BRD1_HUMAN
ID BRD1_HUMAN Reviewed; 1058 AA.
AC O95696; A6ZJA4;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=Bromodomain-containing protein 1 {ECO:0000303|PubMed:16387653};
DE AltName: Full=BR140-like protein {ECO:0000303|PubMed:10602503};
DE AltName: Full=Bromodomain and PHD finger-containing protein 2 {ECO:0000303|PubMed:16387653};
GN Name=BRD1 {ECO:0000303|PubMed:16387653, ECO:0000312|HGNC:HGNC:1102};
GN Synonyms=BRL {ECO:0000303|PubMed:10602503},
GN BRPF2 {ECO:0000303|PubMed:16387653};
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 [GENOMIC DNA / MRNA] (ISOFORM 1), AND TISSUE
RP SPECIFICITY.
RX PubMed=10602503; DOI=10.1038/sj.onc.1203117;
RA McCullagh P., Chaplin T., Meerabux J., Grenzelias D., Lillington D.,
RA Poulsom R., Gregorini A., Saha V., Young B.D.;
RT "The cloning, mapping and expression of a novel gene, BRL, related to the
RT AF10 leukaemia gene.";
RL Oncogene 18:7442-7452(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
RA Beare D.M., Dunham I.;
RT "A genome annotation-driven approach to cloning the human ORFeome.";
RL Genome Biol. 5:R84.1-R84.11(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [7]
RP FUNCTION, AND IDENTIFICATION IN THE MOZ/MORF COMPLEX.
RX PubMed=16387653; DOI=10.1016/j.molcel.2005.12.007;
RA Doyon Y., Cayrou C., Ullah M., Landry A.-J., Cote V., Selleck W.,
RA Lane W.S., Tan S., Yang X.-J., Cote J.;
RT "ING tumor suppressor proteins are critical regulators of chromatin
RT acetylation required for genome expression and perpetuation.";
RL Mol. Cell 21:51-64(2006).
RN [8]
RP IDENTIFICATION IN THE MOZ/MORF COMPLEX.
RX PubMed=18794358; DOI=10.1128/mcb.01297-08;
RA Ullah M., Pelletier N., Xiao L., Zhao S.P., Wang K., Degerny C.,
RA Tahmasebi S., Cayrou C., Doyon Y., Goh S.-L., Champagne N., Cote J.,
RA Yang X.-J.;
RT "Molecular architecture of quartet MOZ/MORF histone acetyltransferase
RT complexes.";
RL Mol. Cell. Biol. 28:6828-6843(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1055, AND IDENTIFICATION BY
RP 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1055, AND IDENTIFICATION BY
RP 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 [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-368; LYS-516; LYS-519 AND
RP LYS-903, AND IDENTIFICATION BY 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., Walther T.C.,
RA 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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1052 AND SER-1055, 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., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [13] {ECO:0007744|PDB:6MAJ, ECO:0007744|PDB:6MAK}
RP FUNCTION, IDENTIFICATION IN THE HBO1 COMPLEX, AND SUBCELLULAR LOCATION.
RX PubMed=21753189; DOI=10.1182/blood-2011-01-331892;
RA Mishima Y., Miyagi S., Saraya A., Negishi M., Endoh M., Endo T.A.,
RA Toyoda T., Shinga J., Katsumoto T., Chiba T., Yamaguchi N., Kitabayashi I.,
RA Koseki H., Iwama A.;
RT "The Hbo1-Brd1/Brpf2 complex is responsible for global acetylation of H3K14
RT and required for fetal liver erythropoiesis.";
RL Blood 118:2443-2453(2011).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-128; SER-1052 AND SER-1055,
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-906 (ISOFORM 2), AND
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., 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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-128 AND SER-803, AND
RP 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 [16]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-554 AND LYS-594, AND
RP 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 [17]
RP STRUCTURE BY NMR OF 208-269, FUNCTION, SUBCELLULAR LOCATION, AND
RP INTERACTION WITH UNMODIFIED HISTONE H3.
RX PubMed=21880731; DOI=10.1074/jbc.m111.244400;
RA Qin S., Jin L., Zhang J., Liu L., Ji P., Wu M., Wu J., Shi Y.;
RT "Recognition of unmodified histone H3 by the first PHD finger of
RT bromodomain-PHD finger protein 2 provides insights into the regulation of
RT histone acetyltransferases monocytic leukemic zinc-finger protein (MOZ) and
RT MOZ-related factor (MORF).";
RL J. Biol. Chem. 286:36944-36955(2011).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 925-1049, AND INTERACTION WITH
RP METHYLATED HISTONE H3.
RX PubMed=21720545; DOI=10.1371/journal.pone.0018919;
RA Wu H., Zeng H., Lam R., Tempel W., Amaya M.F., Xu C., Dombrovski L.,
RA Qiu W., Wang Y., Min J.;
RT "Structural and histone binding ability characterizations of human PWWP
RT domains.";
RL PLoS ONE 6:E18919-E18919(2011).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (2.21 ANGSTROMS) OF 556-688.
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).
RN [20] {ECO:0007744|PDB:5GK9}
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 31-80 IN COMPLEX WITH KAT7,
RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF 41-GLU--GLU-45; ILE-51; LEU-57;
RP ILE-59 AND 62-GLU--ASP-64.
RX PubMed=28334966; DOI=10.1093/nar/gkx142;
RA Tao Y., Zhong C., Zhu J., Xu S., Ding J.;
RT "Structural and mechanistic insights into regulation of HBO1 histone
RT acetyltransferase activity by BRPF2.";
RL Nucleic Acids Res. 45:5707-5719(2017).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (2.13 ANGSTROMS) OF 31-80 IN COMPLEX WITH KAT7.
RX PubMed=31827282; DOI=10.1038/s41586-019-1835-6;
RA MacPherson L., Anokye J., Yeung M.M., Lam E.Y.N., Chan Y.C., Weng C.F.,
RA Yeh P., Knezevic K., Butler M.S., Hoegl A., Chan K.L., Burr M.L.,
RA Gearing L.J., Willson T., Liu J., Choi J., Yang Y., Bilardi R.A., Falk H.,
RA Nguyen N., Stupple P.A., Peat T.S., Zhang M., de Silva M.,
RA Carrasco-Pozo C., Avery V.M., Khoo P.S., Dolezal O., Dennis M.L.,
RA Nuttall S., Surjadi R., Newman J., Ren B., Leaver D.J., Sun Y., Baell J.B.,
RA Dovey O., Vassiliou G.S., Grebien F., Dawson S.J., Street I.P.,
RA Monahan B.J., Burns C.J., Choudhary C., Blewitt M.E., Voss A.K., Thomas T.,
RA Dawson M.A.;
RT "HBO1 is required for the maintenance of leukaemia stem cells.";
RL Nature 577:266-270(2020).
RN [22]
RP VARIANT LEU-230.
RX PubMed=28584052; DOI=10.1074/jbc.m117.790097;
RA Willems A.P., Gundogdu M., Kempers M.J.E., Giltay J.C., Pfundt R.,
RA Elferink M., Loza B.F., Fuijkschot J., Ferenbach A.T., van Gassen K.L.I.,
RA van Aalten D.M.F., Lefeber D.J.;
RT "Mutations in N-acetylglucosamine (O-GlcNAc) transferase in patients with
RT X-linked intellectual disability.";
RL J. Biol. Chem. 292:12621-12631(2017).
CC -!- FUNCTION: Scaffold subunit of various histone acetyltransferase (HAT)
CC complexes, such as the MOZ/MORF and HBO1 complexes, that acts as a
CC regulator of hematopoiesis (PubMed:16387653, PubMed:21753189,
CC PubMed:21880731). Plays a key role in HBO1 complex by directing
CC KAT7/HBO1 specificity towards histone H3 'Lys-14' acetylation
CC (H3K14ac), thereby promoting erythroid differentiation
CC (PubMed:21753189). {ECO:0000269|PubMed:16387653,
CC ECO:0000269|PubMed:21753189, ECO:0000269|PubMed:21880731}.
CC -!- SUBUNIT: Component of some HBO1 complex composed of KAT7/HBO1, MEAF6,
CC ING4 and BRD1/BRPF2 (PubMed:21753189, PubMed:28334966). Component of
CC the MOZ/MORF complex composed at least of ING5, KAT6A, KAT6B, MEAF6 and
CC one of BRPF1, BRD1/BRPF2 and BRPF3 (PubMed:16387653, PubMed:18794358).
