ID PB1_HUMAN Reviewed; 1689 AA. AC Q86U86; A1L381; A1L382; A4FUJ7; Q1RMD1; Q1RMD2; Q96MS2; Q9H2T3; Q9H2T4; AC Q9H2T5; Q9H301; Q9H314; DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2003, sequence version 1. DT 27-MAR-2024, entry version 188. DE RecName: Full=Protein polybromo-1; DE Short=hPB1; DE AltName: Full=BRG1-associated factor 180; DE Short=BAF180; DE AltName: Full=Polybromo-1D; GN Name=PBRM1; Synonyms=BAF180, PB1; 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 4), IDENTIFICATION BY MASS RP SPECTROMETRY, AND IDENTIFICATION IN THE PBAF COMPLEX. RX PubMed=11078522; DOI=10.1073/pnas.240208597; RA Xue Y., Canman J.C., Lee C.S., Nie Z., Yang D., Moreno G.T., Young M.K., RA Salmon E.D., Wang W.; RT "The human SWI/SNF-B chromatin-remodeling complex is related to yeast rsc RT and localizes at kinetochores of mitotic chromosomes."; RL Proc. Natl. Acad. Sci. U.S.A. 97:13015-13020(2000). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3; 5 AND 6), AND TISSUE RP SPECIFICITY. RX PubMed=12487023; DOI=10.1080/1042517021000021590; RA Horikawa I., Barrett J.C.; RT "cDNA cloning of the human polybromo-1 gene on chromosome 3p21."; RL DNA Seq. 13:211-215(2002). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=15735765; DOI=10.1038/sj.onc.1207694; RA Sekine I., Sato M., Sunaga N., Toyooka S., Peyton M., Parsons R., Wang W., RA Gazdar A.F., Minna J.D.; RT "The 3p21 candidate tumor suppressor gene BAF180 is normally expressed in RT human lung cancer."; RL Oncogene 24:2735-2738(2005). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 4; 7; 8 AND 9). 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 57-1127 (ISOFORM 7). RC TISSUE=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., 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 [6] RP IDENTIFICATION IN THE PBAF COMPLEX, IDENTIFICATION IN A SWI/SNF COMPLEX, RP AND IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=11780067; DOI=10.1038/414924a; RA Lemon B., Inouye C., King D.S., Tjian R.; RT "Selectivity of chromatin-remodelling cofactors for ligand-activated RT transcription."; RL Nature 414:924-928(2001). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-39, 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1453, AND IDENTIFICATION BY RP 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 phosphorylation RT analysis and site localization."; RL Nat. Biotechnol. 24:1285-1292(2006). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10; SER-39; SER-131; SER-316; RP SER-319; SER-353; SER-355 AND SER-1405, 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 [10] 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., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10; SER-39; SER-353; SER-355; RP SER-371; SER-375; SER-498 AND SER-636, AND IDENTIFICATION BY MASS RP 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 [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-39; SER-353; SER-355; RP SER-636; SER-1405 AND SER-1453, AND IDENTIFICATION BY MASS SPECTROMETRY RP [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] 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., Buerckstuemmer T., RA 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 [14] RP FUNCTION AS NEGATIVE REGULATOR OF CELL PROLIFERATION, INVOLVEMENT IN RCC, RP AND VARIANTS LEU-49; ALA-56; ILE-57 DEL; GLY-66; GLU-90; PHE-144; ALA-160; RP CYS-202; LYS-206; GLY-226; VAL-228; PRO-232; THR-233; THR-256; ALA-340; RP ILE-523; SER-540; ASP-597; GLU-621; ASN-661; GLU-674; CYS-678; CYS-893; RP SER-895; GLN-922; GLN-925; TYR-1079; SER-1098; GLN-1120; SER-1177; RP PRO-1204; 1209-MET--GLU-1214 DEL; GLN-1287; GLU-1414; CYS-1503; HIS-1560; RP ASN-1614 AND CYS-1647. RX PubMed=21248752; DOI=10.1038/nature09639; RA Varela I., Tarpey P., Raine K., Huang D., Ong C.K., Stephens P., Davies H., RA Jones D., Lin M.L., Teague J., Bignell G., Butler A., Cho J., RA Dalgliesh G.L., Galappaththige D., Greenman C., Hardy C., Jia M., RA Latimer C., Lau K.W., Marshall J., McLaren S., Menzies A., Mudie L., RA Stebbings L., Largaespada D.A., Wessels L.F.A., Richard S., Kahnoski R.J., RA Anema J., Tuveson D.A., Perez-Mancera P.A., Mustonen V., Fischer A., RA Adams D.J., Rust A., Chan-On W., Subimerb C., Dykema K., Furge K., RA Campbell P.J., Teh B.T., Stratton M.R., Futreal P.A.; RT "Exome sequencing identifies frequent mutation of the SWI/SNF complex gene RT PBRM1 in renal carcinoma."; RL Nature 469:539-542(2011). RN [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-353; SER-355; SER-636; RP SER-648 AND SER-1453, 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., 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 TYR-134; SER-178; SER-498; RP SER-509; SER-636; SER-689; SER-948; SER-987; SER-1119 AND SER-1405, 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 [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-39 AND SER-948, AND 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., 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-1293, AND