XRCC1

Functionⁱ

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

GO - Molecular functionⁱ

damaged DNA binding Source: InterPro
enzyme binding
Source: BHF-UCL
Inferred from physical interactionⁱ
- 8532526

GO - Biological processⁱ

base-excision repair Source: GO_Central
DNA repair Source: Reactome
hippocampus development Source: Ensembl
response to drug Source: Ensembl
response to hypoxia Source: Ensembl
response to organic substance Source: Ensembl
single strand break repair Source: InterPro

Complete GO annotation...

Keywords - Biological processⁱ

DNA damage, DNA repair

Enzyme and pathway databases

Reactomeⁱ	REACT_933. Resolution of AP sites via the single-nucleotide replacement pathway.
SignaLinkⁱ	P18887.

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: DNA repair protein XRCC1 Alternative name(s): X-ray repair cross-complementing protein 1
Gene namesⁱ	Name:XRCC1
Organismⁱ	Homo sapiens (Human)
Taxonomic identifierⁱ	9606 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo
Proteomesⁱ	UP000005640: Chromosome 19

Organism-specific databases

HGNCⁱ	HGNC:12828. XRCC1.

HGNCⁱ

HGNC:12828. XRCC1.

Subcellular locationⁱ

Nucleus 1 Publication
Note: Accumulates at sites of DNA damage.

GO - Cellular componentⁱ

nucleoplasm Source: HPA
nucleus Source: HPA

Complete GO annotation...

Keywords - Cellular componentⁱ

Nucleus

Pathology & Biotechⁱ

Organism-specific databases

PharmGKBⁱ	PA369.

PharmGKBⁱ

PA369.

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
Chainⁱ	1 – 633	633	DNA repair protein XRCC1		PRO_0000066044	Add BLAST

Amino acid modifications

Feature key	Position(s)	Length	Description
Modified residueⁱ	140 – 140	1	Phosphoserine1 Publication Manual assertion based on experiment inⁱ Ref.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].
Modified residueⁱ	198 – 198	1	Phosphothreonine1 Publication Manual assertion based on experiment inⁱ Ref.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].
Modified residueⁱ	199 – 199	1	Phosphoserine1 Publication Manual assertion based on experiment inⁱ Ref.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].
Modified residueⁱ	202 – 202	1	Phosphothreonine1 Publication Manual assertion based on experiment inⁱ Ref.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].
Modified residueⁱ	204 – 204	1	Phosphoserine1 Publication Manual assertion based on experiment inⁱ Ref.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].
Modified residueⁱ	211 – 211	1	Phosphotyrosine
Modified residueⁱ	226 – 226	1	Phosphoserine2 Publications Manual assertion based on experiment inⁱ Ref.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]. Ref.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].
Modified residueⁱ	241 – 241	1	Phosphoserine4 Publications Manual assertion based on experiment inⁱ Ref.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]. Ref.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]. Ref.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]. Ref.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].
Modified residueⁱ	257 – 257	1	Phosphothreonine2 Publications Manual assertion based on experiment inⁱ Ref.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]. Ref.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].
Modified residueⁱ	259 – 259	1	Phosphoserine1 Publication Manual assertion based on experiment inⁱ Ref.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].
Modified residueⁱ	266 – 266	1	Phosphoserine
Modified residueⁱ	371 – 371	1	Phosphoserine; by PRKDC1 Publication Manual assertion based on experiment inⁱ Ref.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.
Modified residueⁱ	408 – 408	1	Phosphoserine1 Publication Manual assertion based on experiment inⁱ Ref.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].
Modified residueⁱ	409 – 409	1	Phosphoserine1 Publication Manual assertion based on experiment inⁱ Ref.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].
Modified residueⁱ	410 – 410	1	Phosphoserine1 Publication Manual assertion based on experiment inⁱ Ref.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].
Modified residueⁱ	416 – 416	1	Phosphoserine
Modified residueⁱ	418 – 418	1	Phosphoserine
Modified residueⁱ	421 – 421	1	Phosphoserine1 Publication Manual assertion based on experiment inⁱ Ref.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].
Modified residueⁱ	446 – 446	1	Phosphoserine
Modified residueⁱ	447 – 447	1	Phosphoserine
Modified residueⁱ	453 – 453	1	Phosphothreonine3 Publications Manual assertion based on experiment inⁱ Ref.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]. Ref.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]. Ref.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].
Modified residueⁱ	457 – 457	1	Phosphothreonine1 Publication Manual assertion based on experiment inⁱ Ref.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].
Modified residueⁱ	461 – 461	1	Phosphoserine1 Publication Manual assertion based on experiment inⁱ Ref.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].
Modified residueⁱ	485 – 485	1	Phosphoserine2 Publications Manual assertion based on experiment inⁱ Ref.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. Ref.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].
Modified residueⁱ	488 – 488	1	Phosphothreonine2 Publications Manual assertion based on experiment inⁱ Ref.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. Ref.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].
Modified residueⁱ	518 – 518	1	Phosphoserine1 Publication Manual assertion based on experiment inⁱ Ref.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.
Modified residueⁱ	519 – 519	1	Phosphothreonine1 Publication Manual assertion based on experiment inⁱ Ref.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.
Modified residueⁱ	523 – 523	1	Phosphothreonine1 Publication Manual assertion based on experiment inⁱ Ref.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.