CC Interacts (via PHD-type zinc finger domain) with unmodified histone H3
CC (PubMed:21880731). Interacts (via PWWP domain) with dimethylated and
CC trimethylated 'Lys-79' on histone H3 (PubMed:21720545).
CC {ECO:0000269|PubMed:16387653, ECO:0000269|PubMed:18794358,
CC ECO:0000269|PubMed:21720545, ECO:0000269|PubMed:21753189,
CC ECO:0000269|PubMed:21880731, ECO:0000269|PubMed:28334966}.
CC -!- INTERACTION:
CC O95696; Q6NVI2: CASP8; NbExp=3; IntAct=EBI-714754, EBI-12861768;
CC O95696; Q8NHQ1: CEP70; NbExp=3; IntAct=EBI-714754, EBI-739624;
CC O95696; Q9NRI5-2: DISC1; NbExp=3; IntAct=EBI-714754, EBI-11988027;
CC O95696; Q6NT76: HMBOX1; NbExp=3; IntAct=EBI-714754, EBI-2549423;
CC O95696; P43364: MAGEA11; NbExp=3; IntAct=EBI-714754, EBI-739552;
CC O95696; P23508: MCC; NbExp=3; IntAct=EBI-714754, EBI-307531;
CC O95696; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-714754, EBI-79165;
CC O95696; Q92622: RUBCN; NbExp=3; IntAct=EBI-714754, EBI-2952709;
CC O95696; Q9UBB9: TFIP11; NbExp=3; IntAct=EBI-714754, EBI-1105213;
CC O95696; Q9UGI0: ZRANB1; NbExp=3; IntAct=EBI-714754, EBI-527853;
CC O95696-1; Q86U86: PBRM1; NbExp=2; IntAct=EBI-11700916, EBI-637807;
CC O95696-2; Q86U86: PBRM1; NbExp=2; IntAct=EBI-11017508, EBI-637807;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21753189,
CC ECO:0000269|PubMed:21880731}. Chromosome {ECO:0000269|PubMed:21753189,
CC ECO:0000269|PubMed:28334966}. Note=Localizes to transcription start
CC sites. {ECO:0000269|PubMed:21753189, ECO:0000269|PubMed:28334966}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O95696-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O95696-2; Sequence=VSP_040262;
CC -!- TISSUE SPECIFICITY: Highly expressed in testis.
CC {ECO:0000269|PubMed:10602503}.
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DR EMBL; AF005067; AAF34320.1; -; mRNA.
DR EMBL; CR456408; CAG30294.1; -; mRNA.
DR EMBL; AK292428; BAF85117.1; -; mRNA.
DR EMBL; Z98885; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471138; EAW73473.1; -; Genomic_DNA.
DR CCDS; CCDS14080.1; -. [O95696-1]
DR CCDS; CCDS77686.1; -. [O95696-2]
DR RefSeq; NP_001291737.1; NM_001304808.1. [O95696-2]
DR RefSeq; NP_001291738.1; NM_001304809.1. [O95696-1]
DR RefSeq; XP_016884204.1; XM_017028715.1. [O95696-2]
DR RefSeq; XP_016884205.1; XM_017028716.1. [O95696-2]
DR RefSeq; XP_016884206.1; XM_017028717.1.
DR PDB; 2KU3; NMR; -; A=208-269.
DR PDB; 2L43; NMR; -; A=205-269.
DR PDB; 2LQ6; NMR; -; A=317-392.
DR PDB; 3LYI; X-ray; 2.10 A; A/B=925-1049.
DR PDB; 3RCW; X-ray; 2.21 A; A/B/C/D/E/F/G/H=556-688.
DR PDB; 4Z02; X-ray; 1.87 A; A/B=925-1049.
DR PDB; 5AME; X-ray; 1.58 A; A/B=556-688.
DR PDB; 5AMF; X-ray; 1.75 A; A/B=556-688.
DR PDB; 5FG6; X-ray; 1.10 A; A=563-688.
DR PDB; 5GK9; X-ray; 2.40 A; B=31-80.
DR PDB; 5N49; X-ray; 1.94 A; A/B=555-688.
DR PDB; 5PNX; X-ray; 1.47 A; A/B=555-688.
DR PDB; 5PNY; X-ray; 1.48 A; A/B=555-688.
DR PDB; 5PNZ; X-ray; 1.56 A; A/B=555-688.
DR PDB; 5PO0; X-ray; 1.46 A; A/B=555-688.
DR PDB; 5PO1; X-ray; 1.52 A; A/B=555-688.
DR PDB; 5PO2; X-ray; 1.67 A; A/B=555-688.
DR PDB; 5PO3; X-ray; 1.70 A; A/B=555-688.
DR PDB; 5PO4; X-ray; 1.49 A; A/B=555-688.
DR PDB; 5PO5; X-ray; 1.44 A; A/B=555-688.
DR PDB; 5PO6; X-ray; 1.61 A; A/B=555-688.
DR PDB; 5PO7; X-ray; 1.50 A; A/B=555-688.
DR PDB; 5PO8; X-ray; 1.50 A; A/B=555-688.
DR PDB; 5PO9; X-ray; 2.12 A; A/B=555-688.
DR PDB; 5POA; X-ray; 1.62 A; A/B=555-688.
DR PDB; 5POB; X-ray; 1.78 A; A/B=555-688.
DR PDB; 5POC; X-ray; 1.48 A; A/B=555-688.
DR PDB; 5POD; X-ray; 1.56 A; A/B=555-688.
DR PDB; 5POE; X-ray; 1.52 A; A/B=555-688.
DR PDB; 5POF; X-ray; 2.27 A; A/B=555-688.
DR PDB; 5POG; X-ray; 1.77 A; A/B=555-688.
DR PDB; 5POH; X-ray; 1.61 A; A/B=555-688.
DR PDB; 5POI; X-ray; 2.37 A; A/B=555-688.
DR PDB; 5POJ; X-ray; 1.62 A; A/B=555-688.
DR PDB; 5POK; X-ray; 1.56 A; A/B=555-688.
DR PDB; 5POL; X-ray; 1.62 A; A/B=555-688.
DR PDB; 5POM; X-ray; 1.54 A; A/B=555-688.
DR PDB; 5PON; X-ray; 1.52 A; A/B=555-688.
DR PDB; 5POO; X-ray; 1.50 A; A/B=555-688.
DR PDB; 5POP; X-ray; 1.58 A; A/B=555-688.
DR PDB; 5POQ; X-ray; 1.97 A; A/B=555-688.
DR PDB; 5POR; X-ray; 1.58 A; A/B=555-688.
DR PDB; 5POS; X-ray; 1.75 A; A/B=555-688.
DR PDB; 5POT; X-ray; 1.63 A; A/B=555-688.
DR PDB; 5POU; X-ray; 1.43 A; A/B=555-688.
DR PDB; 5POV; X-ray; 1.57 A; A/B=555-688.
DR PDB; 5POW; X-ray; 1.77 A; A/B=555-688.
DR PDB; 5POX; X-ray; 1.75 A; A/B=555-688.
DR PDB; 5POY; X-ray; 1.76 A; A/B=555-688.
DR PDB; 5POZ; X-ray; 1.50 A; A/B=555-688.
DR PDB; 5PP0; X-ray; 1.61 A; A/B=555-688.
DR PDB; 5PP1; X-ray; 2.35 A; A/B=555-688.
DR PDB; 5PP2; X-ray; 1.61 A; A/B=555-688.
DR PDB; 5PP3; X-ray; 2.58 A; A/B=555-688.
DR PDB; 5PP4; X-ray; 1.92 A; A/B=555-688.
DR PDB; 5PP5; X-ray; 1.87 A; A/B=555-688.
DR PDB; 5PP6; X-ray; 1.52 A; A/B=555-688.
DR PDB; 5PP7; X-ray; 1.52 A; A/B=555-688.
DR PDB; 5PP8; X-ray; 1.74 A; A/B=555-688.
DR PDB; 5PP9; X-ray; 1.82 A; A/B=555-688.
DR PDB; 5PPA; X-ray; 1.91 A; A/B=555-688.