IDENTIFICATION BY MASS RP 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 [19] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-1293, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25114211; DOI=10.1073/pnas.1413825111; RA Impens F., Radoshevich L., Cossart P., Ribet D.; RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by RT external stimuli."; RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014). RN [20] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-1293, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033; RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V., RA Vertegaal A.C.; RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage."; RL Cell Rep. 10:1778-1791(2015). RN [21] RP SUBCELLULAR LOCATION. RX PubMed=25593309; DOI=10.1101/gad.252189.114; RA Gong F., Chiu L.Y., Cox B., Aymard F., Clouaire T., Leung J.W., RA Cammarata M., Perez M., Agarwal P., Brodbelt J.S., Legube G., Miller K.M.; RT "Screen identifies bromodomain protein ZMYND8 in chromatin recognition of RT transcription-associated DNA damage that promotes homologous RT recombination."; RL Genes Dev. 29:197-211(2015). RN [22] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-653; LYS-1293; LYS-1308 AND RP LYS-1398, AND 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 [23] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-96; LYS-154; LYS-210; LYS-425; RP LYS-471; LYS-511; LYS-591; LYS-638; LYS-653; LYS-1106; LYS-1111; LYS-1167; RP LYS-1293; LYS-1308; LYS-1398; LYS-1642; LYS-1654 AND LYS-1656, 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 [24] RP REVIEW ON SWI/SNF CHROMATIN-REMODELING COMPLEXES. RX PubMed=12672490; DOI=10.1016/s0959-437x(03)00022-4; RA Martens J.A., Winston F.; RT "Recent advances in understanding chromatin remodeling by SWI/SNF RT complexes."; RL Curr. Opin. Genet. Dev. 13:136-142(2003). RN [25] RP IDENTIFICATION IN THE PBAF COMPLEX. RX PubMed=15985610; DOI=10.1101/gad.1323805; RA Yan Z., Cui K., Murray D.M., Ling C., Xue Y., Gerstein A., Parsons R., RA Zhao K., Wang W.; RT "PBAF chromatin-remodeling complex requires a novel specificity subunit, RT BAF200, to regulate expression of selective interferon-responsive genes."; RL Genes Dev. 19:1662-1667(2005). RN [26] RP REVIEW ON SWI/SNF CHROMATIN REMODELING COMPLEXES. RX PubMed=22952240; DOI=10.1074/jbc.r111.309302; RA Euskirchen G., Auerbach R.K., Snyder M.; RT "SWI/SNF chromatin-remodeling factors: multiscale analyses and diverse RT functions."; RL J. Biol. Chem. 287:30897-30905(2012). RN [27] RP REVIEW ON SWI/SNF CHROMATIN REMODELING COMPLEXES. RX PubMed=26601204; DOI=10.1126/sciadv.1500447; RA Kadoch C., Crabtree G.R.; RT "Mammalian SWI/SNF chromatin remodeling complexes and cancer: Mechanistic RT insights gained from human genomics."; RL Sci. Adv. 1:E1500447-E1500447(2015). RN [28] RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 174-293, AND INTERACTION WITH RP ACETYLATED HISTONE H3. RX PubMed=20368734; DOI=10.1038/cr.2010.43; RA Charlop-Powers Z., Zeng L., Zhang Q., Zhou M.M.; RT "Structural insights into selective histone H3 recognition by the human RT polybromo bromodomain 2."; RL Cell Res. 20:529-538(2010). RN [29] RP X-RAY CRYSTALLOGRAPHY (1.63 ANGSTROMS) OF 43-917, AND INTERACTION WITH RP HISTONE H3. 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: Involved in transcriptional activation and repression of CC select genes by chromatin remodeling (alteration of DNA-nucleosome CC topology). Required for the stability of the SWI/SNF chromatin CC remodeling complex SWI/SNF-B (PBAF). Acts as a negative regulator of CC cell proliferation. {ECO:0000269|PubMed:21248752, CC ECO:0000303|PubMed:22952240, ECO:0000303|PubMed:26601204}. CC -!- SUBUNIT: Component of the SWI/SNF-B (PBAF) chromatin remodeling CC complex, at least composed of SMARCA4/BRG1, SMARCB1/BAF47/SNF5, CC ACTL6A/BAF53A or ACTL6B/BAF53B, SMARCE1/BAF57, SMARCD1/BAF60A, CC SMARCD2/BAF60B, perhaps SMARCD3/BAF60C, SMARCC1/BAF155, SMARCC2/BAF170, CC PBRM1/BAF180, ARID2/BAF200 and actin. Interacts with PHF10/BAF45A (By CC similarity). Interacts with acetylated 'Lys-14' of histone H3 CC (H3K14ac), and may also interact with other acetylated or methylated CC Lys residues on histone H3. {ECO:0000250|UniProtKB:Q8BSQ9, CC ECO:0000269|PubMed:11078522, ECO:0000269|PubMed:11780067, CC ECO:0000269|PubMed:15985610, ECO:0000269|PubMed:20368734, CC ECO:0000269|PubMed:22464331, ECO:0000303|PubMed:22952240, CC ECO:0000303|PubMed:26601204}. CC -!