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Q60596

- XRCC1_MOUSE

UniProt

Q60596 - XRCC1_MOUSE

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Protein
DNA repair protein XRCC1
Gene
Xrcc1, Xrcc-1
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 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

GO - Biological processi

  1. DNA repair Source: MGI
  2. base-excision repair Source: RefGenome
  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
Complete GO annotation...

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 Inferred

GO - Cellular componenti

  1. nucleus Source: RefGenome
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 631631DNA repair protein XRCC1
PRO_0000066045Add
BLAST

Amino acid modifications

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

Post-translational modificationi

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

Protein-protein interaction databases

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

Structurei

Secondary structure

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.

Miscellaneous databases

EvolutionaryTraceiQ60596.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini315 – 40389BRCT 1
Add
BLAST
Domaini536 – 62792BRCT 2
Add
BLAST

Sequence similaritiesi

Contains 2 BRCT domains.

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti28 – 281D → G in AAH85281. 1 Publication
Sequence conflicti68 – 681V → L in BAE40272. 1 Publication
Sequence conflicti108 – 1081N → S in AAH85281. 1 Publication
Sequence conflicti172 – 1721L → F in AAH85281. 1 Publication
Sequence conflicti197 – 1971I → V in AAH85281. 1 Publication
Sequence conflicti263 – 2631P → H in BAE40272. 1 Publication
Sequence conflicti295 – 2951V → I in AAA93115. 1 Publication
Sequence conflicti379 – 3791R → G in BAE40272. 1 Publication
Sequence conflicti391 – 3911H → R in AAA93115. 1 Publication
Sequence conflicti582 – 5821V → A in AAH85281. 1 Publication

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 119 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

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