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P18887 (XRCC1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 157. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
DNA repair protein XRCC1
Alternative name(s):
X-ray repair cross-complementing protein 1
Gene names
Name:XRCC1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length633 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Corrects defective DNA strand-break repair and sister chromatid exchange following treatment with ionizing radiation and alkylating agents.

Subunit structure

Homodimer. Interacts with polynucleotide kinase (PNK), DNA polymerase-beta (POLB) and DNA ligase III (LIG3). Interacts with APTX and APLF. Interacts with APEX1; the interaction is induced by SIRT1 and increases with the acetylated form of APEX1. Ref.6 Ref.7 Ref.9 Ref.10 Ref.13 Ref.14 Ref.15 Ref.19

Subcellular location

Nucleus. Note: Accumulates at sites of DNA damage. Ref.15

Post-translational modification

Phosphorylation of Ser-371 causes dimer dissociation. Phosphorylation by CK2 promotes interaction with APTX and APLF.

Sumoylated. Ref.11

Polymorphism

Carriers of the polymorphic Gln-399 allele may be at greater risk for tobacco- and age-related DNA damage.

Sequence similarities

Contains 2 BRCT domains.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 633633DNA repair protein XRCC1
PRO_0000066044

Regions

Domain315 – 40389BRCT 1
Domain538 – 62992BRCT 2

Amino acid modifications

Modified residue1401Phosphoserine Ref.20
Modified residue1981Phosphothreonine Ref.18
Modified residue1991Phosphoserine Ref.18
Modified residue2021Phosphothreonine Ref.20
Modified residue2041Phosphoserine Ref.20
Modified residue2111Phosphotyrosine
Modified residue2261Phosphoserine Ref.16 Ref.18
Modified residue2411Phosphoserine Ref.16 Ref.18 Ref.20 Ref.21
Modified residue2571Phosphothreonine Ref.16 Ref.20
Modified residue2591Phosphoserine Ref.16
Modified residue2661Phosphoserine
Modified residue3711Phosphoserine; by PRKDC Ref.13
Modified residue4081Phosphoserine Ref.16
Modified residue4091Phosphoserine Ref.16
Modified residue4101Phosphoserine Ref.16
Modified residue4161Phosphoserine
Modified residue4181Phosphoserine
Modified residue4211Phosphoserine Ref.12
Modified residue4461Phosphoserine
Modified residue4471Phosphoserine
Modified residue4531Phosphothreonine Ref.16 Ref.18 Ref.21
Modified residue4571Phosphothreonine Ref.21
Modified residue4611Phosphoserine Ref.18
Modified residue4851Phosphoserine Ref.8 Ref.18
Modified residue4881Phosphothreonine Ref.8 Ref.18
Modified residue5181Phosphoserine Ref.23
Modified residue5191Phosphothreonine Ref.23
Modified residue5231Phosphothreonine Ref.23

Natural variations

Natural variant71R → L.
Corresponds to variant rs2307186 [ dbSNP | Ensembl ].
VAR_014773
Natural variant101V → M.
Corresponds to variant rs2307171 [ dbSNP | Ensembl ].
VAR_014774
Natural variant721V → A. Ref.2
Corresponds to variant rs25496 [ dbSNP | Ensembl ].
VAR_016168
Natural variant1071R → H.
Corresponds to variant rs2228487 [ dbSNP | Ensembl ].
VAR_029228
Natural variant1571E → K.
Corresponds to variant rs2307180 [ dbSNP | Ensembl ].
VAR_014775
Natural variant1611P → L. Ref.2
Corresponds to variant rs2307191 [ dbSNP | Ensembl ].
VAR_014776
Natural variant1941R → W. Ref.2 Ref.24
Corresponds to variant rs1799782 [ dbSNP | Ensembl ].
VAR_013400
Natural variant2801R → H. Ref.2 Ref.24
Corresponds to variant rs25489 [ dbSNP | Ensembl ].
VAR_013401
Natural variant2981K → N.
Corresponds to variant rs2307188 [ dbSNP | Ensembl ].
VAR_014777
Natural variant3041T → A. Ref.2
Corresponds to variant rs25490 [ dbSNP | Ensembl ].
VAR_018775
Natural variant3091P → S. Ref.2
Corresponds to variant rs25491 [ dbSNP | Ensembl ].
VAR_014778
Natural variant3501R → W in a colorectal cancer sample; somatic mutation. Ref.27
VAR_036277
Natural variant3991R → Q. Ref.2 Ref.3 Ref.4 Ref.5 Ref.24 Ref.25 Ref.26
Corresponds to variant rs25487 [ dbSNP | Ensembl ].
VAR_011487
Natural variant4851S → Y.
Corresponds to variant rs2307184 [ dbSNP | Ensembl ].
VAR_014779
Natural variant5141P → L.
Corresponds to variant rs25474 [ dbSNP | Ensembl ].
VAR_016169
Natural variant5591R → Q.
Corresponds to variant rs2307167 [ dbSNP | Ensembl ].
VAR_014780
Natural variant5601R → W.
Corresponds to variant rs2307166 [ dbSNP | Ensembl ].
VAR_014781
Natural variant5761N → S. Ref.2
Corresponds to variant rs2307177 [ dbSNP | Ensembl ].
VAR_014782
Natural variant5761N → Y. Ref.1 Ref.3 Ref.5 Ref.28
Corresponds to variant rs2682557 [ dbSNP | Ensembl ].
VAR_061727

