BRD7_HUMAN
ID BRD7_HUMAN Reviewed; 651 AA.
AC Q9NPI1; Q4VC09; Q8N2L9; Q96KA4; Q9BV48; Q9UH59;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Bromodomain-containing protein 7;
DE AltName: Full=75 kDa bromodomain protein;
DE AltName: Full=Protein CELTIX-1;
GN Name=BRD7; Synonyms=BP75, CELTIX1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), INTERACTION WITH IRF2, AND
RP SUBCELLULAR LOCATION.
RC TISSUE=Cervix carcinoma;
RX PubMed=11025449;
RX DOI=10.1002/1097-4652(200011)185:2<269::aid-jcp12>3.0.co;2-l;
RA Staal A., Enserink J.M., Stein J.L., Stein G.S., van Wijnen A.J.;
RT "Molecular characterization of celtix-1, a bromodomain protein interacting
RT with the transcription factor interferon regulatory factor 2.";
RL J. Cell. Physiol. 185:269-279(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH HNRPUL1, AND
RP ASSOCIATION WITH HISTONES AND HNRPUL1.
RC TISSUE=Fetal brain;
RX PubMed=12489984; DOI=10.1042/bj20021281;
RA Kzhyshkowska J.G., Rusch A., Wolf H., Dobner T.;
RT "Regulation of transcription by the heterogeneous nuclear ribonucleoprotein
RT E1B-AP5 is mediated by complex formation with the novel bromodomain-
RT containing protein BRD7.";
RL Biochem. J. 371:385-393(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Yu Y., Li G.Y.;
RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
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., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., 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., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 198-651 (ISOFORM 2).
RC TISSUE=Brain, and 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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 236-651 (ISOFORM 1).
RC TISSUE=Embryo;
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., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., 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., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-279, AND IDENTIFICATION BY
RP 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., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH ACETYLATED HISTONE H3.
RX PubMed=16265664; DOI=10.1002/jcb.20645;
RA Peng C., Zhou J., Liu H.Y., Zhou M., Wang L.L., Zhang Q.H., Yang Y.X.,
RA Xiong W., Shen S.R., Li X.L., Li G.Y.;
RT "The transcriptional regulation role of BRD7 by binding to acetylated
RT histone through bromodomain.";
RL J. Cell. Biochem. 97:882-892(2006).
RN [9]
RP FUNCTION, NUCLEAR LOCALIZATION SIGNAL, AND SUBCELLULAR LOCATION.
RX PubMed=16475162; DOI=10.1002/jcb.20788;
RA Zhou M., Liu H., Xu X., Zhou H., Li X., Peng C., Shen S., Xiong W., Ma J.,
RA Zeng Z., Fang S., Nie X., Yang Y., Zhou J., Xiang J., Cao L., Peng S.,
RA Li S., Li G.;
RT "Identification of nuclear localization signal that governs nuclear import
RT of BRD7 and its essential roles in inhibiting cell cycle progression.";
RL J. Cell. Biochem. 98:920-930(2006).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=T-cell;
RX PubMed=19367720; DOI=10.1021/pr800500r;
RA Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
RT "Phosphorylation analysis of primary human T lymphocytes using sequential
RT IMAC and titanium oxide enrichment.";
RL J. Proteome Res. 7:5167-5176(2008).
RN [11]
RP FUNCTION, PROMOTER BINDING, AND INTERACTION WITH BRCA1.
RX PubMed=20215511; DOI=10.1158/0008-5472.can-09-2089;
RA Harte M.T., O'Brien G.J., Ryan N.M., Gorski J.J., Savage K.I.,
RA Crawford N.T., Mullan P.B., Harkin D.P.;
RT "BRD7, a subunit of SWI/SNF complexes, binds directly to BRCA1 and
RT regulates BRCA1-dependent transcription.";
RL Cancer Res. 70:2538-2547(2010).
RN [12]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH TP53 AND EP300.
RX PubMed=20228809; DOI=10.1038/ncb2038;
RA Drost J., Mantovani F., Tocco F., Elkon R., Comel A., Holstege H.,
RA Kerkhoven R., Jonkers J., Voorhoeve P.M., Agami R., Del Sal G.;
RT "BRD7 is a candidate tumour suppressor gene required for p53 function.";
RL Nat. Cell Biol. 12:380-389(2010).
RN [13]
RP FUNCTION, AND INTERACTION WITH TP53.