- INTERACTION: CC Q86U86; Q68CP9: ARID2; NbExp=5; IntAct=EBI-637807, EBI-637818; CC Q86U86; O95696-1: BRD1; NbExp=2; IntAct=EBI-637807, EBI-11700916; CC Q86U86; O95696-2: BRD1; NbExp=2; IntAct=EBI-637807, EBI-11017508; CC Q86U86; Q9P2D1: CHD7; NbExp=4; IntAct=EBI-637807, EBI-3951683; CC Q86U86; P51532: SMARCA4; NbExp=6; IntAct=EBI-637807, EBI-302489; CC Q86U86; P04608: tat; Xeno; NbExp=2; IntAct=EBI-637807, EBI-6164389; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:25593309, CC ECO:0000303|PubMed:22952240, ECO:0000303|PubMed:26601204}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=9; CC Name=1; CC IsoId=Q86U86-1; Sequence=Displayed; CC Name=2; CC IsoId=Q86U86-2; Sequence=VSP_015235; CC Name=3; CC IsoId=Q86U86-3; Sequence=VSP_015231, VSP_015235; CC Name=4; CC IsoId=Q86U86-4; Sequence=VSP_015233, VSP_015234, VSP_015235; CC Name=5; CC IsoId=Q86U86-5; Sequence=VSP_015235, VSP_015236; CC Name=6; CC IsoId=Q86U86-6; Sequence=VSP_015232; CC Name=7; CC IsoId=Q86U86-7; Sequence=VSP_035499, VSP_015235, VSP_015236; CC Name=8; CC IsoId=Q86U86-8; Sequence=VSP_035499, VSP_015236; CC Name=9; CC IsoId=Q86U86-9; Sequence=VSP_015233, VSP_015235; CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:12487023}. CC -!- DISEASE: Renal cell carcinoma (RCC) [MIM:144700]: Renal cell carcinoma CC is a heterogeneous group of sporadic or hereditary carcinoma derived CC from cells of the proximal renal tubular epithelium. It is CC subclassified into clear cell renal carcinoma (non-papillary CC carcinoma), papillary renal cell carcinoma, chromophobe renal cell CC carcinoma, collecting duct carcinoma with medullary carcinoma of the CC kidney, and unclassified renal cell carcinoma. Clear cell renal cell CC carcinoma is the most common subtype. {ECO:0000269|PubMed:21248752}. CC Note=The disease is caused by variants affecting the gene represented CC in this entry. CC -!- SEQUENCE CAUTION: CC Sequence=AAI15010.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence.; Evidence={ECO:0000305}; CC Sequence=AAI15011.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC Sequence=AAI15012.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305}; CC Sequence=BAB71210.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF197569; AAG34760.1; -; mRNA. DR EMBL; AF225870; AAG48939.1; -; mRNA. DR EMBL; AF225871; AAG48940.1; -; mRNA. DR EMBL; AF225872; AAG48941.1; -; mRNA. DR EMBL; AF177387; AAG48933.1; -; mRNA. DR EMBL; AY281068; AAP34197.1; -; mRNA. DR EMBL; BC115009; AAI15010.1; ALT_TERM; mRNA. DR EMBL; BC115010; AAI15011.1; ALT_INIT; mRNA. DR EMBL; BC115011; AAI15012.1; ALT_SEQ; mRNA. DR EMBL; BC129934; AAI29935.1; -; mRNA. DR EMBL; BC129935; AAI29936.1; -; mRNA. DR EMBL; AK056541; BAB71210.1; ALT_INIT; mRNA. DR CCDS; CCDS2859.1; -. [Q86U86-3] DR CCDS; CCDS2860.1; -. [Q86U86-5] DR CCDS; CCDS43099.1; -. [Q86U86-4] DR CCDS; CCDS87087.1; -. [Q86U86-2] DR CCDS; CCDS93285.1; -. [Q86U86-9] DR CCDS; CCDS93286.1; -. [Q86U86-1] DR RefSeq; NP_060783.3; NM_018313.4. [Q86U86-4] DR RefSeq; NP_851385.1; NM_181042.4. [Q86U86-5] DR RefSeq; XP_016862237.1; XM_017006748.1. DR RefSeq; XP_016862238.1; XM_017006749.1. DR RefSeq; XP_016862239.1; XM_017006750.1. DR RefSeq; XP_016862246.1; XM_017006757.1. DR RefSeq; XP_016862247.1; XM_017006758.1. DR PDB; 2KTB; NMR; -; B=174-293. DR PDB; 3G0J; X-ray; 1.78 A; A/B=645-766. DR PDB; 3HMF; X-ray; 1.63 A; A=178-291. DR PDB; 3IU5; X-ray; 1.63 A; A=43-154. DR PDB; 3IU6; X-ray; 1.79 A; A=773-914. DR PDB; 3K2J; X-ray; 2.20 A; A/B=388-494. DR PDB; 3LJW; X-ray; 1.50 A; A/B=174-293. DR PDB; 3MB4; X-ray; 1.66 A; A/B=645-766. DR PDB; 3TLP; X-ray; 2.13 A; A/B=496-637. DR PDB; 4Q0N; X-ray; 1.78 A; A/B/C/D/E/F/G/H=645-766. DR PDB; 4Q0O; X-ray; 1.83 A; A=645-766. DR PDB; 4Y03; X-ray; 1.94 A; A/B=645-766. DR PDB; 5E7D; X-ray; 1.87 A; A/B/C/D=645-766. DR PDB; 5FH6; X-ray; 2.30 A; A/B/C/D=645-766. DR PDB; 5FH7; X-ray; 1.47 A; A/B=645-766. DR PDB; 5FH8; X-ray; 1.55 A; A/B/C/D=645-766. DR PDB; 5HRV; X-ray; 1.70 A; A=645-766. DR PDB; 5HRW; X-ray; 1.80 A; A/B=645-766. DR PDB; 5HRX; X-ray; 1.73 A; A/B=645-766. DR PDB; 5II1; X-ray; 2.02 A; A/B=645-766. DR PDB; 5II2; X-ray; 2.10 A; A/B=645-766. DR PDB; 5IID; X-ray; 2.40 A; A/B=645-766. DR PDB; 6OXB; X-ray; 1.86 A; A/B/C/D/E/F=934-1105. DR PDB; 6ZN6; X-ray; 2.02 A; A/B=178-291. DR PDB; 6ZNV; X-ray; 1.14 A; A=178-291. DR PDB; 6ZS3; X-ray; 1.67 A; A/B=645-766. DR PDB; 6ZS4; X-ray; 2.00 A; A=645-766. DR PDB; 7VDV; EM; 3.40 A; a=631-1689. DR PDB; 7Y8R; EM; 4.40 A; U=1-1689. DR PDBsum; 2KTB; -. DR PDBsum; 3G0J; -. DR PDBsum; 3HMF; -. DR PDBsum; 3IU5; -. DR PDBsum; 3IU6; -. DR PDBsum; 3K2J; -. DR PDBsum; 3LJW; -. DR PDBsum; 3MB4; -. DR PDBsum; 3TLP; -. DR PDBsum; 4Q0N; -. DR PDBsum; 4Q0O; -. DR PDBsum; 4Y03; -. DR PDBsum; 5E7D; -. DR PDBsum; 5FH6; -. DR PDBsum; 5FH7; -. DR PDBsum; 5FH8; -. DR PDBsum; 5HRV; -. DR PDBsum; 5HRW; -. DR PDBsum; 5HRX; -. DR PDBsum; 5II1; -. DR PDBsum; 5II2; -. DR PDBsum; 5IID; -. DR PDBsum; 6OXB; -. DR PDBsum; 6ZN6; -. DR PDBsum; 6ZNV; -. DR PDBsum; 6ZS3; -. DR PDBsum; 6ZS4; -. DR PDBsum; 7VDV; -. DR PDBsum; 7Y8R; -. DR AlphaFoldDB; Q86U86; -. DR EMDB; EMD-31926; -. DR EMDB; EMD-33684; -. DR SMR; Q86U86; -. DR BioGRID; 120490; 249. 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; Q86U86; -. DR DIP; DIP-33045N; -. DR IntAct; Q86U86; 87. DR MINT; Q86U86; -. DR STRING; 9606.ENSP00000386593; -. DR BindingDB; Q86U86; -. DR ChEMBL; CHEMBL1795184; -. DR GuidetoPHARMACOLOGY; 2738; -. DR GlyGen; Q86U86; 3 sites, 1 O-linked glycan (3 sites). DR iPTMnet; Q86U86; -. DR MetOSite; Q86U86; -. DR PhosphoSitePlus; Q86U86; -. DR SwissPalm; Q86U86; -. DR BioMuta; PBRM1; -. DR DMDM; 73921624; -. DR CPTAC; CPTAC-1362; -. DR EPD; Q86U86; -. DR jPOST; Q86U86; -. DR MassIVE; Q86U86; -. DR MaxQB; Q86U86; -. DR PaxDb; 9606-ENSP00000378307; -. DR PeptideAtlas; Q86U86; -. DR ProteomicsDB; 69774; -. [Q86U86-1] DR ProteomicsDB; 69775; -. [Q86U86-2] DR ProteomicsDB; 69776; -. [Q86U86-3] DR ProteomicsDB; 69777; -. [Q86U86-4] DR ProteomicsDB; 69778; -. [Q86U86-5] DR ProteomicsDB; 69779; -. [Q86U86-6] DR ProteomicsDB; 69780; -. [Q86U86-7] DR ProteomicsDB; 69781; -. [Q86U86-8] DR ProteomicsDB; 69782; -. [Q86U86-9] DR Pumba; Q86U86; -. DR ABCD; Q86U86; 1 sequenced antibody. DR Antibodypedia; 2905; 214 antibodies from 29 providers. DR DNASU; 55193; -. DR Ensembl; ENST00000296302.11; ENSP00000296302.7; ENSG00000163939.19. [Q86U86-1] DR Ensembl; ENST00000337303.8; ENSP00000338302.4; ENSG00000163939.19. [Q86U86-5] DR Ensembl; ENST00000356770.8; ENSP00000349213.4; ENSG00000163939.19. [Q86U86-3] DR Ensembl; ENST00000394830.7; ENSP00000378307.3; ENSG00000163939.19. [Q86U86-4] DR Ensembl; ENST00000409057.5; ENSP00000386593.1; ENSG00000163939.19. [Q86U86-2] DR Ensembl; ENST00000409114.7; ENSP00000386643.3; ENSG00000163939.19. [Q86U86-8] DR Ensembl; ENST00000409767.5; ENSP00000386601.1; ENSG00000163939.19. [Q86U86-7] DR Ensembl; ENST00000410007.5; ENSP00000386529.1; ENSG00000163939.19. [Q86U86-9] DR Ensembl; ENST00000412587.5; ENSP00000404579.1; ENSG00000163939.19. [Q86U86-6] DR GeneID; 55193; -. DR KEGG; hsa:55193; -. DR UCSC; uc003deq.3; human. [Q86U86-1] DR AGR; HGNC:30064; -. DR CTD; 55193; -. DR DisGeNET; 55193; -. DR GeneCards; PBRM1; -. DR HGNC; HGNC:30064; PBRM1. DR HPA; ENSG00000163939; Low tissue specificity. DR MalaCards; PBRM1; -. DR MIM; 144700; phenotype. DR MIM; 606083; gene. DR neXtProt; NX_Q86U86; -. DR OpenTargets; ENSG00000163939; -. DR Orphanet; 404511; Clear cell papillary renal cell carcinoma. DR PharmGKB; PA162398846; -. DR VEuPathDB; HostDB:ENSG00000163939; -. DR eggNOG; KOG1827; Eukaryota. DR GeneTree; ENSGT00390000003017; -. DR HOGENOM; CLU_001483_1_0_1; -. DR InParanoid; Q86U86; -. DR OMA; WQFYETL; -. DR OrthoDB; 2878065at2759; -. DR PhylomeDB; Q86U86; -. DR TreeFam; TF106120; -. DR PathwayCommons; Q86U86; -. DR Reactome; R-HSA-3214858; RMTs methylate histone arginines. DR Reactome; R-HSA-8939243; RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not known. DR SignaLink; Q86U86; -. DR SIGNOR; Q86U86; -. DR BioGRID-ORCS; 55193; 56 hits in 1215 CRISPR screens. DR ChiTaRS; PBRM1; human. DR EvolutionaryTrace; Q86U86; -. DR GeneWiki; PBRM1; -. DR GenomeRNAi; 55193; -. DR Pharos; Q86U86; Tchem. DR PRO; PR:Q86U86; -. DR Proteomes; UP000005640; Chromosome 3. DR RNAct; Q86U86; Protein. DR Bgee; ENSG00000163939; Expressed in cortical plate and 217 other cell types or tissues. DR ExpressionAtlas; Q86U86; baseline and differential. DR GO; GO:0000785; C:chromatin; NAS:ComplexPortal. DR GO; GO:0000776; C:kinetochore; NAS:ComplexPortal. DR GO; GO:0000228; C:nuclear chromosome; NAS:UniProtKB. DR GO; GO:0016363; C:nuclear matrix; NAS: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; IBA:GO_Central. DR GO; GO:0016514; C:SWI/SNF complex; IDA:BHF-UCL. DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0006338; P:chromatin remodeling; IBA:GO_Central. DR GO; GO:0000278; P:mitotic cell cycle; TAS:UniProtKB. DR GO; GO:0008285; P:negative regulation of cell population proliferation; IMP:UniProtKB. DR GO; GO:0045597; P:positive regulation of cell differentiation; NAS:ComplexPortal. DR GO; GO:2000781; P:positive regulation of double-strand break repair; NAS:ComplexPortal. DR GO; GO:0045663; P:positive regulation of myoblast differentiation; NAS:ComplexPortal. DR GO; GO:0045582; P:positive regulation of T cell differentiation; NAS:ComplexPortal. DR GO; GO:0070316; P:regulation of G0 to G1 transition; NAS:ComplexPortal. DR GO; GO:2000045; P:regulation of G1/S transition of mitotic cell cycle; NAS:ComplexPortal. DR GO; GO:0030071; P:regulation of mitotic metaphase/anaphase transition; NAS:ComplexPortal. DR GO; GO:2000819; P:regulation of nucleotide-excision repair; NAS:ComplexPortal. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; NAS:ComplexPortal. DR GO; GO:0006368; P:transcription elongation by RNA polymerase II; IBA:GO_Central. DR CDD; cd04717; BAH_polybromo; 2. DR CDD; cd05524; Bromo_polybromo_I; 1. DR CDD; cd05517; Bromo_polybromo_II; 1. DR CDD; cd05520; Bromo_polybromo_III; 1. DR CDD; cd05518; Bromo_polybromo_IV; 1. DR CDD; cd05515; Bromo_polybromo_V; 1. DR CDD; cd05526; Bromo_polybromo_VI; 1. DR CDD; cd21984; HMG-box_PB1; 1. DR Gene3D; 2.30.30.490; -; 2. DR Gene3D; 1.20.920.10; Bromodomain-like; 6. DR InterPro; IPR001025; BAH_dom. DR InterPro; IPR043151; BAH_sf. DR InterPro; IPR001487; Bromodomain. DR InterPro; IPR036427; Bromodomain-like_sf. DR InterPro; IPR018359; Bromodomain_CS. DR InterPro; IPR009071; HMG_box_dom. DR InterPro; IPR036910; HMG_box_dom_sf. DR InterPro; IPR037968; PBRM1_BD5. DR InterPro; IPR037382; Rsc/polybromo. DR PANTHER; PTHR16062:SF19; PROTEIN POLYBROMO-1; 1. DR PANTHER; PTHR16062; SWI/SNF-RELATED; 1. DR Pfam; PF01426; BAH; 2. DR Pfam; PF00439; Bromodomain; 6. DR Pfam; PF00505; HMG_box; 1. DR PRINTS; PR00503; BROMODOMAIN. DR SMART; SM00439; BAH; 2. DR SMART; SM00297; BROMO; 6. DR SMART; SM00398; HMG; 1. DR SUPFAM; SSF47370; Bromodomain; 6. DR SUPFAM; SSF47095; HMG-box; 1. DR PROSITE; PS51038; BAH; 2. DR PROSITE; PS00633; BROMODOMAIN_1; 5. DR PROSITE; PS50014; BROMODOMAIN_2; 6. DR PROSITE; PS50118; HMG_BOX_2; 1. DR Genevisible; Q86U86; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Bromodomain; KW Chromatin regulator; DNA-binding; Isopeptide bond; Nucleus; Phosphoprotein; KW Reference proteome; Repeat; Transcription; Transcription regulation; KW Tumor suppressor; Ubl conjugation. FT CHAIN 1..1689 FT /note="Protein polybromo-1" FT /id="PRO_0000211207" FT DOMAIN 64..134 FT /note="Bromo 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035" FT DOMAIN 200..270 FT /note="Bromo 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035" FT DOMAIN 400..470 FT /note="Bromo 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035" FT DOMAIN 538..608 FT /note="Bromo 4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035" FT DOMAIN 676..746 FT /note="Bromo 5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035" FT DOMAIN 792..862 FT /note="Bromo 6" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035" FT DOMAIN 956..1074 FT /note="BAH 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00370" FT DOMAIN 1156..1272 FT /note="BAH 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00370" FT DNA_BIND 1379..1447 FT /note="HMG box" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00267" FT REGION 1..39 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 155..177 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 487..517 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 625..646 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 902..941 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1106..1133 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1354..1378 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1431..1460 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1..21 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 625..639 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 902..933 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 10 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332" FT MOD_RES 39 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:24275569" FT MOD_RES 131 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 134 FT /note="Phosphotyrosine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 178 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 316 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 319 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 353 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692" FT MOD_RES 355 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692" FT MOD_RES 371 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332" FT MOD_RES 375 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332" FT MOD_RES 414 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q8BSQ9" FT MOD_RES 498 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:23186163" FT MOD_RES 509 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 636 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT MOD_RES 648 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692" FT MOD_RES 689 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 948 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 987 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1119 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1289 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:Q8BSQ9" FT MOD_RES 1405 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163" FT MOD_RES 1453 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:16964243, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692" FT CROSSLNK 96 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 154 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 210 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 425 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 471 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 511 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 591 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 638 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 653 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 1106 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 1111 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 1167 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 1293 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO1); alternate" FT /evidence="ECO:0007744|PubMed:25114211" FT CROSSLNK 1293 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0007744|PubMed:25114211, FT ECO:0007744|PubMed:25218447, ECO:0007744|PubMed:25755297, FT ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733" FT CROSSLNK 1308 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 1398 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 1642 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 1654 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 1656 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT VAR_SEQ 300..332 FT /note="RTPSNLAAARLTGPSHSKGSLGEERNPTSKYYR -> S (in isoform FT 3)" FT /evidence="ECO:0000303|PubMed:12487023" FT /id="VSP_015231" FT VAR_SEQ 513 FT /note="K -> KRNTHDSEMLGLRRLS (in isoform 7 and isoform 8)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15489334" FT /id="VSP_035499" FT VAR_SEQ 857..1689 FT /note="Missing (in isoform 6)" FT /evidence="ECO:0000303|PubMed:12487023" FT /id="VSP_015232" FT VAR_SEQ 989..1013 FT /note="Missing (in isoform 4 and isoform 9)" FT /evidence="ECO:0000303|PubMed:11078522, FT ECO:0000303|PubMed:15489334" FT /id="VSP_015233" FT VAR_SEQ 1336..1362 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:11078522, FT ECO:0000303|PubMed:15489334" FT /id="VSP_015234" FT VAR_SEQ 1430..1484 FT /note="Missing (in isoform 2, isoform 3, isoform 4, isoform FT 5, isoform 7 and isoform 9)" FT /evidence="ECO:0000303|PubMed:11078522, FT ECO:0000303|PubMed:12487023, ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15489334" FT /id="VSP_015235" FT VAR_SEQ 1485..1536 FT /note="Missing (in isoform 5, isoform 7 and isoform 8)" FT /evidence="ECO:0000303|PubMed:12487023, FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15489334" FT /id="VSP_015236" FT VARIANT 49 FT /note="V -> L (found in a lung cancer cell line)" FT /evidence="ECO:0000269|PubMed:21248752" FT /id="VAR_064653" FT VARIANT 56 FT /note="T -> A (found in a brain cancer cell line; FT dbSNP:rs923060956)" FT /evidence="ECO:0000269|PubMed:21248752" FT /id="VAR_064654" FT VARIANT 57 FT /note="Missing (found in a case of clear cell renal FT carcinoma; somatic mutation)" FT /evidence="ECO:0000269|PubMed:21248752" FT /id="VAR_064655" FT VARIANT 66 FT /note="R -> G (found in a colon cancer cell line; FT dbSNP:rs368888772)" FT /evidence="ECO:0000269|PubMed:21248752" FT /id="VAR_064656" FT VARIANT 90 FT /note="Q -> E (found in a bladder cancer cell line)" FT /evidence="ECO:0000269|PubMed:21248752" FT /id="VAR_064657" FT VARIANT 144 FT /note="Y -> F (found in a malignant melanoma cell line)" FT /evidence="ECO:0000269|PubMed:21248752" FT /id="VAR_064658" FT VARIANT 160 FT /note="E -> A (found in a malignant melanoma cell line)" FT /evidence="ECO:0000269|PubMed:21248752" FT /id="VAR_064659" FT VARIANT 202 FT /note="R -> C (found in a endometrial cancer cell line; FT dbSNP:rs765525545)" FT /evidence="ECO:0000269|PubMed:21248752" FT /id="VAR_064660" FT VARIANT 206 FT /note="E -> K (found in hematopoietic and lymphoid cancer FT cell lines; dbSNP:rs1359676390)" FT /evidence="ECO:0000269|PubMed:21248752" FT /id="VAR_064661" FT VARIANT 226 FT /note="E -> G (found in hematopoietic and lymphoid cancer FT cell lines)" FT /evidence="ECO:0000269|PubMed:21248752" FT /id="VAR_064662" FT VARIANT 228 FT /note="I -> V (found in a breast cancer cell line; FT dbSNP:rs201022657)" FT /evidence="ECO:0000269|PubMed:21248752" FT /id="VAR_064663" FT VARIANT 232 FT /note="T -> P (found in a case of clear cell renal FT carcinoma; somatic mutation)" FT /evidence="ECO:0000269|PubMed:21248752" FT /id="VAR_064664" FT VARIANT 233 FT /note="I -> T (found in a renal carcinoma cell line)" FT /evidence="ECO:0000269|PubMed:21248752" FT /id="VAR_064665" FT VARIANT 256 FT /note="A -> T (found in an ovary carcinoma cell line; FT dbSNP:rs776146971)" FT /evidence="ECO:0000269|PubMed:21248752" FT /id="VAR_064666" FT VARIANT 340 FT /note="G -> A (found in a malignant melanoma cell line; FT dbSNP:rs200106731)" FT /evidence="ECO:0000269|PubMed:21248752" FT /id="VAR_064667" FT VARIANT 523 FT /note="M -> I (found in a case of clear cell renal FT carcinoma; somatic mutation)" FT /evidence="ECO:0000269|PubMed:21248752" FT /id="VAR_064668" FT VARIANT 540 FT /note="R -> S (found in a case of clear cell renal FT carcinoma; somatic mutation)" FT /evidence="ECO:0000269|PubMed:21248752" FT /id="VAR_064669" FT VARIANT 597 FT /note="A -> D (found in a case of clear cell renal FT carcinoma; somatic mutation)" FT /evidence="ECO:0000269|PubMed:21248752" FT /id="VAR_064670" FT VARIANT 621 FT /note="K -> E (found in a case of clear cell renal FT carcinoma; somatic mutation)" FT /evidence="ECO:0000269|PubMed:21248752" FT /id="VAR_064671" FT VARIANT 661 FT /note="K -> N (found in a case of clear cell renal FT carcinoma; somatic mutation)" FT /evidence="ECO:0000269|PubMed:21248752" FT /id="VAR_064672" FT VARIANT 674 FT /note="D -> E (found in a case of clear cell renal FT carcinoma; somatic mutation)" FT /evidence="ECO:0000269|PubMed:21248752" FT /id="VAR_064673" FT VARIANT 678 FT /note="R -> C (in dbSNP:rs1422119249)" FT /evidence="ECO:0000269|PubMed:21248752" FT /id="VAR_064674" FT VARIANT 893 FT /note="Y -> C (found in hematopoietic, lymphoid, lung and FT liver cancer cell lines; dbSNP:rs753344888)" FT /evidence="ECO:0000269|PubMed:21248752" FT /id="VAR_064675" FT VARIANT 895 FT /note="T -> S (found in a lung cancer cell line)" FT /evidence="ECO:0000269|PubMed:21248752" FT /id="VAR_064676" FT VARIANT 922 FT /note="E -> Q (found in a breast cancer cell line)" FT /evidence="ECO:0000269|PubMed:21248752" FT /id="VAR_064677" FT VARIANT 925 FT /note="K -> Q (found in a colon cancer cell line)" FT /evidence="ECO:0000269|PubMed:21248752" FT /id="VAR_064678" FT VARIANT 1079 FT /note="P -> Y (found in a colon cancer cell line; requires FT 2 nucleotide substitutions)" FT /evidence="ECO:0000269|PubMed:21248752" FT /id="VAR_064679" FT VARIANT 1098 FT /note="A -> S (found in hematopoietic and lymphoid cancer FT cell lines; dbSNP:rs201156614)" FT /evidence="ECO:0000269|PubMed:21248752" FT /id="VAR_064680" FT VARIANT 1120 FT /note="R -> Q (found in hematopoietic and lymphoid cancer FT cell lines; dbSNP:rs35102895)" FT /evidence="ECO:0000269|PubMed:21248752" FT /id="VAR_064681" FT VARIANT 1177 FT /note="G -> S (found in a kidney cancer cell line)" FT /evidence="ECO:0000269|PubMed:21248752" FT /id="VAR_064682" FT VARIANT 1204 FT /note="H -> P (found in a case of clear cell renal FT carcinoma; somatic mutation)" FT /evidence="ECO:0000269|PubMed:21248752" FT /id="VAR_064683" FT VARIANT 1209..1214 FT /note="Missing (found in a case of clear cell renal FT carcinoma; somatic mutation)" FT /evidence="ECO:0000269|PubMed:21248752" FT /id="VAR_064684" FT VARIANT 1287 FT /note="E -> Q (found in a breast cancer cell line)" FT /evidence="ECO:0000269|PubMed:21248752" FT /id="VAR_064685" FT VARIANT 1414 FT /note="G -> E (found in a lung cancer cell line)" FT /evidence="ECO:0000269|PubMed:21248752" FT /id="VAR_064686" FT VARIANT 1503 FT /note="G -> C (found in a stomach cancer cell line)" FT /evidence="ECO:0000269|PubMed:21248752" FT /id="VAR_064687" FT VARIANT 1560 FT /note="Q -> H (found in an endometrial cancer cell line)" FT /evidence="ECO:0000269|PubMed:21248752" FT /id="VAR_064688" FT VARIANT 1614 FT /note="I -> N (found in a case of clear cell renal FT carcinoma; somatic mutation)" FT /evidence="ECO:0000269|PubMed:21248752" FT /id="VAR_064689" FT VARIANT 1647 FT /note="R -> C (found in a breast cancer cell line; FT dbSNP:rs200020801)" FT /evidence="ECO:0000269|PubMed:21248752" FT /id="VAR_064690" FT CONFLICT 1 FT /note="M -> T (in Ref. 4; AAI15011)" FT /evidence="ECO:0000305" FT CONFLICT 65 FT /note="G -> S (in Ref. 4; AAI15011)" FT /evidence="ECO:0000305" FT CONFLICT 242 FT /note="Y -> C (in Ref. 4; AAI15012)" FT /evidence="ECO:0000305" FT CONFLICT 251 FT /note="D -> V (in Ref. 4; AAI15011)" FT /evidence="ECO:0000305" FT CONFLICT 430 FT /note="L -> P (in Ref. 4; AAI15012)" FT /evidence="ECO:0000305" FT CONFLICT 553 FT /note="K -> R (in Ref. 1; AAG34760)" FT /evidence="ECO:0000305" FT CONFLICT 567 FT /note="D -> Y (in Ref. 4; AAI15012)" FT /evidence="ECO:0000305" FT CONFLICT 750 FT /note="L -> P (in Ref. 4; AAI15012)" FT /evidence="ECO:0000305" FT CONFLICT 792 FT /note="H -> R (in Ref. 4; AAI15012)" FT /evidence="ECO:0000305" FT CONFLICT 927 FT /note="Missing (in Ref. 4; AAI15010 and 5; BAB71210)" FT /evidence="ECO:0000305" FT CONFLICT 963 FT /note="Y -> H (in Ref. 5; BAB71210)" FT /evidence="ECO:0000305" FT CONFLICT 1144 FT /note="G -> V (in Ref. 1; AAG34760)" FT /evidence="ECO:0000305" FT CONFLICT 1245 FT /note="R -> K (in Ref. 1; AAG34760)" FT /evidence="ECO:0000305" FT CONFLICT 1306 FT /note="E -> G (in Ref. 1; AAG34760)" FT /evidence="ECO:0000305" FT CONFLICT 1349 FT /note="L -> P (in Ref. 4; AAI15010)" FT /evidence="ECO:0000305" FT CONFLICT 1488 FT /note="G -> D (in Ref. 4; AAI15012)" FT /evidence="ECO:0000305" FT CONFLICT 1568 FT /note="G -> R (in Ref. 1; AAG34760)" FT /evidence="ECO:0000305" FT HELIX 46..59 FT /evidence="ECO:0007829|PDB:3IU5" FT HELIX 68..72 FT /evidence="ECO:0007829|PDB:3IU5" FT HELIX 78..80 FT /evidence="ECO:0007829|PDB:3IU5" FT HELIX 82..87 FT /evidence="ECO:0007829|PDB:3IU5" FT HELIX 94..102 FT /evidence="ECO:0007829|PDB:3IU5" FT HELIX 109..126 FT /evidence="ECO:0007829|PDB:3IU5" FT HELIX 132..152 FT /evidence="ECO:0007829|PDB:3IU5" FT STRAND 176..178 FT /evidence="ECO:0007829|PDB:2KTB" FT HELIX 179..195 FT /evidence="ECO:0007829|PDB:6ZNV" FT HELIX 206..208 FT /evidence="ECO:0007829|PDB:6ZNV" FT TURN 214..216 FT /evidence="ECO:0007829|PDB:6ZNV" FT HELIX 218..223 FT /evidence="ECO:0007829|PDB:6ZNV" FT HELIX 230..239 FT /evidence="ECO:0007829|PDB:6ZNV" FT HELIX 245..262 FT /evidence="ECO:0007829|PDB:6ZNV" FT HELIX 268..289 FT /evidence="ECO:0007829|PDB:6ZNV" FT HELIX 388..394 FT /evidence="ECO:0007829|PDB:3K2J" FT STRAND 399..401 FT /evidence="ECO:0007829|PDB:3K2J" FT HELIX 406..408 