UIMC1_HUMAN
ID UIMC1_HUMAN Reviewed; 719 AA.
AC Q96RL1; A8MSA1; B3KMZ1; B4E3N2; Q5XKQ1; Q7Z3W7; Q8N5B9; Q9BZR1; Q9BZR5;
AC Q9UHX7;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 2.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=BRCA1-A complex subunit RAP80;
DE AltName: Full=Receptor-associated protein 80;
DE AltName: Full=Retinoid X receptor-interacting protein 110;
DE AltName: Full=Ubiquitin interaction motif-containing protein 1;
GN Name=UIMC1; Synonyms=RAP80, RXRIP110;
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 1), FUNCTION IN TRANSCRIPTIONAL
RP REPRESSION, INTERACTION WITH NR6A1, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Testis;
RX PubMed=12080054; DOI=10.1074/jbc.m203475200;
RA Yan Z., Kim Y.-S., Jetten A.M.;
RT "RAP80: a novel nuclear protein that interacts with the retinoid-related
RT testis-associated receptor.";
RL J. Biol. Chem. 277:32379-32388(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
RC TISSUE=Hypothalamus;
RA Peng Y., Gu Y., Gu J., Huang Q., Fu S., Wu T., Dong H., Jin W., Fu G.,
RA Han Z., Chen Z., Wang Y.;
RT "A novel gene expressed in the human hypothalamus.";
RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 4).
RC TISSUE=Hypothalamus;
RA Xu X., Yang Y., Gao G., Xiao H., Chen Z., Han Z.;
RL Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 5).
RC TISSUE=Teratocarcinoma, and Uterus;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Esophageal carcinoma;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Ovary, and Skin;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-44 AND SER-46, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [9]
RP SUMOYLATION, INTERACTION WITH UBE2I, AND MUTAGENESIS OF LYS-9; LYS-19;
RP LYS-31; LYS-52 AND LYS-61.
RX PubMed=17698038; DOI=10.1016/j.bbrc.2007.07.158;
RA Yan J., Yang X.-P., Kim Y.-S., Joo J.H., Jetten A.M.;
RT "RAP80 interacts with the SUMO-conjugating enzyme UBC9 and is a novel
RT target for sumoylation.";
RL Biochem. Biophys. Res. Commun. 362:132-138(2007).
RN [10]
RP FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF ALA-88 AND ALA-113, AND
RP PHOSPHORYLATION AT SER-205 AND SER-402.
RX PubMed=17621610; DOI=10.1158/0008-5472.can-07-0924;
RA Yan J., Kim Y.S., Yang X.-P., Li L.-P., Liao G., Xia F., Jetten A.M.;
RT "The ubiquitin-interacting motif containing protein RAP80 interacts with
RT BRCA1 and functions in DNA damage repair response.";
RL Cancer Res. 67:6647-6656(2007).
RN [11]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH ABRAXAS1.
RX PubMed=17643121; DOI=10.1038/nsmb1279;
RA Liu Z., Wu J., Yu X.;
RT "CCDC98 targets BRCA1 to DNA damage sites.";
RL Nat. Struct. Mol. Biol. 14:716-720(2007).
RN [12]
RP INTERACTION WITH ABRAXAS1.
RX PubMed=17643122; DOI=10.1038/nsmb1277;
RA Kim H., Huang J., Chen J.;
RT "CCDC98 is a BRCA1-BRCT domain-binding protein involved in the DNA damage
RT response.";
RL Nat. Struct. Mol. Biol. 14:710-715(2007).
RN [13]
RP INTERACTION WITH ESR1.
RX PubMed=17311814; DOI=10.1093/nar/gkl1112;
RA Yan J., Kim Y.S., Yang X.-P., Albers M., Koegl M., Jetten A.M.;
RT "Ubiquitin-interaction motifs of RAP80 are critical in its regulation of
RT estrogen receptor alpha.";
RL Nucleic Acids Res. 35:1673-1686(2007).
RN [14]
RP INTERACTION WITH ABRAXAS1.
RX PubMed=18077395; DOI=10.1073/pnas.0710061104;
RA Wang B., Elledge S.J.;
RT "Ubc13/Rnf8 ubiquitin ligases control foci formation of the
RT Rap80/Abraxas/Brca1/Brcc36 complex in response to DNA damage.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:20759-20763(2007).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [16]
RP FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-140; SER-402 AND
RP SER-419, AND MUTAGENESIS OF ALA-88; SER-92; ALA-113 AND SER-117.
RX PubMed=17525340; DOI=10.1126/science.1139476;
RA Wang B., Matsuoka S., Ballif B.A., Zhang D., Smogorzewska A., Giyi S.,
RA Elledge S.J.;
RT "Abraxas and RAP80 form a BRCA1 protein complex required for the DNA damage
RT response.";
RL Science 316:1194-1198(2007).