Post-translational modificationⁱ

Phosphorylation of Ser-371 causes dimer dissociation. Phosphorylation by CK2 promotes interaction with APTX and APLF.10 Publications

Sumoylated.1 Publication

Keywords - PTMⁱ

Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBⁱ	P18887.
PaxDbⁱ	P18887.
PRIDEⁱ	P18887.

PTM databases

PhosphoSiteⁱ	P18887.

PhosphoSiteⁱ

P18887.

Expressionⁱ

Gene expression databases

Bgeeⁱ	P18887.
CleanExⁱ	HS_XRCC1.
ExpressionAtlasⁱ	P18887. baseline and differential.
Genevestigatorⁱ	P18887.

Organism-specific databases

HPAⁱ	CAB005427. HPA006717.

Interactionⁱ

Subunit structureⁱ

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 APEX1.9 Publications

Binary interactionsⁱ

With	Entry	#Exp.	IntAct
APLF	Q8IW19	10	EBI-947466,EBI-1256044
APTX	Q7Z2E3	11	EBI-947466,EBI-847814
CHEK2	O96017	8	EBI-947466,EBI-1180783
PARP1	P09874	5	EBI-947466,EBI-355676
PNKP	Q96T60	5	EBI-947466,EBI-1045072
POLI	Q9UNA4	2	EBI-947466,EBI-741774

With

Entry

#Exp.

IntAct

Notes

APLF

Q8IW19

10

EBI-947466,EBI-1256044

APTX

Q7Z2E3

11

EBI-947466,EBI-847814

CHEK2

O96017

8

EBI-947466,EBI-1180783

PARP1

P09874

5

EBI-947466,EBI-355676

PNKP

Q96T60

5

EBI-947466,EBI-1045072

POLI

Q9UNA4

2

EBI-947466,EBI-741774

Protein-protein interaction databases

BioGridⁱ	113349. 41 interactions.
DIPⁱ	DIP-39067N.
IntActⁱ	P18887. 16 interactions.
MINTⁱ	MINT-245471.
STRINGⁱ	9606.ENSP00000262887.

