BABA2_HUMAN
ID BABA2_HUMAN Reviewed; 383 AA.
AC Q9NXR7; A8K4X1; D6W562; D6W563; Q13880; Q4ZFX8; Q53SD0; Q969X9; Q96P06;
DT 21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 2.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=BRISC and BRCA1-A complex member 2 {ECO:0000312|HGNC:HGNC:1106};
DE AltName: Full=BRCA1-A complex subunit BRE;
DE AltName: Full=BRCA1/BRCA2-containing complex subunit 45 {ECO:0000303|PubMed:14636569};
DE AltName: Full=Brain and reproductive organ-expressed protein {ECO:0000303|PubMed:7826398};
GN Name=BABAM2 {ECO:0000312|HGNC:HGNC:1106}; Synonyms=BRCC45, BRE;
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] {ECO:0000305, ECO:0000312|EMBL:AAA64231.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND INDUCTION.
RX PubMed=7826398; DOI=10.1006/bbrc.1995.1108;
RA Li L., Yoo H., Becker F.F., Ali-Osman F., Chan J.Y.-H.;
RT "Identification of a brain- and reproductive-organs-specific gene
RT responsive to DNA damage and retinoic acid.";
RL Biochem. Biophys. Res. Commun. 206:764-774(1995).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAL17818.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 4), TISSUE SPECIFICITY, AND
RP INDUCTION.
RC TISSUE=Monocyte {ECO:0000269|PubMed:11676476};
RX PubMed=11676476; DOI=10.1006/bbrc.2001.5801;
RA Ching A.K.K., Li P.S., Li Q., Chan B.C.L., Chan J.Y.-H., Lim P.L.,
RA Pang J.C.S., Chui Y.L.;
RT "Expression of human BRE in multiple isoforms.";
RL Biochem. Biophys. Res. Commun. 288:535-545(2001).
RN [3] {ECO:0000305, ECO:0000312|EMBL:AAR30499.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, AND IDENTIFICATION IN
RP BRCC COMPLEX.
RX PubMed=14636569; DOI=10.1016/s1097-2765(03)00424-6;
RA Dong Y., Hakimi M.-A., Chen X., Kumaraswamy E., Cooch N.S., Godwin A.K.,
RA Shiekhattar R.;
RT "Regulation of BRCC, a holoenzyme complex containing BRCA1 and BRCA2, by a
RT signalosome-like subunit and its role in DNA repair.";
RL Mol. Cell 12:1087-1099(2003).
RN [4] {ECO:0000305, ECO:0000312|EMBL:AAB69387.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RA Keeton K.R., Miles W.M.;
RL Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000305, ECO:0000312|EMBL:BAA90943.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Colon {ECO:0000312|EMBL:BAA90943.1}, and 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 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [7] {ECO:0000305, ECO:0000312|EMBL:AAB69387.1}
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8] {ECO:0000305, ECO:0000312|EMBL:AAH01251.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Cervix {ECO:0000312|EMBL:AAH01251.1};
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 [9] {ECO:0000305}
RP FUNCTION, INTERACTION WITH FAS AND TNFRSF1A, AND SUBCELLULAR LOCATION.
RX PubMed=15465831; DOI=10.1074/jbc.m408678200;
RA Li Q., Ching A.K.-K., Chan B.C.-L., Chow S.K.-Y., Lim P.-L., Ho T.C.-Y.,
RA Ip W.-K., Wong C.-K., Lam C.W.-K., Lee K.K.-H., Chan J.Y.-H., Chui Y.-L.;
RT "A death receptor-associated anti-apoptotic protein, BRE, inhibits
RT mitochondrial apoptotic pathway.";
RL J. Biol. Chem. 279:52106-52116(2004).
RN [10]
RP IDENTIFICATION IN THE BRCA1-A COMPLEX.
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 [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP 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 [12]
RP IDENTIFICATION IN THE BRISC COMPLEX.
RX PubMed=19214193; DOI=10.1038/emboj.2009.27;
RA Cooper E.M., Cutcliffe C., Kristiansen T.Z., Pandey A., Pickart C.M.,
RA Cohen R.E.;
RT "K63-specific deubiquitination by two JAMM/MPN+ complexes: BRISC-associated
RT Brcc36 and proteasomal Poh1.";
RL EMBO J. 28:621-631(2009).
RN [13]
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 [14]
RP FUNCTION, IDENTIFICATION IN THE BRCA1-A COMPLEX, DOMAIN UEV-LIKE,
RP UBIQUITIN-BINDING, AND INTERACTION 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 [15]
RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE
RP BRCA1-A COMPLEX, SUBCELLULAR LOCATION, AND INTERACTION WITH ABRAXAS1;
RP BABAM1 AND BRCC3.
