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BRISC and BRCA1-A complex member 2 (BRCA1-A complex subunit BRE) (BRCA1/BRCA2-containing complex subunit 45) (Brain and reproductive organ-expressed protein)

 BABA2_HUMAN             Reviewed;         383 AA.
Q9NXR7; A8K4X1; D6W562; D6W563; Q13880; Q4ZFX8; Q53SD0; Q969X9;
Q96P06;
21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
05-MAY-2009, sequence version 2.
25-OCT-2017, entry version 134.
RecName: Full=BRISC and BRCA1-A complex member 2 {ECO:0000312|HGNC:HGNC:1106};
AltName: Full=BRCA1-A complex subunit BRE;
AltName: Full=BRCA1/BRCA2-containing complex subunit 45 {ECO:0000303|PubMed:14636569};
AltName: Full=Brain and reproductive organ-expressed protein {ECO:0000303|PubMed:7826398};
Name=BABAM2 {ECO:0000312|HGNC:HGNC:1106}; Synonyms=BRCC45, BRE;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1] {ECO:0000305, ECO:0000312|EMBL:AAA64231.1}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND INDUCTION.
PubMed=7826398; DOI=10.1006/bbrc.1995.1108;
Li L., Yoo H., Becker F.F., Ali-Osman F., Chan J.Y.-H.;
"Identification of a brain- and reproductive-organs-specific gene
responsive to DNA damage and retinoic acid.";
Biochem. Biophys. Res. Commun. 206:764-774(1995).
[2] {ECO:0000305, ECO:0000312|EMBL:AAL17818.1}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 4), TISSUE SPECIFICITY, AND
INDUCTION.
TISSUE=Monocyte {ECO:0000269|PubMed:11676476};
PubMed=11676476; DOI=10.1006/bbrc.2001.5801;
Ching A.K.K., Li P.S., Li Q., Chan B.C.L., Chan J.Y.-H., Lim P.L.,
Pang J.C.S., Chui Y.L.;
"Expression of human BRE in multiple isoforms.";
Biochem. Biophys. Res. Commun. 288:535-545(2001).
[3] {ECO:0000305, ECO:0000312|EMBL:AAR30499.1}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, AND IDENTIFICATION
IN BRCC COMPLEX.
PubMed=14636569; DOI=10.1016/S1097-2765(03)00424-6;
Dong Y., Hakimi M.-A., Chen X., Kumaraswamy E., Cooch N.S.,
Godwin A.K., Shiekhattar R.;
"Regulation of BRCC, a holoenzyme complex containing BRCA1 and BRCA2,
by a signalosome-like subunit and its role in DNA repair.";
Mol. Cell 12:1087-1099(2003).
[4] {ECO:0000305, ECO:0000312|EMBL:AAB69387.1}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Keeton K.R., Miles W.M.;
Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases.
[5] {ECO:0000305, ECO:0000312|EMBL:BAA90943.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Colon {ECO:0000312|EMBL:BAA90943.1}, and Teratocarcinoma;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[7] {ECO:0000305, ECO:0000312|EMBL:AAB69387.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[8] {ECO:0000305, ECO:0000312|EMBL:AAH01251.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Cervix {ECO:0000312|EMBL:AAH01251.1};
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9] {ECO:0000305}
FUNCTION, INTERACTION WITH FAS AND TNFRSF1A, AND SUBCELLULAR LOCATION.
PubMed=15465831; DOI=10.1074/jbc.M408678200;
Li Q., Ching A.K.-K., Chan B.C.-L., Chow S.K.-Y., Lim P.-L.,
Ho T.C.-Y., Ip W.-K., Wong C.-K., Lam C.W.-K., Lee K.K.-H.,
Chan J.Y.-H., Chui Y.-L.;
"A death receptor-associated anti-apoptotic protein, BRE, inhibits
mitochondrial apoptotic pathway.";
J. Biol. Chem. 279:52106-52116(2004).
[10]
IDENTIFICATION IN THE BRCA1-A COMPLEX.
PubMed=17525341; DOI=10.1126/science.1139516;
Sobhian B., Shao G., Lilli D.R., Culhane A.C., Moreau L.A., Xia B.,
Livingston D.M., Greenberg R.A.;
"RAP80 targets BRCA1 to specific ubiquitin structures at DNA damage
sites.";
Science 316:1198-1202(2007).
[11]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[12]
IDENTIFICATION IN THE BRISC COMPLEX.
