BABA2_MESAU
ID BABA2_MESAU Reviewed; 383 AA.
AC Q6SP92;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 58.
DE RecName: Full=BRISC and BRCA1-A complex member 2;
DE AltName: Full=BRCA1-A complex subunit BRE;
DE AltName: Full=BRCA1/BRCA2-containing complex subunit 45;
DE AltName: Full=Brain and reproductive organ-expressed protein;
GN Name=Babam2; Synonyms=Bre;
OS Mesocricetus auratus (Golden hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Mesocricetus.
OX NCBI_TaxID=10036;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Ching A.K.K., Chui Y.L.;
RT "Comparison of mouse and primate BRE sequences.";
RL Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases.
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 acts as an adapter that bridges the interaction between BABAM1/NBA1 and
CC the rest of the complex, thereby being required for the complex
CC integrity and modulating the E3 ubiquitin ligase activity of the BRCA1-
CC BARD1 heterodimer. Component of the BRISC complex, a multiprotein
CC complex that specifically cleaves 'Lys-63'-linked ubiquitin in various
CC substrates. Within the BRISC complex, acts as an adapter that bridges
CC the interaction between BABAM1/NBA1 and the rest of the complex,
CC thereby being required for the complex integrity. The BRISC complex is
CC required for normal mitotic spindle assembly and microtubule attachment
CC to kinetochores via its role in deubiquitinating NUMA1. The BRISC
CC complex plays a role in interferon signaling via its role in the
CC deubiquitination of the interferon receptor IFNAR1; deubiquitination
CC increases IFNAR1 activity by enhancing its stability and cell surface
CC expression. Down-regulates the response to bacterial lipopolysaccharide
CC (LPS) via its role in IFNAR1 deubiquitination. May play a role in
CC homeostasis or cellular differentiation in cells of neural, epithelial
CC and germline origins. May also act as a death receptor-associated anti-
CC apoptotic protein, which inhibits the mitochondrial apoptotic pathway.
CC May regulate TNF-alpha signaling through its interactions with
CC TNFRSF1A; however these effects may be indirect.
CC {ECO:0000250|UniProtKB:Q9NXR7}.
CC -!- SUBUNIT: Component of the ARISC complex, at least composed of
CC UIMC1/RAP80, ABRAXAS1, BRCC3/BRCC36, BABAM2 and BABAM1/NBA1. Component
CC of the BRCA1-A complex, at least composed of BRCA1, BARD1, UIMC1/RAP80,
CC ABRAXAS1, BRCC3/BRCC36, BABAM2 and BABAM1/NBA1. In the BRCA1-A complex,
CC interacts directly with ABRAXAS1, BRCC3/BRCC36 and BABAM1/NBA1. Binds
CC polyubiquitin. Component of the BRISC complex, at least composed of
CC ABRAXAS2, BRCC3/BRCC36, BABAM2 and BABAM1/NBA1. Identified in a complex
CC with SHMT2 and the other subunits of the BRISC complex. Component of
CC the BRCA1/BRCA2 containing complex (BRCC), which also contains BRCA1,
CC BRCA2, BARD1, BRCC3/BRCC36 and RAD51. BRCC is a ubiquitin E3 ligase
CC complex that enhances cellular survival following DNA damage. May
CC interact with FAS and TNFRSF1A. {ECO:0000250|UniProtKB:Q9NXR7}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9NXR7}. Nucleus
CC {ECO:0000250|UniProtKB:Q9NXR7}. Note=Localizes at sites of DNA damage
CC at double-strand breaks (DSBs). {ECO:0000250|UniProtKB:Q9NXR7}.
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:0000250|UniProtKB:Q9NXR7}.
CC -!- SIMILARITY: Belongs to the BABAM2 family. {ECO:0000255}.
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DR EMBL; AY454160; AAR21235.1; -; mRNA.
DR RefSeq; NP_001268506.1; NM_001281577.1.
DR AlphaFoldDB; Q6SP92; -.
DR SMR; Q6SP92; -.
DR STRING; 10036.XP_005073622.1; -.
DR GeneID; 101827674; -.
DR CTD; 9577; -.
DR eggNOG; ENOG502QUU0; Eukaryota.
DR OrthoDB; 831092at2759; -.
DR Proteomes; UP000189706; Unplaced.
DR GO; GO:0070531; C:BRCA1-A complex; ISS:UniProtKB.
DR GO; GO:0070552; C:BRISC complex; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0031593; F:polyubiquitin modification-dependent protein binding; ISS:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
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; ISS:UniProtKB.
DR GO; GO:0007095; P:mitotic G2 DNA damage checkpoint signaling; ISS:UniProtKB.
DR GO; GO:0045739; P:positive regulation of DNA repair; ISS:UniProtKB.
DR GO; GO:0010212; P:response to ionizing radiation; ISS:UniProtKB.
DR InterPro; IPR010358; BRE.
DR PANTHER; PTHR15189; PTHR15189; 1.
DR Pfam; PF06113; BRE; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Apoptosis; Cell cycle; Cell division; Chromatin regulator;
KW Cytoplasm; DNA damage; DNA repair; Mitosis; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Ubl conjugation pathway.
FT CHAIN 1..383
FT /note="BRISC and BRCA1-A complex member 2"
FT /id="PRO_0000373932"
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:0000250|UniProtKB:Q9NXR7"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NXR7"
SQ SEQUENCE 383 AA; 43562 MW; C054A6CF2A82D0F0 CRC64;
MSPEIALNRI SPMLSPFISS VVRNGKVGLD ATNCLRITDL KSGCTSLTPG PNCDRFKLHI
PYAGESLKWD IIFNAQYPEL PPDFIFGEDA EFLPDPSALH NLASWNPSDP 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
