BRAP_HUMAN
ID BRAP_HUMAN Reviewed; 592 AA.
AC Q7Z569; B4DRM1; B9EGS8; O43238; O75341;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 2.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=BRCA1-associated protein;
DE EC=2.3.2.27 {ECO:0000269|PubMed:14724641};
DE AltName: Full=BRAP2;
DE AltName: Full=Impedes mitogenic signal propagation;
DE Short=IMP;
DE AltName: Full=RING finger protein 52;
DE AltName: Full=RING-type E3 ubiquitin transferase BRAP2 {ECO:0000305};
DE AltName: Full=Renal carcinoma antigen NY-REN-63;
GN Name=BRAP {ECO:0000312|HGNC:HGNC:1099}; Synonyms=RNF52;
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 {ECO:0000312|EMBL:AAP93638.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND INTERACTION WITH BRCA1.
RC TISSUE=Fibroblast {ECO:0000269|PubMed:9497340};
RX PubMed=9497340; DOI=10.1074/jbc.273.11.6183;
RA Li S., Ku C.-Y., Farmer A.A., Cong Y.-S., Chen C.-F., Lee W.-H.;
RT "Identification of a novel cytoplasmic protein that specifically binds to
RT nuclear localization signal motifs.";
RL J. Biol. Chem. 273:6183-6189(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY,
RP MUTAGENESIS OF CYS-264, AND INTERACTION WITH KSR1.
RC TISSUE=T-cell {ECO:0000269|PubMed:14724641};
RX PubMed=14724641; DOI=10.1038/nature02237;
RA Matheny S.A., Chen C., Kortum R.L., Razidlo G.L., Lewis R.E., White M.A.;
RT "Ras regulates assembly of mitogenic signalling complexes through the
RT effector protein IMP.";
RL Nature 427:256-260(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, and Testis;
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 [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 356-592 (ISOFORM 1), AND INTERACTION WITH
RP DDB1.
RX PubMed=10777491; DOI=10.1074/jbc.m000961200;
RA Liu W., Nichols A.F., Graham J.A., Dualan R., Abbas A., Linn S.;
RT "Nuclear transport of human DDB protein induced by ultraviolet light.";
RL J. Biol. Chem. 275:21429-21434(2000).
RN [8]
RP IDENTIFICATION AS A RENAL CANCER ANTIGEN.
RC TISSUE=Renal cell carcinoma;
RX PubMed=10508479;
RX DOI=10.1002/(sici)1097-0215(19991112)83:4<456::aid-ijc4>3.0.co;2-5;
RA Scanlan M.J., Gordan J.D., Williamson B., Stockert E., Bander N.H.,
RA Jongeneel C.V., Gure A.O., Jaeger D., Jaeger E., Knuth A., Chen Y.-T.,
RA Old L.J.;
RT "Antigens recognized by autologous antibody in patients with renal-cell
RT carcinoma.";
RL Int. J. Cancer 83:456-464(1999).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [10]
RP 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 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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-119, 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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52; SER-97 AND SER-117, 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 [14]
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).
CC -!- FUNCTION: Negatively regulates MAP kinase activation by limiting the
CC formation of Raf/MEK complexes probably by inactivation of the KSR1
CC scaffold protein. Also acts as a Ras responsive E3 ubiquitin ligase
CC that, on activation of Ras, is modified by auto-polyubiquitination
CC resulting in the release of inhibition of Raf/MEK complex formation.
CC May also act as a cytoplasmic retention protein with a role in
CC regulating nuclear transport. {ECO:0000269|PubMed:14724641,
CC ECO:0000303|PubMed:10777491}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27; Evidence={ECO:0000269|PubMed:14724641};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Interacts with the nuclear localization signal of BRCA1 and
CC with the N-terminal of KSR1. The C-terminal portion of BCRA1 interacts
CC with DDB1. {ECO:0000269|PubMed:10777491, ECO:0000269|PubMed:14724641,
CC ECO:0000269|PubMed:9497340}.