PubMed=19214193; DOI=10.1038/emboj.2009.27;
Cooper E.M., Cutcliffe C., Kristiansen T.Z., Pandey A., Pickart C.M.,
Cohen R.E.;
"K63-specific deubiquitination by two JAMM/MPN+ complexes: BRISC-
associated Brcc36 and proteasomal Poh1.";
EMBO J. 28:621-631(2009).
[13]
IDENTIFICATION IN THE BRCA1-A COMPLEX.
PubMed=19261746; DOI=10.1101/gad.1739609;
Shao G., Patterson-Fortin J., Messick T.E., Feng D., Shanbhag N.,
Wang Y., Greenberg R.A.;
"MERIT40 controls BRCA1-Rap80 complex integrity and recruitment to DNA
double-strand breaks.";
Genes Dev. 23:740-754(2009).
[14]
FUNCTION, IDENTIFICATION IN THE BRCA1-A COMPLEX, DOMAIN UEV-LIKE,
UBIQUITIN-BINDING, AND INTERACTION WITH ABRAXAS1.
PubMed=19261749; DOI=10.1101/gad.1770309;
Wang B., Hurov K., Hofmann K., Elledge S.J.;
"NBA1, a new player in the Brca1 A complex, is required for DNA damage
resistance and checkpoint control.";
Genes Dev. 23:729-739(2009).
[15]
FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE
BRCA1-A COMPLEX, SUBCELLULAR LOCATION, AND INTERACTION WITH ABRAXAS1;
BABAM1 AND BRCC3.
PubMed=19261748; DOI=10.1101/gad.1770609;
Feng L., Huang J., Chen J.;
"MERIT40 facilitates BRCA1 localization and DNA damage repair.";
Genes Dev. 23:719-728(2009).
[16]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE
SCALE ANALYSIS] AT SER-2, AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[18]
IDENTIFICATION IN ARISC COMPLEX, IDENTIFICATION IN BRISC COMPLEX, AND
INTERACTION WITH BABAM1.
PubMed=21282113; DOI=10.1074/jbc.M110.200857;
Hu X., Kim J.A., Castillo A., Huang M., Liu J., Wang B.;
"NBA1/MERIT40 and BRE interaction is required for the integrity of two
distinct deubiquitinating enzyme BRCC36-containing complexes.";
J. Biol. Chem. 286:11734-11745(2011).
[19]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[20]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[21]
FUNCTION, IDENTIFICATION IN THE BRISC COMPLEX, IDENTIFICATION BY MASS
SPECTROMETRY, IDENTIFICATION IN THE ARISC COMPLEX, AND SUBCELLULAR
LOCATION.
PubMed=24075985; DOI=10.1016/j.celrep.2013.08.025;
Zheng H., Gupta V., Patterson-Fortin J., Bhattacharya S.,
Katlinski K., Wu J., Varghese B., Carbone C.J., Aressy B., Fuchs S.Y.,
Greenberg R.A.;
"A BRISC-SHMT complex deubiquitinates IFNAR1 and regulates interferon
responses.";
Cell Rep. 5:180-193(2013).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[23]
IDENTIFICATION IN THE BRISC COMPLEX.
PubMed=25283148; DOI=10.1038/ncomms6059;
Zhang J., Cao M., Dong J., Li C., Xu W., Zhan Y., Wang X., Yu M.,
Ge C., Ge Z., Yang X.;
"ABRO1 suppresses tumourigenesis and regulates the DNA damage response
by stabilizing p53.";
Nat. Commun. 5:5059-5059(2014).
[24]
FUNCTION OF THE BRISC COMPLEX.
PubMed=26195665; DOI=10.1083/jcb.201503039;
Yan K., Li L., Wang X., Hong R., Zhang Y., Yang H., Lin M., Zhang S.,
He Q., Zheng D., Tang J., Yin Y., Shao G.;
"The deubiquitinating enzyme complex BRISC is required for proper
mitotic spindle assembly in mammalian cells.";
J. Cell Biol. 210:209-224(2015).
-!- FUNCTION: Component of the BRCA1-A complex, a complex that
specifically recognizes 'Lys-63'-linked ubiquitinated histones H2A
and H2AX at DNA lesions sites, leading to target the BRCA1-BARD1
heterodimer to sites of DNA damage at double-strand breaks (DSBs).
The BRCA1-A complex also possesses deubiquitinase activity that
specifically removes 'Lys-63'-linked ubiquitin on histones H2A and
H2AX (PubMed:17525341, PubMed:19261746, PubMed:19261749,
PubMed:19261748). In the BRCA1-A complex, it acts as an adapter
that bridges the interaction between BABAM1/NBA1 and the rest of
the complex, thereby being required for the complex integrity and
modulating the E3 ubiquitin ligase activity of the BRCA1-BARD1
heterodimer (PubMed:21282113, PubMed:19261748). Component of the
BRISC complex, a multiprotein complex that specifically cleaves
'Lys-63'-linked ubiquitin in various substrates (PubMed:19214193,
PubMed:24075985, PubMed:25283148, PubMed:26195665). Within the
BRISC complex, acts as an adapter that bridges the interaction
between BABAM1/NBA1 and the rest of the complex, thereby being
required for the complex integrity (PubMed:21282113). The BRISC
complex is required for normal mitotic spindle assembly and
microtubule attachment to kinetochores via its role in
deubiquitinating NUMA1 (PubMed:26195665). The BRISC complex plays
a role in interferon signaling via its role in the
deubiquitination of the interferon receptor IFNAR1;
deubiquitination increases IFNAR1 activity by enhancing its
stability and cell surface expression (PubMed:24075985). Down-
regulates the response to bacterial lipopolysaccharide (LPS) via
its role in IFNAR1 deubiquitination (PubMed:24075985). May play a
role in homeostasis or cellular differentiation in cells of
neural, epithelial and germline origins. May also act as a death
receptor-associated anti-apoptotic protein, which inhibits the
mitochondrial apoptotic pathway. May regulate TNF-alpha signaling
through its interactions with TNFRSF1A; however these effects may
be indirect (PubMed:15465831). {ECO:0000269|PubMed:14636569,
ECO:0000269|PubMed:19261748, ECO:0000269|PubMed:19261749,
ECO:0000269|PubMed:24075985, ECO:0000269|PubMed:26195665,
ECO:0000305|PubMed:15465831}.
-!- SUBUNIT: Component of the ARISC complex, at least composed of
UIMC1/RAP80, ABRAXAS1, BRCC3/BRCC36, BABAM2 and BABAM1/NBA1
(PubMed:21282113, PubMed:24075985). Component of the BRCA1-A
complex, at least composed of BRCA1, BARD1, UIMC1/RAP80, ABRAXAS1,
BRCC3/BRCC36, BABAM2 and BABAM1/NBA1. In the BRCA1-A complex,
interacts directly with ABRAXAS1, BRCC3/BRCC36 and BABAM1/NBA1.
Binds polyubiquitin. Component of the BRISC complex, at least
composed of ABRAXAS2, BRCC3/BRCC36, BABAM2 and BABAM1/NBA1
(PubMed:19214193, PubMed:21282113, PubMed:24075985,
PubMed:25283148). Identified in a complex with SHMT2 and the other
subunits of the BRISC complex (PubMed:24075985). Component of the
BRCA1/BRCA2 containing complex (BRCC), which also contains BRCA1,
BRCA2, BARD1, BRCC3/BRCC36 and RAD51. BRCC is a ubiquitin E3
ligase complex that enhances cellular survival following DNA
damage. May interact with FAS and TNFRSF1A (PubMed:15465831).
{ECO:0000269|PubMed:14636569, ECO:0000269|PubMed:17525341,
ECO:0000269|PubMed:19214193, ECO:0000269|PubMed:19261746,
ECO:0000269|PubMed:19261748, ECO:0000269|PubMed:19261749,
ECO:0000269|PubMed:24075985, ECO:0000269|PubMed:25283148,
ECO:0000305|PubMed:15465831}.
-!- INTERACTION:
Q9NWV8:BABAM1; NbExp=3; IntAct=EBI-949389, EBI-745725;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15465831,
ECO:0000269|PubMed:24075985}. Nucleus
{ECO:0000269|PubMed:15465831, ECO:0000269|PubMed:19261748,
ECO:0000269|PubMed:24075985}. Note=Localizes at sites of DNA
damage at double-strand breaks (DSBs).
{ECO:0000269|PubMed:19261748}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Comment=Additional isoforms may exist. {ECO:0000305};
Name=2 {ECO:0000269|PubMed:14636569};
IsoId=Q9NXR7-2; Sequence=Displayed;
Name=1 {ECO:0000305};
IsoId=Q9NXR7-1; Sequence=VSP_051956;
Name=3 {ECO:0000269|PubMed:11676476}; Synonyms=Alpha a';
IsoId=Q9NXR7-3; Sequence=VSP_051957;
Name=4;
IsoId=Q9NXR7-4; Sequence=VSP_037261;
-!- TISSUE SPECIFICITY: Expressed in all cell lines examined. Highly
expressed in placenta. {ECO:0000269|PubMed:11676476}.
