ID   ABRX1_XENLA             Reviewed;         408 AA.
AC   Q6GR31;
DT   20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 61.
DE   RecName: Full=BRCA1-A complex subunit Abraxas 1 {ECO:0000250|UniProtKB:Q6UWZ7};
DE   AltName: Full=Coiled-coil domain-containing protein 98;
DE   AltName: Full=Protein FAM175A;
GN   Name=abraxas1 {ECO:0000250|UniProtKB:Q6UWZ7};
GN   Synonyms=abra1, ccdc98, fam175a;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Ovary;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in DNA damage response and double-strand break (DSB)
CC       repair. Component of the BRCA1-A complex, acting as a central scaffold
CC       protein that assembles the various components of the complex and
CC       mediates the recruitment of brca1. The BRCA1-A complex specifically
CC       recognizes 'Lys-63'-linked ubiquitinated histones H2A and H2AX at DNA
CC       lesion sites, leading to target the brca1-bard1 heterodimer to sites of
CC       DNA damage at DSBs. This complex also possesses deubiquitinase activity
CC       that specifically removes 'Lys-63'-linked ubiquitin on histones H2A and
CC       H2AX (By similarity). {ECO:0000250|UniProtKB:Q6UWZ7}.
CC   -!- SUBUNIT: Component of the BRCA1-A complex. Component of the BRISC
CC       complex. Homodimer. Interacts directly (when phosphorylated at Ser-405)
CC       with brca1. The phosphorylated homodimer can interact directly with two
CC       brca1 chains, giving rise to a heterotetramer (By similarity).
CC       {ECO:0000250|UniProtKB:Q6UWZ7}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q6UWZ7}.
CC       Note=Localizes at sites of DNA damage at double-strand breaks (DSBs).
CC       {ECO:0000250|UniProtKB:Q6UWZ7}.
CC   -!- PTM: Phosphorylation of Ser-405 of the pSXXF motif by ATM or ATR
CC       constitutes a specific recognition motif for the BRCT domain of BRCA1.
CC       {ECO:0000250|UniProtKB:Q6UWZ7}.
CC   -!- SIMILARITY: Belongs to the FAM175 family. Abraxas subfamily.
CC       {ECO:0000305}.
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DR   EMBL; BC071103; AAH71103.1; -; mRNA.
DR   RefSeq; NP_001085339.1; NM_001091870.1.
DR   AlphaFoldDB; Q6GR31; -.
DR   SMR; Q6GR31; -.
DR   BioGRID; 101928; 1.
DR   IntAct; Q6GR31; 1.
DR   DNASU; 443765; -.
DR   GeneID; 443765; -.
DR   KEGG; xla:443765; -.
DR   CTD; 443765; -.
DR   Xenbase; XB-GENE-5730339; abraxas1.S.
DR   OMA; QESVIGW; -.
DR   OrthoDB; 954711at2759; -.
DR   Proteomes; UP000186698; Chromosome 1S.
DR   Bgee; 443765; Expressed in blastula and 19 other tissues.
DR   GO; GO:0070531; C:BRCA1-A complex; 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: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; IPR023238; FAM175.
DR   InterPro; IPR023239; FAM175_Abraxas1.
DR   InterPro; IPR037518; MPN.
DR   PANTHER; PTHR31728; PTHR31728; 1.
DR   PRINTS; PR02052; ABRAXAS.
DR   PRINTS; PR02051; PROTEINF175.
DR   PROSITE; PS50249; MPN; 1.
PE   2: Evidence at transcript level;
KW   Chromatin regulator; Coiled coil; DNA damage; DNA repair; Nucleus;
KW   Phosphoprotein; Reference proteome.
FT   CHAIN           1..408
FT                   /note="BRCA1-A complex subunit Abraxas 1"
FT                   /id="PRO_0000278579"
FT   DOMAIN          7..155
FT                   /note="MPN"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT   REGION          335..408
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          210..272
FT                   /evidence="ECO:0000255"
FT   MOTIF           405..408
FT                   /note="pSXXF motif"
FT                   /evidence="ECO:0000305"
FT   COMPBIAS        338..352
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        353..408
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         405
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6UWZ7"
SQ   SEQUENCE   408 AA;  45823 MW;  8D4CDA8F80EAF622 CRC64;
     MEGESTTAVI SGFVFGALTF HHLNSGSDTE GFLLGDVMGE AKNSITDSQM DDVEVLYTID
     IQKHVPCYQL SRFYNALGDL NIPELKKLLA GQKKSQNVIG WYKFRHNTEQ IMTFRERLLH
     KNLQEHFSNS GLVFLLLTSN PATETKSTHR LEYALHKPQD GFFHKVPLVI SNLGMSDQQG
     YKTLCGSCVS VGLNTAIKKH RLEFFNEDGA LAEVNRISDM HMTLQEELKK TCSQLVESEN
     SVEQLLEAVN DLKKQIAEKK LLMEEKGNKV SEDTEENVLL CEAFRRFFPQ SALLQSCRLS
     LGGRQIPHSC SVSHNSSDVN ELTLMVKQYD FPEAHRRQAG KRKAHSKQLG KTSTKKSRLP
     PFQRPQSDNS DSESSDSEKL LCTSGTETDG DIVQSLNVEV SRSKSPTF