGFTELH TLWQNEERAA ISSGKLNEIW
     HRRHDYWLLA GIVLHGYARW QDIQNDAQFA IINEPFKTEA NKGNFLEMKN KFLARRFKLL
     EQALVIEEQL RRAAYLNLSQ EPAHPAMALH ARFAEAECLA ESHQHLSKES LAGNKPANAV
     LHKVLNQLEE LLSDMKADVT RLPATLSRIP PIAARLQMSE RSILSRLASK GTEPHPTPAY
     PPGPYATPPG YGAAFSAAPV GALAAAGANY SQMPAGSFIT AATNGPPVLV KKEKEMVGAL
     VSDGLDRKEP RAGEVICIDD
//
ID   COM1_HUMAN              Reviewed;         897 AA.
AC   Q99708; A6NKN2; A8K8W6; E7ETY1; O75371; Q8NHQ3;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 2.
DT   11-NOV-2015, entry version 147.
DE   RecName: Full=DNA endonuclease RBBP8;
DE            EC=3.1.-.-;
DE   AltName: Full=CtBP-interacting protein;
DE            Short=CtIP;
DE   AltName: Full=Retinoblastoma-binding protein 8;
DE            Short=RBBP-8;
DE   AltName: Full=Retinoblastoma-interacting protein and myosin-like;
DE            Short=RIM;
DE   AltName: Full=Sporulation in the absence of SPO11 protein 2 homolog;
DE            Short=SAE2;
GN   Name=RBBP8; Synonyms=CTIP;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND INTERACTION WITH RB1.
RX   PubMed=9721205; DOI=10.1006/geno.1998.5368;
RA   Fusco C., Reymond A., Zervos A.S.;
RT   "Molecular cloning and characterization of a novel retinoblastoma-
RT   binding protein.";
RL   Genomics 51:351-358(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND INTERACTION WITH CTBP1.
RX   PubMed=9535825; DOI=10.1074/jbc.273.15.8549;
RA   Schaeper U., Subramanian T., Lim L., Boyd J.M., Chinnadurai G.;
RT   "Interaction between a cellular protein that binds to the C-terminal
RT   region of adenovirus E1A (CtBP) and a novel cellular protein is
RT   disrupted by E1A through a conserved PLDLS motif.";
RL   J. Biol. Chem. 273:8549-8552(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Testis;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   TISSUE=Endometrial cancer;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA   Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA   Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16177791; DOI=10.1038/nature03983;
RA   Nusbaum C., Zody M.C., Borowsky M.L., Kamal M., Kodira C.D.,
RA   Taylor T.D., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K.,
RA   FitzGerald M.G., Yang X., Abouelleil A., Allen N.R., Anderson S.,
RA   Bloom T., Bugalter B., Butler J., Cook A., DeCaprio D., Engels R.,
RA   Garber M., Gnirke A., Hafez N., Hall J.L., Norman C.H., Itoh T.,
RA   Jaffe D.B., Kuroki Y., Lehoczky J., Lui A., Macdonald P., Mauceli E.,
RA   Mikkelsen T.S., Naylor J.W., Nicol R., Nguyen C., Noguchi H.,
RA   O'Leary S.B., Piqani B., Smith C.L., Talamas J.A., Topham K.,
RA   Totoki Y., Toyoda A., Wain H.M., Young S.K., Zeng Q., Zimmer A.R.,
RA   Fujiyama A., Hattori M., Birren B.W., Sakaki Y., Lander E.S.;
RT   "DNA sequence and analysis of human chromosome 18.";
RL   Nature 437:551-555(2005).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Testis;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [8]
RP   FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH BRCA1.
RX   PubMed=10764811; DOI=10.1074/jbc.M909494199;
RA   Yu X., Baer R.;
RT   "Nuclear localization and cell cycle-specific expression of CtIP, a
RT   protein that associates with the BRCA1 tumor suppressor.";
RL   J. Biol. Chem. 275:18541-18549(2000).
RN   [9]
RP   FUNCTION, PHOSPHORYLATION AT SER-664 AND SER-745, AND MUTAGENESIS OF
RP   SER-664 AND SER-745.
RX   PubMed=10910365; DOI=10.1038/35018134;
RA   Li S., Ting N.S.Y., Zheng L., Chen P.-L., Ziv Y., Shiloh Y.,
RA   Lee E.Y.-H.P., Lee W.-H.;
RT   "Functional link of BRCA1 and ataxia telangiectasia gene product in
RT   DNA damage response.";
RL   Nature 406:210-215(2000).
RN   [10]
RP   INTERACTION WITH LMO4.
RX   PubMed=11751867; DOI=10.1074/jbc.M110603200;
RA   Sum E.Y., Peng B., Yu X., Chen J., Byrne J., Lindeman G.J.,
RA   Visvader J.E.;
RT   "The LIM domain protein LMO4 interacts with the cofactor CtIP and the
RT   tumor suppressor BRCA1 and inhibits BRCA1 activity.";
RL   J. Biol. Chem. 277:7849-7856(2002).
RN   [11]
RP   INTERACTION WITH SIAH1, AND UBIQUITINATION.
RX   PubMed=14654780; DOI=10.1038/sj.onc.1206994;
RA   Germani A., Prabel A., Mourah S., Podgorniak M.-P., Di Carlo A.,
RA   Ehrlich R., Gisselbrecht S., Varin-Blank N., Calvo F.,
RA   Bruzzoni-Giovanelli H.;
RT   "SIAH-1 interacts with CtIP and promotes its degradation by the
RT   proteasome pathway.";
RL   Oncogene 22:8845-8851(2003).
RN   [12]
RP   SUBUNIT, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=15084581; DOI=10.1074/jbc.M313974200;
RA   Dubin M.J., Stokes P.H., Sum E.Y., Williams R.S., Valova V.A.,
RA   Robinson P.J., Lindeman G.J., Glover J.N., Visvader J.E.,
RA   Matthews J.M.;
RT   "Dimerization of CtIP, a BRCA1- and CtBP-interacting protein, is
RT   mediated by an N-terminal coiled-coil motif.";
RL   J. Biol. Chem. 279:26932-26938(2004).
RN   [13]
RP   FUNCTION, PHOSPHORYLATION AT SER-327, INTERACTION WITH BRCA1, AND
RP   MUTAGENESIS OF SER-327.
RX   PubMed=15485915; DOI=10.1128/MCB.24.21.9478-9486.2004;
RA   Yu X., Chen J.;
RT   "DNA damage-induced cell cycle checkpoint control requires CtIP, a
RT   phosphorylation-dependent binding partner of BRCA1 C-terminal
RT   domains.";
RL   Mol. Cell. Biol. 24:9478-9486(2004).
RN   [14]
RP   INTERACTION WITH BRCA1, FUNCTION, UBIQUITINATION, AND MUTAGENESIS OF
RP   SER-327.
RX   PubMed=16818604; DOI=10.1101/gad.1431006;
RA   Yu X., Fu S., Lai M., Baer R., Chen J.;
RT   "BRCA1 ubiquitinates its phosphorylation-dependent binding partner
RT   CtIP.";
RL   Genes Dev. 20:1721-1726(2006).
RN   [15]
RP   FUNCTION.
RX   PubMed=16581787; DOI=10.1128/MCB.26.8.3124-3134.2006;
RA   Liu F., Lee W.H.;
RT   "CtIP activates its own and cyclin D1 promoters via the E2F/RB pathway
RT   during G1/S progression.";
RL   Mol. Cell. Biol. 26:3124-3134(2006).
RN   [16]
RP   FUNCTION, PHOSPHORYLATION, SUBCELLULAR LOCATION, AND INTERACTION WITH
RP   BRCA1; MRE11A AND RAD50.
RX   PubMed=17965729; DOI=10.1038/nature06337;
RA   Sartori A.A., Lukas C., Coates J., Mistrik M., Fu S., Bartek J.,
RA   Baer R., Lukas J., Jackson S.P.;
RT   "Human CtIP promotes DNA end resection.";
RL   Nature 450:509-514(2007).
RN   [17]
RP   ASSOCIATION WITH OVARIAN CANCER SURVIVAL.
RX   PubMed=19270026; DOI=10.1093/hmg/ddp107;
RA   Quaye L., Dafou D., Ramus S.J., Song H., Gentry-Maharaj A.,
RA   Notaridou M., Hogdall E., Kjaer S.K., Christensen L., Hogdall C.,
RA   Easton D.F., Jacobs I., Menon U., Pharoah P.D., Gayther S.A.;
RT   "Functional complementation studies identify candidate genes and
RT   common genetic variants associated with ovarian cancer survival.";
RL   Hum. Mol. Genet. 18:1869-1878(2009).
RN   [18]
RP   FUNCTION, DNA-BINDING, PHOSPHORYLATION AT THR-847, AND MUTAGENESIS OF
RP   THR-847.
RX   PubMed=19202191; DOI=10.1074/jbc.M808906200;
RA   Huertas P., Jackson S.P.;
RT   "Human CtIP mediates cell cycle control of DNA end resection and
RT   double strand break repair.";
RL   J. Biol. Chem. 284:9558-9565(2009).
RN   [19]
RP   FUNCTION, INTERACTION WITH MRE11A; RAD50 AND NBN, AND MUTAGENESIS OF
RP   HIS-31; VAL-35; LYS-41 AND LEU-45.
RX   PubMed=19759395; DOI=10.1074/jbc.M109.023424;
RA   Yuan J., Chen J.;
RT   "N terminus of CtIP is critical for homologous recombination-mediated
RT   double-strand break repair.";
RL   J. Biol. Chem. 284:31746-31752(2009).
RN   [20]
RP   FUNCTION, AND MUTAGENESIS OF LYS-513 AND LYS-515.
RX   PubMed=20064462; DOI=10.1016/j.molcel.2009.12.002;
RA   You Z., Shi L.Z., Zhu Q., Wu P., Zhang Y.W., Basilio A., Tonnu N.,
RA   Verma I.M., Berns M.W., Hunter T.;
RT   "CtIP links DNA double-strand break sensing to resection.";
RL   Mol. Cell 36:954-969(2009).
RN   [21]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA   Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA   Rodionov V., Han D.K.;
RT   "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT   reveals system-wide modulation of protein-protein interactions.";
RL   Sci. Signal. 2:RA46-RA46(2009).
RN   [22]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-723, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA   Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full
RT   phosphorylation site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [23]
RP   FUNCTION, ACETYLATION AT LYS-432; LYS-526 AND LYS-604, INTERACTION
RP   WITH SIRT6, IDENTIFICATION BY MASS SPECTROMETRY, AND MUTAGENESIS OF
RP   LYS-432; LYS-526 AND LYS-604.
RX   PubMed=20829486; DOI=10.1126/science.1192049;
RA   Kaidi A., Weinert B.T., Choudhary C., Jackson S.P.;
RT   "Human SIRT6 promotes DNA end resection through CtIP deacetylation.";
RL   Science 329:1348-1353(2010).
RN   [24]
RP   ASSOCIATION WITH BREAST CANCER.
RX   PubMed=21799032; DOI=10.1158/0008-5472.CAN-11-0773;
RA   Rebbeck T.R., Mitra N., Domchek S.M., Wan F., Friebel T.M., Tran T.V.,
RA   Singer C.F., Tea M.K., Blum J.L., Tung N., Olopade O.I., Weitzel J.N.,
RA   Lynch H.T., Snyder C.L., Garber J.E., Antoniou A.C., Peock S.,
RA   Evans D.G., Paterson J., Kennedy M.J., Donaldson A., Dorkins H.,
RA   Easton D.F., Rubinstein W.S., Daly M.B., Isaacs C., Nevanlinna H.,
RA   Couch F.J., Andrulis I.L., Freidman E., Laitman Y., Ganz P.A.,
RA   Tomlinson G.E., Neuhausen S.L., Narod S.A., Phelan C.M., Greenberg R.,
RA   Nathanson K.L.;
RT   "Modification of BRCA1-associated breast and ovarian cancer risk by
RT   BRCA1-interacting genes.";
RL   Cancer Res. 71:5792-5805(2011).
RN   [25]
RP   INVOLVEMENT IN JWDS, AND INVOLVEMENT IN SCKL2.
RX   PubMed=21998596; DOI=10.1371/journal.pgen.1002310;
RA   Jackson S.P., Borglum A.D.;
RT   "CtIP mutations cause Seckel and Jawad syndromes.";
RL   PLoS Genet. 7:E1002310-E1002310(2011).
RN   [26]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-869, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25218447; DOI=10.1038/nsmb.2890;
RA   Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA   Vertegaal A.C.;
RT   "Uncovering global SUMOylation signaling networks in a site-specific
RT   manner.";
RL   Nat. Struct. Mol. Biol. 21:927-936(2014).
CC   -!- FUNCTION: Endonuclease that cooperates with the MRE11-RAD50-NBN
CC       (MRN) complex in processing meiotic and mitotic double-strand
CC       breaks (DSBs) by ensuring both resection and intrachromosomal
CC       association of the broken ends. Functions downstream of the MRN
CC       complex and ATM, promotes ATR activation and its recruitment to
CC       DSBs in the S/G2 phase facilitating the generation of ssDNA.
CC       Component of the BRCA1-RBBP8 complex that regulates CHEK1
CC       activation and controls cell cycle G2/M checkpoints on DNA damage.
CC       Promotes microhomology-mediated alternative end joining (A-NHEJ)
CC       during class-switch recombination and plays an essential role in
CC       chromosomal translocations. {ECO:0000269|PubMed:10764811,
CC       ECO:0000269|PubMed:10910365, ECO:0000269|PubMed:15485915,
CC       ECO:0000269|PubMed:16581787, ECO:0000269|PubMed:16818604,
CC       ECO:0000269|PubMed:17965729, ECO:0000269|PubMed:19202191,
CC       ECO:0000269|PubMed:19759395, ECO:0000269|PubMed:20064462,
CC       ECO:0000269|PubMed:20829486}.
CC   -!- SUBUNIT: Homodimer; dimerizes via the coiled coil domain.
CC       Interacts (via the PXDLS motif) with CTBP1; the interaction is
CC       disrupted via binding of the adenovirus E1A to CTBP1. Component of
CC       the BRCA1-RBBBP8 complex. Interacts (the Ser-327 phosphorylated
CC       form) with BRCA1 (via the C-terminal BRCA1 domains): the
CC       interaction occurs in the G2 phase, ubiquitinates RBBP8 and
CC       involves RBBP8 in BRCA1-dependent G2/M checkpoint control on DNA
CC       damage. Interacts with RB1. Interacts with the MRN complex.
CC       Interacts directly with MRE11A; the interaction is required for
CC       efficient homologous recombination (HR) and regulation of the MRN
CC       complex. Interacts directly with RAD50. Interacts directly with
CC       NBN. Interacts with SIRT6; the interaction deacetylates RBBP8 upon
CC       DNA damage. Interacts with LM04 (via the LIM zinc-binding 1
CC       domain). {ECO:0000269|PubMed:10764811,
CC       ECO:0000269|PubMed:11751867, ECO:0000269|PubMed:14654780,
CC       ECO:0000269|PubMed:15084581, ECO:0000269|PubMed:15485915,
CC       ECO:0000269|PubMed:16818604, ECO:0000269|PubMed:17965729,
CC       ECO:0000269|PubMed:19759395, ECO:0000269|PubMed:20829486,
CC       ECO:0000269|PubMed:9535825, ECO:0000269|PubMed:9721205}.
CC   -!- INTERACTION:
CC       P38398:BRCA1; NbExp=9; IntAct=EBI-745715, EBI-349905;
CC       Q9UQ84:EXO1; NbExp=3; IntAct=EBI-745715, EBI-944667;
CC       P25800:LMO1; NbExp=3; IntAct=EBI-10203615, EBI-8639312;
CC       P61968:LMO4; NbExp=3; IntAct=EBI-10203615, EBI-2798728;
CC       Q13526:PIN1; NbExp=3; IntAct=EBI-10203615, EBI-714158;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10764811,
CC       ECO:0000269|PubMed:17965729}. Note=Associates with sites of DNA
CC       damage in S/G2 phase. Ubiquitinated RBBP8 binds to chromatin
CC       following DNA damage.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q99708-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q99708-2; Sequence=VSP_043220;
CC       Name=3;
CC         IsoId=Q99708-3; Sequence=VSP_045247, VSP_045248;
CC         Note=No experimental confirmation available. Ref.4 (BX648221)
CC         sequence is in conflict in position: 862:S->G. {ECO:0000305};
CC   -!- INDUCTION: Levels increase dramatically as dividing cells traverse
CC       the G1/S boubdary. Down-regulated in tamoxifen-resistant breast
CC       cancer cells.
CC   -!- DOMAIN: The PXDLS motif binds to a cleft in CtBP proteins.
CC   -!- DOMAIN: The damage-recruitment motif is required for DNA binding
CC       and translocation to sites of DNA damage.
CC   -!- PTM: Acetylated. Deacetylation by SIRT6 upon DNA damage promotes
CC       DNA end resection. {ECO:0000269|PubMed:20829486}.
CC   -!- PTM: Hyperphosphorylation upon ionizing radiation results in
CC       dissociation from BRCA1. Phosphorylation at Thr-847 by CDK1 is
CC       essential for the recruitment to DNA and the DNA repair function.
CC       Phosphorylated on Ser-327 as cells enter G2 phase. This
CC       phosphorylation is required for binding BRCA1 and for the G2/M DNA
CC       damage transition checkpoint control.
CC       {ECO:0000269|PubMed:10910365, ECO:0000269|PubMed:15485915,
CC       ECO:0000269|PubMed:17965729, ECO:0000269|PubMed:19202191}.
CC   -!- PTM: Ubiquitinated. Ubiquitination at multiple sites by BRCA1 (via
CC       its N-terminal RING domain) does not lead to its proteosomal
CC       degradation but instead the ubiquitinated RBBP8 binds to chromatin
CC       following DNA damage and may play a role in G2/M checkpoint
CC       control. {ECO:0000269|PubMed:14654780,
CC       ECO:0000269|PubMed:16818604}.
CC   -!- DISEASE: Seckel syndrome 2 (SCKL2) [MIM:606744]: A rare autosomal
CC       recessive disorder characterized by proportionate dwarfism of
CC       prenatal onset associated with low birth weight, growth
CC       retardation, severe microcephaly with a bird-headed like
CC       appearance, and mental retardation. {ECO:0000269|PubMed:21998596}.
CC       Note=The disease is caused by mutations affecting the gene
CC       represented in this entry.
CC   -!- DISEASE: Jawad syndrome (JWDS) [MIM:251255]: A syndrome
CC       characterized by congenital microcephaly, moderately severe mental
CC       retardation, and symmetrical digital anomalies. Digital
CC       malformations of variable degree include hallux valgus, syndactyly
CC       of toes 4 and 5, short fifth fingers, single flexion crease of
CC       fifth fingers, polydactyly and synpolydactyly.
CC       {ECO:0000269|PubMed:21998596}. Note=The disease is caused by
CC       mutations affecting the gene represented in this entry.
CC   -!- DISEASE: Note=Genetic variability in RBBP8 is noted as a factor in
CC       BRCA1-associated breast cancer risk. Exhibits sensitivity to
CC       tamoxifen in certain breast cancer cell lines.
CC   -!- SIMILARITY: Belongs to the COM1/SAE2/CtIP family. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC       and Haematology;
CC       URL="http://atlasgeneticsoncology.org/Genes/RBBP8ID42066ch18q11.html";
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DR   EMBL; AF043431; AAC34368.1; -; mRNA.
DR   EMBL; U72066; AAC14371.1; -; mRNA.
DR   EMBL; AK292481; BAF85170.1; -; mRNA.
DR   EMBL; BX648221; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AC091147; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC106033; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471088; EAX01144.1; -; Genomic_DNA.
DR   EMBL; BC030590; AAH30590.1; -; mRNA.
DR   CCDS; CCDS11874.1; -. [Q99708-3]
DR   CCDS; CCDS11875.1; -. [Q99708-1]
DR   RefSeq; NP_002885.1; NM_002894.2. [Q99708-1]
DR   RefSeq; NP_976036.1; NM_203291.1. [Q99708-1]
DR   RefSeq; NP_976037.1; NM_203292.1. [Q99708-3]
DR   RefSeq; XP_006722582.1; XM_006722519.1. [Q99708-1]
DR   RefSeq; XP_006722583.1; XM_006722520.1. [Q99708-1]
DR   RefSeq; XP_006722584.1; XM_006722521.1. [Q99708-1]
DR   RefSeq; XP_011524434.1; XM_011526132.1. [Q99708-1]
DR   UniGene; Hs.546282; -.
DR   PDB; 2L4Z; NMR; -; A=641-685.
DR   PDB; 4D2H; X-ray; 1.90 A; A/B/C/D/E/F/G/H=18-52.
DR   PDBsum; 2L4Z; -.
DR   PDBsum; 4D2H; -.
DR   ProteinModelPortal; Q99708; -.
DR   SMR; Q99708; 18-52, 641-677.
DR   BioGrid; 111867; 43.
DR   DIP; DIP-24244N; -.
DR   IntAct; Q99708; 27.
DR   MINT; MINT-102295; -.
DR   STRING; 9606.ENSP00000323050; -.
DR   PhosphoSite; Q99708; -.
DR   BioMuta; RBBP8; -.
DR   DMDM; 116242745; -.
DR   MaxQB; Q99708; -.
DR   PaxDb; Q99708; -.
DR   PRIDE; Q99708; -.
DR   DNASU; 5932; -.
DR   Ensembl; ENST00000327155; ENSP00000323050; ENSG00000101773. [Q99708-1]
DR   Ensembl; ENST00000399722; ENSP00000382628; ENSG00000101773. [Q99708-1]
DR   Ensembl; ENST00000399725; ENSP00000382630; ENSG00000101773. [Q99708-3]
DR   GeneID; 5932; -.
DR   KEGG; hsa:5932; -.
DR   UCSC; uc002ktw.3; human. [Q99708-1]
DR   UCSC; uc002ktz.3; human.
DR   CTD; 5932; -.
DR   GeneCards; RBBP8; -.
DR   GeneReviews; RBBP8; -.
DR   HGNC; HGNC:9891; RBBP8.
DR   HPA; HPA039890; -.
DR   HPA; HPA052946; -.
DR   MIM; 251255; phenotype.
DR   MIM; 604124; gene.
DR   MIM; 606744; phenotype.
DR   neXtProt; NX_Q99708; -.
DR   Orphanet; 313795; Jawad syndrome.
DR   Orphanet; 808; Seckel syndrome.
DR   PharmGKB; PA34255; -.
DR   eggNOG; ENOG410IJ39; Eukaryota.
DR   eggNOG; ENOG410ZSBE; LUCA.
DR   GeneTree; ENSGT00530000063835; -.
DR   HOGENOM; HOG000293331; -.
DR   HOVERGEN; HBG057046; -.
DR   InParanoid; Q99708; -.
DR   OrthoDB; EOG771274; -.
DR   PhylomeDB; Q99708; -.
DR   TreeFam; TF106469; -.
DR   Reactome; R-HSA-912446; Meiotic recombination.
DR   ChiTaRS; RBBP8; human.
DR   EvolutionaryTrace; Q99708; -.
DR   GeneWiki; RBBP8; -.
DR   GenomeRNAi; 5932; -.
DR   NextBio; 23118; -.
DR   PRO; PR:Q99708; -.
DR   Proteomes; UP000005640; Chromosome 18.
DR   Bgee; Q99708; -.
DR   CleanEx; HS_RBBP8; -.
DR   ExpressionAtlas; Q99708; baseline and differential.
DR   Genevisible; Q99708; HS.
DR   GO; GO:0005730; C:nucleolus; IDA:HPA.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; TAS:ProtInc.
DR   GO; GO:0017053; C:transcriptional repressor complex; IDA:BHF-UCL.
DR   GO; GO:0003684; F:damaged DNA binding; IDA:UniProtKB.
DR   GO; GO:0001103; F:RNA polymerase II repressing transcription factor binding; IPI:BHF-UCL.
DR   GO; GO:0001106; F:RNA polymerase II transcription corepressor activity; IDA:BHF-UCL.
DR   GO; GO:0000014; F:single-stranded DNA endodeoxyribonuclease activity; IMP:UniProtKB.
DR   GO; GO:0001835; P:blastocyst hatching; IEA:Ensembl.
DR   GO; GO:0000075; P:cell cycle checkpoint; TAS:ProtInc.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0010792; P:DNA double-strand break processing involved in repair via single-strand annealing; IMP:UniProtKB.
DR   GO; GO:0006281; P:DNA repair; TAS:ProtInc.
DR   GO; GO:0000724; P:double-strand break repair via homologous recombination; IDA:UniProtKB.
DR   GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IEA:Ensembl.
DR   GO; GO:0031572; P:G2 DNA damage checkpoint; IDA:UniProtKB.
DR   GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0007067; P:mitotic nuclear division; IEA:UniProtKB-KW.
DR   GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:GOC.
DR   GO; GO:0006289; P:nucleotide-excision repair; IMP:CACAO.
DR   GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; TAS:ProtInc.
DR   GO; GO:0032355; P:response to estradiol; IEA:Ensembl.
DR   InterPro; IPR013882; Com1/Ctip_fam.
DR   InterPro; IPR019518; CtIP_N.
DR   Pfam; PF10482; CtIP_N; 1.
DR   Pfam; PF08573; SAE2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative splicing; Cell cycle;
KW   Cell division; Coiled coil; Complete proteome; DNA damage; DNA repair;
KW   DNA-binding; Dwarfism; Endonuclease; Hydrolase; Isopeptide bond;
KW   Meiosis; Mental retardation; Mitosis; Nuclease; Nucleus;
KW   Phosphoprotein; Polymorphism; Reference proteome; Ubl conjugation.
FT   CHAIN         1    897       DNA endonuclease RBBP8.
FT                                /FTId=PRO_0000097179.
FT   REGION       22     45       Essential for binding to the MRN complex
FT                                and for RPA focus formation on DNA
FT                                damage.
FT   REGION      509    557       Damage-recruitment motif.
FT   COILED       28    157       {ECO:0000255}.
FT   MOTIF       490    494       PXDLS motif.
FT   COMPBIAS    750    753       Poly-Glu.
FT   MOD_RES     233    233       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q80YR6}.
FT   MOD_RES     326    326       Phosphoserine.
FT                                {ECO:0000269|PubMed:17965729}.
FT   MOD_RES     327    327       Phosphoserine.
FT                                {ECO:0000269|PubMed:15485915}.
FT   MOD_RES     349    349       Phosphoserine.
FT                                {ECO:0000269|PubMed:17965729}.
FT   MOD_RES     432    432       N6-acetyllysine.
FT                                {ECO:0000269|PubMed:20829486}.
FT   MOD_RES     526    526       N6-acetyllysine.
FT                                {ECO:0000269|PubMed:20829486}.
FT   MOD_RES     604    604       N6-acetyllysine.
FT                                {ECO:0000269|PubMed:20829486}.
FT   MOD_RES     664    664       Phosphoserine; by ATM.
FT                                {ECO:0000269|PubMed:10910365}.
FT   MOD_RES     679    679       Phosphoserine.
FT                                {ECO:0000269|PubMed:17965729}.
FT   MOD_RES     723    723       Phosphoserine.
FT                                {ECO:0000244|PubMed:20068231}.
FT   MOD_RES     745    745       Phosphoserine; by ATM.
FT                                {ECO:0000269|PubMed:10910365}.
FT   MOD_RES     847    847       Phosphothreonine; by CDK1.
FT                                {ECO:0000269|PubMed:19202191}.
FT   CROSSLNK    869    869       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:25218447}.
FT   VAR_SEQ     714    714       S -> SMLFYI (in isoform 2).
FT                                {ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_043220.
FT   VAR_SEQ     786    867       RETSLQNFPHIEVVRKKEERRKLLGHTCKECEIYYADMPAE
FT                                EREKKLASCSRHRFRYIPPNTPENFWEVGFPSTQTCMERGY
FT                                -> SIMQICQQKKEKRNWLPAQDTDSATFHPTHQRIFGKLV
FT                                FLPLRLVWKEVILRKILILVLVQKDVSLTTQYFLQKARSRR
FT                                HRR (in isoform 3).
FT                                {ECO:0000303|PubMed:17974005}.
FT                                /FTId=VSP_045247.
FT   VAR_SEQ     868    897       Missing (in isoform 3).
FT                                {ECO:0000303|PubMed:17974005}.
FT                                /FTId=VSP_045248.
FT   VARIANT     357    357       K -> N (in dbSNP:rs34678569).
FT                                /FTId=VAR_051308.
FT   VARIANT     387    387       H -> Y (in dbSNP:rs1804732).
FT                                /FTId=VAR_028308.
FT   MUTAGEN      31     31       H->A: No effect on RPA focus formation on
FT                                DNA damage.
FT                                {ECO:0000269|PubMed:19759395}.
FT   MUTAGEN      35     35       V->A: No effect on RPA focus formation on
FT                                DNA damage.
FT                                {ECO:0000269|PubMed:19759395}.
FT   MUTAGEN      41     41       K->A: No effect on RPA focus formation on
FT                                DNA damage.
FT                                {ECO:0000269|PubMed:19759395}.
FT   MUTAGEN      45     45       L->A: No effect on RPA focus formation on
FT                                DNA damage.
FT                                {ECO:0000269|PubMed:19759395}.
FT   MUTAGEN     327    327       S->A: Abolishes BRCA1 interaction and
FT                                ubiquitination. No activation of CHEK1
FT                                after DNA damage.
FT                                {ECO:0000269|PubMed:15485915,
FT                                ECO:0000269|PubMed:16818604}.
FT   MUTAGEN     432    432       K->R: Greatly reduced acetylation.
FT                                Alleviates resection defects caused by
FT                                depletion of SIRT6; when associated with
FT                                R-526 and R-604.
FT                                {ECO:0000269|PubMed:20829486}.
FT   MUTAGEN     513    513       K->A: Abolishes damage recruitment
FT                                capability.
FT                                {ECO:0000269|PubMed:20064462}.
FT   MUTAGEN     515    515       K->A: Abolishes damage recruitment
FT                                capability.
FT                                {ECO:0000269|PubMed:20064462}.
FT   MUTAGEN     526    526       K->R: Greatly reduced acetylation.
FT                                Alleviates resection defects caused by
FT                                depletion of SIRT6; when associated with
FT                                R-432 and R-604.
FT                                {ECO:0000269|PubMed:20829486}.
FT   MUTAGEN     604    604       K->R: Greatly reduced acetylation.
FT                                Alleviates resection defects caused by
FT                                depletion of SIRT6; when associated with
FT                                R-432 and R-526.
FT                                {ECO:0000269|PubMed:20829486}.
FT   MUTAGEN     664    664       S->A: Abrogates dissociation of BRCA1.
FT                                {ECO:0000269|PubMed:10910365}.
FT   MUTAGEN     745    745       S->A: Abrogates dissociation of BRCA1.
FT                                {ECO:0000269|PubMed:10910365}.
FT   MUTAGEN     847    847       T->A: Impairs DNA resection.
FT                                {ECO:0000269|PubMed:19202191}.
FT   MUTAGEN     847    847       T->E: Mimics constitutive
FT                                phosphorylation.
FT                                {ECO:0000269|PubMed:19202191}.
FT   CONFLICT      4      4       S -> L (in Ref. 1; AAC14371).
FT                                {ECO:0000305}.
FT   CONFLICT     74     74       H -> Q (in Ref. 4; BX648221).
FT                                {ECO:0000305}.
FT   CONFLICT     92     92       C -> Y (in Ref. 3; BAF85170).
FT                                {ECO:0000305}.
FT   CONFLICT    123    123       E -> G (in Ref. 3; BAF85170).
FT                                {ECO:0000305}.
FT   CONFLICT    341    341       D -> G (in Ref. 4; BX648221).
FT                                {ECO:0000305}.
FT   CONFLICT    515    515       K -> R (in Ref. 4; BX648221).
FT                                {ECO:0000305}.
FT   CONFLICT    521    521       L -> P (in Ref. 3; BAF85170).
FT                                {ECO:0000305}.
FT   CONFLICT    642    642       L -> P (in Ref. 4; BX648221).
FT                                {ECO:0000305}.
FT   HELIX        18     50       {ECO:0000244|PDB:4D2H}.
FT   STRAND      648    650       {ECO:0000244|PDB:2L4Z}.
FT   HELIX       651    653       {ECO:0000244|PDB:2L4Z}.
FT   TURN        662    666       {ECO:0000244|PDB:2L4Z}.
FT   STRAND      677    679       {ECO:0000244|PDB:2L4Z}.
SQ   SEQUENCE   897 AA;  101942 MW;  E028DE56DE55C0F2 CRC64;
     MNISGSSCGS PNSADTSSDF KDLWTKLKEC HDREVQGLQV KVTKLKQERI LDAQRLEEFF
     TKNQQLREQQ KVLHETIKVL EDRLRAGLCD RCAVTEEHMR KKQQEFENIR QQNLKLITEL
     MNERNTLQEE NKKLSEQLQQ KIENDQQHQA AELECEEDVI PDSPITAFSF SGVNRLRRKE
     NPHVRYIEQT HTKLEHSVCA NEMRKVSKSS THPQHNPNEN EILVADTYDQ SQSPMAKAHG
     TSSYTPDKSS FNLATVVAET LGLGVQEESE TQGPMSPLGD ELYHCLEGNH KKQPFEESTR
     NTEDSLRFSD STSKTPPQEE LPTRVSSPVF GATSSIKSGL DLNTSLSPSL LQPGKKKHLK
     TLPFSNTCIS RLEKTRSKSE DSALFTHHSL GSEVNKIIIQ SSNKQILINK NISESLGEQN
     RTEYGKDSNT DKHLEPLKSL GGRTSKRKKT EEESEHEVSC PQASFDKENA FPFPMDNQFS
     MNGDCVMDKP LDLSDRFSAI QRQEKSQGSE TSKNKFRQVT LYEALKTIPK GFSSSRKASD
     GNCTLPKDSP GEPCSQECII LQPLNKCSPD NKPSLQIKEE NAVFKIPLRP RESLETENVL
     DDIKSAGSHE PIKIQTRSDH GGCELASVLQ LNPCRTGKIK SLQNNQDVSF ENIQWSIDPG
     ADLSQYKMDV TVIDTKDGSQ SKLGGETVDM DCTLVSETVL LKMKKQEQKG EKSSNEERKM
     NDSLEDMFDR TTHEEYESCL ADSFSQAADE EEELSTATKK LHTHGDKQDK VKQKAFVEPY
     FKGDERETSL QNFPHIEVVR KKEERRKLLG HTCKECEIYY ADMPAEEREK KLASCSRHRF
     RYIPPNTPEN FWEVGFPSTQ TCMERGYIKE DLDPCPRPKR RQPYNAIFSP KGKEQKT
//
ID   CTBP1_HUMAN             Reviewed;         440 AA.
AC   Q13363; Q4W5N3; Q7Z2Q5;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1999, sequence version 2.
DT   11-NOV-2015, entry version 173.
DE   RecName: Full=C-terminal-binding protein 1;
DE            Short=CtBP1;
DE            EC=1.1.1.-;
GN   Name=CTBP1; Synonyms=CTBP;
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), PROTEIN SEQUENCE OF 98-108,
RP   AND INTERACTION WITH RBBP8 AND ADENOVIRUS E1A.
RC   TISSUE=B-cell, and Cervix carcinoma;
RX   PubMed=7479821; DOI=10.1073/pnas.92.23.10467;
RA   Schaeper U., Boyd J.M., Verma S., Uhlmann E., Subramanian T.,
RA   Chinnadurai G.;
RT   "Molecular cloning and characterization of a cellular phosphoprotein
RT   that interacts with a conserved C-terminal domain of adenovirus E1A
RT   involved in negative modulation of oncogenic transformation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 92:10467-10471(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SEQUENCE REVISION, AND
RP   FUNCTION.
RX   PubMed=9858600;
RA   Sewalt R.G.A.B., Gunster M.J., van der Vlag J., Satijn D.P.E.,
RA   Otte A.P.;
RT   "C-terminal binding protein is a transcriptional repressor that
RT   interacts with a specific class of vertebrate polycomb proteins.";
RL   Mol. Cell. Biol. 19:777-787(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15815621; DOI=10.1038/nature03466;
RA   Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
RA   Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA   Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA   Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA   Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA   Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA   Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA   Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA   Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA   Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA   McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA   Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
RA   Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA   Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA   Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA   Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA   Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA   Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA   Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA   Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA   McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA   Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA   Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
RA   Waterston R.H., Wilson R.K.;
RT   "Generation and annotation of the DNA sequences of human chromosomes 2
RT   and 4.";
RL   Nature 434:724-731(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Brain, and Lung;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   INTERACTION WITH ADENOVIRUS E1A, AND PHOSPHORYLATION.
RX   PubMed=8440238;
RA   Boyd J.M., Subramanian T., Schaeper U., la Regina M., Bayley S.,
RA   Chinnadurai G.;
RT   "A region in the C-terminus of adenovirus 2/5 E1a protein is required
RT   for association with a cellular phosphoprotein and important for the
RT   negative modulation of T24-ras mediated transformation, tumorigenesis
RT   and metastasis.";
RL   EMBO J. 12:469-478(1993).
RN   [7]
RP   INTERACTION WITH MECOM.
RX   PubMed=11568182; DOI=10.1074/jbc.M106733200;
RA   Chakraborty S., Senyuk V., Sitailo S., Chi Y., Nucifora G.;
RT   "Interaction of EVI1 with cAMP-responsive element-binding protein-
RT   binding protein (CBP) and p300/CBP-associated factor (P/CAF) results
RT   in reversible acetylation of EVI1 and in co-localization in nuclear
RT   speckles.";
RL   J. Biol. Chem. 276:44936-44943(2001).
RN   [8]
RP   INTERACTION WITH EBV EBNA6.
RX   PubMed=11462050; DOI=10.1128/JVI.75.16.7749-7755.2001;
RA   Touitou R., Hickabottom M., Parker G., Crook T., Allday M.J.;
RT   "Physical and functional interactions between the corepressor CtBP and
RT   the Epstein-Barr virus nuclear antigen EBNA3C.";
RL   J. Virol. 75:7749-7755(2001).
RN   [9]
RP   INTERACTION WITH NRIP1.
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   [10]
RP   INTERACTION WITH EBV EBNA3.
RX   PubMed=12372828; DOI=10.1074/jbc.M208116200;
RA   Hickabottom M., Parker G.A., Freemont P., Crook T., Allday M.J.;
RT   "Two nonconsensus sites in the Epstein-Barr virus oncoprotein EBNA3A
RT   cooperate to bind the co-repressor carboxyl-terminal-binding protein
RT   (CtBP).";
RL   J. Biol. Chem. 277:47197-47204(2002).
RN   [11]
RP   SUMOYLATION AT LYS-428, AND SUBCELLULAR LOCATION.
RX   PubMed=12679040; DOI=10.1016/S0092-8674(03)00159-4;
RA   Kagey M.H., Melhuish T.A., Wotton D.;
RT   "The polycomb protein Pc2 is a SUMO E3.";
RL   Cell 113:127-137(2003).
RN   [12]
RP   INTERACTION WITH HIPK2, PHOSPHORYLATION AT SER-422, AND MUTAGENESIS OF
RP   SER-422.
RX   PubMed=14567915; DOI=10.1016/S0092-8674(03)00802-X;
RA   Zhang Q., Yoshimatsu Y., Hildebrand J., Frisch S.M., Goodman R.H.;
RT   "Homeodomain interacting protein kinase 2 promotes apoptosis by
RT   downregulating the transcriptional corepressor CtBP.";
RL   Cell 115:177-186(2003).
RN   [13]
RP   FUNCTION IN TRANSCRIPTIONAL REPRESSION, AND INTERACTION WITH PNN.
RX   PubMed=15542832; DOI=10.1128/MCB.24.23.10223-10235.2004;
RA   Alpatov R., Munguba G.C., Caton P., Joo J.H., Shi Y., Shi Y.,
RA   Hunt M.E., Sugrue S.P.;
RT   "Nuclear speckle-associated protein Pnn/DRS binds to the
RT   transcriptional corepressor CtBP and relieves CtBP-mediated repression
RT   of the E-cadherin gene.";
RL   Mol. Cell. Biol. 24:10223-10235(2004).
RN   [14]
RP   INTERACTION WITH NRIP1.
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   [15]
RP   INTERACTION WITH ZFHX1B.
RX   PubMed=16061479; DOI=10.1074/jbc.M504477200;
RA   Long J., Zuo D., Park M.;
RT   "Pc2-mediated sumoylation of Smad-interacting protein 1 attenuates
RT   transcriptional repression of E-cadherin.";
RL   J. Biol. Chem. 280:35477-35489(2005).
RN   [16]
RP   INTERACTION WITH MECOM.
RX   PubMed=15897867; DOI=10.1038/sj.onc.1208754;
RA   Nitta E., Izutsu K., Yamaguchi Y., Imai Y., Ogawa S., Chiba S.,
RA   Kurokawa M., Hirai H.;
RT   "Oligomerization of Evi-1 regulated by the PR domain contributes to
RT   recruitment of corepressor CtBP.";
RL   Oncogene 24:6165-6173(2005).
RN   [17]
RP   INTERACTION WITH FOXP1.
RX   PubMed=16609867; DOI=10.1007/s00427-006-0073-8;
RA   Schoen C., Wochnik A., Roessner A., Donow C., Knoechel W.;
RT   "The FoxP subclass in Xenopus laevis development.";
RL   Dev. Genes Evol. 216:641-646(2006).
RN   [18]
RP   INTERACTION WITH WIZ.
RX   PubMed=16702210; DOI=10.1074/jbc.M603087200;
RA   Ueda J., Tachibana M., Ikura T., Shinkai Y.;
RT   "Zinc finger protein Wiz links G9a/GLP histone methyltransferases to
RT   the co-repressor molecule CtBP.";
RL   J. Biol. Chem. 281:20120-20128(2006).
RN   [19]
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   [20]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-300, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic kidney;
RX   PubMed=17525332; DOI=10.1126/science.1140321;
RA   Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
RA   Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
RA   Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
RT   "ATM and ATR substrate analysis reveals extensive protein networks
RT   responsive to DNA damage.";
RL   Science 316:1160-1166(2007).
RN   [21]
RP   FUNCTION AS COREPRESSOR, INTERACTION WITH BCL6, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=18212045; DOI=10.1128/MCB.01400-07;
RA   Mendez L.M., Polo J.M., Yu J.J., Krupski M., Ding B.B., Melnick A.,
RA   Ye B.H.;
RT   "CtBP is an essential corepressor for BCL6 autoregulation.";
RL   Mol. Cell. Biol. 28:2175-2186(2008).
RN   [22]
RP   FUNCTION, AND INTERACTION WITH SATB1.
RX   PubMed=19103759; DOI=10.1128/MCB.00822-08;
RA   Purbey P.K., Singh S., Notani D., Kumar P.P., Limaye A.S., Galande S.;
RT   "Acetylation-dependent interaction of SATB1 and CtBP1 mediates
RT   transcriptional repression by SATB1.";
RL   Mol. Cell. Biol. 29:1321-1337(2009).
RN   [23]
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   [24]
RP   INTERACTION WITH HADV5 E1A.
RX   PubMed=23747199; DOI=10.1016/j.virol.2013.05.018;
RA   Subramanian T., Zhao L.J., Chinnadurai G.;
RT   "Interaction of CtBP with adenovirus E1A suppresses immortalization of
RT   primary epithelial cells and enhances virus replication during
RT   productive infection.";
RL   Virology 443:313-320(2013).
RN   [25]
RP   INTERACTION WITH FAM195B.
RX   PubMed=25728771; DOI=10.1016/j.molcel.2015.01.023;
RA   Ichikawa K., Kubota Y., Nakamura T., Weng J.S., Tomida T., Saito H.,
RA   Takekawa M.;
RT   "MCRIP1, an ERK substrate, mediates ERK-induced gene silencing during
RT   epithelial-mesenchymal transition by regulating the co-repressor
RT   CtBP.";
RL   Mol. Cell 58:35-46(2015).
RN   [26]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
RA   Wang L., Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human
RT   liver phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [27]
RP   X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 28-353 IN COMPLEX WITH NAD,
RP   FUNCTION, COFACTOR, MUTAGENESIS OF CYS-134; ASN-138; ARG-141;
RP   141-ARG-ARG-142; LEU-150; ARG-163; ARG-171; GLY-181; GLY-183; ASP-204;
RP   ARG-266; ASP-290; GLU-295 AND HIS-315, AND DIMERIZATION.
RX   PubMed=12419229; DOI=10.1016/S1097-2765(02)00650-0;
RA   Kumar V., Carlson J.E., Ohgi K.A., Edwards T.A., Rose D.W.,
RA   Escalante C.R., Rosenfeld M.G., Aggarwal A.K.;
RT   "Transcription corepressor CtBP is an NAD(+)-regulated
RT   dehydrogenase.";
RL   Mol. Cell 10:857-869(2002).
CC   -!- FUNCTION: Corepressor targeting diverse transcription regulators
CC       such as GLIS2 or BCL6. Has dehydrogenase activity. Involved in
CC       controlling the equilibrium between tubular and stacked structures
CC       in the Golgi complex. Functions in brown adipose tissue (BAT)
CC       differentiation. {ECO:0000269|PubMed:12419229,
CC       ECO:0000269|PubMed:15542832, ECO:0000269|PubMed:18212045,
CC       ECO:0000269|PubMed:19103759, ECO:0000269|PubMed:9858600}.
CC   -!- COFACTOR:
CC       Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC         Evidence={ECO:0000269|PubMed:12419229};
CC       Note=NAD is required for efficient interaction with E1A. Cofactor
CC       binding induces a conformation change.
CC       {ECO:0000269|PubMed:12419229};
CC   -!- SUBUNIT: Homo- or heterodimer. Heterodimer with CTBP2. Interacts
CC       with PRDM16; the interaction represses white adipose tissue (WAT)-
CC       specific genes expression. Interacts with GLIS2, FOXP2, HDAC4,
CC       HDAC5, HDAC9 and ZNF217. Interacts with adenovirus E1A protein
CC       (via its C-terminus); the interaction disrupts the interaction of
CC       CTBP1 with RBBP8. Interacts with Epstein-Barr virus EBNA3 and
CC       EBNA6. Interacts with ELK3 (via its PXDLS motif). Interacts with
CC       RBBP8 (via its PXDLS motif); the interaction is disrupted by
CC       binding to adenovirus E1A. Interacts with FOXP1, HIPK2, PNN,
CC       NRIP1, MECOM, ZNF366, ZFHX1B and WIZ. Interaction with SATB1 (non-
CC       acetylated form); the interaction stabilizes its attachment to DNA
CC       and promotes transcription repression. Interacts with BCL6; the
CC       interaction is required for BCL6 transcriptional autoinhibition
CC       and inhibition of some BCL6 target genes. Interacts with IKZF4 (By
CC       similarity). Interacts with human adenovirus 5 E1A protein; this
CC       interaction seems to potentiate viral replication
CC       (PubMed:23747199). Interacts with FAM195B (unphosphorylated form,
CC       via the PXDLS motif); competitively inhibiting CTBP-ZEB1
CC       interaction (PubMed:25728771). {ECO:0000250|UniProtKB:O88712,
CC       ECO:0000269|PubMed:11462050, ECO:0000269|PubMed:11509661,
CC       ECO:0000269|PubMed:11568182, ECO:0000269|PubMed:12372828,
CC       ECO:0000269|PubMed:12419229, ECO:0000269|PubMed:14567915,
CC       ECO:0000269|PubMed:15060175, ECO:0000269|PubMed:15542832,
CC       ECO:0000269|PubMed:15897867, ECO:0000269|PubMed:16061479,
CC       ECO:0000269|PubMed:16609867, ECO:0000269|PubMed:16702210,
CC       ECO:0000269|PubMed:17085477, ECO:0000269|PubMed:18212045,
CC       ECO:0000269|PubMed:19103759, ECO:0000269|PubMed:23747199,
CC       ECO:0000269|PubMed:25728771, ECO:0000269|PubMed:7479821,
CC       ECO:0000269|PubMed:8440238}.
CC   -!- INTERACTION:
CC       Q9H6U6:BCAS3; NbExp=3; IntAct=EBI-10171858, EBI-6083685;
CC       Q76N32:CEP68; NbExp=3; IntAct=EBI-10171858, EBI-9051024;
CC       Q49AN0:CRY2; NbExp=3; IntAct=EBI-10171858, EBI-2212355;
CC       P56545:CTBP2; NbExp=3; IntAct=EBI-10171858, EBI-741533;
CC       Q8IY44:CTBP2; NbExp=3; IntAct=EBI-10171858, EBI-10171902;
CC       I6L9A0:DMRTB1; NbExp=3; IntAct=EBI-10171858, EBI-10178554;
CC       O15409:FOXP2; NbExp=3; IntAct=EBI-10171858, EBI-983612;
CC       Q9BXL5:HEMGN; NbExp=2; IntAct=EBI-908846, EBI-3916399;
CC       Q14526:HIC1; NbExp=4; IntAct=EBI-908846, EBI-2507362;
CC       P09067:HOXB5; NbExp=3; IntAct=EBI-10171858, EBI-3893317;
CC       Q13422:IKZF1; NbExp=3; IntAct=EBI-10171858, EBI-745305;
CC       Q9Y4X4:KLF12; NbExp=3; IntAct=EBI-10171858, EBI-750750;
CC       O43474:KLF4; NbExp=4; IntAct=EBI-908846, EBI-7232405;
CC       P45984:MAPK9; NbExp=3; IntAct=EBI-10171858, EBI-713568;
CC       O94818-2:NOL4; NbExp=3; IntAct=EBI-10171858, EBI-10190763;
CC       Q96MY1:NOL4L; NbExp=3; IntAct=EBI-10171858, EBI-6660790;
CC       Q9NQ66:PLCB1; NbExp=3; IntAct=EBI-10171858, EBI-3396023;
CC       Q13131:PRKAA1; NbExp=3; IntAct=EBI-10171858, EBI-1181405;
CC       Q15583:TGIF1; NbExp=3; IntAct=EBI-10171858, EBI-714215;
CC       Q96EK4:THAP11; NbExp=2; IntAct=EBI-908846, EBI-1790529;
CC       A1L0U7:TSHZ3; NbExp=3; IntAct=EBI-10171858, EBI-10171826;
CC       A2APF7:Zbp1 (xeno); NbExp=2; IntAct=EBI-908846, EBI-6115394;
CC       Q8N895:ZNF366; NbExp=5; IntAct=EBI-908846, EBI-2813661;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12679040}.
