ABRX1_DANRE
ID ABRX1_DANRE Reviewed; 391 AA.
AC Q1LVP6; Q5XJ91;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 93.
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; ORFNames=si:ch211-85e10.4, zgc:103522;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (OCT-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-388)
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-388 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; BX649525; CAK05015.1; -; Genomic_DNA.
DR EMBL; BC083413; AAH83413.1; -; mRNA.
DR RefSeq; NP_001005993.1; NM_001005993.1.
DR AlphaFoldDB; Q1LVP6; -.
DR SMR; Q1LVP6; -.
DR STRING; 7955.ENSDARP00000063620; -.
DR PaxDb; Q1LVP6; -.
DR Ensembl; ENSDART00000063621; ENSDARP00000063620; ENSDARG00000043339.
DR Ensembl; ENSDART00000184956; ENSDARP00000155024; ENSDARG00000115196.
DR GeneID; 449820; -.
DR KEGG; dre:449820; -.
DR CTD; 84142; -.
DR ZFIN; ZDB-GENE-041010-70; abraxas1.
DR eggNOG; ENOG502QVCD; Eukaryota.
DR GeneTree; ENSGT00530000063424; -.
DR HOGENOM; CLU_056671_0_1_1; -.
DR InParanoid; Q1LVP6; -.
DR OMA; QESVIGW; -.
DR OrthoDB; 954711at2759; -.
DR PhylomeDB; Q1LVP6; -.
DR TreeFam; TF331751; -.
DR Reactome; R-DRE-5689901; Metalloprotease DUBs.
DR Reactome; R-DRE-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
DR Reactome; R-DRE-5693607; Processing of DNA double-strand break ends.
DR Reactome; R-DRE-69473; G2/M DNA damage checkpoint.
DR PRO; PR:Q1LVP6; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 21.
DR Bgee; ENSDARG00000043339; Expressed in mature ovarian follicle and 20 other tissues.
DR GO; GO:0070531; C:BRCA1-A complex; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0031593; F:polyubiquitin modification-dependent protein binding; ISS:UniProtKB.
DR GO; GO:0008608; P:attachment of spindle microtubules to kinetochore; IBA:GO_Central.
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:0090307; P:mitotic spindle assembly; IBA:GO_Central.
DR GO; GO:0045739; P:positive regulation of DNA repair; ISS:UniProtKB.
DR GO; GO:0070536; P:protein K63-linked deubiquitination; IBA:GO_Central.
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..391
FT /note="BRCA1-A complex subunit Abraxas 1"
FT /id="PRO_0000278578"
FT DOMAIN 8..156
FT /note="MPN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT REGION 354..391
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 223..261
FT /evidence="ECO:0000255"
FT MOTIF 388..391
FT /note="pSXXF motif"
FT /evidence="ECO:0000305"
FT COMPBIAS 371..391
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 388
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6UWZ7"
FT CONFLICT 185
FT /note="S -> G (in Ref. 2; AAH83413)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 391 AA; 44635 MW; 937EE4C4BF57F897 CRC64;
MEEFNTTVRI SGFVLSSLMF HHLNSDADVE GLILGESVGE ENCRITDSQI DHIQFEHTLN
IQKHIPCHKL HSFYSNVGDV SEQKIRQILS DYKEENVIGW YRQRRNTRQQ MTFMEQVIHR
NMRKILSNQE LVFMLLTPSQ GTASGSTHRL EFSAFIWHSS QYINIPISVS NLGNLEQQDY
WRVSSTCPSL GQSQAVNQHR AKFFCSGDDL REVRNVSDMN DALLAEMQKV CVEVEKSERT
VEKLQEDIAQ LKEAIGKQKT HPEEHETPIS ACPEEPKENT LLCSALRTLF PSVPSLRTQT
LTVHGFPVLQ LCCNTDHNID ISTKLPQILE NQHSRRKVTA PRLRKKCLVA SFPQRLKRKR
KTREVSESAS ESGSDTEIEM NGQSGSNSPV F
