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Protein

DNA repair protein XRCC1

Gene

XRCC1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in DNA single-strand break repair by mediating the assembly of DNA break repair protein complexes. Probably during DNA repair, negatively regulates ADP-ribose levels by modulating ADP-ribosyltransferase PARP1 activity.1 Publication

GO - Molecular functioni

  • 3' overhang single-stranded DNA endodeoxyribonuclease activity Source: Ensembl
  • DNA ligase activity Source: Reactome
  • enzyme binding Source: BHF-UCL
  • oxidized DNA binding Source: UniProtKB

GO - Biological processi

Keywordsi

Biological processDNA damage, DNA repair

Enzyme and pathway databases

ReactomeiR-HSA-110381. Resolution of AP sites via the single-nucleotide replacement pathway.
R-HSA-5649702. APEX1-Independent Resolution of AP Sites via the Single Nucleotide Replacement Pathway.
R-HSA-5685939. HDR through MMEJ (alt-NHEJ).
R-HSA-5696397. Gap-filling DNA repair synthesis and ligation in GG-NER.
R-HSA-6782210. Gap-filling DNA repair synthesis and ligation in TC-NER.
SignaLinkiP18887.
SIGNORiP18887.

Names & Taxonomyi

Protein namesi
Recommended name:
DNA repair protein XRCC1
Alternative name(s):
X-ray repair cross-complementing protein 1
Gene namesi
Name:XRCC1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 19

Organism-specific databases

EuPathDBiHostDB:ENSG00000073050.11.
HGNCiHGNC:12828. XRCC1.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

Spinocerebellar ataxia, autosomal recessive, 26 (SCAR26)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA form of spinocerebellar ataxia, a clinically and genetically heterogeneous group of cerebellar disorders due to degeneration of the cerebellum with variable involvement of the brainstem and spinal cord. SCAR26 is a progressive disease characterized by gait and limb ataxia, loss of independent ambulation, oculomotor apraxia, and peripheral neuropathy with distal muscle weakness and areflexia.
See also OMIM:617633
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_079140431K → N in SCAR26; may result in aberrant splicing. 1 PublicationCorresponds to variant dbSNP:rs761564262Ensembl.1
Natural variantiVAR_079141465 – 633Missing in SCAR26. 1 PublicationAdd BLAST169

Keywords - Diseasei

Neurodegeneration

Organism-specific databases

DisGeNETi7515.
MIMi617633. phenotype.
PharmGKBiPA369.

Polymorphism and mutation databases

BioMutaiXRCC1.
DMDMi317373290.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000660441 – 633DNA repair protein XRCC1Add BLAST633

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei140PhosphoserineCombined sources1
Cross-linki176Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)Combined sources
Cross-linki176Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei198PhosphothreonineCombined sources1
Modified residuei199PhosphoserineCombined sources1
Modified residuei202PhosphothreonineCombined sources1
Modified residuei204PhosphoserineCombined sources1
Modified residuei226PhosphoserineCombined sources1
Modified residuei241PhosphoserineCombined sources1
Modified residuei257PhosphothreonineCombined sources1
Modified residuei259PhosphoserineCombined sources1
Modified residuei266PhosphoserineCombined sources1
Modified residuei281PhosphothreonineCombined sources1
Modified residuei371Phosphoserine; by PRKDC1 Publication1
Modified residuei408PhosphoserineCombined sources1
Modified residuei409PhosphoserineCombined sources1
Modified residuei410PhosphoserineCombined sources1
Modified residuei421PhosphoserineCombined sources1
Modified residuei446PhosphoserineCombined sources1
Modified residuei447PhosphoserineCombined sources1
Modified residuei453PhosphothreonineCombined sources1
Modified residuei457PhosphothreonineCombined sources1
Modified residuei461PhosphoserineCombined sources1
Modified residuei485PhosphoserineCombined sources1 Publication1
Modified residuei488PhosphothreonineCombined sources1 Publication1
Modified residuei518Phosphoserine1 Publication1
Modified residuei519Phosphothreonine1 Publication1
Modified residuei523Phosphothreonine1 Publication1

Post-translational modificationi

Phosphorylation of Ser-371 causes dimer dissociation. Phosphorylation by CK2 promotes interaction with APTX and APLF.5 Publications
Sumoylated.1 Publication

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP18887.
MaxQBiP18887.
PaxDbiP18887.
PeptideAtlasiP18887.
PRIDEiP18887.

PTM databases

iPTMnetiP18887.
PhosphoSitePlusiP18887.

Expressioni

Tissue specificityi

Expressed in fibroblasts, retinal pigmented epithelial cells and lymphoblastoid cells (at protein level).1 Publication

Gene expression databases

BgeeiENSG00000073050.
CleanExiHS_XRCC1.
ExpressionAtlasiP18887. baseline and differential.
GenevisibleiP18887. HS.

Organism-specific databases

HPAiCAB005427.
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

Show more details

GO - Molecular functioni

  • enzyme binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi113349. 77 interactors.
CORUMiP18887.
DIPiDIP-39067N.
IntActiP18887. 45 interactors.
MINTiMINT-245471.
STRINGi9606.ENSP00000262887.