DR PDB; 5PPB; X-ray; 1.48 A; A/B=555-688.
DR PDB; 5PPC; X-ray; 1.61 A; A/B=555-688.
DR PDB; 5PPD; X-ray; 1.67 A; A/B=555-688.
DR PDB; 5PPE; X-ray; 1.46 A; A/B=555-688.
DR PDB; 5PPF; X-ray; 1.64 A; A/B=555-688.
DR PDB; 5PPG; X-ray; 1.55 A; A/B=555-688.
DR PDB; 5PPH; X-ray; 1.89 A; A/B=555-688.
DR PDB; 5PPI; X-ray; 1.56 A; A/B=555-688.
DR PDB; 5PPJ; X-ray; 1.61 A; A/B=555-688.
DR PDB; 5PPK; X-ray; 1.87 A; A/B=555-688.
DR PDB; 5PPL; X-ray; 1.63 A; A/B=555-688.
DR PDB; 5PPM; X-ray; 1.87 A; A/B=555-688.
DR PDB; 5PPN; X-ray; 1.80 A; A/B=555-688.
DR PDB; 5PPO; X-ray; 1.84 A; A/B=555-688.
DR PDB; 5PPP; X-ray; 1.68 A; A/B=555-688.
DR PDB; 5PPQ; X-ray; 1.70 A; A/B=555-688.
DR PDB; 5PPR; X-ray; 2.69 A; A/B=555-688.
DR PDB; 5PPS; X-ray; 1.53 A; A/B=555-688.
DR PDB; 5PPT; X-ray; 1.61 A; A/B=555-688.
DR PDB; 5PPU; X-ray; 1.63 A; A/B=555-688.
DR PDB; 5PPV; X-ray; 1.70 A; A/B=555-688.
DR PDB; 5PPW; X-ray; 1.45 A; A/B=555-688.
DR PDB; 5PPX; X-ray; 1.44 A; A/B=555-688.
DR PDB; 5PPY; X-ray; 1.45 A; A/B=555-688.
DR PDB; 5PPZ; X-ray; 1.55 A; A/B=555-688.
DR PDB; 5PQ0; X-ray; 1.81 A; A/B=555-688.
DR PDB; 5PQ1; X-ray; 1.55 A; A/B=555-688.
DR PDB; 5PQ2; X-ray; 1.47 A; A/B=555-688.
DR PDB; 5PQ3; X-ray; 1.72 A; A/B=555-688.
DR PDB; 5PQ4; X-ray; 1.63 A; A/B=555-688.
DR PDB; 5PQ5; X-ray; 1.60 A; A/B=555-688.
DR PDB; 5PQ6; X-ray; 1.64 A; A/B=555-688.
DR PDB; 5PQ7; X-ray; 1.56 A; A/B=555-688.
DR PDB; 5PQ8; X-ray; 1.65 A; A/B=555-688.
DR PDB; 5PQ9; X-ray; 1.60 A; A/B=555-688.
DR PDB; 5PQA; X-ray; 1.78 A; A/B=555-688.
DR PDB; 5PQB; X-ray; 1.58 A; A/B=555-688.
DR PDB; 5PQC; X-ray; 1.45 A; A/B=555-688.
DR PDB; 5PQD; X-ray; 1.65 A; A/B=555-688.
DR PDB; 5PQE; X-ray; 1.53 A; A/B=555-688.
DR PDB; 5PQF; X-ray; 1.65 A; A/B=555-688.
DR PDB; 5PQG; X-ray; 1.82 A; A/B=555-688.
DR PDB; 5PQH; X-ray; 1.52 A; A/B=555-688.
DR PDB; 5PQI; X-ray; 1.33 A; A/B=555-688.
DR PDB; 5PQJ; X-ray; 1.59 A; A/B=555-688.
DR PDB; 5PQK; X-ray; 1.58 A; A/B=555-688.
DR PDB; 5PQL; X-ray; 1.52 A; A/B=555-688.
DR PDB; 5PQM; X-ray; 2.56 A; A/B=555-688.
DR PDB; 5PQN; X-ray; 2.00 A; A/B=555-688.
DR PDB; 5PQO; X-ray; 1.75 A; A/B=555-688.
DR PDB; 5PQP; X-ray; 1.97 A; A/B=555-688.
DR PDB; 5PQQ; X-ray; 2.30 A; A/B=555-688.
DR PDB; 5PQR; X-ray; 2.43 A; A/B=555-688.
DR PDB; 5PQS; X-ray; 1.82 A; A/B=555-688.
DR PDB; 5PQT; X-ray; 1.89 A; A/B=555-688.
DR PDB; 5PQU; X-ray; 2.00 A; A/B=555-688.
DR PDB; 5PQV; X-ray; 1.97 A; A/B=555-688.
DR PDB; 5PQW; X-ray; 2.00 A; A/B=555-688.
DR PDB; 5PQX; X-ray; 1.95 A; A/B=555-688.
DR PDB; 5PQY; X-ray; 1.89 A; A/B=555-688.
DR PDB; 5PQZ; X-ray; 2.58 A; A/B=555-688.
DR PDB; 5PR0; X-ray; 2.23 A; A/B=555-688.
DR PDB; 5PR1; X-ray; 2.10 A; A/B=555-688.
DR PDB; 5PR2; X-ray; 2.10 A; A/B=555-688.
DR PDB; 5PR4; X-ray; 1.82 A; A/B=555-688.
DR PDB; 5PR5; X-ray; 1.95 A; A/B=555-688.
DR PDB; 5PR6; X-ray; 1.80 A; A/B=555-688.
DR PDB; 5PR7; X-ray; 1.80 A; A/B=555-688.
DR PDB; 5PR8; X-ray; 1.92 A; A/B=555-688.
DR PDB; 5PR9; X-ray; 1.82 A; A/B=555-688.
DR PDB; 5PRA; X-ray; 1.87 A; A/B=555-688.
DR PDB; 5PRB; X-ray; 2.23 A; A/B=555-688.
DR PDB; 5PRD; X-ray; 1.90 A; A/B=555-688.
DR PDB; 5PRE; X-ray; 1.73 A; A/B=555-688.
DR PDB; 5PRF; X-ray; 1.82 A; A/B=555-688.
DR PDB; 5PRG; X-ray; 2.68 A; A/B=555-688.
DR PDB; 5PRH; X-ray; 1.95 A; A/B=555-688.
DR PDB; 5PRI; X-ray; 1.90 A; A/B=555-688.
DR PDB; 5PRJ; X-ray; 2.17 A; A/B=555-688.
DR PDB; 5PRK; X-ray; 2.23 A; A/B=555-688.
DR PDB; 5PRL; X-ray; 1.75 A; A/B=555-688.
DR PDB; 5PRM; X-ray; 3.58 A; A/B=555-688.
DR PDB; 5PRO; X-ray; 1.55 A; A/B=555-688.
DR PDB; 5PRP; X-ray; 1.45 A; A/B=555-688.
DR PDB; 5PRQ; X-ray; 1.68 A; A/B=555-688.
DR PDB; 5PRR; X-ray; 1.63 A; A/B=555-688.
DR PDB; 5PRS; X-ray; 1.72 A; A/B=555-688.
DR PDB; 5PRT; X-ray; 1.89 A; A/B=555-688.
DR PDB; 5PRU; X-ray; 1.58 A; A/B=555-688.
DR PDB; 5PRV; X-ray; 1.62 A; A/B=555-688.
DR PDB; 5PRW; X-ray; 1.65 A; A/B=555-688.
DR PDB; 5PRX; X-ray; 1.87 A; A/B=555-688.
DR PDB; 5PRY; X-ray; 1.80 A; A/B=555-688.
DR PDB; 5PRZ; X-ray; 1.62 A; A/B=555-688.
DR PDB; 5PS0; X-ray; 1.68 A; A/B=555-688.
DR PDB; 5PS1; X-ray; 1.71 A; A/B=555-688.
DR PDB; 5PS2; X-ray; 1.55 A; A/B=555-688.
DR PDB; 5PS3; X-ray; 1.93 A; A/B=555-688.
DR PDB; 5PS4; X-ray; 1.70 A; A/B=555-688.
DR PDB; 5PS5; X-ray; 2.15 A; A/B=555-688.
DR PDB; 5PS6; X-ray; 1.52 A; A/B=555-688.