RX PubMed=20660729; DOI=10.1073/pnas.1009559107;
RA Burrows A.E., Smogorzewska A., Elledge S.J.;
RT "Polybromo-associated BRG1-associated factor components BRD7 and BAF180 are
RT critical regulators of p53 required for induction of replicative
RT senescence.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:14280-14285(2010).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-279, AND IDENTIFICATION BY
RP 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., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-279, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-279; SER-289; SER-380 AND
RP THR-514, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-621, AND IDENTIFICATION BY
RP 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., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [18]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-21; LYS-127 AND LYS-305, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25755297; DOI=10.1074/mcp.o114.044792;
RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
RA Vertegaal A.C.;
RT "System-wide analysis of SUMOylation dynamics in response to replication
RT stress reveals novel small ubiquitin-like modified target proteins and
RT acceptor lysines relevant for genome stability.";
RL Mol. Cell. Proteomics 14:1419-1434(2015).
RN [19]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-21; LYS-52; LYS-127; LYS-186;
RP LYS-197; LYS-201; LYS-212; LYS-241; LYS-305; LYS-307; LYS-344 AND LYS-389,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [20]
RP STRUCTURE BY NMR OF 129-236, AND INTERACTION WITH ACETYLATED HISTONE
RP PEPTIDES.
RX PubMed=17498659; DOI=10.1016/j.bbrc.2007.04.139;
RA Sun H., Liu J., Zhang J., Shen W., Huang H., Xu C., Dai H., Wu J., Shi Y.;
RT "Solution structure of BRD7 bromodomain and its interaction with acetylated
RT peptides from histone H3 and H4.";
RL Biochem. Biophys. Res. Commun. 358:435-441(2007).
CC -!- FUNCTION: Acts both as coactivator and as corepressor. May play a role
CC in chromatin remodeling. Activator of the Wnt signaling pathway in a
CC DVL1-dependent manner by negatively regulating the GSK3B
CC phosphotransferase activity. Induces dephosphorylation of GSK3B at
CC 'Tyr-216'. Down-regulates TRIM24-mediated activation of transcriptional
CC activation by AR (By similarity). Transcriptional corepressor that
CC down-regulates the expression of target genes. Binds to target
CC promoters, leading to increased histone H3 acetylation at 'Lys-9'
CC (H3K9ac). Binds to the ESR1 promoter. Recruits BRCA1 and POU2F1 to the
CC ESR1 promoter. Coactivator for TP53-mediated activation of
CC transcription of a set of target genes. Required for TP53-mediated
CC cell-cycle arrest in response to oncogene activation. Promotes
CC acetylation of TP53 at 'Lys-382', and thereby promotes efficient
CC recruitment of TP53 to target promoters. Inhibits cell cycle
CC progression from G1 to S phase. {ECO:0000250,
CC ECO:0000269|PubMed:16265664, ECO:0000269|PubMed:16475162,
CC ECO:0000269|PubMed:20215511, ECO:0000269|PubMed:20228809,
CC ECO:0000269|PubMed:20660729}.
CC -!- SUBUNIT: Interacts with TRIM24, PTPN13 and DVL1. Identified in a
CC complex with SMARCA4/BRG1, SMARCC1/BAF155, SMARCE1/BAF57, DPF2/BAF45D
CC and ARID2, subunits of the SWI/SNF-B (PBAF) chromatin remodeling
CC complex (By similarity). Interacts with IRF2 and HNRPUL1. Interacts
CC (via N-terminus) with TP53. Interacts (via C-terminus) with EP300.
CC Interacts with BRCA1. Interacts (via bromo domain) with histone H3 (via
CC N-terminus) acetylated at 'Lys-14' (H3K14ac). Has low affinity for
CC histone H3 acetylated at 'Lys-9' (H3K9ac). Has the highest affinity for
CC histone H3 that is acetylated both at 'Lys-9' (H3K9ac) and at 'Lys-14'
CC (H3K14ac). Has very low affinity for non-acetylated histone H3.
CC Interacts (via bromo domain) with histone H4 (via N-terminus)
CC acetylated at 'Lys-8' (H3K8ac) (in vitro). {ECO:0000250,
CC ECO:0000269|PubMed:11025449, ECO:0000269|PubMed:12489984,
CC ECO:0000269|PubMed:16265664, ECO:0000269|PubMed:17498659,
CC ECO:0000269|PubMed:20215511, ECO:0000269|PubMed:20228809,
CC ECO:0000269|PubMed:20660729}.