Structurei

Secondary structure

1633
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi4 – 6Combined sources3
Beta strandi7 – 12Combined sources6
Helixi17 – 25Combined sources9
Helixi28 – 36Combined sources9
Turni37 – 39Combined sources3
Beta strandi41 – 53Combined sources13
Beta strandi57 – 64Combined sources8
Beta strandi66 – 73Combined sources8
Beta strandi75 – 77Combined sources3
Helixi81 – 83Combined sources3
Beta strandi85 – 93Combined sources9
Helixi96 – 101Combined sources6
Beta strandi108 – 111Combined sources4
Helixi113 – 115Combined sources3
Helixi118 – 121Combined sources4
Beta strandi125 – 133Combined sources9
Beta strandi138 – 140Combined sources3
Beta strandi143 – 150Combined sources8
Helixi313 – 316Combined sources4
Turni317 – 319Combined sources3
Beta strandi323 – 329Combined sources7
Helixi334 – 344Combined sources11
Beta strandi347 – 352Combined sources6
Beta strandi359 – 366Combined sources8
Helixi368 – 376Combined sources9
Beta strandi379 – 382Combined sources4
Helixi384 – 391Combined sources8
Helixi398 – 401Combined sources4
Beta strandi404 – 407Combined sources4
Turni542 – 545Combined sources4
Beta strandi547 – 550Combined sources4
Helixi557 – 568Combined sources12
Beta strandi582 – 585Combined sources4
Helixi592 – 598Combined sources7
Beta strandi605 – 607Combined sources3
Helixi610 – 616Combined sources7
Turni617 – 619Combined sources3
Helixi624 – 627Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
5E6QX-ray2.31A241-276[»]
ProteinModelPortaliP18887.
SMRiP18887.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP18887.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini315 – 403BRCT 1PROSITE-ProRule annotationAdd BLAST89
Domaini538 – 629BRCT 2PROSITE-ProRule annotationAdd BLAST92

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG3226. Eukaryota.
ENOG410ZE1H. LUCA.
HOVERGENiHBG052992.
InParanoidiP18887.
KOiK10803.
OrthoDBiEOG091G0KP0.
PhylomeDBiP18887.
TreeFamiTF101201.

Family and domain databases

CDDicd00027. BRCT. 2 hits.
Gene3Di2.60.120.260. 1 hit.
3.40.50.10190. 2 hits.
InterProiView protein in InterPro
IPR001357. BRCT_dom.
IPR036420. BRCT_dom_sf.
IPR008979. Galactose-bd-like_sf.
IPR002706. Xrcc1_N.
PfamiView protein in Pfam
PF00533. BRCT. 1 hit.
PF16589. BRCT_2. 1 hit.
PF01834. XRCC1_N. 1 hit.
SMARTiView protein in SMART
SM00292. BRCT. 2 hits.
SUPFAMiSSF49785. SSF49785. 1 hit.
SSF52113. SSF52113. 2 hits.
PROSITEiView protein in PROSITE
PS50172. BRCT. 2 hits.

Sequencei

Sequence statusi: Complete.

P18887-1 [UniParc]FASTAAdd 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 keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0147737R → L. Corresponds to variant dbSNP:rs2307186Ensembl.1
Natural variantiVAR_01477410V → M. Corresponds to variant dbSNP:rs2307171Ensembl.1
Natural variantiVAR_01616872V → A1 PublicationCorresponds to variant dbSNP:rs25496Ensembl.1
Natural variantiVAR_029228107R → H. Corresponds to variant dbSNP:rs2228487Ensembl.1
Natural variantiVAR_014775157E → K. Corresponds to variant dbSNP:rs2307180Ensembl.1
Natural variantiVAR_014776161P → L1 PublicationCorresponds to variant dbSNP:rs2307191Ensembl.1
Natural variantiVAR_013400194R → W2 PublicationsCorresponds to variant dbSNP:rs1799782Ensembl.1
Natural variantiVAR_013401280R → H2 PublicationsCorresponds to variant dbSNP:rs25489Ensembl.1
Natural variantiVAR_014777298K → N. Corresponds to variant dbSNP:rs2307188Ensembl.1
Natural variantiVAR_018775304T → A1 PublicationCorresponds to variant dbSNP:rs25490Ensembl.1
Natural variantiVAR_014778309P → S1 PublicationCorresponds to variant dbSNP:rs25491Ensembl.1
Natural variantiVAR_036277350R → W in a colorectal cancer sample; somatic mutation. 1 Publication1
Natural variantiVAR_011487399R → Q7 PublicationsCorresponds to variant dbSNP:rs25487Ensembl.1
Natural variantiVAR_079140431K → N in SCAR26; may result in aberrant splicing. 1 PublicationCorresponds to variant dbSNP:rs761564262Ensembl.1
Natural variantiVAR_079141465 – 633Missing in SCAR26. 1 PublicationAdd BLAST169
Natural variantiVAR_014779485S → Y. Corresponds to variant dbSNP:rs2307184Ensembl.1
Natural variantiVAR_016169514P → L. Corresponds to variant dbSNP:rs25474Ensembl.1
Natural variantiVAR_014780559R → Q. Corresponds to variant dbSNP:rs2307167Ensembl.1
Natural variantiVAR_014781560R → W. Corresponds to variant dbSNP:rs2307166Ensembl.1
Natural variantiVAR_014782576N → S1 PublicationCorresponds to variant dbSNP:rs2307177Ensembl.1
Natural variantiVAR_061727576N → YCombined sources3 PublicationsCorresponds to variant dbSNP:rs2682557Ensembl.1

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.
CCDSiCCDS12624.1.
PIRiA36353.
RefSeqiNP_006288.2. NM_006297.2.
UniGeneiHs.98493.

Genome annotation databases

EnsembliENST00000262887; ENSP00000262887; ENSG00000073050.
GeneIDi7515.
KEGGihsa:7515.
UCSCiuc002owt.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Similar proteinsi

Entry informationi

Entry nameiXRCC1_HUMAN
AccessioniPrimary (citable) accession number: P18887
Secondary accession number(s): Q6IBS4, Q9HCB1
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: January 11, 2011
Last modified: November 22, 2017
This is version 192 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references