DR PDB; 5PS7; X-ray; 2.21 A; A/B=555-688.
DR PDB; 5PS8; X-ray; 1.93 A; A/B=555-688.
DR PDB; 5PS9; X-ray; 1.71 A; A/B=555-688.
DR PDB; 5PSA; X-ray; 1.64 A; A/B=555-688.
DR PDB; 5PSB; X-ray; 1.62 A; A/B=555-688.
DR PDB; 5PSC; X-ray; 1.68 A; A/B=555-688.
DR PDB; 5PSD; X-ray; 1.63 A; A/B=555-688.
DR PDB; 5PSE; X-ray; 2.19 A; A/B=555-688.
DR PDB; 5PSF; X-ray; 2.31 A; A/B=555-688.
DR PDB; 5PSG; X-ray; 1.55 A; A/B=555-688.
DR PDB; 5PSH; X-ray; 3.43 A; A/B=555-688.
DR PDB; 5PSI; X-ray; 1.62 A; A/B=555-688.
DR PDB; 5PSJ; X-ray; 1.38 A; A/B=555-688.
DR PDB; 5PSK; X-ray; 1.38 A; A/B=555-688.
DR PDB; 5PSL; X-ray; 1.39 A; A/B=555-688.
DR PDB; 5PSM; X-ray; 1.53 A; A/B=555-688.
DR PDB; 5PSN; X-ray; 1.48 A; A/B=555-688.
DR PDB; 5PSO; X-ray; 1.55 A; A/B=555-688.
DR PDB; 5PSP; X-ray; 1.58 A; A/B=555-688.
DR PDB; 5PSQ; X-ray; 1.43 A; A/B=555-688.
DR PDB; 5PSR; X-ray; 1.59 A; A/B=555-688.
DR PDB; 5PSS; X-ray; 1.59 A; A/B=555-688.
DR PDB; 5PST; X-ray; 1.39 A; A/B=555-688.
DR PDB; 5PSU; X-ray; 1.56 A; A/B=555-688.
DR PDB; 5PSV; X-ray; 1.53 A; A/B=555-688.
DR PDB; 5PSW; X-ray; 1.53 A; A/B=555-688.
DR PDB; 5PSX; X-ray; 1.59 A; A/B=555-688.
DR PDB; 5PSY; X-ray; 1.82 A; A/B=555-688.
DR PDB; 5PSZ; X-ray; 1.53 A; A/B=555-688.
DR PDB; 5PT0; X-ray; 1.43 A; A/B=555-688.
DR PDB; 5PT1; X-ray; 1.54 A; A/B=555-688.
DR PDB; 5PT2; X-ray; 1.52 A; A/B=555-688.
DR PDB; 5PT3; X-ray; 1.70 A; A/B=555-688.
DR PDB; 5PT4; X-ray; 1.54 A; A/B=555-688.
DR PDB; 5PT5; X-ray; 1.76 A; A/B=555-688.
DR PDB; 5PT6; X-ray; 1.53 A; A/B=555-688.
DR PDB; 5PT7; X-ray; 1.55 A; A/B=555-688.
DR PDB; 5PT8; X-ray; 1.66 A; A/B=555-688.
DR PDB; 5PT9; X-ray; 1.47 A; A/B=555-688.
DR PDB; 5PTA; X-ray; 2.19 A; A/B=555-688.
DR PDB; 5PTB; X-ray; 1.88 A; A/B=555-688.
DR PDB; 5PTC; X-ray; 1.78 A; A/B=555-688.
DR PDB; 5PTE; X-ray; 1.63 A; A/B=555-688.
DR PDB; 5PTF; X-ray; 1.49 A; A/B=555-688.
DR PDB; 5PTG; X-ray; 1.46 A; A/B=555-688.
DR PDB; 5PTH; X-ray; 1.56 A; A/B=555-688.
DR PDB; 5PTJ; X-ray; 1.69 A; A/B=555-688.
DR PDB; 5PTK; X-ray; 1.48 A; A/B=555-688.
DR PDB; 5PTL; X-ray; 1.53 A; A/B=555-688.
DR PDB; 5PTM; X-ray; 1.41 A; A/B=555-688.
DR PDB; 5PTN; X-ray; 1.47 A; A/B=555-688.
DR PDB; 5PTO; X-ray; 1.67 A; A/B=555-688.
DR PDB; 5PTQ; X-ray; 1.49 A; A/B=555-688.
DR PDB; 5PTR; X-ray; 1.52 A; A/B=555-688.
DR PDB; 5PTS; X-ray; 1.45 A; A/B=555-688.
DR PDB; 5PTT; X-ray; 1.47 A; A/B=555-688.
DR PDB; 5PTU; X-ray; 1.69 A; A/B=555-688.
DR PDB; 5PTV; X-ray; 1.70 A; A/B=555-688.
DR PDB; 5PTW; X-ray; 1.82 A; A/B=555-688.
DR PDB; 5PTX; X-ray; 1.60 A; A/B=555-688.
DR PDB; 5PTY; X-ray; 2.10 A; A/B=555-688.
DR PDB; 5PTZ; X-ray; 1.51 A; A/B=555-688.
DR PDB; 5PU0; X-ray; 1.89 A; A/B=555-688.
DR PDB; 5PU1; X-ray; 1.73 A; A/B=555-688.
DR PDB; 5PU2; X-ray; 1.59 A; A/B=555-688.
DR PDB; 5PU3; X-ray; 2.37 A; A/B=555-688.
DR PDB; 5PU4; X-ray; 1.55 A; A/B=555-688.
DR PDB; 5PU5; X-ray; 1.55 A; A/B=555-688.
DR PDB; 5PU6; X-ray; 1.74 A; A/B=555-688.
DR PDB; 5PU7; X-ray; 1.62 A; A/B=555-688.
DR PDB; 5PU8; X-ray; 1.55 A; A/B=555-688.
DR PDB; 5PU9; X-ray; 1.56 A; A/B=555-688.
DR PDB; 5PUA; X-ray; 1.63 A; A/B=555-688.
DR PDB; 5PUB; X-ray; 2.23 A; A/B=555-688.
DR PDB; 5PUC; X-ray; 1.64 A; A/B=555-688.
DR PDB; 5PUD; X-ray; 2.01 A; A/B=555-688.
DR PDB; 5PUE; X-ray; 1.70 A; A/B=555-688.
DR PDB; 5PUF; X-ray; 1.82 A; A/B=555-688.
DR PDB; 5PUG; X-ray; 2.00 A; A/B=555-688.
DR PDB; 5PUH; X-ray; 1.92 A; A/B=555-688.
DR PDB; 5PUI; X-ray; 1.51 A; A/B=555-688.
DR PDB; 5PUJ; X-ray; 1.90 A; A/B=555-688.
DR PDB; 5PUK; X-ray; 1.64 A; A/B=555-688.
DR PDB; 5PUL; X-ray; 1.95 A; A/B=555-688.
DR PDB; 5PUM; X-ray; 2.15 A; A/B=555-688.
DR PDB; 5PUN; X-ray; 1.84 A; A/B=555-688.
DR PDB; 5PUO; X-ray; 2.06 A; A/B=555-688.
DR PDB; 5PUP; X-ray; 1.60 A; A/B=555-688.
DR PDB; 5PUQ; X-ray; 1.70 A; A/B=555-688.
DR PDB; 5PUR; X-ray; 1.73 A; A/B=555-688.
DR PDB; 5PUS; X-ray; 1.67 A; A/B=555-688.
DR PDB; 5PUT; X-ray; 2.32 A; A/B=555-688.
DR PDB; 5PUU; X-ray; 1.69 A; A/B=555-688.
DR PDB; 5PUV; X-ray; 1.69 A; A/B=555-688.
DR PDB; 5PUW; X-ray; 1.82 A; A/B=555-688.
DR PDB; 5PUX; X-ray; 1.51 A; A/B=555-688.
DR PDB; 5PUY; X-ray; 2.01 A; A/B=555-688.
DR PDB; 5PUZ; X-ray; 1.49 A; A/B=555-688.
DR PDB; 5PV0; X-ray; 1.76 A; A/B=555-688.
DR PDB; 5PV1; X-ray; 1.73 A; A/B=555-688.
DR PDB; 5PV2; X-ray; 1.63 A; A/B=555-688.