CC       Nucleus {ECO:0000269|PubMed:12679040}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q13363-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q13363-2; Sequence=VSP_043305;
CC         Note=No experimental confirmation available.;
CC   -!- TISSUE SPECIFICITY: Expressed in germinal center B-cells.
CC       {ECO:0000269|PubMed:18212045}.
CC   -!- PTM: The level of phosphorylation appears to be regulated during
CC       the cell cycle. Phosphorylation by HIPK2 on Ser-422 induces
CC       proteasomal degradation. {ECO:0000269|PubMed:14567915,
CC       ECO:0000269|PubMed:8440238}.
CC   -!- PTM: ADP-ribosylated; when cells are exposed to brefeldin A.
CC       {ECO:0000250}.
CC   -!- PTM: Sumoylation on Lys-428 is promoted by the E3 SUMO-protein
CC       ligase CBX4. {ECO:0000269|PubMed:12679040}.
CC   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. {ECO:0000305}.
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DR   EMBL; U37408; AAC62822.1; -; mRNA.
DR   EMBL; AF091555; AAD14597.1; -; mRNA.
DR   EMBL; AC092535; AAY40989.1; -; Genomic_DNA.
DR   EMBL; CH471131; EAW82599.1; -; Genomic_DNA.
DR   EMBL; CH471131; EAW82600.1; -; Genomic_DNA.
DR   EMBL; CH471131; EAW82601.1; -; Genomic_DNA.
DR   EMBL; BC011655; AAH11655.1; -; mRNA.
DR   EMBL; BC053320; AAH53320.1; -; mRNA.
DR   CCDS; CCDS3348.1; -. [Q13363-1]
DR   CCDS; CCDS43203.1; -. [Q13363-2]
DR   RefSeq; NP_001012632.1; NM_001012614.1. [Q13363-2]
DR   RefSeq; NP_001319.1; NM_001328.2. [Q13363-1]
DR   UniGene; Hs.208597; -.
DR   PDB; 1MX3; X-ray; 1.95 A; A=28-353.
DR   PDB; 4LCE; X-ray; 2.38 A; A=28-353.
DR   PDB; 4U6Q; X-ray; 2.30 A; A=28-353.
DR   PDB; 4U6S; X-ray; 2.10 A; A=28-353.
DR   PDBsum; 1MX3; -.
DR   PDBsum; 4LCE; -.
DR   PDBsum; 4U6Q; -.
DR   PDBsum; 4U6S; -.
DR   ProteinModelPortal; Q13363; -.
DR   SMR; Q13363; 28-352.
DR   BioGrid; 107869; 137.
DR   DIP; DIP-24245N; -.
DR   IntAct; Q13363; 40.
DR   MINT; MINT-94454; -.
DR   STRING; 9606.ENSP00000290921; -.
DR   PhosphoSite; Q13363; -.
DR   BioMuta; CTBP1; -.
DR   DMDM; 6014741; -.
DR   MaxQB; Q13363; -.
DR   PaxDb; Q13363; -.
DR   PRIDE; Q13363; -.
DR   DNASU; 1487; -.
DR   Ensembl; ENST00000290921; ENSP00000290921; ENSG00000159692. [Q13363-1]
DR   Ensembl; ENST00000382952; ENSP00000372411; ENSG00000159692. [Q13363-2]
DR   GeneID; 1487; -.
DR   KEGG; hsa:1487; -.
DR   UCSC; uc003gcu.1; human. [Q13363-2]
DR   UCSC; uc003gcv.1; human. [Q13363-1]
DR   CTD; 1487; -.
DR   GeneCards; CTBP1; -.
DR   HGNC; HGNC:2494; CTBP1.
DR   HPA; CAB004217; -.
DR   HPA; HPA018987; -.
DR   HPA; HPA044971; -.
DR   MIM; 602618; gene.
DR   neXtProt; NX_Q13363; -.
DR   PharmGKB; PA26995; -.
DR   eggNOG; KOG0067; Eukaryota.
DR   eggNOG; COG0111; LUCA.
DR   GeneTree; ENSGT00530000063021; -.
DR   HOGENOM; HOG000136701; -.
DR   HOVERGEN; HBG001898; -.
DR   InParanoid; Q13363; -.
DR   KO; K04496; -.
DR   OMA; DRDHPSD; -.
DR   OrthoDB; EOG761BT9; -.
DR   PhylomeDB; Q13363; -.
DR   TreeFam; TF313593; -.
DR   Reactome; R-HSA-3769402; deactivation of the beta-catenin transactivating complex.
DR   Reactome; R-HSA-4641265; repression of WNT target genes.
DR   Reactome; R-HSA-5339700; TCF7L2 mutants don't bind CTBP.
DR   SignaLink; Q13363; -.
DR   ChiTaRS; CTBP1; human.
DR   EvolutionaryTrace; Q13363; -.
DR   GeneWiki; CTBP1; -.
DR   GenomeRNAi; 1487; -.
DR   NextBio; 6105; -.
DR   PRO; PR:Q13363; -.
DR   Proteomes; UP000005640; Chromosome 4.
DR   Bgee; Q13363; -.
DR   CleanEx; HS_CTBP1; -.
DR   ExpressionAtlas; Q13363; baseline and differential.
DR   Genevisible; Q13363; HS.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0005667; C:transcription factor complex; IEA:Ensembl.
DR   GO; GO:0017053; C:transcriptional repressor complex; ISS:UniProtKB.
DR   GO; GO:0051287; F:NAD binding; ISS:UniProtKB.
DR   GO; GO:0070404; F:NADH binding; IBA:GO_Central.
DR   GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IBA:GO_Central.
DR   GO; GO:0008022; F:protein C-terminus binding; TAS:ProtInc.
DR   GO; GO:0019904; F:protein domain specific binding; IPI:UniProtKB.
DR   GO; GO:0042803; F:protein homodimerization activity; IBA:GO_Central.
DR   GO; GO:0070491; F:repressing transcription factor binding; IPI:BHF-UCL.
DR   GO; GO:0001106; F:RNA polymerase II transcription corepressor activity; IDA:BHF-UCL.
DR   GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IEA:Ensembl.
DR   GO; GO:0008134; F:transcription factor binding; IPI:UniProtKB.
DR   GO; GO:0008285; P:negative regulation of cell proliferation; TAS:ProtInc.
DR   GO; GO:0035067; P:negative regulation of histone acetylation; IMP:BHF-UCL.
DR   GO; GO:0090241; P:negative regulation of histone H4 acetylation; IMP:BHF-UCL.
DR   GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IMP:BHF-UCL.
DR   GO; GO:1903758; P:negative regulation of transcription from RNA polymerase II promoter by histone modification; IMP:BHF-UCL.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR   GO; GO:0031065; P:positive regulation of histone deacetylation; IMP:BHF-UCL.
DR   GO; GO:0006468; P:protein phosphorylation; TAS:ProtInc.
DR   GO; GO:0051726; P:regulation of cell cycle; IMP:BHF-UCL.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
DR   GO; GO:0019079; P:viral genome replication; TAS:ProtInc.
DR   GO; GO:0050872; P:white fat cell differentiation; ISS:UniProtKB.
DR   InterPro; IPR006139; D-isomer_2_OHA_DH_cat_dom.
DR   InterPro; IPR029753; D-isomer_DH_CS.
DR   InterPro; IPR029752; D-isomer_DH_CS1.
DR   InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   Pfam; PF00389; 2-Hacid_dh; 1.
DR   Pfam; PF02826; 2-Hacid_dh_C; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   PROSITE; PS00065; D_2_HYDROXYACID_DH_1; 1.
DR   PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE   1: Evidence at protein level;
KW   3D-structure; ADP-ribosylation; Alternative splicing;
KW   Complete proteome; Cytoplasm; Differentiation;
KW   Direct protein sequencing; Host-virus interaction; Isopeptide bond;
KW   NAD; Nucleus; Oxidoreductase; Phosphoprotein; Reference proteome;
KW   Repressor; Transcription; Transcription regulation; Ubl conjugation.
FT   CHAIN         1    440       C-terminal-binding protein 1.
FT                                /FTId=PRO_0000076041.
FT   NP_BIND     180    185       NAD. {ECO:0000250}.
FT   NP_BIND     237    243       NAD. {ECO:0000250}.
FT   NP_BIND     264    266       NAD. {ECO:0000250}.
FT   NP_BIND     315    318       NAD. {ECO:0000250}.
FT   REGION        1     70       Interaction with GLIS2 1. {ECO:0000250}.
FT   REGION      288    360       Interaction with GLIS2 2. {ECO:0000250}.
FT   ACT_SITE    266    266       {ECO:0000250}.
FT   ACT_SITE    295    295       {ECO:0000250}.
FT   ACT_SITE    315    315       Proton donor. {ECO:0000250}.
FT   BINDING     100    100       NAD. {ECO:0000250}.
FT   BINDING     204    204       NAD. {ECO:0000250}.
FT   BINDING     290    290       NAD. {ECO:0000250}.
FT   MOD_RES     300    300       Phosphoserine.
FT                                {ECO:0000244|PubMed:17525332}.
FT   MOD_RES     422    422       Phosphoserine; by HIPK2.
FT                                {ECO:0000269|PubMed:14567915}.
FT   CROSSLNK    428    428       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO).
FT   VAR_SEQ       1     13       MGSSHLLNKGLPL -> MS (in isoform 2).
FT                                {ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_043305.
FT   MUTAGEN     134    134       C->A: Strongly reduces E1A binding; when
FT                                associated with A-138; A-141 and A-150.
FT                                {ECO:0000269|PubMed:12419229}.
FT   MUTAGEN     138    138       N->A: Strongly reduces E1A binding; when
FT                                associated with A-134; A-141 and A-150.
FT                                {ECO:0000269|PubMed:12419229}.
FT   MUTAGEN     141    142       RR->AA: Strongly reduces E1A binding;
FT                                when associated with A-163 and A-171.
FT                                {ECO:0000269|PubMed:12419229}.
FT   MUTAGEN     141    141       R->A: Strongly reduces E1A binding; when
FT                                associated with A-134; A-138 and A-150.
FT                                {ECO:0000269|PubMed:12419229}.
FT   MUTAGEN     150    150       L->A: Strongly reduces E1A binding; when
FT                                associated with A-134; A-138 and A-141.
FT                                {ECO:0000269|PubMed:12419229}.
FT   MUTAGEN     163    163       R->A: Strongly reduces E1A binding; when
FT                                associated with A-141; A-142 and A-171.
FT                                {ECO:0000269|PubMed:12419229}.
FT   MUTAGEN     171    171       R->A: Strongly reduces E1A binding; when
FT                                associated with A-141; A-142 and A-163.
FT                                {ECO:0000269|PubMed:12419229}.
FT   MUTAGEN     181    181       G->V: Strongly reduces E1A binding; when
FT                                associated with V-183 and A-204.
FT                                {ECO:0000269|PubMed:12419229}.
FT   MUTAGEN     183    183       G->V: Strongly reduces E1A binding; when
FT                                associated with V-181 and A-204.
FT                                {ECO:0000269|PubMed:12419229}.
FT   MUTAGEN     204    204       D->A: Strongly reduces E1A binding; when
FT                                associated with V-181 and V-183.
FT                                {ECO:0000269|PubMed:12419229}.
FT   MUTAGEN     266    266       R->A: Strongly reduces E1A binding; when
FT                                associated with A-290; A-295 and A-315.
FT                                {ECO:0000269|PubMed:12419229}.
FT   MUTAGEN     290    290       D->A: Strongly reduces E1A binding; when
FT                                associated with A-266; A-295 and A-315.
FT                                {ECO:0000269|PubMed:12419229}.
FT   MUTAGEN     295    295       E->A: Strongly reduces E1A binding; when
FT                                associated with A-266; A-290 and A-315.
FT                                {ECO:0000269|PubMed:12419229}.
FT   MUTAGEN     315    315       H->A: Strongly reduces E1A binding; when
FT                                associated with A-266; A-290 and A-295.
FT                                {ECO:0000269|PubMed:12419229}.
FT   MUTAGEN     422    422       S->A: Abolishes phosphorylation by HIPK2
FT                                and prevents UV-induced clearance.
FT                                {ECO:0000269|PubMed:14567915}.
FT   STRAND       29     34       {ECO:0000244|PDB:1MX3}.
FT   TURN         39     41       {ECO:0000244|PDB:1MX3}.
FT   HELIX        42     45       {ECO:0000244|PDB:1MX3}.
FT   TURN         46     48       {ECO:0000244|PDB:1MX3}.
FT   STRAND       50     53       {ECO:0000244|PDB:1MX3}.
FT   HELIX        59     61       {ECO:0000244|PDB:1MX3}.
FT   HELIX        64     69       {ECO:0000244|PDB:1MX3}.
FT   STRAND       70     75       {ECO:0000244|PDB:1MX3}.
FT   STRAND       77     79       {ECO:0000244|PDB:1MX3}.
FT   HELIX        83     86       {ECO:0000244|PDB:1MX3}.
FT   STRAND       94    100       {ECO:0000244|PDB:1MX3}.
FT   HELIX       107    112       {ECO:0000244|PDB:1MX3}.
FT   STRAND      116    118       {ECO:0000244|PDB:1MX3}.
FT   TURN        121    124       {ECO:0000244|PDB:4U6S}.
FT   HELIX       125    141       {ECO:0000244|PDB:1MX3}.
FT   HELIX       143    151       {ECO:0000244|PDB:1MX3}.
FT   HELIX       159    165       {ECO:0000244|PDB:1MX3}.
FT   TURN        166    168       {ECO:0000244|PDB:1MX3}.
FT   STRAND      176    180       {ECO:0000244|PDB:1MX3}.
FT   HELIX       184    194       {ECO:0000244|PDB:1MX3}.
FT   TURN        195    197       {ECO:0000244|PDB:1MX3}.
FT   STRAND      199    203       {ECO:0000244|PDB:1MX3}.
FT   HELIX       211    215       {ECO:0000244|PDB:1MX3}.
FT   HELIX       223    229       {ECO:0000244|PDB:1MX3}.
FT   STRAND      231    235       {ECO:0000244|PDB:1MX3}.
FT   STRAND      246    248       {ECO:0000244|PDB:1MX3}.
FT   HELIX       249    252       {ECO:0000244|PDB:1MX3}.
FT   STRAND      259    263       {ECO:0000244|PDB:1MX3}.
FT   HELIX       267    269       {ECO:0000244|PDB:4U6S}.
FT   HELIX       272    280       {ECO:0000244|PDB:1MX3}.
FT   STRAND      283    290       {ECO:0000244|PDB:1MX3}.
FT   STRAND      293    296       {ECO:0000244|PDB:1MX3}.
FT   TURN        303    306       {ECO:0000244|PDB:1MX3}.
FT   STRAND      308    312       {ECO:0000244|PDB:1MX3}.
FT   HELIX       321    340       {ECO:0000244|PDB:1MX3}.
FT   TURN        343    346       {ECO:0000244|PDB:1MX3}.
FT   STRAND      348    350       {ECO:0000244|PDB:1MX3}.
SQ   SEQUENCE   440 AA;  47535 MW;  F071DD30B385603F CRC64;
     MGSSHLLNKG LPLGVRPPIM NGPLHPRPLV ALLDGRDCTV EMPILKDVAT VAFCDAQSTQ
     EIHEKVLNEA VGALMYHTIT LTREDLEKFK ALRIIVRIGS GFDNIDIKSA GDLGIAVCNV
     PAASVEETAD STLCHILNLY RRATWLHQAL REGTRVQSVE QIREVASGAA RIRGETLGII
     GLGRVGQAVA LRAKAFGFNV LFYDPYLSDG VERALGLQRV STLQDLLFHS DCVTLHCGLN
     EHNHHLINDF TVKQMRQGAF LVNTARGGLV DEKALAQALK EGRIRGAALD VHESEPFSFS
     QGPLKDAPNL ICTPHAAWYS EQASIEMREE AAREIRRAIT GRIPDSLKNC VNKDHLTAAT
     HWASMDPAVV HPELNGAAYR YPPGVVGVAP TGIPAAVEGI VPSAMSLSHG LPPVAHPPHA
     PSPGQTVKPE ADRDHASDQL
//
ID   CTNA1_HUMAN             Reviewed;         906 AA.
AC   P35221; Q12795; Q8N1C0;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   11-NOV-2015, entry version 166.
DE   RecName: Full=Catenin alpha-1;
DE   AltName: Full=Alpha E-catenin;
DE   AltName: Full=Cadherin-associated protein;
DE   AltName: Full=Renal carcinoma antigen NY-REN-13;
GN   Name=CTNNA1;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
RX   PubMed=8404069;
RA   Furukawa Y., Nakatsuru S., Nagafuchi A., Tsukita S., Muto T.,
RA   Nakamura Y., Horii A.;
RT   "Structure, expression and chromosome assignment of the human catenin
RT   (cadherin-associated protein) alpha 1 gene (CTNNA1).";
RL   Cytogenet. Cell Genet. 65:74-78(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Colon, and Lung;
RX   PubMed=8323564; DOI=10.1006/bbrc.1993.1710;
RA   Oda T., Kanai Y., Shimoyama Y., Nagafuchi A., Tsukita S.,
RA   Hirohashi S.;
RT   "Cloning of the human alpha-catenin cDNA and its aberrant mRNA in a
RT   human cancer cell line.";
RL   Biochem. Biophys. Res. Commun. 193:897-904(1993).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Colon;
RX   PubMed=7945318; DOI=10.1006/bbrc.1994.2381;
RA   Rimm D.L., Kebriaei P., Morrow J.S.;
RT   "Molecular cloning reveals alternative splice forms of human alpha(E)-
RT   catenin.";
RL   Biochem. Biophys. Res. Commun. 203:1691-1699(1994).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), ALTERNATIVE SPLICING, AND
RP   SUBCELLULAR LOCATION (ISOFORM 3).
RC   TISSUE=Hippocampus;
RX   PubMed=21708131; DOI=10.1016/j.bbrc.2011.06.085;
RA   Kask M., Pruunsild P., Timmusk T.;
RT   "Bidirectional transcription from human LRRTM2/CTNNA1 and
RT   LRRTM1/CTNNA2 gene loci leads to expression of N-terminally truncated
RT   CTNNA1 and CTNNA2 isoforms.";
RL   Biochem. Biophys. Res. Commun. 411:56-61(2011).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Nollet F.H., Vanpoucke G.G., van Roy F.M.;
RT   "Genomic organization of the human alphaE-catenin gene (CTNNA1).";
RL   Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS VAL-179 AND SER-219.
RG   NIEHS SNPs program;
RL   Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15372022; DOI=10.1038/nature02919;
RA   Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA   Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA   She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA   Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA   Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T.,
RA   Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M.,
RA   Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K.,
RA   Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C.,
RA   Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M.,
RA   Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A.,
RA   Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M.,
RA   Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M.,
RA   Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S.,
RA   Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT   "The DNA sequence and comparative analysis of human chromosome 5.";
RL   Nature 431:268-274(2004).
RN   [8]
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   [9]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC   TISSUE=Brain, and 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   [10]
RP   PROTEIN SEQUENCE OF 2-12; 166-178 AND 617-623, CLEAVAGE OF INITIATOR
RP   METHIONINE, ACETYLATION AT THR-2, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RC   TISSUE=Colon carcinoma;
RA   Bienvenut W.V., Zebisch A., Kolch W.;
RL   Submitted (DEC-2008) to UniProtKB.
RN   [11]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 159-250.
RC   TISSUE=Prostate;
RX   PubMed=8188230; DOI=10.1006/geno.1994.1042;
RA   McPherson J.D., Morton R.A., Ewing C.M., Wasmuth J.J., Overhauser J.,
RA   Nagafuchi A., Tsukita S., Isaacs W.B.;
RT   "Assignment of the human alpha-catenin gene (CTNNA1) to chromosome
RT   5q21-q22.";
RL   Genomics 19:188-190(1994).
RN   [12]
RP   IDENTIFICATION IN AN E-CADHERIN/CATENIN ADHESION COMPLEX.
RX   PubMed=7982500; DOI=10.1016/0014-5793(94)01205-9;
RA   Butz S., Kemler R.;
RT   "Distinct cadherin-catenin complexes in Ca(2+)-dependent cell-cell
RT   adhesion.";
RL   FEBS Lett. 355:195-200(1994).
RN   [13]
RP   SUBUNIT, AND INTERACTION WITH CTNNB1.
RX   PubMed=9341178; DOI=10.1074/jbc.272.43.27301;
RA   Koslov E.R., Maupin P., Pradhan D., Morrow J.S., Rimm D.L.;
RT   "Alpha-catenin can form asymmetric homodimeric complexes and/or
RT   heterodimeric complexes with beta-catenin.";
RL   J. Biol. Chem. 272:27301-27306(1997).
RN   [14]
RP   INTERACTION WITH JUP; CTNNB1 AND ALPHA-ACTININ.
RX   PubMed=9152027;
RA   Nieset J.E., Redfield A.R., Jin F., Knudsen K.A., Johnson K.R.,
RA   Wheelock M.J.;
RT   "Characterization of the interactions of alpha-catenin with alpha-
RT   actinin and beta-catenin/plakoglobin.";
RL   J. Cell Sci. 110:1013-1022(1997).
RN   [15]
RP   IDENTIFICATION AS A RENAL CANCER ANTIGEN.
RC   TISSUE=Renal cell carcinoma;
RX   PubMed=10508479;
RX   DOI=10.1002/(SICI)1097-0215(19991112)83:4<456::AID-IJC4>3.0.CO;2-5;
RA   Scanlan M.J., Gordan J.D., Williamson B., Stockert E., Bander N.H.,
RA   Jongeneel C.V., Gure A.O., Jaeger D., Jaeger E., Knuth A., Chen Y.-T.,
RA   Old L.J.;
RT   "Antigens recognized by autologous antibody in patients with renal-
RT   cell carcinoma.";
RL   Int. J. Cancer 83:456-464(1999).
RN   [16]
RP   INTERACTION WITH AJUBA.
RX   PubMed=12417594; DOI=10.1074/jbc.M205391200;
RA   Marie H., Pratt S.J., Betson M., Epple H., Kittler J.T., Meek L.,
RA   Moss S.J., Troyanovsky S., Attwell D., Longmore G.D., Braga V.M.;
RT   "The LIM protein Ajuba is recruited to cadherin-dependent cell
RT   junctions through an association with alpha-catenin.";
RL   J. Biol. Chem. 278:1220-1228(2003).
RN   [17]
RP   SUMOYLATION.
RX   PubMed=15561718; DOI=10.1074/jbc.M411718200;
RA   Gocke C.B., Yu H., Kang J.;
RT   "Systematic identification and analysis of mammalian small ubiquitin-
RT   like modifier substrates.";
RL   J. Biol. Chem. 280:5004-5012(2005).
RN   [18]
RP   INTERACTION WITH ARHGAP21.
RX   PubMed=16184169; DOI=10.1038/ncb1308;
RA   Sousa S., Cabanes D., Archambaud C., Colland F., Lemichez E.,
RA   Popoff M., Boisson-Dupuis S., Gouin E., Lecuit M., Legrain P.,
RA   Cossart P.;
RT   "ARHGAP10 is necessary for alpha-catenin recruitment at adherens
RT   junctions and for Listeria invasion.";
RL   Nat. Cell Biol. 7:954-960(2005).
RN   [19]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-641, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA   Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA   Mann M.;
RT   "Global, in vivo, and site-specific phosphorylation dynamics in
RT   signaling networks.";
RL   Cell 127:635-648(2006).
RN   [20]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=16964243; DOI=10.1038/nbt1240;
RA   Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT   "A probability-based approach for high-throughput protein
RT   phosphorylation analysis and site localization.";
RL   Nat. Biotechnol. 24:1285-1292(2006).
RN   [21]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-641, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Pituitary;
RX   PubMed=16807684; DOI=10.1007/s11102-006-8916-x;
RA   Beranova-Giorgianni S., Zhao Y., Desiderio D.M., Giorgianni F.;
RT   "Phosphoproteomic analysis of the human pituitary.";
RL   Pituitary 9:109-120(2006).
RN   [22]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-652, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Prostate cancer;
RX   PubMed=17487921; DOI=10.1002/elps.200600782;
RA   Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.;
RT   "Toward a global characterization of the phosphoproteome in prostate
RT   cancer cells: identification of phosphoproteins in the LNCaP cell
RT   line.";
RL   Electrophoresis 28:2027-2034(2007).
RN   [23]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-641, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18220336; DOI=10.1021/pr0705441;
RA   Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
RA   Yates J.R. III;
RT   "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
RT   efficient phosphoproteomic analysis.";
RL   J. Proteome Res. 7:1346-1351(2008).
RN   [24]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-641 AND SER-652, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [25]
RP   INTERACTION WITH LIMA1.
RX   PubMed=18093941; DOI=10.1073/pnas.0710504105;
RA   Abe K., Takeichi M.;
RT   "EPLIN mediates linkage of the cadherin catenin complex to F-actin and
RT   stabilizes the circumferential actin belt.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:13-19(2008).
RN   [26]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-641 AND THR-645, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=18318008; DOI=10.1002/pmic.200700884;
RA   Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
RA   Zou H., Gu J.;
RT   "Large-scale phosphoproteome analysis of human liver tissue by
RT   enrichment and fractionation of phosphopeptides with strong anion
RT   exchange chromatography.";
RL   Proteomics 8:1346-1361(2008).
RN   [27]
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   [28]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-641, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
RA   Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA   Mann M., Daub H.;
RT   "Large-scale proteomics analysis of the human kinome.";
RL   Mol. Cell. Proteomics 8:1751-1764(2009).
RN   [29]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-641, 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   [30]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-641, 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   [31]
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   [32]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-634; SER-641 AND
RP   SER-652, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   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   [33]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-264; SER-268; SER-295;
RP   SER-297; THR-634; SER-641 AND SER-851, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
RA   Wang L., Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human
RT   liver phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [34]
RP   X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 377-632, PARTIAL PROTEIN
RP   SEQUENCE, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=11447106; DOI=10.1093/emboj/20.14.3645;
RA   Yang J., Dokurno P., Tonks N.K., Barford D.;
RT   "Crystal structure of the M-fragment of alpha-catenin: implications
RT   for modulation of cell adhesion.";
RL   EMBO J. 20:3645-3656(2001).
RN   [35]
RP   POSSIBLE INVOLVEMENT IN HDGC.
RX   PubMed=23208944; DOI=10.1002/path.4152;
RA   Majewski I.J., Kluijt I., Cats A., Scerri T.S., de Jong D.,
RA   Kluin R.J., Hansford S., Hogervorst F.B., Bosma A.J., Hofland I.,
RA   Winter M., Huntsman D., Jonkers J., Bahlo M., Bernards R.;
RT   "An alpha-E-catenin (CTNNA1) mutation in hereditary diffuse gastric
RT   cancer.";
RL   J. Pathol. 229:621-629(2013).
CC   -!- FUNCTION: Associates with the cytoplasmic domain of a variety of
CC       cadherins. The association of catenins to cadherins produces a
CC       complex which is linked to the actin filament network, and which
CC       seems to be of primary importance for cadherins cell-adhesion
CC       properties. Can associate with both E- and N-cadherins. Originally
CC       believed to be a stable component of E-cadherin/catenin adhesion
CC       complexes and to mediate the linkage of cadherins to the actin
CC       cytoskeleton at adherens junctions. In contrast, cortical actin
CC       was found to be much more dynamic than E-cadherin/catenin
CC       complexes and CTNNA1 was shown not to bind to F-actin when
CC       assembled in the complex suggesting a different linkage between
CC       actin and adherens junctions components. The homodimeric form may
CC       regulate actin filament assembly and inhibit actin branching by
CC       competing with the Arp2/3 complex for binding to actin filaments.
CC       May play a crucial role in cell differentiation.
CC   -!- SUBUNIT: Monomer and homodimer; the monomer preferentially binds
CC       to CTNNB1 and the homodimer to actin. Binds MLLT4 and F-actin.
CC       Possible component of an E-cadherin/ catenin adhesion complex
CC       together with E-cadherin/CDH1 and beta-catenin/CTNNB1 or gamma-
CC       catenin/JUP; the complex is located to adherens junctions. The
CC       stable association of CTNNA1 is controversial as CTNNA1 was shown
CC       not to bind to F-actin when assembled in the complex.
CC       Alternatively, the CTNNA1-containing complex may be linked to F-
CC       actin by other proteins such as LIMA1. Interacts with ARHGAP21 and
CC       with AJUBA. Interacts with LIMA1 (By similarity). {ECO:0000250}.
CC   -!- INTERACTION:
CC       P25054:APC; NbExp=2; IntAct=EBI-701918, EBI-727707;
CC       P32121:ARRB2; NbExp=3; IntAct=EBI-701918, EBI-714559;
CC       P00533:EGFR; NbExp=4; IntAct=EBI-701918, EBI-297353;
CC       P14923:JUP; NbExp=2; IntAct=EBI-701918, EBI-702484;
CC   -!- SUBCELLULAR LOCATION: Isoform 1: Cytoplasm, cytoskeleton. Cell
CC       junction, adherens junction. Cell membrane; Peripheral membrane
CC       protein; Cytoplasmic side. Cell junction. Note=Found at cell-cell
CC       boundaries and probably at cell-matrix boundaries.
CC   -!- SUBCELLULAR LOCATION: Isoform 3: Cell membrane
CC       {ECO:0000269|PubMed:21708131}; Peripheral membrane protein
CC       {ECO:0000269|PubMed:21708131}; Cytoplasmic side
CC       {ECO:0000269|PubMed:21708131}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1; Synonyms=CTNNA1a;
CC         IsoId=P35221-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P35221-2; Sequence=VSP_017494;
CC       Name=3; Synonyms=CTNNA1b;
CC         IsoId=P35221-3; Sequence=VSP_047810;
CC         Note=Expressed at high levels in the nervous system. Lacks the
CC         beta-catenin interaction domain.;
CC   -!- TISSUE SPECIFICITY: Expressed ubiquitously in normal tissues.
CC   -!- PTM: Sumoylated. {ECO:0000269|PubMed:15561718}.
CC   -!- DISEASE: Hereditary diffuse gastric cancer (HDGC) [MIM:137215]: A
CC       cancer predisposition syndrome with increased susceptibility to
CC       diffuse gastric cancer. Diffuse gastric cancer is a malignant
CC       disease characterized by poorly differentiated infiltrating
CC       lesions resulting in thickening of the stomach. Malignant tumors
CC       start in the stomach, can spread to the esophagus or the small
CC       intestine, and can extend through the stomach wall to nearby lymph
CC       nodes and organs. It also can metastasize to other parts of the
CC       body. {ECO:0000269|PubMed:23208944}. Note=The gene represented in
CC       this entry may be involved in disease pathogenesis.
CC   -!- SIMILARITY: Belongs to the vinculin/alpha-catenin family.
CC       {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC       URL="http://egp.gs.washington.edu/data/ctnna1/";
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DR   EMBL; D14705; BAA03530.1; -; mRNA.
DR   EMBL; D13866; BAA02979.1; -; mRNA.
DR   EMBL; L23805; AAA86430.1; -; mRNA.
DR   EMBL; U03100; AAA18949.1; -; mRNA.
DR   EMBL; HQ589335; AEF32483.1; -; mRNA.
DR   EMBL; AF102803; AAC99459.1; -; Genomic_DNA.
DR   EMBL; AF102787; AAC99459.1; JOINED; Genomic_DNA.
DR   EMBL; AF102788; AAC99459.1; JOINED; Genomic_DNA.
DR   EMBL; AF102789; AAC99459.1; JOINED; Genomic_DNA.
DR   EMBL; AF102790; AAC99459.1; JOINED; Genomic_DNA.
DR   EMBL; AF102791; AAC99459.1; JOINED; Genomic_DNA.
DR   EMBL; AF102792; AAC99459.1; JOINED; Genomic_DNA.
DR   EMBL; AF102793; AAC99459.1; JOINED; Genomic_DNA.
DR   EMBL; AF102794; AAC99459.1; JOINED; Genomic_DNA.
DR   EMBL; AF102795; AAC99459.1; JOINED; Genomic_DNA.
DR   EMBL; AF102796; AAC99459.1; JOINED; Genomic_DNA.
DR   EMBL; AF102797; AAC99459.1; JOINED; Genomic_DNA.
DR   EMBL; AF102798; AAC99459.1; JOINED; Genomic_DNA.
DR   EMBL; AF102799; AAC99459.1; JOINED; Genomic_DNA.
DR   EMBL; AF102800; AAC99459.1; JOINED; Genomic_DNA.
DR   EMBL; AF102801; AAC99459.1; JOINED; Genomic_DNA.
DR   EMBL; AF102802; AAC99459.1; JOINED; Genomic_DNA.
DR   EMBL; AY884207; AAW56940.1; -; Genomic_DNA.
DR   EMBL; AC010453; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC011405; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC034243; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC113340; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471062; EAW62124.1; -; Genomic_DNA.
DR   EMBL; BC000385; AAH00385.1; -; mRNA.
DR   EMBL; BC031262; AAH31262.1; -; mRNA.
DR   EMBL; L22080; AAA35502.1; -; mRNA.
DR   CCDS; CCDS34243.1; -. [P35221-1]
DR   CCDS; CCDS75315.1; -. [P35221-3]
DR   PIR; JC2542; JC2542.
DR   PIR; JN0607; JN0607.
DR   RefSeq; NP_001277236.1; NM_001290307.1.
DR   RefSeq; NP_001277238.1; NM_001290309.1.
DR   RefSeq; NP_001277239.1; NM_001290310.1.
DR   RefSeq; NP_001277241.1; NM_001290312.1. [P35221-3]
DR   RefSeq; NP_001894.2; NM_001903.3. [P35221-1]
DR   RefSeq; XP_005271956.1; XM_005271899.2. [P35221-3]
DR   RefSeq; XP_006714599.1; XM_006714536.2. [P35221-1]
DR   RefSeq; XP_011541474.1; XM_011543172.1. [P35221-1]
DR   UniGene; Hs.445981; -.
DR   PDB; 1H6G; X-ray; 2.20 A; A/B=377-632.
DR   PDB; 4EHP; X-ray; 2.66 A; B=277-382.
DR   PDB; 4IGG; X-ray; 3.66 A; A/B=82-906.
DR   PDBsum; 1H6G; -.
DR   PDBsum; 4EHP; -.
DR   PDBsum; 4IGG; -.
DR   ProteinModelPortal; P35221; -.
DR   SMR; P35221; 19-878.
DR   BioGrid; 107876; 57.
DR   DIP; DIP-515N; -.
DR   IntAct; P35221; 40.
DR   MINT; MINT-4998962; -.
DR   STRING; 9606.ENSP00000304669; -.
DR   PhosphoSite; P35221; -.
DR   BioMuta; CTNNA1; -.
DR   DMDM; 461853; -.
DR   MaxQB; P35221; -.
DR   PaxDb; P35221; -.
DR   PeptideAtlas; P35221; -.
DR   PRIDE; P35221; -.
DR   DNASU; 1495; -.
DR   Ensembl; ENST00000302763; ENSP00000304669; ENSG00000044115. [P35221-1]
DR   Ensembl; ENST00000540387; ENSP00000438476; ENSG00000044115. [P35221-3]
DR   GeneID; 1495; -.
DR   KEGG; hsa:1495; -.
DR   UCSC; uc003ldh.3; human. [P35221-1]
DR   CTD; 1495; -.
DR   GeneCards; CTNNA1; -.
DR   HGNC; HGNC:2509; CTNNA1.
DR   HPA; CAB021089; -.
DR   HPA; HPA046119; -.
DR   MIM; 116805; gene.
DR   MIM; 137215; phenotype.
DR   neXtProt; NX_P35221; -.
DR   PharmGKB; PA27008; -.
DR   eggNOG; KOG3681; Eukaryota.
DR   eggNOG; ENOG410XSRU; LUCA.
DR   GeneTree; ENSGT00550000074411; -.
DR   HOGENOM; HOG000280724; -.
DR   HOVERGEN; HBG000069; -.
DR   InParanoid; P35221; -.
DR   KO; K05691; -.
DR   OMA; WERQVRV; -.
DR   OrthoDB; EOG7HQN7B; -.
DR   PhylomeDB; P35221; -.
DR   TreeFam; TF313686; -.
DR   Reactome; R-HSA-375170; CDO in myogenesis.
DR   Reactome; R-HSA-418990; Adherens junctions interactions.
DR   Reactome; R-HSA-5218920; VEGFR2 mediated vascular permeability.
DR   Reactome; R-HSA-5626467; RHO GTPases activate IQGAPs.
DR   ChiTaRS; CTNNA1; human.
DR   EvolutionaryTrace; P35221; -.
DR   GeneWiki; Catenin_(cadherin-associated_protein),_alpha_1; -.
DR   GenomeRNAi; 1495; -.
DR   NextBio; 6145; -.
DR   PRO; PR:P35221; -.
DR   Proteomes; UP000005640; Chromosome 5.
DR   Bgee; P35221; -.
DR   CleanEx; HS_CTNNA1; -.
DR   ExpressionAtlas; P35221; baseline and differential.
DR   Genevisible; P35221; HS.
DR   GO; GO:0001669; C:acrosomal vesicle; IEA:Ensembl.
DR   GO; GO:0015629; C:actin cytoskeleton; IEA:InterPro.
DR   GO; GO:0016342; C:catenin complex; IDA:BHF-UCL.
DR   GO; GO:0005911; C:cell-cell junction; IDA:UniProtKB.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0016600; C:flotillin complex; IEA:Ensembl.
DR   GO; GO:0005925; C:focal adhesion; IDA:UniProtKB.
DR   GO; GO:0014704; C:intercalated disc; IEA:Ensembl.
DR   GO; GO:0030027; C:lamellipodium; IEA:Ensembl.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0005915; C:zonula adherens; IEA:Ensembl.
DR   GO; GO:0008013; F:beta-catenin binding; IPI:BHF-UCL.
DR   GO; GO:0045296; F:cadherin binding; IPI:UniProtKB.
DR   GO; GO:0045295; F:gamma-catenin binding; IPI:BHF-UCL.
DR   GO; GO:0044822; F:poly(A) RNA binding; IDA:UniProtKB.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   GO; GO:0017166; F:vinculin binding; IPI:UniProtKB.
DR   GO; GO:0007015; P:actin filament organization; IEA:InterPro.
DR   GO; GO:0034332; P:adherens junction organization; TAS:Reactome.
DR   GO; GO:0007568; P:aging; IEA:Ensembl.
DR   GO; GO:0043297; P:apical junction assembly; NAS:UniProtKB.
DR   GO; GO:0031103; P:axon regeneration; IEA:Ensembl.
DR   GO; GO:0007155; P:cell adhesion; NAS:ProtInc.
DR   GO; GO:0034329; P:cell junction assembly; TAS:Reactome.
DR   GO; GO:0045216; P:cell-cell junction organization; TAS:Reactome.
DR   GO; GO:0034613; P:cellular protein localization; IEA:Ensembl.
DR   GO; GO:0071681; P:cellular response to indole-3-methanol; IDA:UniProtKB.
DR   GO; GO:0090136; P:epithelial cell-cell adhesion; IEA:Ensembl.
DR   GO; GO:0007163; P:establishment or maintenance of cell polarity; IEA:Ensembl.
DR   GO; GO:0016264; P:gap junction assembly; IEA:Ensembl.
DR   GO; GO:0008584; P:male gonad development; IEA:Ensembl.
DR   GO; GO:0042692; P:muscle cell differentiation; TAS:Reactome.
DR   GO; GO:2000146; P:negative regulation of cell motility; IEA:Ensembl.
DR   GO; GO:2001240; P:negative regulation of extrinsic apoptotic signaling pathway in absence of ligand; IEA:Ensembl.
DR   GO; GO:2001045; P:negative regulation of integrin-mediated signaling pathway; IEA:Ensembl.
DR   GO; GO:0007406; P:negative regulation of neuroblast proliferation; IEA:Ensembl.
DR   GO; GO:0042475; P:odontogenesis of dentin-containing tooth; IEA:Ensembl.
DR   GO; GO:0001541; P:ovarian follicle development; IEA:Ensembl.
DR   GO; GO:2001241; P:positive regulation of extrinsic apoptotic signaling pathway in absence of ligand; IEA:Ensembl.
DR   GO; GO:0051149; P:positive regulation of muscle cell differentiation; TAS:Reactome.
DR   GO; GO:0045880; P:positive regulation of smoothened signaling pathway; IEA:Ensembl.
DR   GO; GO:0051291; P:protein heterooligomerization; IEA:Ensembl.
DR   GO; GO:0043627; P:response to estrogen; IEA:Ensembl.
DR   GO; GO:0007264; P:small GTPase mediated signal transduction; TAS:Reactome.
DR   GO; GO:0048010; P:vascular endothelial growth factor receptor signaling pathway; TAS:Reactome.
DR   InterPro; IPR001033; Alpha_catenin.
DR   InterPro; IPR030047; CTNNA1.
DR   InterPro; IPR006077; Vinculin/catenin.
DR   InterPro; IPR000633; Vinculin_CS.
DR   PANTHER; PTHR18914; PTHR18914; 1.
DR   PANTHER; PTHR18914:SF24; PTHR18914:SF24; 1.
DR   Pfam; PF01044; Vinculin; 2.
DR   PRINTS; PR00805; ALPHACATENIN.
DR   SUPFAM; SSF47220; SSF47220; 4.
DR   PROSITE; PS00663; VINCULIN_1; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative splicing; Cell adhesion;
KW   Cell junction; Cell membrane; Complete proteome; Cytoplasm;
KW   Cytoskeleton; Direct protein sequencing; Membrane; Phosphoprotein;
KW   Polymorphism; Reference proteome; Ubl conjugation.
FT   INIT_MET      1      1       Removed. {ECO:0000269|Ref.10}.
FT   CHAIN         2    906       Catenin alpha-1.
FT                                /FTId=PRO_0000064261.
FT   REGION        2    228       Involved in homodimerization.
FT   REGION       97    148       Interaction with JUP and CTNNB1.
FT   REGION      325    394       Interaction with alpha-actinin.
FT   MOD_RES       2      2       N-acetylthreonine. {ECO:0000269|Ref.10}.
FT   MOD_RES     264    264       Phosphoserine.
FT                                {ECO:0000244|PubMed:24275569}.
FT   MOD_RES     268    268       Phosphoserine.
FT                                {ECO:0000244|PubMed:24275569}.
FT   MOD_RES     295    295       Phosphoserine.
FT                                {ECO:0000244|PubMed:24275569}.
FT   MOD_RES     297    297       Phosphoserine.
FT                                {ECO:0000244|PubMed:24275569}.
FT   MOD_RES     634    634       Phosphothreonine.
FT                                {ECO:0000244|PubMed:21406692,
FT                                ECO:0000244|PubMed:24275569}.
FT   MOD_RES     641    641       Phosphoserine.
FT                                {ECO:0000244|PubMed:16807684,
FT                                ECO:0000244|PubMed:17081983,
FT                                ECO:0000244|PubMed:18220336,
FT                                ECO:0000244|PubMed:18318008,
FT                                ECO:0000244|PubMed:18669648,
FT                                ECO:0000244|PubMed:19369195,
FT                                ECO:0000244|PubMed:19690332,
FT                                ECO:0000244|PubMed:20068231,
FT                                ECO:0000244|PubMed:21406692,
FT                                ECO:0000244|PubMed:24275569}.
FT   MOD_RES     645    645       Phosphothreonine.
FT                                {ECO:0000244|PubMed:18318008}.
FT   MOD_RES     652    652       Phosphoserine.
FT                                {ECO:0000244|PubMed:17487921,
FT                                ECO:0000244|PubMed:18669648,
FT                                ECO:0000244|PubMed:21406692}.
FT   MOD_RES     655    655       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P26231}.
FT   MOD_RES     658    658       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:P26231}.
FT   MOD_RES     851    851       Phosphoserine.
FT                                {ECO:0000244|PubMed:24275569}.
FT   VAR_SEQ       1    370       Missing (in isoform 3).
FT                                {ECO:0000303|PubMed:15489334,
FT                                ECO:0000303|PubMed:21708131}.
FT                                /FTId=VSP_047810.
FT   VAR_SEQ     811    811       G -> GNCDTCGALQGLKGWPPPLCLATHW (in
FT                                isoform 2). {ECO:0000303|PubMed:7945318}.
FT                                /FTId=VSP_017494.
FT   VARIANT     179    179       A -> V (in dbSNP:rs28363394).
FT                                {ECO:0000269|Ref.6}.
FT                                /FTId=VAR_022303.
FT   VARIANT     219    219       P -> S (in dbSNP:rs28363406).
FT                                {ECO:0000269|Ref.6}.
FT                                /FTId=VAR_022304.
FT   CONFLICT     92     92       A -> V (in Ref. 3; AAA86430/AAA18949).
FT                                {ECO:0000305}.
FT   CONFLICT    129    129       R -> P (in Ref. 3; AAA18949).
FT                                {ECO:0000305}.
FT   CONFLICT    175    175       I -> N (in Ref. 3; AAA86430/AAA18949).
FT                                {ECO:0000305}.
FT   CONFLICT    216    216       K -> S (in Ref. 3; AAA86430/AAA18949).
FT                                {ECO:0000305}.
FT   CONFLICT    342    342       Q -> K (in Ref. 1; BAA03530).
FT                                {ECO:0000305}.
FT   CONFLICT    344    348       LQDLL -> CRTCV (in Ref. 3; AAA86430).
FT                                {ECO:0000305}.
FT   CONFLICT    460    460       L -> G (in Ref. 3; AAA86430/AAA18949).
FT                                {ECO:0000305}.
FT   CONFLICT    469    469       L -> TW (in Ref. 3; AAA86430/AAA18949).
FT                                {ECO:0000305}.
FT   CONFLICT    473    473       A -> P (in Ref. 3; AAA86430/AAA18949).
FT                                {ECO:0000305}.
FT   CONFLICT    653    653       R -> E (in Ref. 3; AAA86430/AAA18949).
FT                                {ECO:0000305}.
FT   CONFLICT    685    685       A -> R (in Ref. 3; AAA86430/AAA18949).
FT                                {ECO:0000305}.
FT   CONFLICT    764    764       A -> R (in Ref. 3; AAA86430/AAA18949).
FT                                {ECO:0000305}.
FT   CONFLICT    789    789       Q -> H (in Ref. 1; BAA03530).
FT                                {ECO:0000305}.
FT   CONFLICT    859    859       W -> M (in Ref. 3; AAA86430/AAA18949).
FT                                {ECO:0000305}.
FT   HELIX       293    299       {ECO:0000244|PDB:4EHP}.
FT   STRAND      300    302       {ECO:0000244|PDB:4EHP}.
FT   HELIX       305    316       {ECO:0000244|PDB:4EHP}.
FT   HELIX       325    327       {ECO:0000244|PDB:4EHP}.
FT   HELIX       328    352       {ECO:0000244|PDB:4EHP}.
FT   HELIX       353    355       {ECO:0000244|PDB:4EHP}.
FT   HELIX       378    386       {ECO:0000244|PDB:1H6G}.
FT   HELIX       387    389       {ECO:0000244|PDB:1H6G}.
FT   TURN        393    395       {ECO:0000244|PDB:1H6G}.
FT   HELIX       398    409       {ECO:0000244|PDB:1H6G}.
FT   HELIX       413    438       {ECO:0000244|PDB:1H6G}.
FT   HELIX       444    473       {ECO:0000244|PDB:1H6G}.
FT   HELIX       478    506       {ECO:0000244|PDB:1H6G}.
FT   HELIX       509    531       {ECO:0000244|PDB:1H6G}.
FT   HELIX       535    559       {ECO:0000244|PDB:1H6G}.
FT   TURN        560    562       {ECO:0000244|PDB:1H6G}.
FT   HELIX       567    581       {ECO:0000244|PDB:1H6G}.
FT   HELIX       583    598       {ECO:0000244|PDB:1H6G}.
FT   STRAND      600    602       {ECO:0000244|PDB:1H6G}.
FT   HELIX       608    630       {ECO:0000244|PDB:1H6G}.
SQ   SEQUENCE   906 AA;  100071 MW;  7AAE6F5DDBAF5099 CRC64;
     MTAVHAGNIN FKWDPKSLEI RTLAVERLLE PLVTQVTTLV NTNSKGPSNK KRGRSKKAHV
     LAASVEQATE NFLEKGDKIA KESQFLKEEL VAAVEDVRKQ GDLMKAAAGE FADDPCSSVK
     RGNMVRAARA LLSAVTRLLI LADMADVYKL LVQLKVVEDG ILKLRNAGNE QDLGIQYKAL
     KPEVDKLNIM AAKRQQELKD VGHRDQMAAA RGILQKNVPI LYTASQACLQ HPDVAAYKAN
     RDLIYKQLQQ AVTGISNAAQ ATASDDASQH QGGGGGELAY ALNNFDKQII VDPLSFSEER
     FRPSLEERLE SIISGAALMA DSSCTRDDRR ERIVAECNAV RQALQDLLSE YMGNAGRKER
     SDALNSAIDK MTKKTRDLRR QLRKAVMDHV SDSFLETNVP LLVLIEAAKN GNEKEVKEYA
     QVFREHANKL IEVANLACSI SNNEEGVKLV RMSASQLEAL CPQVINAALA LAAKPQSKLA
     QENMDLFKEQ WEKQVRVLTD AVDDITSIDD FLAVSENHIL EDVNKCVIAL QEKDVDGLDR
     TAGAIRGRAA RVIHVVTSEM DNYEPGVYTE KVLEATKLLS NTVMPRFTEQ VEAAVEALSS
     DPAQPMDENE FIDASRLVYD GIRDIRKAVL MIRTPEELDD SDFETEDFDV RSRTSVQTED
     DQLIAGQSAR AIMAQLPQEQ KAKIAEQVAS FQEEKSKLDA EVSKWDDSGN DIIVLAKQMC
     MIMMEMTDFT RGKGPLKNTS DVISAAKKIA EAGSRMDKLG RTIADHCPDS ACKQDLLAYL
     QRIALYCHQL NICSKVKAEV QNLGGELVVS GVDSAMSLIQ AAKNLMNAVV QTVKASYVAS
     TKYQKSQGMA SLNLPAVSWK MKAPEKKPLV KREKQDETQT KIKRASQKKH VNPVQALSEF
     KAMDSI
//
ID   E1A_ADE02               Reviewed;         289 AA.