CC -!- INTERACTION:
CC Q9NPI1; Q09472: EP300; NbExp=3; IntAct=EBI-711221, EBI-447295;
CC Q9NPI1; Q9BUJ2: HNRNPUL1; NbExp=5; IntAct=EBI-711221, EBI-1018153;
CC Q9NPI1; Q9H8W4: PLEKHF2; NbExp=3; IntAct=EBI-711221, EBI-742388;
CC Q9NPI1; P04637: TP53; NbExp=9; IntAct=EBI-711221, EBI-366083;
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9NPI1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NPI1-2; Sequence=VSP_017564;
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH01611.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB55031.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC11089.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF213969; AAF19526.1; -; mRNA.
DR EMBL; AJ271881; CAB72445.1; -; mRNA.
DR EMBL; AF152604; AAF75126.1; -; mRNA.
DR EMBL; BC001611; AAH01611.1; ALT_INIT; mRNA.
DR EMBL; AC007493; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC007597; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC023826; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC050728; AAH50728.1; -; mRNA.
DR EMBL; BC094706; AAH94706.1; -; mRNA.
DR EMBL; AK027308; BAB55031.1; ALT_INIT; mRNA.
DR EMBL; AK074613; BAC11089.1; ALT_INIT; mRNA.
DR CCDS; CCDS10742.1; -. [Q9NPI1-1]
DR CCDS; CCDS54007.1; -. [Q9NPI1-2]
DR RefSeq; NP_001167455.1; NM_001173984.2. [Q9NPI1-2]
DR RefSeq; NP_037395.2; NM_013263.4. [Q9NPI1-1]
DR PDB; 2I7K; NMR; -; A=129-236.
DR PDB; 5MQ1; X-ray; 1.50 A; A=128-239.
DR PDB; 6PPA; X-ray; 1.77 A; A=130-250.
DR PDB; 6V0Q; X-ray; 1.69 A; A/B/C/D=130-250.
DR PDB; 6V16; X-ray; 1.90 A; A/B=130-250.
DR PDB; 6V17; X-ray; 2.05 A; A/B=130-250.
DR PDB; 6V1E; X-ray; 2.30 A; A=129-250.
DR PDB; 6V1F; X-ray; 2.00 A; A=129-250.
DR PDB; 6V1H; X-ray; 1.93 A; A=129-250.
DR PDBsum; 2I7K; -.
DR PDBsum; 5MQ1; -.
DR PDBsum; 6PPA; -.
DR PDBsum; 6V0Q; -.
DR PDBsum; 6V16; -.
DR PDBsum; 6V17; -.
DR PDBsum; 6V1E; -.
DR PDBsum; 6V1F; -.
DR PDBsum; 6V1H; -.
DR AlphaFoldDB; Q9NPI1; -.
DR BMRB; Q9NPI1; -.
DR SMR; Q9NPI1; -.
DR BioGRID; 118883; 609.
DR ComplexPortal; CPX-1196; Polybromo-associated SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B variant.
DR ComplexPortal; CPX-1199; Polybromo-associated SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A variant.
DR CORUM; Q9NPI1; -.
DR DIP; DIP-32509N; -.
DR IntAct; Q9NPI1; 85.
DR MINT; Q9NPI1; -.
DR STRING; 9606.ENSP00000378181; -.
DR BindingDB; Q9NPI1; -.
DR ChEMBL; CHEMBL3085622; -.
DR GuidetoPHARMACOLOGY; 2726; -.
DR GlyGen; Q9NPI1; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9NPI1; -.
DR MetOSite; Q9NPI1; -.
DR PhosphoSitePlus; Q9NPI1; -.
DR BioMuta; BRD7; -.
DR DMDM; 74734307; -.
DR EPD; Q9NPI1; -.
DR jPOST; Q9NPI1; -.
DR MassIVE; Q9NPI1; -.
DR MaxQB; Q9NPI1; -.
DR PaxDb; Q9NPI1; -.
DR PeptideAtlas; Q9NPI1; -.
DR PRIDE; Q9NPI1; -.
DR ProteomicsDB; 82017; -. [Q9NPI1-1]
DR ProteomicsDB; 82018; -. [Q9NPI1-2]
DR ABCD; Q9NPI1; 1 sequenced antibody.
