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Q60596

- XRCC1_MOUSE

UniProt

Q60596 - XRCC1_MOUSE

Protein

DNA repair protein XRCC1

Gene

Xrcc1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 120 (01 Oct 2014)
      Sequence version 2 (20 Dec 2005)
      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

    GO - Biological processi

    1. base-excision repair Source: RefGenome
    2. DNA repair Source: MGI
    3. hippocampus development Source: MGI
    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

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    DNA repair protein XRCC1
    Alternative name(s):
    X-ray repair cross-complementing protein 1
    Gene namesi
    Name:Xrcc1
    Synonyms:Xrcc-1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 7

    Organism-specific databases

    MGIiMGI:99137. Xrcc1.

    Subcellular locationi

    Nucleus Curated

    GO - Cellular componenti

    1. nucleus Source: RefGenome

    Keywords - Cellular componenti

    Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 631631DNA repair protein XRCC1PRO_0000066045Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei142 – 1421PhosphoserineBy similarity
    Modified residuei200 – 2001PhosphothreonineBy similarity
    Modified residuei201 – 2011PhosphoserineBy similarity
    Modified residuei206 – 2061PhosphoserineBy similarity
    Modified residuei213 – 2131PhosphotyrosineBy similarity
    Modified residuei228 – 2281PhosphoserineBy similarity
    Modified residuei261 – 2611PhosphoserineBy similarity
    Modified residuei371 – 3711PhosphoserineBy similarity
    Modified residuei408 – 4081PhosphoserineBy similarity
    Modified residuei409 – 4091PhosphoserineBy similarity
    Modified residuei410 – 4101PhosphoserineBy similarity
    Modified residuei416 – 4161PhosphoserineBy similarity
    Modified residuei418 – 4181PhosphoserineBy similarity
    Modified residuei445 – 4451PhosphoserineBy similarity
    Modified residuei446 – 4461Phosphoserine1 Publication
    Modified residuei452 – 4521Phosphothreonine2 Publications
    Modified residuei456 – 4561PhosphothreonineBy similarity
    Modified residuei460 – 4601PhosphoserineBy similarity
    Modified residuei484 – 4841PhosphoserineBy similarity
    Modified residuei487 – 4871PhosphothreonineBy similarity
    Modified residuei517 – 5171PhosphoserineBy similarity
    Modified residuei518 – 5181PhosphothreonineBy similarity
    Modified residuei522 – 5221PhosphothreonineBy similarity

    Post-translational modificationi

    Phosphorylation of Ser-371 causes dimer dissociation. Phosphorylation by CK2 promotes interaction with APTX and APLF By similarity.By similarity
    Sumoylated.

    Keywords - PTMi

    Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ60596.
    PaxDbiQ60596.
    PRIDEiQ60596.

    PTM databases

    PhosphoSiteiQ60596.

    Expressioni

    Gene expression databases

    BgeeiQ60596.
    GenevestigatoriQ60596.

    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 By similarity.By similarity

    Protein-protein interaction databases

    BioGridi204607. 3 interactions.
    IntActiQ60596. 3 interactions.
    MINTiMINT-4140428.

    Structurei

    Secondary structure

    1
    631
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni540 – 5434
    Beta strandi545 – 5506
    Helixi556 – 56611
    Beta strandi573 – 5753
    Beta strandi581 – 5866
    Helixi590 – 5967
    Beta strandi603 – 6053
    Helixi607 – 61610
    Helixi622 – 6254

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3PC6X-ray1.90A/B535-631[»]
    3PC8X-ray2.31A/B534-631[»]
    3QVGX-ray2.26B/D531-631[»]
    ProteinModelPortaliQ60596.
    SMRiQ60596. Positions 2-155, 301-413, 536-631.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ60596.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini315 – 40389BRCT 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini536 – 62792BRCT 2PROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 2 BRCT domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiNOG295271.
    GeneTreeiENSGT00390000004140.
    HOGENOMiHOG000111006.
    HOVERGENiHBG052992.
    InParanoidiQ60596.
    KOiK10803.
    OMAiYSCNEKQ.
    OrthoDBiEOG77WWD8.
    PhylomeDBiQ60596.
    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.

