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P18887

- XRCC1_HUMAN

UniProt

P18887 - XRCC1_HUMAN

Protein

DNA repair protein XRCC1

Gene

XRCC1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 159 (01 Oct 2014)
      Sequence version 2 (11 Jan 2011)
      Previous versions | rss
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    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

    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

    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 1 Publication
    Note: Accumulates at sites of DNA damage.

    GO - Cellular componenti

    1. nucleoplasm Source: Reactome
    2. nucleus Source: HPA

    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

    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 APEX1.9 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. 39 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 – 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.
    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.
    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

    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...
    MobiDBi 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

    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

    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: October 1, 2014
    This is version 159 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

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