-!- INDUCTION: Down-regulated by DNA-damaging agents in fibroblasts,
by retinoic acid in brain glioma U-251MG and promyelocytic HL-60
cell lines, and by bacterial lipopolysaccharides (LPS) in
peripheral blood mononuclear cells (PBMC).
{ECO:0000269|PubMed:11676476, ECO:0000269|PubMed:7826398}.
-!- DOMAIN: Contains 2 ubiquitin-conjugating enzyme family-like (UEV-
like) regions. These regions lack the critical Cys residues
required for ubiquitination but retain the ability to bind
ubiquitin. {ECO:0000269|PubMed:19261749}.
-!- SIMILARITY: Belongs to the BABAM2 family. {ECO:0000255}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/BREID839ch2p23.html";
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EMBL; L38616; AAA64231.1; -; mRNA.
EMBL; AF420605; AAL17818.1; -; mRNA.
EMBL; AY438031; AAR30499.1; -; mRNA.
EMBL; AF015767; AAB69387.1; -; mRNA.
EMBL; AF420602; AAL17814.1; -; mRNA.
EMBL; AF420603; AAL17816.1; -; mRNA.
EMBL; AK000097; BAA90943.1; -; mRNA.
EMBL; AK291086; BAF83775.1; -; mRNA.
EMBL; AC021171; AAY24156.1; -; Genomic_DNA.
EMBL; AC093690; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC096552; AAX88935.1; -; Genomic_DNA.
EMBL; CH471053; EAX00545.1; -; Genomic_DNA.
EMBL; CH471053; EAX00546.1; -; Genomic_DNA.
EMBL; CH471053; EAX00547.1; -; Genomic_DNA.
EMBL; CH471053; EAX00548.1; -; Genomic_DNA.
EMBL; BC001251; AAH01251.1; -; mRNA.
CCDS; CCDS1763.1; -. [Q9NXR7-2]
CCDS; CCDS1764.1; -. [Q9NXR7-1]
CCDS; CCDS1765.1; -. [Q9NXR7-4]
PIR; JC2472; JC2472.
RefSeq; NP_001248769.1; NM_001261840.1. [Q9NXR7-3]
RefSeq; NP_001316041.1; NM_001329112.1. [Q9NXR7-2]
RefSeq; NP_001316042.1; NM_001329113.1. [Q9NXR7-1]
RefSeq; NP_004890.2; NM_004899.4. [Q9NXR7-1]
RefSeq; NP_954661.1; NM_199191.2. [Q9NXR7-2]
RefSeq; NP_954662.1; NM_199192.2. [Q9NXR7-4]
RefSeq; NP_954663.1; NM_199193.2. [Q9NXR7-4]
RefSeq; NP_954664.1; NM_199194.2. [Q9NXR7-2]
UniGene; Hs.258314; -.
ProteinModelPortal; Q9NXR7; -.
BioGrid; 114946; 61.
CORUM; Q9NXR7; -.
IntAct; Q9NXR7; 24.
MINT; MINT-2867020; -.
STRING; 9606.ENSP00000343412; -.
BindingDB; Q9NXR7; -.
iPTMnet; Q9NXR7; -.
PhosphoSitePlus; Q9NXR7; -.
BioMuta; BRE; -.
DMDM; 229462810; -.
EPD; Q9NXR7; -.
PaxDb; Q9NXR7; -.
PeptideAtlas; Q9NXR7; -.
PRIDE; Q9NXR7; -.
DNASU; 9577; -.
Ensembl; ENST00000342045; ENSP00000339371; ENSG00000158019. [Q9NXR7-2]
Ensembl; ENST00000344773; ENSP00000343412; ENSG00000158019. [Q9NXR7-1]
Ensembl; ENST00000361704; ENSP00000354699; ENSG00000158019. [Q9NXR7-4]
Ensembl; ENST00000379624; ENSP00000368945; ENSG00000158019. [Q9NXR7-2]
Ensembl; ENST00000379632; ENSP00000368953; ENSG00000158019. [Q9NXR7-4]
GeneID; 9577; -.
KEGG; hsa:9577; -.
UCSC; uc002rlq.4; human. [Q9NXR7-2]
CTD; 9577; -.