    Q60596-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPEISLRHVV SCSSQDSTHC AENLLKADTY RKWRAAKAGE KTISVVLQLE    50
    KEEQIHSVDI GNDGSAFVEV LVGSSAGGAT AGEQDYEVLL VTSSFMSPSE 100
    SRSGSNPNRV RIFGPDKLVR AAAEKRWDRV KIVCSQPYSK DSPYGLSFVK 150
    FHSPPDKDEA EATSQKVTVT KLGQFRVKEE DDSANSLKPG ALFFSRINKT 200
    SSASTSDPAG PSYAAATLQA SSAASSASPV PKVVGSSSKP QEPPKGKRKL 250
    DLSLEDRKPP SKPSAGPSTL KRPKLSVPSR TPAAAPASTP AQRAVPGKPR 300
    GEGTEPRGAR TGPQELGKIL QGVVVVLSGF QNPFRSELRD KALELGAKYR 350
    PDWTPDSTHL ICAFANTPKY SQVLGLGGRI VRKEWVLDCH HMRRRLPSRR 400
    YLMAGLGSSS EDEGDSHSES GEDEAPKLPQ KRPQPKAKTQ AAGPSSPPRP 450
    PTPKETKAPS PGPQDNSDTE GEESEGRDNG AEDSGDTEDE LRRVAKQREQ 500
    RQPPAPEENG EDPYAGSTDE NTDSETPSEA DLPIPELPDF FEGKHFFLYG 550
    EFPGDERRRL IRYVTAFNGE LEDYMNERVQ FVITAQEWDP NFEEALMENP 600
    SLAFVRPRWI YSCNEKQKLL PHQLYGVVPQ A 631
    Length:631
    Mass (Da):68,971
    Last modified:December 20, 2005 - v2
    Checksum:i1A730F206E5B8879
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti28 – 281D → G in AAH85281. (PubMed:15489334)Curated
    Sequence conflicti68 – 681V → L in BAE40272. (PubMed:16141072)Curated
    Sequence conflicti108 – 1081N → S in AAH85281. (PubMed:15489334)Curated
    Sequence conflicti172 – 1721L → F in AAH85281. (PubMed:15489334)Curated
    Sequence conflicti197 – 1971I → V in AAH85281. (PubMed:15489334)Curated
    Sequence conflicti263 – 2631P → H in BAE40272. (PubMed:16141072)Curated
    Sequence conflicti295 – 2951V → I in AAA93115. (PubMed:7959765)Curated
    Sequence conflicti379 – 3791R → G in BAE40272. (PubMed:16141072)Curated
    Sequence conflicti391 – 3911H → R in AAA93115. (PubMed:7959765)Curated
    Sequence conflicti582 – 5821V → A in AAH85281. (PubMed:15489334)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U02887 mRNA. Translation: AAA93115.1.
    AK168334 mRNA. Translation: BAE40272.1.
    BC055900 mRNA. Translation: AAH55900.1.
    BC085281 mRNA. Translation: AAH85281.1.
    CCDSiCCDS20955.1.
    PIRiA54659.
    RefSeqiNP_033558.3. NM_009532.4.
    XP_006539800.1. XM_006539737.1.
    UniGeneiMm.4347.

    Genome annotation databases

    EnsembliENSMUST00000063249; ENSMUSP00000070995; ENSMUSG00000051768.
    GeneIDi22594.
    KEGGimmu:22594.
    UCSCiuc009fpx.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U02887 mRNA. Translation: AAA93115.1 .
    AK168334 mRNA. Translation: BAE40272.1 .
    BC055900 mRNA. Translation: AAH55900.1 .
    BC085281 mRNA. Translation: AAH85281.1 .
    CCDSi CCDS20955.1.
    PIRi A54659.
    RefSeqi NP_033558.3. NM_009532.4.
    XP_006539800.1. XM_006539737.1.
    UniGenei Mm.4347.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3PC6 X-ray 1.90 A/B 535-631 [» ]
    3PC8 X-ray 2.31 A/B 534-631 [» ]
    3QVG X-ray 2.26 B/D 531-631 [» ]
    ProteinModelPortali Q60596.
    SMRi Q60596. Positions 2-155, 301-413, 536-631.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 204607. 3 interactions.
    IntActi Q60596. 3 interactions.
    MINTi MINT-4140428.

    PTM databases

    PhosphoSitei Q60596.

    Proteomic databases

    MaxQBi Q60596.
    PaxDbi Q60596.
    PRIDEi Q60596.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000063249 ; ENSMUSP00000070995 ; ENSMUSG00000051768 .
    GeneIDi 22594.
    KEGGi mmu:22594.
    UCSCi uc009fpx.2. mouse.

    Organism-specific databases

    CTDi 7515.
    MGIi MGI:99137. Xrcc1.

    Phylogenomic databases

    eggNOGi NOG295271.
    GeneTreei ENSGT00390000004140.
    HOGENOMi HOG000111006.
    HOVERGENi HBG052992.
    InParanoidi Q60596.
    KOi K10803.
    OMAi YSCNEKQ.
    OrthoDBi EOG77WWD8.
    PhylomeDBi Q60596.
    TreeFami TF101201.

    Miscellaneous databases

    EvolutionaryTracei Q60596.
    NextBioi 302941.
    PROi Q60596.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q60596.
    Genevestigatori Q60596.

    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. "Isolation and characterization of mouse Xrcc-1, a DNA repair gene affecting ligation."
      Brookman K.W., Tebbs R.S., Allen S.A., Tucker J.D., Swiger R.R., Lamerdin J.E., Carrano A.V., Thompson L.H.
      Genomics 22:180-188(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Brain.
    2. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: DBA/2.
    3. "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].
      Strain: C57BL/6J and FVB/N.
      Tissue: Colon and Egg.
    4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-452, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    5. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
      Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
      Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-446 AND THR-452, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.

    Entry informationi

    Entry nameiXRCC1_MOUSE
    AccessioniPrimary (citable) accession number: Q60596
    Secondary accession number(s): Q3THC5, Q5U435, Q7TNQ5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: December 20, 2005
    Last modified: October 1, 2014
    This is version 120 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3