BABA2_BRAFL
ID BABA2_BRAFL Reviewed; 383 AA.
AC B6NXD5;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 1.
DT 25-MAY-2022, entry version 46.
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; ORFNames=BRAFLDRAFT_269508;
OS Branchiostoma floridae (Florida lancelet) (Amphioxus).
OC Eukaryota; Metazoa; Chordata; Cephalochordata; Leptocardii; Amphioxiformes;
OC Branchiostomidae; Branchiostoma.
OX NCBI_TaxID=7739;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S238N-H82; TISSUE=Testis;
RX PubMed=18563158; DOI=10.1038/nature06967;
RA Putnam N.H., Butts T., Ferrier D.E.K., Furlong R.F., Hellsten U.,
RA Kawashima T., Robinson-Rechavi M., Shoguchi E., Terry A., Yu J.-K.,
RA Benito-Gutierrez E.L., Dubchak I., Garcia-Fernandez J., Gibson-Brown J.J.,
RA Grigoriev I.V., Horton A.C., de Jong P.J., Jurka J., Kapitonov V.V.,
RA Kohara Y., Kuroki Y., Lindquist E., Lucas S., Osoegawa K., Pennacchio L.A.,
RA Salamov A.A., Satou Y., Sauka-Spengler T., Schmutz J., Shin-I T.,
RA Toyoda A., Bronner-Fraser M., Fujiyama A., Holland L.Z., Holland P.W.H.,
RA Satoh N., Rokhsar D.S.;
RT "The amphioxus genome and the evolution of the chordate karyotype.";
RL Nature 453:1064-1071(2008).
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.
CC {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; ABEP02001063; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; B6NXD5; -.
DR SMR; B6NXD5; -.
DR InParanoid; B6NXD5; -.
DR OMA; KPTEARF; -.
DR Proteomes; UP000001554; Partially assembled WGS sequence.
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 3: Inferred from homology;
KW Apoptosis; Cell cycle; Cell division; Chromatin regulator; Cytoplasm;
KW DNA damage; DNA repair; Mitosis; Nucleus; Reference proteome; Repeat;
KW Ubl conjugation pathway.
FT CHAIN 1..383
FT /note="BRISC and BRCA1-A complex member 2"
FT /id="PRO_0000373939"
FT REGION 31..150
FT /note="UEV-like 1"
FT REGION 274..364
FT /note="UEV-like 2"
SQ SEQUENCE 383 AA; 43818 MW; F68D4E2CE363ED7F CRC64;
MSSGQSVLKQ LHPLIRPYAE TVLRKGNVGV CMGNLRISDV KSGRPTLTQT KEPCGDRFKI
YIPFAGDSLK WEVIFDSCQP SNPPDFIFLG ENGNFDPDIE KLENLTHWDP KNPESLVLAI
EDLMREYRCY QKQLIEGYSR LQFEYSSLQG MEACDDVEVH MGNRLPGTLD SPVNFLIRLP
IDLSPIPQYL VKDDPGEDLA VLLAKFHNSE GSRVTPQLFL SPKVEHALGD NTALRIPRFP
TGGCLMDYVP QVQDFLQKQI DHIVEGYQRR REYVAAFISR FGGSVLEYDA ESFTKLSLVL
EWNEFFFVLH IELPSRFPQD MPVFTFQSCY HLSKTNGEPY VSVQKSYPYS PRWTGEEMAH
RAKLFILDFI PQFKKVSVSS NKL