Secondary structure

......................................................................... 633
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P18887 [UniParc].

Last modified January 11, 2011. Version 2.
Checksum: 30DB3321234DBFC2

FASTA63369,477
        10         20         30         40         50         60 
MPEIRLRHVV SCSSQDSTHC AENLLKADTY RKWRAAKAGE KTISVVLQLE KEEQIHSVDI 

        70         80         90        100        110        120 
GNDGSAFVEV LVGSSAGGAG EQDYEVLLVT SSFMSPSESR SGSNPNRVRM FGPDKLVRAA 

       130        140        150        160        170        180 
AEKRWDRVKI VCSQPYSKDS PFGLSFVRFH SPPDKDEAEA PSQKVTVTKL GQFRVKEEDE 

       190        200        210        220        230        240 
SANSLRPGAL FFSRINKTSP VTASDPAGPS YAAATLQASS AASSASPVSR AIGSTSKPQE 

       250        260        270        280        290        300 
SPKGKRKLDL NQEEKKTPSK PPAQLSPSVP KRPKLPAPTR TPATAPVPAR AQGAVTGKPR 

       310        320        330        340        350        360 
GEGTEPRRPR AGPEELGKIL QGVVVVLSGF QNPFRSELRD KALELGAKYR PDWTRDSTHL 

       370        380        390        400        410        420 
ICAFANTPKY SQVLGLGGRI VRKEWVLDCH RMRRRLPSRR YLMAGPGSSS EEDEASHSGG 

       430        440        450        460        470        480 
SGDEAPKLPQ KQPQTKTKPT QAAGPSSPQK PPTPEETKAA SPVLQEDIDI EGVQSEGQDN 

       490        500        510        520        530        540 
GAEDSGDTED ELRRVAEQKE HRLPPGQEEN GEDPYAGSTD ENTDSEEHQE PPDLPVPELP 

       550        560        570        580        590        600 
DFFQGKHFFL YGEFPGDERR KLIRYVTAFN GELEDNMSDR VQFVITAQEW DPSFEEALMD 