CC -!- INTERACTION:
CC Q7Z569; O75969: AKAP3; NbExp=2; IntAct=EBI-349900, EBI-9033101;
CC Q7Z569; Q7Z569: BRAP; NbExp=2; IntAct=EBI-349900, EBI-349900;
CC Q7Z569; P38398: BRCA1; NbExp=3; IntAct=EBI-349900, EBI-349905;
CC Q7Z569; P01112: HRAS; NbExp=3; IntAct=EBI-349900, EBI-350145;
CC Q7Z569; Q9BW85: YJU2; NbExp=3; IntAct=EBI-349900, EBI-10300345;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9497340}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q7Z569-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q7Z569-2; Sequence=VSP_055881, VSP_055882;
CC -!- TISSUE SPECIFICITY: Expressed in breast epithelial cell lines.
CC {ECO:0000269|PubMed:9497340}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC24200.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF035620; AAC24200.1; ALT_FRAME; mRNA.
DR EMBL; AY332222; AAP93638.1; -; mRNA.
DR EMBL; AK299326; BAG61333.1; -; mRNA.
DR EMBL; AC002996; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC137055; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471054; EAW97972.1; -; Genomic_DNA.
DR EMBL; BC136698; AAI36699.1; -; mRNA.
DR EMBL; BC136699; AAI36700.1; -; mRNA.
DR EMBL; AF035950; AAB88538.1; -; mRNA.
DR CCDS; CCDS9154.1; -. [Q7Z569-1]
DR RefSeq; NP_006759.3; NM_006768.4. [Q7Z569-1]
DR AlphaFoldDB; Q7Z569; -.
DR SMR; Q7Z569; -.
DR BioGRID; 113912; 69.
DR IntAct; Q7Z569; 47.
DR MINT; Q7Z569; -.
DR STRING; 9606.ENSP00000403524; -.
DR iPTMnet; Q7Z569; -.
DR MetOSite; Q7Z569; -.
DR PhosphoSitePlus; Q7Z569; -.
DR BioMuta; BRAP; -.
DR DMDM; 296434410; -.
DR EPD; Q7Z569; -.
DR jPOST; Q7Z569; -.
DR MassIVE; Q7Z569; -.
DR MaxQB; Q7Z569; -.
DR PaxDb; Q7Z569; -.
DR PeptideAtlas; Q7Z569; -.
DR PRIDE; Q7Z569; -.
DR ProteomicsDB; 4961; -.
DR ProteomicsDB; 69260; -. [Q7Z569-1]
DR Antibodypedia; 31107; 195 antibodies from 30 providers.
DR DNASU; 8315; -.
DR Ensembl; ENST00000419234.9; ENSP00000403524.3; ENSG00000089234.16. [Q7Z569-1]
DR GeneID; 8315; -.
DR KEGG; hsa:8315; -.
DR MANE-Select; ENST00000419234.9; ENSP00000403524.3; NM_006768.5; NP_006759.3.
DR UCSC; uc001tsn.4; human. [Q7Z569-1]
DR CTD; 8315; -.
DR DisGeNET; 8315; -.
DR GeneCards; BRAP; -.
DR HGNC; HGNC:1099; BRAP.
DR HPA; ENSG00000089234; Tissue enhanced (testis).
DR MIM; 604986; gene.
DR neXtProt; NX_Q7Z569; -.
DR OpenTargets; ENSG00000089234; -.
DR PharmGKB; PA25410; -.
DR VEuPathDB; HostDB:ENSG00000089234; -.
DR eggNOG; KOG0804; Eukaryota.
DR GeneTree; ENSGT00500000044909; -.
DR InParanoid; Q7Z569; -.
DR OMA; GIIHLYK; -.
DR OrthoDB; 659103at2759; -.
DR PhylomeDB; Q7Z569; -.
DR TreeFam; TF313622; -.
DR PathwayCommons; Q7Z569; -.
DR Reactome; R-HSA-5673000; RAF activation.
DR Reactome; R-HSA-5675221; Negative regulation of MAPK pathway.
DR Reactome; R-HSA-6802946; Signaling by moderate kinase activity BRAF mutants.
DR Reactome; R-HSA-6802955; Paradoxical activation of RAF signaling by kinase inactive BRAF.
DR Reactome; R-HSA-9649948; Signaling downstream of RAS mutants.
DR SignaLink; Q7Z569; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 8315; 111 hits in 1127 CRISPR screens.
DR ChiTaRS; BRAP; human.
DR GenomeRNAi; 8315; -.
DR Pharos; Q7Z569; Tbio.
DR PRO; PR:Q7Z569; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q7Z569; protein.
DR Bgee; ENSG00000089234; Expressed in left testis and 205 other tissues.
DR ExpressionAtlas; Q7Z569; baseline and differential.
DR Genevisible; Q7Z569; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0031965; C:nuclear membrane; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0000151; C:ubiquitin ligase complex; IDA:MGI.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0008139; F:nuclear localization sequence binding; IDA:MGI.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:MGI.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0000165; P:MAPK cascade; IDA:MGI.
DR GO; GO:0009968; P:negative regulation of signal transduction; IDA:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; IDA:FlyBase.
DR GO; GO:0007265; P:Ras protein signal transduction; IDA:MGI.
DR CDD; cd12718; RRM_BRAP2; 1.
DR Gene3D; 3.30.40.10; -; 2.
DR InterPro; IPR011422; BRAP2.
DR InterPro; IPR034932; BRAP2_RRM.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR001607; Znf_UBP.
DR Pfam; PF07576; BRAP2; 1.
DR Pfam; PF13639; zf-RING_2; 1.
DR Pfam; PF02148; zf-UBP; 1.
DR SMART; SM00184; RING; 1.
DR SMART; SM00290; ZnF_UBP; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
DR PROSITE; PS50271; ZF_UBP; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Cytoplasm; Metal-binding;
KW Phosphoprotein; Reference proteome; Transferase; Ubl conjugation pathway;
KW Zinc; Zinc-finger.
FT CHAIN 1..592
FT /note="BRCA1-associated protein"
FT /id="PRO_0000055825"
FT ZN_FING 264..304
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175,
FT ECO:0000305"
FT ZN_FING 301..393
FT /note="UBP-type; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT REGION 78..124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 565..592
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 429..537
FT /evidence="ECO:0000255"
FT COMPBIAS 82..111
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 317
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 320
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 329
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 332
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 337
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 344
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 348
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 354
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT MOD_RES 52
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 97
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 117
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 119
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT VAR_SEQ 1..141
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055881"
FT VAR_SEQ 212..249
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055882"
FT MUTAGEN 264
FT /note="C->A: Loss of E3 ubiquitin-protein ligase activity."
FT /evidence="ECO:0000269|PubMed:14724641"
FT CONFLICT 186
FT /note="E -> D (in Ref. 1; AAC24200 and 2; AAP93638)"
FT /evidence="ECO:0000305"
FT CONFLICT 356
FT /note="Y -> H (in Ref. 7; AAB88538)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 592 AA; 67305 MW; 70CFEAB560D1952C CRC64;
MSVSLVVIRL ELAEHSPVPA GFGFSAAAGE MSDEEIKKTT LASAVACLEG KSPGEKVAII
HQHLGRREMT DVIIETMKSN PDELKTTVEE RKSSEASPTA QRSKDHSKEC INAAPDSPSK
QLPDQISFFS GNPSVEIVHG IMHLYKTNKM TSLKEDVRRS AMLCILTVPA AMTSHDLMKF
VAPFNEVIEQ MKIIRDSTPN QYMVLIKFRA QADADSFYMT CNGRQFNSIE DDVCQLVYVE
RAEVLKSEDG ASLPVMDLTE LPKCTVCLER MDESVNGILT TLCNHSFHSQ CLQRWDDTTC
PVCRYCQTPE PVEENKCFEC GVQENLWICL ICGHIGCGRY VSRHAYKHFE ETQHTYAMQL
TNHRVWDYAG DNYVHRLVAS KTDGKIVQYE CEGDTCQEEK IDALQLEYSY LLTSQLESQR
IYWENKIVRI EKDTAEEINN MKTKFKETIE KCDNLEHKLN DLLKEKQSVE RKCTQLNTKV
AKLTNELKEE QEMNKCLRAN QVLLQNKLKE EERVLKETCD QKDLQITEIQ EQLRDVMFYL
ETQQKINHLP AETRQEIQEG QINIAMASAS SPASSGGSGK LPSRKGRSKR GK
