ABRX1_XENTR
ID ABRX1_XENTR Reviewed; 408 AA.
AC Q28HX0; B1H0Y5; Q28II5;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 76.
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=TEgg007h13.1, TNeu015k14.1;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Egg, and Neurula;
RG Sanger Xenopus tropicalis EST/cDNA project;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (MAR-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. Interacts directly (when phosphorylated at Ser-405) with
CC brca1. Homodimer. The phosphorylated homodimer can interact directly
CC with two 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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q28HX0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q28HX0-2; Sequence=VSP_037269;
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; CR760374; CAJ82841.1; -; mRNA.
DR EMBL; CR760699; CAJ83656.1; -; mRNA.
DR EMBL; BC160397; AAI60397.1; -; mRNA.
DR RefSeq; NP_001037959.1; NM_001044494.1. [Q28HX0-1]
DR RefSeq; XP_012819559.1; XM_012964105.2. [Q28HX0-1]
DR RefSeq; XP_012819566.1; XM_012964112.2. [Q28HX0-1]
DR RefSeq; XP_012819571.1; XM_012964117.2. [Q28HX0-1]
DR RefSeq; XP_012819575.1; XM_012964121.2. [Q28HX0-2]
DR RefSeq; XP_017949436.1; XM_018093947.1.
DR RefSeq; XP_017949439.1; XM_018093950.1.
DR AlphaFoldDB; Q28HX0; -.
DR SMR; Q28HX0; -.
DR STRING; 8364.ENSXETP00000032477; -.
DR PaxDb; Q28HX0; -.
DR PRIDE; Q28HX0; -.
DR Ensembl; ENSXETT00000032477; ENSXETP00000032477; ENSXETG00000014838.
DR GeneID; 733722; -.
DR KEGG; xtr:733722; -.
DR CTD; 84142; -.
DR Xenbase; XB-GENE-5730310; abraxas1.
DR eggNOG; ENOG502QVCD; Eukaryota.
DR HOGENOM; CLU_056671_0_1_1; -.
DR InParanoid; Q28HX0; -.
DR OrthoDB; 954711at2759; -.
DR Reactome; R-XTR-5689901; Metalloprotease DUBs.
DR Proteomes; UP000008143; Chromosome 1.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000014838; Expressed in testis and 12 other tissues.
DR ExpressionAtlas; Q28HX0; baseline.
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 Alternative splicing; Chromatin regulator; Coiled coil; DNA damage;
KW DNA repair; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..408
FT /note="BRCA1-A complex subunit Abraxas 1"
FT /id="PRO_0000278580"
FT DOMAIN 7..155
FT /note="MPN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT REGION 360..408
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 210..273
FT /evidence="ECO:0000255"
FT MOTIF 405..408
FT /note="pSXXF motif"
FT /evidence="ECO:0000305"
FT COMPBIAS 360..390
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 405
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6UWZ7"
FT VAR_SEQ 1..49
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_037269"
SQ SEQUENCE 408 AA; 45828 MW; 1A13A9F081BC4F7D CRC64;
MEGESTTAVM SGFVFGALTF HHLNSGSDTE GFLLGDVVGE AKNSITDSQM DDVEVLYTID
IQKHVPCYKL SRFYNVLGDL NIPELKKLLA DQKKSQNVIG WYKFRHNTEQ IMTFRERLLH
KNLQEHLSNS GLVFLLLTSN PATETKSTHR LEYALHKPQD GFFHKVPLVI SNLGMSDQQG
YKTLCGSCVS VGLNTTIKKH RLEFFNEDGA LAEVNRISNM YTTLQDELKK TCSQLVESEH
SVEQLLEAIN ELKKQIAEKK KLNEETGNKV SEAPEENVLL CEALRKFFPQ STLLQSCRLS
LGGRQIPHSC TASHNISDVN ELTLMVKQYD IPEAHTRQAG KRKACSKQLG RTLTKKSRLL
QLQKQHSQNG DSEGSDSERP LCNSGTETDG DILESLHMDV SRSKSPIF
