ABRX1_RAT
ID ABRX1_RAT Reviewed; 405 AA.
AC Q5I0F1;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 25-MAY-2022, entry version 90.
DE RecName: Full=BRCA1-A complex subunit Abraxas 1 {ECO:0000312|RGD:1305287};
DE AltName: Full=Coiled-coil domain-containing protein 98;
DE AltName: Full=Protein FAM175A;
GN Name=ABRAXAS1 {ECO:0000312|RGD:1305287}; Synonyms=Abra1, Ccdc98, Fam175a;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-392, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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-402) 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-402 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; BC088408; AAH88408.1; -; mRNA.
DR RefSeq; NP_001009633.1; NM_001009633.1.
DR AlphaFoldDB; Q5I0F1; -.
DR SMR; Q5I0F1; -.
DR STRING; 10116.ENSRNOP00000002956; -.
DR iPTMnet; Q5I0F1; -.
DR PhosphoSitePlus; Q5I0F1; -.
DR PaxDb; Q5I0F1; -.
DR PRIDE; Q5I0F1; -.
DR GeneID; 289468; -.
DR KEGG; rno:289468; -.
DR CTD; 84142; -.
DR RGD; 1305287; Abraxas1.
DR eggNOG; ENOG502QVCD; Eukaryota.
DR InParanoid; Q5I0F1; -.
DR OrthoDB; 954711at2759; -.
DR PhylomeDB; Q5I0F1; -.
DR Reactome; R-RNO-5689901; Metalloprotease DUBs.
DR Reactome; R-RNO-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
DR Reactome; R-RNO-5693607; Processing of DNA double-strand break ends.
DR Reactome; R-RNO-69473; G2/M DNA damage checkpoint.
DR PRO; PR:Q5I0F1; -.
DR Proteomes; UP000002494; Unplaced.
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 1: Evidence at protein level;
KW Chromatin regulator; Coiled coil; DNA damage; DNA repair; Nucleus;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..405
FT /note="BRCA1-A complex subunit Abraxas 1"
FT /id="PRO_0000278577"
FT DOMAIN 7..154
FT /note="MPN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT REGION 333..405
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 208..262
FT /evidence="ECO:0000255"
FT MOTIF 402..405
FT /note="pSXXF motif"
FT /evidence="ECO:0000305"
FT COMPBIAS 349..363
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 48
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BPZ8"
FT MOD_RES 382
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6UWZ7"
FT MOD_RES 383
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6UWZ7"
FT MOD_RES 392
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 402
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6UWZ7"
SQ SEQUENCE 405 AA; 45690 MW; B9A0C4BF979D9473 CRC64;
MEGESTLGVL SGFVLGALTF QHLNTDSDTE GLLLGEMKGE AKNSITDSQM DSVKVVYTID
IQKYIPCYRL FSFYNSLGEV NEHALKKILS NVKKTVVGWY KFRRHSDQIM TFREQLLHRN
LQTHLSSPEL VFLLLTPSIT TESCCTHCLE HGLYKPQSGL FHKVPLVVTN LGMSDQLGYK
TESVSCTSTV FSRAVRTYSS QFFNEDGSLK EVRKINEMYA AIQEELKTIC QKVEQSEREV
EKLLMDVNRL KEVRKKQQAQ AKGAGEKSQN HPQENILLCQ ALRTFFPESR VLHSCVISLK
NRHISHSGCN TDHHLDVVDK LTLMVEYVYS PEASPAPAAP LSKRKALDTQ DQWPAKRPRL
LESESRPGPA FRGSHQDKAS SSSLDIDTEV GSPEDDTDYP RSPTF
