ID   ABRX1_SALSA             Reviewed;         404 AA.
AC   B5X1P9;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 1.
DT   03-AUG-2022, entry version 49.
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   Salmo salar (Atlantic salmon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC   Salmonidae; Salmoninae; Salmo.
OX   NCBI_TaxID=8030;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RA   Leong J., von Schalburg K., Cooper G.A., Moore R., Holt R., Davidson W.S.,
RA   Koop B.F.;
RT   "Salmo salar full-length cDNAs.";
RL   Submitted (OCT-2008) 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-401)
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-401 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; BT044968; ACI33230.1; -; mRNA.
DR   RefSeq; NP_001133437.1; NM_001139965.1.
DR   AlphaFoldDB; B5X1P9; -.
DR   SMR; B5X1P9; -.
DR   STRING; 8030.ENSSSAP00000094760; -.
DR   PRIDE; B5X1P9; -.
DR   GeneID; 100194936; -.
DR   KEGG; sasa:100194936; -.
DR   OMA; QESVIGW; -.
DR   OrthoDB; 954711at2759; -.
DR   Proteomes; UP000087266; Chromosome ssa13.
DR   Bgee; ENSSSAG00000072520; Expressed in semen and 15 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..404
FT                   /note="BRCA1-A complex subunit Abraxas 1"
FT                   /id="PRO_0000373941"
FT   DOMAIN          7..161
FT                   /note="MPN"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT   REGION          339..404
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          219..268
FT                   /evidence="ECO:0000255"
FT   MOTIF           401..404
FT                   /note="pSXXF motif"
FT                   /evidence="ECO:0000305"
FT   COMPBIAS        355..371
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        380..404
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         401
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6UWZ7"
SQ   SEQUENCE   404 AA;  45769 MW;  31045322245FC5BB CRC64;
     MEDSNSYIRV SGFVLGSLMF QHLNSDSDVE GLILGETKAE ERSNITDSQI DNIQFEHTIN
     IQKHISCRKL NSFYNRIGEV NRDEIRHILS NYKEENVIGW YKQRRNTDQQ ITFREQVVHE
     NLKRALSNHE LIFLLLTPSE ITTSGSTHKL EYAVYRSHGS QYCSVPVLVS NLGLLEEQDY
     WRLSASCSSV NYNHAVRKHR SKFFSSDGSL HEVDEINDMN NSLQGELKMA CKKVEESERL
     VEKLLADVSD LRRMVNERKQ ELREISADGA STPAQPRENV LLCEVIKTLF PGASLLQTQA
     LNFQGFPLPE FCCSTDHGID IATTLPLILS HTLPKARKGR LGRGGGTSWR KCPLRESSEV
     PKRRKGMLEE TDETLSVSGS ETEEDLIPAN RNGNNLDVSN SPVF