Structureⁱ

Secondary structure

1

633

Legend: HelixTurnBeta strand

Show more details

Feature key	Position(s)	Length	Description
Helixⁱ	4 – 6	3	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:3LQC
Beta strandⁱ	7 – 12	6	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:3LQC
Helixⁱ	17 – 25	9	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:3LQC
Helixⁱ	28 – 36	9	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:3LQC
Turnⁱ	37 – 39	3	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:3LQC
Beta strandⁱ	41 – 53	13	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:3LQC
Beta strandⁱ	57 – 64	8	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:3LQC
Beta strandⁱ	66 – 73	8	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:3LQC
Beta strandⁱ	75 – 77	3	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:1XNA
Helixⁱ	81 – 83	3	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:3LQC
Beta strandⁱ	85 – 93	9	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:3LQC
Helixⁱ	96 – 101	6	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:3LQC
Beta strandⁱ	108 – 111	4	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:3LQC
Helixⁱ	113 – 115	3	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:3LQC
Helixⁱ	118 – 121	4	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:3LQC
Beta strandⁱ	125 – 133	9	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:3LQC
Beta strandⁱ	138 – 140	3	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:3K75
Beta strandⁱ	143 – 150	8	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:3LQC
Helixⁱ	313 – 316	4	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:2D8M
Turnⁱ	317 – 319	3	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:2D8M
Beta strandⁱ	323 – 329	7	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:2D8M
Helixⁱ	334 – 344	11	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:2D8M
Beta strandⁱ	347 – 352	6	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:2D8M
Beta strandⁱ	359 – 366	8	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:2D8M
Helixⁱ	368 – 376	9	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:2D8M
Beta strandⁱ	379 – 382	4	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:2D8M
Helixⁱ	384 – 391	8	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:2D8M
Helixⁱ	398 – 401	4	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:2D8M
Beta strandⁱ	404 – 407	4	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:2D8M
Turnⁱ	542 – 545	4	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:1CDZ
Beta strandⁱ	547 – 550	4	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:1CDZ
Helixⁱ	557 – 568	12	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:1CDZ
Beta strandⁱ	582 – 585	4	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:1CDZ
Helixⁱ	592 – 598	7	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:1CDZ
Beta strandⁱ	605 – 607	3	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:1CDZ
Helixⁱ	610 – 616	7	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:1CDZ
Turnⁱ	617 – 619	3	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:1CDZ
Helixⁱ	624 – 627	4	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:1CDZ

3D structure databases

Select the link destinations:
PDBeⁱ
RCSB PDBⁱ
PDBjⁱ

Links Updated

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1CDZ	X-ray	3.20	A	538-633	[»]
1XNA	NMR	-	A	1-183	[»]
1XNT	NMR	-	A	1-183	[»]
2D8M	NMR	-	A	305-420	[»]
2W3O	X-ray	1.85	C/D	515-522	[»]
3K75	X-ray	2.95	B/C	1-183	[»]
3K77	X-ray	2.60	A/B/C/D/E/F/G/H	1-155	[»]
3LQC	X-ray	2.35	A	1-183	[»]

ProteinModelPortalⁱ

P18887.

SMRⁱ

P18887. Positions 2-153, 301-415, 538-633.

ModBaseⁱ

Search...

MobiDBⁱ

Search...

Miscellaneous databases

EvolutionaryTraceⁱ	P18887.

EvolutionaryTraceⁱ

P18887.

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
Domainⁱ	315 – 403	89	BRCT 1PROSITE-ProRule annotation Manual assertion according to rulesⁱ PROSITE-ProRule:PRU00033			Add BLAST
Domainⁱ	538 – 629	92	BRCT 2PROSITE-ProRule annotation Manual assertion according to rulesⁱ PROSITE-ProRule:PRU00033			Add BLAST

Sequence similaritiesⁱ

Contains 2 BRCT domains.PROSITE-ProRule annotation

Keywords - Domainⁱ

Repeat

Phylogenomic databases

eggNOGⁱ	NOG295271.
GeneTreeⁱ	ENSGT00390000004140.
HOVERGENⁱ	HBG052992.
InParanoidⁱ	P18887.
KOⁱ	K10803.
OrthoDBⁱ	EOG77WWD8.
PhylomeDBⁱ	P18887.
TreeFamⁱ	TF101201.

Family and domain databases

Gene3Dⁱ	2.60.120.260. 1 hit. 3.40.50.10190. 2 hits.
InterProⁱ	IPR001357. BRCT_dom. IPR008979. Galactose-bd-like. IPR002706. Xrcc1_N. [Graphical view]
Pfamⁱ	PF00533. BRCT. 2 hits. PF01834. XRCC1_N. 1 hit. [Graphical view]
SMARTⁱ	SM00292. BRCT. 2 hits. [Graphical view]
SUPFAMⁱ	SSF49785. SSF49785. 1 hit. SSF52113. SSF52113. 2 hits.
PROSITEⁱ	PS50172. BRCT. 2 hits. [Graphical view]

Sequenceⁱ

Sequence statusⁱ: Complete.