DR Antibodypedia; 14527; 231 antibodies from 32 providers.
DR DNASU; 29117; -.
DR Ensembl; ENST00000394688.8; ENSP00000378180.3; ENSG00000166164.16. [Q9NPI1-1]
DR Ensembl; ENST00000394689.2; ENSP00000378181.2; ENSG00000166164.16. [Q9NPI1-2]
DR GeneID; 29117; -.
DR KEGG; hsa:29117; -.
DR MANE-Select; ENST00000394688.8; ENSP00000378180.3; NM_013263.5; NP_037395.2.
DR UCSC; uc002ege.3; human. [Q9NPI1-1]
DR CTD; 29117; -.
DR DisGeNET; 29117; -.
DR GeneCards; BRD7; -.
DR HGNC; HGNC:14310; BRD7.
DR HPA; ENSG00000166164; Low tissue specificity.
DR MIM; 618489; gene.
DR neXtProt; NX_Q9NPI1; -.
DR OpenTargets; ENSG00000166164; -.
DR PharmGKB; PA25417; -.
DR VEuPathDB; HostDB:ENSG00000166164; -.
DR eggNOG; KOG1828; Eukaryota.
DR GeneTree; ENSGT00950000183170; -.
DR HOGENOM; CLU_020704_0_1_1; -.
DR InParanoid; Q9NPI1; -.
DR OMA; PADDNSI; -.
DR OrthoDB; 439339at2759; -.
DR PhylomeDB; Q9NPI1; -.
DR TreeFam; TF106439; -.
DR PathwayCommons; Q9NPI1; -.
DR Reactome; R-HSA-6804758; Regulation of TP53 Activity through Acetylation.
DR SignaLink; Q9NPI1; -.
DR SIGNOR; Q9NPI1; -.
DR BioGRID-ORCS; 29117; 94 hits in 1084 CRISPR screens.
DR ChiTaRS; BRD7; human.
DR EvolutionaryTrace; Q9NPI1; -.
DR GeneWiki; BRD7; -.
DR GenomeRNAi; 29117; -.
DR Pharos; Q9NPI1; Tchem.
DR PRO; PR:Q9NPI1; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q9NPI1; protein.
DR Bgee; ENSG00000166164; Expressed in sural nerve and 148 other tissues.
DR ExpressionAtlas; Q9NPI1; baseline and differential.
DR Genevisible; Q9NPI1; HS.
DR GO; GO:0000785; C:chromatin; IC:ComplexPortal.
DR GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0000776; C:kinetochore; IC:ComplexPortal.
DR GO; GO:0016363; C:nuclear matrix; IC:ComplexPortal.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0016586; C:RSC-type complex; IC:ComplexPortal.
DR GO; GO:0042393; F:histone binding; IDA:MGI.
DR GO; GO:0070577; F:lysine-acetylated histone binding; IDA:UniProtKB.
DR GO; GO:0002039; F:p53 binding; IPI:UniProtKB.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:UniProtKB.
DR GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB.
DR GO; GO:0003714; F:transcription corepressor activity; IDA:UniProtKB.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0006338; P:chromatin remodeling; IC:ComplexPortal.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IDA:UniProtKB.
DR GO; GO:2000134; P:negative regulation of G1/S transition of mitotic cell cycle; IDA:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0045597; P:positive regulation of cell differentiation; IC:ComplexPortal.
DR GO; GO:2000781; P:positive regulation of double-strand break repair; IC:ComplexPortal.
DR GO; GO:0035066; P:positive regulation of histone acetylation; IDA:UniProtKB.
DR GO; GO:0045663; P:positive regulation of myoblast differentiation; IC:ComplexPortal.
DR GO; GO:0045582; P:positive regulation of T cell differentiation; IC:ComplexPortal.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0070316; P:regulation of G0 to G1 transition; IC:ComplexPortal.
DR GO; GO:2000045; P:regulation of G1/S transition of mitotic cell cycle; IC:ComplexPortal.
DR GO; GO:0030071; P:regulation of mitotic metaphase/anaphase transition; IC:ComplexPortal.
DR GO; GO:2000819; P:regulation of nucleotide-excision repair; IC:ComplexPortal.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR Gene3D; 1.20.920.10; -; 1.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR021900; DUF3512.
DR Pfam; PF00439; Bromodomain; 1.
DR Pfam; PF12024; DUF3512; 1.