RN [17]
RP FUNCTION, IDENTIFICATION IN THE BRCA1-A COMPLEX, SUBCELLULAR LOCATION,
RP UBIQUITIN-BINDING, AND PHOSPHORYLATION AT SER-101.
RX PubMed=17525341; DOI=10.1126/science.1139516;
RA Sobhian B., Shao G., Lilli D.R., Culhane A.C., Moreau L.A., Xia B.,
RA Livingston D.M., Greenberg R.A.;
RT "RAP80 targets BRCA1 to specific ubiquitin structures at DNA damage
RT sites.";
RL Science 316:1198-1202(2007).
RN [18]
RP FUNCTION, IDENTIFICATION IN THE BRCA1-A COMPLEX, SUBCELLULAR LOCATION,
RP UBIQUITIN-BINDING, PHOSPHORYLATION AT SER-101, AND MUTAGENESIS OF ALA-88;
RP SER-92; ALA-113 AND SER-117.
RX PubMed=17525342; DOI=10.1126/science.1139621;
RA Kim H., Chen J., Yu X.;
RT "Ubiquitin-binding protein RAP80 mediates BRCA1-dependent DNA damage
RT response.";
RL Science 316:1202-1205(2007).
RN [19]
RP PHOSPHORYLATION AT SER-205, AND MUTAGENESIS OF SER-205.
RX PubMed=18519686; DOI=10.1158/0008-5472.can-07-5950;
RA Yan J., Yang X.-P., Kim Y.-S., Jetten A.M.;
RT "RAP80 responds to DNA damage induced by both ionizing radiation and UV
RT irradiation and is phosphorylated at Ser 205.";
RL Cancer Res. 68:4269-4276(2008).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-627; SER-653 AND SER-677, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [21]
RP IDENTIFICATION IN THE BRCA1-A COMPLEX.
RX PubMed=19261746; DOI=10.1101/gad.1739609;
RA Shao G., Patterson-Fortin J., Messick T.E., Feng D., Shanbhag N., Wang Y.,
RA Greenberg R.A.;
RT "MERIT40 controls BRCA1-Rap80 complex integrity and recruitment to DNA
RT double-strand breaks.";
RL Genes Dev. 23:740-754(2009).
RN [22]
RP IDENTIFICATION IN THE BRCA1-A COMPLEX, UBIQUITIN-BINDING, AND INTERACTION
RP WITH ABRAXAS1.
RX PubMed=19261749; DOI=10.1101/gad.1770309;
RA Wang B., Hurov K., Hofmann K., Elledge S.J.;
RT "NBA1, a new player in the Brca1 A complex, is required for DNA damage
RT resistance and checkpoint control.";
RL Genes Dev. 23:729-739(2009).
RN [23]
RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE
RP BRCA1-A COMPLEX, AND INTERACTION WITH ABRAXAS1.
RX PubMed=19261748; DOI=10.1101/gad.1770609;
RA Feng L., Huang J., Chen J.;
RT "MERIT40 facilitates BRCA1 localization and DNA damage repair.";
RL Genes Dev. 23:719-728(2009).
RN [24]
RP FUNCTION IN UBIQUITIN-BINDING, DOMAIN UIM-LINKER, AND MUTAGENESIS OF
RP 97-ARG--GLU-103 AND SER-101.
RX PubMed=19328070; DOI=10.1016/j.molcel.2009.02.011;
RA Sims J.J., Cohen R.E.;
RT "Linkage-specific avidity defines the lysine 63-linked polyubiquitin-
RT binding preference of rap80.";
RL Mol. Cell 33:775-783(2009).
RN [25]
RP FUNCTION, AND MUTAGENESIS OF CYS-508.
RX PubMed=19015238; DOI=10.1128/mcb.01302-08;
RA Wu J., Huen M.S.Y., Lu L.-Y., Ye L., Dou Y., Ljungman M., Chen J., Yu X.;
RT "Histone ubiquitination associates with BRCA1-dependent DNA damage
RT response.";
RL Mol. Cell. Biol. 29:849-860(2009).
RN [26]
RP FUNCTION.
RX PubMed=19202061; DOI=10.1073/pnas.0807485106;
RA Shao G., Lilli D.R., Patterson-Fortin J., Coleman K.A., Morrissey D.E.,
RA Greenberg R.A.;
RT "The Rap80-BRCC36 de-ubiquitinating enzyme complex antagonizes RNF8-Ubc13-
RT dependent ubiquitination events at DNA double strand breaks.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:3166-3171(2009).
RN [27]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-44, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [28]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-44; SER-46 AND SER-677, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [29]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-677, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [30]
RP UBIQUITIN-BINDING, AND LR MOTIF.
RX PubMed=22742833; DOI=10.1016/j.molcel.2012.05.045;
RA Panier S., Ichijima Y., Fradet-Turcotte A., Leung C.C., Kaustov L.,
RA Arrowsmith C.H., Durocher D.;
RT "Tandem protein interaction modules organize the ubiquitin-dependent
RT response to DNA double-strand breaks.";
RL Mol. Cell 47:383-395(2012).
