BABA1_CALJA
ID BABA1_CALJA Reviewed; 329 AA.
AC B0KWQ2;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 2.
DT 25-MAY-2022, entry version 50.
DE RecName: Full=BRISC and BRCA1-A complex member 1;
DE AltName: Full=Mediator of RAP80 interactions and targeting subunit of 40 kDa;
DE AltName: Full=New component of the BRCA1-A complex;
GN Name=BABAM1; Synonyms=MERIT40, NBA1;
OS Callithrix jacchus (White-tufted-ear marmoset).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Callitrichinae; Callithrix; Callithrix.
OX NCBI_TaxID=9483;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Antonellis A., Ayele K., Benjamin B., Blakesley R.W., Boakye A.,
RA Bouffard G.G., Brinkley C., Brooks S., Chu G., Coleman H., Engle J.,
RA Gestole M., Greene A., Guan X., Gupta J., Haghighi P., Han J., Hansen N.,
RA Ho S.-L., Hu P., Hunter G., Hurle B., Idol J.R., Kwong P., Laric P.,
RA Larson S., Lee-Lin S.-Q., Legaspi R., Madden M., Maduro Q.L., Maduro V.B.,
RA Margulies E.H., Masiello C., Maskeri B., McDowell J., Mojidi H.A.,
RA Mullikin J.C., Oestreicher J.S., Park M., Portnoy M.E., Prasad A., Puri O.,
RA Reddix-Dugue N., Schandler K., Schueler M.G., Sison C., Stantripop S.,
RA Stephen E., Taye A., Thomas J.W., Thomas P.J., Tsipouri V., Ung L.,
RA Vogt J.L., Wetherby K.D., Young A., Green E.D.;
RT "NISC comparative sequencing initiative.";
RL Submitted (FEB-2008) 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 is required for the complex integrity and its localization at DSBs.
CC Component of the BRISC complex, a multiprotein complex that
CC specifically cleaves 'Lys-63'-linked ubiquitin in various substrates.
CC In these 2 complexes, it is probably required to maintain the stability
CC of BABAM2 and help the 'Lys-63'-linked deubiquitinase activity mediated
CC by BRCC3/BRCC36 component. The BRISC complex is required for normal
CC mitotic spindle assembly and microtubule attachment to kinetochores via
CC its role in deubiquitinating NUMA1. Plays a role in interferon
CC signaling via its role in the deubiquitination of the interferon
CC receptor IFNAR1; deubiquitination increases IFNAR1 activity by
CC enhancing its stability and cell surface expression. Down-regulates the
CC response to bacterial lipopolysaccharide (LPS) via its role in IFNAR1
CC deubiquitination. {ECO:0000250|UniProtKB:Q9NWV8}.
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 and BABAM2. Component of the BRISC
CC complex, at least composed of ABRAXAS2, BRCC3/BRCC36, BABAM2 and
CC BABAM1/NBA1. Identified in a complex with SHMT2 and the other subunits
CC of the BRISC complex. {ECO:0000250|UniProtKB:Q9NWV8}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9NWV8}. Nucleus
CC {ECO:0000250|UniProtKB:Q9NWV8}. Note=Localizes at sites of DNA damage
CC at double-strand breaks (DSBs). {ECO:0000250|UniProtKB:Q9NWV8}.
CC -!- DOMAIN: The VWFA-like region is similar to the VWFA domain. Its
CC presence reveals similarities between the structure of the 19S
CC proteasome and the BRCA1-A complexes. {ECO:0000250|UniProtKB:Q9NWV8}.
CC -!- SIMILARITY: Belongs to the BABAM1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABZ10512.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; DP000584; ABZ10512.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_008989697.1; XM_008991449.2.
DR AlphaFoldDB; B0KWQ2; -.
DR SMR; B0KWQ2; -.
DR STRING; 9483.ENSCJAP00000017682; -.
DR GeneID; 100410892; -.
DR KEGG; cjc:100410892; -.
DR eggNOG; ENOG502QPZP; Eukaryota.
DR InParanoid; B0KWQ2; -.
DR OrthoDB; 1583424at2759; -.
DR Proteomes; UP000008225; 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: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:0070536; P:protein K63-linked deubiquitination; ISS:UniProtKB.
DR GO; GO:0010212; P:response to ionizing radiation; ISS:UniProtKB.
DR InterPro; IPR026126; BABAM1.
DR InterPro; IPR036465; vWFA_dom_sf.
DR PANTHER; PTHR15660; PTHR15660; 1.
DR SUPFAM; SSF53300; SSF53300; 1.
PE 3: Inferred from homology;
KW Acetylation; Cell cycle; Cell division; Chromatin regulator; Cytoplasm;
KW DNA damage; DNA repair; Mitosis; Nucleus; Phosphoprotein;
KW Reference proteome; Ubl conjugation pathway.
FT CHAIN 1..329
FT /note="BRISC and BRCA1-A complex member 1"
FT /id="PRO_0000373928"
FT REGION 1..86
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 95..298
FT /note="VWFA-like"
FT COMPBIAS 1..18
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..33
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q9NWV8"
FT MOD_RES 8
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5XIJ6"
FT MOD_RES 29
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NWV8"
FT MOD_RES 49
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NWV8"
FT MOD_RES 57
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NWV8"
FT MOD_RES 62
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NWV8"
FT MOD_RES 65
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9NWV8"
FT MOD_RES 66
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NWV8"
SQ SEQUENCE 329 AA; 36541 MW; 68D293EF77E0C243 CRC64;
MEVAEPSSPT EEEEEEEEHS AEPRPHTRSN PEGAEDRAVA AQASVGSHSE GEGEAASADD
GSPSTSGAGP KSWQVPPPAP EVQIRTPRVN CPEKVIICLD LSEEMSLPKL ESFNGSKTNA
LNISQKMIEM FVRTKHKIDK SHEFALVVVN DDTAWLSGLT SDPRELCSCL YDLETASCST
FNLEGLFSLI QQKTEFPVTE NVQTIPPPYV VRTILVYSRP PCQPQFSLTE PMKKMFQCPY
FFFDLVYIHN GAEEKEEEMS WKDMFAFMGS LDTKGTSYKY EVALAGPALE LHNCMVKLLA
HPLQRPCQSH ASYSLLEEED EATEVEATV