DR PRINTS; PR00503; BROMODOMAIN.
DR SMART; SM00297; BROMO; 1.
DR SUPFAM; SSF47370; SSF47370; 1.
DR PROSITE; PS50014; BROMODOMAIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Bromodomain; Cell cycle;
KW Coiled coil; Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation; Tumor suppressor; Ubl conjugation;
KW Wnt signaling pathway.
FT CHAIN 1..651
FT /note="Bromodomain-containing protein 7"
FT /id="PRO_0000227664"
FT DOMAIN 148..218
FT /note="Bromo"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT REGION 35..132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 253..301
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 536..567
FT /evidence="ECO:0000255"
FT MOTIF 65..96
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000269|PubMed:16475162"
FT COMPBIAS 90..109
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 270..301
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 279
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 289
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 328
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O88665"
FT MOD_RES 380
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 482
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O88665"
FT MOD_RES 514
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 621
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT CROSSLNK 21
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 52
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 127
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 186
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 197
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 201
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 212
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 241
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 305
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 307
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 344
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 389
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 500
FT /note="E -> EQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11025449,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_017564"
FT CONFLICT 66
FT /note="R -> G (in Ref. 1; AAF19526)"
FT /evidence="ECO:0000305"
FT CONFLICT 83
FT /note="R -> T (in Ref. 1; AAF19526)"
FT /evidence="ECO:0000305"
FT CONFLICT 96
FT /note="R -> Q (in Ref. 1; AAF19526)"
FT /evidence="ECO:0000305"
FT CONFLICT 170
FT /note="M -> I (in Ref. 5; AAH94706)"
FT /evidence="ECO:0000305"
FT CONFLICT 485
FT /note="E -> G (in Ref. 6; BAB55031)"
FT /evidence="ECO:0000305"
FT HELIX 135..149
FT /evidence="ECO:0007829|PDB:5MQ1"
FT HELIX 152..154
FT /evidence="ECO:0007829|PDB:2I7K"
FT STRAND 155..158
FT /evidence="ECO:0007829|PDB:5MQ1"
FT TURN 162..164
FT /evidence="ECO:0007829|PDB:5MQ1"
FT STRAND 165..167
FT /evidence="ECO:0007829|PDB:2I7K"
FT HELIX 168..171
FT /evidence="ECO:0007829|PDB:5MQ1"
FT HELIX 178..186
FT /evidence="ECO:0007829|PDB:5MQ1"
FT HELIX 193..210
FT /evidence="ECO:0007829|PDB:5MQ1"
FT HELIX 216..232
FT /evidence="ECO:0007829|PDB:5MQ1"
FT HELIX 234..246
FT /evidence="ECO:0007829|PDB:6V0Q"
SQ SEQUENCE 651 AA; 74139 MW; 29B7947644C215E7 CRC64;
MGKKHKKHKS DKHLYEEYVE KPLKLVLKVG GNEVTELSTG SSGHDSSLFE DKNDHDKHKD
RKRKKRKKGE KQIPGEEKGR KRRRVKEDKK KRDRDRVENE AEKDLQCHAP VRLDLPPEKP
LTSSLAKQEE VEQTPLQEAL NQLMRQLQRK DPSAFFSFPV TDFIAPGYSM IIKHPMDFST
MKEKIKNNDY QSIEELKDNF KLMCTNAMIY NKPETIYYKA AKKLLHSGMK ILSQERIQSL
KQSIDFMADL QKTRKQKDGT DTSQSGEDGG CWQREREDSG DAEAHAFKSP SKENKKKDKD
MLEDKFKSNN LEREQEQLDR IVKESGGKLT RRLVNSQCEF ERRKPDGTTT LGLLHPVDPI
VGEPGYCPVR LGMTTGRLQS GVNTLQGFKE DKRNKVTPVL YLNYGPYSSY APHYDSTFAN
ISKDDSDLIY STYGEDSDLP SDFSIHEFLA TCQDYPYVMA DSLLDVLTKG GHSRTLQEME
MSLPEDEGHT RTLDTAKEME ITEVEPPGRL DSSTQDRLIA LKAVTNFGVP VEVFDSEEAE
IFQKKLDETT RLLRELQEAQ NERLSTRPPP NMICLLGPSY REMHLAEQVT NNLKELAQQV
TPGDIVSTYG VRKAMGISIP SPVMENNFVD LTEDTEEPKK TDVAECGPGG S