AC   P03254; P24934; Q67788;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   11-NOV-2015, entry version 96.
DE   RecName: Full=Early E1A protein {ECO:0000305};
DE   AltName: Full=Early E1A 32 kDa protein;
OS   Human adenovirus C serotype 2 (HAdV-2) (Human adenovirus 2).
OC   Viruses; dsDNA viruses, no RNA stage; Adenoviridae; Mastadenovirus.
OX   NCBI_TaxID=10515;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS EARLY E1A 32 KDA PROTEIN
RP   AND EARLY E1A 26 KDA PROTEIN).
RX   PubMed=551290; DOI=10.1038/281694a0;
RA   Perricaudet M., Akusjaervi G., Virtanen A., Pettersson U.;
RT   "Structure of two spliced mRNAs from the transforming region of human
RT   subgroup C adenoviruses.";
RL   Nature 281:694-696(1979).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS EARLY E1A 32 KDA PROTEIN;
RP   EARLY E1A 26 KDA PROTEIN AND EARLY E1A 6 KDA PROTEIN).
RX   PubMed=7142161;
RA   Gingeras T.R., Sciaky D., Gelinas R.E., Bing-Dong J., Yen C.E.,
RA   Kelly M.M., Bullock P.A., Parsons B.L., O'Neill K.E., Roberts R.J.;
RT   "Nucleotide sequences from the adenovirus-2 genome.";
RL   J. Biol. Chem. 257:13475-13491(1982).
RN   [3]
RP   INTERACTION WITH HOST ATF7, AND MUTAGENESIS OF CYS-157; THR-178 AND
RP   SER-185.
RX   PubMed=8417352;
RA   Chatton B., Bocco J.L., Gaire M., Hauss C., Reimund B., Goetz J.,
RA   Kedinger C.;
RT   "Transcriptional activation by the adenovirus larger E1a product is
RT   mediated by members of the cellular transcription factor ATF family
RT   which can directly associate with E1a.";
RL   Mol. Cell. Biol. 13:561-570(1993).
CC   -!- FUNCTION: Plays a role in viral genome replication by driving
CC       entry of quiescent cells into the cell cycle. Stimulation of
CC       progression from G1 to S phase allows the virus to efficiently use
CC       the cellular DNA replicating machinery to achieve viral genome
CC       replication. E1A protein has both transforming and trans-
CC       activating activities. Induces the disassembly of the E2F1
CC       transcription factor from RB1 by direct competition for the same
CC       binding site on RB1, with subsequent transcriptional activation of
CC       E2F1-regulated S-phase genes and of the E2 region of the
CC       adenoviral genome. Release of E2F1 leads to the ARF-mediated
CC       inhibition of MDM2 and causes TP53/p53 to accumulate because it is
CC       not targeted for degradation by MDM2-mediated ubiquitination
CC       anymore. This increase in TP53, in turn, would arrest the cell
CC       proliferation and direct its death but this effect is counteracted
CC       by the viral protein E1B-55K. Inactivation of the ability of RB1
CC       to arrest the cell cycle is critical for cellular transformation,
CC       uncontrolled cellular growth and proliferation induced by viral
CC       infection. Interaction with RBX1 and CUL1 inhibits ubiquitination
CC       of the proteins targeted by SCF(FBXW7) ubiquitin ligase complex,
CC       and may be linked to unregulated host cell proliferation. The
CC       tumorigenesis-restraining activity of E1A may be related to the
CC       disruption of the host CtBP-CtIP complex through the CtBP binding
CC       motif. Interacts with host TBP protein; this interaction probably
CC       disrupts the TBP-TATA complex. {ECO:0000250|UniProtKB:P03255}.
CC   -!- SUBUNIT: Interacts with host UBE2I; this interaction interferes
CC       with polySUMOylation. Interacts with host RB1; this interaction
CC       induces the aberrant dissociation of RB1-E2F1 complex thereby
CC       disrupting the activity of RB1 and activating E2F1-regulated
CC       genes. Interacts with host ATF7; the interaction enhances ATF7-
CC       mediated viral transactivation activity which requires the zinc
CC       binding domains of both proteins. Isoform early E1A 32 kDa protein
CC       and isoform early E1A 26 kDa protein interact (via N-terminus)
CC       with CUL1 and E3 ubiquitin ligase RBX1; these interactions inhibit
CC       RBX1-CUL1-dependent elongation reaction of ubiquitin chains and
CC       attenuate ubiquitination of SCF(FBXW7) target proteins. Interacts
CC       (via PXLXP motif) with host ZMYND11/BS69 (via MYND-type zinc
CC       finger); this interaction inhibits E1A mediated transactivation.
CC       Interacts with host EP300; this interaction stimulates the
CC       acetylation of RB1 by recruiting EP300 and RB1 into a multimeric-
CC       protein complex. Interacts with host CTBP1 and CTBP2; this
CC       interaction seems to potentiate viral replication. Interacts with
CC       host DCAF7. Interacts with host DYRK1A. Interacts with host KPNA4;
CC       this interaction allows E1A import into the host nucleus.
CC       Interacts with host EP400; this interaction stabilizes MYC.
CC       {ECO:0000250|UniProtKB:P03255}.
CC   -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000250|UniProtKB:P03255}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC         Comment=Isoforms are derived from the E1 region of the genome.;
CC       Name=early E1A 32 kDa protein; Synonyms=289R, L-E1A;
CC         IsoId=P03254-1; Sequence=Displayed;
CC       Name=early E1A 26 kDa protein; Synonyms=243R, S-E1A;
CC         IsoId=P03254-2; Sequence=VSP_000197;
CC       Name=early E1A 6 kDa protein;
CC         IsoId=P03254-3; Sequence=VSP_028916, VSP_028917;
CC   -!- SIMILARITY: Belongs to the adenoviridae E1A protein family.
CC       {ECO:0000305}.
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DR   EMBL; J01917; AAA92197.1; -; Genomic_DNA.
DR   EMBL; J01917; AAA92198.1; -; Genomic_DNA.
DR   EMBL; J01917; AAA92199.1; -; Genomic_DNA.
DR   PIR; A03824; Q2AD2.
DR   RefSeq; AP_000161.1; AC_000007.1.
DR   DIP; DIP-570N; -.
DR   IntAct; P03254; 1.
DR   MINT; MINT-198575; -.
DR   Proteomes; UP000008167; Genome.
DR   GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0039695; P:DNA-templated viral transcription; IDA:UniProtKB.
DR   GO; GO:0039645; P:modulation by virus of host G1/S transition checkpoint; IEA:UniProtKB-KW.
DR   GO; GO:0039649; P:modulation by virus of host ubiquitin-protein ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
DR   GO; GO:0039657; P:suppression by virus of host gene expression; IEA:UniProtKB-KW.
DR   GO; GO:0039563; P:suppression by virus of host STAT1 activity; IEA:UniProtKB-KW.
DR   GO; GO:0039502; P:suppression by virus of host type I interferon-mediated signaling pathway; IEA:UniProtKB-KW.
DR   InterPro; IPR014410; Aden_E1A.
DR   Pfam; PF02703; Adeno_E1A; 1.
PE   1: Evidence at protein level;
KW   Activator; Alternative splicing; Complete proteome; Early protein;
KW   Eukaryotic host gene expression shutoff by virus;
KW   Eukaryotic host transcription shutoff by virus;
KW   G1/S host cell cycle checkpoint dysregulation by virus;
KW   Host gene expression shutoff by virus; Host nucleus;
KW   Host-virus interaction;
KW   Inhibition of eukaryotic host transcription initiation by virus;
KW   Inhibition of host innate immune response by virus;
KW   Inhibition of host interferon signaling pathway by virus;
KW   Inhibition of host STAT1 by virus; Metal-binding;
KW   Modulation of host cell cycle by virus;
KW   Modulation of host E3 ubiquitin ligases by virus;
KW   Modulation of host ubiquitin pathway by virus; Oncogene;
KW   Phosphoprotein; Reference proteome; Transcription;
KW   Transcription regulation; Viral immunoevasion; Zinc; Zinc-finger.
FT   CHAIN         1    289       Early E1A protein.
FT                                /FTId=PRO_0000221692.
FT   ZN_FING     154    174       {ECO:0000250|UniProtKB:P03255}.
FT   REGION       41     49       Interaction with RB1 in competition with
FT                                E2F1. {ECO:0000250}.
FT   REGION       76    140       Interaction with UBE2I. {ECO:0000250}.
FT   MOTIF       113    117       PXLXP motif, interaction with host
FT                                ZMYND11. {ECO:0000250}.
FT   MOTIF       122    126       LXCXE motif, interaction with host RB1.
FT                                {ECO:0000255}.
FT   MOTIF       258    289       Bipartite nuclear localization signal.
FT                                {ECO:0000250|UniProtKB:P03255,
FT                                ECO:0000255}.
FT   MOTIF       279    283       PXDLS motif, CTBP-binding.
FT                                {ECO:0000250|UniProtKB:P03255}.
FT   MOD_RES      89     89       Phosphoserine; by host. {ECO:0000250}.
FT   MOD_RES     219    219       Phosphoserine; by host. {ECO:0000250}.
FT   MOD_RES     231    231       Phosphoserine; by host. {ECO:0000250}.
FT   VAR_SEQ      29     55       ADNLPPPSHFEPPTLHELYDLDVTAPE -> CLNLSLSPSQ
FT                                NRSLQDLPGVLNWCLLS (in isoform early E1A 6
FT                                kDa protein). {ECO:0000305}.
FT                                /FTId=VSP_028916.
FT   VAR_SEQ      56    289       Missing (in isoform early E1A 6 kDa
FT                                protein). {ECO:0000305}.
FT                                /FTId=VSP_028917.
FT   VAR_SEQ     140    185       Missing (in isoform early E1A 26 kDa
FT                                protein). {ECO:0000305}.
FT                                /FTId=VSP_000197.
FT   MUTAGEN     157    157       C->S: Abolishes ATF7-mediated
FT                                transcriptional activation.
FT                                {ECO:0000269|PubMed:8417352}.
FT   MUTAGEN     178    178       T->P: No effect on ATF7-mediated
FT                                transcriptional activation.
FT                                {ECO:0000269|PubMed:8417352}.
FT   MUTAGEN     185    185       S->R: Abolishes ATF7-mediated
FT                                transcriptional activation.
FT                                {ECO:0000269|PubMed:8417352}.
FT   CONFLICT     68     68       D -> E (in Ref. 2; AAA92197/AAA92199).
FT                                {ECO:0000305}.
FT   CONFLICT     81     81       L -> F (in Ref. 2; AAA92197/AAA92199).
FT                                {ECO:0000305}.
SQ   SEQUENCE   289 AA;  31851 MW;  4264747DAD74FFC5 CRC64;
     MRHIICHGGV ITEEMAASLL DQLIEEVLAD NLPPPSHFEP PTLHELYDLD VTAPEDPNEE
     AVSQIFPDSV MLAVQEGIDL LTFPPAPGSP EPPHLSRQPE QPEQRALGPV SMPNLVPEVI
     DLTCHEAGFP PSDDEDEEGE EFVLDYVEHP GHGCRSCHYH RRNTGDPDIM CSLCYMRTCG
     MFVYSPVSEP EPEPEPEPEP ARPTRRPKLV PAILRRPTSP VSRECNSSTD SCDSGPSNTP
     PEIHPVVPLC PIKPVAVRVG GRRQAVECIE DLLNESGQPL DLSCKRPRP
//
ID   FOG1_HUMAN              Reviewed;        1006 AA.
AC   Q8IX07;
DT   15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 2.
DT   11-NOV-2015, entry version 120.
DE   RecName: Full=Zinc finger protein ZFPM1;
DE   AltName: Full=Friend of GATA protein 1;
DE            Short=FOG-1;
DE            Short=Friend of GATA 1;
DE   AltName: Full=Zinc finger protein 89A;
DE   AltName: Full=Zinc finger protein multitype 1;
GN   Name=ZFPM1; Synonyms=FOG1, ZFN89A;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND INTERACTION WITH
RP   GATA1 AND GATA2.
RC   TISSUE=Megakaryocyte;
RX   PubMed=12483298; DOI=10.1007/s00439-002-0832-1;
RA   Freson K., Thys C., Wittewrongel C., Vermylen J., Hoylaerts M.F.,
RA   Van Geet C.;
RT   "Molecular cloning and characterization of the GATA1 cofactor human
RT   FOG1 and assessment of its binding to GATA1 proteins carrying D218
RT   substitutions.";
RL   Hum. Genet. 112:42-49(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15616553; DOI=10.1038/nature03187;
RA   Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X.,
RA   Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A.,
RA   Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.,
RA   Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L.,
RA   Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A.,
RA   Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D.,
RA   Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J.,
RA   Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA   Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I.,
RA   Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W.,
RA   Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A.,
RA   Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S.,
RA   Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA   Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA   Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L.,
RA   Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A.,
RA   Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L.,
RA   Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N.,
RA   Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M.,
RA   Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L.,
RA   Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D.,
RA   Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P.,
RA   Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M.,
RA   Rubin E.M., Pennacchio L.A.;
RT   "The sequence and analysis of duplication-rich human chromosome 16.";
RL   Nature 432:988-994(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Prostate cancer;
RX   PubMed=17487921; DOI=10.1002/elps.200600782;
RA   Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.;
RT   "Toward a global characterization of the phosphoproteome in prostate
RT   cancer cells: identification of phosphoproteins in the LNCaP cell
RT   line.";
RL   Electrophoresis 28:2027-2034(2007).
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic kidney;
RX   PubMed=17525332; DOI=10.1126/science.1140321;
RA   Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
RA   Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
RA   Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
RT   "ATM and ATR substrate analysis reveals extensive protein networks
RT   responsive to DNA damage.";
RL   Science 316:1160-1166(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-786, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA   Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT   a refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-901 AND SER-909, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA   Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA   Rodionov V., Han D.K.;
RT   "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT   reveals system-wide modulation of protein-protein interactions.";
RL   Sci. Signal. 2:RA46-RA46(2009).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-671; SER-786; SER-901
RP   AND SER-914, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
RA   Wang L., Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human
RT   liver phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
CC   -!- FUNCTION: Transcription regulator that plays an essential role in
CC       erythroid and megakaryocytic cell differentiation. Essential
CC       cofactor that acts via the formation of a heterodimer with
CC       transcription factors of the GATA family GATA1, GATA2 and GATA3.
CC       Such heterodimer can both activate or repress transcriptional
CC       activity, depending on the cell and promoter context. The
CC       heterodimer formed with GATA proteins is essential to activate
CC       expression of genes such as NFE2, ITGA2B, alpha- and beta-globin,
CC       while it represses expression of KLF1. May be involved in
CC       regulation of some genes in gonads. May also be involved in
CC       cardiac development, in a non-redundant way with ZFPM2/FOG2 (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with corepressor CTBP2; this interaction is
CC       however not essential for corepressor activity (By similarity).
CC       Interacts with the N-terminal zinc-finger of GATA1, GATA2 and
CC       probably GATA3. {ECO:0000250, ECO:0000269|PubMed:12483298}.
CC   -!- INTERACTION:
CC       P49841:GSK3B; NbExp=2; IntAct=EBI-3942619, EBI-373586;
CC       Q09028:RBBP4; NbExp=4; IntAct=EBI-3942619, EBI-620823;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Mainly expressed in hematopoietic tissues.
CC       Also expressed in adult cerebellum, stomach, lymph node, liver and
CC       pancreas. Expressed in fetal heart, liver and spleen.
CC       {ECO:0000269|PubMed:12483298}.
CC   -!- DOMAIN: The CCHC-type zinc fingers 1, 5, 6 and 9 directly bind to
CC       GATA-type zinc fingers. The Tyr residue adjacent to the last Cys
CC       of the CCHC-type zinc finger is essential for the interaction with
CC       GATA-type zinc fingers (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the FOG (Friend of GATA) family.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Contains 4 C2H2-type zinc fingers.
CC       {ECO:0000255|PROSITE-ProRule:PRU00042}.
CC   -!- SIMILARITY: Contains 5 C2HC-type zinc fingers. {ECO:0000305}.
CC   -----------------------------------------------------------------------
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DR   EMBL; AF488691; AAN45858.1; -; mRNA.
DR   EMBL; AC116552; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC135049; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471184; EAW66806.1; -; Genomic_DNA.
DR   CCDS; CCDS32502.1; -.
DR   RefSeq; NP_722520.2; NM_153813.2.
DR   UniGene; Hs.632218; -.
DR   PDB; 2XU7; X-ray; 1.90 A; C/D=1-15.
DR   PDBsum; 2XU7; -.
DR   ProteinModelPortal; Q8IX07; -.
DR   SMR; Q8IX07; 85-209, 315-347.
DR   BioGrid; 127806; 10.
DR   DIP; DIP-48415N; -.
DR   IntAct; Q8IX07; 3.
DR   STRING; 9606.ENSP00000326630; -.
DR   PhosphoSite; Q8IX07; -.
DR   BioMuta; ZFPM1; -.
DR   DMDM; 296434508; -.
DR   MaxQB; Q8IX07; -.
DR   PaxDb; Q8IX07; -.
DR   PRIDE; Q8IX07; -.
DR   Ensembl; ENST00000319555; ENSP00000326630; ENSG00000179588.
DR   GeneID; 161882; -.
DR   KEGG; hsa:161882; -.
DR   UCSC; uc002fkv.3; human.
DR   CTD; 161882; -.
DR   GeneCards; ZFPM1; -.
DR   HGNC; HGNC:19762; ZFPM1.
DR   HPA; HPA046603; -.
DR   MIM; 601950; gene.
DR   neXtProt; NX_Q8IX07; -.
DR   PharmGKB; PA134920282; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   eggNOG; COG5048; LUCA.
DR   GeneTree; ENSGT00530000063823; -.
DR   HOGENOM; HOG000112626; -.
DR   HOVERGEN; HBG101018; -.
DR   InParanoid; Q8IX07; -.
DR   KO; K17441; -.
DR   OMA; YSCPAAP; -.
DR   OrthoDB; EOG74TWXR; -.
DR   PhylomeDB; Q8IX07; -.
DR   TreeFam; TF331342; -.
DR   Reactome; R-HSA-983231; Factors involved in megakaryocyte development and platelet production.
DR   ChiTaRS; ZFPM1; human.
DR   GeneWiki; ZFPM1; -.
DR   GenomeRNAi; 161882; -.
DR   NextBio; 88126; -.
DR   PRO; PR:Q8IX07; -.
DR   Proteomes; UP000005640; Chromosome 16.
DR   Bgee; Q8IX07; -.
DR   CleanEx; HS_ZFPM1; -.
DR   ExpressionAtlas; Q8IX07; baseline and differential.
DR   Genevisible; Q8IX07; HS.
DR   GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0005667; C:transcription factor complex; IDA:BHF-UCL.
DR   GO; GO:0017053; C:transcriptional repressor complex; IDA:BHF-UCL.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0001085; F:RNA polymerase II transcription factor binding; IPI:BHF-UCL.
DR   GO; GO:0008134; F:transcription factor binding; IPI:BHF-UCL.
DR   GO; GO:0001078; F:transcriptional repressor activity, RNA polymerase II core promoter proximal region sequence-specific binding; IDA:BHF-UCL.
DR   GO; GO:0060413; P:atrial septum morphogenesis; ISS:BHF-UCL.
DR   GO; GO:0003181; P:atrioventricular valve morphogenesis; ISS:BHF-UCL.
DR   GO; GO:0007596; P:blood coagulation; TAS:Reactome.
DR   GO; GO:0055008; P:cardiac muscle tissue morphogenesis; ISS:BHF-UCL.
DR   GO; GO:0060318; P:definitive erythrocyte differentiation; IEA:Ensembl.
DR   GO; GO:0035162; P:embryonic hemopoiesis; ISS:BHF-UCL.
DR   GO; GO:0030218; P:erythrocyte differentiation; ISS:BHF-UCL.
DR   GO; GO:0030851; P:granulocyte differentiation; IEA:Ensembl.
DR   GO; GO:0007507; P:heart development; IBA:GO_Central.
DR   GO; GO:0035855; P:megakaryocyte development; IEA:Ensembl.
DR   GO; GO:0030219; P:megakaryocyte differentiation; ISS:BHF-UCL.
DR   GO; GO:0003192; P:mitral valve formation; ISS:BHF-UCL.
DR   GO; GO:0045599; P:negative regulation of fat cell differentiation; ISS:BHF-UCL.
DR   GO; GO:0045403; P:negative regulation of interleukin-4 biosynthetic process; IDA:BHF-UCL.
DR   GO; GO:0060377; P:negative regulation of mast cell differentiation; ISS:BHF-UCL.
DR   GO; GO:0032091; P:negative regulation of protein binding; ISS:BHF-UCL.
DR   GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:GOC.
DR   GO; GO:0003151; P:outflow tract morphogenesis; ISS:BHF-UCL.
DR   GO; GO:0030220; P:platelet formation; IGI:BHF-UCL.
DR   GO; GO:0045078; P:positive regulation of interferon-gamma biosynthetic process; IDA:BHF-UCL.
DR   GO; GO:0060319; P:primitive erythrocyte differentiation; IEA:Ensembl.
DR   GO; GO:0032642; P:regulation of chemokine production; IEA:Ensembl.
DR   GO; GO:0010724; P:regulation of definitive erythrocyte differentiation; IDA:BHF-UCL.
DR   GO; GO:0002295; P:T-helper cell lineage commitment; IC:BHF-UCL.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
DR   GO; GO:0071733; P:transcriptional activation by promoter-enhancer looping; ISS:BHF-UCL.
DR   GO; GO:0003195; P:tricuspid valve formation; ISS:BHF-UCL.
DR   GO; GO:0060412; P:ventricular septum morphogenesis; ISS:BHF-UCL.
DR   Gene3D; 3.30.160.60; -; 2.
DR   InterPro; IPR007087; Znf_C2H2.
DR   InterPro; IPR015880; Znf_C2H2-like.
DR   InterPro; IPR013087; Znf_C2H2/integrase_DNA-bd.
DR   SMART; SM00355; ZnF_C2H2; 9.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 2.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 2.
PE   1: Evidence at protein level;
KW   3D-structure; Activator; Complete proteome; DNA-binding;
KW   Metal-binding; Nucleus; Phosphoprotein; Polymorphism;
KW   Reference proteome; Repeat; Repressor; Transcription;
KW   Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN         1   1006       Zinc finger protein ZFPM1.
FT                                /FTId=PRO_0000221041.
FT   ZN_FING     241    264       C2HC-type 1.
FT   ZN_FING     290    314       C2H2-type 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     320    342       C2H2-type 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     348    371       C2H2-type 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     577    699       C2HC-type 2.
FT   ZN_FING     683    705       C2HC-type 3.
FT   ZN_FING     817    839       C2HC-type 4.
FT   ZN_FING     854    877       C2H2-type 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     974   1000       C2HC-type 5.
FT   REGION      330    341       Interaction with TACC3. {ECO:0000250}.
FT   REGION      794    800       Interaction with CTBP2. {ECO:0000250}.
FT   MOD_RES     128    128       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:O35615}.
FT   MOD_RES     272    272       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:O35615}.
FT   MOD_RES     491    491       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:O35615}.
FT   MOD_RES     494    494       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:O35615}.
FT   MOD_RES     671    671       Phosphoserine.
FT                                {ECO:0000244|PubMed:24275569}.
FT   MOD_RES     786    786       Phosphoserine.
FT                                {ECO:0000244|PubMed:18669648,
FT                                ECO:0000244|PubMed:24275569}.
FT   MOD_RES     901    901       Phosphoserine.
FT                                {ECO:0000244|PubMed:19690332,
FT                                ECO:0000244|PubMed:24275569}.
FT   MOD_RES     909    909       Phosphoserine.
FT                                {ECO:0000244|PubMed:19690332}.
FT   MOD_RES     914    914       Phosphoserine.
FT                                {ECO:0000244|PubMed:24275569}.
FT   MOD_RES     935    935       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:O35615}.
FT   VARIANT      70     70       G -> A (in dbSNP:rs34916016).
FT                                /FTId=VAR_057491.
FT   CONFLICT     22     22       R -> G (in Ref. 1; AAN45858).
FT                                {ECO:0000305}.
FT   CONFLICT    444    447       EPLA -> AP (in Ref. 1; AAN45858).
FT                                {ECO:0000305}.
SQ   SEQUENCE   1006 AA;  104888 MW;  E9C2363503A64898 CRC64;
     MSRRKQSNPR QIKRSLGDME AREEVQLVGA SHMEQKATAP EAPSPPSADV NSPPPLPPPT
     SPGGPKELEG QEPEPRPTEE EPGSPWSGPD ELEPVVQDGQ RRIRARLSLA TGLSWGPFHG
     SVQTRASSPR QAEPSPALTL LLVDEACWLR TLPQALTEAE ANTEIHRKDD ALWCRVTKPV
     PAGGLLSVLL TAEPHSTPGH PVKKEPAEPT CPAPAHDLQL LPQQAGMASI LATAVINKDV
     FPCKDCGIWY RSERNLQAHL LYYCASRQGT GSPAAAATDE KPKETYPNER VCPFPQCRKS
     CPSASSLEIH MRSHSGERPF VCLICLSAFT TKANCERHLK VHTDTLSGVC HSCGFISTTR
     DILYSHLVTN HMVCQPGSKG EIYSPGAGHP ATKLPPDSLG SFQQQHTALQ GPLASADLGL
     APTPSPGLDR KALAEATNGE ARAEPLAQNG GSSEPPAAPR SIKVEAVEEP EAAPILGPGE
     PGPQAPSRTP SPRSPAPARV KAELSSPTPG SSPVPGELGL AGALFLPQYV FGPDAAPPAS
     EILAKMSELV HSRLQQGAGA GAGGAQTGLF PGAPKGATCF ECEITFSNVN NYYVHKRLYC
     SGRRAPEDAP AARRPKAPPG PARAPPGQPA EPDAPRSSPG PGAREEGAGG AATPEDGAGG
     RGSEGSQSPG SSVDDAEDDP SRTLCEACNI RFSRHETYTV HKRYYCASRH DPPPRRPAAP
     PGPPGPAAPP APSPAAPVRT RRRRKLYELH AAGAPPPPPP GHAPAPESPR PGSGSGSGPG
     LAPARSPGPA ADGPIDLSKK PRRPLPGAPA PALADYHECT ACRVSFHSLE AYLAHKKYSC
     PAAPPPGALG LPAAACPYCP PNGPVRGDLL EHFRLAHGLL LGAPLAGPGV EARTPADRGP
     SPAPAPAASP QPGSRGPRDG LGPEPQEPPP GPPPSPAAAP EAVPPPPAPP SYSDKGVQTP
     SKGTPAPLPN GNHRYCRLCN IKFSSLSTFI AHKKYYCSSH AAEHVK
//
ID   HDAC2_HUMAN             Reviewed;         488 AA.
AC   Q92769; B3KRS5; B4DL58; E1P561; Q5SRI8; Q5SZ86; Q8NEH4;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   21-JUN-2005, sequence version 2.
DT   11-NOV-2015, entry version 177.
DE   RecName: Full=Histone deacetylase 2;
DE            Short=HD2;
DE            EC=3.5.1.98;
GN   Name=HDAC2;
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 VARIANT CYS-230.
RC   TISSUE=Mammary gland;
RX   PubMed=8917507; DOI=10.1073/pnas.93.23.12845;
RA   Yang W.-M., Inouye C.J., Zeng Y., Bearss D., Seto E.;
RT   "Transcriptional repression by YY1 is mediated by interaction with a
RT   mammalian homolog of the yeast global regulator RPD3.";
RL   Proc. Natl. Acad. Sci. U.S.A. 93:12845-12850(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=14574404; DOI=10.1038/nature02055;
RA   Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA   Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
RA   Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
RA   Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
RA   Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
RA   Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
RA   Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
RA   Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA   Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA   Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA   Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
RA   Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
RA   Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
RA   Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
RA   Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
RA   Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
RA   Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
RA   Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
RA   Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
RA   Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
RA   Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA   Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
RA   McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
RA   Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
RA   Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
RA   Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
RA   Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
RA   Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
RA   Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
RA   Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
RA   Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
RA   Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
RA   Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
RT   "The DNA sequence and analysis of human chromosome 6.";
RL   Nature 425:805-811(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
RP   HIS-315.
RC   TISSUE=Testis;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   INTERACTION WITH ATR, AND IDENTIFICATION IN A COMPLEX CONTAINING ATR
RP   AND CHD4.
RX   PubMed=10545197; DOI=10.1021/bi991614n;
RA   Schmidt D.R., Schreiber S.L.;
RT   "Molecular association between ATR and two components of the
RT   nucleosome remodeling and deacetylating complex, HDAC2 and CHD4.";
RL   Biochemistry 38:14711-14717(1999).
RN   [7]
RP   INTERACTION WITH SNW1.
RX   PubMed=10644367; DOI=10.1128/JVI.74.4.1939-1947.2000;
RA   Zhou S., Fujimuro M., Hsieh J.J., Chen L., Hayward S.D.;
RT   "A role for SKIP in EBNA2 activation of CBF1-repressed promoters.";
RL   J. Virol. 74:1939-1947(2000).
RN   [8]
RP   INTERACTION WITH DNMT1 AND DMAP1.
RX   PubMed=10888872; DOI=10.1038/77023;
RA   Rountree M.R., Bachman K.E., Baylin S.B.;
RT   "DNMT1 binds HDAC2 and a new co-repressor, DMAP1, to form a complex at
RT   replication foci.";
RL   Nat. Genet. 25:269-277(2000).
RN   [9]
RP   REVIEW ON DEACETYLASE COMPLEXES.
RX   PubMed=10904264; DOI=10.1016/S0168-9525(00)02066-7;
RA   Ahringer J.;
RT   "NuRD and SIN3 histone deacetylase complexes in development.";
RL   Trends Genet. 16:351-356(2000).
RN   [10]
RP   INTERACTION WITH MINT.
RX   PubMed=11331609; DOI=10.1101/gad.871201;
RA   Shi Y., Downes M., Xie W., Kao H.-Y., Ordentlich P., Tsai C.-C.,
RA   Hon M., Evans R.M.;
RT   "Sharp, an inducible cofactor that integrates nuclear receptor
RT   repression and activation.";
RL   Genes Dev. 15:1140-1151(2001).
RN   [11]
RP   INTERACTION WITH CBFA2T3.
RX   PubMed=11533236; DOI=10.1128/MCB.21.19.6470-6483.2001;
RA   Amann J.M., Nip J., Strom D.K., Lutterbach B., Harada H., Lenny N.,
RA   Downing J.R., Meyers S., Hiebert S.W.;
RT   "ETO, a target of t(8;21) in acute leukemia, makes distinct contacts
RT   with multiple histone deacetylases and binds mSin3A through its
RT   oligomerization domain.";
RL   Mol. Cell. Biol. 21:6470-6483(2001).
RN   [12]
RP   INTERACTION WITH HDAC10.
RX   PubMed=11739383; DOI=10.1074/jbc.M108055200;
RA   Fischer D.D., Cai R., Bhatia U., Asselbergs F.A.M., Song C., Terry R.,
RA   Trogani N., Widmer R., Atadja P., Cohen D.;
RT   "Isolation and characterization of a novel class II histone
RT   deacetylase, HDAC10.";
RL   J. Biol. Chem. 277:6656-6666(2002).
RN   [13]
RP   INTERACTION WITH SP3.
RX   PubMed=12176973; DOI=10.1074/jbc.C200378200;
RA   Sun J.M., Chen H.Y., Moniwa M., Litchfield D.W., Seto E., Davie J.R.;
RT   "The transcriptional repressor Sp3 is associated with CK2-
RT   phosphorylated histone deacetylase 2.";
RL   J. Biol. Chem. 277:35783-35786(2002).
RN   [14]
RP   INTERACTION WITH DAXX AND DEK.
RX   PubMed=12140263;
RA   Hollenbach A.D., McPherson C.J., Mientjes E.J., Iyengar R.,
RA   Grosveld G.;
RT   "Daxx and histone deacetylase II associate with chromatin through an
RT   interaction with core histones and the chromatin-associated protein
RT   Dek.";
RL   J. Cell Sci. 115:3319-3330(2002).
RN   [15]
RP   INTERACTION WITH BCL6.
RX   PubMed=12402037; DOI=10.1038/ng1018;
RA   Bereshchenko O.R., Gu W., Dalla-Favera R.;
RT   "Acetylation inactivates the transcriptional repressor BCL6.";
RL   Nat. Genet. 32:606-613(2002).
RN   [16]
RP   INTERACTION WITH APEX1.
RX   PubMed=14633989; DOI=10.1093/emboj/cdg595;
RA   Bhakat K.K., Izumi T., Yang S.H., Hazra T.K., Mitra S.;
RT   "Role of acetylated human AP-endonuclease (APE1/Ref-1) in regulation
RT   of the parathyroid hormone gene.";
RL   EMBO J. 22:6299-6309(2003).
RN   [17]
RP   INTERACTION WITH HCFC1.
RX   PubMed=12670868; DOI=10.1101/gad.252103;
RA   Wysocka J., Myers M.P., Laherty C.D., Eisenman R.N., Herr W.;
RT   "Human Sin3 deacetylase and trithorax-related Set1/Ash2 histone H3-K4
RT   methyltransferase are tethered together selectively by the cell-
RT   proliferation factor HCF-1.";
RL   Genes Dev. 17:896-911(2003).
RN   [18]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE BHC
RP   COMPLEX WITH PHF21A; HDAC1; HMG20B; KDM1A; RCOR1; ZMYM2; ZNF217;
RP   ZMYM3; KIAA0182 AND GTF2I.
RX   PubMed=12493763; DOI=10.1074/jbc.M208992200;
RA   Hakimi M.-A., Dong Y., Lane W.S., Speicher D.W., Shiekhattar R.;
RT   "A candidate X-linked mental retardation gene is a component of a new
RT   family of histone deacetylase-containing complexes.";
RL   J. Biol. Chem. 278:7234-7239(2003).
RN   [19]
RP   IDENTIFICATION IN A MSIN3A COREPRESSOR COMPLEX WITH SIN3A; SAP130;
RP   SUDS3; ARID4B; HDAC1 AND HDAC2.
RX   PubMed=12724404; DOI=10.1128/MCB.23.10.3456-3467.2003;
RA   Fleischer T.C., Yun U.J., Ayer D.E.;
RT   "Identification and characterization of three new components of the
RT   mSin3A corepressor complex.";
RL   Mol. Cell. Biol. 23:3456-3467(2003).
RN   [20]
RP   INTERACTION WITH PELP1.
RX   PubMed=15456770; DOI=10.1074/jbc.M406831200;
RA   Choi Y.B., Ko J.K., Shin J.;
RT   "The transcriptional corepressor, PELP1, recruits HDAC2 and masks
RT   histones using two separate domains.";
RL   J. Biol. Chem. 279:50930-50941(2004).
RN   [21]
RP   INTERACTION WITH NRIP1.
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   [22]
RP   INTERACTION WITH JMJD2A.
RX   PubMed=15927959; DOI=10.1074/jbc.M413687200;
RA   Gray S.G., Iglesias A.H., Lizcano F., Villanueva R., Camelo S.,
RA   Jingu H., Teh B.T., Koibuchi N., Chin W.W., Kokkotou E., Dangond F.;
RT   "Functional characterization of JMJD2A, a histone deacetylase- and
RT   retinoblastoma-binding protein.";
RL   J. Biol. Chem. 280:28507-28518(2005).
RN   [23]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-394; SER-422 AND
RP   SER-424, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA   Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA   Mann M.;
RT   "Global, in vivo, and site-specific phosphorylation dynamics in
RT   signaling networks.";
RL   Cell 127:635-648(2006).
RN   [24]
RP   INTERACTION WITH SAP30L.
RX   PubMed=16820529; DOI=10.1093/nar/gkl401;
RA   Viiri K.M., Korkeamaeki H., Kukkonen M.K., Nieminen L.K., Lindfors K.,
RA   Peterson P., Maeki M., Kainulainen H., Lohi O.;
RT   "SAP30L interacts with members of the Sin3A corepressor complex and
RT   targets Sin3A to the nucleolus.";
RL   Nucleic Acids Res. 34:3288-3298(2006).
RN   [25]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-394, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA   Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA   Greff Z., Keri G., Stemmann O., Mann M.;
RT   "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT   the kinome across the cell cycle.";
RL   Mol. Cell 31:438-448(2008).
RN   [26]
RP   IDENTIFICATION IN A COMPLEX WITH CDYL; MIER1; MIER2 AND HDAC1.
RX   PubMed=19061646; DOI=10.1016/j.molcel.2008.10.025;
RA   Mulligan P., Westbrook T.F., Ottinger M., Pavlova N., Chang B.,
RA   Macia E., Shi Y.J., Barretina J., Liu J., Howley P.M., Elledge S.J.,
RA   Shi Y.;
RT   "CDYL bridges REST and histone methyltransferases for gene repression
RT   and suppression of cellular transformation.";
RL   Mol. Cell 32:718-726(2008).
RN   [27]
RP   INTERACTION WITH BCL6.
RX   PubMed=18212045; DOI=10.1128/MCB.01400-07;
RA   Mendez L.M., Polo J.M., Yu J.J., Krupski M., Ding B.B., Melnick A.,
RA   Ye B.H.;
RT   "CtBP is an essential corepressor for BCL6 autoregulation.";
RL   Mol. Cell. Biol. 28:2175-2186(2008).
RN   [28]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [29]
RP   INTERACTION WITH FAM64A.
RX   PubMed=18757745; DOI=10.1073/pnas.0709227105;
RA   Zhao W.M., Coppinger J.A., Seki A., Cheng X.L., Yates J.R. III,
RA   Fang G.;
RT   "RCS1, a substrate of APC/C, controls the metaphase to anaphase
RT   transition.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:13415-13420(2008).
RN   [30]
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   [31]
RP   FUNCTION, AND INTERACTION WITH TSHZ3.
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   [32]
RP   INTERACTION WITH CHFR.
RX   PubMed=19182791; DOI=10.1038/ncb1837;
RA   Oh Y.M., Kwon Y.E., Kim J.M., Bae S.J., Lee B.K., Yoo S.J.,
RA   Chung C.H., Deshaies R.J., Seol J.H.;
RT   "Chfr is linked to tumour metastasis through the downregulation of
RT   HDAC1.";
RL   Nat. Cell Biol. 11:295-302(2009).
RN   [33]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-394 AND SER-422, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA   Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA   Rodionov V., Han D.K.;
RT   "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT   reveals system-wide modulation of protein-protein interactions.";
RL   Sci. Signal. 2:RA46-RA46(2009).
RN   [34]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-394; SER-422 AND
RP   SER-424, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA   Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full
RT   phosphorylation site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [35]
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   [36]
RP   FUNCTION, AND INTERACTION WITH MTA1.
RX   PubMed=21965678; DOI=10.1074/jbc.M111.267237;
RA   Cong L., Pakala S.B., Ohshiro K., Li D.Q., Kumar R.;
RT   "SUMOylation and SUMO-interacting motif (SIM) of metastasis tumor
RT   antigen 1 (MTA1) synergistically regulate its transcriptional
RT   repressor function.";
RL   J. Biol. Chem. 286:43793-43808(2011).
RN   [37]
RP   INTERACTION WITH BEND3.
RX   PubMed=21914818; DOI=10.1242/jcs.086603;
RA   Sathyan K.M., Shen Z., Tripathi V., Prasanth K.V., Prasanth S.G.;
RT   "A BEN-domain-containing protein associates with heterochromatin and
RT   represses transcription.";
RL   J. Cell Sci. 124:3149-3163(2011).
RN   [38]
RP   INTERACTION WITH SMARCAD1.
RX   PubMed=21549307; DOI=10.1016/j.molcel.2011.02.036;
RA   Rowbotham S.P., Barki L., Neves-Costa A., Santos F., Dean W.,
RA   Hawkes N., Choudhary P., Will W.R., Webster J., Oxley D., Green C.M.,
RA   Varga-Weisz P., Mermoud J.E.;
RT   "Maintenance of silent chromatin through replication requires SWI/SNF-
RT   like chromatin remodeler SMARCAD1.";
RL   Mol. Cell 42:285-296(2011).
RN   [39]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-394; SER-422 AND
RP   SER-424, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   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   [40]
RP   INTERACTION WITH NACC2.
RX   PubMed=22926524; DOI=10.1038/onc.2012.386;
RA   Xuan C., Wang Q., Han X., Duan Y., Li L., Shi L., Wang Y., Shan L.,
RA   Yao Z., Shang Y.;
RT   "RBB, a novel transcription repressor, represses the transcription of
RT   HDM2 oncogene.";
RL   Oncogene 32:3711-3721(2013).
RN   [41]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-394; SER-422 AND
RP   SER-424, 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   [42]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-462, 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).
RN   [43]
RP   SUBCELLULAR LOCATION, AND INTERACTION WITH MTA1.
RX   PubMed=24970816;
RA   Liu J., Xu D., Wang H., Zhang Y., Chang Y., Zhang J., Wang J., Li C.,
RA   Liu H., Zhao M., Lin C., Zhan Q., Huang C., Qian H.;
RT   "The subcellular distribution and function of MTA1 in cancer
RT   differentiation.";
RL   Oncotarget 5:5153-5164(2014).
RN   [44]
RP   X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 9-374 IN COMPLEX WITH
RP   SUBSTITUTED N-(2-AMINOPHENYL)BENZAMIDE INHIBITORS.
RX   PubMed=20392638; DOI=10.1016/j.bmcl.2010.03.091;
RA   Bressi J.C., Jennings A.J., Skene R., Wu Y., Melkus R., De Jong R.,
RA   O'Connell S., Grimshaw C.E., Navre M., Gangloff A.R.;
RT   "Exploration of the HDAC2 foot pocket: Synthesis and SAR of
RT   substituted N-(2-aminophenyl)benzamides.";
RL   Bioorg. Med. Chem. Lett. 20:3142-3145(2010).
CC   -!- FUNCTION: Responsible for the deacetylation of lysine residues on
CC       the N-terminal part of the core histones (H2A, H2B, H3 and H4).
CC       Histone deacetylation gives a tag for epigenetic repression and
CC       plays an important role in transcriptional regulation, cell cycle
CC       progression and developmental events. Histone deacetylases act via
CC       the formation of large multiprotein complexes. Forms
CC       transcriptional repressor complexes by associating with MAD, SIN3,
CC       YY1 and N-COR. Interacts in the late S-phase of DNA-replication
CC       with DNMT1 in the other transcriptional repressor complex composed
CC       of DNMT1, DMAP1, PCNA, CAF1. Deacetylates TSHZ3 and regulates its
CC       transcriptional repressor activity. Component of a
CC       RCOR/GFI/KDM1A/HDAC complex that suppresses, via histone
CC       deacetylase (HDAC) recruitment, a number of genes implicated in
CC       multilineage blood cell development. May be involved in the
CC       transcriptional repression of circadian target genes, such as
CC       PER1, mediated by CRY1 through histone deacetylation. Involved in
CC       MTA1-mediated transcriptional corepression of TFF1 and CDKN1A.
CC       {ECO:0000269|PubMed:19343227, ECO:0000269|PubMed:21965678}.
CC   -!- CATALYTIC ACTIVITY: Hydrolysis of an N(6)-acetyl-lysine residue of
CC       a histone to yield a deacetylated histone.
CC   -!- SUBUNIT: Part of the core histone deacetylase (HDAC) complex
CC       composed of HDAC1, HDAC2, RBBP4 and RBBP7. The core complex
CC       associates with MTA2, MBD3, MTA1L1, CHD3 and CHD4 to form the
CC       nucleosome remodeling and histone deacetylation (NuRD) complex, or
CC       with SIN3, SAP18 and SAP30 to form the SIN3 HDAC complex.
CC       Component of a RCOR/GFI/KDM1A/HDAC complex. Interacts directly
CC       with GFI1 and GFI1B. Interacts with SNW1, HDAC7, PRDM6, SAP30,
CC       SETDB1 and SUV39H1. Interacts with the H2AFY (via the non-histone
CC       region). Component of a BHC histone deacetylase complex that
CC       contains HDAC1, HDAC2, HMG20B, KDM1A, RCOR1 and PHF21A. The BHC
CC       complex may also contain ZMYM2, ZNF217, ZMYM3, GSE1 and GTF2I.
CC       Part of a complex containing the core histones H2A, H2B, H3 and
CC       H4, DEK and unphosphorylated DAXX. Part of a complex containing
CC       ATR and CHD4. Forms a heterologous complex at least with YY1.
CC       Interacts with ATR, CBFA2T3, DNMT1, MINT, HDAC10, HCFC1, NRIP1,
CC       KDM4A and PELP1. Component of a mSin3A corepressor complex that
CC       contains SIN3A, SAP130, SUDS3, ARID4B, HDAC1 and HDAC2. Interacts
CC       with CHFR and SAP30L. Interacts (CK2 phosphorylated form) with
CC       SP3. Interacts with TSHZ3 (via its N-terminus). Interacts with
CC       APEX1; the interaction is not dependent on the acetylated status
CC       of APEX1. Part of a complex composed of TRIM28, HDAC1, HDAC2 and
CC       EHMT2. Interacts with FAM64A. Interacts with BCL6 (non-acetylated
CC       form). Part of a complex containing at least CDYL, MIER1, MIER2,
CC       HDAC1 and HDAC2. Interacts with CRY1, INSM1 and ZNF431. Interacts
CC       with NACC2. Interacts with MTA1, with a preference for sumoylated
CC       MTA1. Interacts with SIX3 (By similarity). Interacts with BEND3.
CC       {ECO:0000250|UniProtKB:P70288, ECO:0000269|PubMed:10545197,
CC       ECO:0000269|PubMed:10644367, ECO:0000269|PubMed:10888872,
CC       ECO:0000269|PubMed:11331609, ECO:0000269|PubMed:11533236,
CC       ECO:0000269|PubMed:11739383, ECO:0000269|PubMed:12140263,
CC       ECO:0000269|PubMed:12176973, ECO:0000269|PubMed:12402037,
CC       ECO:0000269|PubMed:12493763, ECO:0000269|PubMed:12670868,
CC       ECO:0000269|PubMed:12724404, ECO:0000269|PubMed:14633989,
CC       ECO:0000269|PubMed:15060175, ECO:0000269|PubMed:15456770,
CC       ECO:0000269|PubMed:15927959, ECO:0000269|PubMed:16820529,
CC       ECO:0000269|PubMed:18212045, ECO:0000269|PubMed:18757745,
CC       ECO:0000269|PubMed:19061646, ECO:0000269|PubMed:19182791,
CC       ECO:0000269|PubMed:19343227, ECO:0000269|PubMed:20392638,
CC       ECO:0000269|PubMed:21549307, ECO:0000269|PubMed:21914818,
CC       ECO:0000269|PubMed:21965678, ECO:0000269|PubMed:22926524,
CC       ECO:0000269|PubMed:24970816}.
CC   -!- INTERACTION:
CC       Q9C0K0:BCL11B; NbExp=3; IntAct=EBI-301821, EBI-6597578;
CC       Q9HCU9:BRMS1; NbExp=4; IntAct=EBI-301821, EBI-714781;
CC       Q9UER7:DAXX; NbExp=2; IntAct=EBI-301821, EBI-77321;
CC       P51610:HCFC1; NbExp=2; IntAct=EBI-301821, EBI-396176;
CC       Q13547:HDAC1; NbExp=10; IntAct=EBI-301821, EBI-301834;
CC       Q2HR82:K8 (xeno); NbExp=7; IntAct=EBI-301821, EBI-9006943;
CC       Q9UIS9:MBD1; NbExp=2; IntAct=EBI-301821, EBI-867196;
CC       Q13330:MTA1; NbExp=4; IntAct=EBI-301821, EBI-714236;
CC       P01106:MYC; NbExp=2; IntAct=EBI-301821, EBI-447544;
CC       P06748:NPM1; NbExp=2; IntAct=EBI-301821, EBI-78579;
CC       P48382:RFX5; NbExp=4; IntAct=EBI-301821, EBI-923266;
CC       Q96ST3:SIN3A; NbExp=5; IntAct=EBI-301821, EBI-347218;
CC       O95863:SNAI1; NbExp=2; IntAct=EBI-301821, EBI-1045459;
CC       Q9HD15:SRA1; NbExp=2; IntAct=EBI-301821, EBI-727136;
CC       O43463:SUV39H1; NbExp=3; IntAct=EBI-301821, EBI-349968;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:24970816}.
CC       Cytoplasm {ECO:0000269|PubMed:24970816}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q92769-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q92769-3; Sequence=VSP_056175;
CC         Note=No experimental confirmation available.;
CC   -!- TISSUE SPECIFICITY: Widely expressed; lower levels in brain and
CC       lung.
CC   -!- PTM: S-nitrosylated by GAPDH. In neurons, S-Nitrosylation at Cys-
CC       262 and Cys-274 does not affect the enzyme activity but abolishes
CC       chromatin-binding, leading to increases acetylation of histones
CC       and activate genes that are associated with neuronal development.
CC       In embryonic cortical neurons, S-Nitrosylation regulates dendritic
CC       growth and branching. S-Nitrosylation interferes with its
CC       interaction with MTA1 (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the histone deacetylase family. HD type 1
CC       subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH31055.2; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
CC       Sequence=BAG59420.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
CC   -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC       and Haematology;
CC       URL="http://atlasgeneticsoncology.org/Genes/HDAC2ID40803ch6q22.html";
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DR   EMBL; U31814; AAC50814.1; -; mRNA.
DR   EMBL; AK092156; BAG52487.1; -; mRNA.
DR   EMBL; AK296856; BAG59420.1; ALT_INIT; mRNA.
DR   EMBL; AL590398; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL671967; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; FO393415; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471051; EAW48252.1; -; Genomic_DNA.
DR   EMBL; CH471051; EAW48253.1; -; Genomic_DNA.
DR   EMBL; CH471051; EAW48254.1; -; Genomic_DNA.
DR   EMBL; CH471051; EAW48255.1; -; Genomic_DNA.
DR   EMBL; BC031055; AAH31055.2; ALT_INIT; mRNA.
DR   CCDS; CCDS43493.2; -. [Q92769-1]
DR   RefSeq; NP_001518.3; NM_001527.3. [Q92769-1]
DR   RefSeq; XP_011534090.1; XM_011535788.1. [Q92769-3]
DR   UniGene; Hs.3352; -.
