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P18887

- XRCC1_HUMAN

UniProt

P18887 - XRCC1_HUMAN

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Protein

DNA repair protein XRCC1

Gene

XRCC1

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

Display
All None

  • Function
  • Names & Taxonomy
  • Subcellular locationSubcell. location
  • Pathology & BiotechPathol./Biotech
  • PTM / Processing
  • Expression
  • Interaction
  • Structure
  • Family & Domains
  • Sequence
  • Cross-references
  • Publications
  • Entry information
  • Miscellaneous
  • Similar proteins
Top

Functioni

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

GO - Molecular functioni

  1. damaged DNA binding Source: InterPro

GO - Biological processi

  1. base-excision repair Source: RefGenome
  2. DNA repair Source: Reactome
  3. hippocampus development Source: Ensembl
  4. response to drug Source: Ensembl
  5. response to hypoxia Source: Ensembl
  6. response to organic substance Source: Ensembl
  7. single strand break repair Source: InterPro
Complete GO annotation...

Keywords - Biological processi

DNA damage, DNA repair

Enzyme and pathway databases

ReactomeiREACT_933. Resolution of AP sites via the single-nucleotide replacement pathway.
SignaLinkiP18887.

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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
ProteomesiUP000005640: Chromosome 19

Organism-specific databases

HGNCiHGNC:12828. XRCC1.

Subcellular locationi

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

GO - Cellular componenti

  1. nucleoplasm Source: Reactome
  2. nucleus Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA369.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 633633DNA repair protein XRCC1PRO_0000066044Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei140 – 1401Phosphoserine1 Publication
Modified residuei198 – 1981Phosphothreonine1 Publication
Modified residuei199 – 1991Phosphoserine1 Publication
Modified residuei202 – 2021Phosphothreonine1 Publication
Modified residuei204 – 2041Phosphoserine1 Publication
Modified residuei211 – 2111Phosphotyrosine
Modified residuei226 – 2261Phosphoserine2 Publications
Modified residuei241 – 2411Phosphoserine4 Publications
Modified residuei257 – 2571Phosphothreonine2 Publications
Modified residuei259 – 2591Phosphoserine1 Publication
Modified residuei266 – 2661Phosphoserine
Modified residuei371 – 3711Phosphoserine; by PRKDC1 Publication
Modified residuei408 – 4081Phosphoserine1 Publication
Modified residuei409 – 4091Phosphoserine1 Publication
Modified residuei410 – 4101Phosphoserine1 Publication
Modified residuei416 – 4161Phosphoserine
Modified residuei418 – 4181Phosphoserine
Modified residuei421 – 4211Phosphoserine1 Publication
Modified residuei446 – 4461Phosphoserine
Modified residuei447 – 4471Phosphoserine
Modified residuei453 – 4531Phosphothreonine3 Publications
Modified residuei457 – 4571Phosphothreonine1 Publication
Modified residuei461 – 4611Phosphoserine1 Publication
Modified residuei485 – 4851Phosphoserine2 Publications
Modified residuei488 – 4881Phosphothreonine2 Publications
Modified residuei518 – 5181Phosphoserine1 Publication
Modified residuei519 – 5191Phosphothreonine1 Publication
Modified residuei523 – 5231Phosphothreonine1 Publication

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

MaxQBiP18887.
PaxDbiP18887.
PRIDEiP18887.

PTM databases

PhosphoSiteiP18887.

Expressioni

Gene expression databases

BgeeiP18887.
CleanExiHS_XRCC1.
ExpressionAtlasiP18887. baseline and differential.
GenevestigatoriP18887.

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

WithEntry#Exp.IntActNotes
APLFQ8IW1910EBI-947466,EBI-1256044
APTXQ7Z2E311EBI-947466,EBI-847814
CHEK2O960178EBI-947466,EBI-1180783
PARP1P098745EBI-947466,EBI-355676
PNKPQ96T605EBI-947466,EBI-1045072
POLIQ9UNA42EBI-947466,EBI-741774

Protein-protein interaction databases

BioGridi113349. 41 interactions.
DIPiDIP-39067N.
IntActiP18887. 16 interactions.
MINTiMINT-245471.
STRINGi9606.ENSP00000262887.

