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BRISC and BRCA1-A complex member 1 (Mediator of RAP80 interactions and targeting subunit of 40 kDa) (New component of the BRCA1-A complex)

 BABA1_HUMAN             Reviewed;         329 AA.
Q9NWV8; A8MQT0; B4DRY9; B4DVR1; Q6FIA0; Q9P018;
29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
01-OCT-2000, sequence version 1.
25-OCT-2017, entry version 129.
RecName: Full=BRISC and BRCA1-A complex member 1;
AltName: Full=Mediator of RAP80 interactions and targeting subunit of 40 kDa {ECO:0000303|PubMed:19261746};
AltName: Full=New component of the BRCA1-A complex {ECO:0000303|PubMed:19261749};
Name=BABAM1;
Synonyms=C19orf62, MERIT40 {ECO:0000303|PubMed:19261746},
NBA1 {ECO:0000303|PubMed:19261749}; ORFNames=HSPC142;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Umbilical cord blood;
PubMed=11042152; DOI=10.1101/gr.140200;
Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
"Cloning and functional analysis of cDNAs with open reading frames for
300 previously undefined genes expressed in CD34+ hematopoietic
stem/progenitor cells.";
Genome Res. 10:1546-1560(2000).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=11230166; DOI=10.1101/gr.GR1547R;
Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H.,
Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N.,
Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D.,
Wambutt R., Korn B., Klein M., Poustka A.;
"Towards a catalog of human genes and proteins: sequencing and
analysis of 500 novel complete protein coding human cDNAs.";
Genome Res. 11:422-435(2001).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
TISSUE=Brain, and Spleen;
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).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15057824; DOI=10.1038/nature02399;
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
Rubin E.M., Lucas S.M.;
"The DNA sequence and biology of human chromosome 19.";
Nature 428:529-535(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Ovary, Pituitary, and Placenta;
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).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-62, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49 AND SER-66, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[10]
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).
[11]
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).
[12]
FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE
BRCA1-A COMPLEX, AND SUBCELLULAR LOCATION.
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).
[13]
FUNCTION, IDENTIFICATION IN THE BRCA1-A COMPLEX, SUBCELLULAR LOCATION,
DOMAIN VWFA-LIKE, 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).
[14]
FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE
BRCA1-A COMPLEX, SUBCELLULAR LOCATION, AND INTERACTION WITH BABAM2.
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).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29; SER-49; THR-65 AND
SER-66, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[16]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, 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 BRISC COMPLEX, IDENTIFICATION IN THE BRCA1-A
COMPLEX, INTERACTION WITH BABAM2, AND SUBCELLULAR LOCATION.
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, PHOSPHORYLATION [LARGE
SCALE ANALYSIS] AT SER-49, AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[20]
FUNCTION, IDENTIFICATION IN THE BRISC COMPLEX, IDENTIFICATION IN THE
ARISC COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY, 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).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49; SER-57 AND SER-62,
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).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-62 AND SER-66, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[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.
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. In the BRCA1-A complex, it is required for the complex
integrity and its localization at DSBs. Component of the BRISC
complex, a multiprotein complex that specifically cleaves 'Lys-
63'-linked ubiquitin in various substrates (PubMed:24075985,
PubMed:26195665). In these 2 complexes, it is probably required to
maintain the stability of BABAM2 and help the 'Lys-63'-linked
deubiquitinase activity mediated by BRCC3/BRCC36 component. The
BRISC complex is required for normal mitotic spindle assembly and
microtubule attachment to kinetochores via its role in
deubiquitinating NUMA1 (PubMed:26195665). 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). {ECO:0000269|PubMed:19261746,
ECO:0000269|PubMed:19261748, ECO:0000269|PubMed:19261749}.
-!- SUBUNIT: Component of the ARISC complex, at least composed of
UIMC1/RAP80, ABRAXAS1, BRCC3/BRCC36, BABAM2 and BABAM1/NBA1
(PubMed:24075985). Component of the BRCA1-A complex, at least
composed of BRCA1, BARD1, UIMC1/RAP80, ABRAXAS1, BRCC3/BRCC36,
BABAM2 and BABAM1/NBA1 (PubMed:19261746, PubMed:19261749,
PubMed:19261748, PubMed:21282113). In the BRCA1-A complex,
interacts directly with ABRAXAS1 and BABAM2 (PubMed:19261749,
PubMed:19261748). 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).