DR   PDB; 3MAX; X-ray; 2.05 A; A/B/C=9-374.
DR   PDB; 4LXZ; X-ray; 1.85 A; A/B/C=8-376.
DR   PDB; 4LY1; X-ray; 1.57 A; A/B/C=8-376.
DR   PDBsum; 3MAX; -.
DR   PDBsum; 4LXZ; -.
DR   PDBsum; 4LY1; -.
DR   ProteinModelPortal; Q92769; -.
DR   SMR; Q92769; 9-376.
DR   BioGrid; 109316; 293.
DR   DIP; DIP-24220N; -.
DR   IntAct; Q92769; 112.
DR   MINT; MINT-90593; -.
DR   STRING; 9606.ENSP00000430432; -.
DR   BindingDB; Q92769; -.
DR   ChEMBL; CHEMBL2093865; -.
DR   DrugBank; DB01223; Aminophylline.
DR   DrugBank; DB00227; Lovastatin.
DR   DrugBank; DB01303; Oxtriphylline.
DR   DrugBank; DB00277; Theophylline.
DR   DrugBank; DB00313; Valproic Acid.
DR   DrugBank; DB02546; Vorinostat.
DR   GuidetoPHARMACOLOGY; 2616; -.
DR   PhosphoSite; Q92769; -.
DR   BioMuta; HDAC2; -.
DR   DMDM; 68068066; -.
DR   MaxQB; Q92769; -.
DR   PaxDb; Q92769; -.
DR   PRIDE; Q92769; -.
DR   DNASU; 3066; -.
DR   Ensembl; ENST00000368632; ENSP00000357621; ENSG00000196591. [Q92769-3]
DR   Ensembl; ENST00000519065; ENSP00000430432; ENSG00000196591. [Q92769-1]
DR   Ensembl; ENST00000519108; ENSP00000430008; ENSG00000196591. [Q92769-3]
DR   GeneID; 3066; -.
DR   KEGG; hsa:3066; -.
DR   UCSC; uc003pwc.2; human. [Q92769-1]
DR   CTD; 3066; -.
DR   GeneCards; HDAC2; -.
DR   HGNC; HGNC:4853; HDAC2.
DR   HPA; CAB005054; -.
DR   HPA; HPA011727; -.
DR   MIM; 605164; gene.
DR   neXtProt; NX_Q92769; -.
DR   PharmGKB; PA29227; -.
DR   eggNOG; KOG1342; Eukaryota.
DR   eggNOG; COG0123; LUCA.
DR   GeneTree; ENSGT00530000062889; -.
DR   HOGENOM; HOG000225180; -.
DR   HOVERGEN; HBG057112; -.
DR   InParanoid; Q92769; -.
DR   KO; K06067; -.
DR   OMA; ACPSPRD; -.
DR   PhylomeDB; Q92769; -.
DR   TreeFam; TF106171; -.
DR   BRENDA; 3.5.1.98; 2681.
DR   Reactome; R-HSA-193670; p75NTR negatively regulates cell cycle via SC1.
DR   Reactome; R-HSA-2122947; NOTCH1 Intracellular Domain Regulates Transcription.
DR   Reactome; R-HSA-2644606; Constitutive Signaling by NOTCH1 PEST Domain Mutants.
DR   Reactome; R-HSA-2894862; Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
DR   Reactome; R-HSA-3214815; HDACs deacetylate histones.
DR   Reactome; R-HSA-427413; NoRC negatively regulates rRNA expression.
DR   Reactome; R-HSA-73762; RNA Polymerase I Transcription Initiation.
DR   Reactome; R-HSA-983231; Factors involved in megakaryocyte development and platelet production.
DR   SABIO-RK; Q92769; -.
DR   ChiTaRS; HDAC2; human.
DR   EvolutionaryTrace; Q92769; -.
DR   GeneWiki; Histone_deacetylase_2; -.
DR   GenomeRNAi; 3066; -.
DR   NextBio; 12129; -.
DR   PRO; PR:Q92769; -.
DR   Proteomes; UP000005640; Chromosome 6.
DR   Bgee; Q92769; -.
DR   CleanEx; HS_HDAC2; -.
DR   ExpressionAtlas; Q92769; baseline and differential.
DR   Genevisible; Q92769; HS.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0035098; C:ESC/E(Z) complex; IDA:UniProtKB.
DR   GO; GO:0000790; C:nuclear chromatin; IDA:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0016581; C:NuRD complex; IDA:UniProtKB.
DR   GO; GO:0043234; C:protein complex; IDA:UniProtKB.
DR   GO; GO:0016580; C:Sin3 complex; IDA:UniProtKB.
DR   GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR   GO; GO:0001047; F:core promoter binding; IEA:Ensembl.
DR   GO; GO:0019213; F:deacetylase activity; ISS:UniProtKB.
DR   GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
DR   GO; GO:0004407; F:histone deacetylase activity; IDA:BHF-UCL.
DR   GO; GO:0032041; F:NAD-dependent histone deacetylase activity (H3-K14 specific); IEA:UniProtKB-EC.
DR   GO; GO:0051059; F:NF-kappaB binding; IPI:UniProtKB.
DR   GO; GO:0044822; F:poly(A) RNA binding; IDA:UniProtKB.
DR   GO; GO:0033558; F:protein deacetylase activity; IMP:BHF-UCL.
DR   GO; GO:0001103; F:RNA polymerase II repressing transcription factor binding; IPI:BHF-UCL.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IDA:BHF-UCL.
DR   GO; GO:0008134; F:transcription factor binding; IPI:BHF-UCL.
DR   GO; GO:0043044; P:ATP-dependent chromatin remodeling; IDA:UniProtKB.
DR   GO; GO:0048149; P:behavioral response to ethanol; IEA:Ensembl.
DR   GO; GO:0007596; P:blood coagulation; TAS:Reactome.
DR   GO; GO:0003300; P:cardiac muscle hypertrophy; IEA:Ensembl.
DR   GO; GO:1903351; P:cellular response to dopamine; IEA:Ensembl.
DR   GO; GO:0034605; P:cellular response to heat; IEA:Ensembl.
DR   GO; GO:0070301; P:cellular response to hydrogen peroxide; IEA:Ensembl.
DR   GO; GO:0071300; P:cellular response to retinoic acid; IEA:Ensembl.
DR   GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; IEA:Ensembl.
DR   GO; GO:0006325; P:chromatin organization; TAS:Reactome.
DR   GO; GO:0006338; P:chromatin remodeling; IC:BHF-UCL.
DR   GO; GO:0032922; P:circadian regulation of gene expression; ISS:UniProtKB.
DR   GO; GO:0016358; P:dendrite development; ISS:UniProtKB.
DR   GO; GO:0042733; P:embryonic digit morphogenesis; ISS:BHF-UCL.
DR   GO; GO:0009913; P:epidermal cell differentiation; ISS:BHF-UCL.
DR   GO; GO:0061029; P:eyelid development in camera-type eye; ISS:BHF-UCL.
DR   GO; GO:0061198; P:fungiform papilla formation; ISS:BHF-UCL.
DR   GO; GO:0010467; P:gene expression; TAS:Reactome.
DR   GO; GO:0060789; P:hair follicle placode formation; ISS:BHF-UCL.
DR   GO; GO:0016575; P:histone deacetylation; IMP:BHF-UCL.
DR   GO; GO:0070932; P:histone H3 deacetylation; ISS:UniProtKB.
DR   GO; GO:0070933; P:histone H4 deacetylation; ISS:UniProtKB.
DR   GO; GO:0006344; P:maintenance of chromatin silencing; IMP:BHF-UCL.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; ISS:BHF-UCL.
DR   GO; GO:0045786; P:negative regulation of cell cycle; TAS:Reactome.
DR   GO; GO:0061000; P:negative regulation of dendritic spine development; IEA:Ensembl.
DR   GO; GO:0043392; P:negative regulation of DNA binding; IEA:Ensembl.
DR   GO; GO:0045814; P:negative regulation of gene expression, epigenetic; TAS:Reactome.
DR   GO; GO:0045347; P:negative regulation of MHC class II biosynthetic process; IC:BHF-UCL.
DR   GO; GO:0010977; P:negative regulation of neuron projection development; ISS:BHF-UCL.
DR   GO; GO:2000757; P:negative regulation of peptidyl-lysine acetylation; IEA:Ensembl.
DR   GO; GO:0043433; P:negative regulation of sequence-specific DNA binding transcription factor activity; IMP:BHF-UCL.
DR   GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IMP:BHF-UCL.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:BHF-UCL.
DR   GO; GO:0048011; P:neurotrophin TRK receptor signaling pathway; TAS:Reactome.
DR   GO; GO:0042475; P:odontogenesis of dentin-containing tooth; ISS:BHF-UCL.
DR   GO; GO:0008284; P:positive regulation of cell proliferation; IMP:BHF-UCL.
DR   GO; GO:0032967; P:positive regulation of collagen biosynthetic process; IC:BHF-UCL.
DR   GO; GO:0010718; P:positive regulation of epithelial to mesenchymal transition; IEA:Ensembl.
DR   GO; GO:0032732; P:positive regulation of interleukin-1 production; IEA:Ensembl.
DR   GO; GO:0048714; P:positive regulation of oligodendrocyte differentiation; IEA:Ensembl.
DR   GO; GO:0045862; P:positive regulation of proteolysis; IMP:BHF-UCL.
DR   GO; GO:0010870; P:positive regulation of receptor biosynthetic process; IMP:BHF-UCL.
DR   GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IMP:BHF-UCL.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IC:BHF-UCL.
DR   GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IEA:Ensembl.
DR   GO; GO:0042517; P:positive regulation of tyrosine phosphorylation of Stat3 protein; IEA:Ensembl.
DR   GO; GO:0040029; P:regulation of gene expression, epigenetic; TAS:Reactome.
DR   GO; GO:0001975; P:response to amphetamine; IEA:Ensembl.
DR   GO; GO:0031000; P:response to caffeine; IEA:Ensembl.
DR   GO; GO:0042220; P:response to cocaine; IEA:Ensembl.
DR   GO; GO:0042493; P:response to drug; IEA:Ensembl.
DR   GO; GO:0055093; P:response to hyperoxia; IEA:Ensembl.
DR   GO; GO:0032496; P:response to lipopolysaccharide; IEA:Ensembl.
DR   GO; GO:0035094; P:response to nicotine; IEA:Ensembl.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.800.20; -; 1.
DR   InterPro; IPR000286; His_deacetylse.
DR   InterPro; IPR003084; His_deacetylse_1.
DR   InterPro; IPR023801; His_deacetylse_dom.
DR   PANTHER; PTHR10625; PTHR10625; 1.
DR   Pfam; PF00850; Hist_deacetyl; 1.
DR   PIRSF; PIRSF037913; His_deacetylse_1; 1.
DR   PRINTS; PR01270; HDASUPER.
DR   PRINTS; PR01271; HISDACETLASE.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative splicing; Biological rhythms;
KW   Chromatin regulator; Complete proteome; Cytoplasm; Hydrolase;
KW   Isopeptide bond; Nucleus; Phosphoprotein; Polymorphism;
KW   Reference proteome; Repressor; S-nitrosylation; Transcription;
KW   Transcription regulation; Ubl conjugation.
FT   CHAIN         1    488       Histone deacetylase 2.
FT                                /FTId=PRO_0000114693.
FT   REGION        9    322       Histone deacetylase.
FT   COMPBIAS    300    303       Poly-Gly.
FT   ACT_SITE    142    142       {ECO:0000250}.
FT   MOD_RES     262    262       S-nitrosocysteine.
FT                                {ECO:0000250|UniProtKB:P70288}.
FT   MOD_RES     274    274       S-nitrosocysteine.
FT                                {ECO:0000250|UniProtKB:P70288}.
FT   MOD_RES     394    394       Phosphoserine.
FT                                {ECO:0000244|PubMed:17081983,
FT                                ECO:0000244|PubMed:18691976,
FT                                ECO:0000244|PubMed:19690332,
FT                                ECO:0000244|PubMed:20068231,
FT                                ECO:0000244|PubMed:21406692,
FT                                ECO:0000244|PubMed:24275569}.
FT   MOD_RES     422    422       Phosphoserine.
FT                                {ECO:0000244|PubMed:17081983,
FT                                ECO:0000244|PubMed:19690332,
FT                                ECO:0000244|PubMed:20068231,
FT                                ECO:0000244|PubMed:21406692,
FT                                ECO:0000244|PubMed:24275569}.
FT   MOD_RES     424    424       Phosphoserine.
FT                                {ECO:0000244|PubMed:17081983,
FT                                ECO:0000244|PubMed:20068231,
FT                                ECO:0000244|PubMed:21406692,
FT                                ECO:0000244|PubMed:24275569}.
FT   CROSSLNK    462    462       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:25218447}.
FT   VAR_SEQ       1     30       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:14702039}.
FT                                /FTId=VSP_056175.
FT   VARIANT     230    230       R -> C (in dbSNP:rs1042903).
FT                                {ECO:0000269|PubMed:8917507}.
FT                                /FTId=VAR_025311.
FT   VARIANT     315    315       Y -> H (in dbSNP:rs17852888).
FT                                {ECO:0000269|PubMed:15489334}.
FT                                /FTId=VAR_025312.
FT   CONFLICT     93     94       QR -> HI (in Ref. 1; AAC50814).
FT                                {ECO:0000305}.
FT   CONFLICT    103    103       V -> A (in Ref. 1; AAC50814).
FT                                {ECO:0000305}.
FT   CONFLICT    146    146       S -> Y (in Ref. 1; AAC50814).
FT                                {ECO:0000305}.
FT   CONFLICT    248    248       K -> M (in Ref. 2; BAG59420).
FT                                {ECO:0000305}.
FT   CONFLICT    281    281       G -> D (in Ref. 2; BAG59420).
FT                                {ECO:0000305}.
FT   STRAND       12     15       {ECO:0000244|PDB:4LY1}.
FT   HELIX        20     22       {ECO:0000244|PDB:4LY1}.
FT   HELIX        34     45       {ECO:0000244|PDB:4LY1}.
FT   HELIX        48     51       {ECO:0000244|PDB:4LY1}.
FT   STRAND       52     55       {ECO:0000244|PDB:4LY1}.
FT   HELIX        62     65       {ECO:0000244|PDB:4LY1}.
FT   TURN         66     68       {ECO:0000244|PDB:4LY1}.
FT   HELIX        71     79       {ECO:0000244|PDB:4LY1}.
FT   TURN         82     84       {ECO:0000244|PDB:4LY1}.
FT   HELIX        85     88       {ECO:0000244|PDB:4LY1}.
FT   HELIX        89     95       {ECO:0000244|PDB:4LY1}.
FT   STRAND       98    101       {ECO:0000244|PDB:4LY1}.
FT   HELIX       107    126       {ECO:0000244|PDB:4LY1}.
FT   STRAND      131    135       {ECO:0000244|PDB:4LY1}.
FT   HELIX       156    164       {ECO:0000244|PDB:4LY1}.
FT   TURN        165    167       {ECO:0000244|PDB:4LY1}.
FT   STRAND      171    175       {ECO:0000244|PDB:4LY1}.
FT   STRAND      177    179       {ECO:0000244|PDB:4LY1}.
FT   HELIX       182    187       {ECO:0000244|PDB:4LY1}.
FT   TURN        188    190       {ECO:0000244|PDB:4LY1}.
FT   STRAND      192    201       {ECO:0000244|PDB:4LY1}.
FT   HELIX       218    220       {ECO:0000244|PDB:4LY1}.
FT   STRAND      224    229       {ECO:0000244|PDB:4LY1}.
FT   HELIX       235    253       {ECO:0000244|PDB:4LY1}.
FT   STRAND      256    261       {ECO:0000244|PDB:4LY1}.
FT   HELIX       264    266       {ECO:0000244|PDB:4LY1}.
FT   HELIX       279    291       {ECO:0000244|PDB:4LY1}.
FT   STRAND      296    299       {ECO:0000244|PDB:4LY1}.
FT   HELIX       306    320       {ECO:0000244|PDB:4LY1}.
FT   HELIX       335    338       {ECO:0000244|PDB:4LY1}.
FT   TURN        339    341       {ECO:0000244|PDB:4LY1}.
FT   STRAND      343    345       {ECO:0000244|PDB:4LY1}.
FT   HELIX       357    371       {ECO:0000244|PDB:4LY1}.
SQ   SEQUENCE   488 AA;  55364 MW;  775419CCCDAE07FA CRC64;
     MAYSQGGGKK KVCYYYDGDI GNYYYGQGHP MKPHRIRMTH NLLLNYGLYR KMEIYRPHKA
     TAEEMTKYHS DEYIKFLRSI RPDNMSEYSK QMQRFNVGED CPVFDGLFEF CQLSTGGSVA
     GAVKLNRQQT DMAVNWAGGL HHAKKSEASG FCYVNDIVLA ILELLKYHQR VLYIDIDIHH
     GDGVEEAFYT TDRVMTVSFH KYGEYFPGTG DLRDIGAGKG KYYAVNFPMR DGIDDESYGQ
     IFKPIISKVM EMYQPSAVVL QCGADSLSGD RLGCFNLTVK GHAKCVEVVK TFNLPLLMLG
     GGGYTIRNVA RCWTYETAVA LDCEIPNELP YNDYFEYFGP DFKLHISPSN MTNQNTPEYM
     EKIKQRLFEN LRMLPHAPGV QMQAIPEDAV HEDSGDEDGE DPDKRISIRA SDKRIACDEE
     FSDSEDEGEG GRRNVADHKK GAKKARIEED KKETEDKKTD VKEEDKSKDN SGEKTDTKGT
     KSEQLSNP
//
ID   HIC1_HUMAN              Reviewed;         733 AA.
AC   Q14526; D3DTI4;
DT   02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 5.
DT   11-NOV-2015, entry version 147.
DE   RecName: Full=Hypermethylated in cancer 1 protein;
DE            Short=Hic-1;
DE   AltName: Full=Zinc finger and BTB domain-containing protein 29;
GN   Name=HIC1; Synonyms=ZBTB29;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 2), AND VARIANT GLY-725.
RX   PubMed=7585125; DOI=10.1038/nm0695-570;
RA   Wales M.M., Biel M.A., el Deiry W., Nelkin B.D., Issa J.-P.,
RA   Cavenee W.K., Kuerbitz S.J., Baylin S.B.;
RT   "p53 activates expression of HIC-1, a new candidate tumour suppressor
RT   gene on 17p13.3.";
RL   Nat. Med. 1:570-577(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16625196; DOI=10.1038/nature04689;
RA   Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA   Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA   Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA   Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA   DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R.,
RA   Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
RA   Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
RA   Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
RA   Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
RA   Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
RA   Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
RA   Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA   Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA   Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT   "DNA sequence of human chromosome 17 and analysis of rearrangement in
RT   the human lineage.";
RL   Nature 440:1045-1049(2006).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   SELF-ASSOCIATION.
RX   PubMed=10611298; DOI=10.1073/pnas.96.26.14831;
RA   Deltour S., Guerardel C., Leprince D.;
RT   "Recruitment of SMRT/N-CoR-mSin3A-HDAC-repressing complexes is not a
RT   general mechanism for BTB/POZ transcriptional repressors: the case of
RT   HIC-1 and gammaFBP-B.";
RL   Proc. Natl. Acad. Sci. U.S.A. 96:14831-14836(1999).
RN   [5]
RP   ALTERNATIVE SPLICING, INTERACTION WITH HIC2, AND SUBCELLULAR LOCATION.
RX   PubMed=11554746; DOI=10.1006/bbrc.2001.5624;
RA   Deltour S., Pinte S., Guerardel C., Leprince D.;
RT   "Characterization of HRG22, a human homologue of the putative tumor
RT   suppressor gene HIC1.";
RL   Biochem. Biophys. Res. Commun. 287:427-434(2001).
RN   [6]
RP   FUNCTION, SELF-ASSOCIATION, AND INTERACTION WITH CTBP1.
RX   PubMed=12052894; DOI=10.1128/MCB.22.13.4890-4901.2002;
RA   Deltour S., Pinte S., Guerardel C., Wasylyk B., Leprince D.;
RT   "The human candidate tumor suppressor gene HIC1 recruits CtBP through
RT   a degenerate GLDLSKK motif.";
RL   Mol. Cell. Biol. 22:4890-4901(2002).
RN   [7]
RP   FUNCTION, DNA-BINDING, AND MUTAGENESIS OF CYS-540.
RX   PubMed=15231840; DOI=10.1074/jbc.M401610200;
RA   Pinte S., Stankovic-Valentin N., Deltour S., Rood B.R., Guerardel C.,
RA   Leprince D.;
RT   "The tumor suppressor gene HIC1 (hypermethylated in cancer 1) is a
RT   sequence-specific transcriptional repressor: definition of its
RT   consensus binding sequence and analysis of its DNA binding and
RT   repressive properties.";
RL   J. Biol. Chem. 279:38313-38324(2004).
RN   [8]
RP   FUNCTION.
RX   PubMed=16269335; DOI=10.1016/j.cell.2005.08.011;
RA   Chen W.Y., Wang D.H., Yen R.C., Luo J., Gu W., Baylin S.B.;
RT   "Tumor suppressor HIC1 directly regulates SIRT1 to modulate p53-
RT   dependent DNA-damage responses.";
RL   Cell 123:437-448(2005).
RN   [9]
RP   FUNCTION.
RX   PubMed=16690027; DOI=10.1016/j.bbrc.2006.04.052;
RA   Briones V.R., Chen S., Riegel A.T., Lechleider R.J.;
RT   "Mechanism of fibroblast growth factor-binding protein 1 repression by
RT   TGF-beta.";
RL   Biochem. Biophys. Res. Commun. 345:595-601(2006).
RN   [10]
RP   FUNCTION IN WNT SIGNALING, AND INTERACTION WITH TCF7L2.
RX   PubMed=16724116; DOI=10.1038/sj.emboj.7601147;
RA   Valenta T., Lukas J., Doubravska L., Fafilek B., Korinek V.;
RT   "HIC1 attenuates Wnt signaling by recruitment of TCF-4 and beta-
RT   catenin to the nuclear bodies.";
RL   EMBO J. 25:2326-2337(2006).
RN   [11]
RP   INTERACTION WITH CTBP1 AND CTBP2, AND MUTAGENESIS OF LEU-244.
RX   PubMed=16762039; DOI=10.1111/j.1742-4658.2006.05301.x;
RA   Stankovic-Valentin N., Verger A., Deltour-Balerdi S., Quinlan K.G.,
RA   Crossley M., Leprince D.;
RT   "A L225A substitution in the human tumour suppressor HIC1 abolishes
RT   its interaction with the corepressor CtBP.";
RL   FEBS J. 273:2879-2890(2006).
RN   [12]
RP   SUMOYLATION AT LYS-333, ACETYLATION AT LYS-333, AND MUTAGENESIS OF
RP   LYS-333; GLU-335 AND PRO-336.
RX   PubMed=17283066; DOI=10.1128/MCB.01098-06;
RA   Stankovic-Valentin N., Deltour S., Seeler J., Pinte S., Vergoten G.,
RA   Guerardel C., Dejean A., Leprince D.;
RT   "An acetylation/deacetylation-SUMOylation switch through a
RT   phylogenetically conserved psiKXEP motif in the tumor suppressor HIC1
RT   regulates transcriptional repression activity.";
RL   Mol. Cell. Biol. 27:2661-2675(2007).
RN   [13]
RP   FUNCTION, AND INTERACTION WITH CTBP1.
RX   PubMed=17213307; DOI=10.1073/pnas.0610590104;
RA   Zhang Q., Wang S.Y., Fleuriel C., Leprince D., Rocheleau J.V.,
RA   Piston D.W., Goodman R.H.;
RT   "Metabolic regulation of SIRT1 transcription via a HIC1:CtBP
RT   corepressor complex.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:829-833(2007).
RN   [14]
RP   FUNCTION.
RX   PubMed=18347096; DOI=10.1101/gad.1640908;
RA   Briggs K.J., Corcoran-Schwartz I.M., Zhang W., Harcke T.,
RA   Devereux W.L., Baylin S.B., Eberhart C.G., Watkins D.N.;
RT   "Cooperation between the Hic1 and Ptch1 tumor suppressors in
RT   medulloblastoma.";
RL   Genes Dev. 22:770-785(2008).
RN   [15]
RP   ERRATUM.
RA   Briggs K.J., Corcoran-Schwartz I.M., Zhang W., Harcke T.,
RA   Devereux W.L., Baylin S.B., Eberhart C.G., Watkins D.N.;
RL   Genes Dev. 22:1410-1410(2008).
RN   [16]
RP   FUNCTION, AND INTERACTION WITH ARID1A.
RX   PubMed=19486893; DOI=10.1016/j.bbrc.2009.05.115;
RA   Van Rechem C., Boulay G., Leprince D.;
RT   "HIC1 interacts with a specific subunit of SWI/SNF complexes,
RT   ARID1A/BAF250A.";
RL   Biochem. Biophys. Res. Commun. 385:586-590(2009).
RN   [17]
RP   FUNCTION.
RX   PubMed=19525223; DOI=10.1074/jbc.M109.022350;
RA   Van Rechem C., Rood B.R., Touka M., Pinte S., Jenal M., Guerardel C.,
RA   Ramsey K., Monte D., Begue A., Tschan M.P., Stephan D.A., Leprince D.;
RT   "Scavenger chemokine (CXC motif) receptor 7 (CXCR7) is a direct target
RT   gene of HIC1 (hypermethylated in cancer 1).";
RL   J. Biol. Chem. 284:20927-20935(2009).
RN   [18]
RP   FUNCTION, INTERACTION WITH MTA1 AND MBD3, AND MUTAGENESIS OF LYS-333;
RP   GLU-335 AND PRO-336.
RX   PubMed=20547755; DOI=10.1128/MCB.00582-09;
RA   Van Rechem C., Boulay G., Pinte S., Stankovic-Valentin N.,
RA   Guerardel C., Leprince D.;
RT   "Differential regulation of HIC1 target genes by CtBP and NuRD, via an
RT   acetylation/SUMOylation switch, in quiescent versus proliferating
RT   cells.";
RL   Mol. Cell. Biol. 30:4045-4059(2010).
RN   [19]
RP   FUNCTION.
RX   PubMed=20154726; DOI=10.1038/onc.2010.12;
RA   Zhang W., Zeng X., Briggs K.J., Beaty R., Simons B., Chiu Yen R.W.,
RA   Tyler M.A., Tsai H.C., Ye Y., Gesell G.S., Herman J.G., Baylin S.B.,
RA   Watkins D.N.;
RT   "A potential tumor suppressor role for Hic1 in breast cancer through
RT   transcriptional repression of ephrin-A1.";
RL   Oncogene 29:2467-2476(2010).
RN   [20]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-237; SER-248 AND
RP   SER-366, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
RA   Wang L., Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human
RT   liver phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
CC   -!- FUNCTION: Transcriptional repressor. Recognizes and binds to the
CC       consensus sequence '5-[CG]NG[CG]GGGCA[CA]CC-3'. May act as a tumor
CC       suppressor. May be involved in development of head, face, limbs
CC       and ventral body wall. Involved in down-regulation of SIRT1 and
CC       thereby is involved in regulation of p53/TP53-dependent apoptotic
CC       DNA-damage responses. The specific target gene promoter
CC       association seems to be depend on corepressors, such as CTBP1 or
CC       CTBP2 and MTA1. The regulation of SIRT1 transcription in response
CC       to nutrient deprivation seems to involve CTBP1. In cooperation
CC       with MTA1 (indicative for an association with the NuRD complex)
CC       represses transcription from CCND1/cyclin-D1 and CDKN1C/p57Kip2
CC       specifically in quiescent cells. Involved in regulation of the Wnt
CC       signaling pathway probably by association with TCF7L2 and
CC       preventing TCF7L2 and CTNNB1 association with promoters of TCF-
CC       responsive genes. Seems to repress transcription from E2F1 and
CC       ATOH1 which involves ARID1A, indicative for the participation of a
CC       distinct SWI/SNF-type chromatin-remodeling complex. Probably
CC       represses transcription from ACKR3, FGFBP1 and EFNA1.
CC       {ECO:0000269|PubMed:12052894, ECO:0000269|PubMed:15231840,
CC       ECO:0000269|PubMed:16269335, ECO:0000269|PubMed:16690027,
CC       ECO:0000269|PubMed:16724116, ECO:0000269|PubMed:17213307,
CC       ECO:0000269|PubMed:18347096, ECO:0000269|PubMed:19486893,
CC       ECO:0000269|PubMed:19525223, ECO:0000269|PubMed:20154726,
CC       ECO:0000269|PubMed:20547755}.
CC   -!- SUBUNIT: Self-associates. Interacts with HIC2. Interacts with
CC       CTBP1 and CTBP2. Interacts with TCF7L2 and ARID1A. Interacts with
CC       MTA1 and MBD3; indicative for an association with the NuRD
CC       complex. {ECO:0000269|PubMed:11554746,
CC       ECO:0000269|PubMed:12052894, ECO:0000269|PubMed:16724116,
CC       ECO:0000269|PubMed:16762039, ECO:0000269|PubMed:17213307,
CC       ECO:0000269|PubMed:19486893, ECO:0000269|PubMed:20547755}.
CC   -!- INTERACTION:
CC       O14497:ARID1A; NbExp=2; IntAct=EBI-2507362, EBI-637887;
CC       Q13363:CTBP1; NbExp=4; IntAct=EBI-2507362, EBI-908846;
CC       O88712:Ctbp1 (xeno); NbExp=10; IntAct=EBI-2507362, EBI-604547;
CC       P56545:CTBP2; NbExp=2; IntAct=EBI-2507362, EBI-741533;
CC       P56546:Ctbp2 (xeno); NbExp=2; IntAct=EBI-2507362, EBI-1384883;
CC       Q9NQB0:TCF7L2; NbExp=6; IntAct=EBI-2507362, EBI-924724;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11554746}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC         Comment=Additional isoforms seem to exist.;
CC       Name=1;
CC         IsoId=Q14526-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q14526-2; Sequence=VSP_006826;
CC   -!- TISSUE SPECIFICITY: Ubiquitously expressed with highest levels
CC       found in lung, colon, prostate, thymus, testis and ovary.
CC       Expression is absent or decreased in many tumor cells.
CC   -!- DOMAIN: The BTB domain inhibits the binding to a single consensus
CC       binding site, but mediates cooperative binding to multiple binding
CC       sites.
CC   -!- PTM: Acetylated on several residues, including Lys-333. Lys-333 is
CC       deacetylated by SIRT1. {ECO:0000269|PubMed:17283066}.
CC   -!- PTM: Sumoylated on Lys-333 by a PIAS family member, which enhances
CC       interaction with MTA1, positively regulates transcriptional
CC       repression activity and is enhanced by HDAC4.
CC       {ECO:0000269|PubMed:17283066}.
CC   -!- MISCELLANEOUS: The HIC1 gene is frequently found epigenetically
CC       silenced or deleted in different types of solid tumors.
CC   -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC       family. Hic subfamily. {ECO:0000305}.
CC   -!- SIMILARITY: Contains 1 BTB (POZ) domain. {ECO:0000255|PROSITE-
CC       ProRule:PRU00037}.
CC   -!- SIMILARITY: Contains 5 C2H2-type zinc fingers.
CC       {ECO:0000255|PROSITE-ProRule:PRU00042}.
CC   -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC       and Haematology;
CC       URL="http://atlasgeneticsoncology.org/Genes/HIC1ID40819ch17p13.html";
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DR   EMBL; L41919; AAD09201.1; -; Genomic_DNA.
DR   EMBL; AC090617; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471108; EAW90562.1; -; Genomic_DNA.
DR   EMBL; CH471108; EAW90563.1; -; Genomic_DNA.
DR   CCDS; CCDS42229.1; -. [Q14526-1]
DR   CCDS; CCDS42230.1; -. [Q14526-2]
DR   RefSeq; NP_001091672.1; NM_001098202.1. [Q14526-1]
DR   RefSeq; NP_006488.2; NM_006497.3. [Q14526-2]
DR   UniGene; Hs.695682; -.
DR   UniGene; Hs.72956; -.
DR   ProteinModelPortal; Q14526; -.
DR   SMR; Q14526; 25-145, 429-613.
DR   BioGrid; 109337; 26.
DR   IntAct; Q14526; 11.
DR   MINT; MINT-2730619; -.
DR   STRING; 9606.ENSP00000314080; -.
DR   PhosphoSite; Q14526; -.
DR   BioMuta; HIC1; -.
DR   DMDM; 296439502; -.
DR   PaxDb; Q14526; -.
DR   PRIDE; Q14526; -.
DR   DNASU; 3090; -.
DR   Ensembl; ENST00000322941; ENSP00000314080; ENSG00000177374. [Q14526-1]
DR   Ensembl; ENST00000399849; ENSP00000382742; ENSG00000177374. [Q14526-2]
DR   Ensembl; ENST00000619757; ENSP00000477858; ENSG00000177374. [Q14526-2]
DR   GeneID; 3090; -.
DR   KEGG; hsa:3090; -.
DR   UCSC; uc002fty.4; human. [Q14526-1]
DR   CTD; 3090; -.
DR   GeneCards; HIC1; -.
DR   H-InvDB; HIX0039113; -.
DR   HGNC; HGNC:4909; HIC1.
DR   HPA; HPA043372; -.
DR   MIM; 603825; gene.
DR   neXtProt; NX_Q14526; -.
DR   Orphanet; 531; Miller-Dieker syndrome.
DR   PharmGKB; PA29282; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   eggNOG; COG5048; LUCA.
DR   GeneTree; ENSGT00800000124025; -.
DR   HOGENOM; HOG000026793; -.
DR   HOVERGEN; HBG031606; -.
DR   InParanoid; Q14526; -.
DR   OMA; PPDPFRG; -.
DR   OrthoDB; EOG74J97F; -.
DR   PhylomeDB; Q14526; -.
DR   TreeFam; TF333488; -.
DR   SignaLink; Q14526; -.
DR   GeneWiki; HIC1; -.
DR   GenomeRNAi; 3090; -.
DR   NextBio; 12259; -.
DR   PRO; PR:Q14526; -.
DR   Proteomes; UP000005640; Chromosome 17.
DR   Bgee; Q14526; -.
DR   CleanEx; HS_HIC1; -.
DR   ExpressionAtlas; Q14526; baseline and differential.
DR   Genevisible; Q14526; HS.
DR   GO; GO:0000785; C:chromatin; ISS:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; IDA:HPA.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0042826; F:histone deacetylase binding; IDA:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
DR   GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IDA:UniProtKB.
DR   GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; IDA:UniProtKB.
DR   GO; GO:0007275; P:multicellular organismal development; IEA:UniProtKB-KW.
DR   GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
DR   GO; GO:0030178; P:negative regulation of Wnt signaling pathway; IDA:UniProtKB.
DR   GO; GO:0043517; P:positive regulation of DNA damage response, signal transduction by p53 class mediator; ISS:UniProtKB.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; TAS:UniProtKB.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
DR   GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.160.60; -; 4.
DR   InterPro; IPR000210; BTB/POZ_dom.
DR   InterPro; IPR028424; HIC1.
DR   InterPro; IPR011333; POZ_dom.
DR   InterPro; IPR007087; Znf_C2H2.
DR   InterPro; IPR015880; Znf_C2H2-like.
DR   InterPro; IPR013087; Znf_C2H2/integrase_DNA-bd.
DR   PANTHER; PTHR24409:SF69; PTHR24409:SF69; 1.
DR   Pfam; PF00651; BTB; 1.
DR   Pfam; PF00096; zf-C2H2; 1.
DR   SMART; SM00225; BTB; 1.
DR   SMART; SM00355; ZnF_C2H2; 5.
DR   SUPFAM; SSF54695; SSF54695; 1.
DR   PROSITE; PS50097; BTB; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 5.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 5.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Complete proteome;
KW   Developmental protein; DNA-binding; Isopeptide bond; Metal-binding;
KW   Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repeat;
KW   Repressor; Transcription; Transcription regulation; Tumor suppressor;
KW   Ubl conjugation; Wnt signaling pathway; Zinc; Zinc-finger.
FT   CHAIN         1    733       Hypermethylated in cancer 1 protein.
FT                                /FTId=PRO_0000046942.
FT   DOMAIN       47    110       BTB. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00037}.
FT   ZN_FING     439    459       C2H2-type 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     509    529       C2H2-type 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     537    557       C2H2-type 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     565    585       C2H2-type 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     593    613       C2H2-type 5. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   REGION      154    315       Mediates HDAC-dependent transcriptional
FT                                repression.
FT   REGION      241    247       Interaction with CTBP1.
FT   COMPBIAS    110    119       Poly-Ala.
FT   COMPBIAS    160    167       Poly-Gly.
FT   COMPBIAS    195    199       Poly-Pro.
FT   MOD_RES     237    237       Phosphoserine.
FT                                {ECO:0000244|PubMed:24275569}.
FT   MOD_RES     248    248       Phosphoserine.
FT                                {ECO:0000244|PubMed:24275569}.
FT   MOD_RES     333    333       N6-acetyllysine; alternate.
FT                                {ECO:0000269|PubMed:17283066}.
FT   MOD_RES     366    366       Phosphoserine.
FT                                {ECO:0000244|PubMed:24275569}.
FT   MOD_RES     704    704       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9R1Y5}.
FT   CROSSLNK    333    333       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO);
FT                                alternate.
FT   VAR_SEQ       1     19       Missing (in isoform 2). {ECO:0000305}.
FT                                /FTId=VSP_006826.
FT   VARIANT     725    725       R -> G (in dbSNP:rs1063317).
FT                                {ECO:0000269|PubMed:7585125}.
FT                                /FTId=VAR_063109.
FT   MUTAGEN     244    244       L->A: Abolishes interaction with CTBP1
FT                                and CTBP2. Impairs transcriptional
FT                                repression.
FT                                {ECO:0000269|PubMed:16762039}.
FT   MUTAGEN     333    333       K->Q: Mimicks acetylation. Impairs
FT                                interaction with RBBP4 and MTA1 and no
FT                                effect on interaction with CTBP2. Reduces
FT                                transcriptional repression.
FT                                {ECO:0000269|PubMed:17283066,
FT                                ECO:0000269|PubMed:20547755}.
FT   MUTAGEN     333    333       K->R: Abolishes sumoylation; impairs
FT                                transcriptional repression activity.
FT                                {ECO:0000269|PubMed:17283066,
FT                                ECO:0000269|PubMed:20547755}.
FT   MUTAGEN     335    335       E->A: Impairs transcriptional repression
FT                                activity. Decreases interaction with
FT                                MTA1. {ECO:0000269|PubMed:17283066,
FT                                ECO:0000269|PubMed:20547755}.
FT   MUTAGEN     336    336       P->A: Impairs K-333 acetylation; no
FT                                effect on sumoylation. Decreases
FT                                interaction with MTA1.
FT                                {ECO:0000269|PubMed:17283066,
FT                                ECO:0000269|PubMed:20547755}.
FT   MUTAGEN     540    540       C->S: Abolishes repression activity.
FT                                {ECO:0000269|PubMed:15231840}.
FT   CONFLICT    190    190       P -> R (in Ref. 1; AAD09201).
FT                                {ECO:0000305}.
SQ   SEQUENCE   733 AA;  76508 MW;  6DDD0F49C4E490D3 CRC64;
     MTFPEADILL KSGECAGQTM LDTMEAPGHS RQLLLQLNNQ RTKGFLCDVI IVVQNALFRA
     HKNVLAASSA YLKSLVVHDN LLNLDHDMVS PAVFRLVLDF IYTGRLADGA EAAAAAAVAP
     GAEPSLGAVL AAASYLQIPD LVALCKKRLK RHGKYCHLRG GGGGGGGYAP YGRPGRGLRA
     ATPVIQACYP SPVGPPPPPA AEPPSGPEAA VNTHCAELYA SGPGPAAALC ASERRCSPLC
     GLDLSKKSPP GSAAPERPLA ERELPPRPDS PPSAGPAAYK EPPLALPSLP PLPFQKLEEA
     APPSDPFRGG SGSPGPEPPG RPDGPSLLYR WMKHEPGLGS YGDELGRERG SPSERCEERG
     GDAAVSPGGP PLGLAPPPRY PGSLDGPGAG GDGDDYKSSS EETGSSEDPS PPGGHLEGYP
     CPHLAYGEPE SFGDNLYVCI PCGKGFPSSE QLNAHVEAHV EEEEALYGRA EAAEVAAGAA
     GLGPPFGGGG DKVAGAPGGL GELLRPYRCA SCDKSYKDPA TLRQHEKTHW LTRPYPCTIC
     GKKFTQRGTM TRHMRSHLGL KPFACDACGM RFTRQYRLTE HMRIHSGEKP YECQVCGGKF
     AQQRNLISHM KMHAVGGAAG AAGALAGLGG LPGVPGPDGK GKLDFPEGVF AVARLTAEQL
     SLKQQDKAAA AELLAQTTHF LHDPKVALES LYPLAKFTAE LGLSPDKAAE VLSQGAHLAA
     GPDGRTIDRF SPT
//
ID   IKZF1_HUMAN             Reviewed;         519 AA.
AC   Q13422; A4D260; B4E0Z1; D3DVM5; O00598; Q53XL2; Q69BM4; Q8WVA3;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   11-NOV-2015, entry version 150.
DE   RecName: Full=DNA-binding protein Ikaros;
DE   AltName: Full=Ikaros family zinc finger protein 1;
DE   AltName: Full=Lymphoid transcription factor LyF-1;
GN   Name=IKZF1; Synonyms=IK1, IKAROS, LYF1, ZNFN1A1;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], ALTERNATIVE SPLICING, AND TISSUE
RP   SPECIFICITY.
RC   TISSUE=Bone marrow;
RX   PubMed=8964602; DOI=10.1016/0165-2478(95)02479-4;
RA   Nietfeld W., Meyerhans A.;
RT   "Cloning and sequencing of hIk-1, a cDNA encoding a human homologue of
RT   mouse Ikaros/LyF-1.";
RL   Immunol. Lett. 49:139-141(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], ALTERNATIVE SPLICING, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=8543809;
RA   Molnar A., Wu P., Largespada D.A., Vortkamp A., Scherer S.,
RA   Copeland N.G., Jenkins N.A., Bruns G., Georgopoulos K.;
RT   "The Ikaros gene encodes a family of lymphocyte-restricted zinc finger
RT   DNA binding proteins, highly conserved in human and mouse.";
RL   J. Immunol. 156:585-592(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM IKX).
RA   Sanchez-Tapia E.M., Rodriguez R.E., Gonzalez-Sarmiento R.;
RT   "Molecular misreading is involved in generation of Ikaros diversity.";
RL   Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM IK2).
RC   TISSUE=Thymus;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM IK7).
RA   Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA   Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA   Phelan M., Farmer A.;
RT   "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT   vector.";
RL   Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12853948; DOI=10.1038/nature01782;
RA   Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA   Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R.,
RA   Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E.,
RA   Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H.,
RA   Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A.,
RA   Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J.,
RA   Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A.,
RA   Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S.,
RA   Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M.,
RA   Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C.,
RA   Latreille P., Miller N., Johnson D., Murray J., Woessner J.P.,
RA   Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J.,
RA   Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L.,
RA   Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R.,
RA   Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA   Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K.,
RA   Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S.,
RA   Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M.,
RA   Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R.,
RA   Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D.,
RA   Waterston R.H., Wilson R.K.;
RT   "The DNA sequence of human chromosome 7.";
RL   Nature 424:157-164(2003).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12690205; DOI=10.1126/science.1083423;
RA   Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA   Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA   Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA   Kanematsu E., Gentles S., Christopoulos C.C., Choufani S.,
RA   Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z.,
RA   Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C.,
RA   Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J.,
RA   Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F.,
RA   Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F.,
RA   Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H.,
RA   Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G.,
RA   Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P.,
RA   Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J.,
RA   Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F.,
RA   Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B.,
RA   Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA   Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W.,
RA   Mural R.J., Adams M.D., Tsui L.-C.;
RT   "Human chromosome 7: DNA sequence and biology.";
RL   Science 300:767-772(2003).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [9]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM IK7).
RC   TISSUE=Lymph;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [10]
RP   IDENTIFICATION IN THE NURD COMPLEX, IDENTIFICATION IN THE BAF COMPLEX,
RP   INTERACTION WITH SMARCA4 AND CHD4, AND FUNCTION.
RX   PubMed=10204490; DOI=10.1016/S1074-7613(00)80034-5;
RA   Kim J., Sif S., Jones B., Jackson A., Koipally J., Heller E.,
RA   Winandy S., Viel A., Sawyer A., Ikeda T., Kingston R.,
RA   Georgopoulos K.;
RT   "Ikaros DNA-binding proteins direct formation of chromatin remodeling
RT   complexes in lymphocytes.";
RL   Immunity 10:345-355(1999).
RN   [11]
RP   INVOLVEMENT IN B-CELL NON-HODGKIN LYMPHOMA, AND CHROMOSOMAL
RP   TRANSLOCATION WITH BCL6.
RX   PubMed=10753856;
RA   Hosokawa Y., Maeda Y., Ichinohasama R., Miura I., Taniwaki M.,
RA   Seto M.;
RT   "The Ikaros gene, a central regulator of lymphoid differentiation,
RT   fuses to the BCL6 gene as a result of t(3;7)(q27;p12) translocation in
RT   a patient with diffuse large B-cell lymphoma.";
RL   Blood 95:2719-2721(2000).
RN   [12]
RP   INTERACTION WITH IKZF4 AND IKZF5.
RX   PubMed=10978333; DOI=10.1074/jbc.M005457200;
RA   Perdomo J., Holmes M., Chong B., Crossley M.;
RT   "Eos and pegasus, two members of the Ikaros family of proteins with
RT   distinct DNA binding activities.";
RL   J. Biol. Chem. 275:38347-38354(2000).
RN   [13]
RP   FUNCTION, ALTERNATIVE SPLICING, SUBCELLULAR LOCATION, AND SUBUNIT.
RX   PubMed=17135265; DOI=10.1074/jbc.M605627200;
RA   Ronni T., Payne K.J., Ho S., Bradley M.N., Dorsam G., Dovat S.;
RT   "Human Ikaros function in activated T cells is regulated by
RT   coordinated expression of its largest isoforms.";
RL   J. Biol. Chem. 282:2538-2547(2007).
RN   [14]
RP   FUNCTION, AND ALTERNATIVE SPLICING.
RX   PubMed=17934067; DOI=10.1182/blood-2007-07-098202;
RA   Dijon M., Bardin F., Murati A., Batoz M., Chabannon C., Tonnelle C.;
RT   "The role of Ikaros in human erythroid differentiation.";
RL   Blood 111:1138-1146(2008).
RN   [15]
RP   FUNCTION IN GAMMA SATELLITE DNA BINDING.
RX   PubMed=19141594; DOI=10.1101/gr.086496.108;
RA   Kim J.-H., Ebersole T., Kouprina N., Noskov V.N., Ohzeki J.-I.,
RA   Masumoto H., Mravinac B., Sullivan B.A., Pavlicek A., Dovat S.,
RA   Pack S.D., Kwon Y.-W., Flanagan P.T., Loukinov D., Lobanenkov V.,
RA   Larionov V.;
RT   "Human gamma-satellite DNA maintains open chromatin structure and
RT   protects a transgene from epigenetic silencing.";
RL   Genome Res. 19:533-544(2009).
RN   [16]
RP   INVOLVEMENT IN ACUTE LYMPHOBLASIC LEUKEMIA.
RX   PubMed=19129520; DOI=10.1056/NEJMoa0808253;
RA   Mullighan C.G., Su X., Zhang J., Radtke I., Phillips L.A.,
RA   Miller C.B., Ma J., Liu W., Cheng C., Schulman B.A., Harvey R.C.,
RA   Chen I.-M., Clifford R.J., Carroll W.L., Reaman G., Bowman W.P.,
RA   Devidas M., Gerhard D.S., Yang W., Relling M.V., Shurtleff S.A.,
RA   Campana D., Borowitz M.J., Pui C.H., Smith M., Hunger S.P.,
RA   Willman C.L., Downing J.R.;
RT   "Deletion of IKZF1 and prognosis in acute lymphoblastic leukemia.";
RL   N. Engl. J. Med. 360:470-480(2009).
RN   [17]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-63; SER-258; SER-361 AND
RP   SER-364, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA   Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA   Rodionov V., Han D.K.;
RT   "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT   reveals system-wide modulation of protein-protein interactions.";
RL   Sci. Signal. 2:RA46-RA46(2009).
RN   [18]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA   Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [19]
RP   FUNCTION IN DNA BINDING, SUBCELLULAR LOCATION, PHOSPHORYLATION, AND
RP   ALTERNATIVE SPLICING.
RX   PubMed=22106042; DOI=10.1002/pbc.23406;
RA   Li Z., Song C., Ouyang H., Lai L., Payne K.J., Dovat S.;
RT   "Cell cycle-specific function of Ikaros in human leukemia.";
RL   Pediatr. Blood Cancer 59:69-76(2012).
RN   [20]
RP   PHOSPHORYLATION AT SER-361 AND SER-364 BY SYK, AND SUBCELLULAR
RP   LOCATION.
RX   PubMed=23071339; DOI=10.1073/pnas.1209828109;
RA   Uckun F.M., Ma H., Zhang J., Ozer Z., Dovat S., Mao C., Ishkhanian R.,
RA   Goodman P., Qazi S.;
RT   "Serine phosphorylation by SYK is critical for nuclear localization
RT   and transcription factor function of Ikaros.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:18072-18077(2012).
RN   [21]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-445, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
RA   Wang L., Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human
RT   liver phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
CC   -!- FUNCTION: Transcription regulator of hematopoietic cell
CC       differentiation (PubMed:17934067). Binds gamma-satellite DNA
CC       (PubMed:17135265, PubMed:19141594). Plays a role in the
CC       development of lymphocytes, B- and T-cells. Binds and activates
CC       the enhancer (delta-A element) of the CD3-delta gene. Repressor of
CC       the TDT (fikzfterminal deoxynucleotidyltransferase) gene during
CC       thymocyte differentiation. Regulates transcription through
CC       association with both HDAC-dependent and HDAC-independent
CC       complexes. Targets the 2 chromatin-remodeling complexes, NuRD and
CC       BAF (SWI/SNF), in a single complex (PYR complex), to the beta-
CC       globin locus in adult erythrocytes. Increases normal apoptosis in
CC       adult erythroid cells. Confers early temporal competence to
CC       retinal progenitor cells (RPCs) (By similarity). Function is
CC       isoform-specific and is modulated by dominant-negative inactive
CC       isoforms (PubMed:17135265, PubMed:17934067).