DR PDB; 5PV3; X-ray; 1.48 A; A/B=555-688.
DR PDB; 5PV4; X-ray; 1.58 A; A/B=555-688.
DR PDB; 5PV5; X-ray; 1.68 A; A/B=555-688.
DR PDB; 5PV6; X-ray; 1.62 A; A/B=555-688.
DR PDB; 5PV7; X-ray; 1.58 A; A/B=555-688.
DR PDB; 5PV8; X-ray; 1.49 A; A/B=555-688.
DR PDB; 5PV9; X-ray; 1.67 A; A/B=555-688.
DR PDB; 5PVA; X-ray; 1.98 A; A/B=555-688.
DR PDB; 5PVB; X-ray; 1.53 A; A/B=555-688.
DR PDB; 5PVC; X-ray; 1.56 A; A/B=555-688.
DR PDB; 5PVD; X-ray; 1.53 A; A/B=555-688.
DR PDB; 5PVE; X-ray; 2.29 A; A/B=555-688.
DR PDB; 5PVF; X-ray; 1.71 A; A/B=555-688.
DR PDB; 5PVG; X-ray; 1.69 A; A/B=555-688.
DR PDB; 5PVH; X-ray; 1.69 A; A/B=555-688.
DR PDB; 5PVI; X-ray; 2.19 A; A/B=555-688.
DR PDB; 5PVJ; X-ray; 1.57 A; A/B=555-688.
DR PDB; 5PVK; X-ray; 1.58 A; A/B=555-688.
DR PDB; 5PVL; X-ray; 1.53 A; A/B=555-688.
DR PDB; 5PVM; X-ray; 1.65 A; A/B=555-688.
DR PDB; 5PVN; X-ray; 1.63 A; A/B=555-688.
DR PDB; 5PVO; X-ray; 1.96 A; A/B=555-688.
DR PDB; 5PVP; X-ray; 1.69 A; A/B=555-688.
DR PDB; 5PVQ; X-ray; 1.61 A; A/B=555-688.
DR PDB; 5PVR; X-ray; 1.57 A; A/B=555-688.
DR PDB; 5PVS; X-ray; 1.55 A; A/B=555-688.
DR PDB; 5PVT; X-ray; 1.48 A; A/B=555-688.
DR PDB; 5PVU; X-ray; 3.01 A; A/B=555-688.
DR PDB; 5PVV; X-ray; 1.80 A; A/B=555-688.
DR PDB; 5PVW; X-ray; 2.18 A; A/B=555-688.
DR PDB; 5PVX; X-ray; 1.74 A; A/B=555-688.
DR PDB; 5PVY; X-ray; 2.49 A; A/B=555-688.
DR PDB; 5PVZ; X-ray; 1.64 A; A/B=555-688.
DR PDB; 5PW0; X-ray; 2.13 A; A/B=555-688.
DR PDB; 5PW1; X-ray; 1.57 A; A/B=555-688.
DR PDB; 5PW2; X-ray; 2.32 A; A/B=555-688.
DR PDB; 5PW3; X-ray; 2.21 A; A/B=555-688.
DR PDB; 5PW4; X-ray; 1.91 A; A/B=555-688.
DR PDB; 5PW5; X-ray; 2.09 A; A/B=555-688.
DR PDB; 5PW6; X-ray; 2.75 A; A/B=555-688.
DR PDB; 5PW7; X-ray; 1.85 A; A/B=555-688.
DR PDB; 5PW8; X-ray; 2.08 A; A/B=555-688.
DR PDB; 5PW9; X-ray; 3.44 A; A/B=555-688.
DR PDB; 5PWA; X-ray; 1.86 A; A/B=555-688.
DR PDB; 5PWB; X-ray; 2.09 A; A/B=555-688.
DR PDB; 6IN2; X-ray; 1.75 A; A=563-680.
DR PDB; 6MAJ; X-ray; 2.14 A; B=31-80.
DR PDB; 6MAK; X-ray; 2.13 A; B=31-80.
DR PDB; 7D0O; X-ray; 2.51 A; B=31-80.
DR PDB; 7D0P; X-ray; 1.80 A; B=31-80.
DR PDB; 7D0Q; X-ray; 2.21 A; B=31-80.
DR PDB; 7D0R; X-ray; 1.95 A; B=31-80.
DR PDB; 7D0S; X-ray; 2.30 A; B=31-80.
DR PDB; 7LH9; X-ray; 2.60 A; A/B/C/D=925-1049.
DR PDBsum; 2KU3; -.
DR PDBsum; 2L43; -.
DR PDBsum; 2LQ6; -.
DR PDBsum; 3LYI; -.
DR PDBsum; 3RCW; -.
DR PDBsum; 4Z02; -.
DR PDBsum; 5AME; -.
DR PDBsum; 5AMF; -.
DR PDBsum; 5FG6; -.
DR PDBsum; 5GK9; -.
DR PDBsum; 5N49; -.
DR PDBsum; 5PNX; -.
DR PDBsum; 5PNY; -.
DR PDBsum; 5PNZ; -.
DR PDBsum; 5PO0; -.
DR PDBsum; 5PO1; -.
DR PDBsum; 5PO2; -.
DR PDBsum; 5PO3; -.
DR PDBsum; 5PO4; -.
DR PDBsum; 5PO5; -.
DR PDBsum; 5PO6; -.
DR PDBsum; 5PO7; -.
DR PDBsum; 5PO8; -.
DR PDBsum; 5PO9; -.
DR PDBsum; 5POA; -.
DR PDBsum; 5POB; -.
DR PDBsum; 5POC; -.
DR PDBsum; 5POD; -.
DR PDBsum; 5POE; -.
DR PDBsum; 5POF; -.
DR PDBsum; 5POG; -.
DR PDBsum; 5POH; -.
DR PDBsum; 5POI; -.
DR PDBsum; 5POJ; -.
DR PDBsum; 5POK; -.
DR PDBsum; 5POL; -.
DR PDBsum; 5POM; -.
DR PDBsum; 5PON; -.
DR PDBsum; 5POO; -.
DR PDBsum; 5POP; -.
DR PDBsum; 5POQ; -.
DR PDBsum; 5POR; -.
DR PDBsum; 5POS; -.
DR PDBsum; 5POT; -.
DR PDBsum; 5POU; -.
DR PDBsum; 5POV; -.
DR PDBsum; 5POW; -.
DR PDBsum; 5POX; -.
DR PDBsum; 5POY; -.
DR PDBsum; 5POZ; -.
DR PDBsum; 5PP0; -.
DR PDBsum; 5PP1; -.
DR PDBsum; 5PP2; -.
DR PDBsum; 5PP3; -.
DR PDBsum; 5PP4; -.
DR PDBsum; 5PP5; -.
DR PDBsum; 5PP6; -.
DR PDBsum; 5PP7; -.
DR PDBsum; 5PP8; -.
DR PDBsum; 5PP9; -.
DR PDBsum; 5PPA; -.
DR PDBsum; 5PPB; -.
DR PDBsum; 5PPC; -.
DR PDBsum; 5PPD; -.
DR PDBsum; 5PPE; -.
DR PDBsum; 5PPF; -.
DR PDBsum; 5PPG; -.
DR PDBsum; 5PPH; -.
DR PDBsum; 5PPI; -.
DR PDBsum; 5PPJ; -.
DR PDBsum; 5PPK; -.
DR PDBsum; 5PPL; -.
DR PDBsum; 5PPM; -.
DR PDBsum; 5PPN; -.
DR PDBsum; 5PPO; -.
DR PDBsum; 5PPP; -.
DR PDBsum; 5PPQ; -.
DR PDBsum; 5PPR; -.
DR PDBsum; 5PPS; -.
DR PDBsum; 5PPT; -.
DR PDBsum; 5PPU; -.
DR PDBsum; 5PPV; -.
DR PDBsum; 5PPW; -.
DR PDBsum; 5PPX; -.
DR PDBsum; 5PPY; -.
DR PDBsum; 5PPZ; -.
DR PDBsum; 5PQ0; -.
DR PDBsum; 5PQ1; -.
DR PDBsum; 5PQ2; -.
DR PDBsum; 5PQ3; -.
DR PDBsum; 5PQ4; -.
DR PDBsum; 5PQ5; -.
DR PDBsum; 5PQ6; -.
DR PDBsum; 5PQ7; -.