RN [31]
RP IDENTIFICATION IN THE ARISC COMPLEX.
RX PubMed=24075985; DOI=10.1016/j.celrep.2013.08.025;
RA Zheng H., Gupta V., Patterson-Fortin J., Bhattacharya S., Katlinski K.,
RA Wu J., Varghese B., Carbone C.J., Aressy B., Fuchs S.Y., Greenberg R.A.;
RT "A BRISC-SHMT complex deubiquitinates IFNAR1 and regulates interferon
RT responses.";
RL Cell Rep. 5:180-193(2013).
RN [32]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29; SER-101; SER-140;
RP SER-466; SER-627; SER-653 AND SER-677, AND IDENTIFICATION BY MASS
RP 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 [33]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-20; LYS-31; LYS-382; LYS-544;
RP LYS-562 AND LYS-607, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [34]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-20, 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 [35]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-607, AND IDENTIFICATION BY MASS
RP 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 [36]
RP INTERACTION WITH TRAIP.
RX PubMed=26781088; DOI=10.1038/ncomms10463;
RA Soo Lee N., Jin Chung H., Kim H.J., Yun Lee S., Ji J.H., Seo Y.,
RA Hun Han S., Choi M., Yun M., Lee S.G., Myung K., Kim Y., Chul Kang H.,
RA Kim H.;
RT "TRAIP/RNF206 is required for recruitment of RAP80 to sites of DNA
RT damage.";
RL Nat. Commun. 7:10463-10463(2016).
RN [37]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-20; LYS-31; LYS-75; LYS-90;
RP LYS-188; LYS-245; LYS-382; LYS-387; LYS-428; LYS-544; LYS-559; LYS-587;
RP LYS-607; LYS-635; LYS-642; LYS-696 AND LYS-697, AND IDENTIFICATION BY MASS
RP 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 [38]
RP STRUCTURE BY NMR OF 79-124, FUNCTION IN UBIQUITIN BINDING, AND DOMAIN.
RA Sekiyama N., Jee J., Isogai S., Akagi K., Huang T., Ariyoshi M., Tochio H.,
RA Shirakawa M.;
RT "The solution structure of the K63-Ub2:tUIMs complex.";
RL Submitted (JUN-2010) to the PDB data bank.
RN [39]
RP STRUCTURE BY NMR OF 74-131, MUTAGENESIS OF GLU-81, FUNCTION IN UBIQUITIN
RP BINDING, AND DOMAIN.
RX PubMed=24627472; DOI=10.1074/jbc.m113.538280;
RA Anamika X., Markin C.J., Rout M.K., Spyracopoulos L.;
RT "Molecular basis for impaired DNA damage response function associated with
RT the RAP80 E81 defect.";
RL J. Biol. Chem. 289:12852-12862(2014).
RN [40]
RP VARIANTS TRP-15; THR-353; LEU-435 AND ARG-511.
RX PubMed=18695986; DOI=10.1007/s10549-008-0134-y;
RA Novak D.J., Sabbaghian N., Maillet P., Chappuis P.O., Foulkes W.D.,
RA Tischkowitz M.;
RT "Analysis of the genes coding for the BRCA1-interacting proteins, RAP80 and
RT Abraxas (CCDC98), in high-risk, non-BRCA1/2, multiethnic breast cancer
RT cases.";
RL Breast Cancer Res. Treat. 117:453-459(2009).
CC -!- FUNCTION: Ubiquitin-binding protein (PubMed:24627472). Specifically
CC recognizes and binds 'Lys-63'-linked ubiquitin (PubMed:19328070,
CC Ref.38). Plays a central role in the BRCA1-A complex by specifically
CC binding 'Lys-63'-linked ubiquitinated histones H2A and H2AX at DNA
CC lesions sites, leading to target the BRCA1-BARD1 heterodimer to sites
CC of DNA damage at double-strand breaks (DSBs). The BRCA1-A complex also
CC possesses deubiquitinase activity that specifically removes 'Lys-63'-
CC linked ubiquitin on histones H2A and H2AX. Also weakly binds
CC monoubiquitin but with much less affinity than 'Lys-63'-linked
CC ubiquitin. May interact with monoubiquitinated histones H2A and H2B;
CC the relevance of such results is however unclear in vivo. Does not bind
CC Lys-48'-linked ubiquitin. May indirectly act as a transcriptional
CC repressor by inhibiting the interaction of NR6A1 with the corepressor
CC NCOR1. {ECO:0000269|PubMed:12080054, ECO:0000269|PubMed:17525340,
CC ECO:0000269|PubMed:17525341, ECO:0000269|PubMed:17525342,
CC ECO:0000269|PubMed:17621610, ECO:0000269|PubMed:17643121,
CC ECO:0000269|PubMed:19015238, ECO:0000269|PubMed:19202061,
CC ECO:0000269|PubMed:19261748, ECO:0000269|PubMed:19328070,
CC ECO:0000269|PubMed:24627472, ECO:0000269|Ref.38}.
