P18887 (XRCC1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
DNA repair protein XRCC1

Alternative name(s):
X-ray repair cross-complementing protein 1

Gene names

Name:

XRCC1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	633 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	DNA damage DNA repair
Cellular component	Nucleus
Coding sequence diversity	Polymorphism
Domain	Repeat
PTM	Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	base-excision repair Traceable author statement. Source: Reactome hippocampus development Inferred from electronic annotation. Source: Ensembl response to drug Inferred from electronic annotation. Source: Ensembl response to hypoxia Inferred from electronic annotation. Source: Ensembl response to organic substance Inferred from electronic annotation. Source: Ensembl single strand break repair Inferred from electronic annotation. Source: InterPro
Cellular_component	nucleoplasm Traceable author statement. Source: Reactome
Molecular_function	damaged DNA binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

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
POLI	Q9UNA4	2	EBI-947466,EBI-741774

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 633

633

DNA repair protein XRCC1

PRO_0000066044

Regions

Domain

315 – 403

89

BRCT 1

Domain

538 – 629

92

BRCT 2

Amino acid modifications

Modified residue

140

1

Phosphoserine Ref.20

Modified residue

198

1

Phosphothreonine Ref.18

Modified residue

199

1

Phosphoserine Ref.18

Modified residue

202

1

Phosphothreonine Ref.20

Modified residue

204

1

Phosphoserine Ref.20

Modified residue

211

1

Phosphotyrosine

Modified residue

226

1

Phosphoserine Ref.16 Ref.18

Modified residue

241

1

Phosphoserine Ref.16 Ref.18 Ref.20 Ref.21

Modified residue

257

1

Phosphothreonine Ref.16 Ref.20

Modified residue

259

1

Phosphoserine Ref.16

Modified residue

266

1

Phosphoserine

Modified residue

371

1

Phosphoserine; by PRKDC Ref.13

Modified residue

408

1

Phosphoserine Ref.16

Modified residue

409

1

Phosphoserine Ref.16

Modified residue

410

1

Phosphoserine Ref.16

Modified residue

416

1

Phosphoserine

Modified residue

418

1

Phosphoserine

Modified residue

421

1

Phosphoserine Ref.12

Modified residue

446

1

Phosphoserine

Modified residue

447

1

Phosphoserine

Modified residue

453

1

Phosphothreonine Ref.16 Ref.18 Ref.21

Modified residue

457

1

Phosphothreonine Ref.21

Modified residue

461

1

Phosphoserine Ref.18

Modified residue

485

1

Phosphoserine Ref.8 Ref.18

Modified residue

488

1

Phosphothreonine Ref.8 Ref.18

Modified residue

518

1

Phosphoserine Ref.23

Modified residue

519

1

Phosphothreonine Ref.23

Modified residue

523

1

Phosphothreonine Ref.23

Natural variations

Natural variant

7

1

R → L.
Corresponds to variant rs2307186 [ dbSNP | Ensembl ].

VAR_014773

Natural variant

10

1

V → M.
Corresponds to variant rs2307171 [ dbSNP | Ensembl ].

VAR_014774

Natural variant

72

1

V → A. Ref.2
Corresponds to variant rs25496 [ dbSNP | Ensembl ].

VAR_016168

Natural variant

107

1

R → H.
Corresponds to variant rs2228487 [ dbSNP | Ensembl ].

VAR_029228

Natural variant

157

1

E → K.
Corresponds to variant rs2307180 [ dbSNP | Ensembl ].

VAR_014775

Natural variant

161

1

P → L. Ref.2
Corresponds to variant rs2307191 [ dbSNP | Ensembl ].

VAR_014776

Natural variant

194

1

R → W. Ref.2 Ref.24
Corresponds to variant rs1799782 [ dbSNP | Ensembl ].

VAR_013400

Natural variant

280

1

R → H. Ref.2 Ref.24
Corresponds to variant rs25489 [ dbSNP | Ensembl ].

VAR_013401

Natural variant

298

1

K → N.
Corresponds to variant rs2307188 [ dbSNP | Ensembl ].

VAR_014777

Natural variant

304

1

T → A. Ref.2
Corresponds to variant rs25490 [ dbSNP | Ensembl ].

VAR_018775

Natural variant

309

1

P → S. Ref.2
Corresponds to variant rs25491 [ dbSNP | Ensembl ].

VAR_014778

Natural variant

350

1

R → W in a colorectal cancer sample; somatic mutation. Ref.27

VAR_036277

Natural variant

399

1

R → Q. Ref.2 Ref.3 Ref.4 Ref.5 Ref.24 Ref.25 Ref.26
Corresponds to variant rs25487 [ dbSNP | Ensembl ].

VAR_011487

Natural variant

485

1

S → Y.
Corresponds to variant rs2307184 [ dbSNP | Ensembl ].