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 [16]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-2, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [17]
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 [18]
RP IDENTIFICATION IN ARISC COMPLEX, IDENTIFICATION IN BRISC COMPLEX, AND
RP INTERACTION WITH BABAM1.
RX PubMed=21282113; DOI=10.1074/jbc.m110.200857;
RA Hu X., Kim J.A., Castillo A., Huang M., Liu J., Wang B.;
RT "NBA1/MERIT40 and BRE interaction is required for the integrity of two
RT distinct deubiquitinating enzyme BRCC36-containing complexes.";
RL J. Biol. Chem. 286:11734-11745(2011).
RN [19]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [20]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [21]
RP FUNCTION, IDENTIFICATION IN THE BRISC COMPLEX, IDENTIFICATION BY MASS
RP SPECTROMETRY, IDENTIFICATION IN THE ARISC COMPLEX, AND SUBCELLULAR
RP LOCATION.
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 [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2, 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 [23]
RP IDENTIFICATION IN THE BRISC COMPLEX.
RX PubMed=25283148; DOI=10.1038/ncomms6059;
RA Zhang J., Cao M., Dong J., Li C., Xu W., Zhan Y., Wang X., Yu M., Ge C.,
RA Ge Z., Yang X.;
RT "ABRO1 suppresses tumourigenesis and regulates the DNA damage response by
RT stabilizing p53.";
RL Nat. Commun. 5:5059-5059(2014).
RN [24]
RP FUNCTION OF THE BRISC COMPLEX.
RX PubMed=26195665; DOI=10.1083/jcb.201503039;
RA Yan K., Li L., Wang X., Hong R., Zhang Y., Yang H., Lin M., Zhang S.,
RA He Q., Zheng D., Tang J., Yin Y., Shao G.;
RT "The deubiquitinating enzyme complex BRISC is required for proper mitotic
RT spindle assembly in mammalian cells.";
RL J. Cell Biol. 210:209-224(2015).
CC -!- FUNCTION: Component of the BRCA1-A complex, a complex that specifically
CC recognizes '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 (PubMed:17525341,
CC PubMed:19261746, PubMed:19261749, PubMed:19261748). In the BRCA1-A
CC complex, it acts as an adapter that bridges the interaction between
CC BABAM1/NBA1 and the rest of the complex, thereby being required for the
CC complex integrity and modulating the E3 ubiquitin ligase activity of
CC the BRCA1-BARD1 heterodimer (PubMed:21282113, PubMed:19261748).
CC Component of the BRISC complex, a multiprotein complex that
CC specifically cleaves 'Lys-63'-linked ubiquitin in various substrates
CC (PubMed:19214193, PubMed:24075985, PubMed:25283148, PubMed:26195665).
CC Within the BRISC complex, acts as an adapter that bridges the
CC interaction between BABAM1/NBA1 and the rest of the complex, thereby
CC being required for the complex integrity (PubMed:21282113). The BRISC
CC complex is required for normal mitotic spindle assembly and microtubule
CC attachment to kinetochores via its role in deubiquitinating NUMA1
CC (PubMed:26195665). The BRISC complex plays a role in interferon
CC signaling via its role in the deubiquitination of the interferon
CC receptor IFNAR1; deubiquitination increases IFNAR1 activity by
CC enhancing its stability and cell surface expression (PubMed:24075985).
CC Down-regulates the response to bacterial lipopolysaccharide (LPS) via
CC its role in IFNAR1 deubiquitination (PubMed:24075985). May play a role
CC in homeostasis or cellular differentiation in cells of neural,
CC epithelial and germline origins. May also act as a death receptor-
CC associated anti-apoptotic protein, which inhibits the mitochondrial
CC apoptotic pathway. May regulate TNF-alpha signaling through its
CC interactions with TNFRSF1A; however these effects may be indirect
CC (PubMed:15465831). {ECO:0000269|PubMed:14636569,
CC ECO:0000269|PubMed:19261748, ECO:0000269|PubMed:19261749,
CC ECO:0000269|PubMed:24075985, ECO:0000269|PubMed:26195665,
CC ECO:0000305|PubMed:15465831}.
CC -!- SUBUNIT: Component of the ARISC complex, at least composed of
CC UIMC1/RAP80, ABRAXAS1, BRCC3/BRCC36, BABAM2 and BABAM1/NBA1
CC (PubMed:21282113, PubMed:24075985). Component of the BRCA1-A complex,
CC at least composed of BRCA1, BARD1, UIMC1/RAP80, ABRAXAS1, BRCC3/BRCC36,
CC BABAM2 and BABAM1/NBA1. In the BRCA1-A complex, interacts directly with
CC ABRAXAS1, BRCC3/BRCC36 and BABAM1/NBA1. Binds polyubiquitin. Component
CC of the BRISC complex, at least composed of ABRAXAS2, BRCC3/BRCC36,
CC BABAM2 and BABAM1/NBA1 (PubMed:19214193, PubMed:21282113,
CC PubMed:24075985, PubMed:25283148). Identified in a complex with SHMT2
CC and the other subunits of the BRISC complex (PubMed:24075985).
CC Component of the BRCA1/BRCA2 containing complex (BRCC), which also
CC contains BRCA1, BRCA2, BARD1, BRCC3/BRCC36 and RAD51. BRCC is a
CC ubiquitin E3 ligase complex that enhances cellular survival following
CC DNA damage. May interact with FAS and TNFRSF1A (PubMed:15465831).
CC {ECO:0000269|PubMed:14636569, ECO:0000269|PubMed:17525341,
CC ECO:0000269|PubMed:19214193, ECO:0000269|PubMed:19261746,
CC ECO:0000269|PubMed:19261748, ECO:0000269|PubMed:19261749,
CC ECO:0000269|PubMed:24075985, ECO:0000269|PubMed:25283148,
CC ECO:0000305|PubMed:15465831}.
CC -!- INTERACTION:
CC Q9NXR7; Q9NWV8: BABAM1; NbExp=6; IntAct=EBI-949389, EBI-745725;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15465831,
CC ECO:0000269|PubMed:24075985}. Nucleus {ECO:0000269|PubMed:15465831,
CC ECO:0000269|PubMed:19261748, ECO:0000269|PubMed:24075985}.
CC Note=Localizes at sites of DNA damage at double-strand breaks (DSBs).
CC {ECO:0000269|PubMed:19261748}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Comment=Additional isoforms may exist. {ECO:0000305};
CC Name=2 {ECO:0000269|PubMed:14636569};
CC IsoId=Q9NXR7-2; Sequence=Displayed;
CC Name=1 {ECO:0000305};
CC IsoId=Q9NXR7-1; Sequence=VSP_051956;
CC Name=3 {ECO:0000269|PubMed:11676476}; Synonyms=Alpha a';
CC IsoId=Q9NXR7-3; Sequence=VSP_051957;
CC Name=4;
CC IsoId=Q9NXR7-4; Sequence=VSP_037261;
CC -!- TISSUE SPECIFICITY: Expressed in all cell lines examined. Highly
CC expressed in placenta. {ECO:0000269|PubMed:11676476}.
CC -!- INDUCTION: Down-regulated by DNA-damaging agents in fibroblasts, by
CC retinoic acid in brain glioma U-251MG and promyelocytic HL-60 cell
CC lines, and by bacterial lipopolysaccharides (LPS) in peripheral blood
CC mononuclear cells (PBMC). {ECO:0000269|PubMed:11676476,
CC ECO:0000269|PubMed:7826398}.
CC -!- DOMAIN: Contains 2 ubiquitin-conjugating enzyme family-like (UEV-like)
CC regions. These regions lack the critical Cys residues required for
CC ubiquitination but retain the ability to bind ubiquitin.
CC {ECO:0000269|PubMed:19261749}.
CC -!- SIMILARITY: Belongs to the BABAM2 family. {ECO:0000255}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/BREID839ch2p23.html";
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DR EMBL; L38616; AAA64231.1; -; mRNA.
DR EMBL; AF420605; AAL17818.1; -; mRNA.
DR EMBL; AY438031; AAR30499.1; -; mRNA.
DR EMBL; AF015767; AAB69387.1; -; mRNA.
DR EMBL; AF420602; AAL17814.1; -; mRNA.
DR EMBL; AF420603; AAL17816.1; -; mRNA.
DR EMBL; AK000097; BAA90943.1; -; mRNA.
DR EMBL; AK291086; BAF83775.1; -; mRNA.
DR EMBL; AC021171; AAY24156.1; -; Genomic_DNA.
DR EMBL; AC093690; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC096552; AAX88935.1; -; Genomic_DNA.
DR EMBL; CH471053; EAX00545.1; -; Genomic_DNA.
DR EMBL; CH471053; EAX00546.1; -; Genomic_DNA.
DR EMBL; CH471053; EAX00547.1; -; Genomic_DNA.
DR EMBL; CH471053; EAX00548.1; -; Genomic_DNA.
DR EMBL; BC001251; AAH01251.1; -; mRNA.
DR CCDS; CCDS1763.1; -. [Q9NXR7-2]
DR CCDS; CCDS1764.1; -. [Q9NXR7-1]
DR CCDS; CCDS1765.1; -. [Q9NXR7-4]
DR PIR; JC2472; JC2472.
DR RefSeq; NP_001248769.1; NM_001261840.1. [Q9NXR7-3]
DR RefSeq; NP_001316041.1; NM_001329112.1. [Q9NXR7-2]
DR RefSeq; NP_001316042.1; NM_001329113.1. [Q9NXR7-1]
DR RefSeq; NP_004890.2; NM_004899.4. [Q9NXR7-1]
DR RefSeq; NP_954661.1; NM_199191.2. [Q9NXR7-2]
DR RefSeq; NP_954662.1; NM_199192.2. [Q9NXR7-4]
DR RefSeq; NP_954663.1; NM_199193.2. [Q9NXR7-4]
DR RefSeq; NP_954664.1; NM_199194.2. [Q9NXR7-2]
DR PDB; 6H3C; EM; 3.90 A; C/H=1-383.
DR PDB; 6R8F; EM; 3.80 A; E/G=1-133.
DR PDBsum; 6H3C; -.
DR PDBsum; 6R8F; -.
DR AlphaFoldDB; Q9NXR7; -.
DR SMR; Q9NXR7; -.
DR BioGRID; 114946; 75.
DR ComplexPortal; CPX-4425; BRCA1-A complex.
DR ComplexPortal; CPX-955; BRCC ubiquitin ligase complex.
DR CORUM; Q9NXR7; -.
DR IntAct; Q9NXR7; 33.
DR MINT; Q9NXR7; -.
DR STRING; 9606.ENSP00000343412; -.
DR BindingDB; Q9NXR7; -.
DR iPTMnet; Q9NXR7; -.
DR PhosphoSitePlus; Q9NXR7; -.
DR BioMuta; BABAM2; -.
DR DMDM; 229462810; -.
DR EPD; Q9NXR7; -.
DR jPOST; Q9NXR7; -.
DR MassIVE; Q9NXR7; -.
DR MaxQB; Q9NXR7; -.
DR PaxDb; Q9NXR7; -.
DR PeptideAtlas; Q9NXR7; -.
DR PRIDE; Q9NXR7; -.
DR ProteomicsDB; 83124; -. [Q9NXR7-2]
DR ProteomicsDB; 83125; -. [Q9NXR7-1]
DR ProteomicsDB; 83126; -. [Q9NXR7-3]
DR ProteomicsDB; 83127; -. [Q9NXR7-4]
DR Antibodypedia; 13903; 260 antibodies from 35 providers.
DR DNASU; 9577; -.
DR Ensembl; ENST00000342045.6; ENSP00000339371.2; ENSG00000158019.21. [Q9NXR7-2]
DR Ensembl; ENST00000344773.6; ENSP00000343412.2; ENSG00000158019.21. [Q9NXR7-1]
DR Ensembl; ENST00000361704.6; ENSP00000354699.2; ENSG00000158019.21. [Q9NXR7-4]
DR Ensembl; ENST00000379624.6; ENSP00000368945.1; ENSG00000158019.21. [Q9NXR7-2]
DR Ensembl; ENST00000379632.6; ENSP00000368953.2; ENSG00000158019.21. [Q9NXR7-4]
DR GeneID; 9577; -.
DR KEGG; hsa:9577; -.
DR MANE-Select; ENST00000379624.6; ENSP00000368945.1; NM_199191.3; NP_954661.1.
DR UCSC; uc002rlq.4; human. [Q9NXR7-2]
DR CTD; 9577; -.
DR DisGeNET; 9577; -.
DR GeneCards; BABAM2; -.
DR HGNC; HGNC:1106; BABAM2.
DR HPA; ENSG00000158019; Tissue enriched (adrenal).
DR MIM; 610497; gene.
DR neXtProt; NX_Q9NXR7; -.
DR OpenTargets; ENSG00000158019; -.
DR PharmGKB; PA25419; -.
DR VEuPathDB; HostDB:ENSG00000158019; -.
DR eggNOG; ENOG502QUU0; Eukaryota.
DR GeneTree; ENSGT00390000004208; -.
DR HOGENOM; CLU_057019_0_0_1; -.
DR InParanoid; Q9NXR7; -.
DR OMA; KPTEARF; -.
DR PhylomeDB; Q9NXR7; -.
DR TreeFam; TF328507; -.
DR PathwayCommons; Q9NXR7; -.
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; Q9NXR7; -.
DR SIGNOR; Q9NXR7; -.
DR BioGRID-ORCS; 9577; 18 hits in 1089 CRISPR screens.
DR ChiTaRS; BRE; human.
DR GeneWiki; BRE_(gene); -.
DR GenomeRNAi; 9577; -.
DR Pharos; Q9NXR7; Tbio.
DR PRO; PR:Q9NXR7; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q9NXR7; protein.
DR Bgee; ENSG00000158019; Expressed in right adrenal gland and 199 other tissues.
DR ExpressionAtlas; Q9NXR7; baseline and differential.
DR Genevisible; Q9NXR7; HS.
DR GO; GO:0070531; C:BRCA1-A complex; IDA:UniProtKB.
DR GO; GO:0070552; C:BRISC complex; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0000152; C:nuclear ubiquitin ligase complex; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0000268; F:peroxisome targeting sequence binding; TAS:UniProtKB.
DR GO; GO:0031593; F:polyubiquitin modification-dependent protein binding; IDA:UniProtKB.
DR GO; GO:0005164; F:tumor necrosis factor receptor binding; IDA:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IEP:UniProtKB.
DR GO; GO:0071479; P:cellular response to ionizing radiation; IMP:ComplexPortal.
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; IC:ComplexPortal.
DR GO; GO:0035518; P:histone H2A monoubiquitination; IC:ComplexPortal.
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:0043066; P:negative regulation of apoptotic process; IDA:UniProtKB.
DR GO; GO:0045739; P:positive regulation of DNA repair; IMP:UniProtKB.
DR GO; GO:0051865; P:protein autoubiquitination; IC:ComplexPortal.
DR GO; GO:0070536; P:protein K63-linked deubiquitination; IC:UniProtKB.
DR GO; GO:2000001; P:regulation of DNA damage checkpoint; IC:ComplexPortal.
DR GO; GO:0006282; P:regulation of DNA repair; IC:ComplexPortal.
DR GO; GO:0010212; P:response to ionizing radiation; IMP:UniProtKB.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR InterPro; IPR010358; BRE.
DR PANTHER; PTHR15189; PTHR15189; 1.
DR Pfam; PF06113; BRE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Apoptosis; Cell cycle;
KW Cell division; Chromatin regulator; Cytoplasm; DNA damage; DNA repair;
KW Mitosis; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Ubl conjugation pathway.
FT CHAIN 1..383
FT /note="BRISC and BRCA1-A complex member 2"
FT /id="PRO_0000224189"
FT REGION 30..147
FT /note="UEV-like 1"
FT REGION 275..364
FT /note="UEV-like 2"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:22223895"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT VAR_SEQ 363..383
FT /note="KAYFKTFVPQFQEAAFANGKL -> NSRRQHLPMESSRKHQS (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:11676476"
FT /id="VSP_051957"
FT VAR_SEQ 364..383
FT /note="AYFKTFVPQFQEAAFANGKL -> GCQGSRDACSPWEQVLAFAVAKTGCKLL
FT QPQRNWPSSRGPPWRASEGERTAQ (in isoform 1)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_051956"
FT VAR_SEQ 364..383
FT /note="AYFKTFVPQFQEAAFANGKL -> RESNRDGEESSSA (in isoform
FT 4)"
FT /evidence="ECO:0000303|PubMed:11676476"
FT /id="VSP_037261"
FT CONFLICT 192
FT /note="V -> L (in Ref. 5; BAF83775)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 383 AA; 43552 MW; D830226E2B8F2C4B CRC64;
MSPEVALNRI SPMLSPFISS VVRNGKVGLD ATNCLRITDL KSGCTSLTPG PNCDRFKLHI
PYAGETLKWD IIFNAQYPEL PPDFIFGEDA EFLPDPSALQ NLASWNPSNP ECLLLVVKEL
VQQYHQFQCS RLRESSRLMF EYQTLLEEPQ YGENMEIYAG KKNNWTGEFS ARFLLKLPVD
FSNIPTYLLK DVNEDPGEDV ALLSVSFEDT EATQVYPKLY LSPRIEHALG GSSALHIPAF
PGGGCLIDYV PQVCHLLTNK VQYVIQGYHK RREYIAAFLS HFGTGVVEYD AEGFTKLTLL
LMWKDFCFLV HIDLPLFFPR DQPTLTFQSV YHFTNSGQLY SQAQKNYPYS PRWDGNEMAK
RAKAYFKTFV PQFQEAAFAN GKL