{ECO:0000269|PubMed:19214193, ECO:0000269|PubMed:19261746,
ECO:0000269|PubMed:19261748, ECO:0000269|PubMed:19261749,
ECO:0000269|PubMed:21282113, ECO:0000269|PubMed:24075985,
ECO:0000269|PubMed:25283148}.
-!- INTERACTION:
Q9NXR7:BABAM2; NbExp=3; IntAct=EBI-745725, EBI-949389;
Q9NYB0:TERF2IP; NbExp=2; IntAct=EBI-745725, EBI-750109;
Q9H2K2:TNKS2; NbExp=4; IntAct=EBI-745725, EBI-4398527;
P14373:TRIM27; NbExp=5; IntAct=EBI-745725, EBI-719493;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19261749,
ECO:0000269|PubMed:24075985}. Nucleus
{ECO:0000269|PubMed:19261746, ECO:0000269|PubMed:19261748,
ECO:0000269|PubMed:19261749, ECO:0000269|PubMed:21282113,
ECO:0000269|PubMed:24075985}. Note=Localizes at sites of DNA
damage at double-strand breaks (DSBs).
{ECO:0000269|PubMed:19261746, ECO:0000269|PubMed:19261748,
ECO:0000269|PubMed:19261749, ECO:0000269|PubMed:21282113}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q9NWV8-1; Sequence=Displayed;
Name=2;
IsoId=Q9NWV8-2; Sequence=VSP_037246, VSP_037249;
Note=No experimental confirmation available.;
Name=3;
IsoId=Q9NWV8-3; Sequence=VSP_037247, VSP_037248;
Note=No experimental confirmation available.;
-!- DOMAIN: The VWFA-like region is similar to the VWFA domain. Its
presence reveals similarities between the structure of the 19S
proteasome and the BRCA1-A complexes.
{ECO:0000269|PubMed:19261749}.
-!- SIMILARITY: Belongs to the BABAM1 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAF29106.1; Type=Frameshift; Positions=263; Evidence={ECO:0000305};
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EMBL; AF161491; AAF29106.1; ALT_FRAME; mRNA.
EMBL; AL136692; CAB66627.1; -; mRNA.
EMBL; AK000578; BAA91268.1; -; mRNA.
EMBL; AK299493; BAG61451.1; -; mRNA.
EMBL; AK301193; BAG62773.1; -; mRNA.
EMBL; CR533526; CAG38557.1; -; mRNA.
EMBL; AC104522; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC000788; AAH00788.1; -; mRNA.
EMBL; BC006244; AAH06244.1; -; mRNA.
EMBL; BC091491; AAH91491.1; -; mRNA.
CCDS; CCDS46012.1; -. [Q9NWV8-1]
RefSeq; NP_001028721.1; NM_001033549.2. [Q9NWV8-1]
RefSeq; NP_001275685.1; NM_001288756.1. [Q9NWV8-1]
RefSeq; NP_001275686.1; NM_001288757.1.
RefSeq; NP_054892.2; NM_014173.3. [Q9NWV8-1]
UniGene; Hs.190722; -.
ProteinModelPortal; Q9NWV8; -.
BioGrid; 118855; 70.
ELM; Q9NWV8; -.
IntAct; Q9NWV8; 52.
MINT; MINT-4712566; -.
STRING; 9606.ENSP00000352408; -.
BindingDB; Q9NWV8; -.
iPTMnet; Q9NWV8; -.
PhosphoSitePlus; Q9NWV8; -.
DMDM; 74734678; -.
EPD; Q9NWV8; -.
MaxQB; Q9NWV8; -.
PaxDb; Q9NWV8; -.
PeptideAtlas; Q9NWV8; -.
PRIDE; Q9NWV8; -.
DNASU; 29086; -.
Ensembl; ENST00000359435; ENSP00000352408; ENSG00000105393. [Q9NWV8-1]
Ensembl; ENST00000598188; ENSP00000471605; ENSG00000105393. [Q9NWV8-1]
Ensembl; ENST00000601043; ENSP00000470920; ENSG00000105393. [Q9NWV8-1]
GeneID; 29086; -.
KEGG; hsa:29086; -.
UCSC; uc002nfu.5; human. [Q9NWV8-1]
CTD; 29086; -.
DisGeNET; 29086; -.
EuPathDB; HostDB:ENSG00000105393.15; -.
GeneCards; BABAM1; -.
H-InvDB; HIX0014885; -.
HGNC; HGNC:25008; BABAM1.
HPA; HPA054386; -.
HPA; HPA068786; -.
MIM; 612766; gene.
neXtProt; NX_Q9NWV8; -.
OpenTargets; ENSG00000105393; -.
PharmGKB; PA162378767; -.
eggNOG; ENOG410IF7E; Eukaryota.
eggNOG; ENOG4111NFW; LUCA.
GeneTree; ENSGT00390000016934; -.
InParanoid; Q9NWV8; -.
KO; K20776; -.
OMA; RPFQSHA; -.
OrthoDB; EOG091G0SJH; -.
PhylomeDB; Q9NWV8; -.
TreeFam; TF329070; -.
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; BABAM1; human.
GeneWiki; C19orf62; -.
GenomeRNAi; 29086; -.
PRO; PR:Q9NWV8; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000105393; -.
CleanEx; HS_C19orf62; -.
ExpressionAtlas; Q9NWV8; baseline and differential.
Genevisible; Q9NWV8; 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:0016604; C:nuclear body; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
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:0071425; P:hematopoietic stem cell proliferation; IEA:Ensembl.
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; IMP:UniProtKB.
GO; GO:0010212; P:response to ionizing radiation; IMP:UniProtKB.
Gene3D; 3.40.50.410; -; 1.
InterPro; IPR026126; BABAM1.
InterPro; IPR036465; vWFA_dom_sf.
PANTHER; PTHR15660; PTHR15660; 1.
SUPFAM; SSF53300; SSF53300; 1.
1: Evidence at protein level;
Acetylation; Alternative splicing; Cell cycle; Cell division;
Chromatin regulator; Complete proteome; Cytoplasm; DNA damage;
DNA repair; Mitosis; Nucleus; Phosphoprotein; Reference proteome;
Ubl conjugation pathway.
CHAIN 1 329 BRISC and BRCA1-A complex member 1.
/FTId=PRO_0000288458.
REGION 95 298 VWFA-like.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692}.
MOD_RES 8 8 Phosphoserine.
{ECO:0000250|UniProtKB:Q5XIJ6}.
MOD_RES 29 29 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 49 49 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 57 57 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 62 62 Phosphoserine.
{ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 65 65 Phosphothreonine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 66 66 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:24275569}.
VAR_SEQ 1 115 MEVAEPSSPTEEEEEEEEHSAEPRPRTRSNPEGAEDRAVGA
QASVGSRSEGEGEAASADDGSLNTSGAGPKSWQVPPPAPEV
QIRTPRVNCPEKVIICLDLSEEMSLPKLESFNG -> MMGA
STLQEPALSPGRCPRQPLRSKFGHHGSTVQRKC (in
isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_037246.
VAR_SEQ 116 190 Missing (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_037247.
VAR_SEQ 234 329 KMFQCPYFFFDVVYIHNGTEEKEEEMSWKDMFAFMGSLDTK
GTSYKYEVALAGPALELHNCMAKLLAHPLQRPCQSHASYSL
LEEEDEAIEVEATV -> VGEAWEREGCLQP (in
isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_037248.
VAR_SEQ 263 329 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_037249.
CONFLICT 76 76 P -> S (in Ref. 4; CAG38557).
{ECO:0000305}.
CONFLICT 288 288 A -> V (in Ref. 4; CAG38557).
{ECO:0000305}.
CONFLICT 302 302 P -> S (in Ref. 4; CAG38557).
{ECO:0000305}.
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


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