XRCC1_CRIGR
ID XRCC1_CRIGR Reviewed; 633 AA.
AC O54935;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 25-MAY-2022, entry version 95.
DE RecName: Full=DNA repair protein XRCC1;
DE AltName: Full=X-ray repair cross-complementing protein 1;
GN Name=XRCC1;
OS Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Cricetulus.
OX NCBI_TaxID=10029;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS LYS-102 AND TYR-390.
RC TISSUE=Ovary;
RX PubMed=9461464; DOI=10.1093/nar/26.4.1032;
RA Shen M.R., Zdzienicka M.Z., Mohrenweiser H., Thompson L.H., Thelen M.P.;
RT "Mutations in hamster single-strand break repair gene XRCC1 causing
RT defective DNA repair.";
RL Nucleic Acids Res. 26:1032-1037(1998).
CC -!- FUNCTION: Involved in DNA single-strand break repair by mediating the
CC assembly of DNA break repair protein complexes. Probably during DNA
CC repair, negatively regulates ADP-ribose levels by modulating ADP-
CC ribosyltransferase PARP1 activity. {ECO:0000250|UniProtKB:P18887}.
CC -!- SUBUNIT: Homodimer. Interacts with polynucleotide kinase (PNK), DNA
CC polymerase-beta (POLB) and DNA ligase III (LIG3). Interacts with APTX
CC and APLF. Interacts with APEX1; the interaction is induced by SIRT1 and
CC increases with the acetylated form of APEX1 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P18887}. Nucleus,
CC nucleolus {ECO:0000250|UniProtKB:P18887}. Note=Moves from the nucleoli
CC to the global nuclear chromatin upon DNA damage.
CC {ECO:0000250|UniProtKB:P18887}.
CC -!- PTM: Phosphorylation of Ser-372 causes dimer dissociation.
CC Phosphorylation by CK2 promotes interaction with APTX and APLF (By
CC similarity). {ECO:0000250}.
CC -!- PTM: Sumoylated. {ECO:0000250}.
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DR EMBL; AF034203; AAC40038.1; -; mRNA.
DR RefSeq; NP_001233608.1; NM_001246679.1.
DR AlphaFoldDB; O54935; -.
DR SMR; O54935; -.
DR STRING; 10029.NP_001233608.1; -.
DR GeneID; 100689414; -.
DR KEGG; cge:100689414; -.
DR CTD; 7515; -.
DR eggNOG; KOG3226; Eukaryota.
DR OrthoDB; 539462at2759; -.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
DR GO; GO:0003684; F:damaged DNA binding; IEA:InterPro.
DR GO; GO:0006284; P:base-excision repair; IEA:InterPro.
DR GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IEA:InterPro.
DR GO; GO:0000012; P:single strand break repair; IEA:InterPro.
DR CDD; cd17725; BRCT_XRCC1_rpt1; 1.
DR Gene3D; 3.40.50.10190; -; 2.
DR InterPro; IPR001357; BRCT_dom.
DR InterPro; IPR036420; BRCT_dom_sf.
DR InterPro; IPR045080; BRCT_XRCC1_rpt1.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR002706; Xrcc1_N.
DR Pfam; PF00533; BRCT; 1.
DR Pfam; PF16589; BRCT_2; 1.
DR Pfam; PF01834; XRCC1_N; 1.
DR SMART; SM00292; BRCT; 2.
DR SUPFAM; SSF49785; SSF49785; 1.
DR SUPFAM; SSF52113; SSF52113; 2.
DR PROSITE; PS50172; BRCT; 2.
PE 2: Evidence at transcript level;
KW DNA damage; DNA repair; Isopeptide bond; Nucleus; Phosphoprotein; Repeat;
KW Ubl conjugation.
FT CHAIN 1..633
FT /note="DNA repair protein XRCC1"
FT /id="PRO_0000066043"
FT DOMAIN 316..404
FT /note="BRCT 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT DOMAIN 538..629
FT /note="BRCT 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT REGION 151..172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 234..316
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 407..538
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 244..260
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 470..487
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 144
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P18887"
FT MOD_RES 202
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P18887"
FT MOD_RES 203
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P18887"
FT MOD_RES 230
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P18887"
FT MOD_RES 245
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P18887"
FT MOD_RES 263
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P18887"
FT MOD_RES 372
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P18887"
FT MOD_RES 409
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P18887"
FT MOD_RES 410
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P18887"
FT MOD_RES 411
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P18887"
FT MOD_RES 447
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P18887"
FT MOD_RES 448
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P18887"
FT MOD_RES 454
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P18887"
FT MOD_RES 458
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P18887"
FT MOD_RES 462
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P18887"
FT MOD_RES 486
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P18887"
FT MOD_RES 489
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P18887"
FT MOD_RES 519
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P18887"
FT MOD_RES 520
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P18887"
FT MOD_RES 524
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P18887"
FT CROSSLNK 180
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:P18887"
FT CROSSLNK 180
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P18887"
FT VARIANT 102
FT /note="E -> K (in a mutant cell line defective in DNA
FT repair)"
FT /evidence="ECO:0000269|PubMed:9461464"
FT VARIANT 390
FT /note="C -> Y (in a mutant cell line defective in DNA
FT repair)"
FT /evidence="ECO:0000269|PubMed:9461464"
SQ SEQUENCE 633 AA; 69147 MW; 1C0A1427D9059FC6 CRC64;
MPEISLRHVV SGSSQDSTHC AENLLKADTY RKWRAATAGE KTISVVLQLE KEEQIHSIDI
GNDGSAFVEV LVTRSAGGGG ATAIEQDYEV LLVTSSFMSP SESRSGSNPN RVRMFGPDKL
VRAAAEKRWD RVKIVCSQPY SKDSPYGLSF VRFHSPPDKD EAETPSQKGT VTKLGQFRVK
EEDDGASSLK PGALFFSRIN KTSSASARGP AGPSYAAATL QASNATSSAS SVSKALGSSC
KPQESPKGKR KLDLNLEDRR PASKPSAGPP TLKRPKLTVP SRSPAAAAAS TPAQKAAPGK
PREGTEPRGA RAGPQELGKI LQGVVVVLSG FQNPFRSELR DKALELGAKY RPDWTPDSTH
LICAFANTPK YSQVLGLGGR IVRKEWVLDC YRLRRRLPSR RYLMAGLGSS SEDEEDDSPG
ESGEDEAPKL SRKRPQAKAK TQAAGPSSPQ RPPTPKETKS PSPEPQDNSD TEGEQSEGQD
NGAEDSGDTE DELRRVAEQR EQRQPPAPGE NGEDPYAGST DENTDNEAST EADLPIPELP
DFFQGKHFFL YGEFPGDERR KLIRYVTAFN GELEDYMSER VQFVITAQEW DPIFEEALME
NPSLAFVRPR WIYSCNEKQK LLPHQLYGVV PQA