P18887-1 [UniParc]FASTA Add to Basket

« Hide

        10         20         30         40         50
MPEIRLRHVV SCSSQDSTHC AENLLKADTY RKWRAAKAGE KTISVVLQLE 
        60         70         80         90        100
KEEQIHSVDI GNDGSAFVEV LVGSSAGGAG EQDYEVLLVT SSFMSPSESR 
       110        120        130        140        150
SGSNPNRVRM FGPDKLVRAA AEKRWDRVKI VCSQPYSKDS PFGLSFVRFH 
       160        170        180        190        200
SPPDKDEAEA PSQKVTVTKL GQFRVKEEDE SANSLRPGAL FFSRINKTSP 
       210        220        230        240        250
VTASDPAGPS YAAATLQASS AASSASPVSR AIGSTSKPQE SPKGKRKLDL 
       260        270        280        290        300
NQEEKKTPSK PPAQLSPSVP KRPKLPAPTR TPATAPVPAR AQGAVTGKPR 
       310        320        330        340        350
GEGTEPRRPR AGPEELGKIL QGVVVVLSGF QNPFRSELRD KALELGAKYR 
       360        370        380        390        400
PDWTRDSTHL ICAFANTPKY SQVLGLGGRI VRKEWVLDCH RMRRRLPSRR 
       410        420        430        440        450
YLMAGPGSSS EEDEASHSGG SGDEAPKLPQ KQPQTKTKPT QAAGPSSPQK 
       460        470        480        490        500
PPTPEETKAA SPVLQEDIDI EGVQSEGQDN GAEDSGDTED ELRRVAEQKE 
       510        520        530        540        550
HRLPPGQEEN GEDPYAGSTD ENTDSEEHQE PPDLPVPELP DFFQGKHFFL 
       560        570        580        590        600
YGEFPGDERR KLIRYVTAFN GELEDNMSDR VQFVITAQEW DPSFEEALMD 
       610        620        630 
NPSLAFVRPR WIYSCNEKQK LLPHQLYGVV PQA

Length:633

Mass (Da):69,477

Last modified:January 11, 2011 - v2

Checksum:ⁱ30DB3321234DBFC2

GO

Polymorphismⁱ

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

Natural variant

Feature key	Position(s)	Length	Description	Feature identifier
Natural variantⁱ	7 – 7	1	R → L. Corresponds to variant rs2307186 [ dbSNP \| Ensembl ].	VAR_014773
Natural variantⁱ	10 – 10	1	V → M. Corresponds to variant rs2307171 [ dbSNP \| Ensembl ].	VAR_014774
Natural variantⁱ	72 – 72	1	V → A.1 Publication Manual assertion based on experiment inⁱ Ref.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. Corresponds to variant rs25496 [ dbSNP \| Ensembl ].	VAR_016168
Natural variantⁱ	107 – 107	1	R → H. Corresponds to variant rs2228487 [ dbSNP \| Ensembl ].	VAR_029228
Natural variantⁱ	157 – 157	1	E → K. Corresponds to variant rs2307180 [ dbSNP \| Ensembl ].	VAR_014775
Natural variantⁱ	161 – 161	1	P → L.1 Publication Manual assertion based on experiment inⁱ Ref.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. Corresponds to variant rs2307191 [ dbSNP \| Ensembl ].	VAR_014776
Natural variantⁱ	194 – 194	1	R → W.2 Publications Manual assertion based on experiment inⁱ Ref.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. Ref.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. Corresponds to variant rs1799782 [ dbSNP \| Ensembl ].	VAR_013400
Natural variantⁱ	280 – 280	1	R → H.2 Publications Manual assertion based on experiment inⁱ Ref.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. Ref.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. Corresponds to variant rs25489 [ dbSNP \| Ensembl ].	VAR_013401
Natural variantⁱ	298 – 298	1	K → N. Corresponds to variant rs2307188 [ dbSNP \| Ensembl ].	VAR_014777
Natural variantⁱ	304 – 304	1	T → A.1 Publication Manual assertion based on experiment inⁱ Ref.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. Corresponds to variant rs25490 [ dbSNP \| Ensembl ].	VAR_018775
Natural variantⁱ	309 – 309	1	P → S.1 Publication Manual assertion based on experiment inⁱ Ref.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. Corresponds to variant rs25491 [ dbSNP \| Ensembl ].	VAR_014778
Natural variantⁱ	350 – 350	1	R → W in a colorectal cancer sample; somatic mutation. 1 Publication Manual assertion based on experiment inⁱ Ref.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. Velculescu V.E. Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] TRP-350.	VAR_036277
Natural variantⁱ	399 – 399	1	R → Q.7 Publications Manual assertion based on experiment inⁱ Ref.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. Ref.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. Ref.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. Lucas S.M. Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT GLN-399. Ref.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. Ref.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. Ref.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. Ref.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. Corresponds to variant rs25487 [ dbSNP \| Ensembl ].	VAR_011487
Natural variantⁱ	485 – 485	1	S → Y. Corresponds to variant rs2307184 [ dbSNP \| Ensembl ].	VAR_014779
Natural variantⁱ	514 – 514	1	P → L. Corresponds to variant rs25474 [ dbSNP \| Ensembl ].	VAR_016169
Natural variantⁱ	559 – 559	1	R → Q. Corresponds to variant rs2307167 [ dbSNP \| Ensembl ].	VAR_014780
Natural variantⁱ	560 – 560	1	R → W. Corresponds to variant rs2307166 [ dbSNP \| Ensembl ].	VAR_014781
Natural variantⁱ	576 – 576	1	N → S.1 Publication Manual assertion based on experiment inⁱ Ref.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. Corresponds to variant rs2307177 [ dbSNP \| Ensembl ].	VAR_014782
Natural variantⁱ	576 – 576	1	N → Y.4 Publications Manual assertion based on experiment inⁱ Ref.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. Ref.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. Ref.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. Ref.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]. Corresponds to variant rs2682557 [ dbSNP \| Ensembl ].	VAR_061727