       610        620        630 
NPSLAFVRPR WIYSCNEKQK LLPHQLYGVV PQA 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning of the human XRCC1 gene, which corrects defective DNA strand break repair and sister chromatid exchange."
Thompson L.H., Brookman K.W., Jones N.J., Allen S.A., Carrano A.V.
Mol. Cell. Biol. 10:6160-6171(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT TYR-576.
[2]NIEHS SNPs program
Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ALA-72; LEU-161; TRP-194; HIS-280; ALA-304; SER-309; GLN-399 AND SER-576.
[3]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANTS GLN-399 AND TYR-576.
[4]"The DNA sequence and biology of human chromosome 19."
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V. expand/collapse author list , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT GLN-399.
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANTS GLN-399 AND TYR-576.
Tissue: Eye.
[6]"XRCC1 stimulates human polynucleotide kinase activity at damaged DNA termini and accelerates DNA single-strand break repair."
Whitehouse C.J., Taylor R.M., Thistlethwaite A., Zhang H., Karimi-Busheri F., Lasko D.D., Weinfeld M., Caldecott K.W.
Cell 104:107-117(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION.
[7]"Aprataxin, the causative protein for EAOH is a nuclear protein with a potential role as a DNA repair protein."
Sano Y., Date H., Igarashi S., Onodera O., Oyake M., Takahashi T., Hayashi S., Morimatsu M., Takahashi H., Makifuchi T., Fukuhara N., Tsuji S.
Ann. Neurol. 55:241-249(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH APTX.
[8]"The protein kinase CK2 facilitates repair of chromosomal DNA single-strand breaks."
Loizou J.I., El-Khamisy S.F., Zlatanou A., Moore D.J., Chan D.W., Qin J., Sarno S., Meggio F., Pinna L.A., Caldecott K.W.
Cell 117:17-28(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-485 AND THR-488, IDENTIFICATION BY MASS SPECTROMETRY.
[9]"The ataxia-oculomotor apraxia 1 gene product has a role distinct from ATM and interacts with the DNA strand break repair proteins XRCC1 and XRCC4."
Clements P.M., Breslin C., Deeks E.D., Byrd P.J., Ju L., Bieganowski P., Brenner C., Moreira M.-C., Taylor A.M.R., Caldecott K.W.
DNA Repair 3:1493-1502(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH APTX, PHOSPHORYLATION.
[10]"Aprataxin, a novel protein that protects against genotoxic stress."
Gueven N., Becherel O.J., Kijas A.W., Chen P., Howe O., Rudolph J.H., Gatti R., Date H., Onodera O., Taucher-Scholz G., Lavin M.F.
Hum. Mol. Genet. 13:1081-1093(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH APTX.
[11]"Systematic identification and analysis of mammalian small ubiquitin-like modifier substrates."
Gocke C.B., Yu H., Kang J.
J. Biol. Chem. 280:5004-5012(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: SUMOYLATION.
[12]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-421, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"XRCC1 is phosphorylated by DNA-dependent protein kinase in response to DNA damage."
Levy N., Martz A., Bresson A., Spenlehauer C., de Murcia G., Menissier-de Murcia J.
Nucleic Acids Res. 34:32-41(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT, PHOSPHORYLATION AT SER-371.
[14]"Human Xip1 (C2orf13) is a novel regulator of cellular responses to DNA strand breaks."
Bekker-Jensen S., Fugger K., Danielsen J.R., Gromova I., Sehested M., Celis J., Bartek J., Lukas J., Mailand N.
J. Biol. Chem. 282:19638-19643(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH APLF.
[15]"APLF (C2orf13) is a novel human protein involved in the cellular response to chromosomal DNA strand breaks."
Iles N., Rulten S., El-Khamisy S.F., Caldecott K.W.
Mol. Cell. Biol. 27:3793-3803(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH APLF, PHOSPHORYLATION, SUBCELLULAR LOCATION.
[16]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226; SER-241; THR-257; SER-259; SER-408; SER-409; SER-410 AND THR-453, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[17]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-198; SER-199; SER-226; SER-241; THR-453; SER-461; SER-485 AND THR-488, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[19]"SIRT1 deacetylates APE1 and regulates cellular base excision repair."
Yamamori T., DeRicco J., Naqvi A., Hoffman T.A., Mattagajasingh I., Kasuno K., Jung S.B., Kim C.S., Irani K.
Nucleic Acids Res. 38:832-845(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH APEX1.
[20]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-140; THR-202; SER-204; SER-241 AND THR-257, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[21]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-241; THR-453 AND THR-457, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[22]"Solution structure of the first BRCT domain of DNA-repair protein XRCC1."
RIKEN structural genomics initiative (RSGI)
Submitted (JUN-2006) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 306-422.
[23]"Specific recognition of a multiply phosphorylated motif in the DNA repair scaffold XRCC1 by the FHA domain of human PNK."
Ali A.A., Jukes R.M., Pearl L.H., Oliver A.W.
Nucleic Acids Res. 37:1701-1712(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 515-522 IN COMPLEX WITH PNKP, PHOSPHORYLATION AT SER-518; THR-519 AND THR-523.
[24]"Nonconservative amino acid substitution variants exist at polymorphic frequency in DNA repair genes in healthy humans."
Shen M.R., Jones I.M., Mohrenweiser H.
Cancer Res. 58:604-608(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS TRP-194; HIS-280 AND GLN-399.
[25]"Polymorphisms in the DNA repair genes XRCC1 and ERCC2 and biomarkers of DNA damage in human blood mononuclear cells."
Duell E.J., Wiencke J.K., Cheng T.J., Varkonyi A., Zuo Z.F., Ashok T.D., Mark E.J., Wain J.C., Christiani D.C., Kelsey K.T.
Carcinogenesis 21:965-971(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT GLN-399.
[26]"The XRCC1 Arg399Gln polymorphism, sunburn, and non-melanoma skin cancer: evidence of gene-environment interaction."
Nelson H.H., Kelsey K.T., Mott L.A., Karagas M.R.
Cancer Res. 62:152-155(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT GLN-399.
[27]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] TRP-350.
[28]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] TYR-576, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M36089 mRNA. Translation: AAA63270.1.
AF512504 Genomic DNA. Translation: AAM34791.1.
CR456728 mRNA. Translation: CAG33009.1.
AC018758 Genomic DNA. Translation: AAG09061.1.
L34079 Genomic DNA. No translation available.
BC023593 mRNA. Translation: AAH23593.1.
CCDSCCDS12624.1.
PIRA36353.
RefSeqNP_006288.2. NM_006297.2.
UniGeneHs.98493.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1CDZX-ray3.20A538-633[»]
1XNANMR-A1-183[»]
1XNTNMR-A1-183[»]
2D8MNMR-A305-420[»]
2W3OX-ray1.85C/D515-522[»]
3K75X-ray2.95B/C1-183[»]
3K77X-ray2.60A/B/C/D/E/F/G/H1-155[»]
3LQCX-ray2.35A1-183[»]
ProteinModelPortalP18887.
SMRP18887. Positions 2-153, 301-415, 538-633.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113349. 39 interactions.
DIPDIP-39067N.
IntActP18887. 16 interactions.
MINTMINT-245471.
STRING9606.ENSP00000262887.