CC -!- SUBUNIT: Component of the ARISC complex, at least composed of
CC UIMC1/RAP80, ABRAXAS1, BRCC3/BRCC36, BABAM2 and BABAM1/NBA1
CC (PubMed:24075985). Component of the BRCA1-A complex, at least composed
CC of the BRCA1, BARD1, UIMC1/RAP80, ABRAXAS1, BRCC3/BRCC36, BABAM2 and
CC BABAM1/NBA1 (PubMed:17525341, PubMed:17525342, PubMed:19261746,
CC PubMed:19261749). In the BRCA1-A complex, interacts directly with
CC ABRAXAS1 (PubMed:17643121, PubMed:17643122, PubMed:19261749,
CC PubMed:19261748, PubMed:18077395). Interacts with UBE2I
CC (PubMed:17698038). Interacts with NR6A1 (PubMed:12080054). Interacts
CC with ESR1 (PubMed:17311814). Interacts with TSP57 (By similarity).
CC Interacts with TRAIP (PubMed:26781088). {ECO:0000250|UniProtKB:Q5U5Q9,
CC ECO:0000269|PubMed:12080054, ECO:0000269|PubMed:17311814,
CC ECO:0000269|PubMed:17525341, ECO:0000269|PubMed:17525342,
CC ECO:0000269|PubMed:17643121, ECO:0000269|PubMed:17643122,
CC ECO:0000269|PubMed:17698038, ECO:0000269|PubMed:18077395,
CC ECO:0000269|PubMed:19261746, ECO:0000269|PubMed:19261748,
CC ECO:0000269|PubMed:19261749, ECO:0000269|PubMed:24075985,
CC ECO:0000269|PubMed:26781088}.
CC -!- INTERACTION:
CC Q96RL1; Q6UWZ7: ABRAXAS1; NbExp=9; IntAct=EBI-725300, EBI-1263451;
CC Q96RL1; P54132: BLM; NbExp=2; IntAct=EBI-725300, EBI-621372;
CC Q96RL1; P38398: BRCA1; NbExp=10; IntAct=EBI-725300, EBI-349905;
CC Q96RL1; O14641: DVL2; NbExp=4; IntAct=EBI-725300, EBI-740850;
CC Q96RL1-1; Q6UWZ7: ABRAXAS1; NbExp=4; IntAct=EBI-9640371, EBI-1263451;
CC Q96RL1-1; P38398: BRCA1; NbExp=2; IntAct=EBI-9640371, EBI-349905;
CC Q96RL1-1; P46736: BRCC3; NbExp=4; IntAct=EBI-9640371, EBI-750352;
CC Q96RL1-2; Q14203-5: DCTN1; NbExp=3; IntAct=EBI-17761788, EBI-25840379;
CC Q96RL1-2; O60260-5: PRKN; NbExp=3; IntAct=EBI-17761788, EBI-21251460;
CC Q96RL1-2; P54725: RAD23A; NbExp=3; IntAct=EBI-17761788, EBI-746453;
CC Q96RL1-2; Q9Y3C5: RNF11; NbExp=3; IntAct=EBI-17761788, EBI-396669;
CC Q96RL1-2; P37840: SNCA; NbExp=3; IntAct=EBI-17761788, EBI-985879;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12080054,
CC ECO:0000269|PubMed:17525340, ECO:0000269|PubMed:17525341,
CC ECO:0000269|PubMed:17525342, ECO:0000269|PubMed:17621610,
CC ECO:0000269|PubMed:17643121}. Note=Localizes at sites of DNA damage at
CC double-strand breaks (DSBs).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q96RL1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96RL1-2; Sequence=VSP_012935;
CC Name=3; Synonyms=XHRIP110;
CC IsoId=Q96RL1-3; Sequence=VSP_012932;
CC Name=4; Synonyms=X2HRIP110;
CC IsoId=Q96RL1-4; Sequence=VSP_012933, VSP_012934;
CC Name=5;
CC IsoId=Q96RL1-5; Sequence=VSP_037264, VSP_037265;
CC -!- TISSUE SPECIFICITY: Expressed in testis, ovary, thymus and heart.
CC Expressed in germ cells of the testis. {ECO:0000269|PubMed:12080054}.
CC -!- DOMAIN: The tandem UIM domains form a continuous 60 Angstrom-long
CC alpha-helix and mediate binding to 'Lys-63'-linked ubiquitins. UIM1 and
CC UIM2 bind to the proximal and distal ubiquitin moieties and recognize
CC an 'Ile-44'-centered hydrophobic patch. Since UIMs don't interact with
CC the 'Lys-63' isopeptide bond the UIM-linker region between the 2 UIM
CC domains determines the selectivity for 'Lys-63'-linkage, and its length
CC is very important for specificity. {ECO:0000250|UniProtKB:Q5U5Q9,
CC ECO:0000269|PubMed:19328070, ECO:0000269|PubMed:24627472,
CC ECO:0000269|Ref.38}.