CC       {ECO:0000250|UniProtKB:Q03267, ECO:0000269|PubMed:10204490,
CC       ECO:0000269|PubMed:17135265, ECO:0000269|PubMed:17934067,
CC       ECO:0000269|PubMed:19141594}.
CC   -!- SUBUNIT: Heterodimer formed by the various isoforms; this
CC       modulates transcription regulator activity (PubMed:17135265,
CC       PubMed:17934067). Heterodimer with other IKAROS family members.
CC       Interacts with IKZF4 AND IKZF5 (PubMed:10978333). Component of the
CC       chromatin-remodeling NuRD repressor complex which includes at
CC       least HDAC1, HDAC2, RBBP4, RBBP7, IKZF1, MTA2, MBD2, MBD3, MTA1L1,
CC       CHD3 and CHD4. Interacts directly with the CHD4 component of the
CC       NuRD complex. Component of the BAF (SWI/SNF) gene activator
CC       complex which includes ACTB, ARID1A, ARID1B, IKZF1, ARID1A,
CC       ARID1B, SMARCA2, SMARCA4 and at least one BAF subunit. Interacts
CC       directly with the SMARCA4 component of the BAF complex (By
CC       similarity). Interacts with SUMO1; the interaction sumoylates
CC       IKAROS, promoted by PIAS2 and PIAS3. Interacts with PIAS2 (isoform
CC       alpha); the interaction promotes sumoylation and reduces
CC       transcription repression. Interacts, to a lesser extent, with
CC       PIAS3. Interacts with PPP1CC; the interaction targets PPP1CC to
CC       pericentromeric heterochromatin, dephosphorylates IKAROS,
CC       stabilizes it and prevents it from degradation. Interacts with
CC       IKZF3 (By similarity). {ECO:0000250, ECO:0000269|PubMed:10204490,
CC       ECO:0000269|PubMed:10978333, ECO:0000305|PubMed:17135265,
CC       ECO:0000305|PubMed:17934067}.
CC   -!- INTERACTION:
CC       A8K932:-; NbExp=3; IntAct=EBI-745305, EBI-10174671;
CC       Q8WTP8:AEN; NbExp=3; IntAct=EBI-745305, EBI-8637627;
CC       Q96Q83:ALKBH3; NbExp=3; IntAct=EBI-745305, EBI-6658697;
CC       Q9BXS5:AP1M1; NbExp=3; IntAct=EBI-745305, EBI-541426;
CC       Q9H6L4:ARMC7; NbExp=3; IntAct=EBI-745305, EBI-742909;
CC       Q13895:BYSL; NbExp=5; IntAct=EBI-745305, EBI-358049;
CC       Q9NUL5:C19orf66; NbExp=3; IntAct=EBI-745305, EBI-10313866;
CC       Q9NX04:C1orf109; NbExp=3; IntAct=EBI-745305, EBI-8643161;
CC       Q8IYL3:C1orf174; NbExp=3; IntAct=EBI-745305, EBI-715898;
CC       Q9H7E9:C8orf33; NbExp=3; IntAct=EBI-745305, EBI-715389;
CC       Q9HC52:CBX8; NbExp=3; IntAct=EBI-745305, EBI-712912;
CC       Q8IYX8-2:CEP57L1; NbExp=3; IntAct=EBI-745305, EBI-10181988;
CC       P61024:CKS1B; NbExp=3; IntAct=EBI-745305, EBI-456371;
CC       Q13363-2:CTBP1; NbExp=3; IntAct=EBI-745305, EBI-10171858;
CC       P56545:CTBP2; NbExp=5; IntAct=EBI-745305, EBI-741533;
CC       Q8IY44:CTBP2; NbExp=3; IntAct=EBI-745305, EBI-10171902;
CC       O43602:DCX; NbExp=4; IntAct=EBI-745305, EBI-8646694;
CC       P26196:DDX6; NbExp=3; IntAct=EBI-745305, EBI-351257;
CC       Q92630:DYRK2; NbExp=3; IntAct=EBI-745305, EBI-749432;
CC       Q3B820:FAM161A; NbExp=3; IntAct=EBI-745305, EBI-719941;
CC       Q7L5A3:FAM214B; NbExp=4; IntAct=EBI-745305, EBI-745689;
CC       Q9Y247:FAM50B; NbExp=4; IntAct=EBI-745305, EBI-742802;
CC       Q5TZK3:FAM74A6; NbExp=3; IntAct=EBI-745305, EBI-10247271;
CC       P61328:FGF12; NbExp=3; IntAct=EBI-745305, EBI-6657662;
CC       Q96NE9:FRMD6; NbExp=3; IntAct=EBI-745305, EBI-741729;
CC       O76003:GLRX3; NbExp=3; IntAct=EBI-745305, EBI-374781;
CC       Q8NEA9:GMCL1P1; NbExp=3; IntAct=EBI-745305, EBI-745707;
CC       Q9H1K1:ISCU; NbExp=3; IntAct=EBI-745305, EBI-1047335;
CC       Q8TAP4:LMO3; NbExp=3; IntAct=EBI-745305, EBI-742259;
CC       Q9Y4Z0:LSM4; NbExp=3; IntAct=EBI-745305, EBI-372521;
CC       Q9UI95:MAD2L2; NbExp=3; IntAct=EBI-745305, EBI-77889;
CC       Q96EZ8:MCRS1; NbExp=3; IntAct=EBI-745305, EBI-348259;
CC       Q9UBU8:MORF4L1; NbExp=3; IntAct=EBI-745305, EBI-399246;
CC       Q15014:MORF4L2; NbExp=3; IntAct=EBI-745305, EBI-399257;
CC       Q13330:MTA1; NbExp=3; IntAct=EBI-745305, EBI-714236;
CC       Q9HC98:NEK6; NbExp=3; IntAct=EBI-745305, EBI-740364;
CC       Q9BVI4:NOC4L; NbExp=3; IntAct=EBI-745305, EBI-395927;
CC       Q13526:PIN1; NbExp=3; IntAct=EBI-745305, EBI-714158;
CC       Q96T60:PNKP; NbExp=3; IntAct=EBI-745305, EBI-1045072;
CC       O43741:PRKAB2; NbExp=3; IntAct=EBI-745305, EBI-1053424;
CC       P25786:PSMA1; NbExp=3; IntAct=EBI-745305, EBI-359352;
CC       P25789:PSMA4; NbExp=3; IntAct=EBI-745305, EBI-359310;
CC       Q7Z474:PSMA4; NbExp=3; IntAct=EBI-745305, EBI-10257551;
CC       O75771:RAD51D; NbExp=4; IntAct=EBI-745305, EBI-1055693;
CC       P57060:RWDD2B; NbExp=4; IntAct=EBI-745305, EBI-724442;
CC       Q9BWG6:SCNM1; NbExp=3; IntAct=EBI-745305, EBI-748391;
CC       O00560:SDCBP; NbExp=3; IntAct=EBI-745305, EBI-727004;
CC       Q9H788:SH2D4A; NbExp=3; IntAct=EBI-745305, EBI-747035;
CC       P62306:SNRPF; NbExp=3; IntAct=EBI-745305, EBI-356900;
CC       Q13573:SNW1; NbExp=3; IntAct=EBI-745305, EBI-632715;
CC       Q9H0A9:SPATC1L; NbExp=3; IntAct=EBI-745305, EBI-372911;
CC       Q9BSW7:SYT17; NbExp=3; IntAct=EBI-745305, EBI-745392;
CC       Q7KZS0:UBE2I; NbExp=3; IntAct=EBI-745305, EBI-10180829;
CC       Q15007:WTAP; NbExp=3; IntAct=EBI-745305, EBI-751647;
CC       Q96NC0:ZMAT2; NbExp=3; IntAct=EBI-745305, EBI-2682299;
CC       Q8TAU3:ZNF417; NbExp=3; IntAct=EBI-745305, EBI-740727;
CC       Q9P0T4:ZNF581; NbExp=3; IntAct=EBI-745305, EBI-745520;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17135265,
CC       ECO:0000269|PubMed:22106042, ECO:0000269|PubMed:23071339}. Note=In
CC       resting lymphocytes, distributed diffusely throughout the nucleus.
CC       Localizes to pericentromeric heterochromatin in proliferating
CC       cells. This localization requires DNA binding which is regulated
CC       by phosphorylation / dephosphorylation events.
CC       {ECO:0000269|PubMed:17135265, ECO:0000269|PubMed:22106042}.
CC   -!- SUBCELLULAR LOCATION: Isoform Ik2: Nucleus. Note=In resting
CC       lymphocytes, distributed diffusely throughout the nucleus.
CC       Localizes to pericentromeric heterochromatin in proliferating
CC       cells. This localization requires DNA binding which is regulated
CC       by phosphorylation / dephosphorylation events (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Isoform Ik6: Cytoplasm {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=8;
CC       Name=Ik1;
CC         IsoId=Q13422-1; Sequence=Displayed;
CC       Name=Ik2;
CC         IsoId=Q13422-2; Sequence=VSP_006848;
CC       Name=Ik3;
CC         IsoId=Q13422-3; Sequence=VSP_006850;
CC       Name=Ik4;
CC         IsoId=Q13422-4; Sequence=VSP_006847, VSP_006850;
CC       Name=Ik5;
CC         IsoId=Q13422-5; Sequence=VSP_006852;
CC       Name=Ik6;
CC         IsoId=Q13422-6; Sequence=VSP_006849;
CC       Name=Ik7;
CC         IsoId=Q13422-7; Sequence=VSP_006851;
CC       Name=Ikx;
CC         IsoId=Q13422-8; Sequence=VSP_006851, VSP_053404, VSP_053405;
CC   -!- TISSUE SPECIFICITY: Abundantly expressed in thymus, spleen and
CC       peripheral blood Leukocytes and lymph nodes. Lower expression in
CC       bone marrow and small intestine. {ECO:0000269|PubMed:8543809,
CC       ECO:0000269|PubMed:8964602}.
CC   -!- DOMAIN: The N-terminal zinc-fingers 2 and 3 are required for DNA
CC       binding as well as for targeting IKFZ1 to pericentromeric
CC       heterochromatin. {ECO:0000250}.
CC   -!- DOMAIN: The C-terminal zinc-finger domain is required for
CC       dimerization. {ECO:0000250}.
CC   -!- PTM: Phosphorylation controls cell-cycle progression from late
CC       G(1) stage to S stage. Hyperphosphorylated during G2/M phase.
CC       Dephosphorylated state during late G(1) phase. Phosphorylation on
CC       Thr-140 is required for DNA and pericentromeric location during
CC       mitosis. CK2 is the main kinase, in vitro. GSK3 and CDK may also
CC       contribute to phosphorylation of the C-terminal serine and
CC       threonine residues. Phosphorylation on these C-terminal residues
CC       reduces the DNA-binding ability. Phosphorylation/dephosphorylation
CC       events on Ser-13 and Ser-295 regulate TDT expression during
CC       thymocyte differentiation. Dephosphorylation by protein
CC       phosphatase 1 regulates stability and pericentromeric
CC       heterochromatin location. Phosphorylated in both lymphoid and non-
CC       lymphoid tissues (By similarity). Phosphorylation at Ser-361 and
CC       Ser-364 downstream of SYK induces nuclear translocation.
CC       {ECO:0000250, ECO:0000269|PubMed:22106042,
CC       ECO:0000269|PubMed:23071339}.
CC   -!- PTM: Sumoylated. Simulataneous sumoylation on the 2 sites results
CC       in a loss of both HDAC-dependent and HDAC-independent repression.
CC       Has no effect on pericentromeric heterochromatin location.
CC       Desumoylated by SENP1 (By similarity). {ECO:0000250}.
CC   -!- PTM: Polyubiquitinated. {ECO:0000250}.
CC   -!- DISEASE: Note=Defects in IKZF1 are frequent occurrences (28.6%) in
CC       acute lymphoblasic leukemia (ALL). Such alterations or deletions
CC       lead to poor prognosis for ALL.
CC   -!- DISEASE: Note=Chromosomal aberrations involving IKZF1 are a cause
CC       of B-cell non-Hodgkin lymphomas (B-cell NHL). Translocation
CC       t(3;7)(q27;p12), with BCL6.
CC   -!- SIMILARITY: Belongs to the Ikaros C2H2-type zinc-finger protein
CC       family. {ECO:0000305}.
CC   -!- SIMILARITY: Contains 6 C2H2-type zinc fingers.
CC       {ECO:0000255|PROSITE-ProRule:PRU00042}.
CC   -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC       and Haematology;
CC       URL="http://atlasgeneticsoncology.org/Genes/IkarosID258.html";
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DR   EMBL; U40462; AAC50459.1; -; mRNA.
DR   EMBL; S80876; AAB50683.1; -; mRNA.
DR   EMBL; AY377974; AAR84585.1; -; mRNA.
DR   EMBL; AK303586; BAG64603.1; -; mRNA.
DR   EMBL; BT009836; AAP88838.1; -; mRNA.
DR   EMBL; AC124014; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC233268; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471128; EAW60977.1; -; Genomic_DNA.
DR   EMBL; CH471128; EAW60978.1; -; Genomic_DNA.
DR   EMBL; CH471128; EAW60981.1; -; Genomic_DNA.
DR   EMBL; CH236955; EAL23900.1; -; Genomic_DNA.
DR   EMBL; CH471128; EAW60979.1; -; Genomic_DNA.
DR   EMBL; BC018349; AAH18349.1; -; mRNA.
DR   CCDS; CCDS59055.1; -. [Q13422-7]
DR   CCDS; CCDS69299.1; -. [Q13422-5]
DR   CCDS; CCDS75596.1; -. [Q13422-1]
DR   CCDS; CCDS75597.1; -. [Q13422-3]
DR   CCDS; CCDS78233.1; -. [Q13422-2]
DR   RefSeq; NP_001207694.1; NM_001220765.2. [Q13422-7]
DR   RefSeq; NP_001207696.1; NM_001220767.2.
DR   RefSeq; NP_001207697.1; NM_001220768.2. [Q13422-3]
DR   RefSeq; NP_001207699.1; NM_001220770.2.
DR   RefSeq; NP_001207700.1; NM_001220771.2. [Q13422-5]
DR   RefSeq; NP_001278766.1; NM_001291837.1. [Q13422-7]
DR   RefSeq; NP_001278767.1; NM_001291838.1. [Q13422-2]
DR   RefSeq; NP_001278768.1; NM_001291839.1.
DR   RefSeq; NP_001278769.1; NM_001291840.1. [Q13422-6]
DR   RefSeq; NP_001278770.1; NM_001291841.1.
DR   RefSeq; NP_001278771.1; NM_001291842.1.
DR   RefSeq; NP_001278772.1; NM_001291843.1.
DR   RefSeq; NP_001278773.1; NM_001291844.1.
DR   RefSeq; NP_006051.1; NM_006060.5. [Q13422-1]
DR   RefSeq; XP_011513370.1; XM_011515068.1. [Q13422-1]
DR   RefSeq; XP_011513371.1; XM_011515069.1. [Q13422-1]
DR   RefSeq; XP_011513377.1; XM_011515075.1. [Q13422-2]
DR   RefSeq; XP_011513378.1; XM_011515076.1. [Q13422-2]
DR   UniGene; Hs.435949; -.
DR   UniGene; Hs.488251; -.
DR   UniGene; Hs.646004; -.
DR   UniGene; Hs.731495; -.
DR   ProteinModelPortal; Q13422; -.
DR   SMR; Q13422; 112-220, 460-509.
DR   BioGrid; 115604; 118.
DR   DIP; DIP-41110N; -.
DR   IntAct; Q13422; 68.
DR   MINT; MINT-129252; -.
DR   STRING; 9606.ENSP00000331614; -.
DR   PhosphoSite; Q13422; -.
DR   BioMuta; IKZF1; -.
DR   DMDM; 3913926; -.
DR   MaxQB; Q13422; -.
DR   PaxDb; Q13422; -.
DR   PRIDE; Q13422; -.
DR   DNASU; 10320; -.
DR   Ensembl; ENST00000331340; ENSP00000331614; ENSG00000185811. [Q13422-1]
DR   Ensembl; ENST00000343574; ENSP00000342750; ENSG00000185811. [Q13422-2]
DR   Ensembl; ENST00000349824; ENSP00000342485; ENSG00000185811. [Q13422-5]
DR   Ensembl; ENST00000357364; ENSP00000349928; ENSG00000185811. [Q13422-3]
DR   Ensembl; ENST00000359197; ENSP00000352123; ENSG00000185811. [Q13422-7]
DR   Ensembl; ENST00000438033; ENSP00000396554; ENSG00000185811. [Q13422-2]
DR   Ensembl; ENST00000439701; ENSP00000413025; ENSG00000185811. [Q13422-7]
DR   GeneID; 10320; -.
DR   KEGG; hsa:10320; -.
DR   UCSC; uc003tow.4; human. [Q13422-1]
DR   UCSC; uc003tox.4; human. [Q13422-7]
DR   UCSC; uc003tpa.4; human. [Q13422-6]
DR   UCSC; uc011kck.2; human. [Q13422-2]
DR   UCSC; uc022acq.1; human. [Q13422-5]
DR   UCSC; uc022acs.1; human. [Q13422-4]
DR   UCSC; uc022acx.1; human. [Q13422-3]
DR   CTD; 10320; -.
DR   GeneCards; IKZF1; -.
DR   HGNC; HGNC:13176; IKZF1.
DR   HPA; CAB009247; -.
DR   HPA; HPA035221; -.
DR   HPA; HPA035222; -.
DR   MIM; 603023; gene.
DR   neXtProt; NX_Q13422; -.
DR   Orphanet; 317473; Pancytopenia due to IKZF1 mutations.
DR   Orphanet; 99860; Precursor B-cell acute lymphoblastic leukemia.
DR   PharmGKB; PA37748; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   eggNOG; COG5048; LUCA.
DR   GeneTree; ENSGT00550000074392; -.
DR   HOVERGEN; HBG004752; -.
DR   InParanoid; Q13422; -.
DR   KO; K09220; -.
DR   OMA; GDKCLSD; -.
DR   PhylomeDB; Q13422; -.
DR   TreeFam; TF331189; -.
DR   SignaLink; Q13422; -.
DR   ChiTaRS; IKZF1; human.
DR   GeneWiki; IKZF1; -.
DR   GenomeRNAi; 10320; -.
DR   NextBio; 39123; -.
DR   PRO; PR:Q13422; -.
DR   Proteomes; UP000005640; Chromosome 7.
DR   Bgee; Q13422; -.
DR   CleanEx; HS_IKZF1; -.
DR   ExpressionAtlas; Q13422; baseline and differential.
DR   Genevisible; Q13422; HS.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0005721; C:pericentric heterochromatin; IEA:Ensembl.
DR   GO; GO:0043234; C:protein complex; IDA:MGI.
DR   GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IEA:Ensembl.
DR   GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0044212; F:transcription regulatory region DNA binding; IBA:GO_Central.
DR   GO; GO:0035881; P:amacrine cell differentiation; IEA:Ensembl.
DR   GO; GO:0030183; P:B cell differentiation; IEA:Ensembl.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0016568; P:chromatin modification; IEA:UniProtKB-KW.
DR   GO; GO:0030218; P:erythrocyte differentiation; IMP:UniProtKB.
DR   GO; GO:0030900; P:forebrain development; IEA:Ensembl.
DR   GO; GO:0048535; P:lymph node development; IEA:Ensembl.
DR   GO; GO:0030098; P:lymphocyte differentiation; IMP:UniProtKB.
DR   GO; GO:0007498; P:mesoderm development; TAS:ProtInc.
DR   GO; GO:0001779; P:natural killer cell differentiation; IEA:Ensembl.
DR   GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IBA:GO_Central.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR   GO; GO:0048541; P:Peyer's patch development; IEA:Ensembl.
DR   GO; GO:0045579; P:positive regulation of B cell differentiation; IEA:Ensembl.
DR   GO; GO:0040018; P:positive regulation of multicellular organism growth; IEA:Ensembl.
DR   GO; GO:0045660; P:positive regulation of neutrophil differentiation; IEA:Ensembl.
DR   GO; GO:0051138; P:positive regulation of NK T cell differentiation; IEA:Ensembl.
DR   GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IBA:GO_Central.
DR   GO; GO:0060040; P:retinal bipolar neuron differentiation; IEA:Ensembl.
DR   GO; GO:0030217; P:T cell differentiation; IEA:Ensembl.
DR   GO; GO:0048538; P:thymus development; IEA:Ensembl.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.160.60; -; 4.
DR   InterPro; IPR007087; Znf_C2H2.
DR   InterPro; IPR015880; Znf_C2H2-like.
DR   InterPro; IPR013087; Znf_C2H2/integrase_DNA-bd.
DR   Pfam; PF00096; zf-C2H2; 1.
DR   SMART; SM00355; ZnF_C2H2; 6.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 5.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 4.
PE   1: Evidence at protein level;
KW   Activator; Alternative splicing; Cell cycle; Chromatin regulator;
KW   Chromosomal rearrangement; Complete proteome; Cytoplasm;
KW   Developmental protein; DNA-binding; Isopeptide bond; Metal-binding;
KW   Nucleus; Phosphoprotein; Reference proteome; Repeat; Repressor;
KW   Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW   Zinc-finger.
FT   CHAIN         1    519       DNA-binding protein Ikaros.
FT                                /FTId=PRO_0000047094.
FT   ZN_FING     117    139       C2H2-type 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     145    167       C2H2-type 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     173    195       C2H2-type 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     201    224       C2H2-type 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     462    484       C2H2-type 5. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     490    514       C2H2-type 6. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   REGION      154    163       Required for both high-affinity DNA
FT                                binding and pericentromeric
FT                                heterochromatin localization.
FT                                {ECO:0000250}.
FT   REGION      180    195       Required for both high-affinity DNA
FT                                binding and pericentromeric
FT                                heterochromatin localization.
FT                                {ECO:0000250}.
FT   REGION      468    471       Required for binding PP1CC.
FT                                {ECO:0000250}.
FT   COMPBIAS    373    376       Poly-Leu.
FT   SITE        159    159       Required for both pericentromeric
FT                                heterochromatin localization and complete
FT                                DNA binding. {ECO:0000250}.
FT   SITE        162    162       Required for both pericentromeric
FT                                heterochromatin localization and complete
FT                                DNA binding. {ECO:0000250}.
FT   SITE        188    188       Required for both pericentromeric
FT                                heterochromatin localization and DNA
FT                                binding. {ECO:0000250}.
FT   MOD_RES      13     13       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q03267}.
FT   MOD_RES      23     23       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:Q03267}.
FT   MOD_RES      63     63       Phosphoserine.
FT                                {ECO:0000244|PubMed:19690332}.
FT   MOD_RES     101    101       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q03267}.
FT   MOD_RES     140    140       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:Q03267}.
FT   MOD_RES     168    168       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q03267}.
FT   MOD_RES     196    196       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q03267}.
FT   MOD_RES     258    258       Phosphoserine.
FT                                {ECO:0000244|PubMed:19690332}.
FT   MOD_RES     295    295       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q03267}.
FT   MOD_RES     361    361       Phosphoserine.
FT                                {ECO:0000244|PubMed:19690332,
FT                                ECO:0000269|PubMed:23071339}.
FT   MOD_RES     364    364       Phosphoserine.
FT                                {ECO:0000244|PubMed:19690332,
FT                                ECO:0000269|PubMed:23071339}.
FT   MOD_RES     389    389       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q03267}.
FT   MOD_RES     391    391       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q03267}.
FT   MOD_RES     393    393       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q03267}.
FT   MOD_RES     397    397       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q03267}.
FT   MOD_RES     398    398       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:Q03267}.
FT   MOD_RES     402    402       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q03267}.
FT   MOD_RES     445    445       Phosphoserine.
FT                                {ECO:0000244|PubMed:24275569}.
FT   CROSSLNK     58     58       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO).
FT                                {ECO:0000250}.
FT   CROSSLNK    241    241       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO).
FT                                {ECO:0000250}.
FT   VAR_SEQ      10     53       Missing (in isoform Ik4). {ECO:0000305}.
FT                                /FTId=VSP_006847.
FT   VAR_SEQ      54    283       Missing (in isoform Ik6). {ECO:0000305}.
FT                                /FTId=VSP_006849.
FT   VAR_SEQ      54    140       Missing (in isoform Ik2).
FT                                {ECO:0000303|PubMed:14702039}.
FT                                /FTId=VSP_006848.
FT   VAR_SEQ     141    283       Missing (in isoform Ik5). {ECO:0000305}.
FT                                /FTId=VSP_006852.
FT   VAR_SEQ     197    283       Missing (in isoform Ik3 and isoform Ik4).
FT                                {ECO:0000305}.
FT                                /FTId=VSP_006850.
FT   VAR_SEQ     197    238       Missing (in isoform Ik7 and isoform Ikx).
FT                                {ECO:0000303|PubMed:15489334,
FT                                ECO:0000303|Ref.3, ECO:0000303|Ref.5}.
FT                                /FTId=VSP_006851.
FT   VAR_SEQ     260    268       RSLVLDRLA -> ISRAGQTSK (in isoform Ikx).
FT                                {ECO:0000303|Ref.3}.
FT                                /FTId=VSP_053404.
FT   VAR_SEQ     269    519       Missing (in isoform Ikx).
FT                                {ECO:0000303|Ref.3}.
FT                                /FTId=VSP_053405.
FT   CONFLICT     11     12       QV -> FS (in Ref. 2; AAB50683).
FT                                {ECO:0000305}.
FT   CONFLICT    214    214       S -> T (in Ref. 2; AAB50683).
FT                                {ECO:0000305}.
FT   CONFLICT    245    245       N -> K (in Ref. 2; AAB50683).
FT                                {ECO:0000305}.
FT   CONFLICT    296    296       Missing (in Ref. 2; AAB50683).
FT                                {ECO:0000305}.
FT   CONFLICT    298    298       S -> T (in Ref. 2; AAB50683).
FT                                {ECO:0000305}.
FT   CONFLICT    352    355       KPLA -> RRS (in Ref. 2; AAB50683).
FT                                {ECO:0000305}.
FT   CONFLICT    372    372       N -> Y (in Ref. 2; AAB50683).
FT                                {ECO:0000305}.
FT   CONFLICT    420    426       PHARNGL -> RRAQRV (in Ref. 2; AAB50683).
FT                                {ECO:0000305}.
SQ   SEQUENCE   519 AA;  57528 MW;  7B0129C4E3FE41A8 CRC64;
     MDADEGQDMS QVSGKESPPV SDTPDEGDEP MPIPEDLSTT SGGQQSSKSD RVVASNVKVE
     TQSDEENGRA CEMNGEECAE DLRMLDASGE KMNGSHRDQG SSALSGVGGI RLPNGKLKCD
     ICGIICIGPN VLMVHKRSHT GERPFQCNQC GASFTQKGNL LRHIKLHSGE KPFKCHLCNY
     ACRRRDALTG HLRTHSVGKP HKCGYCGRSY KQRSSLEEHK ERCHNYLESM GLPGTLYPVI
     KEETNHSEMA EDLCKIGSER SLVLDRLASN VAKRKSSMPQ KFLGDKGLSD TPYDSSASYE
     KENEMMKSHV MDQAINNAIN YLGAESLRPL VQTPPGGSEV VPVISPMYQL HKPLAEGTPR
     SNHSAQDSAV ENLLLLSKAK LVPSEREASP SNSCQDSTDT ESNNEEQRSG LIYLTNHIAP
     HARNGLSLKE EHRAYDLLRA ASENSQDALR VVSTSGEQMK VYKCEHCRVL FLDHVMYTIH
     MGCHGFRDPF ECNMCGYHSQ DRYEFSSHIT RGEHRFHMS
//
ID   ITF2_HUMAN              Reviewed;         667 AA.
AC   P15884; B3KT62; B3KUC0; B4DT37; B4DUG3; B7Z5M6; B7Z6Y1; G0LNT9;
AC   G0LNU0; G0LNU1; G0LNU2; G0LNU4; G0LNU5; G0LNU8; G0LNU9; G0LNV0;
AC   G0LNV1; G0LNV2; H3BPQ1; Q08AP2; Q08AP3; Q15439; Q15440; Q15441;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-1998, sequence version 3.
DT   11-NOV-2015, entry version 171.
DE   RecName: Full=Transcription factor 4;
DE            Short=TCF-4;
DE   AltName: Full=Class B basic helix-loop-helix protein 19;
DE            Short=bHLHb19;
DE   AltName: Full=Immunoglobulin transcription factor 2;
DE            Short=ITF-2;
DE   AltName: Full=SL3-3 enhancer factor 2;
DE            Short=SEF-2;
GN   Name=TCF4; Synonyms=BHLHB19, ITF2, SEF2;
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 SEF2-1A; SEF2-1B AND SEF2-1D),
RP   AND ALTERNATIVE SPLICING (ISOFORM SEF2-1C).
RC   TISSUE=Thymocyte, and Thymus;
RX   PubMed=1681116;
RA   Corneliussen B., Thornell A., Hallberg B., Grundstroem T.;
RT   "Helix-loop-helix transcriptional activators bind to a sequence in
RT   glucocorticoid response elements of retrovirus enhancers.";
RL   J. Virol. 65:6084-6093(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A-; B-DELTA; B+DELTA; C-;
RP   C-DELTA; D-; E-; F-; G-; H-; I-; SEF2-1A; SEF2-1B AND SEF2-1D), AND
RP   ALTERNATIVE SPLICING.
RX   PubMed=21789225; DOI=10.1371/journal.pone.0022138;
RA   Sepp M., Kannike K., Eesmaa A., Urb M., Timmusk T.;
RT   "Functional diversity of human basic helix-loop-helix transcription
RT   factor TCF4 isoforms generated by alternative 5' exon usage and
RT   splicing.";
RL   PLoS ONE 6:E22138-E22138(2011).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS SEF2-1A; C-; D-; F-;
RP   11 AND 13).
RC   TISSUE=Brain, Hippocampus, Spleen, and Teratocarcinoma;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS SEF2-1B AND SEF2-1D).
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-278 (ISOFORM SEF2-1A).
RA   Gu J., Zhao M., Huang Q., Xu X., Li Y., Peng Y., Song H., Xiao H.,
RA   Gu Y., Li N., Qian B., Liu F., Qu J., Gao X., Cheng Z., Xu Z.,
RA   Zeng L., Xu S., Gu W., Tu Y., Jia J., Fu G., Ren S., Zhong M., Lu G.,
RA   Yang Y., Gao G., Zhang Q., Chen S., Han Z., Chen Z.;
RT   "MDSDCE06_MDS Homo sapiens cDNA clone MDSDCE06 5',mRNA sequence.";
RL   Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases.
RN   [8]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 25-48.
RC   TISSUE=Skin fibroblast;
RX   PubMed=9302263; DOI=10.1093/hmg/6.11.1855;
RA   Breschel T.S., McInnis M.G., Margolis R.L., Sirugo G.,
RA   Corneliussen B., Simpson S.G., McMahon F.J., Mackinnon D.F., Xu J.F.,
RA   Pleasant N., Huo Y., Ashworth R.G., Grundstrom C., Grundstrom T.,
RA   Kidd K.K., Depaulo J.R., Ross C.A.;
RT   "A novel, heritable, expanding CTG repeat in an intron of the SEF2-1
RT   gene on chromosome 18q21.1.";
RL   Hum. Mol. Genet. 6:1855-1863(1997).
RN   [9]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 46-667 (ISOFORM SEF2-1B).
RX   PubMed=2308860; DOI=10.1093/nar/18.3.678;
RA   Henthorn P., McCarrick-Walmsley R., Kadesch T.;
RT   "Sequence of the cDNA encoding ITF-2, a positive-acting transcription
RT   factor.";
RL   Nucleic Acids Res. 18:678-678(1990).
RN   [10]
RP   DISCUSSION OF SEQUENCE.
RX   PubMed=2105528; DOI=10.1126/science.2105528;
RA   Henthorn P., Kiledjian M., Kadesch T.;
RT   "Two distinct transcription factors that bind the immunoglobulin
RT   enhancer microE5/kappa 2 motif.";
RL   Science 247:467-470(1990).
RN   [11]
RP   DOMAIN.
RX   PubMed=17467953; DOI=10.1016/j.ygeno.2007.02.003;
RA   Piskacek S., Gregor M., Nemethova M., Grabner M., Kovarik P.,
RA   Piskacek M.;
RT   "Nine-amino-acid transactivation domain: establishment and prediction
RT   utilities.";
RL   Genomics 89:756-768(2007).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-515, 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   [13]
RP   SUBCELLULAR LOCATION, AND CHARACTERIZATION OF VARIANTS PTHS VAL-358;
RP   GLY-535; PRO-574; TRP-576 AND VAL-610.
RX   PubMed=22777675; DOI=10.1002/humu.22160;
RA   Forrest M., Chapman R.M., Doyle A.M., Tinsley C.L., Waite A.,
RA   Blake D.J.;
RT   "Functional analysis of TCF4 missense mutations that cause Pitt-
RT   Hopkins syndrome.";
RL   Hum. Mutat. 33:1676-1686(2012).
RN   [14]
RP   INTERACTION WITH AGBL1.
RX   PubMed=24094747; DOI=10.1016/j.ajhg.2013.08.010;
RA   Riazuddin S.A., Vasanth S., Katsanis N., Gottsch J.D.;
RT   "Mutations in AGBL1 cause dominant late-onset Fuchs corneal dystrophy
RT   and alter protein-protein interaction with TCF4.";
RL   Am. J. Hum. Genet. 93:758-764(2013).
RN   [15]
RP   INTERACTION WITH BHLHA9.
RX   PubMed=25466284; DOI=10.1016/j.ajhg.2014.10.012;
RA   Malik S., Percin F.E., Bornholdt D., Albrecht B., Percesepe A.,
RA   Koch M.C., Landi A., Fritz B., Khan R., Mumtaz S., Akarsu N.A.,
RA   Grzeschik K.H.;
RT   "Mutations affecting the BHLHA9 DNA-binding domain cause MSSD,
RT   mesoaxial synostotic syndactyly with phalangeal reduction, Malik-
RT   Percin type.";
RL   Am. J. Hum. Genet. 95:649-659(2014).
RN   [16]
RP   VARIANTS PTHS TRP-576 AND GLN-576.
RX   PubMed=17436254; DOI=10.1086/515582;
RA   Amiel J., Rio M., de Pontual L., Redon R., Malan V., Boddaert N.,
RA   Plouin P., Carter N.P., Lyonnet S., Munnich A., Colleaux L.;
RT   "Mutations in TCF4, encoding a class I basic helix-loop-helix
RT   transcription factor, are responsible for Pitt-Hopkins syndrome, a
RT   severe epileptic encephalopathy associated with autonomic
RT   dysfunction.";
RL   Am. J. Hum. Genet. 80:988-993(2007).
RN   [17]
RP   VARIANT PTHS TRP-576.
RX   PubMed=17436255; DOI=10.1086/515583;
RA   Zweier C., Peippo M.M., Hoyer J., Sousa S., Bottani A.,
RA   Clayton-Smith J., Reardon W., Saraiva J., Cabral A., Goehring I.,
RA   Devriendt K., de Ravel T., Bijlsma E.K., Hennekam R.C.M., Orrico A.,
RA   Cohen M., Dreweke A., Reis A., Nuernberg P., Rauch A.;
RT   "Haploinsufficiency of TCF4 causes syndromal mental retardation with
RT   intermittent hyperventilation (Pitt-Hopkins syndrome).";
RL   Am. J. Hum. Genet. 80:994-1001(2007).
RN   [18]
RP   VARIANTS PTHS VAL-358; PRO-574 AND HIS-578.
RX   PubMed=18728071; DOI=10.1136/jmg.2008.060129;
RA   Zweier C., Sticht H., Bijlsma E.K., Clayton-Smith J., Boonen S.E.,
RA   Fryer A., Greally M.T., Hoffmann L., den Hollander N.S., Jongmans M.,
RA   Kant S.G., King M.D., Lynch S.A., McKee S., Midro A.T., Park S.M.,
RA   Ricotti V., Tarantino E., Wessels M., Peippo M., Rauch A.;
RT   "Further delineation of Pitt-Hopkins syndrome: phenotypic and
RT   genotypic description of 16 novel patients.";
RL   J. Med. Genet. 45:738-744(2008).
RN   [19]
RP   VARIANTS PTHS GLY-535; GLY-572; GLN-576 AND VAL-610, AND
RP   CHARACTERIZATION OF VARIANTS PTHS GLY-535; GLY-572; GLN-576 AND
RP   VAL-610.
RX   PubMed=19235238; DOI=10.1002/humu.20935;
RA   de Pontual L., Mathieu Y., Golzio C., Rio M., Malan V., Boddaert N.,
RA   Soufflet C., Picard C., Durandy A., Dobbie A., Heron D., Isidor B.,
RA   Motte J., Newburry-Ecob R., Pasquier L., Tardieu M., Viot G.,
RA   Jaubert F., Munnich A., Colleaux L., Vekemans M., Etchevers H.,
RA   Lyonnet S., Amiel J.;
RT   "Mutational, functional, and expression studies of the TCF4 gene in
RT   Pitt-Hopkins syndrome.";
RL   Hum. Mutat. 30:669-676(2009).
RN   [20]
RP   VARIANT PTHS PRO-578.
RX   PubMed=20184619; DOI=10.1111/j.1399-0004.2010.01380.x;
RA   Takano K., Lyons M., Moyes C., Jones J., Schwartz C.E.;
RT   "Two percent of patients suspected of having Angelman syndrome have
RT   TCF4 mutations.";
RL   Clin. Genet. 78:282-288(2010).
RN   [21]
RP   VARIANTS PTHS TRP-565; GLY-572; GLN-572; HIS-574; PRO-574; TRP-576;
RP   GLN-576; PRO-578; PRO-583 AND VAL-610.
RX   PubMed=22045651; DOI=10.1002/humu.21639;
RA   Whalen S., Heron D., Gaillon T., Moldovan O., Rossi M., Devillard F.,
RA   Giuliano F., Soares G., Mathieu-Dramard M., Afenjar A., Charles P.,
RA   Mignot C., Burglen L., Van Maldergem L., Piard J., Aftimos S.,
RA   Mancini G., Dias P., Philip N., Goldenberg A., Le Merrer M., Rio M.,
RA   Josifova D., Van Hagen J.M., Lacombe D., Edery P., Dupuis-Girod S.,
RA   Putoux A., Sanlaville D., Fischer R., Drevillon L., Briand-Suleau A.,
RA   Metay C., Goossens M., Amiel J., Jacquette A., Giurgea I.;
RT   "Novel comprehensive diagnostic strategy in Pitt-Hopkins syndrome:
RT   clinical score and further delineation of the TCF4 mutational
RT   spectrum.";
RL   Hum. Mutat. 33:64-72(2012).
CC   -!- FUNCTION: Transcription factor that binds to the immunoglobulin
CC       enchancer Mu-E5/KE5-motif. Involved in the initiation of neuronal
CC       differentiation. Activates transcription by binding to the E box
CC       (5'-CANNTG-3'). Binds to the E-box present in the somatostatin
CC       receptor 2 initiator element (SSTR2-INR) to activate transcription
CC       (By similarity). Preferentially binds to either 5'-ACANNTGT-3' or
CC       5'-CCANNTGG-3'. {ECO:0000250}.
CC   -!- SUBUNIT: Efficient DNA binding requires dimerization with another
CC       bHLH protein. Forms homo- or heterooligomers with myogenin.
CC       Interacts with HIVEP2. Interacts with NEUROD2 (By similarity).
CC       Interacts with AGBL1. Interacts with BHLHA9. {ECO:0000250,
CC       ECO:0000269|PubMed:24094747, ECO:0000269|PubMed:25466284}.
CC   -!- INTERACTION:
CC       Q53FW8:-; NbExp=3; IntAct=EBI-533224, EBI-10242473;
CC       Q08117:AES; NbExp=3; IntAct=EBI-533224, EBI-717810;
CC       P29972:AQP1; NbExp=3; IntAct=EBI-533224, EBI-745213;
CC       Q92888:ARHGEF1; NbExp=3; IntAct=EBI-533224, EBI-465400;
CC       Q9H6L4:ARMC7; NbExp=3; IntAct=EBI-533224, EBI-742909;
CC       P50553:ASCL1; NbExp=7; IntAct=EBI-533224, EBI-957042;
CC       Q6XD76:ASCL4; NbExp=3; IntAct=EBI-533224, EBI-10254793;
CC       Q9BZE9:ASPSCR1; NbExp=3; IntAct=EBI-533224, EBI-1993677;
CC       P21281:ATP6V1B2; NbExp=3; IntAct=EBI-533224, EBI-4290814;
CC       O75934:BCAS2; NbExp=3; IntAct=EBI-533224, EBI-1050106;
CC       Q92843:BCL2L2; NbExp=3; IntAct=EBI-533224, EBI-707714;
CC       Q9NUL5:C19orf66; NbExp=3; IntAct=EBI-533224, EBI-10313866;
CC       Q9NX04:C1orf109; NbExp=3; IntAct=EBI-533224, EBI-8643161;
CC       Q6ZQR2:C9orf171; NbExp=3; IntAct=EBI-533224, EBI-10255140;
CC       Q9NP86:CABP5; NbExp=3; IntAct=EBI-533224, EBI-10311131;
CC       Q96ES7:CCDC101; NbExp=3; IntAct=EBI-533224, EBI-743117;
CC       P38936:CDKN1A; NbExp=3; IntAct=EBI-533224, EBI-375077;
CC       P42773:CDKN2C; NbExp=3; IntAct=EBI-533224, EBI-711290;
CC       Q13111:CHAF1A; NbExp=3; IntAct=EBI-533224, EBI-1020839;
CC       Q9Y6H1:CHCHD2; NbExp=3; IntAct=EBI-533224, EBI-2321769;
CC       Q9UKJ5:CHIC2; NbExp=3; IntAct=EBI-533224, EBI-741528;
CC       P61024:CKS1B; NbExp=3; IntAct=EBI-533224, EBI-456371;
CC       P35222:CTNNB1; NbExp=19; IntAct=EBI-533224, EBI-491549;
CC       P26233:ctnnb1 (xeno); NbExp=2; IntAct=EBI-533224, EBI-7373758;
CC       P26196:DDX6; NbExp=3; IntAct=EBI-533224, EBI-351257;
CC       Q9H4E7:DEF6; NbExp=3; IntAct=EBI-533224, EBI-745369;
CC       Q9NQL9:DMRT3; NbExp=3; IntAct=EBI-533224, EBI-9679045;
CC       Q5JVL4:EFHC1; NbExp=6; IntAct=EBI-533224, EBI-743105;
CC       O60573:EIF4E2; NbExp=3; IntAct=EBI-533224, EBI-398610;
CC       Q13541:EIF4EBP1; NbExp=3; IntAct=EBI-533224, EBI-74090;
CC       Q9Y2J2-3:EPB41L3; NbExp=3; IntAct=EBI-533224, EBI-10326138;
CC       O15197-2:EPHB6; NbExp=3; IntAct=EBI-533224, EBI-10182490;
CC       Q9Y3B2:EXOSC1; NbExp=3; IntAct=EBI-533224, EBI-371892;
CC       P16930:FAH; NbExp=3; IntAct=EBI-533224, EBI-4397076;
CC       Q9H5Z6:FAM124B; NbExp=3; IntAct=EBI-533224, EBI-741626;
CC       Q5TZK3:FAM74A6; NbExp=3; IntAct=EBI-533224, EBI-10247271;
CC       Q96RJ6:FERD3L; NbExp=3; IntAct=EBI-533224, EBI-10183007;
CC       Q96AC1:FERMT2; NbExp=6; IntAct=EBI-533224, EBI-4399465;
CC       Q8NFF5:FLAD1; NbExp=3; IntAct=EBI-533224, EBI-742815;
CC       P21333-2:FLNA; NbExp=3; IntAct=EBI-533224, EBI-9641086;
CC       O43559:FRS3; NbExp=3; IntAct=EBI-533224, EBI-725515;
CC       P55040:GEM; NbExp=3; IntAct=EBI-533224, EBI-744104;
CC       O76003:GLRX3; NbExp=3; IntAct=EBI-533224, EBI-374781;
CC       P50151:GNG10; NbExp=3; IntAct=EBI-533224, EBI-10211741;
CC       Q0D2H9:GOLGA8DP; NbExp=3; IntAct=EBI-533224, EBI-10181276;
CC       Q08AF8:GOLGA8G; NbExp=3; IntAct=EBI-533224, EBI-10181260;
CC       Q9H8Y8:GORASP2; NbExp=3; IntAct=EBI-533224, EBI-739467;
CC       Q96NT3:GUCD1; NbExp=3; IntAct=EBI-533224, EBI-8293751;
CC       P61296:HAND2; NbExp=3; IntAct=EBI-533224, EBI-10218584;
CC       O14929:HAT1; NbExp=3; IntAct=EBI-533224, EBI-2339359;
CC       V9HWF5:HEL-S-69p; NbExp=3; IntAct=EBI-533224, EBI-10330249;
CC       Q9UBY9:HSPB7; NbExp=3; IntAct=EBI-533224, EBI-739361;
CC       Q02535:ID3; NbExp=3; IntAct=EBI-533224, EBI-1387094;
CC       I3WAC9:INS; NbExp=3; IntAct=EBI-533224, EBI-10178524;
CC       Q9BQ13:KCTD14; NbExp=3; IntAct=EBI-533224, EBI-10189448;
CC       Q6P597:KLC3; NbExp=3; IntAct=EBI-533224, EBI-1643885;
CC       Q5THT1:KLHL32; NbExp=3; IntAct=EBI-533224, EBI-10247181;
CC       Q14847:LASP1; NbExp=3; IntAct=EBI-533224, EBI-742828;
CC       Q96BZ8:LENG1; NbExp=3; IntAct=EBI-533224, EBI-726510;
CC       Q8TCE9:LGALS14; NbExp=3; IntAct=EBI-533224, EBI-10274069;
CC       P25800:LMO1; NbExp=3; IntAct=EBI-533224, EBI-8639312;
CC       P61968:LMO4; NbExp=3; IntAct=EBI-533224, EBI-2798728;
CC       Q9UIQ6:LNPEP; NbExp=3; IntAct=EBI-533224, EBI-2805360;
CC       Q9UI95:MAD2L2; NbExp=3; IntAct=EBI-533224, EBI-77889;
CC       Q96A72:MAGOHB; NbExp=3; IntAct=EBI-533224, EBI-746778;
CC       O60336:MAPKBP1; NbExp=3; IntAct=EBI-533224, EBI-947402;
CC       O15232:MATN3; NbExp=3; IntAct=EBI-533224, EBI-6262458;
CC       Q9Y316:MEMO1; NbExp=3; IntAct=EBI-533224, EBI-1104564;
CC       Q6P2C6:MLLT6; NbExp=3; IntAct=EBI-533224, EBI-5773143;
CC       Q8NDC4:MORN4; NbExp=3; IntAct=EBI-533224, EBI-10269566;
CC       Q96HT8:MRFAP1L1; NbExp=3; IntAct=EBI-533224, EBI-748896;
CC       Q7Z7H8:MRPL10; NbExp=3; IntAct=EBI-533224, EBI-723524;
CC       Q8IXL7:MSRB3; NbExp=3; IntAct=EBI-533224, EBI-8634060;
CC       Q9ULV0:MYO5B; NbExp=3; IntAct=EBI-533224, EBI-311356;
CC       O43639:NCK2; NbExp=3; IntAct=EBI-533224, EBI-713635;
CC       Q9UHB4:NDOR1; NbExp=3; IntAct=EBI-533224, EBI-10249760;
CC       Q9HC98:NEK6; NbExp=3; IntAct=EBI-533224, EBI-740364;
CC       Q86SG6:NEK8; NbExp=3; IntAct=EBI-533224, EBI-1752987;
CC       Q8WWR8-2:NEU4; NbExp=3; IntAct=EBI-533224, EBI-10277551;
CC       Q92886:NEUROG1; NbExp=3; IntAct=EBI-533224, EBI-10279647;
CC       Q9Y5B8:NME7; NbExp=3; IntAct=EBI-533224, EBI-744782;
CC       Q9GZQ4:NMUR2; NbExp=3; IntAct=EBI-533224, EBI-10303844;
CC       Q5SY16:NOL9; NbExp=3; IntAct=EBI-533224, EBI-1055462;
CC       Q86WQ0:NR2C2AP; NbExp=3; IntAct=EBI-533224, EBI-10260040;
CC       Q8NFP7:NUDT10; NbExp=3; IntAct=EBI-533224, EBI-726826;
CC       O43929:ORC4; NbExp=3; IntAct=EBI-533224, EBI-374889;
CC       Q9UJX0:OSGIN1; NbExp=3; IntAct=EBI-533224, EBI-9057006;
CC       Q01804:OTUD4; NbExp=3; IntAct=EBI-533224, EBI-1054396;
CC       Q8WXA2:PATE1; NbExp=3; IntAct=EBI-533224, EBI-10277790;
CC       P30039:PBLD; NbExp=3; IntAct=EBI-533224, EBI-750589;
CC       Q13526:PIN1; NbExp=3; IntAct=EBI-533224, EBI-714158;
CC       Q494U1:PLEKHN1; NbExp=3; IntAct=EBI-533224, EBI-10241513;
CC       O95602:POLR1A; NbExp=3; IntAct=EBI-533224, EBI-359472;
CC       O15160:POLR1C; NbExp=3; IntAct=EBI-533224, EBI-1055079;
CC       Q9Y3C6:PPIL1; NbExp=3; IntAct=EBI-533224, EBI-2557649;
CC       Q6NYC8:PPP1R18; NbExp=3; IntAct=EBI-533224, EBI-2557469;
CC       P54646:PRKAA2; NbExp=3; IntAct=EBI-533224, EBI-1383852;
CC       P25786:PSMA1; NbExp=3; IntAct=EBI-533224, EBI-359352;
CC       Q969U7:PSMG2; NbExp=3; IntAct=EBI-533224, EBI-723276;
CC       Q147X8:PTGER3; NbExp=3; IntAct=EBI-533224, EBI-10234038;
CC       Q5JT25:RAB41; NbExp=3; IntAct=EBI-533224, EBI-10244509;
CC       P47224:RABIF; NbExp=3; IntAct=EBI-533224, EBI-713992;
CC       Q6P9E2:RECK; NbExp=3; IntAct=EBI-533224, EBI-10253121;
CC       Q04206-3:RELA; NbExp=3; IntAct=EBI-533224, EBI-10223388;
CC       Q8IX06:REXO1L1P; NbExp=3; IntAct=EBI-533224, EBI-10262361;
CC       Q9UHP6:RSPH14; NbExp=3; IntAct=EBI-533224, EBI-748350;
CC       Q9UIL1:SCOC; NbExp=3; IntAct=EBI-533224, EBI-2686537;
CC       Q9UDX3:SEC14L4; NbExp=3; IntAct=EBI-533224, EBI-10320311;
CC       Q6NXQ0:SFRS2; NbExp=3; IntAct=EBI-533224, EBI-10251550;
CC       O43699:SIGLEC6; NbExp=3; IntAct=EBI-533224, EBI-2814604;
CC       Q96H72:SLC39A13; NbExp=3; IntAct=EBI-533224, EBI-10287091;
CC       Q9BWU0:SLC4A1AP; NbExp=3; IntAct=EBI-533224, EBI-1999704;
CC       P49901:SMCP; NbExp=3; IntAct=EBI-533224, EBI-750494;
CC       Q9H4F8:SMOC1; NbExp=3; IntAct=EBI-533224, EBI-2801103;
CC       Q61473:Sox17 (xeno); NbExp=5; IntAct=EBI-533224, EBI-9106822;
CC       Q06831:Sox4 (xeno); NbExp=2; IntAct=EBI-533224, EBI-6262177;
CC       Q9H0A9:SPATC1L; NbExp=3; IntAct=EBI-533224, EBI-372911;
CC       Q9NZD8:SPG21; NbExp=3; IntAct=EBI-533224, EBI-742688;
CC       Q96FJ0:STAMBPL1; NbExp=3; IntAct=EBI-533224, EBI-745021;
CC       O75716:STK16; NbExp=3; IntAct=EBI-533224, EBI-749295;
CC       O75558:STX11; NbExp=3; IntAct=EBI-533224, EBI-714135;
CC       Q5T011-5:SZT2; NbExp=3; IntAct=EBI-533224, EBI-10245139;
CC       Q16559:TAL2; NbExp=3; IntAct=EBI-533224, EBI-10237959;
CC       Q15560:TCEA2; NbExp=3; IntAct=EBI-533224, EBI-710310;
CC       P56279:TCL1A; NbExp=3; IntAct=EBI-533224, EBI-749995;
CC       Q9UL33:TRAPPC2L; NbExp=3; IntAct=EBI-533224, EBI-747601;
CC       Q96PN8:TSSK3; NbExp=3; IntAct=EBI-533224, EBI-3918381;
CC       Q8WVJ9:TWIST2; NbExp=3; IntAct=EBI-533224, EBI-1797313;
CC       Q9NX01:TXNL4B; NbExp=3; IntAct=EBI-533224, EBI-10309345;
CC       Q9BRU9:UTP23; NbExp=3; IntAct=EBI-533224, EBI-5457544;
CC       Q548N1:VPS28; NbExp=3; IntAct=EBI-533224, EBI-10243107;
CC       Q6UX98:ZDHHC24; NbExp=3; IntAct=EBI-533224, EBI-10254561;
CC       Q15973:ZNF124; NbExp=3; IntAct=EBI-533224, EBI-2555767;
CC       Q8TAU3:ZNF417; NbExp=3; IntAct=EBI-533224, EBI-740727;
CC       Q96SQ5:ZNF587; NbExp=3; IntAct=EBI-533224, EBI-6427977;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-
CC       ProRule:PRU00981, ECO:0000269|PubMed:22777675}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=16;
CC         Comment=Additional isoforms seem to exist.;
CC       Name=SEF2-1B; Synonyms=B-;
CC         IsoId=P15884-1; Sequence=Displayed;
CC       Name=SEF2-1A; Synonyms=A+;
CC         IsoId=P15884-2; Sequence=VSP_030819, VSP_002111, VSP_002112;
CC       Name=SEF2-1D; Synonyms=B+;
CC         IsoId=P15884-3; Sequence=VSP_002112;
CC       Name=B+delta;
CC         IsoId=P15884-4; Sequence=VSP_044340, VSP_002112;
CC       Name=B-delta;
CC         IsoId=P15884-5; Sequence=VSP_044340;
CC       Name=A-;
CC         IsoId=P15884-6; Sequence=VSP_044336, VSP_044337, VSP_044340;
CC       Name=G-;
CC         IsoId=P15884-7; Sequence=VSP_044334, VSP_044338, VSP_044339;
CC       Name=H-;
CC         IsoId=P15884-8; Sequence=VSP_044335, VSP_057364;
CC       Name=D-;
CC         IsoId=P15884-9; Sequence=VSP_045149;
CC       Name=F-;
CC         IsoId=P15884-10; Sequence=VSP_045151;
CC       Name=11;
CC         IsoId=P15884-11; Sequence=VSP_045150, VSP_044339, VSP_002112;
CC       Name=E-;
CC         IsoId=P15884-12; Sequence=VSP_047082, VSP_047083;
CC       Name=13;
CC         IsoId=P15884-13; Sequence=VSP_047081, VSP_002112;
CC       Name=C-;
CC         IsoId=P15884-14; Sequence=VSP_047081;
CC       Name=C-delta;
CC         IsoId=P15884-15; Sequence=VSP_047081, VSP_044340;
CC       Name=I-;
CC         IsoId=P15884-16; Sequence=VSP_054279;
CC   -!- TISSUE SPECIFICITY: Expressed in adult heart, brain, placenta,
CC       skeletal muscle and to a lesser extent in the lung. In developing
CC       embryonic tissues, expression mostly occurs in the brain.