FT /evidence="ECO:0007829|PDB:3K2J" FT TURN 414..416 FT /evidence="ECO:0007829|PDB:3K2J" FT HELIX 418..423 FT /evidence="ECO:0007829|PDB:3K2J" FT HELIX 430..438 FT /evidence="ECO:0007829|PDB:3K2J" FT HELIX 445..462 FT /evidence="ECO:0007829|PDB:3K2J" FT HELIX 468..490 FT /evidence="ECO:0007829|PDB:3K2J" FT HELIX 511..532 FT /evidence="ECO:0007829|PDB:3TLP" FT TURN 536..538 FT /evidence="ECO:0007829|PDB:3TLP" FT HELIX 542..546 FT /evidence="ECO:0007829|PDB:3TLP" FT TURN 552..554 FT /evidence="ECO:0007829|PDB:3TLP" FT HELIX 556..561 FT /evidence="ECO:0007829|PDB:3TLP" FT HELIX 568..576 FT /evidence="ECO:0007829|PDB:3TLP" FT HELIX 583..600 FT /evidence="ECO:0007829|PDB:3TLP" FT HELIX 606..625 FT /evidence="ECO:0007829|PDB:3TLP" FT HELIX 657..671 FT /evidence="ECO:0007829|PDB:5FH7" FT HELIX 680..684 FT /evidence="ECO:0007829|PDB:5FH7" FT TURN 690..692 FT /evidence="ECO:0007829|PDB:5FH7" FT HELIX 696..699 FT /evidence="ECO:0007829|PDB:5FH7" FT STRAND 700..702 FT /evidence="ECO:0007829|PDB:3G0J" FT HELIX 706..714 FT /evidence="ECO:0007829|PDB:5FH7" FT HELIX 721..738 FT /evidence="ECO:0007829|PDB:5FH7" FT HELIX 744..762 FT /evidence="ECO:0007829|PDB:5FH7" FT TURN 763..765 FT /evidence="ECO:0007829|PDB:5FH7" FT HELIX 777..790 FT /evidence="ECO:0007829|PDB:3IU6" FT HELIX 800..804 FT /evidence="ECO:0007829|PDB:3IU6" FT HELIX 822..830 FT /evidence="ECO:0007829|PDB:3IU6" FT HELIX 837..854 FT /evidence="ECO:0007829|PDB:3IU6" FT HELIX 860..882 FT /evidence="ECO:0007829|PDB:3IU6" FT HELIX 889..892 FT /evidence="ECO:0007829|PDB:3IU6" FT HELIX 895..909 FT /evidence="ECO:0007829|PDB:3IU6" FT HELIX 910..913 FT /evidence="ECO:0007829|PDB:3IU6" FT STRAND 945..953 FT /evidence="ECO:0007829|PDB:6OXB" FT STRAND 956..959 FT /evidence="ECO:0007829|PDB:6OXB" FT STRAND 963..966 FT /evidence="ECO:0007829|PDB:6OXB" FT STRAND 969..972 FT /evidence="ECO:0007829|PDB:6OXB" FT STRAND 976..979 FT /evidence="ECO:0007829|PDB:6OXB" FT STRAND 982..986 FT /evidence="ECO:0007829|PDB:6OXB" FT STRAND 991..999 FT /evidence="ECO:0007829|PDB:6OXB" FT HELIX 1001..1003 FT /evidence="ECO:0007829|PDB:6OXB" FT STRAND 1011..1013 FT /evidence="ECO:0007829|PDB:6OXB" FT STRAND 1016..1027 FT /evidence="ECO:0007829|PDB:6OXB" FT HELIX 1028..1030 FT /evidence="ECO:0007829|PDB:6OXB" FT STRAND 1031..1039 FT /evidence="ECO:0007829|PDB:6OXB" FT HELIX 1040..1043 FT /evidence="ECO:0007829|PDB:6OXB" FT STRAND 1046..1048 FT /evidence="ECO:0007829|PDB:6OXB" FT HELIX 1053..1055 FT /evidence="ECO:0007829|PDB:6OXB" FT STRAND 1056..1064 FT /evidence="ECO:0007829|PDB:6OXB" FT TURN 1065..1068 FT /evidence="ECO:0007829|PDB:6OXB" FT STRAND 1069..1072 FT /evidence="ECO:0007829|PDB:6OXB" FT STRAND 1085..1087 FT /evidence="ECO:0007829|PDB:6OXB" FT STRAND 1096..1098 FT /evidence="ECO:0007829|PDB:6OXB" FT HELIX 1602..1615 FT /evidence="ECO:0007829|PDB:7VDV" FT HELIX 1627..1632 FT /evidence="ECO:0007829|PDB:7VDV" FT HELIX 1643..1646 FT /evidence="ECO:0007829|PDB:7VDV" FT HELIX 1650..1652 FT /evidence="ECO:0007829|PDB:7VDV" FT HELIX 1663..1678 FT /evidence="ECO:0007829|PDB:7VDV" SQ SEQUENCE 1689 AA; 192948 MW; 0A656E319C4FC748 CRC64; MGSKRRRATS PSSSVSGDFD DGHHSVSTPG PSRKRRRLSN LPTVDPIAVC HELYNTIRDY KDEQGRLLCE LFIRAPKRRN QPDYYEVVSQ PIDLMKIQQK LKMEEYDDVN LLTADFQLLF NNAKSYYKPD SPEYKAACKL WDLYLRTRNE FVQKGEADDE DDDEDGQDNQ GTVTEGSSPA YLKEILEQLL EAIVVATNPS GRLISELFQK LPSKVQYPDY YAIIKEPIDL KTIAQRIQNG SYKSIHAMAK DIDLLAKNAK TYNEPGSQVF KDANSIKKIF YMKKAEIEHH EMAKSSLRMR TPSNLAAARL TGPSHSKGSL GEERNPTSKY YRNKRAVQGG RLSAITMALQ YGSESEEDAA LAAARYEEGE SEAESITSFM DVSNPFYQLY DTVRSCRNNQ GQLIAEPFYH LPSKKKYPDY YQQIKMPISL QQIRTKLKNQ EYETLDHLEC DLNLMFENAK RYNVPNSAIY KRVLKLQQVM QAKKKELARR DDIEDGDSMI SSATSDTGSA KRKSKKNIRK QRMKILFNVV LEAREPGSGR RLCDLFMVKP SKKDYPDYYK IILEPMDLKI IEHNIRNDKY AGEEGMIEDM KLMFRNARHY NEEGSQVYND AHILEKLLKE KRKELGPLPD DDDMASPKLK LSRKSGISPK KSKYMTPMQQ KLNEVYEAVK NYTDKRGRRL SAIFLRLPSR SELPDYYLTI KKPMDMEKIR SHMMANKYQD IDSMVEDFVM MFNNACTYNE PESLIYKDAL VLHKVLLETR RDLEGDEDSH VPNVTLLIQE LIHNLFVSVM SHQDDEGRCY SDSLAEIPAV DPNFPNKPPL TFDIIRKNVE NNRYRRLDLF QEHMFEVLER ARRMNRTDSE IYEDAVELQQ FFIKIRDELC KNGEILLSPA LSYTTKHLHN DVEKERKEKL PKEIEEDKLK REEEKREAEK SEDSSGAAGL SGLHRTYSQD CSFKNSMYHV GDYVYVEPAE ANLQPHIVCI ERLWEDSAGE KWLYGCWFYR PNETFHLATR KFLEKEVFKS DYYNKVPVSK ILGKCVVMFV KEYFKLCPEN FRDEDVFVCE SRYSAKTKSF KKIKLWTMPI SSVRFVPRDV PLPVVRVASV FANADKGDDE KNTDNSEDSR AEDNFNLEKE KEDVPVEMSN GEPGCHYFEQ LHYNDMWLKV GDCVFIKSHG LVRPRVGRIE KVWVRDGAAY FYGPIFIHPE ETEHEPTKMF YKKEVFLSNL EETCPMTCIL GKCAVLSFKD FLSCRPTEIP ENDILLCESR YNESDKQMKK FKGLKRFSLS AKVVDDEIYY FRKPIVPQKE PSPLLEKKIQ LLEAKFAELE GGDDDIEEMG EEDSEVIEPP SLPQLQTPLA SELDLMPYTP PQSTPKSAKG SAKKEGSKRK INMSGYILFS SEMRAVIKAQ HPDYSFGELS RLVGTEWRNL ETAKKAEYEE RAAKVAEQQE RERAAQQQQP SASPRAGTPV GALMGVVPPP TPMGMLNQQL TPVAGMMGGY PPGLPPLQGP VDGLVSMGSM QPLHPGGPPP HHLPPGVPGL PGIPPPGVMN QGVAPMVGTP APGGSPYGQQ VGVLGPPGQQ APPPYPGPHP AGPPVIQQPT TPMFVAPPPK TQRLLHSEAY LKYIEGLSAE SNSISKWDQT LAARRRDVHL SKEQESRLPS HWLKSKGAHT TMADALWRLR DLMLRDTLNI RQAYNLENV //