CC -!- DOMAIN: The Abraxas-interacting region (AIR) mediates the interaction
CC with ABRAXAS1. {ECO:0000269|PubMed:19328070}.
CC -!- PTM: Sumoylated. {ECO:0000269|PubMed:17698038}.
CC -!- PTM: Phosphorylated upon DNA damage by ATM or ATR.
CC {ECO:0000269|PubMed:17525340, ECO:0000269|PubMed:17525341,
CC ECO:0000269|PubMed:17525342, ECO:0000269|PubMed:17621610,
CC ECO:0000269|PubMed:18519686}.
CC -!- SIMILARITY: Belongs to the RAP80 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH06078.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
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DR EMBL; AF349313; AAK61871.1; -; mRNA.
DR EMBL; AF113538; AAF14875.1; -; mRNA.
DR EMBL; AF284749; AAG59851.1; -; mRNA.
DR EMBL; AF284753; AAG59855.1; -; mRNA.
DR EMBL; AK023044; BAG51153.1; -; mRNA.
DR EMBL; AK304794; BAG65544.1; -; mRNA.
DR EMBL; BX537376; CAD97618.1; -; mRNA.
DR EMBL; AC027318; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC006078; AAH06078.1; ALT_TERM; mRNA.
DR EMBL; BC032561; AAH32561.1; -; mRNA.
DR CCDS; CCDS4408.1; -. [Q96RL1-1]
DR CCDS; CCDS83050.1; -. [Q96RL1-2]
DR RefSeq; NP_001186226.1; NM_001199297.2. [Q96RL1-1]
DR RefSeq; NP_001186227.1; NM_001199298.1. [Q96RL1-1]
DR RefSeq; NP_001304890.1; NM_001317961.1. [Q96RL1-2]
DR RefSeq; NP_057374.3; NM_016290.4. [Q96RL1-1]
DR RefSeq; XP_005265987.1; XM_005265930.2. [Q96RL1-1]
DR RefSeq; XP_005265993.1; XM_005265936.2. [Q96RL1-4]
DR RefSeq; XP_006714934.1; XM_006714871.2. [Q96RL1-1]
DR RefSeq; XP_016865063.1; XM_017009574.1. [Q96RL1-3]
DR RefSeq; XP_016865067.1; XM_017009578.1. [Q96RL1-4]
DR RefSeq; XP_016865068.1; XM_017009579.1. [Q96RL1-4]
DR PDB; 2MKF; NMR; -; A=74-131.
DR PDB; 2MKG; NMR; -; A=74-131.
DR PDB; 2N9E; NMR; -; A=37-49.
DR PDB; 2RR9; NMR; -; C=79-124.
DR PDBsum; 2MKF; -.
DR PDBsum; 2MKG; -.
DR PDBsum; 2N9E; -.
DR PDBsum; 2RR9; -.
DR AlphaFoldDB; Q96RL1; -.
DR SMR; Q96RL1; -.
DR BioGRID; 119697; 98.
DR ComplexPortal; CPX-4425; BRCA1-A complex.
DR CORUM; Q96RL1; -.
DR DIP; DIP-29936N; -.
DR IntAct; Q96RL1; 64.
DR MINT; Q96RL1; -.
DR STRING; 9606.ENSP00000366434; -.
DR iPTMnet; Q96RL1; -.
DR MetOSite; Q96RL1; -.
DR PhosphoSitePlus; Q96RL1; -.
DR BioMuta; UIMC1; -.
DR DMDM; 60390957; -.
DR EPD; Q96RL1; -.
DR jPOST; Q96RL1; -.
DR MassIVE; Q96RL1; -.
DR MaxQB; Q96RL1; -.
DR PaxDb; Q96RL1; -.
DR PeptideAtlas; Q96RL1; -.
DR PRIDE; Q96RL1; -.
DR ProteomicsDB; 77977; -. [Q96RL1-1]
DR ProteomicsDB; 77978; -. [Q96RL1-2]
DR ProteomicsDB; 77979; -. [Q96RL1-3]
DR ProteomicsDB; 77980; -. [Q96RL1-4]
DR ProteomicsDB; 77981; -. [Q96RL1-5]
DR Antibodypedia; 29168; 276 antibodies from 35 providers.
DR DNASU; 51720; -.
DR Ensembl; ENST00000377227.8; ENSP00000366434.4; ENSG00000087206.17. [Q96RL1-1]
DR Ensembl; ENST00000506128.5; ENSP00000427480.1; ENSG00000087206.17. [Q96RL1-2]
DR Ensembl; ENST00000510698.2; ENSP00000423717.2; ENSG00000087206.17. [Q96RL1-4]
DR Ensembl; ENST00000511320.6; ENSP00000421926.1; ENSG00000087206.17. [Q96RL1-1]
DR GeneID; 51720; -.