CC   -!- DOMAIN: the 9aaTAD motif is a transactivation domain present in a
CC       large number of yeast and animal transcription factors.
CC       {ECO:0000269|PubMed:17467953}.
CC   -!- DISEASE: Pitt-Hopkins syndrome (PTHS) [MIM:610954]: A syndrome
CC       characterized by mental retardation, wide mouth and distinctive
CC       facial features, and intermittent hyperventilation followed by
CC       apnea. Features include intellectual disability with severe speech
CC       impairment, normal growth parameters at birth, postnatal
CC       microcephaly, breathing anomalies, severe motor developmental
CC       delay, motor incoordination, ocular anomalies, constipation,
CC       seizures, typical behavior and subtle brain abnormalities.
CC       {ECO:0000269|PubMed:17436254, ECO:0000269|PubMed:17436255,
CC       ECO:0000269|PubMed:18728071, ECO:0000269|PubMed:19235238,
CC       ECO:0000269|PubMed:20184619, ECO:0000269|PubMed:22045651}.
CC       Note=The disease is caused by mutations affecting the gene
CC       represented in this entry.
CC   -!- SIMILARITY: Contains 1 bHLH (basic helix-loop-helix) domain.
CC       {ECO:0000255|PROSITE-ProRule:PRU00981}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA60310.1; Type=Miscellaneous discrepancy; Note=Incomplete and probable erroneous sequence.; Evidence={ECO:0000305};
CC       Sequence=AAA60312.1; Type=Miscellaneous discrepancy; Note=Incomplete and probable erroneous sequence.; Evidence={ECO:0000305};
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DR   EMBL; M74718; AAA60310.1; ALT_SEQ; mRNA.
DR   EMBL; M74719; AAA60311.1; -; mRNA.
DR   EMBL; M74720; AAA60312.1; ALT_SEQ; mRNA.
DR   EMBL; FR748210; CBY80189.1; -; mRNA.
DR   EMBL; FR748211; CBY80190.1; -; mRNA.
DR   EMBL; FR748212; CBY80191.1; -; mRNA.
DR   EMBL; FR748213; CBY80192.1; -; mRNA.
DR   EMBL; FR748214; CBY80193.1; -; mRNA.
DR   EMBL; FR748215; CBY80194.1; -; mRNA.
DR   EMBL; FR748216; CBY80195.1; -; mRNA.
DR   EMBL; FR748217; CBY80196.1; -; mRNA.
DR   EMBL; FR748218; CBY80197.1; -; mRNA.
DR   EMBL; FR748219; CBY80198.1; -; mRNA.
DR   EMBL; FR748220; CBY80199.1; -; mRNA.
DR   EMBL; FR748221; CBY80200.1; -; mRNA.
DR   EMBL; FR748222; CBY80201.1; -; mRNA.
DR   EMBL; FR748223; CBY80202.1; -; mRNA.
DR   EMBL; AK095041; BAG52974.1; -; mRNA.
DR   EMBL; AK096862; BAG53382.1; -; mRNA.
DR   EMBL; AK299169; BAH12962.1; -; mRNA.
DR   EMBL; AK300636; BAG62325.1; -; mRNA.
DR   EMBL; AK300038; BAG61849.1; -; mRNA.
DR   EMBL; AK301144; BAH13417.1; -; mRNA.
DR   EMBL; AK300612; BAH13314.1; -; mRNA.
DR   EMBL; AK316165; BAH14536.1; -; mRNA.
DR   EMBL; AC013587; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC018994; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC090383; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC090684; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC091103; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471096; EAW63017.1; -; Genomic_DNA.
DR   EMBL; CH471096; EAW63018.1; -; Genomic_DNA.
DR   EMBL; BC125084; AAI25085.1; -; mRNA.
DR   EMBL; BC125085; AAI25086.1; -; mRNA.
DR   EMBL; AV761952; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; U75701; AAC51824.1; -; Genomic_DNA.
DR   EMBL; X52079; CAA36298.1; -; mRNA.
DR   CCDS; CCDS11960.1; -. [P15884-1]
DR   CCDS; CCDS42438.1; -. [P15884-3]
DR   CCDS; CCDS58623.1; -. [P15884-8]
DR   CCDS; CCDS58624.1; -. [P15884-2]
DR   CCDS; CCDS58625.1; -. [P15884-6]
DR   CCDS; CCDS58626.1; -. [P15884-9]
DR   CCDS; CCDS58627.1; -. [P15884-11]
DR   CCDS; CCDS58628.1; -. [P15884-10]
DR   CCDS; CCDS58629.1; -. [P15884-13]
DR   CCDS; CCDS59321.1; -. [P15884-12]
DR   CCDS; CCDS77191.1; -. [P15884-7]
DR   CCDS; CCDS77192.1; -. [P15884-14]
DR   PIR; A41311; A41311.
DR   RefSeq; NP_001077431.1; NM_001083962.1. [P15884-3]
DR   RefSeq; NP_001230155.2; NM_001243226.2.
DR   RefSeq; NP_001230156.1; NM_001243227.1. [P15884-13]
DR   RefSeq; NP_001230157.1; NM_001243228.1.
DR   RefSeq; NP_001230159.1; NM_001243230.1. [P15884-12]
DR   RefSeq; NP_001230160.1; NM_001243231.1. [P15884-10]
DR   RefSeq; NP_001230161.1; NM_001243232.1. [P15884-11]
DR   RefSeq; NP_001230162.1; NM_001243233.1. [P15884-9]
DR   RefSeq; NP_001230163.1; NM_001243234.1. [P15884-2]
DR   RefSeq; NP_001230164.1; NM_001243235.1. [P15884-6]
DR   RefSeq; NP_001230165.1; NM_001243236.1. [P15884-8]
DR   RefSeq; NP_001293136.1; NM_001306207.1. [P15884-14]
DR   RefSeq; NP_001293137.1; NM_001306208.1. [P15884-7]
DR   RefSeq; NP_003190.1; NM_003199.2. [P15884-1]
DR   RefSeq; XP_005266796.2; XM_005266739.3. [P15884-13]
DR   RefSeq; XP_005266800.1; XM_005266743.3. [P15884-13]
DR   RefSeq; XP_005266801.1; XM_005266744.3. [P15884-13]
DR   RefSeq; XP_006722599.1; XM_006722536.2. [P15884-3]
DR   RefSeq; XP_006722600.1; XM_006722537.2. [P15884-3]
DR   RefSeq; XP_006722603.1; XM_006722540.2. [P15884-9]
DR   RefSeq; XP_011524466.1; XM_011526164.1. [P15884-9]
DR   UniGene; Hs.605153; -.
DR   UniGene; Hs.742885; -.
DR   PDB; 2KWF; NMR; -; B=11-27.
DR   PDBsum; 2KWF; -.
DR   DisProt; DP00224; -.
DR   ProteinModelPortal; P15884; -.
DR   SMR; P15884; 565-624.
DR   BioGrid; 112787; 193.
DR   DIP; DIP-163N; -.
DR   IntAct; P15884; 151.
DR   MINT; MINT-4508073; -.
DR   STRING; 9606.ENSP00000346440; -.
DR   PhosphoSite; P15884; -.
DR   BioMuta; TCF4; -.
DR   MaxQB; P15884; -.
DR   PaxDb; P15884; -.
DR   PRIDE; P15884; -.
DR   Ensembl; ENST00000354452; ENSP00000346440; ENSG00000196628. [P15884-3]
DR   Ensembl; ENST00000356073; ENSP00000348374; ENSG00000196628. [P15884-1]
DR   Ensembl; ENST00000457482; ENSP00000409447; ENSG00000196628. [P15884-2]
DR   Ensembl; ENST00000537578; ENSP00000440731; ENSG00000196628. [P15884-13]
DR   Ensembl; ENST00000537856; ENSP00000439827; ENSG00000196628. [P15884-9]
DR   Ensembl; ENST00000540999; ENSP00000445202; ENSG00000196628. [P15884-14]
DR   Ensembl; ENST00000543082; ENSP00000439656; ENSG00000196628. [P15884-10]
DR   Ensembl; ENST00000544241; ENSP00000441562; ENSG00000196628. [P15884-11]
DR   Ensembl; ENST00000561831; ENSP00000457765; ENSG00000196628. [P15884-8]
DR   Ensembl; ENST00000561992; ENSP00000455179; ENSG00000196628. [P15884-9]
DR   Ensembl; ENST00000564228; ENSP00000455261; ENSG00000196628. [P15884-7]
DR   Ensembl; ENST00000564999; ENSP00000457649; ENSG00000196628. [P15884-1]
DR   Ensembl; ENST00000565018; ENSP00000455984; ENSG00000196628. [P15884-15]
DR   Ensembl; ENST00000566279; ENSP00000456125; ENSG00000196628. [P15884-4]
DR   Ensembl; ENST00000566286; ENSP00000455418; ENSG00000196628. [P15884-12]
DR   Ensembl; ENST00000567880; ENSP00000454366; ENSG00000196628. [P15884-5]
DR   Ensembl; ENST00000568673; ENSP00000455135; ENSG00000196628. [P15884-13]
DR   Ensembl; ENST00000570177; ENSP00000454647; ENSG00000196628. [P15884-9]
DR   Ensembl; ENST00000570287; ENSP00000455763; ENSG00000196628. [P15884-6]
DR   Ensembl; ENST00000616053; ENSP00000478549; ENSG00000196628. [P15884-15]
DR   Ensembl; ENST00000626584; ENSP00000486072; ENSG00000196628. [P15884-16]
DR   Ensembl; ENST00000629387; ENSP00000486670; ENSG00000196628. [P15884-3]
DR   GeneID; 6925; -.
DR   KEGG; hsa:6925; -.
DR   UCSC; uc002lfw.4; human. [P15884-2]
DR   UCSC; uc002lfx.2; human.
DR   UCSC; uc002lfy.2; human.
DR   UCSC; uc002lfz.2; human. [P15884-1]
DR   UCSC; uc010dph.1; human. [P15884-3]
DR   UCSC; uc010xdy.1; human.
DR   UCSC; uc021ukh.1; human. [P15884-6]
DR   UCSC; uc021uki.1; human. [P15884-7]
DR   UCSC; uc021ukj.1; human. [P15884-5]
DR   UCSC; uc021ukk.1; human. [P15884-4]
DR   CTD; 6925; -.
DR   GeneCards; TCF4; -.
DR   GeneReviews; TCF4; -.
DR   HGNC; HGNC:11634; TCF4.
DR   HPA; CAB020722; -.
DR   HPA; HPA025958; -.
DR   MIM; 602272; gene.
DR   MIM; 610954; phenotype.
DR   neXtProt; NX_P15884; -.
DR   Orphanet; 178469; Autosomal dominant non-syndromic intellectual disability.
DR   Orphanet; 98974; Fuchs endothelial corneal dystrophy.
DR   Orphanet; 2896; Pitt-Hopkins syndrome.
DR   Orphanet; 171; Primary sclerosing cholangitis.
DR   Orphanet; 3140; Schizophrenia.
DR   PharmGKB; PA164742621; -.
DR   eggNOG; KOG3910; Eukaryota.
DR   eggNOG; ENOG410XYUA; LUCA.
DR   GeneTree; ENSGT00510000046438; -.
DR   HOGENOM; HOG000234180; -.
DR   HOVERGEN; HBG003854; -.
DR   InParanoid; P15884; -.
DR   KO; K15603; -.
DR   OrthoDB; EOG72G16Q; -.
DR   PhylomeDB; P15884; -.
DR   TreeFam; TF321672; -.
DR   Reactome; R-HSA-375170; CDO in myogenesis.
DR   SignaLink; P15884; -.
DR   ChiTaRS; TCF4; human.
DR   EvolutionaryTrace; P15884; -.
DR   GeneWiki; TCF4; -.
DR   GenomeRNAi; 6925; -.
DR   NextBio; 27093; -.
DR   PRO; PR:P15884; -.
DR   Proteomes; UP000005640; Chromosome 18.
DR   Bgee; P15884; -.
DR   CleanEx; HS_TCF4; -.
DR   ExpressionAtlas; P15884; baseline and differential.
DR   Genevisible; P15884; HS.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0005667; C:transcription factor complex; ISS:BHF-UCL.
DR   GO; GO:0043425; F:bHLH transcription factor binding; IBA:GO_Central.
DR   GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR   GO; GO:0070888; F:E-box binding; ISS:UniProtKB.
DR   GO; GO:0008022; F:protein C-terminus binding; IPI:UniProtKB.
DR   GO; GO:0046982; F:protein heterodimerization activity; ISS:UniProtKB.
DR   GO; GO:0042803; F:protein homodimerization activity; IBA:GO_Central.
DR   GO; GO:0000978; F:RNA polymerase II core promoter proximal region sequence-specific DNA binding; ISS:BHF-UCL.
DR   GO; GO:0001093; F:TFIIB-class transcription factor binding; ISS:BHF-UCL.
DR   GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IDA:UniProtKB.
DR   GO; GO:0001011; F:transcription factor activity, sequence-specific DNA binding, RNA polymerase recruiting; ISS:BHF-UCL.
DR   GO; GO:0001087; F:transcription factor activity, TFIIB-class binding; ISS:BHF-UCL.
DR   GO; GO:0001077; F:transcriptional activator activity, RNA polymerase II core promoter proximal region sequence-specific binding; ISS:BHF-UCL.
DR   GO; GO:0006352; P:DNA-templated transcription, initiation; ISS:BHF-UCL.
DR   GO; GO:0045666; P:positive regulation of neuron differentiation; ISS:UniProtKB.
DR   GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; ISS:BHF-UCL.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR   GO; GO:0065004; P:protein-DNA complex assembly; ISS:BHF-UCL.
DR   GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; ISS:BHF-UCL.
DR   Gene3D; 4.10.280.10; -; 1.
DR   InterPro; IPR011598; bHLH_dom.
DR   Pfam; PF00010; HLH; 1.
DR   SMART; SM00353; HLH; 1.
DR   SUPFAM; SSF47459; SSF47459; 1.
DR   PROSITE; PS50888; BHLH; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Activator; Alternative splicing; Complete proteome;
KW   Differentiation; Disease mutation; DNA-binding; Epilepsy;
KW   Mental retardation; Neurogenesis; Nucleus; Phosphoprotein;
KW   Polymorphism; Primary microcephaly; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN         1    667       Transcription factor 4.
FT                                /FTId=PRO_0000127256.
FT   DOMAIN      564    617       bHLH. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00981}.
FT   REGION        1     83       Essential for MYOD1 inhibition.
FT                                {ECO:0000250}.
FT   REGION      379    400       Leucine-zipper.
FT   REGION      619    642       Class A specific domain.
FT   MOTIF        18     26       9aaTAD.
FT   COMPBIAS    228    231       Poly-Ser.
FT   MOD_RES     372    372       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q62655}.
FT   MOD_RES     515    515       Phosphoserine.
FT                                {ECO:0000244|PubMed:21406692}.
FT   VAR_SEQ       1    216       Missing (in isoform I-).
FT                                {ECO:0000303|PubMed:21789225}.
FT                                /FTId=VSP_054279.
FT   VAR_SEQ       1    160       Missing (in isoform SEF2-1A).
FT                                {ECO:0000303|PubMed:14702039,
FT                                ECO:0000303|PubMed:1681116,
FT                                ECO:0000303|PubMed:21789225,
FT                                ECO:0000303|Ref.7}.
FT                                /FTId=VSP_030819.
FT   VAR_SEQ       1    130       Missing (in isoform D-).
FT                                {ECO:0000303|PubMed:14702039,
FT                                ECO:0000303|PubMed:21789225}.
FT                                /FTId=VSP_045149.
FT   VAR_SEQ       1    102       MHHQQRMAALGTDKELSDLLDFSAMFSPPVSSGKNGPTSLA
FT                                SGHFTGSNVEDRSSSGSWGNGGHPSPSRNYGDGTPYDHMTS
FT                                RDLGSHDNLSPPFVNSRIQS -> MKDIFFQFIIARVRKCY
FT                                SLSCLHTLPVVPTLR (in isoform 11).
FT                                {ECO:0000303|PubMed:14702039}.
FT                                /FTId=VSP_045150.
FT   VAR_SEQ       1     49       MHHQQRMAALGTDKELSDLLDFSAMFSPPVSSGKNGPTSLA
FT                                SGHFTGSN -> MEEDSRD (in isoform F-).
FT                                {ECO:0000303|PubMed:14702039,
FT                                ECO:0000303|PubMed:21789225}.
FT                                /FTId=VSP_045151.
FT   VAR_SEQ       1     32       MHHQQRMAALGTDKELSDLLDFSAMFSPPVSS -> MKDIF
FT                                FQFIIARVRKCYSLSCLHTLPVVPTLR (in isoform
FT                                G-). {ECO:0000303|PubMed:21789225}.
FT                                /FTId=VSP_044334.
FT   VAR_SEQ       1     24       Missing (in isoform 13, isoform C- and
FT                                isoform C-delta).
FT                                {ECO:0000303|PubMed:14702039,
FT                                ECO:0000303|PubMed:21789225}.
FT                                /FTId=VSP_047081.
FT   VAR_SEQ       1     24       MHHQQRMAALGTDKELSDLLDFSA -> MQRAKTELFRLQI
FT                                VTDDLRKNE (in isoform E-).
FT                                {ECO:0000303|PubMed:21789225}.
FT                                /FTId=VSP_047082.
FT   VAR_SEQ       1     23       MHHQQRMAALGTDKELSDLLDFS -> MYCAYTIPGMGGNS
FT                                LMYYYNGKA (in isoform A-).
FT                                {ECO:0000303|PubMed:21789225}.
FT                                /FTId=VSP_044336.
FT   VAR_SEQ       1     23       MHHQQRMAALGTDKELSDLLDFS -> MKFKQCRCSDTGLC
FT                                CLDHEGKAE (in isoform H-).
FT                                {ECO:0000303|PubMed:21789225}.
FT                                /FTId=VSP_044335.
FT   VAR_SEQ      24    183       Missing (in isoform H-).
FT                                {ECO:0000303|PubMed:21789225}.
FT                                /FTId=VSP_057364.
FT   VAR_SEQ      24    123       Missing (in isoform A-).
FT                                {ECO:0000303|PubMed:21789225}.
FT                                /FTId=VSP_044337.
FT   VAR_SEQ      33    102       Missing (in isoform G-).
FT                                {ECO:0000303|PubMed:21789225}.
FT                                /FTId=VSP_044338.
FT   VAR_SEQ     123    123       Missing (in isoform G- and isoform 11).
FT                                {ECO:0000303|PubMed:14702039,
FT                                ECO:0000303|PubMed:21789225}.
FT                                /FTId=VSP_044339.
FT   VAR_SEQ     124    183       Missing (in isoform A-, isoform B-delta,
FT                                isoform B+delta and isoform C-delta).
FT                                {ECO:0000303|PubMed:21789225}.
FT                                /FTId=VSP_044340.
FT   VAR_SEQ     161    183       LHSSAMEVQTKKVRKVPPGLPSS -> MYCAYTIPGMGGNS
FT                                LMYYYNGKA (in isoform SEF2-1A).
FT                                {ECO:0000303|PubMed:14702039,
FT                                ECO:0000303|PubMed:1681116,
FT                                ECO:0000303|PubMed:21789225,
FT                                ECO:0000303|Ref.7}.
FT                                /FTId=VSP_002111.
FT   VAR_SEQ     357    357       Missing (in isoform E-).
FT                                {ECO:0000303|PubMed:21789225}.
FT                                /FTId=VSP_047083.
FT   VAR_SEQ     545    545       T -> TRSRS (in isoform B+delta, isoform
FT                                SEF2-1A, isoform SEF2-1D, isoform 11 and
FT                                isoform 13).
FT                                {ECO:0000303|PubMed:14702039,
FT                                ECO:0000303|PubMed:15489334,
FT                                ECO:0000303|PubMed:1681116,
FT                                ECO:0000303|PubMed:21789225,
FT                                ECO:0000303|Ref.7}.
FT                                /FTId=VSP_002112.
FT   VARIANT     358    358       G -> V (in PTHS; also expressed in the
FT                                nucleus with a pattern indistinguishable
FT                                from the wild-type; does not have a major
FT                                impact on homodimer formation; affects
FT                                transcriptional activity in a context-
FT                                dependent manner).
FT                                {ECO:0000269|PubMed:18728071,
FT                                ECO:0000269|PubMed:22777675}.
FT                                /FTId=VAR_066839.
FT   VARIANT     450    450       M -> I (in dbSNP:rs11660217).
FT                                /FTId=VAR_049545.
FT   VARIANT     535    535       D -> G (in PTHS; loss of function; also
FT                                expressed in the nucleus with a pattern
FT                                indistinguishable from the wild-type;
FT                                does not have a major impact on homodimer
FT                                formation; affects transcriptional
FT                                activity in a context-dependent manner).
FT                                {ECO:0000269|PubMed:19235238,
FT                                ECO:0000269|PubMed:22777675}.
FT                                /FTId=VAR_058632.
FT   VARIANT     565    565       R -> W (in PTHS).
FT                                {ECO:0000269|PubMed:22045651}.
FT                                /FTId=VAR_066970.
FT   VARIANT     572    572       R -> G (in PTHS; loss of function).
FT                                {ECO:0000269|PubMed:19235238,
FT                                ECO:0000269|PubMed:22045651}.
FT                                /FTId=VAR_058633.
FT   VARIANT     572    572       R -> Q (in PTHS).
FT                                {ECO:0000269|PubMed:22045651}.
FT                                /FTId=VAR_066971.
FT   VARIANT     574    574       R -> H (in PTHS).
FT                                {ECO:0000269|PubMed:22045651}.
FT                                /FTId=VAR_066972.
FT   VARIANT     574    574       R -> P (in PTHS; mislocalized to small
FT                                spherical punctae that are dispersed
FT                                throughout the nucleus; can attenuate
FT                                homo- and heterodimer formation; affects
FT                                transcriptional activity in a context-
FT                                dependent manner).
FT                                {ECO:0000269|PubMed:18728071,
FT                                ECO:0000269|PubMed:22045651,
FT                                ECO:0000269|PubMed:22777675}.
FT                                /FTId=VAR_066840.
FT   VARIANT     576    576       R -> Q (in PTHS; loss of function).
FT                                {ECO:0000269|PubMed:17436254,
FT                                ECO:0000269|PubMed:19235238,
FT                                ECO:0000269|PubMed:22045651}.
FT                                /FTId=VAR_034704.
FT   VARIANT     576    576       R -> W (in PTHS; mislocalized to small
FT                                spherical punctae that are dispersed
FT                                throughout the nucleus; can attenuate
FT                                homo- and heterodimer formation; affects
FT                                transcriptional activity in a context-
FT                                dependent manner).
FT                                {ECO:0000269|PubMed:17436254,
FT                                ECO:0000269|PubMed:17436255,
FT                                ECO:0000269|PubMed:22045651,
FT                                ECO:0000269|PubMed:22777675}.
FT                                /FTId=VAR_034705.
FT   VARIANT     578    578       R -> H (in PTHS).
FT                                {ECO:0000269|PubMed:18728071}.
FT                                /FTId=VAR_066841.
FT   VARIANT     578    578       R -> P (in PTHS).
FT                                {ECO:0000269|PubMed:20184619,
FT                                ECO:0000269|PubMed:22045651}.
FT                                /FTId=VAR_066973.
FT   VARIANT     583    583       A -> P (in PTHS).
FT                                {ECO:0000269|PubMed:22045651}.
FT                                /FTId=VAR_066974.
FT   VARIANT     610    610       A -> V (in PTHS; loss of function;
FT                                mislocalized to small spherical punctae
FT                                that are dispersed throughout the
FT                                nucleus; can attenuate homo- and
FT                                heterodimer formation; affects
FT                                transcriptional activity in a context-
FT                                dependent manner).
FT                                {ECO:0000269|PubMed:19235238,
FT                                ECO:0000269|PubMed:22045651,
FT                                ECO:0000269|PubMed:22777675}.
FT                                /FTId=VAR_058634.
FT   CONFLICT     46     49       TGSN -> EFGG (in Ref. 9; CAA36298).
FT                                {ECO:0000305}.
FT   CONFLICT    205    205       Missing (in Ref. 7; AV761952).
FT                                {ECO:0000305}.
FT   CONFLICT    334    334       P -> S (in Ref. 9; CAA36298).
FT                                {ECO:0000305}.
FT   HELIX        15     25       {ECO:0000244|PDB:2KWF}.
SQ   SEQUENCE   667 AA;  71308 MW;  53459FC7989D9487 CRC64;
     MHHQQRMAAL GTDKELSDLL DFSAMFSPPV SSGKNGPTSL ASGHFTGSNV EDRSSSGSWG
     NGGHPSPSRN YGDGTPYDHM TSRDLGSHDN LSPPFVNSRI QSKTERGSYS SYGRESNLQG
     CHQQSLLGGD MDMGNPGTLS PTKPGSQYYQ YSSNNPRRRP LHSSAMEVQT KKVRKVPPGL
     PSSVYAPSAS TADYNRDSPG YPSSKPATST FPSSFFMQDG HHSSDPWSSS SGMNQPGYAG
     MLGNSSHIPQ SSSYCSLHPH ERLSYPSHSS ADINSSLPPM STFHRSGTNH YSTSSCTPPA
     NGTDSIMANR GSGAAGSSQT GDALGKALAS IYSPDHTNNS FSSNPSTPVG SPPSLSAGTA
     VWSRNGGQAS SSPNYEGPLH SLQSRIEDRL ERLDDAIHVL RNHAVGPSTA MPGGHGDMHG
     IIGPSHNGAM GGLGSGYGTG LLSANRHSLM VGTHREDGVA LRGSHSLLPN QVPVPQLPVQ
     SATSPDLNPP QDPYRGMPPG LQGQSVSSGS SEIKSDDEGD ENLQDTKSSE DKKLDDDKKD
     IKSITSNNDD EDLTPEQKAE REKERRMANN ARERLRVRDI NEAFKELGRM VQLHLKSDKP
     QTKLLILHQA VAVILSLEQQ VRERNLNPKA ACLKRREEEK VSSEPPPLSL AGPHPGMGDA
     SNHMGQM
//
ID   KAT2B_HUMAN             Reviewed;         832 AA.
AC   Q92831; Q6NSK1;
DT   19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2005, sequence version 3.
DT   11-NOV-2015, entry version 171.
DE   RecName: Full=Histone acetyltransferase KAT2B;
DE            EC=2.3.1.48;
DE   AltName: Full=Histone acetyltransferase PCAF;
DE            Short=Histone acetylase PCAF;
DE   AltName: Full=Lysine acetyltransferase 2B;
DE   AltName: Full=P300/CBP-associated factor;
DE            Short=P/CAF;
GN   Name=KAT2B; Synonyms=PCAF;
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 {ECO:0000312|EMBL:AAC50890.2};
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBUNIT, TISSUE SPECIFICITY, AND
RP   INTERACTION WITH EP300 AND CREBBP.
RC   TISSUE=Liver;
RX   PubMed=8684459; DOI=10.1038/382319a0;
RA   Yang X.-J., Ogryzko V.V., Nishikawa J., Howard B.H., Nakatani Y.;
RT   "A p300/CBP-associated factor that competes with the adenoviral
RT   oncoprotein E1A.";
RL   Nature 382:319-324(1996).
RN   [2] {ECO:0000305}
RP   SEQUENCE REVISION.
RC   TISSUE=Liver;
RA   Nakatani Y.;
RL   Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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   ENZYME ACTIVITY.
RX   PubMed=8945521; DOI=10.1016/S0092-8674(00)82001-2;
RA   Ogryzko V.V., Schiltz R.L., Russanova V., Howard B.H., Nakatani Y.;
RT   "The transcriptional coactivators p300 and CBP are histone
RT   acetyltransferases.";
RL   Cell 87:953-959(1996).
RN   [5]
RP   INTERACTION WITH NCOA3.
RX   PubMed=9346901; DOI=10.1074/jbc.272.44.27629;
RA   Takeshita A., Cardona G.R., Koibuchi N., Suen C.-S., Chin W.W.;
RT   "TRAM-1, a novel 160-kDa thyroid hormone receptor activator molecule,
RT   exhibits distinct properties from steroid receptor coactivator-1.";
RL   J. Biol. Chem. 272:27629-27634(1997).
RN   [6]
RP   INTERACTION WITH NCOA1.
RX   PubMed=9296499; DOI=10.1038/38304;
RA   Spencer T.E., Jenster G., Burcin M.M., Allis C.D., Zhou J.,
RA   Mizzen C.A., McKenna N.J., Onate S.A., Tsai S.Y., Tsai M.-J.,
RA   O'Malley B.W.;
RT   "Steroid receptor coactivator-1 is a histone acetyltransferase.";
RL   Nature 389:194-198(1997).
RN   [7]
RP   INTERACTION WITH KLF1, AND FUNCTION.
RX   PubMed=9707565; DOI=10.1073/pnas.95.17.9855;
RA   Zhang W., Bieker J.J.;
RT   "Acetylation and modulation of erythroid Krueppel-like factor (EKLF)
RT   activity by interaction with histone acetyltransferases.";
RL   Proc. Natl. Acad. Sci. U.S.A. 95:9855-9860(1998).
RN   [8]
RP   INTERACTION WITH E2F1, AND FUNCTION.
RX   PubMed=10675335; DOI=10.1093/emboj/19.4.662;
RA   Martinez-Balbas M.A., Bauer U.M., Nielsen S.J., Brehm A.,
RA   Kouzarides T.;
RT   "Regulation of E2F1 activity by acetylation.";
RL   EMBO J. 19:662-671(2000).
RN   [9]
RP   INTERACTION WITH HTLV-1 TAX.
RX   PubMed=10766811; DOI=10.1074/jbc.275.16.11852;
RA   Harrod R., Kuo Y.-L., Tang Y., Yao Y., Vassilev A., Nakatani Y.,
RA   Giam C.-Z.;
RT   "p300 and p300/cAMP-responsive element-binding protein associated
RT   factor interact with human T-cell lymphotropic virus type-1 Tax in a
RT   multi-histone acetyltransferase/activator-enhancer complex.";
RL   J. Biol. Chem. 275:11852-11857(2000).
RN   [10]
RP   INTERACTION WITH MECOM.
RX   PubMed=11568182; DOI=10.1074/jbc.M106733200;
RA   Chakraborty S., Senyuk V., Sitailo S., Chi Y., Nucifora G.;
RT   "Interaction of EVI1 with cAMP-responsive element-binding protein-
RT   binding protein (CBP) and p300/CBP-associated factor (P/CAF) results
RT   in reversible acetylation of EVI1 and in co-localization in nuclear
RT   speckles.";
RL   J. Biol. Chem. 276:44936-44943(2001).
RN   [11]
RP   INTERACTION WITH HIV-1 TAT.
RX   PubMed=12486002; DOI=10.1093/emboj/cdf669;
RA   Bres V., Tagami H., Peloponese J.-M., Loret E., Jeang K.-T.,
RA   Nakatani Y., Emiliani S., Benkirane M., Kiernan R.E.;
RT   "Differential acetylation of Tat coordinates its interaction with the
RT   co-activators cyclin T1 and PCAF.";
RL   EMBO J. 21:6811-6819(2002).
RN   [12]
RP   FUNCTION, AND INTERACTION WITH NPAS2; ARNTL/BMAL1 AND CLOCK.
RX   PubMed=14645221; DOI=10.1074/jbc.M311973200;
RA   Curtis A.M., Seo S.B., Westgate E.J., Rudic R.D., Smyth E.M.,
RA   Chakravarti D., FitzGerald G.A., McNamara P.;
RT   "Histone acetyltransferase-dependent chromatin remodeling and the
RT   vascular clock.";
RL   J. Biol. Chem. 279:7091-7097(2004).
RN   [13]
RP   INTERACTION WITH NFE4.
RX   PubMed=15273251; DOI=10.1074/jbc.M405129200;
RA   Zhao Q., Cumming H., Cerruti L., Cunningham J.M., Jane S.M.;
RT   "Site-specific acetylation of the fetal globin activator NF-E4
RT   prevents its ubiquitination and regulates its interaction with the
RT   histone deacetylase, HDAC1.";
RL   J. Biol. Chem. 279:41477-41486(2004).
RN   [14]
RP   INTERACTION WITH TACC1; TACC2 AND TACC3.
RX   PubMed=14767476; DOI=10.1038/sj.onc.1207424;
RA   Gangisetty O., Lauffart B., Sondarva G.V., Chelsea D.M., Still I.H.;
RT   "The transforming acidic coiled coil proteins interact with nuclear
RT   histone acetyltransferases.";
RL   Oncogene 23:2559-2563(2004).
RN   [15]
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   [16]
RP   INTERACTION WITH DDX17.
RX   PubMed=17226766; DOI=10.1002/jcb.21250;
RA   Shin S., Janknecht R.;
RT   "Concerted activation of the Mdm2 promoter by p72 RNA helicase and the
RT   coactivators p300 and P/CAF.";
RL   J. Cell. Biochem. 101:1252-1265(2007).
RN   [17]
RP   INTERACTION WITH CEBPB.
RX   PubMed=17301242; DOI=10.1073/pnas.0607378104;
RA   Wiper-Bergeron N., Salem H.A., Tomlinson J.J., Wu D., Hache R.J.;
RT   "Glucocorticoid-stimulated preadipocyte differentiation is mediated
RT   through acetylation of C/EBPbeta by GCN5.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:2703-2708(2007).
RN   [18]
RP   IDENTIFICATION IN A LARGE CHROMATIN REMODELING COMPLEX.
RX   PubMed=17707232; DOI=10.1016/j.molcel.2007.07.024;
RA   Zhu P., Zhou W., Wang J., Puc J., Ohgi K.A., Erdjument-Bromage H.,
RA   Tempst P., Glass C.K., Rosenfeld M.G.;
RT   "A histone H2A deubiquitinase complex coordinating histone acetylation
RT   and H1 dissociation in transcriptional regulation.";
RL   Mol. Cell 27:609-621(2007).
RN   [19]
RP   INTERACTION WITH BCAS3.
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   [20]
RP   FUNCTION.
RX   PubMed=23932781; DOI=10.1016/j.molcel.2013.07.002;
RA   Lin R., Tao R., Gao X., Li T., Zhou X., Guan K.L., Xiong Y., Lei Q.Y.;
RT   "Acetylation stabilizes ATP-citrate lyase to promote lipid
RT   biosynthesis and tumor growth.";
RL   Mol. Cell 51:506-518(2013).
RN   [21]
RP   X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 493-658 IN COMPLEX WITH
RP   COENZYME A, AND ACTIVE SITE.
RX   PubMed=10393169; DOI=10.1093/emboj/18.13.3521;
RA   Clements A., Rojas J.R., Trievel R.C., Wang L., Berger S.L.,
RA   Marmorstein R.;
RT   "Crystal structure of the histone acetyltransferase domain of the
RT   human PCAF transcriptional regulator bound to coenzyme A.";
RL   EMBO J. 18:3521-3532(1999).
RN   [22]
RP   STRUCTURE BY NMR OF 715-832, AND MUTAGENESIS OF VAL-752; TYR-760;
RP   TYR-802 AND TYR-809.
RC   TISSUE=Liver;
RX   PubMed=10365964; DOI=10.1038/20974;
RA   Dhalluin C., Carlson J.E., Zeng L., He C., Aggarwal A.K., Zhou M.-M.;
RT   "Structure and ligand of a histone acetyltransferase bromodomain.";
RL   Nature 399:491-496(1999).
RN   [23]
RP   STRUCTURE BY NMR OF 719-832 IN COMPLEX WITH HIV-1 TAT.
RX   PubMed=11931765; DOI=10.1016/S1097-2765(02)00483-5;
RA   Mujtaba S., He Y., Zeng L., Farooq A., Carlson J.E., Ott M.,
RA   Verdin E., Zhou M.-M.;
RT   "Structural basis of lysine-acetylated HIV-1 Tat recognition by PCAF
RT   bromodomain.";
RL   Mol. Cell 9:575-586(2002).
RN   [24]
RP   X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 715-831.
RX   PubMed=22464331; DOI=10.1016/j.cell.2012.02.013;
RA   Filippakopoulos P., Picaud S., Mangos M., Keates T., Lambert J.P.,
RA   Barsyte-Lovejoy D., Felletar I., Volkmer R., Muller S., Pawson T.,
RA   Gingras A.C., Arrowsmith C.H., Knapp S.;
RT   "Histone recognition and large-scale structural analysis of the human
RT   bromodomain family.";
RL   Cell 149:214-231(2012).
CC   -!- FUNCTION: Functions as a histone acetyltransferase (HAT) to
CC       promote transcriptional activation. Has significant histone
CC       acetyltransferase activity with core histones (H3 and H4), and
CC       also with nucleosome core particles. Also acetylates non-histone
CC       proteins, such as ACLY. Inhibits cell-cycle progression and
CC       counteracts the mitogenic activity of the adenoviral oncoprotein
CC       E1A. In case of HIV-1 infection, it is recruited by the viral
CC       protein Tat. Regulates Tat's transactivating activity and may help
CC       inducing chromatin remodeling of proviral genes. Acts as a
CC       circadian transcriptional coactivator which enhances the activity
CC       of the circadian transcriptional activators: NPAS2-ARNTL/BMAL1 and
CC       CLOCK-ARNTL/BMAL1 heterodimers. {ECO:0000269|PubMed:10675335,
CC       ECO:0000269|PubMed:14645221, ECO:0000269|PubMed:23932781,
CC       ECO:0000269|PubMed:8684459, ECO:0000269|PubMed:9707565}.
CC   -!- CATALYTIC ACTIVITY: Acetyl-CoA + [histone] = CoA + acetyl-
CC       [histone]. {ECO:0000269|PubMed:8945521}.
CC   -!- SUBUNIT: Interacts with SIRT1. Interacts (unsumoylated form) with
CC       NR2C1; the interaction promotes transactivation activity (By
CC       similarity). Interacts with EP300, CREBBP and DDX17. Interacts
CC       with NCOA1 and NCOA3. Component of a large chromatin remodeling
CC       complex, at least composed of MYSM1, KAT2B/PCAF, RBM10 and
CC       KIF11/TRIP5. Interacts with NR2C2 (hypophosphorylated and
CC       unsumoylated form); the interaction promotes the transactivation
CC       activity of NR2C2. Binds to HTLV-1 Tax. Interacts with and
CC       acetylates HIV-1 Tat. Interacts with KLF1; the interaction does
CC       not acetylate KLF1 and there is no enhancement of its
CC       transactivational activity. Interacts with NFE4. Interacts with
CC       MECOM. Interacts with E2F1; the interaction acetylates E2F1
CC       augmenting its DNA-binding and transcriptional activity. Interacts
CC       with NPAS2, ARNTL/BMAL1 and CLOCK. Interacts with BCAS3. Interacts
CC       with CEBPB (PubMed:17301242). Interacts with NR4A3 (By
CC       similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q9JHD1,
CC       ECO:0000269|PubMed:10675335, ECO:0000269|PubMed:10766811,
CC       ECO:0000269|PubMed:11568182, ECO:0000269|PubMed:11931765,
CC       ECO:0000269|PubMed:12486002, ECO:0000269|PubMed:14645221,
CC       ECO:0000269|PubMed:14767476, ECO:0000269|PubMed:15273251,
CC       ECO:0000269|PubMed:16887930, ECO:0000269|PubMed:17226766,
CC       ECO:0000269|PubMed:17301242, ECO:0000269|PubMed:17505058,
CC       ECO:0000269|PubMed:17707232, ECO:0000269|PubMed:8684459,
CC       ECO:0000269|PubMed:9296499, ECO:0000269|PubMed:9346901,
CC       ECO:0000269|PubMed:9707565}.
CC   -!- INTERACTION:
CC       P03255:- (xeno); NbExp=3; IntAct=EBI-477430, EBI-2603114;
CC       P03255-2:- (xeno); NbExp=3; IntAct=EBI-477430, EBI-6859460;
CC       O60566:BUB1B; NbExp=14; IntAct=EBI-477430, EBI-1001438;
CC       Q92793:CREBBP; NbExp=4; IntAct=EBI-477430, EBI-81215;
CC       P03129:E7 (xeno); NbExp=3; IntAct=EBI-477430, EBI-866453;
CC       Q96KQ7:EHMT2; NbExp=3; IntAct=EBI-477430, EBI-744366;
CC       Q09472:EP300; NbExp=2; IntAct=EBI-477430, EBI-447295;
CC       Q16665:HIF1A; NbExp=2; IntAct=EBI-477430, EBI-447269;
CC       P02299:His3:CG33854 (xeno); NbExp=2; IntAct=EBI-477430, EBI-522090;
CC       P84040:His4:CG33909 (xeno); NbExp=2; IntAct=EBI-477430, EBI-185028;
CC       Q96EB6:SIRT1; NbExp=3; IntAct=EBI-477430, EBI-1802965;
CC       Q8IXJ6:SIRT2; NbExp=4; IntAct=EBI-477430, EBI-477232;
CC       Q16594:TAF9; NbExp=3; IntAct=EBI-477430, EBI-712521;
CC       O88898-2:Tp63 (xeno); NbExp=3; IntAct=EBI-477430, EBI-2338228;
CC       Q15672:TWIST1; NbExp=2; IntAct=EBI-477430, EBI-1797287;
CC       P22415:USF1; NbExp=5; IntAct=EBI-477430, EBI-1054489;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Ubiquitously expressed but most abundant in
CC       heart and skeletal muscle. {ECO:0000269|PubMed:8684459}.
CC   -!- DOMAIN: The bromodomain mediates binding to HIV-1 Tat.
CC   -!- SIMILARITY: Belongs to the acetyltransferase family. GCN5
CC       subfamily. {ECO:0000305}.
CC   -!- SIMILARITY: Contains 1 bromo domain. {ECO:0000255|PROSITE-
CC       ProRule:PRU00035}.
CC   -!- SIMILARITY: Contains 1 N-acetyltransferase domain.
CC       {ECO:0000255|PROSITE-ProRule:PRU00532}.
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DR   EMBL; U57317; AAC50890.2; -; mRNA.
DR   EMBL; BC060823; AAH60823.1; -; mRNA.
DR   EMBL; BC070075; AAH70075.1; -; mRNA.
DR   CCDS; CCDS2634.1; -.
DR   PIR; S71788; S71788.
DR   RefSeq; NP_003875.3; NM_003884.4.
DR   UniGene; Hs.533055; -.
DR   PDB; 1CM0; X-ray; 2.30 A; A/B=493-658.
DR   PDB; 1JM4; NMR; -; B=719-832.
DR   PDB; 1N72; NMR; -; A=719-832.
DR   PDB; 1WUG; NMR; -; A=719-832.
DR   PDB; 1WUM; NMR; -; A=719-832.
DR   PDB; 1ZS5; NMR; -; A=719-832.
DR   PDB; 2RNW; NMR; -; A=719-832.
DR   PDB; 2RNX; NMR; -; A=719-832.
DR   PDB; 3GG3; X-ray; 2.25 A; A/B=715-831.
DR   PDB; 4NSQ; X-ray; 2.31 A; A/B/C/D=493-658.
DR   PDBsum; 1CM0; -.
DR   PDBsum; 1JM4; -.
DR   PDBsum; 1N72; -.
DR   PDBsum; 1WUG; -.
DR   PDBsum; 1WUM; -.
DR   PDBsum; 1ZS5; -.
DR   PDBsum; 2RNW; -.
DR   PDBsum; 2RNX; -.
DR   PDBsum; 3GG3; -.
DR   PDBsum; 4NSQ; -.
DR   ProteinModelPortal; Q92831; -.
DR   SMR; Q92831; 493-653, 719-832.
DR   BioGrid; 114375; 175.
DR   DIP; DIP-29778N; -.
DR   IntAct; Q92831; 36.
DR   MINT; MINT-150079; -.
DR   STRING; 9606.ENSP00000263754; -.
DR   BindingDB; Q92831; -.
DR   ChEMBL; CHEMBL5500; -.
DR   GuidetoPHARMACOLOGY; 2737; -.
DR   PhosphoSite; Q92831; -.
DR   BioMuta; KAT2B; -.
DR   DMDM; 83287776; -.
DR   REPRODUCTION-2DPAGE; Q92831; -.
DR   MaxQB; Q92831; -.
DR   PaxDb; Q92831; -.
DR   PRIDE; Q92831; -.
DR   Ensembl; ENST00000263754; ENSP00000263754; ENSG00000114166.
DR   GeneID; 8850; -.
DR   KEGG; hsa:8850; -.
DR   UCSC; uc003cbq.3; human.
DR   CTD; 8850; -.
DR   GeneCards; KAT2B; -.