DR PDBsum; 5PQ8; -.
DR PDBsum; 5PQ9; -.
DR PDBsum; 5PQA; -.
DR PDBsum; 5PQB; -.
DR PDBsum; 5PQC; -.
DR PDBsum; 5PQD; -.
DR PDBsum; 5PQE; -.
DR PDBsum; 5PQF; -.
DR PDBsum; 5PQG; -.
DR PDBsum; 5PQH; -.
DR PDBsum; 5PQI; -.
DR PDBsum; 5PQJ; -.
DR PDBsum; 5PQK; -.
DR PDBsum; 5PQL; -.
DR PDBsum; 5PQM; -.
DR PDBsum; 5PQN; -.
DR PDBsum; 5PQO; -.
DR PDBsum; 5PQP; -.
DR PDBsum; 5PQQ; -.
DR PDBsum; 5PQR; -.
DR PDBsum; 5PQS; -.
DR PDBsum; 5PQT; -.
DR PDBsum; 5PQU; -.
DR PDBsum; 5PQV; -.
DR PDBsum; 5PQW; -.
DR PDBsum; 5PQX; -.
DR PDBsum; 5PQY; -.
DR PDBsum; 5PQZ; -.
DR PDBsum; 5PR0; -.
DR PDBsum; 5PR1; -.
DR PDBsum; 5PR2; -.
DR PDBsum; 5PR4; -.
DR PDBsum; 5PR5; -.
DR PDBsum; 5PR6; -.
DR PDBsum; 5PR7; -.
DR PDBsum; 5PR8; -.
DR PDBsum; 5PR9; -.
DR PDBsum; 5PRA; -.
DR PDBsum; 5PRB; -.
DR PDBsum; 5PRD; -.
DR PDBsum; 5PRE; -.
DR PDBsum; 5PRF; -.
DR PDBsum; 5PRG; -.
DR PDBsum; 5PRH; -.
DR PDBsum; 5PRI; -.
DR PDBsum; 5PRJ; -.
DR PDBsum; 5PRK; -.
DR PDBsum; 5PRL; -.
DR PDBsum; 5PRM; -.
DR PDBsum; 5PRO; -.
DR PDBsum; 5PRP; -.
DR PDBsum; 5PRQ; -.
DR PDBsum; 5PRR; -.
DR PDBsum; 5PRS; -.
DR PDBsum; 5PRT; -.
DR PDBsum; 5PRU; -.
DR PDBsum; 5PRV; -.
DR PDBsum; 5PRW; -.
DR PDBsum; 5PRX; -.
DR PDBsum; 5PRY; -.
DR PDBsum; 5PRZ; -.
DR PDBsum; 5PS0; -.
DR PDBsum; 5PS1; -.
DR PDBsum; 5PS2; -.
DR PDBsum; 5PS3; -.
DR PDBsum; 5PS4; -.
DR PDBsum; 5PS5; -.
DR PDBsum; 5PS6; -.
DR PDBsum; 5PS7; -.
DR PDBsum; 5PS8; -.
DR PDBsum; 5PS9; -.
DR PDBsum; 5PSA; -.
DR PDBsum; 5PSB; -.
DR PDBsum; 5PSC; -.
DR PDBsum; 5PSD; -.
DR PDBsum; 5PSE; -.
DR PDBsum; 5PSF; -.
DR PDBsum; 5PSG; -.
DR PDBsum; 5PSH; -.
DR PDBsum; 5PSI; -.
DR PDBsum; 5PSJ; -.
DR PDBsum; 5PSK; -.
DR PDBsum; 5PSL; -.
DR PDBsum; 5PSM; -.
DR PDBsum; 5PSN; -.
DR PDBsum; 5PSO; -.
DR PDBsum; 5PSP; -.
DR PDBsum; 5PSQ; -.
DR PDBsum; 5PSR; -.
DR PDBsum; 5PSS; -.
DR PDBsum; 5PST; -.
DR PDBsum; 5PSU; -.
DR PDBsum; 5PSV; -.
DR PDBsum; 5PSW; -.
DR PDBsum; 5PSX; -.
DR PDBsum; 5PSY; -.
DR PDBsum; 5PSZ; -.
DR PDBsum; 5PT0; -.
DR PDBsum; 5PT1; -.
DR PDBsum; 5PT2; -.
DR PDBsum; 5PT3; -.
DR PDBsum; 5PT4; -.
DR PDBsum; 5PT5; -.
DR PDBsum; 5PT6; -.
DR PDBsum; 5PT7; -.
DR PDBsum; 5PT8; -.
DR PDBsum; 5PT9; -.
DR PDBsum; 5PTA; -.
DR PDBsum; 5PTB; -.
DR PDBsum; 5PTC; -.
DR PDBsum; 5PTE; -.
DR PDBsum; 5PTF; -.
DR PDBsum; 5PTG; -.
DR PDBsum; 5PTH; -.
DR PDBsum; 5PTJ; -.
DR PDBsum; 5PTK; -.
DR PDBsum; 5PTL; -.
DR PDBsum; 5PTM; -.
DR PDBsum; 5PTN; -.
DR PDBsum; 5PTO; -.
DR PDBsum; 5PTQ; -.
DR PDBsum; 5PTR; -.
DR PDBsum; 5PTS; -.
DR PDBsum; 5PTT; -.
DR PDBsum; 5PTU; -.
DR PDBsum; 5PTV; -.
DR PDBsum; 5PTW; -.
DR PDBsum; 5PTX; -.
DR PDBsum; 5PTY; -.
DR PDBsum; 5PTZ; -.
DR PDBsum; 5PU0; -.
DR PDBsum; 5PU1; -.
DR PDBsum; 5PU2; -.
DR PDBsum; 5PU3; -.
DR PDBsum; 5PU4; -.
DR PDBsum; 5PU5; -.
DR PDBsum; 5PU6; -.
DR PDBsum; 5PU7; -.
DR PDBsum; 5PU8; -.
DR PDBsum; 5PU9; -.
DR PDBsum; 5PUA; -.
DR PDBsum; 5PUB; -.
DR PDBsum; 5PUC; -.
DR PDBsum; 5PUD; -.
DR PDBsum; 5PUE; -.
DR PDBsum; 5PUF; -.
DR PDBsum; 5PUG; -.
DR PDBsum; 5PUH; -.
DR PDBsum; 5PUI; -.
DR PDBsum; 5PUJ; -.
DR PDBsum; 5PUK; -.
DR PDBsum; 5PUL; -.
DR PDBsum; 5PUM; -.
DR PDBsum; 5PUN; -.
DR PDBsum; 5PUO; -.
DR PDBsum; 5PUP; -.
DR PDBsum; 5PUQ; -.
DR PDBsum; 5PUR; -.
DR PDBsum; 5PUS; -.
DR PDBsum; 5PUT; -.
DR PDBsum; 5PUU; -.
DR PDBsum; 5PUV; -.
DR PDBsum; 5PUW; -.
DR PDBsum; 5PUX; -.
DR PDBsum; 5PUY; -.
DR PDBsum; 5PUZ; -.
DR PDBsum; 5PV0; -.
DR PDBsum; 5PV1; -.
DR PDBsum; 5PV2; -.
DR PDBsum; 5PV3; -.
DR PDBsum; 5PV4; -.
DR PDBsum; 5PV5; -.
DR PDBsum; 5PV6; -.
DR PDBsum; 5PV7; -.
DR PDBsum; 5PV8; -.
DR PDBsum; 5PV9; -.
DR PDBsum; 5PVA; -.
DR PDBsum; 5PVB; -.
DR PDBsum; 5PVC; -.
DR PDBsum; 5PVD; -.
DR PDBsum; 5PVE; -.
DR PDBsum; 5PVF; -.
DR PDBsum; 5PVG; -.
DR PDBsum; 5PVH; -.
DR PDBsum; 5PVI; -.
DR PDBsum; 5PVJ; -.
DR PDBsum; 5PVK; -.
DR PDBsum; 5PVL; -.
DR PDBsum; 5PVM; -.
DR PDBsum; 5PVN; -.
DR PDBsum; 5PVO; -.
DR PDBsum; 5PVP; -.
DR PDBsum; 5PVQ; -.
DR PDBsum; 5PVR; -.
DR PDBsum; 5PVS; -.