Structurei

Secondary structure

1
633
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 63Combined sources
Beta strandi7 – 126Combined sources
Helixi17 – 259Combined sources
Helixi28 – 369Combined sources
Turni37 – 393Combined sources
Beta strandi41 – 5313Combined sources
Beta strandi57 – 648Combined sources
Beta strandi66 – 738Combined sources
Beta strandi75 – 773Combined sources
Helixi81 – 833Combined sources
Beta strandi85 – 939Combined sources
Helixi96 – 1016Combined sources
Beta strandi108 – 1114Combined sources
Helixi113 – 1153Combined sources
Helixi118 – 1214Combined sources
Beta strandi125 – 1339Combined sources
Beta strandi138 – 1403Combined sources
Beta strandi143 – 1508Combined sources
Helixi313 – 3164Combined sources
Turni317 – 3193Combined sources
Beta strandi323 – 3297Combined sources
Helixi334 – 34411Combined sources
Beta strandi347 – 3526Combined sources
Beta strandi359 – 3668Combined sources
Helixi368 – 3769Combined sources
Beta strandi379 – 3824Combined sources
Helixi384 – 3918Combined sources
Helixi398 – 4014Combined sources
Beta strandi404 – 4074Combined sources
Turni542 – 5454Combined sources
Beta strandi547 – 5504Combined sources
Helixi557 – 56812Combined sources
Beta strandi582 – 5854Combined sources
Helixi592 – 5987Combined sources
Beta strandi605 – 6073Combined sources
Helixi610 – 6167Combined sources
Turni617 – 6193Combined sources
Helixi624 – 6274Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP18887.
SMRiP18887. Positions 2-153, 301-415, 538-633.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP18887.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini315 – 40389BRCT 1PROSITE-ProRule annotationAdd
BLAST
Domaini538 – 62992BRCT 2PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 2 BRCT domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG295271.
GeneTreeiENSGT00390000004140.
HOVERGENiHBG052992.
InParanoidiP18887.
KOiK10803.
OrthoDBiEOG77WWD8.
PhylomeDBiP18887.
TreeFamiTF101201.

Family and domain databases

Gene3Di2.60.120.260. 1 hit.
3.40.50.10190. 2 hits.
InterProiIPR001357. BRCT_dom.
IPR008979. Galactose-bd-like.
IPR002706. Xrcc1_N.
[Graphical view]
PfamiPF00533. BRCT. 2 hits.
PF01834. XRCC1_N. 1 hit.
[Graphical view]
SMARTiSM00292. BRCT. 2 hits.
[Graphical view]
SUPFAMiSSF49785. SSF49785. 1 hit.
SSF52113. SSF52113. 2 hits.
PROSITEiPS50172. BRCT. 2 hits.
[Graphical view]

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)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti7 – 71R → L.
Corresponds to variant rs2307186 [ dbSNP | Ensembl ].		VAR_014773
Natural varianti10 – 101V → M.
Corresponds to variant rs2307171 [ dbSNP | Ensembl ].		VAR_014774
Natural varianti72 – 721V → A.1 Publication
Corresponds to variant rs25496 [ dbSNP | Ensembl ].		VAR_016168
Natural varianti107 – 1071R → H.
Corresponds to variant rs2228487 [ dbSNP | Ensembl ].		VAR_029228
Natural varianti157 – 1571E → K.
Corresponds to variant rs2307180 [ dbSNP | Ensembl ].		VAR_014775
Natural varianti161 – 1611P → L.1 Publication
Corresponds to variant rs2307191 [ dbSNP | Ensembl ].		VAR_014776
Natural varianti194 – 1941R → W.2 Publications
Corresponds to variant rs1799782 [ dbSNP | Ensembl ].		VAR_013400
Natural varianti280 – 2801R → H.2 Publications
Corresponds to variant rs25489 [ dbSNP | Ensembl ].		VAR_013401
Natural varianti298 – 2981K → N.
Corresponds to variant rs2307188 [ dbSNP | Ensembl ].		VAR_014777
Natural varianti304 – 3041T → A.1 Publication
Corresponds to variant rs25490 [ dbSNP | Ensembl ].		VAR_018775
Natural varianti309 – 3091P → S.1 Publication
Corresponds to variant rs25491 [ dbSNP | Ensembl ].		VAR_014778
Natural varianti350 – 3501R → W in a colorectal cancer sample; somatic mutation. 1 Publication
VAR_036277
Natural varianti399 – 3991R → Q.7 Publications
Corresponds to variant rs25487 [ dbSNP | Ensembl ].		VAR_011487
Natural varianti485 – 4851S → Y.
Corresponds to variant rs2307184 [ dbSNP | Ensembl ].		VAR_014779
Natural varianti514 – 5141P → L.
Corresponds to variant rs25474 [ dbSNP | Ensembl ].		VAR_016169
Natural varianti559 – 5591R → Q.
Corresponds to variant rs2307167 [ dbSNP | Ensembl ].		VAR_014780
Natural varianti560 – 5601R → W.
Corresponds to variant rs2307166 [ dbSNP | Ensembl ].		VAR_014781
Natural varianti576 – 5761N → S.1 Publication
Corresponds to variant rs2307177 [ dbSNP | Ensembl ].		VAR_014782
Natural varianti576 – 5761N → Y.4 Publications
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.
CCDSiCCDS12624.1.
PIRiA36353.
RefSeqiNP_006288.2. NM_006297.2.
UniGeneiHs.98493.

Genome annotation databases

EnsembliENST00000262887; ENSP00000262887; ENSG00000073050.
GeneIDi7515.
KEGGihsa:7515.

Polymorphism databases

DMDMi317373290.

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.

Polymorphism databases

DMDMi 317373290.

Proteomic databases

MaxQBi P18887.
PaxDbi P18887.
PRIDEi P18887.

Protocols and materials databases

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
  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, 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. 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. 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. 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. Cited for: VARIANT [LARGE SCALE ANALYSIS] TRP-350.
  28. Cited for: VARIANT [LARGE SCALE ANALYSIS] TYR-576, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Entry informationi

Entry nameiXRCC1_HUMAN
AccessioniPrimary (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: January 7, 2015
This is version 162 of the entry and version 2 of the sequence. [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
  6. 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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