DisGeNET; 9577; -.
EuPathDB; HostDB:ENSG00000158019.20; -.
GeneCards; BABAM2; -.
HGNC; HGNC:1106; BABAM2.
HPA; HPA017926; -.
MIM; 610497; gene.
neXtProt; NX_Q9NXR7; -.
OpenTargets; ENSG00000158019; -.
PharmGKB; PA25419; -.
eggNOG; ENOG410IFRG; Eukaryota.
eggNOG; ENOG410Y1T7; LUCA.
GeneTree; ENSGT00390000004208; -.
HOVERGEN; HBG071492; -.
InParanoid; Q9NXR7; -.
KO; K12173; -.
OMA; FSNIPVY; -.
OrthoDB; EOG091G0TW1; -.
PhylomeDB; Q9NXR7; -.
TreeFam; TF328507; -.
Reactome; R-HSA-5689901; Metalloprotease DUBs.
Reactome; R-HSA-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
Reactome; R-HSA-5693571; Nonhomologous End-Joining (NHEJ).
Reactome; R-HSA-5693607; Processing of DNA double-strand break ends.
Reactome; R-HSA-69473; G2/M DNA damage checkpoint.
ChiTaRS; BRE; human.
GeneWiki; BRE_(gene); -.
GenomeRNAi; 9577; -.
PRO; PR:Q9NXR7; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000158019; -.
CleanEx; HS_BRE; -.
ExpressionAtlas; Q9NXR7; baseline and differential.
Genevisible; Q9NXR7; HS.
GO; GO:0070531; C:BRCA1-A complex; IDA:UniProtKB.
GO; GO:0070552; C:BRISC complex; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0000152; C:nuclear ubiquitin ligase complex; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0000268; F:peroxisome targeting sequence binding; TAS:UniProtKB.
GO; GO:0031593; F:polyubiquitin modification-dependent protein binding; IDA:UniProtKB.
GO; GO:0005164; F:tumor necrosis factor receptor binding; IDA:UniProtKB.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0006974; P:cellular response to DNA damage stimulus; IEP:UniProtKB.
GO; GO:0016569; P:covalent chromatin modification; IEA:UniProtKB-KW.
GO; GO:0006302; P:double-strand break repair; IMP:UniProtKB.
GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; TAS:Reactome.
GO; GO:0031572; P:G2 DNA damage checkpoint; IMP:UniProtKB.
GO; GO:0043066; P:negative regulation of apoptotic process; IDA:UniProtKB.
GO; GO:0045739; P:positive regulation of DNA repair; IMP:UniProtKB.
GO; GO:0016579; P:protein deubiquitination; TAS:Reactome.
GO; GO:0070536; P:protein K63-linked deubiquitination; IC:UniProtKB.
GO; GO:0010212; P:response to ionizing radiation; IMP:UniProtKB.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
Gene3D; 3.10.110.10; -; 2.
InterPro; IPR010358; BRE.
InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
PANTHER; PTHR15189; PTHR15189; 1.
Pfam; PF06113; BRE; 1.
1: Evidence at protein level;
Acetylation; Alternative splicing; Apoptosis; Cell cycle;
Cell division; Chromatin regulator; Complete proteome; Cytoplasm;
DNA damage; DNA repair; Mitosis; Nucleus; Phosphoprotein;
Reference proteome; Repeat; Ubl conjugation pathway.
CHAIN 1 383 BRISC and BRCA1-A complex member 2.
/FTId=PRO_0000224189.
REGION 30 147 UEV-like 1.
REGION 275 364 UEV-like 2.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:22223895}.
MOD_RES 2 2 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
VAR_SEQ 363 383 KAYFKTFVPQFQEAAFANGKL -> NSRRQHLPMESSRKHQ
S (in isoform 3).
{ECO:0000303|PubMed:11676476}.
/FTId=VSP_051957.
VAR_SEQ 364 383 AYFKTFVPQFQEAAFANGKL -> GCQGSRDACSPWEQVLA
FAVAKTGCKLLQPQRNWPSSRGPPWRASEGERTAQ (in
isoform 1).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_051956.
VAR_SEQ 364 383 AYFKTFVPQFQEAAFANGKL -> RESNRDGEESSSA (in
isoform 4).
{ECO:0000303|PubMed:11676476}.
/FTId=VSP_037261.
CONFLICT 192 192 V -> L (in Ref. 5; BAF83775).
{ECO:0000305}.
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


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