DR PDBsum; 5PVT; -.
DR PDBsum; 5PVU; -.
DR PDBsum; 5PVV; -.
DR PDBsum; 5PVW; -.
DR PDBsum; 5PVX; -.
DR PDBsum; 5PVY; -.
DR PDBsum; 5PVZ; -.
DR PDBsum; 5PW0; -.
DR PDBsum; 5PW1; -.
DR PDBsum; 5PW2; -.
DR PDBsum; 5PW3; -.
DR PDBsum; 5PW4; -.
DR PDBsum; 5PW5; -.
DR PDBsum; 5PW6; -.
DR PDBsum; 5PW7; -.
DR PDBsum; 5PW8; -.
DR PDBsum; 5PW9; -.
DR PDBsum; 5PWA; -.
DR PDBsum; 5PWB; -.
DR PDBsum; 6IN2; -.
DR PDBsum; 6MAJ; -.
DR PDBsum; 6MAK; -.
DR PDBsum; 7D0O; -.
DR PDBsum; 7D0P; -.
DR PDBsum; 7D0Q; -.
DR PDBsum; 7D0R; -.
DR PDBsum; 7D0S; -.
DR PDBsum; 7LH9; -.
DR AlphaFoldDB; O95696; -.
DR BMRB; O95696; -.
DR SMR; O95696; -.
DR BioGRID; 117273; 338.
DR ComplexPortal; CPX-733; MOZ2 histone acetyltransferase complex.
DR ComplexPortal; CPX-739; MORF2 histone acetyltransferase complex.
DR CORUM; O95696; -.
DR IntAct; O95696; 65.
DR MINT; O95696; -.
DR STRING; 9606.ENSP00000216267; -.
DR BindingDB; O95696; -.
DR ChEMBL; CHEMBL2176774; -.
DR GuidetoPHARMACOLOGY; 2724; -.
DR iPTMnet; O95696; -.
DR PhosphoSitePlus; O95696; -.
DR BioMuta; BRD1; -.
DR OGP; O95696; -.
DR EPD; O95696; -.
DR jPOST; O95696; -.
DR MassIVE; O95696; -.
DR MaxQB; O95696; -.
DR PaxDb; O95696; -.
DR PeptideAtlas; O95696; -.
DR PRIDE; O95696; -.
DR ProteomicsDB; 51000; -. [O95696-1]
DR ProteomicsDB; 51001; -. [O95696-2]
DR ABCD; O95696; 5 sequenced antibodies.
DR Antibodypedia; 251; 178 antibodies from 24 providers.
DR DNASU; 23774; -.
DR Ensembl; ENST00000216267.12; ENSP00000216267.8; ENSG00000100425.19. [O95696-1]
DR Ensembl; ENST00000404034.5; ENSP00000384076.1; ENSG00000100425.19. [O95696-1]
DR Ensembl; ENST00000404760.6; ENSP00000385858.1; ENSG00000100425.19. [O95696-2]
DR Ensembl; ENST00000457780.3; ENSP00000410042.3; ENSG00000100425.19. [O95696-2]
DR GeneID; 23774; -.
DR KEGG; hsa:23774; -.
DR MANE-Select; ENST00000404760.6; ENSP00000385858.1; NM_001304808.3; NP_001291737.1. [O95696-2]
DR UCSC; uc003biu.6; human. [O95696-1]
DR CTD; 23774; -.
DR DisGeNET; 23774; -.
DR GeneCards; BRD1; -.
DR HGNC; HGNC:1102; BRD1.
DR HPA; ENSG00000100425; Low tissue specificity.
DR MIM; 604589; gene.
DR neXtProt; NX_O95696; -.
DR OpenTargets; ENSG00000100425; -.
DR PharmGKB; PA25413; -.
DR VEuPathDB; HostDB:ENSG00000100425; -.
DR eggNOG; KOG0955; Eukaryota.
DR GeneTree; ENSGT00940000157236; -.
DR HOGENOM; CLU_003589_1_0_1; -.
DR InParanoid; O95696; -.
DR OMA; RHASSPC; -.
DR PhylomeDB; O95696; -.
DR TreeFam; TF316118; -.
DR PathwayCommons; O95696; -.
DR Reactome; R-HSA-3214847; HATs acetylate histones.
DR Reactome; R-HSA-6804758; Regulation of TP53 Activity through Acetylation.
DR SignaLink; O95696; -.
DR BioGRID-ORCS; 23774; 76 hits in 1095 CRISPR screens.
DR ChiTaRS; BRD1; human.
DR EvolutionaryTrace; O95696; -.
DR GenomeRNAi; 23774; -.
DR Pharos; O95696; Tchem.
DR PRO; PR:O95696; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; O95696; protein.
DR Bgee; ENSG00000100425; Expressed in oocyte and 207 other tissues.
DR ExpressionAtlas; O95696; baseline and differential.
DR Genevisible; O95696; HS.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0030425; C:dendrite; IEA:Ensembl.
DR GO; GO:0036409; C:histone H3-K14 acetyltransferase complex; IDA:UniProtKB.
DR GO; GO:0070776; C:MOZ/MORF histone acetyltransferase complex; IDA:UniProtKB.
DR GO; GO:0016607; C:nuclear speck; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0043204; C:perikaryon; IEA:Ensembl.
DR GO; GO:0042393; F:histone binding; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0043249; P:erythrocyte maturation; IEA:UniProtKB-KW.
DR GO; GO:0043966; P:histone H3 acetylation; IDA:UniProtKB.
DR GO; GO:0044154; P:histone H3-K14 acetylation; ISS:UniProtKB.
DR GO; GO:0045648; P:positive regulation of erythrocyte differentiation; ISS:UniProtKB.
DR GO; GO:0050793; P:regulation of developmental process; IC:ComplexPortal.
DR GO; GO:1903706; P:regulation of hemopoiesis; IC:ComplexPortal.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0051602; P:response to electrical stimulus; IEA:Ensembl.
DR GO; GO:0035902; P:response to immobilization stress; IEA:Ensembl.
DR CDD; cd05839; BR140_related; 1.
DR CDD; cd15702; ePHD_BRPF2; 1.
DR CDD; cd15677; PHD_BRPF2; 1.
DR Gene3D; 1.20.920.10; -; 1.
DR Gene3D; 3.30.40.10; -; 2.
DR InterPro; IPR035502; BR140-rel_PWWD.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR018359; Bromodomain_CS.
DR InterPro; IPR042004; BRPF2_ePHD.
DR InterPro; IPR042009; BRPF2_PHD.
DR InterPro; IPR019542; Enhancer_polycomb-like_N.
DR InterPro; IPR034732; EPHD.
DR InterPro; IPR000313; PWWP_dom.
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; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF00439; Bromodomain; 1.
DR Pfam; PF10513; EPL1; 1.
DR Pfam; PF00855; PWWP; 1.
DR PRINTS; PR00503; BROMODOMAIN.
DR SMART; SM00297; BROMO; 1.
DR SMART; SM00249; PHD; 2.
DR SMART; SM00293; PWWP; 1.
DR SUPFAM; SSF47370; SSF47370; 1.
DR SUPFAM; SSF57903; SSF57903; 1.
DR PROSITE; PS00633; BROMODOMAIN_1; 1.
DR PROSITE; PS50014; BROMODOMAIN_2; 1.
DR PROSITE; PS51805; EPHD; 1.