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	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.
CCDSⁱ	CCDS12624.1.
PIRⁱ	A36353.
RefSeqⁱ	NP_006288.2. NM_006297.2.
UniGeneⁱ	Hs.98493.

Genome annotation databases

Ensemblⁱ	ENST00000262887; ENSP00000262887; ENSG00000073050.
GeneIDⁱ	7515.
KEGGⁱ	hsa:7515.

Polymorphism databases

DMDMⁱ	317373290.

DMDMⁱ

317373290.

Keywords - Coding sequence diversityⁱ

Polymorphism

Cross-referencesⁱ

Web resourcesⁱ

NIEHS-SNPs

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	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.
CCDSⁱ	CCDS12624.1.
PIRⁱ	A36353.
RefSeqⁱ	NP_006288.2. NM_006297.2.
UniGeneⁱ	Hs.98493.

3D structure databases

Select the link destinations:
PDBeⁱ
RCSB PDBⁱ
PDBjⁱ

Links Updated

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1CDZ	X-ray	3.20	A	538-633	[»]
1XNA	NMR	-	A	1-183	[»]
1XNT	NMR	-	A	1-183	[»]
2D8M	NMR	-	A	305-420	[»]
2W3O	X-ray	1.85	C/D	515-522	[»]
3K75	X-ray	2.95	B/C	1-183	[»]
3K77	X-ray	2.60	A/B/C/D/E/F/G/H	1-155	[»]
3LQC	X-ray	2.35	A	1-183	[»]

ProteinModelPortalⁱ

P18887.

SMRⁱ

P18887. Positions 2-153, 301-415, 538-633.

ModBaseⁱ

Search...

MobiDBⁱ

Search...

Protein-protein interaction databases

BioGridⁱ	113349. 41 interactions.
DIPⁱ	DIP-39067N.
IntActⁱ	P18887. 16 interactions.
MINTⁱ	MINT-245471.
STRINGⁱ	9606.ENSP00000262887.

PTM databases

PhosphoSiteⁱ	P18887.

PhosphoSiteⁱ

P18887.

Polymorphism databases

DMDMⁱ	317373290.

DMDMⁱ

317373290.

Proteomic databases

MaxQBⁱ	P18887.
PaxDbⁱ	P18887.
PRIDEⁱ	P18887.

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

Ensemblⁱ	ENST00000262887; ENSP00000262887; ENSG00000073050.
GeneIDⁱ	7515.
KEGGⁱ	hsa:7515.

Organism-specific databases

CTDⁱ	7515.
GeneCardsⁱ	GC19M044047.
H-InvDB	HIX0040090.
HGNCⁱ	HGNC:12828. XRCC1.
HPAⁱ	CAB005427. HPA006717.
MIMⁱ	194360. gene.
neXtProtⁱ	NX_P18887.
PharmGKBⁱ	PA369.
GenAtlasⁱ	Search...