DR   HGNC; HGNC:8638; KAT2B.
DR   HPA; CAB004526; -.
DR   HPA; HPA055839; -.
DR   MIM; 602303; gene.
DR   neXtProt; NX_Q92831; -.
DR   PharmGKB; PA162392705; -.
DR   eggNOG; KOG1472; Eukaryota.
DR   eggNOG; COG5076; LUCA.
DR   GeneTree; ENSGT00760000119099; -.
DR   HOGENOM; HOG000007151; -.
DR   InParanoid; Q92831; -.
DR   KO; K06062; -.
DR   OMA; HEDASNY; -.
DR   OrthoDB; EOG7ZKS9B; -.
DR   PhylomeDB; Q92831; -.
DR   TreeFam; TF105399; -.
DR   BRENDA; 2.3.1.48; 2681.
DR   Reactome; R-HSA-1912408; Pre-NOTCH Transcription and Translation.
DR   Reactome; R-HSA-2032785; YAP1- and WWTR1 (TAZ)-stimulated gene expression.
DR   Reactome; R-HSA-2122947; NOTCH1 Intracellular Domain Regulates Transcription.
DR   Reactome; R-HSA-2644606; Constitutive Signaling by NOTCH1 PEST Domain Mutants.
DR   Reactome; R-HSA-2894862; Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
DR   Reactome; R-HSA-3214847; HATs acetylate histones.
DR   Reactome; R-HSA-350054; Notch-HLH transcription pathway.
DR   Reactome; R-HSA-73762; RNA Polymerase I Transcription Initiation.
DR   ChiTaRS; KAT2B; human.
DR   EvolutionaryTrace; Q92831; -.
DR   GeneWiki; PCAF; -.
DR   GenomeRNAi; 8850; -.
DR   NextBio; 33221; -.
DR   PRO; PR:Q92831; -.
DR   Proteomes; UP000005640; Chromosome 3.
DR   Bgee; Q92831; -.
DR   CleanEx; HS_KAT2B; -.
DR   Genevisible; Q92831; HS.
DR   GO; GO:0031672; C:A band; IEA:Ensembl.
DR   GO; GO:0042641; C:actomyosin; IEA:Ensembl.
DR   GO; GO:0005671; C:Ada2/Gcn5/Ada3 transcription activator complex; IDA:BHF-UCL.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0031674; C:I band; IEA:Ensembl.
DR   GO; GO:0000776; C:kinetochore; IEA:Ensembl.
DR   GO; GO:0000790; C:nuclear chromatin; IEA:Ensembl.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0000125; C:PCAF complex; NAS:UniProtKB.
DR   GO; GO:0016407; F:acetyltransferase activity; IDA:UniProtKB.
DR   GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
DR   GO; GO:0004861; F:cyclin-dependent protein serine/threonine kinase inhibitor activity; ISS:UniProtKB.
DR   GO; GO:0004402; F:histone acetyltransferase activity; IDA:UniProtKB.
DR   GO; GO:0042826; F:histone deacetylase binding; IPI:UniProtKB.
DR   GO; GO:0004468; F:lysine N-acetyltransferase activity, acting on acetyl phosphate as donor; IDA:UniProtKB.
DR   GO; GO:0032403; F:protein complex binding; IDA:UniProtKB.
DR   GO; GO:0019901; F:protein kinase binding; ISS:UniProtKB.
DR   GO; GO:0000977; F:RNA polymerase II regulatory region sequence-specific DNA binding; IEA:Ensembl.
DR   GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB.
DR   GO; GO:0003712; F:transcription cofactor activity; IPI:UniProtKB.
DR   GO; GO:0008134; F:transcription factor binding; IPI:UniProtKB.
DR   GO; GO:0007050; P:cell cycle arrest; TAS:ProtInc.
DR   GO; GO:0032869; P:cellular response to insulin stimulus; IDA:BHF-UCL.
DR   GO; GO:0034599; P:cellular response to oxidative stress; IEA:Ensembl.
DR   GO; GO:0071374; P:cellular response to parathyroid hormone stimulus; IEA:Ensembl.
DR   GO; GO:0006325; P:chromatin organization; TAS:Reactome.
DR   GO; GO:0006338; P:chromatin remodeling; IDA:UniProtKB.
DR   GO; GO:0010467; P:gene expression; TAS:Reactome.
DR   GO; GO:0043966; P:histone H3 acetylation; IDA:BHF-UCL.
DR   GO; GO:0043970; P:histone H3-K9 acetylation; IEA:Ensembl.
DR   GO; GO:0018393; P:internal peptidyl-lysine acetylation; IDA:UniProtKB.
DR   GO; GO:0007613; P:memory; IEA:Ensembl.
DR   GO; GO:0018076; P:N-terminal peptidyl-lysine acetylation; IDA:UniProtKB.
DR   GO; GO:0008285; P:negative regulation of cell proliferation; IDA:UniProtKB.
DR   GO; GO:0045736; P:negative regulation of cyclin-dependent protein serine/threonine kinase activity; IEA:Ensembl.
DR   GO; GO:0007219; P:Notch signaling pathway; TAS:Reactome.
DR   GO; GO:0018394; P:peptidyl-lysine acetylation; IDA:BHF-UCL.
DR   GO; GO:0035563; P:positive regulation of chromatin binding; IEA:Ensembl.
DR   GO; GO:0035948; P:positive regulation of gluconeogenesis by positive regulation of transcription from RNA polymerase II promoter; IEA:Ensembl.
DR   GO; GO:0071442; P:positive regulation of histone H3-K14 acetylation; IEA:Ensembl.
DR   GO; GO:2000617; P:positive regulation of histone H3-K9 acetylation; IEA:Ensembl.
DR   GO; GO:0010976; P:positive regulation of neuron projection development; IEA:Ensembl.
DR   GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:BHF-UCL.
DR   GO; GO:0045909; P:positive regulation of vasodilation; IEA:Ensembl.
DR   GO; GO:0006473; P:protein acetylation; TAS:ProtInc.
DR   GO; GO:0010835; P:regulation of protein ADP-ribosylation; IDA:BHF-UCL.
DR   GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
DR   GO; GO:0006360; P:transcription from RNA polymerase I promoter; TAS:Reactome.
DR   GO; GO:0006361; P:transcription initiation from RNA polymerase I promoter; TAS:Reactome.
DR   GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; TAS:Reactome.
DR   GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
DR   Gene3D; 1.20.920.10; -; 1.
DR   Gene3D; 3.40.630.30; -; 1.
DR   InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR   InterPro; IPR001487; Bromodomain.
DR   InterPro; IPR018359; Bromodomain_CS.
DR   InterPro; IPR000182; GNAT_dom.
DR   InterPro; IPR016376; Hist_acetylase_PCAF.
DR   InterPro; IPR009464; PCAF_N.
DR   Pfam; PF13508; Acetyltransf_7; 1.
DR   Pfam; PF00439; Bromodomain; 1.
DR   Pfam; PF06466; PCAF_N; 1.
DR   PIRSF; PIRSF003048; Histone_acetylase_PCAF; 1.
DR   PRINTS; PR00503; BROMODOMAIN.
DR   SMART; SM00297; BROMO; 1.
DR   SUPFAM; SSF47370; SSF47370; 1.
DR   SUPFAM; SSF55729; SSF55729; 1.
DR   PROSITE; PS00633; BROMODOMAIN_1; 1.
DR   PROSITE; PS50014; BROMODOMAIN_2; 1.
DR   PROSITE; PS51186; GNAT; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Activator; Acyltransferase; Biological rhythms;
KW   Bromodomain; Cell cycle; Complete proteome; Host-virus interaction;
KW   Nucleus; Polymorphism; Reference proteome; Transcription;
KW   Transcription regulation; Transferase.
FT   CHAIN         1    832       Histone acetyltransferase KAT2B.
FT                                /FTId=PRO_0000211208.
FT   DOMAIN      503    651       N-acetyltransferase.
FT                                {ECO:0000250|UniProtKB:Q92830,
FT                                ECO:0000255|PROSITE-ProRule:PRU00532}.
FT   DOMAIN      740    810       Bromo. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00035, ECO:0000305}.
FT   REGION      574    576       Acetyl-CoA binding.
FT                                {ECO:0000269|PubMed:10393169}.
FT   REGION      581    587       Acetyl-CoA binding.
FT                                {ECO:0000269|PubMed:10393169}.
FT   REGION      612    615       Acetyl-CoA binding.
FT                                {ECO:0000269|PubMed:10393169}.
FT   ACT_SITE    570    570       Proton donor/acceptor.
FT                                {ECO:0000303|PubMed:10393169}.
FT   VARIANT     386    386       N -> S (in dbSNP:rs17006625).
FT                                /FTId=VAR_034372.
FT   MUTAGEN     752    752       V->A: Reduced acetyl-lysine binding.
FT                                {ECO:0000269|PubMed:10365964}.
FT   MUTAGEN     760    760       Y->A: Reduced acetyl-lysine binding.
FT                                {ECO:0000269|PubMed:10365964}.
FT   MUTAGEN     802    802       Y->A: Reduced acetyl-lysine binding.
FT                                {ECO:0000269|PubMed:10365964}.
FT   MUTAGEN     809    809       Y->A: Complete loss of acetyl-lysine
FT                                binding. {ECO:0000269|PubMed:10365964}.
FT   CONFLICT    804    805       PP -> AA (in Ref. 1; AAC50890).
FT                                {ECO:0000305}.
FT   STRAND      494    499       {ECO:0000244|PDB:1CM0}.
FT   STRAND      503    505       {ECO:0000244|PDB:1CM0}.
FT   HELIX       509    525       {ECO:0000244|PDB:1CM0}.
FT   HELIX       531    538       {ECO:0000244|PDB:1CM0}.
FT   STRAND      543    550       {ECO:0000244|PDB:1CM0}.
FT   STRAND      553    563       {ECO:0000244|PDB:1CM0}.
FT   TURN        564    567       {ECO:0000244|PDB:1CM0}.
FT   STRAND      568    576       {ECO:0000244|PDB:1CM0}.
FT   HELIX       578    580       {ECO:0000244|PDB:1CM0}.
FT   STRAND      582    584       {ECO:0000244|PDB:1CM0}.
FT   HELIX       585    599       {ECO:0000244|PDB:1CM0}.
FT   STRAND      604    609       {ECO:0000244|PDB:1CM0}.
FT   TURN        611    613       {ECO:0000244|PDB:1CM0}.
FT   HELIX       614    618       {ECO:0000244|PDB:1CM0}.
FT   TURN        619    621       {ECO:0000244|PDB:1CM0}.
FT   STRAND      623    625       {ECO:0000244|PDB:1CM0}.
FT   HELIX       630    633       {ECO:0000244|PDB:1CM0}.
FT   STRAND      644    649       {ECO:0000244|PDB:1CM0}.
FT   HELIX       727    741       {ECO:0000244|PDB:3GG3}.
FT   STRAND      742    744       {ECO:0000244|PDB:1WUM}.
FT   HELIX       746    748       {ECO:0000244|PDB:3GG3}.
FT   HELIX       754    756       {ECO:0000244|PDB:3GG3}.
FT   STRAND      757    759       {ECO:0000244|PDB:1ZS5}.
FT   HELIX       760    763       {ECO:0000244|PDB:3GG3}.
FT   STRAND      764    766       {ECO:0000244|PDB:1JM4}.
FT   HELIX       770    778       {ECO:0000244|PDB:3GG3}.
FT   HELIX       785    802       {ECO:0000244|PDB:3GG3}.
FT   STRAND      805    807       {ECO:0000244|PDB:1WUG}.
FT   HELIX       808    826       {ECO:0000244|PDB:3GG3}.
FT   STRAND      828    830       {ECO:0000244|PDB:1N72}.
SQ   SEQUENCE   832 AA;  93013 MW;  72F516E8BC00CC0C CRC64;
     MSEAGGAGPG GCGAGAGAGA GPGALPPQPA ALPPAPPQGS PCAAAAGGSG ACGPATAVAA
     AGTAEGPGGG GSARIAVKKA QLRSAPRAKK LEKLGVYSAC KAEESCKCNG WKNPNPSPTP
     PRADLQQIIV SLTESCRSCS HALAAHVSHL ENVSEEEMNR LLGIVLDVEY LFTCVHKEED
     ADTKQVYFYL FKLLRKSILQ RGKPVVEGSL EKKPPFEKPS IEQGVNNFVQ YKFSHLPAKE
     RQTIVELAKM FLNRINYWHL EAPSQRRLRS PNDDISGYKE NYTRWLCYCN VPQFCDSLPR
     YETTQVFGRT LLRSVFTVMR RQLLEQARQE KDKLPLEKRT LILTHFPKFL SMLEEEVYSQ
     NSPIWDQDFL SASSRTSQLG IQTVINPPPV AGTISYNSTS SSLEQPNAGS SSPACKASSG
     LEANPGEKRK MTDSHVLEEA KKPRVMGDIP MELINEVMST ITDPAAMLGP ETNFLSAHSA
     RDEAARLEER RGVIEFHVVG NSLNQKPNKK ILMWLVGLQN VFSHQLPRMP KEYITRLVFD
     PKHKTLALIK DGRVIGGICF RMFPSQGFTE IVFCAVTSNE QVKGYGTHLM NHLKEYHIKH
     DILNFLTYAD EYAIGYFKKQ GFSKEIKIPK TKYVGYIKDY EGATLMGCEL NPRIPYTEFS
     VIIKKQKEII KKLIERKQAQ IRKVYPGLSC FKDGVRQIPI ESIPGIRETG WKPSGKEKSK
     EPRDPDQLYS TLKSILQQVK SHQSAWPFME PVKRTEAPGY YEVIRFPMDL KTMSERLKNR
     YYVSKKLFMA DLQRVFTNCK EYNPPESEYY KCANILEKFF FSKIKEAGLI DK
//
ID   LCORL_HUMAN             Reviewed;         602 AA.
AC   Q8N3X6; Q96NK1;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 4.
DT   11-NOV-2015, entry version 103.
DE   RecName: Full=Ligand-dependent nuclear receptor corepressor-like protein;
DE            Short=LCoR-like protein;
GN   Name=LCORL;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Brain;
RX   PubMed=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=15815621; DOI=10.1038/nature03466;
RA   Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
RA   Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA   Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA   Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA   Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA   Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA   Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA   Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA   Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA   Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA   McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA   Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
RA   Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA   Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA   Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA   Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA   Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA   Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA   Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA   Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA   McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA   Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA   Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
RA   Waterston R.H., Wilson R.K.;
RT   "Generation and annotation of the DNA sequences of human chromosomes 2
RT   and 4.";
RL   Nature 434:724-731(2005).
RN   [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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
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   [5]
RP   IDENTIFICATION.
RX   PubMed=19139490; DOI=10.1074/mcp.M800504-MCP200;
RA   Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F.,
RA   Zheng Z.B., Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y.,
RA   Zhang Y.K., Deng Y.L., Ying W.T., He S.M., Qian X.H.;
RT   "A strategy for precise and large scale identification of core
RT   fucosylated glycoproteins.";
RL   Mol. Cell. Proteomics 8:913-923(2009).
CC   -!- FUNCTION: May act as transcription activator that binds DNA
CC       elements with the sequence 5'-CCCTATCGATCGATCTCTACCT-3'. May play
CC       a role in spermatogenesis (By similarity). {ECO:0000250}.
CC   -!- INTERACTION:
CC       P43360:MAGEA6; NbExp=3; IntAct=EBI-7138654, EBI-1045155;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-
CC       ProRule:PRU00320}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q8N3X6-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8N3X6-2; Sequence=VSP_029287;
CC       Name=3;
CC         IsoId=Q8N3X6-3; Sequence=VSP_029288, VSP_029289;
CC   -!- SIMILARITY: Contains 1 HTH psq-type DNA-binding domain.
CC       {ECO:0000255|PROSITE-ProRule:PRU00320}.
CC   -!- CAUTION: A report observed N-glycosylation at Asn-493
CC       (PubMed:19139490). However, as the protein is predicted to act as
CC       a DNA-binding transcription activator, additional evidences are
CC       required to confirm this result. {ECO:0000305|PubMed:19139490}.
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DR   EMBL; AK055258; BAB70892.1; -; mRNA.
DR   EMBL; AC005768; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC079399; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471069; EAW92786.1; -; Genomic_DNA.
DR   EMBL; BC037322; AAH37322.3; -; mRNA.
DR   CCDS; CCDS3425.1; -. [Q8N3X6-3]
DR   CCDS; CCDS54749.1; -. [Q8N3X6-1]
DR   RefSeq; NP_001159611.1; NM_001166139.1. [Q8N3X6-1]
DR   RefSeq; NP_710153.2; NM_153686.7. [Q8N3X6-3]
DR   UniGene; Hs.446201; -.
DR   UniGene; Hs.677572; -.
DR   ProteinModelPortal; Q8N3X6; -.
DR   SMR; Q8N3X6; 522-579.
DR   BioGrid; 129025; 2.
DR   IntAct; Q8N3X6; 2.
DR   MINT; MINT-8247449; -.
DR   STRING; 9606.ENSP00000371661; -.
DR   PhosphoSite; Q8N3X6; -.
DR   BioMuta; LCORL; -.
DR   DMDM; 160395582; -.
DR   MaxQB; Q8N3X6; -.
DR   PaxDb; Q8N3X6; -.
DR   PRIDE; Q8N3X6; -.
DR   DNASU; 254251; -.
DR   Ensembl; ENST00000326877; ENSP00000317566; ENSG00000178177. [Q8N3X6-3]
DR   Ensembl; ENST00000382226; ENSP00000371661; ENSG00000178177. [Q8N3X6-1]
DR   GeneID; 254251; -.
DR   KEGG; hsa:254251; -.
DR   UCSC; uc003gpq.3; human. [Q8N3X6-3]
DR   UCSC; uc021xmr.1; human. [Q8N3X6-1]
DR   CTD; 254251; -.
DR   GeneCards; LCORL; -.
DR   HGNC; HGNC:30776; LCORL.
DR   HPA; HPA028794; -.
DR   HPA; HPA028795; -.
DR   HPA; HPA060033; -.
DR   MIM; 611799; gene.
DR   neXtProt; NX_Q8N3X6; -.
DR   PharmGKB; PA145148507; -.
DR   eggNOG; KOG4565; Eukaryota.
DR   eggNOG; ENOG4111GCI; LUCA.
DR   GeneTree; ENSGT00520000055615; -.
DR   HOGENOM; HOG000253915; -.
DR   HOVERGEN; HBG108084; -.
DR   InParanoid; Q8N3X6; -.
DR   OMA; YKVKERS; -.
DR   OrthoDB; EOG7VHSXQ; -.
DR   PhylomeDB; Q8N3X6; -.
DR   TreeFam; TF319589; -.
DR   ChiTaRS; LCORL; human.
DR   GenomeRNAi; 254251; -.
DR   NextBio; 92303; -.
DR   PRO; PR:Q8N3X6; -.
DR   Proteomes; UP000005640; Chromosome 4.
DR   Bgee; Q8N3X6; -.
DR   CleanEx; HS_LCORL; -.
DR   ExpressionAtlas; Q8N3X6; baseline and differential.
DR   Genevisible; Q8N3X6; HS.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; IEA:Ensembl.
DR   GO; GO:0006366; P:transcription from RNA polymerase II promoter; IEA:Ensembl.
DR   InterPro; IPR009057; Homeodomain-like.
DR   InterPro; IPR007889; HTH_Psq.
DR   Pfam; PF05225; HTH_psq; 2.
DR   SUPFAM; SSF46689; SSF46689; 2.
DR   PROSITE; PS50960; HTH_PSQ; 1.
PE   1: Evidence at protein level;
KW   Activator; Alternative splicing; Complete proteome; DNA-binding;
KW   Nucleus; Reference proteome; Transcription; Transcription regulation.
FT   CHAIN         1    602       Ligand-dependent nuclear receptor
FT                                corepressor-like protein.
FT                                /FTId=PRO_0000310463.
FT   DOMAIN      516    568       HTH psq-type. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00320}.
FT   DNA_BIND    544    564       H-T-H motif. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00320}.
FT   COMPBIAS      9     31       Ala-rich.
FT   VAR_SEQ       1    389       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:14702039}.
FT                                /FTId=VSP_029287.
FT   VAR_SEQ     260    318       RLHRNREDYVERSAEFADGLLSKALKDIQSGALDINKAGIL
FT                                YGIPQKTLLLHLEALPAG -> MLQVKTDEKLNVSDENTAS
FT                                CPLSPIKMCLNRPIEWNLNLTTASLTSCTVHNQNLKSEEK
FT                                (in isoform 3).
FT                                {ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_029288.
FT   VAR_SEQ     319    602       Missing (in isoform 3).
FT                                {ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_029289.
FT   CONFLICT    407    407       N -> S (in Ref. 1; BAB70892).
FT                                {ECO:0000305}.
SQ   SEQUENCE   602 AA;  66964 MW;  05245F999E5A61D7 CRC64;
     MDKGRERMAA AAAAAAAAAA AAQCRSPRCA AERRGFRREL DSWRHRLMHC VGFESILEGL
     YGPRLRRDLS LFEDCEPEEL TDWSMDEKCS FCNLQREAVS DCIPSLDSSQ STPTEELSSQ
     GQSNTDKIEC QAENYLNALF RKKDLPQNCD PNIPLVAQEL MKKMIRQFAI EYISKSGKTQ
     ENRNGSIGPS IVCKSIQMNQ AENSLQEEQE GPLDLTVNRM QEQNTQQGDG VLDLSTKKTS
     IKSEESSICD PSSENSVAGR LHRNREDYVE RSAEFADGLL SKALKDIQSG ALDINKAGIL
     YGIPQKTLLL HLEALPAGKP ASFKNKTRDF HDSYSYKDSK ETCAVLQKVA LWARAQAERT
     EKSKLNLLET SEIKFPTAST YLHQLTLQKM VTQFKEKNES LQYETSNPTV QLKIPQLRVS
     SVSKSQPDGS GLLDVMYQVS KTSSVLEGSA LQKLKNILPK QNKIECSGPV THSSVDSYFL
     HGDLSPLCLN SKNGTVDGTS ENTEDGLDRK DSKQPRKKRG RYRQYDHEIM EEAIAMVMSG
     KMSVSKAQGI YGVPHSTLEY KVKERSGTLK TPPKKKLRLP DTGLYNMTDS GTGSCKNSSK
     PV
//
ID   LCOR_HUMAN              Reviewed;         433 AA.
AC   Q96JN0; D3DR47; Q5VW16; Q7Z723; Q86T32; Q86T33; Q8N3L6;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2006, sequence version 2.
DT   11-NOV-2015, entry version 103.
DE   RecName: Full=Ligand-dependent corepressor;
DE            Short=LCoR;
DE   AltName: Full=Mblk1-related protein 2;
GN   Name=LCOR; Synonyms=KIAA1795, MLR2;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
RX   PubMed=11347906; DOI=10.1093/dnares/8.2.85;
RA   Nagase T., Nakayama M., Nakajima D., Kikuno R., Ohara O.;
RT   "Prediction of the coding sequences of unidentified human genes. XX.
RT   The complete sequences of 100 new cDNA clones from brain which code
RT   for large proteins in vitro.";
RL   DNA Res. 8:85-95(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Bone marrow, and Skeletal muscle;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA   Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA   Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15164054; DOI=10.1038/nature02462;
RA   Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA   Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA   Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA   Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA   Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J.,
RA   Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
RA   Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA   Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
RA   Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
RA   Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
RA   Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
RA   Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
RA   Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
RA   Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
RA   Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
RA   Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
RA   Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
RA   Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
RA   Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA   Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
RA   Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
RA   Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
RA   Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
RA   Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
RA   Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT   "The DNA sequence and comparative analysis of human chromosome 10.";
RL   Nature 429:375-381(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Lung;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   FUNCTION, INTERACTION WITH CTBP1; ESR1; ESR2; HDAC3 AND HDAC6,
RP   SUBCELLULAR LOCATION, MUTAGENESIS OF 56-LEU-LEU-57, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=12535528; DOI=10.1016/S1097-2765(03)00014-5;
RA   Fernandes I., Bastien Y., Wai T., Nygard K., Lin R., Cormier O.,
RA   Lee H.S., Eng F., Bertos N.R., Pelletier N., Mader S., Han V.K.M.,
RA   Yang X.-J., White J.H.;
RT   "Ligand-dependent nuclear receptor corepressor LCoR functions by
RT   histone deacetylase-dependent and -independent mechanisms.";
RL   Mol. Cell 11:139-150(2003).
RN   [7]
RP   IDENTIFICATION IN A COREPRESSOR COMPLEX, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RX   PubMed=12700765; DOI=10.1038/nature01550;
RA   Shi Y., Sawada J., Sui G., Affar E.B., Whetstine J.R., Lan F.,
RA   Ogawa H., Luke M.P.-S., Nakatani Y., Shi Y.;
RT   "Coordinated histone modifications mediated by a CtBP co-repressor
RT   complex.";
RL   Nature 422:735-738(2003).
RN   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [9]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA   Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT   a refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-63 AND SER-249, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA   Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full
RT   phosphorylation site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [11]
RP   STRUCTURE BY NMR OF 343-405.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structures of the HTH domain of human LCOR protein.";
RL   Submitted (NOV-2005) to the PDB data bank.
CC   -!- FUNCTION: May act as transcription activator that binds DNA
CC       elements with the sequence 5'-CCCTATCGATCGATCTCTACCT-3' (By
CC       similarity). Repressor of ligand-dependent transcription
CC       activation by target nuclear receptors. Repressor of ligand-
CC       dependent transcription activation by ESR1, ESR2, NR3C1, PGR,
CC       RARA, RARB, RARG, RXRA and VDR. {ECO:0000250,
CC       ECO:0000269|PubMed:12535528}.
CC   -!- SUBUNIT: Interacts with ESR1 and ESR2 in the presence of
CC       estradiol. Interacts with CTBP1, HDAC3 and HDAC6. Component of a
CC       large corepressor complex that contains about 20 proteins,
CC       including CTBP1, CTBP2, HDAC1 and HDAC2.
CC       {ECO:0000269|PubMed:12535528, ECO:0000269|PubMed:12700765}.
CC   -!- INTERACTION:
CC       P56545:CTBP2; NbExp=3; IntAct=EBI-8833163, EBI-741533;
CC       Q8IY44:CTBP2; NbExp=3; IntAct=EBI-8833163, EBI-10171902;
CC       Q08379:GOLGA2; NbExp=3; IntAct=EBI-8833163, EBI-618309;
CC       Q13077:TRAF1; NbExp=3; IntAct=EBI-8833163, EBI-359224;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-
CC       ProRule:PRU00320, ECO:0000269|PubMed:12535528}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q96JN0-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q96JN0-2; Sequence=VSP_018585, VSP_018586;
CC   -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:12535528}.
CC   -!- SIMILARITY: Contains 1 HTH psq-type DNA-binding domain.
CC       {ECO:0000255|PROSITE-ProRule:PRU00320}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB47424.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AB058698; BAB47424.1; ALT_INIT; mRNA.
DR   EMBL; AL834245; CAD38921.2; -; mRNA.
DR   EMBL; AL832106; CAD91159.1; -; mRNA.
DR   EMBL; AL832044; CAD91160.1; -; mRNA.
DR   EMBL; AL442123; CAH70915.1; -; Genomic_DNA.
DR   EMBL; CH471066; EAW49963.1; -; Genomic_DNA.
DR   EMBL; CH471066; EAW49965.1; -; Genomic_DNA.
DR   EMBL; CH471066; EAW49966.1; -; Genomic_DNA.
DR   EMBL; BC053359; AAH53359.1; -; mRNA.
DR   CCDS; CCDS53561.1; -. [Q96JN0-2]
DR   CCDS; CCDS7451.1; -. [Q96JN0-1]
DR   RefSeq; NP_001164236.1; NM_001170765.1. [Q96JN0-1]
DR   RefSeq; NP_001164237.1; NM_001170766.1. [Q96JN0-2]
DR   RefSeq; NP_115816.2; NM_032440.3. [Q96JN0-1]
DR   RefSeq; XP_006718097.1; XM_006718034.2. [Q96JN0-1]
DR   UniGene; Hs.745068; -.
DR   PDB; 2COB; NMR; -; A=343-405.
DR   PDBsum; 2COB; -.
DR   ProteinModelPortal; Q96JN0; -.
DR   SMR; Q96JN0; 346-405.
DR   BioGrid; 124093; 23.
DR   IntAct; Q96JN0; 4.
DR   STRING; 9606.ENSP00000348298; -.
DR   PhosphoSite; Q96JN0; -.
DR   BioMuta; LCOR; -.
DR   DMDM; 108936028; -.
DR   MaxQB; Q96JN0; -.
DR   PaxDb; Q96JN0; -.
DR   PRIDE; Q96JN0; -.
DR   DNASU; 84458; -.
DR   Ensembl; ENST00000356016; ENSP00000348298; ENSG00000196233. [Q96JN0-1]
DR   Ensembl; ENST00000371097; ENSP00000360138; ENSG00000196233. [Q96JN0-1]
DR   Ensembl; ENST00000371103; ENSP00000360144; ENSG00000196233. [Q96JN0-1]
DR   Ensembl; ENST00000540664; ENSP00000443431; ENSG00000196233. [Q96JN0-2]
DR   GeneID; 84458; -.
DR   KEGG; hsa:84458; -.
DR   UCSC; uc001kmr.3; human. [Q96JN0-2]
DR   UCSC; uc001kms.2; human. [Q96JN0-1]
DR   CTD; 84458; -.
DR   GeneCards; LCOR; -.
DR   HGNC; HGNC:29503; LCOR.
DR   HPA; HPA031428; -.
DR   HPA; HPA031429; -.
DR   MIM; 607698; gene.
DR   neXtProt; NX_Q96JN0; -.
DR   PharmGKB; PA145148487; -.
DR   eggNOG; KOG4565; Eukaryota.
DR   eggNOG; ENOG4111GCI; LUCA.
DR   GeneTree; ENSGT00520000055615; -.
DR   HOVERGEN; HBG079596; -.
DR   InParanoid; Q96JN0; -.
DR   OMA; HYEFNFS; -.
DR   OrthoDB; EOG73RBBB; -.
DR   PhylomeDB; Q96JN0; -.
DR   TreeFam; TF319589; -.
DR   ChiTaRS; LCOR; human.
DR   EvolutionaryTrace; Q96JN0; -.
DR   GeneWiki; LCOR; -.
DR   GenomeRNAi; 84458; -.
DR   NextBio; 74251; -.
DR   PRO; PR:Q96JN0; -.
DR   Proteomes; UP000005640; Chromosome 10.
DR   Bgee; Q96JN0; -.
DR   CleanEx; HS_LCOR; -.
DR   Genevisible; Q96JN0; HS.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IEA:Ensembl.
DR   GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IEA:Ensembl.
DR   GO; GO:0006366; P:transcription from RNA polymerase II promoter; IEA:Ensembl.
DR   InterPro; IPR009057; Homeodomain-like.
DR   InterPro; IPR007889; HTH_Psq.
DR   Pfam; PF05225; HTH_psq; 1.
DR   SUPFAM; SSF46689; SSF46689; 1.
DR   PROSITE; PS50960; HTH_PSQ; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Activator; Alternative splicing; Complete proteome;
KW   DNA-binding; Nucleus; Phosphoprotein; Reference proteome; Repressor;
KW   Transcription; Transcription regulation.
FT   CHAIN         1    433       Ligand-dependent corepressor.
FT                                /FTId=PRO_0000236807.
FT   DOMAIN      340    392       HTH psq-type. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00320}.
FT   DNA_BIND    368    388       H-T-H motif. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00320}.
FT   MOTIF        53     57       Interaction with nuclear receptors.
FT   MOTIF       339    345       Nuclear localization signal.
FT                                {ECO:0000255}.
FT   MOD_RES      63     63       Phosphoserine.
FT                                {ECO:0000244|PubMed:20068231}.
FT   MOD_RES     249    249       Phosphoserine.
FT                                {ECO:0000244|PubMed:20068231}.
FT   VAR_SEQ     405    406       RS -> SG (in isoform 2).
FT                                {ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_018585.
FT   VAR_SEQ     407    433       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_018586.
FT   MUTAGEN      56     57       LL->AA: Loss of estradiol-dependent
FT                                interaction with ESR1 and ESR2.
FT                                {ECO:0000269|PubMed:12535528}.
FT   CONFLICT      6      6       Q -> P (in Ref. 2; CAD91159).
FT                                {ECO:0000305}.
FT   CONFLICT    321    321       S -> P (in Ref. 2; CAD38921).
FT                                {ECO:0000305}.
FT   HELIX       351    362       {ECO:0000244|PDB:2COB}.
FT   HELIX       368    375       {ECO:0000244|PDB:2COB}.
FT   HELIX       379    389       {ECO:0000244|PDB:2COB}.
FT   TURN        390    393       {ECO:0000244|PDB:2COB}.
SQ   SEQUENCE   433 AA;  47007 MW;  5F934FE687417740 CRC64;
     MQRMIQQFAA EYTSKNSSTQ DPSQPNSTKN QSLPKASPVT TSPTAATTQN PVLSKLLMAD
     QDSPLDLTVR KSQSEPSEQD GVLDLSTKKS PCAGSTSLSH SPGCSSTQGN GRPGRPSQYR
     PDGLRSGDGV PPRSLQDGTR EGFGHSTSLK VPLARSLQIS EELLSRNQLS TAASLGPSGL
     QNHGQHLILS REASWAKPHY EFNLSRMKFR GNGALSNISD LPFLAENSAF PKMALQAKQD
     GKKDVSHSSP VDLKIPQVRG MDLSWESRTG DQYSYSSLVM GSQTESALSK KLRAILPKQS
     RKSMLDAGPD SWGSDAEQST SGQPYPTSDQ EGDPGSKQPR KKRGRYRQYN SEILEEAISV
     VMSGKMSVSK AQSIYGIPHS TLEYKVKERL GTLKNPPKKK MKLMRSEGPD VSVKIELDPQ
     GEAAQSANES KNE
//
ID   MDS1_HUMAN              Reviewed;         169 AA.
AC   Q13465; Q13466; Q6FH90;
DT   19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   11-NOV-2015, entry version 110.
DE   RecName: Full=MDS1 and EVI1 complex locus protein MDS1;
DE   AltName: Full=Myelodysplasia syndrome 1 protein;
DE   AltName: Full=Myelodysplasia syndrome-associated protein 1;
GN   Name=MECOM; Synonyms=MDS1;
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].
RC   TISSUE=Kidney, and Pancreas;
RX   PubMed=8643684; DOI=10.1073/pnas.93.4.1642;
RA   Fears S., Mathieu C., Zeleznik-Le N., Huang S., Rowley J.D.,
RA   Nucifora G.;
RT   "Intergenic splicing of MDS1 and EVI1 occurs in normal tissues as well
RT   as in myeloid leukemia and produces a new member of the PR domain
RT   family.";
RL   Proc. Natl. Acad. Sci. U.S.A. 93:1642-1647(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT   "Cloning of human full open reading frames in Gateway(TM) system entry
RT   vector (pDONR201).";
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [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 [LARGE SCALE MRNA].
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).
CC   -!- INTERACTION:
CC       Q5R372-2:RABGAP1L; NbExp=3; IntAct=EBI-8475192, EBI-10692254;
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative promoter usage, Alternative splicing; Named isoforms=6;
CC       Name=3; Synonyms=Mds1;
CC         IsoId=Q13465-1; Sequence=Displayed;
CC         Note=Produced by alternative promoter usage.;
CC       Name=1; Synonyms=Long, Evi-1a;
CC         IsoId=Q03112-1; Sequence=External;
CC       Name=2; Synonyms=Evi-1c, Mds1/Evi1;
CC         IsoId=Q03112-3; Sequence=External;
CC         Note=Produced by alternative promoter usage. Contains an
CC         additional SET domain at positions 79-194. Unable to form
CC         homooligomers, to interact with CTBP1 and SMAD3 and to repress
CC         TGF-beta signaling. Contains a glycyl lysine isopeptide
CC         (Lys-Gly) (interchain with G-Cter in SUMO2) at position 190.;
CC       Name=4;
CC         IsoId=Q03112-4; Sequence=External;
CC         Note=Contains a glycyl lysine isopeptide (Lys-Gly) (interchain
CC         with G-Cter in SUMO2) at position 66.;
CC       Name=5;
CC         IsoId=Q03112-5; Sequence=External;
CC       Name=6;
CC         IsoId=Q03112-6; Sequence=External;
CC   -!- DISEASE: Note=A chromosomal aberration involving MDS1 is found in
CC       a form of acute myeloid leukemia (AML). Translocation t(3;21) with
CC       AML1.
CC   -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC       and Haematology;
CC       URL="http://atlasgeneticsoncology.org/Genes/EVI103q26ID19.html";
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; U43292; AAB05839.1; -; mRNA.
DR   EMBL; U43293; AAB05840.1; ALT_SEQ; mRNA.
DR   EMBL; CR541866; CAG46664.1; -; mRNA.
DR   EMBL; CR541886; CAG46684.1; -; mRNA.
DR   EMBL; CH471052; EAW78549.1; -; Genomic_DNA.
DR   EMBL; BC069498; AAH69498.1; -; mRNA.
DR   RefSeq; NP_004982.2; NM_004991.3.
DR   UniGene; Hs.744090; -.
DR   ProteinModelPortal; Q13465; -.
DR   SMR; Q13465; 47-130.
DR   BioGrid; 108423; 21.
DR   IntAct; Q13465; 3.
DR   MINT; MINT-8417693; -.
DR   PhosphoSite; Q13465; -.
DR   MaxQB; Q13465; -.
DR   PRIDE; Q13465; -.
DR   DNASU; 2122; -.
DR   GeneID; 2122; -.
DR   UCSC; uc011bpl.1; human. [Q13465-1]
DR   CTD; 2122; -.
DR   GeneCards; MECOM; -.
DR   HGNC; HGNC:3498; MECOM.
DR   MIM; 600049; gene.
DR   neXtProt; NX_Q13465; -.
DR   PharmGKB; PA27912; -.
DR   PharmGKB; PA30722; -.
DR   HOVERGEN; HBG031707; -.
DR   PhylomeDB; Q13465; -.
DR   ChiTaRS; MECOM; human.
DR   GenomeRNAi; 2122; -.
DR   NextBio; 8579; -.
DR   Proteomes; UP000005640; Unplaced.
DR   CleanEx; HS_MDS1; -.
DR   GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; TAS:ProtInc.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; TAS:GOC.
DR   InterPro; IPR026710; MDS1.
DR   PANTHER; PTHR21652; PTHR21652; 1.
PE   1: Evidence at protein level;
KW   Alternative promoter usage; Alternative splicing;
KW   Chromosomal rearrangement; Complete proteome; Polymorphism;
KW   Reference proteome; Ubl conjugation.
FT   CHAIN         1    169       MDS1 and EVI1 complex locus protein MDS1.
FT                                /FTId=PRO_0000096338.
FT   VARIANT     120    120       P -> S (in dbSNP:rs7622799).
FT                                /FTId=VAR_051183.
SQ   SEQUENCE   169 AA;  18696 MW;  3EE36C8ACB62EFFE CRC64;
     MRSKGRARKL ATNNECVYGN YPEIPLEEMP DADGVASTPS LNIQEPCSPA TSSEAFTPKE
     GSPYKAPIYI PDDIPIPAEF ELRESNMPGA GLGIWTKRKI EVGEKFGPYV GEQRSNLKDP
     SYGWEVHLPR SRRVSVHSWL YLGKRSSDVG IAFSQADVYM PGLQCAFLS
//
ID   NOL4L_HUMAN             Reviewed;         436 AA.
AC   Q96MY1; Q5JYB7; Q6P0Y4; Q9BR34; Q9NQF6;
DT   01-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2003, sequence version 2.
DT   11-NOV-2015, entry version 111.
DE   RecName: Full=Nucleolar protein 4-like;
GN   Name=NOL4L; Synonyms=C20orf112, C20orf113;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Neuron;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=11780052; DOI=10.1038/414865a;
RA   Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA   Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA   Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M.,
RA   Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J.,
RA   Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P.,
RA   Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M.,
RA   Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R.,
RA   Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M.,
RA   Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA   Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA   Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA   Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA   Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA   Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA   Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA   Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA   Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA   Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H.,
RA   Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S.,
RA   Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E.,
RA   Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A.,
RA   Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M.,
RA   Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A.,
RA   Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S.,
RA   Rogers J.;
RT   "The DNA sequence and comparative analysis of human chromosome 20.";
RL   Nature 414:865-871(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Skin;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-130, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
CC   -!- INTERACTION:
CC       Q13363-2:CTBP1; NbExp=3; IntAct=EBI-6660790, EBI-10171858;
CC       P56545:CTBP2; NbExp=3; IntAct=EBI-6660790, EBI-741533;
CC       Q8IY44:CTBP2; NbExp=3; IntAct=EBI-6660790, EBI-10171902;
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q96MY1-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q96MY1-2; Sequence=VSP_014667, VSP_014668;
CC         Note=No experimental confirmation available.;
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK056286; BAB71138.1; -; mRNA.
DR   EMBL; AL034550; CAI42261.1; -; Genomic_DNA.
DR   EMBL; BC065370; AAH65370.1; -; mRNA.
DR   CCDS; CCDS13202.1; -. [Q96MY1-1]
DR   RefSeq; NP_001243727.1; NM_001256798.1.
DR   RefSeq; NP_542183.2; NM_080616.4. [Q96MY1-1]
DR   RefSeq; XP_005260345.1; XM_005260288.1. [Q96MY1-1]
DR   RefSeq; XP_005260346.1; XM_005260289.3. [Q96MY1-1]
DR   UniGene; Hs.516978; -.
DR   UniGene; Hs.729596; -.
DR   ProteinModelPortal; Q96MY1; -.
DR   BioGrid; 126651; 5.
DR   IntAct; Q96MY1; 4.
DR   STRING; 9606.ENSP00000352704; -.
DR   PhosphoSite; Q96MY1; -.
DR   BioMuta; C20orf112; -.
DR   DMDM; 28212212; -.
DR   MaxQB; Q96MY1; -.
DR   PaxDb; Q96MY1; -.
DR   PRIDE; Q96MY1; -.
DR   DNASU; 140688; -.
DR   Ensembl; ENST00000359676; ENSP00000352704; ENSG00000197183. [Q96MY1-1]
DR   GeneID; 140688; -.
DR   KEGG; hsa:140688; -.
DR   UCSC; uc002wxu.5; human. [Q96MY1-1]
DR   CTD; 140688; -.
DR   GeneCards; NOL4L; -.
DR   H-InvDB; HIX0015727; -.
DR   H-InvDB; HIX0015728; -.
DR   HGNC; HGNC:16106; NOL4L.
DR   HPA; HPA041768; -.
DR   HPA; HPA043600; -.
DR   neXtProt; NX_Q96MY1; -.
DR   PharmGKB; PA25652; -.
DR   eggNOG; ENOG410IHZD; Eukaryota.
DR   eggNOG; ENOG410YIBB; LUCA.
DR   GeneTree; ENSGT00390000017363; -.
DR   HOGENOM; HOG000220856; -.
DR   HOVERGEN; HBG031438; -.
DR   InParanoid; Q96MY1; -.
DR   PhylomeDB; Q96MY1; -.
DR   TreeFam; TF325594; -.
DR   ChiTaRS; C20orf112; human.
DR   GenomeRNAi; 140688; -.
DR   NextBio; 84231; -.
DR   PRO; PR:Q96MY1; -.
DR   Proteomes; UP000005640; Chromosome 20.
DR   Bgee; Q96MY1; -.
DR   CleanEx; HS_C20orf112; -.
DR   ExpressionAtlas; Q96MY1; baseline and differential.
DR   Genevisible; Q96MY1; HS.
DR   GO; GO:0005737; C:cytoplasm; IDA:HPA.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   InterPro; IPR026746; NOL4L.
DR   PANTHER; PTHR12449:SF19; PTHR12449:SF19; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Complete proteome; Phosphoprotein;
KW   Reference proteome.
FT   CHAIN         1    436       Nucleolar protein 4-like.
FT                                /FTId=PRO_0000079456.
FT   COMPBIAS    161    169       Poly-Asp.
FT   MOD_RES     130    130       Phosphoserine.
FT                                {ECO:0000244|PubMed:18669648}.
FT   VAR_SEQ     382    398       TPTPSSTSTSRPVPTAQ -> SALSGEPPTRRWGCSSV
FT                                (in isoform 2).
FT                                {ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_014667.
FT   VAR_SEQ     399    436       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_014668.
FT   CONFLICT    215    215       K -> E (in Ref. 1; BAB71138).
FT                                {ECO:0000305}.
SQ   SEQUENCE   436 AA;  47215 MW;  139A07537D875DF8 CRC64;
     MSDSTWMSAD PHLASSLSPS QDERMRSPQN LHSQEDDDSS SESGSGNGSS TLNPSTSSST
     QGDPAFPEMN GNGAVAPMDF TTAAEDQPIN LCDKLPPATA LGTASYPSDG CGADGLRSRV
     KYGVKTTPES PPYSSGSYDS IKTEVSGCPE DLTVGRAPTA DDDDDDHDDH EDNDKMNDSE
     GMDPERLKAF NMFVRLFVDE NLDRMVPISK QPKEKIQAII ESCSRQFPEF QERARKRIRT
     YLKSCRRMKK NGMEMTRPTP PHLTSAMAEN ILAAACESET RKAAKRMRLE IYQSSQDEPI
     ALDKQHSRDS AAITHSTYSL PASSYSQDPV YANGGLNYSY RGYGALSSNL QPPASLQTGN
     HSNGPTDLSM KGGASTTSTT PTPTPSSTST SRPVPTAQLS PTEISAVRQL IAGYRESAAF
     LLRSADELEN LILQQN
//
ID   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   RBBP5_HUMAN             Reviewed;         538 AA.
AC   Q15291; A8K272; Q7Z6D8; Q8NDZ7;
DT   18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT   14-OCT-2008, sequence version 2.
DT   11-NOV-2015, entry version 147.
DE   RecName: Full=Retinoblastoma-binding protein 5;
DE            Short=RBBP-5;
DE   AltName: Full=Retinoblastoma-binding protein RBQ-3;
GN   Name=RBBP5; Synonyms=RBQ3;
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), PHOSPHORYLATION AT THR-252 AND
RP   SER-497, AND CHARACTERIZATION.
RC   TISSUE=Lung carcinoma, and Testis;
RX   PubMed=7558034; DOI=10.1006/geno.1995.1084;
RA   Saijo M., Sakai Y., Kishino T., Niikawa N., Matsuura Y., Morino K.,
RA   Tamai K., Taya Y.;
RT   "Molecular cloning of a human protein that binds to the retinoblastoma
RT   protein and chromosomal mapping.";
RL   Genomics 27:511-519(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Thalamus;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [3]
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Brain, and Testis;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   IDENTIFICATION IN THE MEN1-ASSOCIATED HISTONE METHYLTRANSFERASE
RP   COMPLEX.
RX   PubMed=14992727; DOI=10.1016/S1097-2765(04)00081-4;
RA   Hughes C.M., Rozenblatt-Rosen O., Milne T.A., Copeland T.D.,
RA   Levine S.S., Lee J.C., Hayes D.N., Shanmugam K.S., Bhattacharjee A.,
RA   Biondi C.A., Kay G.F., Hayward N.K., Hess J.L., Meyerson M.;
RT   "Menin associates with a trithorax family histone methyltransferase
RT   complex and with the hoxc8 locus.";
RL   Mol. Cell 13:587-597(2004).
RN   [7]
RP   IDENTIFICATION IN THE MLL-LIKE COMPLEX.
RX   PubMed=15199122; DOI=10.1128/MCB.24.13.5639-5649.2004;
RA   Yokoyama A., Wang Z., Wysocka J., Sanyal M., Aufiero D.J.,
RA   Kitabayashi I., Herr W., Cleary M.L.;
RT   "Leukemia proto-oncoprotein MLL forms a SET1-like histone
RT   methyltransferase complex with menin to regulate Hox gene
RT   expression.";
RL   Mol. Cell. Biol. 24:5639-5649(2004).
RN   [8]
RP   IDENTIFICATION IN THE MLL1/MLL COMPLEX.
RX   PubMed=15960975; DOI=10.1016/j.cell.2005.04.031;
RA   Dou Y., Milne T.A., Tackett A.J., Smith E.R., Fukuda A., Wysocka J.,
RA   Allis C.D., Chait B.T., Hess J.L., Roeder R.G.;
RT   "Physical association and coordinate function of the H3 K4
RT   methyltransferase MLL1 and the H4 K16 acetyltransferase MOF.";
RL   Cell 121:873-885(2005).
RN   [9]
RP   IDENTIFICATION IN THE SET1 COMPLEX.
RX   PubMed=16253997; DOI=10.1074/jbc.M508312200;
RA   Lee J.-H., Skalnik D.G.;
RT   "CpG-binding protein (CXXC finger protein 1) is a component of the
RT   mammalian Set1 histone H3-Lys4 methyltransferase complex, the analogue
RT   of the yeast Set1/COMPASS complex.";
RL   J. Biol. Chem. 280:41725-41731(2005).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-350, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA   Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA   Mann M.;
RT   "Global, in vivo, and site-specific phosphorylation dynamics in
RT   signaling networks.";
RL   Cell 127:635-648(2006).
RN   [11]
RP   SUBCELLULAR LOCATION, AND IDENTIFICATION IN THE SET1 COMPLEX.
RX   PubMed=17355966; DOI=10.1074/jbc.M609809200;
RA   Lee J.-H., Tate C.M., You J.-S., Skalnik D.G.;
RT   "Identification and characterization of the human Set1B histone H3-
RT   Lys4 methyltransferase complex.";
RL   J. Biol. Chem. 282:13419-13428(2007).
RN   [12]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE MLL2/3
RP   COMPLEX.
RX   PubMed=17500065; DOI=10.1074/jbc.M701574200;
RA   Cho Y.-W., Hong T., Hong S., Guo H., Yu H., Kim D., Guszczynski T.,
RA   Dressler G.R., Copeland T.D., Kalkum M., Ge K.;
RT   "PTIP associates with MLL3- and MLL4-containing histone H3 lysine 4
RT   methyltransferase complex.";
RL   J. Biol. Chem. 282:20395-20406(2007).
RN   [13]
RP   IDENTIFICATION IN SET1 COMPLEX, AND INTERACTION WITH SETD1A.