DR KEGG; hsa:51720; -.
DR MANE-Select; ENST00000511320.6; ENSP00000421926.1; NM_001199298.2; NP_001186227.1.
DR UCSC; uc063kam.1; human. [Q96RL1-1]
DR CTD; 51720; -.
DR DisGeNET; 51720; -.
DR GeneCards; UIMC1; -.
DR HGNC; HGNC:30298; UIMC1.
DR HPA; ENSG00000087206; Low tissue specificity.
DR MIM; 609433; gene.
DR neXtProt; NX_Q96RL1; -.
DR OpenTargets; ENSG00000087206; -.
DR PharmGKB; PA162408624; -.
DR VEuPathDB; HostDB:ENSG00000087206; -.
DR eggNOG; ENOG502QQGN; Eukaryota.
DR GeneTree; ENSGT00390000007635; -.
DR HOGENOM; CLU_023109_1_0_1; -.
DR InParanoid; Q96RL1; -.
DR OMA; PMQIAQS; -.
DR PhylomeDB; Q96RL1; -.
DR TreeFam; TF336575; -.
DR PathwayCommons; Q96RL1; -.
DR Reactome; R-HSA-5689901; Metalloprotease DUBs.
DR Reactome; R-HSA-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
DR Reactome; R-HSA-5693571; Nonhomologous End-Joining (NHEJ).
DR Reactome; R-HSA-5693607; Processing of DNA double-strand break ends.
DR Reactome; R-HSA-69473; G2/M DNA damage checkpoint.
DR SignaLink; Q96RL1; -.
DR SIGNOR; Q96RL1; -.
DR BioGRID-ORCS; 51720; 21 hits in 1084 CRISPR screens.
DR ChiTaRS; UIMC1; human.
DR EvolutionaryTrace; Q96RL1; -.
DR GeneWiki; UIMC1; -.
DR GenomeRNAi; 51720; -.
DR Pharos; Q96RL1; Tbio.
DR PRO; PR:Q96RL1; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q96RL1; protein.
DR Bgee; ENSG00000087206; Expressed in left testis and 184 other tissues.
DR ExpressionAtlas; Q96RL1; baseline and differential.
DR Genevisible; Q96RL1; HS.
DR GO; GO:0070531; C:BRCA1-A complex; IDA:UniProtKB.
DR GO; GO:0016604; C:nuclear body; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0042393; F:histone binding; IDA:UniProtKB.
DR GO; GO:0070530; F:K63-linked polyubiquitin modification-dependent protein binding; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0006302; P:double-strand break repair; IMP:UniProtKB.
DR GO; GO:0070537; P:histone H2A K63-linked deubiquitination; IMP:UniProtKB.
DR GO; GO:0007095; P:mitotic G2 DNA damage checkpoint signaling; IMP:UniProtKB.
DR GO; GO:0044818; P:mitotic G2/M transition checkpoint; IC:ComplexPortal.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:HGNC-UCL.
DR GO; GO:0045739; P:positive regulation of DNA repair; IMP:UniProtKB.
DR GO; GO:0006282; P:regulation of DNA repair; IC:ComplexPortal.
DR GO; GO:0010212; P:response to ionizing radiation; IMP:UniProtKB.
DR InterPro; IPR006642; Rad18_UBZ4.
DR InterPro; IPR038868; RAP80.
DR InterPro; IPR040714; RAP80_UIM.
DR InterPro; IPR003903; UIM_dom.
DR PANTHER; PTHR15932; PTHR15932; 1.
DR Pfam; PF18282; RAP80_UIM; 1.
DR SMART; SM00726; UIM; 2.
DR PROSITE; PS50330; UIM; 1.
