ABRX1_BOVIN
ID ABRX1_BOVIN Reviewed; 410 AA.
AC Q5E9P1; A4FV82;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 92.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal skin;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2006) 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. {ECO:0000250|UniProtKB:Q6UWZ7}.
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 the BRCA1, BARD1,
CC UIMC1/RAP80, ABRAXAS1, BRCC3/BRCC36, BABAM2 and BABAM1/NBA1. In the
CC complex, interacts directly with UIMC1/RAP80, BRCC3/BRCC36 and BABAM2.
CC Homodimer. Interacts directly (when phosphorylated at Ser-407) with
CC BRCA1. The phosphorylated homodimer can interact directly with two
CC BRCA1 chains, giving rise to a heterotetramer. Binds polyubiquitin.
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-407 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; BT020879; AAX08896.1; -; mRNA.
DR EMBL; BC123849; AAI23850.1; -; mRNA.
DR RefSeq; NP_001015516.1; NM_001015516.1.
DR AlphaFoldDB; Q5E9P1; -.
DR SMR; Q5E9P1; -.
DR STRING; 9913.ENSBTAP00000018700; -.
DR PaxDb; Q5E9P1; -.
DR PRIDE; Q5E9P1; -.
DR Ensembl; ENSBTAT00000018700; ENSBTAP00000018700; ENSBTAG00000014076.
DR GeneID; 504796; -.
DR KEGG; bta:504796; -.
DR CTD; 84142; -.
DR VEuPathDB; HostDB:ENSBTAG00000014076; -.
DR VGNC; VGNC:53684; ABRAXAS1.
DR eggNOG; ENOG502QVCD; Eukaryota.
DR GeneTree; ENSGT00530000063424; -.
DR HOGENOM; CLU_056671_0_1_1; -.
DR InParanoid; Q5E9P1; -.
DR OMA; QESVIGW; -.
DR OrthoDB; 954711at2759; -.
DR TreeFam; TF331751; -.
DR Proteomes; UP000009136; Chromosome 6.
DR Bgee; ENSBTAG00000014076; Expressed in oocyte and 109 other tissues.
DR ExpressionAtlas; Q5E9P1; baseline.
DR GO; GO:0070531; C:BRCA1-A complex; ISS:UniProtKB.
DR GO; GO:0016604; C:nuclear body; IEA:Ensembl.
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..410
FT /note="BRCA1-A complex subunit Abraxas 1"
FT /id="PRO_0000278574"
FT DOMAIN 7..160
FT /note="MPN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT REGION 354..410
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 208..261
FT /evidence="ECO:0000255"
FT MOTIF 407..410
FT /note="pSXXF motif"
FT /evidence="ECO:0000305"
FT COMPBIAS 364..389
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 48
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BPZ8"
FT MOD_RES 387
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6UWZ7"
FT MOD_RES 388
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6UWZ7"
FT MOD_RES 391
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q6UWZ7"
FT MOD_RES 407
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6UWZ7"
SQ SEQUENCE 410 AA; 46184 MW; 61851BA672E89B81 CRC64;
MEGESTTAVL SGFVLGALAF QHLNTDSDTE GFLLGEVKGE AKNSITDSQM DDVEVIYTID
IQKYISCYQL FSFYNSSGEV NEQALKKILS NVKKDVVGWY KLRRHSDQIM TFRERLLHRN
LQQHLSSQEL VFLLLTPSII TESCSTHRLE HALYKPQKGL FHRIPLVVAN LGMSEQLGYK
TTSGSCTSAG FSRAVKTHSS EFFKEDGSLK EVQKINEMYT SLQDELKSIC EKVEHSERAV
EKLLNDVNRL KGEIKKRKQA QMQATREKNV QKDPQENILL CQALRTFFPD CELLHSCVIS
LKNRRISGSS CTTTHPLSGV DNLTLMVEYT DFPEASPARS ALLVTKRKAS DTDDGWQFKK
SRLGGIQNRP SKTDTNSSNQ EQASTVSSPE TDEEIERMKG SGEYPQSPTF
