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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

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
  2. protein binding Source: UniProtKB
Complete GO annotation...

GO - Biological processi

  1. DNA repair Source: Reactome
  2. base-excision repair Source: RefGenome
  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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 19

Organism-specific databases

HGNCiHGNC:12828. XRCC1.

Subcellular locationi

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

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 XRCC1
PRO_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.
Sumoylated.1 Publication

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP18887.
PaxDbiP18887.
PRIDEiP18887.

PTM databases

PhosphoSiteiP18887.

Expressioni

Gene expression databases

ArrayExpressiP18887.
BgeeiP18887.
CleanExiHS_XRCC1.
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 APEX1.8 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. 39 interactions.
DIPiDIP-39067N.
IntActiP18887. 16 interactions.
MINTiMINT-245471.
STRINGi9606.ENSP00000262887.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.

Miscellaneous databases

EvolutionaryTraceiP18887.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini315 – 40389BRCT 1
Add
BLAST
Domaini538 – 62992BRCT 2
Add
BLAST

Sequence similaritiesi

Contains 2 BRCT domains.

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG295271.
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

MPEIRLRHVV SCSSQDSTHC AENLLKADTY RKWRAAKAGE KTISVVLQLE    50
KEEQIHSVDI GNDGSAFVEV LVGSSAGGAG EQDYEVLLVT SSFMSPSESR 100
SGSNPNRVRM FGPDKLVRAA AEKRWDRVKI VCSQPYSKDS PFGLSFVRFH 150
SPPDKDEAEA PSQKVTVTKL GQFRVKEEDE SANSLRPGAL FFSRINKTSP 200
VTASDPAGPS YAAATLQASS AASSASPVSR AIGSTSKPQE SPKGKRKLDL 250
NQEEKKTPSK PPAQLSPSVP KRPKLPAPTR TPATAPVPAR AQGAVTGKPR 300
GEGTEPRRPR AGPEELGKIL QGVVVVLSGF QNPFRSELRD KALELGAKYR 350
PDWTRDSTHL ICAFANTPKY SQVLGLGGRI VRKEWVLDCH RMRRRLPSRR 400
YLMAGPGSSS EEDEASHSGG SGDEAPKLPQ KQPQTKTKPT QAAGPSSPQK 450
PPTPEETKAA SPVLQEDIDI EGVQSEGQDN GAEDSGDTED ELRRVAEQKE 500
HRLPPGQEEN GEDPYAGSTD ENTDSEEHQE PPDLPVPELP DFFQGKHFFL 550
YGEFPGDERR KLIRYVTAFN GELEDNMSDR VQFVITAQEW DPSFEEALMD 600
NPSLAFVRPR WIYSCNEKQK LLPHQLYGVV PQA 633
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:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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:
PDBe
RCSB PDB
PDBj
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...

Protein-protein interaction databases

BioGridi 113349. 39 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.
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

ArrayExpressi P18887.
Bgeei P18887.
CleanExi HS_XRCC1.
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].

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: September 3, 2014
This is version 158 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

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