DR PROSITE; PS50812; PWWP; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Bromodomain;
KW Chromatin regulator; Chromosome; Erythrocyte maturation; Isopeptide bond;
KW Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..1058
FT /note="Bromodomain-containing protein 1"
FT /id="PRO_0000211177"
FT DOMAIN 579..649
FT /note="Bromo"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT DOMAIN 929..1012
FT /note="PWWP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00162"
FT ZN_FING 214..264
FT /note="PHD-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT ZN_FING 268..301
FT /note="C2HC pre-PHD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01146"
FT ZN_FING 325..389
FT /note="PHD-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01146"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 31..80
FT /note="Interaction with KAT7/HBO1 and histones"
FT /evidence="ECO:0000269|PubMed:28334966"
FT REGION 92..116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 755..776
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 791..868
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 792..818
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 850..867
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 128
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 368
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 516
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 519
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 803
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 903
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 1052
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 1055
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT CROSSLNK 554
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 594
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 786
FT /note="E -> EGDKSPPKLEPSDALPLPSNSETNSEPPTLKPVELNPEQSKLFKRVT
FT FDNESHSACTQSALVSGRPPEPTRASSGDVPAAAASAVAEPASDVNRRTSVLFCKSKSV
FT SPPKSAKNTETQPTSPQLGTKTFLSV (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_040262"
FT VARIANT 38
FT /note="R -> G (in dbSNP:rs11549978)"
FT /id="VAR_048424"
FT VARIANT 230
FT /note="V -> L"
FT /evidence="ECO:0000269|PubMed:28584052"
FT /id="VAR_079184"
FT VARIANT 321
FT /note="A -> S (in dbSNP:rs12157714)"
FT /id="VAR_048425"
FT VARIANT 730
FT /note="A -> T (in dbSNP:rs35331092)"
FT /id="VAR_048426"
FT MUTAGEN 41..45
FT /note="EIEIE->AIAIA,KIKIK: Decreased interaction with free
FT histones."
FT /evidence="ECO:0000269|PubMed:28334966"
FT MUTAGEN 51
FT /note="I->A,K: Impaired interaction with KAT7/HBO1."
FT /evidence="ECO:0000269|PubMed:28334966"
FT MUTAGEN 57
FT /note="L->A,K: Impaired interaction with KAT7/HBO1."
FT /evidence="ECO:0000269|PubMed:28334966"
FT MUTAGEN 59
FT /note="I->A,K: Impaired interaction with KAT7/HBO1."
FT /evidence="ECO:0000269|PubMed:28334966"
FT MUTAGEN 62..64
FT /note="EDD->AAA,KKK: Decreased interaction with free
FT histones."
FT /evidence="ECO:0000269|PubMed:28334966"
FT STRAND 41..44
FT /evidence="ECO:0007829|PDB:6MAK"
FT STRAND 47..50
FT /evidence="ECO:0007829|PDB:6MAK"
FT STRAND 53..55
FT /evidence="ECO:0007829|PDB:6MAK"
FT STRAND 57..60
FT /evidence="ECO:0007829|PDB:6MAK"
FT TURN 205..208
FT /evidence="ECO:0007829|PDB:2L43"
FT STRAND 218..220
FT /evidence="ECO:0007829|PDB:2KU3"
FT STRAND 222..225
FT /evidence="ECO:0007829|PDB:2L43"
FT STRAND 227..229
FT /evidence="ECO:0007829|PDB:2KU3"
FT STRAND 231..233
FT /evidence="ECO:0007829|PDB:2KU3"
FT STRAND 235..237
FT /evidence="ECO:0007829|PDB:2KU3"
FT STRAND 240..242
FT /evidence="ECO:0007829|PDB:2KU3"
FT HELIX 243..246
FT /evidence="ECO:0007829|PDB:2KU3"
FT HELIX 259..266
FT /evidence="ECO:0007829|PDB:2KU3"
FT TURN 328..331
FT /evidence="ECO:0007829|PDB:2LQ6"
FT STRAND 338..340
FT /evidence="ECO:0007829|PDB:2LQ6"
FT TURN 344..346
FT /evidence="ECO:0007829|PDB:2LQ6"
FT STRAND 349..351
FT /evidence="ECO:0007829|PDB:2LQ6"
FT HELIX 352..358
FT /evidence="ECO:0007829|PDB:2LQ6"
FT STRAND 362..369
FT /evidence="ECO:0007829|PDB:2LQ6"
FT TURN 371..373
FT /evidence="ECO:0007829|PDB:2LQ6"
FT STRAND 376..383
FT /evidence="ECO:0007829|PDB:2LQ6"
FT HELIX 386..388
FT /evidence="ECO:0007829|PDB:2LQ6"
FT STRAND 389..392
FT /evidence="ECO:0007829|PDB:2LQ6"
FT HELIX 566..579
FT /evidence="ECO:0007829|PDB:5FG6"
FT STRAND 586..589
FT /evidence="ECO:0007829|PDB:5PS1"
FT TURN 593..595
FT /evidence="ECO:0007829|PDB:5FG6"
FT HELIX 599..602
FT /evidence="ECO:0007829|PDB:5FG6"
FT HELIX 609..617
FT /evidence="ECO:0007829|PDB:5FG6"
FT HELIX 624..641
FT /evidence="ECO:0007829|PDB:5FG6"
FT STRAND 644..646
FT /evidence="ECO:0007829|PDB:5FG6"
FT HELIX 647..673
FT /evidence="ECO:0007829|PDB:5FG6"
FT HELIX 675..679
FT /evidence="ECO:0007829|PDB:5FG6"
FT STRAND 932..935
FT /evidence="ECO:0007829|PDB:4Z02"
FT STRAND 943..948
FT /evidence="ECO:0007829|PDB:4Z02"
FT STRAND 957..959
FT /evidence="ECO:0007829|PDB:7LH9"
FT HELIX 969..979
FT /evidence="ECO:0007829|PDB:4Z02"
FT STRAND 986..991
FT /evidence="ECO:0007829|PDB:4Z02"
FT STRAND 998..1002
FT /evidence="ECO:0007829|PDB:4Z02"
FT HELIX 1003..1005
FT /evidence="ECO:0007829|PDB:4Z02"
FT STRAND 1006..1011
FT /evidence="ECO:0007829|PDB:4Z02"
FT HELIX 1013..1020
FT /evidence="ECO:0007829|PDB:4Z02"
FT STRAND 1023..1025
FT /evidence="ECO:0007829|PDB:4Z02"
FT HELIX 1026..1046
FT /evidence="ECO:0007829|PDB:4Z02"
FT MOD_RES O95696-2:906
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
SQ SEQUENCE 1058 AA; 119520 MW; 6E7B07E8A030E104 CRC64;
MRRKGRCHRG SAARHPSSPC SVKHSPTRET LTYAQAQRMV EIEIEGRLHR ISIFDPLEII
LEDDLTAQEM SECNSNKENS ERPPVCLRTK RHKNNRVKKK NEALPSAHGT PASASALPEP
KVRIVEYSPP SAPRRPPVYY KFIEKSAEEL DNEVEYDMDE EDYAWLEIVN EKRKGDCVPA
VSQSMFEFLM DRFEKESHCE NQKQGEQQSL IDEDAVCCIC MDGECQNSNV ILFCDMCNLA
VHQECYGVPY IPEGQWLCRH CLQSRARPAD CVLCPNKGGA FKKTDDDRWG HVVCALWIPE
VGFANTVFIE PIDGVRNIPP ARWKLTCYLC KQKGVGACIQ CHKANCYTAF HVTCAQKAGL
YMKMEPVKEL TGGGTTFSVR KTAYCDVHTP PGCTRRPLNI YGDVEMKNGV CRKESSVKTV
RSTSKVRKKA KKAKKALAEP CAVLPTVCAP YIPPQRLNRI ANQVAIQRKK QFVERAHSYW
LLKRLSRNGA PLLRRLQSSL QSQRSSQQRE NDEEMKAAKE KLKYWQRLRH DLERARLLIE
LLRKREKLKR EQVKVEQVAM ELRLTPLTVL LRSVLDQLQD KDPARIFAQP VSLKEVPDYL
DHIKHPMDFA TMRKRLEAQG YKNLHEFEED FDLIIDNCMK YNARDTVFYR AAVRLRDQGG
VVLRQARREV DSIGLEEASG MHLPERPAAA PRRPFSWEDV DRLLDPANRA HLGLEEQLRE
LLDMLDLTCA MKSSGSRSKR AKLLKKEIAL LRNKLSQQHS QPLPTGPGLE GFEEDGAALG
PEAGEEVLPR LETLLQPRKR SRSTCGDSEV EEESPGKRLD AGLTNGFGGA RSEQEPGGGL
GRKATPRRRC ASESSISSSN SPLCDSSFNA PKCGRGKPAL VRRHTLEDRS ELISCIENGN
YAKAARIAAE VGQSSMWIST DAAASVLEPL KVVWAKCSGY PSYPALIIDP KMPRVPGHHN
GVTIPAPPLD VLKIGEHMQT KSDEKLFLVL FFDNKRSWQW LPKSKMVPLG IDETIDKLKM
MEGRNSSIRK AVRIAFDRAM NHLSRVHGEP TSDLSDID
