PB1_HUMAN
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 03-AUG-2022, entry version 179.
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 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 [22]
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 [23]
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 [24]
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 [25]
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 [26]
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 [27]
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 [28]
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:0000303|PubMed:22952240,
CC 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; CCDS2860.1; -. [Q86U86-5]
DR CCDS; CCDS43099.1; -. [Q86U86-4]
DR CCDS; CCDS87087.1; -. [Q86U86-2]
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. [Q86U86-1]
DR RefSeq; XP_016862238.1; XM_017006749.1. [Q86U86-1]
DR RefSeq; XP_016862239.1; XM_017006750.1. [Q86U86-1]
DR RefSeq; XP_016862246.1; XM_017006757.1.
DR RefSeq; XP_016862247.1; XM_017006758.1. [Q86U86-2]
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 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 AlphaFoldDB; Q86U86; -.
DR SMR; Q86U86; -.
DR BioGRID; 120490; 188.
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; 86.
DR MINT; Q86U86; -.
DR STRING; 9606.ENSP00000378307; -.
DR BindingDB; Q86U86; -.
DR ChEMBL; CHEMBL1795184; -.
DR GuidetoPHARMACOLOGY; 2738; -.
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 PeptideAtlas; Q86U86; -.
DR PRIDE; 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 ABCD; Q86U86; 1 sequenced antibody.
DR Antibodypedia; 2905; 188 antibodies from 29 providers.
DR DNASU; 55193; -.
DR Ensembl; ENST00000296302.11; ENSP00000296302.7; ENSG00000163939.18. [Q86U86-1]
DR Ensembl; ENST00000337303.8; ENSP00000338302.4; ENSG00000163939.18. [Q86U86-5]
DR Ensembl; ENST00000356770.8; ENSP00000349213.4; ENSG00000163939.18. [Q86U86-3]
DR Ensembl; ENST00000394830.7; ENSP00000378307.3; ENSG00000163939.18. [Q86U86-4]
DR Ensembl; ENST00000409057.5; ENSP00000386593.1; ENSG00000163939.18. [Q86U86-2]
DR Ensembl; ENST00000409114.7; ENSP00000386643.3; ENSG00000163939.18. [Q86U86-8]
DR Ensembl; ENST00000409767.5; ENSP00000386601.1; ENSG00000163939.18. [Q86U86-7]
DR Ensembl; ENST00000410007.5; ENSP00000386529.1; ENSG00000163939.18. [Q86U86-9]
DR Ensembl; ENST00000412587.5; ENSP00000404579.1; ENSG00000163939.18. [Q86U86-6]
DR GeneID; 55193; -.
DR KEGG; hsa:55193; -.
DR UCSC; uc003deq.3; human. [Q86U86-1]
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; PRKVYPD; -.
DR OrthoDB; 168080at2759; -.
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; 48 hits in 1128 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 215 other tissues.
DR ExpressionAtlas; Q86U86; baseline and differential.
DR Genevisible; Q86U86; HS.
DR GO; GO:0000785; C:chromatin; IC:ComplexPortal.
DR GO; GO:0000776; C:kinetochore; IC:ComplexPortal.
DR GO; GO:0000228; C:nuclear chromosome; NAS:UniProtKB.
DR GO; GO:0016363; C:nuclear matrix; IC:ComplexPortal.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
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; TAS:UniProtKB.
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; IC:ComplexPortal.
DR GO; GO:2000781; P:positive regulation of double-strand break repair; IC:ComplexPortal.
DR GO; GO:0045663; P:positive regulation of myoblast differentiation; IC:ComplexPortal.
DR GO; GO:0045582; P:positive regulation of T cell differentiation; IC:ComplexPortal.
DR GO; GO:0070316; P:regulation of G0 to G1 transition; IC:ComplexPortal.
DR GO; GO:2000045; P:regulation of G1/S transition of mitotic cell cycle; IC:ComplexPortal.
DR GO; GO:0030071; P:regulation of mitotic metaphase/anaphase transition; IC:ComplexPortal.
DR GO; GO:2000819; P:regulation of nucleotide-excision repair; IC:ComplexPortal.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IC:ComplexPortal.
DR CDD; cd05515; Bromo_polybromo_V; 1.
DR Gene3D; 1.20.920.10; -; 6.
DR Gene3D; 2.30.30.490; -; 2.
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; PTHR16062; 2.
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; SSF47095; SSF47095; 1.
DR SUPFAM; SSF47370; SSF47370; 6.
DR PROSITE; PS51038; BAH; 2.
DR PROSITE; PS00633; BROMODOMAIN_1; 5.
DR PROSITE; PS50014; BROMODOMAIN_2; 6.
DR PROSITE; PS50118; HMG_BOX_2; 1.
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 (requires 2 nucleotide substitutions; found
FT in a colon cancer cell line)"
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"
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