PTM databases

PhosphoSiteP18887.

Polymorphism databases

DMDM317373290.

Proteomic databases

MaxQBP18887.
PaxDbP18887.
PRIDEP18887.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000262887; ENSP00000262887; ENSG00000073050.
GeneID7515.
KEGGhsa:7515.

Organism-specific databases

CTD7515.
GeneCardsGC19M044047.
H-InvDBHIX0040090.
HGNCHGNC:12828. XRCC1.
HPACAB005427.
HPA006717.
MIM194360. gene.
neXtProtNX_P18887.
PharmGKBPA369.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG295271.
HOVERGENHBG052992.
InParanoidP18887.
KOK10803.
OrthoDBEOG77WWD8.
PhylomeDBP18887.
TreeFamTF101201.

Enzyme and pathway databases

ReactomeREACT_216. DNA Repair.
SignaLinkP18887.

Gene expression databases

ArrayExpressP18887.
BgeeP18887.
CleanExHS_XRCC1.
GenevestigatorP18887.

Family and domain databases

Gene3D2.60.120.260. 1 hit.
3.40.50.10190. 2 hits.
InterProIPR001357. BRCT_dom.
IPR008979. Galactose-bd-like.
IPR002706. Xrcc1_N.
[Graphical view]
PfamPF00533. BRCT. 2 hits.
PF01834. XRCC1_N. 1 hit.
[Graphical view]
SMARTSM00292. BRCT. 2 hits.
[Graphical view]
SUPFAMSSF49785. SSF49785. 1 hit.
SSF52113. SSF52113. 2 hits.
PROSITEPS50172. BRCT. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSXRCC1. human.
EvolutionaryTraceP18887.
GeneWikiXRCC1.
GenomeRNAi7515.
NextBio29407.
PROP18887.
SOURCESearch...

Entry information

Entry nameXRCC1_HUMAN
AccessionPrimary (citable) accession number: P18887
Secondary accession number(s): Q6IBS4, Q9HCB1
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: January 11, 2011
Last modified: July 9, 2014
This is version 157 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM