BABA1_HUMAN
ID BABA1_HUMAN Reviewed; 329 AA.
AC Q9NWV8; A8MQT0; B4DRY9; B4DVR1; Q6FIA0; Q9P018;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=BRISC and BRCA1-A complex member 1;
DE AltName: Full=Mediator of RAP80 interactions and targeting subunit of 40 kDa {ECO:0000303|PubMed:19261746};
DE AltName: Full=New component of the BRCA1-A complex {ECO:0000303|PubMed:19261749};
GN Name=BABAM1;
GN Synonyms=C19orf62, MERIT40 {ECO:0000303|PubMed:19261746},
GN NBA1 {ECO:0000303|PubMed:19261749}; ORFNames=HSPC142;
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 [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Umbilical cord blood;
RX PubMed=11042152; DOI=10.1101/gr.140200;
RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
RT "Cloning and functional analysis of cDNAs with open reading frames for 300
RT previously undefined genes expressed in CD34+ hematopoietic stem/progenitor
RT cells.";
RL Genome Res. 10:1546-1560(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC TISSUE=Brain, and Spleen;
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 MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Ovary, Pituitary, and Placenta;
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 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-62, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49 AND SER-66, 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 [10]
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 [11]
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 [12]
RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE
RP BRCA1-A COMPLEX, AND SUBCELLULAR LOCATION.
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 [13]
RP FUNCTION, IDENTIFICATION IN THE BRCA1-A COMPLEX, SUBCELLULAR LOCATION,
RP DOMAIN VWFA-LIKE, 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 [14]
RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE
RP BRCA1-A COMPLEX, SUBCELLULAR LOCATION, AND INTERACTION WITH BABAM2.
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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29; SER-49; THR-65 AND
RP SER-66, AND IDENTIFICATION BY 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 [16]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP 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 [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 BRISC COMPLEX, IDENTIFICATION IN THE BRCA1-A COMPLEX,
RP INTERACTION WITH BABAM2, AND SUBCELLULAR LOCATION.
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, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-49, 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 [20]
RP FUNCTION, IDENTIFICATION IN THE BRISC COMPLEX, IDENTIFICATION IN THE ARISC
RP COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR 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 [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49; SER-57 AND SER-62, 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 [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-62 AND SER-66, 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 [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.
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. In the BRCA1-A complex, it
CC is required for the complex integrity and its localization at DSBs.
CC Component of the BRISC complex, a multiprotein complex that
CC specifically cleaves 'Lys-63'-linked ubiquitin in various substrates
CC (PubMed:24075985, PubMed:26195665). In these 2 complexes, it is
CC probably required to maintain the stability of BABAM2 and help the
CC 'Lys-63'-linked deubiquitinase activity mediated by BRCC3/BRCC36
CC component. The BRISC complex is required for normal mitotic spindle
CC assembly and microtubule attachment to kinetochores via its role in
CC deubiquitinating NUMA1 (PubMed:26195665). 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).
CC {ECO:0000269|PubMed:19261746, ECO:0000269|PubMed:19261748,
CC ECO:0000269|PubMed:19261749}.
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 BRCA1, BARD1, UIMC1/RAP80, ABRAXAS1, BRCC3/BRCC36, BABAM2 and
CC BABAM1/NBA1 (PubMed:19261746, PubMed:19261749, PubMed:19261748,
CC PubMed:21282113). In the BRCA1-A complex, interacts directly with
CC ABRAXAS1 and BABAM2 (PubMed:19261749, PubMed:19261748). Component of
CC the BRISC complex, at least composed of ABRAXAS2, BRCC3/BRCC36, BABAM2
CC and BABAM1/NBA1 (PubMed:19214193, PubMed:21282113, PubMed:24075985,
CC PubMed:25283148). Identified in a complex with SHMT2 and the other
CC subunits of the BRISC complex (PubMed:24075985).
CC {ECO:0000269|PubMed:19214193, ECO:0000269|PubMed:19261746,
CC ECO:0000269|PubMed:19261748, ECO:0000269|PubMed:19261749,
CC ECO:0000269|PubMed:21282113, ECO:0000269|PubMed:24075985,
CC ECO:0000269|PubMed:25283148}.
CC -!- INTERACTION:
CC Q9NWV8; Q9NXR7: BABAM2; NbExp=6; IntAct=EBI-745725, EBI-949389;
CC Q9NWV8; Q9NYB0: TERF2IP; NbExp=2; IntAct=EBI-745725, EBI-750109;
CC Q9NWV8; Q9H2K2: TNKS2; NbExp=5; IntAct=EBI-745725, EBI-4398527;
CC Q9NWV8; P14373: TRIM27; NbExp=7; IntAct=EBI-745725, EBI-719493;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19261749,
CC ECO:0000269|PubMed:24075985}. Nucleus {ECO:0000269|PubMed:19261746,
CC ECO:0000269|PubMed:19261748, ECO:0000269|PubMed:19261749,
CC ECO:0000269|PubMed:21282113, ECO:0000269|PubMed:24075985}.
CC Note=Localizes at sites of DNA damage at double-strand breaks (DSBs).
CC {ECO:0000269|PubMed:19261746, ECO:0000269|PubMed:19261748,
CC ECO:0000269|PubMed:19261749, ECO:0000269|PubMed:21282113}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9NWV8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NWV8-2; Sequence=VSP_037246, VSP_037249;
CC Name=3;
CC IsoId=Q9NWV8-3; Sequence=VSP_037247, VSP_037248;
CC -!- DOMAIN: The VWFA-like region is similar to the VWFA domain. Its
CC presence reveals similarities between the structure of the 19S
CC proteasome and the BRCA1-A complexes. {ECO:0000269|PubMed:19261749}.
CC -!- SIMILARITY: Belongs to the BABAM1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF29106.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF161491; AAF29106.1; ALT_FRAME; mRNA.
DR EMBL; AL136692; CAB66627.1; -; mRNA.
DR EMBL; AK000578; BAA91268.1; -; mRNA.
DR EMBL; AK299493; BAG61451.1; -; mRNA.
DR EMBL; AK301193; BAG62773.1; -; mRNA.
DR EMBL; CR533526; CAG38557.1; -; mRNA.
DR EMBL; AC104522; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC000788; AAH00788.1; -; mRNA.
DR EMBL; BC006244; AAH06244.1; -; mRNA.
DR EMBL; BC091491; AAH91491.1; -; mRNA.
DR CCDS; CCDS46012.1; -. [Q9NWV8-1]
DR RefSeq; NP_001028721.1; NM_001033549.2. [Q9NWV8-1]
DR RefSeq; NP_001275685.1; NM_001288756.1. [Q9NWV8-1]
DR RefSeq; NP_001275686.1; NM_001288757.1.
DR RefSeq; NP_054892.2; NM_014173.3. [Q9NWV8-1]
DR PDB; 6H3C; EM; 3.90 A; D/I=1-329.
DR PDBsum; 6H3C; -.
DR AlphaFoldDB; Q9NWV8; -.
DR SMR; Q9NWV8; -.
DR BioGRID; 118855; 91.
DR ComplexPortal; CPX-4425; BRCA1-A complex.
DR ELM; Q9NWV8; -.
DR IntAct; Q9NWV8; 62.
DR MINT; Q9NWV8; -.
DR STRING; 9606.ENSP00000352408; -.
DR BindingDB; Q9NWV8; -.
DR GlyGen; Q9NWV8; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9NWV8; -.
DR PhosphoSitePlus; Q9NWV8; -.
DR BioMuta; BABAM1; -.
DR DMDM; 74734678; -.
DR EPD; Q9NWV8; -.
DR jPOST; Q9NWV8; -.
DR MassIVE; Q9NWV8; -.
DR MaxQB; Q9NWV8; -.
DR PaxDb; Q9NWV8; -.
DR PeptideAtlas; Q9NWV8; -.
DR PRIDE; Q9NWV8; -.
DR ProteomicsDB; 82986; -. [Q9NWV8-1]
DR ProteomicsDB; 82987; -. [Q9NWV8-2]
DR ProteomicsDB; 82988; -. [Q9NWV8-3]
DR Antibodypedia; 27571; 240 antibodies from 25 providers.
DR DNASU; 29086; -.
DR Ensembl; ENST00000359435.8; ENSP00000352408.3; ENSG00000105393.16. [Q9NWV8-1]
DR Ensembl; ENST00000598188.6; ENSP00000471605.1; ENSG00000105393.16. [Q9NWV8-1]
DR Ensembl; ENST00000601043.5; ENSP00000470920.1; ENSG00000105393.16. [Q9NWV8-1]
DR GeneID; 29086; -.
DR KEGG; hsa:29086; -.
DR MANE-Select; ENST00000598188.6; ENSP00000471605.1; NM_014173.4; NP_054892.2.
DR UCSC; uc002nfu.5; human. [Q9NWV8-1]
DR CTD; 29086; -.
DR DisGeNET; 29086; -.
DR GeneCards; BABAM1; -.
DR HGNC; HGNC:25008; BABAM1.
DR HPA; ENSG00000105393; Low tissue specificity.
DR MIM; 612766; gene.
