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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_RAT               Reviewed;         383 AA.
Q6P7Q1;
21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
05-JUL-2004, sequence version 1.
25-OCT-2017, entry version 95.
RecName: Full=BRISC and BRCA1-A complex member 2;
AltName: Full=BRCA1-A complex subunit BRE;
AltName: Full=BRCA1/BRCA2-containing complex subunit 45;
AltName: Full=Brain and reproductive organ-expressed protein;
Name=Babam2 {ECO:0000312|RGD:735111}; Synonyms=Bre;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Pituitary;
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).
[2]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- 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 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.
Component of the BRISC complex, a multiprotein complex that
specifically cleaves 'Lys-63'-linked ubiquitin in various
substrates. 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. The
BRISC complex is required for normal mitotic spindle assembly and
microtubule attachment to kinetochores via its role in
deubiquitinating NUMA1. 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.
Down-regulates the response to bacterial lipopolysaccharide (LPS)
via its role in IFNAR1 deubiquitination. 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. {ECO:0000250|UniProtKB:Q9NXR7}.
-!- SUBUNIT: Component of the ARISC complex, at least composed of
UIMC1/RAP80, ABRAXAS1, BRCC3/BRCC36, BABAM2 and BABAM1/NBA1.
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. Identified in a complex with
SHMT2 and the other subunits of the BRISC complex. 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.
{ECO:0000250|UniProtKB:Q9NXR7}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9NXR7}.
Nucleus {ECO:0000250|UniProtKB:Q9NXR7}. Note=Localizes at sites of
DNA damage at double-strand breaks (DSBs).
{ECO:0000250|UniProtKB:Q9NXR7}.
-!- 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:0000250|UniProtKB:Q9NXR7}.
-!- SIMILARITY: Belongs to the BABAM2 family. {ECO:0000255}.
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EMBL; BC061573; AAH61573.1; -; mRNA.
RefSeq; NP_954891.1; NM_199270.1.
RefSeq; XP_006239864.1; XM_006239802.3.
RefSeq; XP_017449703.1; XM_017594214.1.
UniGene; Rn.224501; -.
STRING; 10116.ENSRNOP00000005855; -.
iPTMnet; Q6P7Q1; -.
PhosphoSitePlus; Q6P7Q1; -.
PaxDb; Q6P7Q1; -.
PRIDE; Q6P7Q1; -.
Ensembl; ENSRNOT00000005855; ENSRNOP00000005855; ENSRNOG00000004364.
GeneID; 362704; -.
KEGG; rno:362704; -.
CTD; 9577; -.
RGD; 735111; Babam2.
eggNOG; ENOG410IFRG; Eukaryota.
eggNOG; ENOG410Y1T7; LUCA.
GeneTree; ENSGT00390000004208; -.
HOGENOM; HOG000095259; -.
HOVERGEN; HBG071492; -.
InParanoid; Q6P7Q1; -.
KO; K12173; -.
OMA; FSNIPVY; -.
OrthoDB; EOG091G0TW1; -.
PhylomeDB; Q6P7Q1; -.
TreeFam; TF328507; -.
Reactome; R-RNO-5689901; Metalloprotease DUBs.
Reactome; R-RNO-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
Reactome; R-RNO-5693571; Nonhomologous End-Joining (NHEJ).
Reactome; R-RNO-5693607; Processing of DNA double-strand break ends.
Reactome; R-RNO-69473; G2/M DNA damage checkpoint.
PRO; PR:Q6P7Q1; -.
Proteomes; UP000002494; Chromosome 6.
Bgee; ENSRNOG00000004364; -.
Genevisible; Q6P7Q1; RN.
GO; GO:0070531; C:BRCA1-A complex; ISS:UniProtKB.
GO; GO:0070552; C:BRISC complex; ISS:UniProtKB.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005829; C:cytosol; IEA:Ensembl.
GO; GO:0000152; C:nuclear ubiquitin ligase complex; ISS:UniProtKB.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0031593; F:polyubiquitin modification-dependent protein binding; ISS:UniProtKB.
GO; GO:0005164; F:tumor necrosis factor receptor binding; ISS: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; ISS:UniProtKB.
GO; GO:0016569; P:covalent chromatin modification; IEA:UniProtKB-KW.
GO; GO:0006302; P:double-strand break repair; ISS:UniProtKB.
GO; GO:0031572; P:G2 DNA damage checkpoint; ISS:UniProtKB.
GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
GO; GO:0045739; P:positive regulation of DNA repair; ISS:UniProtKB.
GO; GO:0010212; P:response to ionizing radiation; ISS:UniProtKB.
Gene3D; 3.10.110.10; -; 1.
InterPro; IPR010358; BRE.
InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
PANTHER; PTHR15189; PTHR15189; 1.
Pfam; PF06113; BRE; 1.
1: Evidence at protein level;
Acetylation; 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_0000224191.
REGION 30 147 UEV-like 1.
REGION 275 364 UEV-like 2.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000250|UniProtKB:Q9NXR7}.
MOD_RES 2 2 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
SEQUENCE 383 AA; 43559 MW; 10DA729CD8AF83A2 CRC64;
MSPEIALNRI SPMLSPFISS VVRNGKVGLD ATNCLRITDL KSGCTSLTPG PNCDRFKLHI
PYAGETLKWD IIFNAQYPEL PPDFIFGEDA EFLPDPSALH NLASWNPSNP ECLLLVVKEL
VQQYHQFQCG RLRESSRLMF EYQTLLEEPQ YGENMEIYAG KKNNWTGEFS ARFLLKLPVD
FSNIPTYLLK DVNEDPGEDV ALLSVSFEDT EATQVYPKLY LSPRIEHALG GSSALHIPAF
PGGGCLIDYV PQVCHLLTNK VQYVIQGYHK RREYIAAFLS HFGTGVVEYD AEGFTKLTLL
LMWKEFCFLV HIDLPLFFPR DQPTLTFQSV YHFTNSGQLY SQAQKNYPYS PRWDGNEMAK
RAKAYFKTFV PQFQEAAFAN GKL


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