RX   PubMed=17998332; DOI=10.1128/MCB.01356-07;
RA   Lee J.H., Skalnik D.G.;
RT   "Wdr82 is a C-terminal domain-binding protein that recruits the Setd1A
RT   Histone H3-Lys4 methyltransferase complex to transcription start sites
RT   of transcribed human genes.";
RL   Mol. Cell. Biol. 28:609-618(2008).
RN   [14]
RP   IDENTIFICATION IN SET1 COMPLEX, AND INTERACTION WITH WDR82.
RX   PubMed=18838538; DOI=10.1128/MCB.00976-08;
RA   Wu M., Wang P.F., Lee J.S., Martin-Brown S., Florens L., Washburn M.,
RA   Shilatifard A.;
RT   "Molecular regulation of H3K4 trimethylation by Wdr82, a component of
RT   human Set1/COMPASS.";
RL   Mol. Cell. Biol. 28:7337-7344(2008).
RN   [15]
RP   IDENTIFICATION IN A COMPLEX WITH HCFC1; MKI67; C11ORF30; MATR3; HSPA8;
RP   ZNF335; CCAR2; ASCL2; ZNF335 AND WDR5.
RX   PubMed=19131338; DOI=10.1074/jbc.M805872200;
RA   Garapaty S., Xu C.F., Trojer P., Mahajan M.A., Neubert T.A.,
RA   Samuels H.H.;
RT   "Identification and characterization of a novel nuclear protein
RT   complex involved in nuclear hormone receptor-mediated gene
RT   regulation.";
RL   J. Biol. Chem. 284:7542-7552(2009).
RN   [16]
RP   FUNCTION, CHARACTERIZATION OF THE MLL1/MLL COMPLEX, AND INTERACTION
RP   WITH WDR5 AND ASH2L.
RX   PubMed=19556245; DOI=10.1074/jbc.M109.014498;
RA   Patel A., Dharmarajan V., Vought V.E., Cosgrove M.S.;
RT   "On the mechanism of multiple lysine methylation by the human mixed
RT   lineage leukemia protein-1 (MLL1) core complex.";
RL   J. Biol. Chem. 284:24242-24256(2009).
RN   [17]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-388 AND SER-389, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA   Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full
RT   phosphorylation site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [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   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-525, 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   [20]
RP   INTERACTION WITH ZNF335.
RX   PubMed=23178126; DOI=10.1016/j.cell.2012.10.043;
RA   Yang Y.J., Baltus A.E., Mathew R.S., Murphy E.A., Evrony G.D.,
RA   Gonzalez D.M., Wang E.P., Marshall-Walker C.A., Barry B.J., Murn J.,
RA   Tatarakis A., Mahajan M.A., Samuels H.H., Shi Y., Golden J.A.,
RA   Mahajnah M., Shenhav R., Walsh C.A.;
RT   "Microcephaly gene links trithorax and REST/NRSF to control neural
RT   stem cell proliferation and differentiation.";
RL   Cell 151:1097-1112(2012).
CC   -!- FUNCTION: In embryonic stem (ES) cells, plays a crucial role in
CC       the differentiation potential, particularly along the neural
CC       lineage, regulating gene induction and H3 'Lys-4' methylation at
CC       key developmental loci, including that mediated by retinoic acid
CC       (By similarity). As part of the MLL1/MLL complex, involved in
CC       mono-, di- and trimethylation at 'Lys-4' of histone H3. Histone H3
CC       'Lys-4' methylation represents a specific tag for epigenetic
CC       transcriptional activation. {ECO:0000250,
CC       ECO:0000269|PubMed:19556245}.
CC   -!- SUBUNIT: Component of the SET1 complex, at least composed of the
CC       catalytic subunit (SETD1A or SETD1B), WDR5, WDR82, RBBP5,
CC       ASH2L/ASH2, CXXC1/CFP1, HCFC1 and DPY30. Core component of several
CC       methyltransferase-containing complexes including MLL1/MLL, MLL2/3
CC       (also named ASCOM complex) and MLL4/WBP7. Each complex is at least
CC       composed of ASH2L, RBBP5, WDR5, DPY30, one or more specific
CC       histone methyltransferases (KMT2A/MLL1, KMT2D/MLL2, KMT2C/MLL3 and
CC       KMT2B/MLL4), and the facultative components PAGR1, BAP18, CHD8,
CC       E2F6, HCFC1, HCFC2, HSP70, INO80C, KDM6A, KANSL1, LAS1L, MAX,
CC       MCRS1, MEN1, MGA, MYST1/MOF, NCOA6, PAXIP1/PTIP, PELP1, PHF20,
CC       PRP31, RING2, RUVB1/TIP49A, RUVB2/TIP49B, SENP3, TAF1, TAF4, TAF6,
CC       TAF7, TAF9, TEX10 and alpha- and beta-tubulin. Interacts with WDR5
CC       and ASH2L; the interaction is direct. Interacts with WDR82 and
CC       SETD1A. Part of a complex composed at least of ASCL2,
CC       C11orf30/EMSY, HCFC1, HSPA8, CCAR2, MATR3, MKI67, RBBP5, TUBB2A,
CC       WDR5 and ZNF335; this complex may have a histone H3-specific
CC       methyltransferase activity (By similarity). {ECO:0000250}.
CC   -!- INTERACTION:
CC       Q9UBL3:ASH2L; NbExp=18; IntAct=EBI-592823, EBI-540797;
CC       Q9HCK8:CHD8; NbExp=2; IntAct=EBI-592823, EBI-1169146;
CC       Q13619:CUL4A; NbExp=3; IntAct=EBI-592823, EBI-456106;
CC       Q9P0U4:CXXC1; NbExp=5; IntAct=EBI-592823, EBI-949911;
CC       Q03164:KMT2A; NbExp=6; IntAct=EBI-592823, EBI-591370;
CC       O15047:SETD1A; NbExp=3; IntAct=EBI-592823, EBI-540779;
CC       P61964:WDR5; NbExp=6; IntAct=EBI-592823, EBI-540834;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17355966}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q15291-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q15291-2; Sequence=VSP_035583;
CC   -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC   -!- SIMILARITY: Contains 6 WD repeats. {ECO:0000255|PROSITE-
CC       ProRule:PRU00221}.
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DR   EMBL; X85134; CAA59446.1; -; mRNA.
DR   EMBL; AK290137; BAF82826.1; -; mRNA.
DR   EMBL; AL583832; CAI15286.1; -; Genomic_DNA.
DR   EMBL; AC093422; CAI15286.1; JOINED; Genomic_DNA.
DR   EMBL; AL583832; CAI15287.1; -; Genomic_DNA.
DR   EMBL; AC093422; CAI15287.1; JOINED; Genomic_DNA.
DR   EMBL; CH471067; EAW91537.1; -; Genomic_DNA.
DR   EMBL; CH471067; EAW91538.1; -; Genomic_DNA.
DR   EMBL; BC037284; AAH37284.1; -; mRNA.
DR   EMBL; BC053856; AAH53856.1; -; mRNA.
DR   EMBL; BC075059; AAH75059.1; -; mRNA.
DR   EMBL; BC075060; AAH75060.1; -; mRNA.
DR   CCDS; CCDS30983.1; -. [Q15291-1]
DR   CCDS; CCDS53463.1; -. [Q15291-2]
DR   PIR; A57624; A57624.
DR   RefSeq; NP_001180201.1; NM_001193272.1. [Q15291-2]
DR   RefSeq; NP_001180202.1; NM_001193273.1.
DR   RefSeq; NP_005048.2; NM_005057.3. [Q15291-1]
DR   UniGene; Hs.519230; -.
DR   PDB; 3P4F; X-ray; 2.35 A; B=371-381.
DR   PDB; 4X8N; X-ray; 2.10 A; B=347-356.
DR   PDB; 4X8P; X-ray; 2.20 A; B=344-355.
DR   PDBsum; 3P4F; -.
DR   PDBsum; 4X8N; -.
DR   PDBsum; 4X8P; -.
DR   ProteinModelPortal; Q15291; -.
DR   SMR; Q15291; 30-320.
DR   BioGrid; 111864; 64.
DR   DIP; DIP-29224N; -.
DR   IntAct; Q15291; 24.
DR   MINT; MINT-3031197; -.
DR   STRING; 9606.ENSP00000264515; -.
DR   ChEMBL; CHEMBL3137282; -.
DR   PhosphoSite; Q15291; -.
DR   BioMuta; RBBP5; -.
DR   DMDM; 209572664; -.
DR   MaxQB; Q15291; -.
DR   PaxDb; Q15291; -.
DR   PRIDE; Q15291; -.
DR   DNASU; 5929; -.
DR   Ensembl; ENST00000264515; ENSP00000264515; ENSG00000117222. [Q15291-1]
DR   Ensembl; ENST00000367164; ENSP00000356132; ENSG00000117222. [Q15291-2]
DR   GeneID; 5929; -.
DR   KEGG; hsa:5929; -.
DR   UCSC; uc001hbu.2; human. [Q15291-1]
DR   UCSC; uc001hbv.2; human. [Q15291-2]
DR   CTD; 5929; -.
DR   GeneCards; RBBP5; -.
DR   H-InvDB; HIX0023636; -.
DR   HGNC; HGNC:9888; RBBP5.
DR   HPA; HPA049042; -.
DR   HPA; HPA058085; -.
DR   MIM; 600697; gene.
DR   neXtProt; NX_Q15291; -.
DR   PharmGKB; PA34252; -.
DR   eggNOG; KOG1273; Eukaryota.
DR   eggNOG; ENOG410XTA2; LUCA.
DR   GeneTree; ENSGT00530000064100; -.
DR   HOVERGEN; HBG054324; -.
DR   InParanoid; Q15291; -.
DR   KO; K14961; -.
DR   OMA; EQGVIEW; -.
DR   OrthoDB; EOG7S21X6; -.
DR   PhylomeDB; Q15291; -.
DR   TreeFam; TF313289; -.
DR   Reactome; R-HSA-201722; formation of the beta-catenin:TCF transactivating complex.
DR   Reactome; R-HSA-3214841; PKMTs methylate histone lysines.
DR   Reactome; R-HSA-3769402; deactivation of the beta-catenin transactivating complex.
DR   SignaLink; Q15291; -.
DR   GeneWiki; RBBP5; -.
DR   GenomeRNAi; 5929; -.
DR   NextBio; 23098; -.
DR   PRO; PR:Q15291; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   Bgee; Q15291; -.
DR   CleanEx; HS_RBBP5; -.
DR   ExpressionAtlas; Q15291; baseline and differential.
DR   Genevisible; Q15291; HS.
DR   GO; GO:0035097; C:histone methyltransferase complex; IDA:UniProtKB.
DR   GO; GO:0071339; C:MLL1 complex; IDA:UniProtKB.
DR   GO; GO:0005730; C:nucleolus; IDA:HPA.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0048188; C:Set1C/COMPASS complex; IDA:UniProtKB.
DR   GO; GO:0035064; F:methylated histone binding; IDA:UniProtKB.
DR   GO; GO:0044212; F:transcription regulatory region DNA binding; IDA:UniProtKB.
DR   GO; GO:0006974; P:cellular response to DNA damage stimulus; IDA:MGI.
DR   GO; GO:0006325; P:chromatin organization; TAS:Reactome.
DR   GO; GO:0051568; P:histone H3-K4 methylation; IDA:UniProtKB.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
DR   GO; GO:0043627; P:response to estrogen; IDA:UniProtKB.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
DR   Gene3D; 2.130.10.10; -; 1.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR017986; WD40_repeat_dom.
DR   Pfam; PF00400; WD40; 1.
DR   SMART; SM00320; WD40; 5.
DR   PROSITE; PS50082; WD_REPEATS_2; 1.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Chromatin regulator;
KW   Complete proteome; Nucleus; Phosphoprotein; Reference proteome;
KW   Repeat; Transcription; Transcription regulation; WD repeat.
FT   CHAIN         1    538       Retinoblastoma-binding protein 5.
FT                                /FTId=PRO_0000051194.
FT   REPEAT       22     63       WD 1.
FT   REPEAT       64    103       WD 2.
FT   REPEAT      148    188       WD 3.
FT   REPEAT      196    235       WD 4.
FT   REPEAT      249    291       WD 5.
FT   REPEAT      293    331       WD 6.
FT   MOD_RES     252    252       Phosphothreonine; by CDK1.
FT                                {ECO:0000269|PubMed:7558034}.
FT   MOD_RES     350    350       Phosphoserine.
FT                                {ECO:0000244|PubMed:17081983}.
FT   MOD_RES     388    388       Phosphoserine.
FT                                {ECO:0000244|PubMed:20068231}.
FT   MOD_RES     389    389       Phosphoserine.
FT                                {ECO:0000244|PubMed:20068231}.
FT   MOD_RES     497    497       Phosphoserine; by CDK1.
FT                                {ECO:0000269|PubMed:7558034}.
FT   MOD_RES     525    525       Phosphoserine.
FT                                {ECO:0000244|PubMed:21406692}.
FT   VAR_SEQ     492    529       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:14702039,
FT                                ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_035583.
FT   CONFLICT    206    206       F -> Y (in Ref. 2; BAF82826).
FT                                {ECO:0000305}.
FT   CONFLICT    244    244       K -> E (in Ref. 1; CAA59446).
FT                                {ECO:0000305}.
FT   CONFLICT    351    351       E -> G (in Ref. 1; CAA59446).
FT                                {ECO:0000305}.
FT   TURN        349    352       {ECO:0000244|PDB:4X8N}.
SQ   SEQUENCE   538 AA;  59153 MW;  095CCB41613CBED9 CRC64;
     MNLELLESFG QNYPEEADGT LDCISMALTC TFNRWGTLLA VGCNDGRIVI WDFLTRGIAK
     IISAHIHPVC SLCWSRDGHK LVSASTDNIV SQWDVLSGDC DQRFRFPSPI LKVQYHPRDQ
     NKVLVCPMKS APVMLTLSDS KHVVLPVDDD SDLNVVASFD RRGEYIYTGN AKGKILVLKT
     DSQDLVASFR VTTGTSNTTA IKSIEFARKG SCFLINTADR IIRVYDGREI LTCGRDGEPE
     PMQKLQDLVN RTPWKKCCFS GDGEYIVAGS ARQHALYIWE KSIGNLVKIL HGTRGELLLD
     VAWHPVRPII ASISSGVVSI WAQNQVENWS AFAPDFKELD ENVEYEERES EFDIEDEDKS
     EPEQTGADAA EDEEVDVTSV DPIAAFCSSD EELEDSKALL YLPIAPEVED PEENPYGPPP
     DAVQTSLMDE GASSEKKRQS SADGSQPPKK KPKTTNIELQ GVPNDEVHPL LGVKGDGKSK
     KKQAGRPKGS KGKEKDSPFK PKLYKGDRGL PLEGSAKGKV QAELSQPLTA GGAISELL
//
ID   SOBP_HUMAN              Reviewed;         873 AA.
AC   A7XYQ1; B0QZ12; Q5BJD4; Q8N2B2;
DT   04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 2.
DT   11-NOV-2015, entry version 67.
DE   RecName: Full=Sine oculis-binding protein homolog;
DE   AltName: Full=Jackson circler protein 1;
GN   Name=SOBP {ECO:0000312|EMBL:AAH91526.2};
GN   Synonyms=JXC1 {ECO:0000312|EMBL:ABF72848.1};
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] {ECO:0000312|EMBL:ABF72848.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT GLY-683.
RA   Chen Z., Noben-Trauth K.;
RT   "Mutations in Jxc1 cause deafness, vestibular deficits and cochlear
RT   malformation in the Jackson circler (jc) mutant mouse.";
RL   Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=14574404; DOI=10.1038/nature02055;
RA   Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA   Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
RA   Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
RA   Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
RA   Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
RA   Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
RA   Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
RA   Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA   Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA   Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA   Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
RA   Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
RA   Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
RA   Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
RA   Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
RA   Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
RA   Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
RA   Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
RA   Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
RA   Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
RA   Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA   Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
RA   McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
RA   Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
RA   Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
RA   Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
RA   Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
RA   Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
RA   Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
RA   Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
RA   Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
RA   Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
RA   Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
RT   "The DNA sequence and analysis of human chromosome 6.";
RL   Nature 425:805-811(2003).
RN   [3] {ECO:0000312|EMBL:BAC03537.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-224.
RC   TISSUE=Amygdala {ECO:0000312|EMBL:BAC03537.1};
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] {ECO:0000312|EMBL:AAH91526.2}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-140.
RC   TISSUE=Brain {ECO:0000312|EMBL:AAH91526.2};
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   INVOLVEMENT IN MRAMS.
RX   PubMed=21035105; DOI=10.1016/j.ajhg.2010.10.005;
RA   Birk E., Har-Zahav A., Manzini C.M., Pasmanik-Chor M., Kornreich L.,
RA   Walsh C.A., Noben-Trauth K., Albin A., Simon A.J., Colleaux L.,
RA   Morad Y., Rainshtein L., Tischfield D.J., Wang P., Magal N., Maya I.,
RA   Shoshani N., Rechavi G., Gothelf D., Maydan G., Shohat M.,
RA   Basel-Vanagaite L.;
RT   "SOBP is mutated in syndromic and nonsyndromic intellectual disability
RT   and is highly expressed in the brain limbic system.";
RL   Am. J. Hum. Genet. 87:694-700(2010).
RN   [6]
RP   IDENTIFICATION OF REPEAT SUMO-INTERACTING MOTIF, AND INTERACTION WITH
RP   SUMO1 AND SUMO2.
RX   PubMed=23086935; DOI=10.1074/jbc.M112.410985;
RA   Sun H., Hunter T.;
RT   "PolySUMO-binding proteins identified through a string search.";
RL   J. Biol. Chem. 287:42071-42083(2012).
CC   -!- FUNCTION: Implicated in development of the cochlea.
CC       {ECO:0000250|UniProtKB:Q0P5V2}.
CC   -!- SUBUNIT: Interacts (via SIM domains) with SUMO1 and SUMO2.
CC       {ECO:0000269|PubMed:23086935}.
CC   -!- DISEASE: Mental retardation, anterior maxillary protrusion, and
CC       strabismus (MRAMS) [MIM:613671]: A syndrome characterized by
CC       severe mental retardation, strabismus and dysmorphic features such
CC       as anterior maxillary protrusion with vertical maxillary excess,
CC       open bite and prominent crowded teeth. Some patients may lack
CC       dysmorphic features and manifest temporal lobe epilepsy and
CC       psychosis. Esotropia and amblyopia are present in some
CC       individuals. {ECO:0000269|PubMed:21035105}. Note=The disease is
CC       caused by mutations affecting the gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the SOBP family. {ECO:0000255}.
CC   -!- SIMILARITY: Contains 2 FCS-type zinc fingers. {ECO:0000255}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH91526.2; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
CC       Sequence=BAC03537.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
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DR   EMBL; DQ507800; ABF72848.1; -; mRNA.
DR   EMBL; AL096816; CAQ08124.1; -; Genomic_DNA.
DR   EMBL; AL121957; CAQ08124.1; JOINED; Genomic_DNA.
DR   EMBL; AL671934; CAQ08124.1; JOINED; Genomic_DNA.
DR   EMBL; AL671934; CAQ10205.1; -; Genomic_DNA.
DR   EMBL; AL096816; CAQ10205.1; JOINED; Genomic_DNA.
DR   EMBL; AL121957; CAQ10205.1; JOINED; Genomic_DNA.
DR   EMBL; AL121957; CAQ10380.1; -; Genomic_DNA.
DR   EMBL; AL096816; CAQ10380.1; JOINED; Genomic_DNA.
DR   EMBL; AL671934; CAQ10380.1; JOINED; Genomic_DNA.
DR   EMBL; AK090879; BAC03537.1; ALT_SEQ; mRNA.
DR   EMBL; BC091526; AAH91526.2; ALT_SEQ; mRNA.
DR   CCDS; CCDS43488.1; -.
DR   RefSeq; NP_060483.3; NM_018013.3.
DR   UniGene; Hs.445244; -.
DR   ProteinModelPortal; A7XYQ1; -.
DR   BioGrid; 120399; 3.
DR   IntAct; A7XYQ1; 2.
DR   MINT; MINT-6778579; -.
DR   STRING; 9606.ENSP00000318900; -.
DR   PhosphoSite; A7XYQ1; -.
DR   BioMuta; SOBP; -.
DR   MaxQB; A7XYQ1; -.
DR   PaxDb; A7XYQ1; -.
DR   PRIDE; A7XYQ1; -.
DR   Ensembl; ENST00000317357; ENSP00000318900; ENSG00000112320.
DR   GeneID; 55084; -.
DR   KEGG; hsa:55084; -.
DR   UCSC; uc003prx.3; human.
DR   CTD; 55084; -.
DR   GeneCards; SOBP; -.
DR   H-InvDB; HIX0006109; -.
DR   HGNC; HGNC:29256; SOBP.
DR   HPA; HPA029242; -.
DR   MIM; 613667; gene.
DR   MIM; 613671; phenotype.
DR   neXtProt; NX_A7XYQ1; -.
DR   PharmGKB; PA162404346; -.
DR   eggNOG; ENOG410IEAE; Eukaryota.
DR   eggNOG; ENOG4111QQS; LUCA.
DR   GeneTree; ENSGT00730000111043; -.
DR   HOGENOM; HOG000008673; -.
DR   HOVERGEN; HBG062766; -.
DR   InParanoid; A7XYQ1; -.
DR   OMA; EHGRSEV; -.
DR   OrthoDB; EOG7F7W8D; -.
DR   PhylomeDB; A7XYQ1; -.
DR   TreeFam; TF324359; -.
DR   ChiTaRS; SOBP; human.
DR   GeneWiki; Sobp; -.
DR   GenomeRNAi; 55084; -.
DR   NextBio; 58645; -.
DR   PRO; PR:A7XYQ1; -.
DR   Proteomes; UP000005640; Chromosome 6.
DR   Bgee; A7XYQ1; -.
DR   CleanEx; HS_SOBP; -.
DR   ExpressionAtlas; A7XYQ1; baseline and differential.
DR   Genevisible; A7XYQ1; HS.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0050890; P:cognition; IMP:HGNC.
DR   GO; GO:0042472; P:inner ear morphogenesis; IEA:Ensembl.
DR   GO; GO:0007626; P:locomotory behavior; IEA:Ensembl.
DR   GO; GO:0007605; P:sensory perception of sound; IEA:Ensembl.
DR   InterPro; IPR026092; RAI2/SOBP.
DR   PANTHER; PTHR23186; PTHR23186; 2.
DR   Pfam; PF15279; SOBP; 1.
PE   1: Evidence at protein level;
KW   Complete proteome; Mental retardation; Metal-binding; Phosphoprotein;
KW   Polymorphism; Reference proteome; Repeat; Zinc; Zinc-finger.
FT   CHAIN         1    873       Sine oculis-binding protein homolog.
FT                                /FTId=PRO_0000312232.
FT   ZN_FING     142    180       FCS-type 1. {ECO:0000255}.
FT   ZN_FING     216    256       FCS-type 2. {ECO:0000255}.
FT   MOTIF       620    624       SUMO interaction motif 1 (SIM); mediates
FT                                the binding to polysumoylated substrates.
FT   MOTIF       653    657       SUMO interaction motif 2 (SIM); mediates
FT                                the binding to polysumoylated substrates.
FT   COMPBIAS    346    552       Pro-rich. {ECO:0000255}.
FT   COMPBIAS    740    763       Pro-rich. {ECO:0000255}.
FT   MOD_RES     629    629       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q0P5V2}.
FT   MOD_RES     699    699       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q0P5V2}.
FT   VARIANT     683    683       S -> G (in dbSNP:rs9486659).
FT                                {ECO:0000269|Ref.1}.
FT                                /FTId=VAR_062215.
FT   CONFLICT    623    623       L -> M (in Ref. 1; ABF72848).
FT                                {ECO:0000305}.
FT   CONFLICT    646    646       L -> M (in Ref. 1; ABF72848).
FT                                {ECO:0000305}.
SQ   SEQUENCE   873 AA;  92658 MW;  894DEF718F6E0CB0 CRC64;
     MAEMEKEGRP PENKRSRKPA HPVKREINEE MKNFAENTMN ELLGWYGYDK VELKDGEDIE
     FRSYPTDGES RQHISVLKEN SLPKPKLPED SVISPYNIST GYSGLATGNG LSDSPAGSKD
     HGSVPIIVPL IPPPFIKPPA EDDVSNVQIM CAWCQKVGIK RYSLSMGSEV KSFCSEKCFA
     ACRRAYFKRN KARDEDGHAE NFPQQHYAKE TPRLAFKNNC ELLVCDWCKH IRHTKEYLDF
     GDGERRLQFC SAKCLNQYKM DIFYKETQAN LPAGLCSTLH PPMENKAEGT GVQLLTPDSW
     NIPLTDARRK APSPVATAGQ SQGPGPSAST TVSPSDTANC SVTKIPTPVP KSIPISETPN
     IPPVSVQPPA SIGPPLGVPP RSPPMVMTNR GPVPLPIFME QQIMQQIRPP FIRGPPHHAS
     NPNSPLSNPM LPGIGPPPGG PRNLGPTSSP MHRPMLSPHI HPPSTPTMPG NPPGLLPPPP
     PGAPLPSLPF PPVSMMPNGP MPVPQMMNFG LPSLAPLVPP PTLLVPYPVI VPLPVPIPIP
     IPIPHVSDSK PPNGFSSNGE NFIPNAPGDS AAAGGKPSGH SLSPRDSKQG SSKSADSPPG
     CSGQALSLAP TPAEHGRSEV VDLTRRAGSP PGPPGAGGQL GFPGVLQGPQ DGVIDLTVGH
     RARLHNVIHR ALHAHVKAER EPSAAERRTC GGCRDGHCSP PAAGDPGPGA PAGPEAAAAC
     NVIVNGTRGA AAEGAKSAEP PPEQPPPPPP PAPPKKLLSP EEPAVSELES VKENNCASNC
     HLDGEAAKKL MGEEALAGGD KSDPNLNNPA DEDHAYALRM LPKTGCVIQP VPKPAEKAAM
     APCIISSPML SAGPEDLEPP LKRRCLRIRN QNK
//
ID   ZN219_HUMAN             Reviewed;         722 AA.
AC   Q9P2Y4; D3DS16; Q53Y57; Q8IYC1; Q9BW28;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 2.
DT   11-NOV-2015, entry version 138.
DE   RecName: Full=Zinc finger protein 219;
GN   Name=ZNF219;
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], AND CHARACTERIZATION.
RC   TISSUE=Testis;
RX   PubMed=10819330; DOI=10.1093/dnares/7.2.137;
RA   Sakai T., Toyoda A., Hashimoto K., Maeda H.;
RT   "Isolation and characterization of a novel zinc finger gene, ZNF219,
RT   and mapping to the human chromosome 14q11 region.";
RL   DNA Res. 7:137-141(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT THR-260.
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   [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 [LARGE SCALE MRNA], AND VARIANT THR-260.
RC   TISSUE=Brain, and Kidney;
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   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA   Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA   Blagoev B.;
RT   "System-wide temporal characterization of the proteome and
RT   phosphoproteome of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
CC   -!- FUNCTION: May be involved in transcriptional regulation.
CC   -!- INTERACTION:
CC       P25800:LMO1; NbExp=3; IntAct=EBI-3937106, EBI-8639312;
CC       Q5I0X7:TTC32; NbExp=3; IntAct=EBI-3937106, EBI-8636434;
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- TISSUE SPECIFICITY: Ubiquitous.
CC   -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC       family. {ECO:0000305}.
CC   -!- SIMILARITY: Contains 6 C2H2-type zinc fingers.
CC       {ECO:0000255|PROSITE-ProRule:PRU00042}.
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DR   EMBL; AB015427; BAA90526.1; -; mRNA.
DR   EMBL; BT006956; AAP35602.1; -; mRNA.
DR   EMBL; CH471078; EAW66404.1; -; Genomic_DNA.
DR   EMBL; CH471078; EAW66405.1; -; Genomic_DNA.
DR   EMBL; CH471078; EAW66406.1; -; Genomic_DNA.
DR   EMBL; CH471078; EAW66407.1; -; Genomic_DNA.
DR   EMBL; BC000694; AAH00694.1; -; mRNA.
DR   EMBL; BC036105; AAH36105.1; -; mRNA.
DR   CCDS; CCDS9568.1; -.
DR   RefSeq; NP_001095142.1; NM_001101672.1.
DR   RefSeq; NP_001095924.1; NM_001102454.1.
DR   RefSeq; NP_057507.2; NM_016423.2.
DR   RefSeq; XP_006720226.1; XM_006720163.2.
DR   RefSeq; XP_006720227.1; XM_006720164.2.
DR   UniGene; Hs.250493; -.
DR   ProteinModelPortal; Q9P2Y4; -.
DR   SMR; Q9P2Y4; 57-210, 269-331, 393-429, 498-549, 635-675.
DR   BioGrid; 119387; 41.
DR   IntAct; Q9P2Y4; 10.
DR   MINT; MINT-8247371; -.
DR   STRING; 9606.ENSP00000354206; -.
DR   PhosphoSite; Q9P2Y4; -.
DR   BioMuta; ZNF219; -.
DR   DMDM; 55977885; -.
DR   MaxQB; Q9P2Y4; -.
DR   PaxDb; Q9P2Y4; -.
DR   PRIDE; Q9P2Y4; -.
DR   DNASU; 51222; -.
DR   Ensembl; ENST00000360947; ENSP00000354206; ENSG00000165804.
DR   Ensembl; ENST00000421093; ENSP00000392401; ENSG00000165804.
DR   Ensembl; ENST00000451119; ENSP00000388558; ENSG00000165804.
DR   GeneID; 51222; -.
DR   KEGG; hsa:51222; -.
DR   UCSC; uc001vzr.2; human.
DR   CTD; 51222; -.
DR   GeneCards; ZNF219; -.
DR   HGNC; HGNC:13011; ZNF219.
DR   HPA; HPA030761; -.
DR   HPA; HPA056168; -.
DR   MIM; 605036; gene.
DR   neXtProt; NX_Q9P2Y4; -.
DR   PharmGKB; PA37590; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   eggNOG; COG5048; LUCA.
DR   GeneTree; ENSGT00530000063100; -.
DR   HOGENOM; HOG000140857; -.
DR   HOVERGEN; HBG054187; -.
DR   InParanoid; Q9P2Y4; -.
DR   OMA; DASPPYA; -.
DR   OrthoDB; EOG7D59N5; -.
DR   PhylomeDB; Q9P2Y4; -.
DR   TreeFam; TF332241; -.
DR   ChiTaRS; ZNF219; human.
DR   GeneWiki; ZNF219; -.
DR   GenomeRNAi; 51222; -.
DR   NextBio; 54298; -.
DR   PRO; PR:Q9P2Y4; -.
DR   Proteomes; UP000005640; Chromosome 14.
DR   Bgee; Q9P2Y4; -.
DR   CleanEx; HS_ZNF219; -.
DR   ExpressionAtlas; Q9P2Y4; baseline and differential.
DR   Genevisible; Q9P2Y4; HS.
DR   GO; GO:0016021; C:integral component of membrane; IEA:InterPro.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR   GO; GO:0004969; F:histamine receptor activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000978; F:RNA polymerase II core promoter proximal region sequence-specific DNA binding; IDA:NTNU_SB.
DR   GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IDA:UniProtKB.
DR   GO; GO:0001078; F:transcriptional repressor activity, RNA polymerase II core promoter proximal region sequence-specific binding; IDA:NTNU_SB.
DR   GO; GO:0007275; P:multicellular organismal development; IBA:GO_Central.
DR   GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:NTNU_SB.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR   GO; GO:0001505; P:regulation of neurotransmitter levels; IEA:InterPro.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:UniProtKB.
DR   GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR   GO; GO:0006351; P:transcription, DNA-templated; IDA:UniProtKB.
DR   Gene3D; 3.30.160.60; -; 6.
DR   InterPro; IPR003980; Histamine_H3_rcpt.
DR   InterPro; IPR007087; Znf_C2H2.
DR   InterPro; IPR015880; Znf_C2H2-like.
DR   InterPro; IPR013087; Znf_C2H2/integrase_DNA-bd.
DR   PRINTS; PR01471; HISTAMINEH3R.
DR   SMART; SM00355; ZnF_C2H2; 9.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 5.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 6.
PE   1: Evidence at protein level;
KW   Complete proteome; DNA-binding; Metal-binding; Nucleus; Polymorphism;
KW   Reference proteome; Repeat; Transcription; Transcription regulation;
KW   Zinc; Zinc-finger.
FT   CHAIN         1    722       Zinc finger protein 219.
FT                                /FTId=PRO_0000047461.
FT   ZN_FING      57     79       C2H2-type 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING      85    107       C2H2-type 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     163    186       C2H2-type 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     274    296       C2H2-type 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     302    324       C2H2-type 5. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     498    520       C2H2-type 6. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   VARIANT     260    260       P -> T (in dbSNP:rs17853549).
FT                                {ECO:0000269|PubMed:15489334,
FT                                ECO:0000269|Ref.2}.
FT                                /FTId=VAR_067624.
FT   CONFLICT    232    233       Missing (in Ref. 4; AAH00694).
FT                                {ECO:0000305}.
FT   CONFLICT    436    436       E -> Q (in Ref. 1; BAA90526).
FT                                {ECO:0000305}.
SQ   SEQUENCE   722 AA;  76877 MW;  AB2B6B37904FC14B CRC64;
     MEGSRPRAPS GHLAPSPPAF DGELDLQRYS NGPAVSAGSL GMGAVSWSES RAGERRFPCP
     VCGKRFRFNS ILALHLRAHP GAQAFQCPHC GHRAAQRALL RSHLRTHQPE RPRSPAARLL
     LELEERALLR EARLGRARSS GGMQATPATE GLARPQAPSS SAFRCPYCKG KFRTSAERER
     HLHILHRPWK CGLCSFGSSQ EEELLHHSLT AHGAPERPLA ATSAAPPPQP QPQPPPQPEP
     RSVPQPEPEP EPEREATPTP APAAPEEPPA PPEFRCQVCG QSFTQSWFLK GHMRKHKASF
     DHACPVCGRC FKEPWFLKNH MKVHASKLGP LRAPGPASGP ARAPQPPDLG LLAYEPLGPA
     LLLAPAPTPA ERREPPSLLG YLSLRAGEGR PNGEGAEPGP GRSFGGFRPL SSALPARARR
     HRAEEPEEEE EVVEAEEETW ARGRSLGSLA SLHPRPGEGP GHSASAAGAQ ARSTATQEEN
     GLLVGGTRPE GGRGATGKDC PFCGKSFRSA HHLKVHLRVH TGERPYKCPH CDYAGTQSGS
     LKYHLQRHHR EQRSGAGPGP PPEPPPPSQR GSAPQSGAKP SPQPATWVEG ASSPRPPSSG
     AGPGSRRKPA SPGRTLRNGR GGEAEPLDLS LRAGPGGEAG PGGALHRCLF CPFATGAPEL
     MALHLQVHHS RRARGRRPPQ ADASPPYARV PSGETPPSPS QEGEEGSGLS RPGEAGLGGQ
     ER
//
#~~# #~+~~+~# #~~#
#LOG 00:00:00 Activity Log for SLiMSuite V1.5.2: Wed Dec 9 00:47:09 2015
#DIR 00:00:00 Run from directory: /srv/slimsuite/logs/prod
#ARG 00:00:00 Commandline arguments: run ip=122.150.74.70 qslimfinder&query=P03254&uniprotid=P0C7T5,P38398,O00257,Q12873,Q99708,Q13363,P35221,Q92769,Q14526,Q13422,P15884,Q92831,Q8N3X6,Q96JN0,Q13465,Q96MY1,P48552,Q15291,A7XYQ1,Q9P2Y4,Q8IX07,P03254&dismask=T&consmask=F&featuremask=F&ambiguity=T&slimlen=5&maxwild=2&jobid=15120900008
#VIO 00:00:00 Verbosity: -1; Interactivity: -1.
#PROG 00:00:00 QSLiMFinder V2.1.1: Query Short Linear Motif Finder
#CMD 00:00:00 Full QSLiMFinder 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=15120900008 rest=format query=P03254 uniprotid=P0C7T5,P38398,O00257,Q12873,Q99708,Q13363,P35221,Q92769,Q14526,Q13422,P15884,Q92831,Q8N3X6,Q96JN0,Q13465,Q96MY1,P48552,Q15291,A7XYQ1,Q9P2Y4,Q8IX07,P03254 dismask=T consmask=F featuremask=F ambiguity=T slimlen=5 maxwild=2 jobid=15120900008 resfile=qslimfinder.csv savespace=0 targz=F megaslim=seqin basefile=qslimfinder
#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=F interpreted as empty FTMask list.
#WARN 00:00:00 NOTE: cloudfix=F. Be wary of ambiguity over-predictions.
#URL 00:00:04 Extracting 22 AccNum from http://www.uniprot.org/uniprot/: 22 read & extracted; 0 failed; 0 duplicates.
#DAT 00:00:05 Extracting entries from qslimfinder.dat: 22 read, 22 extracted.
#SEQ 00:00:05 22 sequences loaded from /srv/slimsuite/scratch/prod/qslimfinder/15120900008/qslimfinder.dat (Format: uniprot).
#FAS 00:00:05 22 Sequences output to /srv/slimsuite/scratch/prod/qslimfinder/15120900008/qslimfinder.fas.
#UPC 00:00:05 No UPC file found.
#FAS 00:00:05 22 Sequences output to /srv/slimsuite/scratch/prod/qslimfinder/15120900008/qslimfinder.slimdb.
#DICT 00:00:05 Made "short" seqName dictionary: 22 seq; 22 keys.
#DB 00:00:05 /share/apps/blast+/2.2.29/bin/makeblastdb -in "/srv/slimsuite/scratch/prod/qslimfinder/15120900008/qslimfinder.slimdb" -out "/srv/slimsuite/scratch/prod/qslimfinder/15120900008/qslimfinder.slimdb" -title "/srv/slimsuite/scratch/prod/qslimfinder/15120900008/qslimfinder.slimdb" -parse_seqids -dbtype prot
#SYS 00:00:05 /share/apps/blast+/2.2.29/bin/blastp -query /srv/slimsuite/scratch/prod/qslimfinder/15120900008/qslimfinder.slimdb -db /srv/slimsuite/scratch/prod/qslimfinder/15120900008/qslimfinder.slimdb -out /srv/slimsuite/scratch/prod/qslimfinder/15120900008/qslimfinder.self.blast -seg yes -comp_based_stats F -soft_masking true -evalue 1.000000e-04 -num_descriptions 22 -num_alignments 22
#INDEX 00:00:05 Indexed "Search" on "Query": 22 unique; 0 missing entries
#CLUST 00:00:05 17 clusters generated from 22 keys (maxdis=1.00)
#DICT 00:00:05 Made "short" seqName dictionary: 22 seq; 22 keys.
#MST 00:00:05 MST for 22 sequences = 20.594.
#UP 00:00:05 qslimfinder: 22 Seq; 17 UPC; 20.594 MST; blaste=1.00e-04, blastcf=F, blastf=T
#MAT 00:00:05 qslimfinder GABLAM Distance matrix out to /srv/slimsuite/scratch/prod/qslimfinder/15120900008/qslimfinder.dis.tdt (text format).
#QRY 00:00:05 Query Sequence = E1A_ADE02__P03254 (289 AA).
#QRY 00:00:05 1 sequences mapped to focal group "Query"
#FOCUS 00:00:05 Mapped 1 focal sequences in 1 group(s)
#MIN 00:00:05 AmbOcc 0.05 & 17 UP => AmbOcc 2 UPC.
#MIN 00:00:05 MinOcc 0.05 & 17 UP => MinOcc 3 UPC.
#DIS 00:00:05 Disorder score file: /srv/slimsuite/scratch/prod/qslimfinder/15120900008/qslimfinder.iupred.txt
#MASK 00:00:05 ATX1L_HUMAN__P0C7T5 masked 21 ordered regions. (107 X added.)
#MASK 00:00:05 BRCA1_HUMAN__P38398 masked 20 ordered regions. (268 X added.)
#MASK 00:00:05 CBX4_HUMAN__O00257 masked 3 ordered regions. (54 X added.)
#MASK 00:00:05 CHD3_HUMAN__Q12873 masked 58 ordered regions. (747 X added.)
#MASK 00:00:05 COM1_HUMAN__Q99708 masked 14 ordered regions. (46 X added.)
#MASK 00:00:05 CTBP1_HUMAN__Q13363 masked 13 ordered regions. (221 X added.)
#MASK 00:00:05 CTNA1_HUMAN__P35221 masked 33 ordered regions. (329 X added.)
#MASK 00:00:05 E1A_ADE02__P03254 masked 7 ordered regions. (54 X added.)
#MASK 00:00:05 FOG1_HUMAN__Q8IX07 masked 15 ordered regions. (245 X added.)
#MASK 00:00:05 HDAC2_HUMAN__Q92769 masked 18 ordered regions. (240 X added.)
#MASK 00:00:05 HIC1_HUMAN__Q14526 masked 22 ordered regions. (221 X added.)
#MASK 00:00:05 IKZF1_HUMAN__Q13422 masked 8 ordered regions. (110 X added.)
#MASK 00:00:05 ITF2_HUMAN__P15884 masked 3 ordered regions. (30 X added.)
#MASK 00:00:05 KAT2B_HUMAN__Q92831 masked 24 ordered regions. (408 X added.)
#MASK 00:00:05 LCORL_HUMAN__Q8N3X6 masked 22 ordered regions. (117 X added.)
#MASK 00:00:05 LCOR_HUMAN__Q96JN0 masked 7 ordered regions. (17 X added.)
#MASK 00:00:05 MDS1_HUMAN__Q13465 masked 3 ordered regions. (35 X added.)
#MASK 00:00:05 NOL4L_HUMAN__Q96MY1 masked 2 ordered regions. (27 X added.)
#MASK 00:00:05 NRIP1_HUMAN__P48552 masked 10 ordered regions. (26 X added.)
#MASK 00:00:05 RBBP5_HUMAN__Q15291 masked 14 ordered regions. (234 X added.)
#MASK 00:00:05 SOBP_HUMAN__A7XYQ1 masked 7 ordered regions. (143 X added.)
#MASK 00:00:05 ZN219_HUMAN__Q9P2Y4 masked 15 ordered regions. (96 X added.)
#FTMASK 00:00:05 FTMask: None
#MASK 00:00:05 Masked ATX1L_HUMAN__P0C7T5 "low complexity" regions. (9 X added.)
#MASK 00:00:05 Masked BRCA1_HUMAN__P38398 "low complexity" regions. (6 X added.)
#MASK 00:00:05 Masked CBX4_HUMAN__O00257 "low complexity" regions. (21 X added.)
#MASK 00:00:05 Masked CHD3_HUMAN__Q12873 "low complexity" regions. (36 X added.)
#MASK 00:00:05 Masked COM1_HUMAN__Q99708 "low complexity" regions. (3 X added.)
#MASK 00:00:05 Masked CTNA1_HUMAN__P35221 "low complexity" regions. (3 X added.)
#MASK 00:00:05 Masked E1A_ADE02__P03254 "low complexity" regions. (3 X added.)
#MASK 00:00:05 Masked FOG1_HUMAN__Q8IX07 "low complexity" regions. (34 X added.)
#MASK 00:00:05 Masked HIC1_HUMAN__Q14526 "low complexity" regions. (33 X added.)
#MASK 00:00:05 Masked ITF2_HUMAN__P15884 "low complexity" regions. (10 X added.)
#MASK 00:00:05 Masked KAT2B_HUMAN__Q92831 "low complexity" regions. (19 X added.)
#MASK 00:00:05 Masked LCORL_HUMAN__Q8N3X6 "low complexity" regions. (9 X added.)
#MASK 00:00:05 Masked NOL4L_HUMAN__Q96MY1 "low complexity" regions. (14 X added.)
#MASK 00:00:05 Masked NRIP1_HUMAN__P48552 "low complexity" regions. (6 X added.)
#MASK 00:00:05 Masked RBBP5_HUMAN__Q15291 "low complexity" regions. (3 X added.)
#MASK 00:00:05 Masked SOBP_HUMAN__A7XYQ1 "low complexity" regions. (23 X added.)
#MASK 00:00:05 Masked ZN219_HUMAN__Q9P2Y4 "low complexity" regions. (35 X added.)
#MASK 00:00:05 MetMask: 22 N-terminal Ms masked
#MASK 00:00:05 Masked HDAC2_HUMAN__Q92769 position-specific AAs. (1 X added.)
#MASK 00:00:05 Masked SOBP_HUMAN__A7XYQ1 position-specific AAs. (1 X added.)
#MASK 00:00:05 qslimfinder: Masking of input sequences complete.
#SPACE 00:00:05 Motif Space, 2 positions: 1,200 motifs
#SPACE 00:00:05 Motif Space, 3 positions: 72,000 motifs
#SPACE 00:00:05 Motif Space, 4 positions: 4,320,000 motifs
#SPACE 00:00:05 Motif Space, 5 positions: 259,200,000 motifs
#DIM 00:00:05 Read dimers from 22 seq: 1,246 dimers -> 407 Query dimers.
#DIM 00:00:05 Reducing dimers: 1,183 >= 2 of 17 UPC
#SPACE 00:00:05 Query Motif Space, 2 positions: 1,200 motifs -> 407 Query motifs
#SLIM 00:00:05 Selecting 2aa SLiMs: 1,183 >= 2 of 17 UPC -> 405 of 407 query motifs
#AMB 00:00:05 Adding Wildcard ambiguity: 100.0% (0 amb motifs)
#AMB 00:00:05 Adding Degeneracy ambiguity: 100.0% (0 amb motifs)
#SLIM 00:00:48 Extending 3aa SLiMs >= 2 of 17 UPC: 22,154 SLiMs
#SPACE 00:00:48 Exact Query Motif Space, 3 positions: 72,000 motifs -> 1,703 Query motifs
#AMB 00:00:49 Adding Wildcard ambiguity: 100.0% (1,026 amb motifs)
#AMB 00:00:51 Adding Degeneracy ambiguity: 100.0% (1,794 amb motifs)
#SLIM 00:03:11 Extending 4aa SLiMs >= 2 of 17 UPC: 23,594 SLiMs
#SPACE 00:03:12 Exact Query Motif Space, 4 positions: 4,320,000 motifs -> 5,089 Query motifs
#AMB 00:03:13 Adding Wildcard ambiguity: 100.0% (595 amb motifs)
#AMB 00:03:14 Adding Degeneracy ambiguity: 100.0% (661 amb motifs)
#SLIM 00:05:01 Extending 5aa SLiMs >= 2 of 17 UPC: 6,180 SLiMs
#SPACE 00:05:06 Exact Query Motif Space, 5 positions: 259,200,000 motifs -> 14,667 Query motifs
#AMB 00:05:06 Adding Wildcard ambiguity: 100.0% (64 amb motifs)
#AMB 00:05:06 Adding Degeneracy ambiguity: 100.0% (12 amb motifs)
#SLIM 00:05:06 57,263 SLiMs >= 2 of 17 UPC
#SAVE 00:05:11 QSLiMFinder Intermediate saved as /srv/slimsuite/scratch/prod/qslimfinder/15120900008/qslimfinder.Ql5w2o2a3.FreqDisComp-5-8.pickle (Python pickle).
#GZIP 00:05:12 /srv/slimsuite/scratch/prod/qslimfinder/15120900008/qslimfinder.Ql5w2o2a3.FreqDisComp-5-8.pickle zipped.
#SLIM 00:05:13 Filtering 57,263 SLiMs: 5,088 retained.
#PROB 00:05:15 Calculating [QSig] SLiM Probabilities (Sig<=0.10) complete: 6 ranked SLiMs.
#COMB 00:05:16 Combined Occurrence Attributes complete.
#CLOUD 00:05:16 Making "Motif Clouds" for 6 Sig Motifs: 1 Clouds
#SLIM 00:05:16 Cloud 1 (P.DLS.[KR]|P[IL]DL|[IL]DLS.[KR]|P.DLS.K|P.DL[ST]|P[IL]DLS) SLiMMaker: P[IL]DL[ST]
#FREQ 00:05:16 SLiMMaker SLiM matches 7 of 16 sequences (43.8%).
#RANK 00:05:16 Rank calculations complete
#CLOUD 00:05:16 Motif cloud data output to /srv/slimsuite/scratch/prod/qslimfinder/15120900008/qslimfinder.Ql5w2o2a3.15120900008.cloud.txt for 1 clouds.
#FAS 00:05:16 22 Sequences output to /srv/slimsuite/scratch/prod/qslimfinder/15120900008/qslimfinder.Ql5w2o2a3.15120900008.masked.fas.
#FAS 00:05:16 66 Sequences output to /srv/slimsuite/scratch/prod/qslimfinder/15120900008/qslimfinder.Ql5w2o2a3.15120900008.mapping.fas.
#ALN 00:05:17 Constructing motif alignments: 6 motifs & 13 seqs.: 100.0%.
#FAS 00:05:17 15 Sequences output to /srv/slimsuite/scratch/prod/qslimfinder/15120900008/qslimfinder.Ql5w2o2a3.15120900008.motifaln.fas.
#ALN 00:05:17 Constructing motif alignments: 6 motifs & 13 seqs.: 100.0%.
#FAS 00:05:17 15 Sequences output to /srv/slimsuite/scratch/prod/qslimfinder/15120900008/qslimfinder.Ql5w2o2a3.15120900008.maskaln.fas.
#OCC 00:05:17 Occurrence data output for 43 motif occurrences.
#RES 00:05:17 QSLiMFinder results output to /srv/slimsuite/scratch/prod/qslimfinder/15120900008/qslimfinder.csv and /srv/slimsuite/scratch/prod/qslimfinder/15120900008/qslimfinder.occ.csv.
#RES 00:05:17 Additional dataset results output to /srv/slimsuite/scratch/prod/qslimfinder/15120900008/qslimfinder*
#WARN 00:05:17 2 warning messages: check log for details.
#LOG 00:05:17 QSLiMFinder V2.1.1 End: Wed Dec 9 00:52:27 2015
#JOBID 00:05:17 15120900008
#REST 00:05:17 URL for future retrieval: http://rest.slimsuite.unsw.edu.au/retrieve&jobid=15120900008&rest=format&password=None
#WARN	00:00:00	Command ftmask=F interpreted as empty FTMask list.
#WARN	00:00:00	NOTE: cloudfix=F. Be wary of ambiguity over-predictions.

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