VAR_014779

Natural variant

514

1

P → L.
Corresponds to variant rs25474 [ dbSNP | Ensembl ].

VAR_016169

Natural variant

559

1

R → Q.
Corresponds to variant rs2307167 [ dbSNP | Ensembl ].

VAR_014780

Natural variant

560

1

R → W.
Corresponds to variant rs2307166 [ dbSNP | Ensembl ].

VAR_014781

Natural variant

576

1

N → S. Ref.2
Corresponds to variant rs2307177 [ dbSNP | Ensembl ].

VAR_014782

Natural variant

576

1

N → Y. Ref.1 Ref.3 Ref.5 Ref.28
Corresponds to variant rs2682557 [ dbSNP | Ensembl ].

VAR_061727

Secondary structure

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633

Helix Strand Turn

Details...

Helix

4 – 6

3

Beta strand

7 – 12

6

Helix

17 – 25

9

Helix

28 – 36

9

Turn

37 – 39

3

Beta strand

41 – 53

13

Beta strand

57 – 64

8

Beta strand

66 – 73

8

Beta strand

75 – 77

3

Helix

81 – 83

3

Beta strand

85 – 93

9

Helix

96 – 101

6

Beta strand

108 – 111

4

Helix

113 – 115

3

Helix

118 – 121

4

Beta strand

125 – 133

9

Beta strand

138 – 140

3

Beta strand

143 – 150

8

Helix

313 – 316

4

Turn

317 – 319

3

Beta strand

323 – 329

7

Helix

334 – 344

11

Beta strand

347 – 352

6

Beta strand

359 – 366

8

Helix

368 – 376

9

Beta strand

379 – 382

4

Helix

384 – 391

8

Helix

398 – 401

4

Beta strand

404 – 407

4

Turn

542 – 545

4

Beta strand

547 – 550

4

Helix

557 – 568

12

Beta strand

582 – 585

4

Helix

592 – 598

7

Beta strand

605 – 607

3

Helix

610 – 616

7

Turn

617 – 619

3

Helix

624 – 627

4

Sequences

	Sequence		Length	Mass (Da)
	P18887 [UniParc]. Last modified January 11, 2011. Version 2. Checksum: 30DB3321234DBFC2	FASTA	633	69,477
	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

References

	« Hide 'large scale' referencesShow '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. , 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, 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY.
[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. , 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, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Web resources

NIEHS-SNPs

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.

IPI

IPI00002564.

PIR

A36353.

RefSeq

NP_006288.2. NM_006297.2.

UniGene

Hs.98493.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P18887.

SMR

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

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-39067N.

IntAct

P18887. 18 interactions.

MINT

MINT-245471.

STRING

9606.ENSP00000262887.

PTM databases

PhosphoSite

P18887.

Polymorphism databases

DMDM

139820.

Proteomic databases

PaxDb

P18887.

PRIDE

P18887.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000262887; ENSP00000262887; ENSG00000073050.

GeneID

7515.

KEGG

hsa:7515.

Organism-specific databases

CTD

7515.

GeneCards

GC19M044047.

H-InvDB

HIX0040090.

HGNC

HGNC:12828. XRCC1.

HPA

CAB005427.
HPA006717.

MIM

194360. gene.

neXtProt

NX_P18887.

PharmGKB

PA369.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG295271.

HOVERGEN

HBG052992.

InParanoid

P18887.

KO

K10803.

OrthoDB

EOG77WWD8.

Enzyme and pathway databases

Reactome

REACT_216. DNA Repair.

SignaLink

P18887.

Gene expression databases

ArrayExpress

P18887.

Bgee

P18887.

CleanEx

HS_XRCC1.

Genevestigator

P18887.

Family and domain databases

Gene3D

2.60.120.260. 1 hit.
3.40.50.10190. 2 hits.

InterPro

IPR001357. BRCT_dom.
IPR008979. Galactose-bd-like.
IPR002706. Xrcc1_N.
[Graphical view]

Pfam

PF00533. BRCT. 2 hits.
PF01834. XRCC1_N. 1 hit.
[Graphical view]

SMART

SM00292. BRCT. 2 hits.
[Graphical view]

SUPFAM

SSF49785. SSF49785. 1 hit.
SSF52113. SSF52113. 2 hits.

PROSITE

PS50172. BRCT. 2 hits.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

XRCC1. human.

EvolutionaryTrace

P18887.

GeneWiki

XRCC1.

GenomeRNAi

7515.

NextBio

29407.

PRO

P18887.

SOURCE

Search...

Entry information

Entry name

XRCC1_HUMAN

Accession

Primary (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:	November 13, 2013
This is version 149 of the entry and version 2 of the sequence. [Complete history]

Entry status

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.