Phylogenomic databases

eggNOGⁱ	NOG295271.
GeneTreeⁱ	ENSGT00390000004140.
HOVERGENⁱ	HBG052992.
InParanoidⁱ	P18887.
KOⁱ	K10803.
OrthoDBⁱ	EOG77WWD8.
PhylomeDBⁱ	P18887.
TreeFamⁱ	TF101201.

Enzyme and pathway databases

Reactomeⁱ	REACT_933. Resolution of AP sites via the single-nucleotide replacement pathway.
SignaLinkⁱ	P18887.

Miscellaneous databases

ChiTaRSⁱ	XRCC1. human.
EvolutionaryTraceⁱ	P18887.
GeneWikiⁱ	XRCC1.
GenomeRNAiⁱ	7515.
NextBioⁱ	29407.
PROⁱ	P18887.
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	P18887.
CleanExⁱ	HS_XRCC1.
ExpressionAtlasⁱ	P18887. baseline and differential.
Genevestigatorⁱ	P18887.

Family and domain databases

Gene3Dⁱ	2.60.120.260. 1 hit. 3.40.50.10190. 2 hits.
InterProⁱ	IPR001357. BRCT_dom. IPR008979. Galactose-bd-like. IPR002706. Xrcc1_N. [Graphical view]
Pfamⁱ	PF00533. BRCT. 2 hits. PF01834. XRCC1_N. 1 hit. [Graphical view]
SMARTⁱ	SM00292. BRCT. 2 hits. [Graphical view]
SUPFAMⁱ	SSF49785. SSF49785. 1 hit. SSF52113. SSF52113. 2 hits.
PROSITEⁱ	PS50172. BRCT. 2 hits. [Graphical view]
ProtoNetⁱ	Search...

Publicationsⁱ

« Hide 'large scale' publications

"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.
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.
"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.
"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.
Lucas S.M.
Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT GLN-399.
"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.
"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.
"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.
"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.
"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.
"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.
"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.
"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.
"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.
"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.
"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.
"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.
"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].
"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.
"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.
"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.
"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].
"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.
"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.
"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.
"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.
"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.
"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.
Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] TRP-350.
"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.

Entry informationⁱ

Entry nameⁱ

XRCC1_HUMAN

Accessionⁱ

Primary (citable) accession number: P18887
Secondary accession number(s): Q6IBS4, Q9HCB1

Entry historyⁱ

Integrated into UniProtKB/Swiss-Prot:	November 1, 1990
Last sequence update:	January 11, 2011
Last modified:	February 4, 2015
This is version 163 of the entry and version 2 of the sequence. [Complete history]

Entry statusⁱ

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.

Miscellaneousⁱ

Keywords - Technical termⁱ

3D-structure, Complete proteome, Reference proteome

Documents

Human chromosome 19
Human chromosome 19: entries, gene names and cross-references to MIM
Human entries with polymorphisms or disease mutations
List of human entries with polymorphisms or disease mutations
Human polymorphisms and disease mutations
Index of human polymorphisms and disease mutations
MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
PDB cross-references
Index of Protein Data Bank (PDB) cross-references
SIMILARITY comments
Index of protein domains and families

External Data

Dasty 3

Similar proteinsⁱ

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:

100%	UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%	UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%	UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.

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P18887 - XRCC1_HUMAN

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P18887 - XRCC1_HUMAN

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DNA repair protein XRCC1

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<p>Provides any useful information about the protein, mostly biological knowledge.</p><p><a href='../manual/function_section' target='_top'>More...</a></p>Functioni

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:</p><p><a href='../manual/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:</p><p><a href='../manual/gene_ontology' target='_top'>More...</a></p>GO - Biological processi

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<p>Provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.</p><p><a href='../manual/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

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<p>Provides information on the location and the topology of the mature protein in the cell.</p><p><a href='../manual/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:</p><p><a href='../manual/gene_ontology' target='_top'>More...</a></p>GO - Cellular componenti

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<p>Contains the literature citations that are the sources of data used to annotate the entry. Each reference is numbered and contains several subsections allowing a precise description of a given citation.</p><p><a href='../manual/publications_section' target='_top'>More...</a></p>Publicationsi

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Functionⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

GO - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Expressionⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Sequenceⁱ

Cross-referencesⁱ

Web resourcesⁱ

Publicationsⁱ

Entry informationⁱ

Miscellaneousⁱ