DR neXtProt; NX_Q9NWV8; -.
DR OpenTargets; ENSG00000105393; -.
DR PharmGKB; PA162378767; -.
DR VEuPathDB; HostDB:ENSG00000105393; -.
DR eggNOG; ENOG502QPZP; Eukaryota.
DR GeneTree; ENSGT00390000016934; -.
DR InParanoid; Q9NWV8; -.
DR OMA; QCTPFKL; -.
DR PhylomeDB; Q9NWV8; -.
DR TreeFam; TF329070; -.
DR PathwayCommons; Q9NWV8; -.
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; Q9NWV8; -.
DR SIGNOR; Q9NWV8; -.
DR BioGRID-ORCS; 29086; 26 hits in 1094 CRISPR screens.
DR ChiTaRS; BABAM1; human.
DR GeneWiki; C19orf62; -.
DR GenomeRNAi; 29086; -.
DR Pharos; Q9NWV8; Tbio.
DR PRO; PR:Q9NWV8; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q9NWV8; protein.
DR Bgee; ENSG00000105393; Expressed in prefrontal cortex and 195 other tissues.
DR ExpressionAtlas; Q9NWV8; baseline and differential.
DR Genevisible; Q9NWV8; 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: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:0051301; P:cell division; 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:0071425; P:hematopoietic stem cell proliferation; IEA:Ensembl.
DR GO; GO:0070537; P:histone H2A K63-linked deubiquitination; 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:0045739; P:positive regulation of DNA repair; IMP:UniProtKB.
DR GO; GO:0070536; P:protein K63-linked deubiquitination; 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 Gene3D; 3.40.50.410; -; 1.
DR InterPro; IPR026126; BABAM1.
DR InterPro; IPR036465; vWFA_dom_sf.
DR PANTHER; PTHR15660; PTHR15660; 1.
DR SUPFAM; SSF53300; SSF53300; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cell cycle; Cell division;
KW Chromatin regulator; Cytoplasm; DNA damage; DNA repair; Mitosis; Nucleus;
KW Phosphoprotein; Reference proteome; Ubl conjugation pathway.
FT CHAIN 1..329
FT /note="BRISC and BRCA1-A complex member 1"
FT /id="PRO_0000288458"
FT REGION 1..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 95..298
FT /note="VWFA-like"
FT COMPBIAS 1..18
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..33
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692"
FT MOD_RES 8
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5XIJ6"
FT MOD_RES 29
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 49
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 57
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 62
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 65
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 66
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:24275569"
FT VAR_SEQ 1..115
FT /note="MEVAEPSSPTEEEEEEEEHSAEPRPRTRSNPEGAEDRAVGAQASVGSRSEGE
FT GEAASADDGSLNTSGAGPKSWQVPPPAPEVQIRTPRVNCPEKVIICLDLSEEMSLPKLE
FT SFNG -> MMGASTLQEPALSPGRCPRQPLRSKFGHHGSTVQRKC (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_037246"
FT VAR_SEQ 116..190
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_037247"
FT VAR_SEQ 234..329
FT /note="KMFQCPYFFFDVVYIHNGTEEKEEEMSWKDMFAFMGSLDTKGTSYKYEVALA
FT GPALELHNCMAKLLAHPLQRPCQSHASYSLLEEEDEAIEVEATV -> VGEAWEREGCL
FT QP (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_037248"
FT VAR_SEQ 263..329
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_037249"
FT CONFLICT 76
FT /note="P -> S (in Ref. 4; CAG38557)"
FT /evidence="ECO:0000305"
FT CONFLICT 288
FT /note="A -> V (in Ref. 4; CAG38557)"
FT /evidence="ECO:0000305"
FT CONFLICT 302
FT /note="P -> S (in Ref. 4; CAG38557)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 329 AA; 36560 MW; 7A84D8EE6D03C1DB CRC64;
MEVAEPSSPT EEEEEEEEHS AEPRPRTRSN PEGAEDRAVG AQASVGSRSE GEGEAASADD
GSLNTSGAGP KSWQVPPPAP EVQIRTPRVN CPEKVIICLD LSEEMSLPKL ESFNGSKTNA
LNVSQKMIEM FVRTKHKIDK SHEFALVVVN DDTAWLSGLT SDPRELCSCL YDLETASCST
FNLEGLFSLI QQKTELPVTE NVQTIPPPYV VRTILVYSRP PCQPQFSLTE PMKKMFQCPY
FFFDVVYIHN GTEEKEEEMS WKDMFAFMGS LDTKGTSYKY EVALAGPALE LHNCMAKLLA
HPLQRPCQSH ASYSLLEEED EAIEVEATV