DR PROSITE; PS51908; ZF_UBZ4; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Chromatin regulator; DNA damage;
KW DNA repair; Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Transcription; Transcription regulation;
KW Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..719
FT /note="BRCA1-A complex subunit RAP80"
FT /id="PRO_0000097547"
FT DOMAIN 80..99
FT /note="UIM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00213"
FT DOMAIN 105..124
FT /note="UIM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00213"
FT ZN_FING 502..529
FT /note="UBZ4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
FT REGION 1..101
FT /note="Necessary for transcriptional repression"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 43..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 93..152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 97..103
FT /note="UIM-linker"
FT REGION 100..200
FT /note="Necessary for interaction with NR6A1 N-terminus"
FT REGION 164..205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 270..400
FT /note="AIR"
FT REGION 320..378
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 391..422
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 400..500
FT /note="Necessary for interaction with NR6A1 C-terminus"
FT REGION 505..582
FT /note="Zinc-finger-like region"
FT REGION 588..668
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 60..78
FT /note="LR motif"
FT COMPBIAS 43..60
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 120..152
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 172..192
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 358..378
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 394..422
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 610..641
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 505
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
FT BINDING 508
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
FT BINDING 520
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
FT BINDING 524
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
FT MOD_RES 29
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 44
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231"
FT MOD_RES 46
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 101
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17525341,
FT ECO:0000269|PubMed:17525342, ECO:0007744|PubMed:23186163"
FT MOD_RES 140
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17525340,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 205
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17621610,
FT ECO:0000269|PubMed:18519686"
FT MOD_RES 379
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5PQK4"
FT MOD_RES 402
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17525340,
FT ECO:0000269|PubMed:17621610"
FT MOD_RES 419
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17525340"
FT MOD_RES 466
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 627
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 653
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 677
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT CROSSLNK 20
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733"
FT CROSSLNK 31
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 75
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 90
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 188
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 245
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 382
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 387
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 428
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 544
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 559
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 562
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447"
FT CROSSLNK 587
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 607
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:28112733"
FT CROSSLNK 635
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 642
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 696
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 697
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..370
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|Ref.2, ECO:0000303|Ref.3"
FT /id="VSP_012933"
FT VAR_SEQ 1..78
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_012932"
FT VAR_SEQ 120..152
FT /note="SCRPSDASATRSRPLATGPSSQSHQEKTTDSGL -> VNMPCCKSLWRLISY
FT IFDFCGVVVALGTSCSHL (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_037264"
FT VAR_SEQ 153..719
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_037265"
FT VAR_SEQ 234..399
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_012935"
FT VAR_SEQ 371..400
FT /note="SKTKDFQESSIKSLKEKLLLEEEPTTSHGQ -> MLPLPDLDLWPLDRLPSP
FT IKRKPQTLGSLK (in isoform 4)"
FT /evidence="ECO:0000303|Ref.2, ECO:0000303|Ref.3"
FT /id="VSP_012934"
FT VARIANT 15
FT /note="R -> W (not associated with susceptibility to breast
FT cancer; dbSNP:rs13167812)"
FT /evidence="ECO:0000269|PubMed:18695986"
FT /id="VAR_051469"
FT VARIANT 353
FT /note="M -> T (not associated with susceptibility to breast
FT cancer; dbSNP:rs143282828)"
FT /evidence="ECO:0000269|PubMed:18695986"
FT /id="VAR_055328"
FT VARIANT 435
FT /note="P -> L (not associated with susceptibility to breast
FT cancer; dbSNP:rs3733876)"
FT /evidence="ECO:0000269|PubMed:18695986"
FT /id="VAR_051470"
FT VARIANT 511
FT /note="C -> R (not associated with susceptibility to breast
FT cancer; dbSNP:rs13360277)"
FT /evidence="ECO:0000269|PubMed:18695986"
FT /id="VAR_051471"
FT VARIANT 596
FT /note="G -> E (in dbSNP:rs10475633)"
FT /id="VAR_051472"
FT MUTAGEN 9
FT /note="K->A: Does not affect symoylation; when associated
FT with A-19; A-31; A-52 and A-61."
FT /evidence="ECO:0000269|PubMed:17698038"
FT MUTAGEN 19
FT /note="K->A: Does not affect symoylation; when associated
FT with A-9; A-31; A-52 and A-61."
FT /evidence="ECO:0000269|PubMed:17698038"
FT MUTAGEN 31
FT /note="K->A: Does not affect symoylation; when associated
FT with A-9; A-19; A-52 and A-61."
FT /evidence="ECO:0000269|PubMed:17698038"
FT MUTAGEN 52
FT /note="K->A: Does not affect symoylation; when associated
FT with A-9; A-19; A-31 and A-61."
FT /evidence="ECO:0000269|PubMed:17698038"
FT MUTAGEN 61
FT /note="K->A: Does not affect symoylation; when associated
FT with A-9; A-19; A-31 and A-52."
FT /evidence="ECO:0000269|PubMed:17698038"
FT MUTAGEN 81
FT /note="Missing: Strongly reduces ubiquitin binding via UIM
FT 1."
FT /evidence="ECO:0000269|PubMed:24627472"
FT MUTAGEN 88
FT /note="A->G,S: Impairs localization to DNA damages sites;
FT when associated with A-92; S-113 and A-117."
FT /evidence="ECO:0000269|PubMed:17525340,
FT ECO:0000269|PubMed:17525342, ECO:0000269|PubMed:17621610"
FT MUTAGEN 92
FT /note="S->A: Impairs localization to DNA damages sites;
FT when associated with S-88; S-113 and A-117."
FT /evidence="ECO:0000269|PubMed:17525340,
FT ECO:0000269|PubMed:17525342"
FT MUTAGEN 97..103
FT /note="REVNSQE->AA: Impairs the selectivity for 'K-63'-
FT linked ubiquitin."
FT /evidence="ECO:0000269|PubMed:19328070"
FT MUTAGEN 97..103
FT /note="REVNSQE->AAAAAAA: Increases the selectivity for 'K-
FT 63'-linked ubiquitin."
FT /evidence="ECO:0000269|PubMed:19328070"
FT MUTAGEN 97..103
FT /note="REVNSQE->AAAAAAAAA: Impairs the selectivity for 'K-
FT 63'-linked ubiquitin."
FT /evidence="ECO:0000269|PubMed:19328070"
FT MUTAGEN 101
FT /note="S->A,E: Slightly impairs the selectivity for 'K-63'-
FT linked ubiquitin."
FT /evidence="ECO:0000269|PubMed:19328070"
FT MUTAGEN 113
FT /note="A->G,S: Impairs ubiquitin-binding and localization
FT to DNA damages sites; when associated with S-88; A-92 and
FT A-117."
FT /evidence="ECO:0000269|PubMed:17525340,
FT ECO:0000269|PubMed:17525342, ECO:0000269|PubMed:17621610"
FT MUTAGEN 117
FT /note="S->A: Impairs ubiquitin-binding and localization to
FT DNA damages sites; when associated with S-88; A-92 and S-
FT 113."
FT /evidence="ECO:0000269|PubMed:17525340,
FT ECO:0000269|PubMed:17525342"
FT MUTAGEN 205
FT /note="S->G: Abolishes phosphorylation at this position."
FT /evidence="ECO:0000269|PubMed:18519686"
FT MUTAGEN 508
FT /note="C->A: Abolishes interaction with histone
FT monoubiquitinated H2B without affecting the interaction
FT with H2A."
FT /evidence="ECO:0000269|PubMed:19015238"
FT CONFLICT 187
FT /note="E -> K (in Ref. 7; AAH06078)"
FT /evidence="ECO:0000305"
FT CONFLICT 192
FT /note="E -> G (in Ref. 4; BAG51153)"
FT /evidence="ECO:0000305"
FT CONFLICT 247
FT /note="V -> C (in Ref. 3; AAG59851)"
FT /evidence="ECO:0000305"
FT CONFLICT 347
FT /note="E -> G (in Ref. 1; AAK61871)"
FT /evidence="ECO:0000305"
FT CONFLICT 518
FT /note="E -> G (in Ref. 1; AAK61871)"
FT /evidence="ECO:0000305"
FT CONFLICT 634
FT /note="H -> R (in Ref. 3; AAG59855)"
FT /evidence="ECO:0000305"
FT CONFLICT 638
FT /note="D -> N (in Ref. 4; BAG51153)"
FT /evidence="ECO:0000305"
FT CONFLICT 694
FT /note="D -> V (in Ref. 3; AAG59855)"
FT /evidence="ECO:0000305"
FT STRAND 40..43
FT /evidence="ECO:0007829|PDB:2N9E"
FT HELIX 84..94
FT /evidence="ECO:0007829|PDB:2MKF"
FT HELIX 101..119
FT /evidence="ECO:0007829|PDB:2MKF"
SQ SEQUENCE 719 AA; 79727 MW; 56B7699E42395861 CRC64;
MPRRKKKVKE VSESRNLEKK DVETTSSVSV KRKRRLEDAF IVISDSDGEE PKEENGLQKT
KTKQSNRAKC LAKRKIAQMT EEEQFALALK MSEQEAREVN SQEEEEEELL RKAIAESLNS
CRPSDASATR SRPLATGPSS QSHQEKTTDS GLTEGIWQLV PPSLFKGSHI SQGNEAEERE
EPWDHTEKTE EEPVSGSSGS WDQSSQPVFE NVNVKSFDRC TGHSAEHTQC GKPQESTGRG
SAFLKAVQGS GDTSRHCLPT LADAKGLQDT GGTVNYFWGI PFCPDGVDPN QYTKVILCQL
EVYQKSLKMA QRQLLNKKGF GEPVLPRPPS LIQNECGQGE QASEKNECIS EDMGDEDKEE
RQESRASDWH SKTKDFQESS IKSLKEKLLL EEEPTTSHGQ SSQGIVEETS EEGNSVPASQ
SVAALTSKRS LVLMPESSAE EITVCPETQL SSSETFDLER EVSPGSRDIL DGVRIIMADK
EVGNKEDAEK EVAISTFSSS NQVSCPLCDQ CFPPTKIERH AMYCNGLMEE DTVLTRRQKE
AKTKSDSGTA AQTSLDIDKN EKCYLCKSLV PFREYQCHVD SCLQLAKADQ GDGPEGSGRA
CSTVEGKWQQ RLKNPKEKGH SEGRLLSFLE QSEHKTSDAD IKSSETGAFR VPSPGMEEAG
CSREMQSSFT RRDLNESPVK SFVSISEATD CLVDFKKQVT VQPGSRTRTK AGRGRRRKF
