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Q60596 (XRCC1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 118. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
DNA repair protein XRCC1
Alternative name(s):
X-ray repair cross-complementing protein 1
Gene names
Name:Xrcc1
Synonyms:Xrcc-1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length631 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Subunit structure

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.

Subcellular location

Nucleus Probable.

Post-translational modification

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

Sumoylated.

Sequence similarities

Contains 2 BRCT domains.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 631631DNA repair protein XRCC1
PRO_0000066045

Regions

Domain315 – 40389BRCT 1
Domain536 – 62792BRCT 2

Amino acid modifications

Modified residue1421Phosphoserine By similarity
Modified residue2001Phosphothreonine By similarity
Modified residue2011Phosphoserine By similarity
Modified residue2061Phosphoserine By similarity
Modified residue2131Phosphotyrosine By similarity
Modified residue2281Phosphoserine By similarity
Modified residue2611Phosphoserine By similarity
Modified residue3711Phosphoserine By similarity
Modified residue4081Phosphoserine By similarity
Modified residue4091Phosphoserine By similarity
Modified residue4101Phosphoserine By similarity
Modified residue4161Phosphoserine By similarity
Modified residue4181Phosphoserine By similarity
Modified residue4451Phosphoserine By similarity
Modified residue4461Phosphoserine Ref.5
Modified residue4521Phosphothreonine Ref.4 Ref.5
Modified residue4561Phosphothreonine By similarity
Modified residue4601Phosphoserine By similarity
Modified residue4841Phosphoserine By similarity
Modified residue4871Phosphothreonine By similarity
Modified residue5171Phosphoserine By similarity
Modified residue5181Phosphothreonine By similarity
Modified residue5221Phosphothreonine By similarity

Experimental info

Sequence conflict281D → G in AAH85281. Ref.3
Sequence conflict681V → L in BAE40272. Ref.2
Sequence conflict1081N → S in AAH85281. Ref.3
Sequence conflict1721L → F in AAH85281. Ref.3
Sequence conflict1971I → V in AAH85281. Ref.3
Sequence conflict2631P → H in BAE40272. Ref.2
Sequence conflict2951V → I in AAA93115. Ref.1
Sequence conflict3791R → G in BAE40272. Ref.2
Sequence conflict3911H → R in AAA93115. Ref.1
Sequence conflict5821V → A in AAH85281. Ref.3

Secondary structure

................... 631
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q60596 [UniParc].

Last modified December 20, 2005. Version 2.
Checksum: 1A730F206E5B8879

FASTA63168,971
        10         20         30         40         50         60 
MPEISLRHVV SCSSQDSTHC AENLLKADTY RKWRAAKAGE KTISVVLQLE KEEQIHSVDI 

        70         80         90        100        110        120 
GNDGSAFVEV LVGSSAGGAT AGEQDYEVLL VTSSFMSPSE SRSGSNPNRV RIFGPDKLVR 

       130        140        150        160        170        180 
AAAEKRWDRV KIVCSQPYSK DSPYGLSFVK FHSPPDKDEA EATSQKVTVT KLGQFRVKEE 

       190        200        210        220        230        240 
DDSANSLKPG ALFFSRINKT SSASTSDPAG PSYAAATLQA SSAASSASPV PKVVGSSSKP 

       250        260        270        280        290        300 
QEPPKGKRKL DLSLEDRKPP SKPSAGPSTL KRPKLSVPSR TPAAAPASTP AQRAVPGKPR 

       310        320        330        340        350        360 
GEGTEPRGAR TGPQELGKIL QGVVVVLSGF QNPFRSELRD KALELGAKYR PDWTPDSTHL 

       370        380        390        400        410        420 
ICAFANTPKY SQVLGLGGRI VRKEWVLDCH HMRRRLPSRR YLMAGLGSSS EDEGDSHSES 

       430        440        450        460        470        480 
GEDEAPKLPQ KRPQPKAKTQ AAGPSSPPRP PTPKETKAPS PGPQDNSDTE GEESEGRDNG 

       490        500        510        520        530        540 
AEDSGDTEDE LRRVAKQREQ RQPPAPEENG EDPYAGSTDE NTDSETPSEA DLPIPELPDF 

       550        560        570        580        590        600 
FEGKHFFLYG EFPGDERRRL IRYVTAFNGE LEDYMNERVQ FVITAQEWDP NFEEALMENP 

       610        620        630 
SLAFVRPRWI YSCNEKQKLL PHQLYGVVPQ A 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U02887 mRNA. Translation: AAA93115.1.
AK168334 mRNA. Translation: BAE40272.1.
BC055900 mRNA. Translation: AAH55900.1.
BC085281 mRNA. Translation: AAH85281.1.
CCDSCCDS20955.1.
PIRA54659.
RefSeqNP_033558.3. NM_009532.4.
XP_006539800.1. XM_006539737.1.
UniGeneMm.4347.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3PC6X-ray1.90A/B535-631[»]
3PC8X-ray2.31A/B534-631[»]
3QVGX-ray2.26B/D531-631[»]
ProteinModelPortalQ60596.
SMRQ60596. Positions 2-155, 301-413, 536-631.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid204607. 3 interactions.
IntActQ60596. 3 interactions.
MINTMINT-4140428.

PTM databases

PhosphoSiteQ60596.

Proteomic databases

MaxQBQ60596.
PaxDbQ60596.
PRIDEQ60596.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000063249; ENSMUSP00000070995; ENSMUSG00000051768.
GeneID22594.
KEGGmmu:22594.
UCSCuc009fpx.2. mouse.

Organism-specific databases

CTD7515.
MGIMGI:99137. Xrcc1.

Phylogenomic databases

eggNOGNOG295271.
GeneTreeENSGT00390000004140.
HOGENOMHOG000111006.
HOVERGENHBG052992.
InParanoidQ60596.
KOK10803.
OMAYSCNEKQ.
OrthoDBEOG77WWD8.
PhylomeDBQ60596.
TreeFamTF101201.

Gene expression databases

BgeeQ60596.
GenevestigatorQ60596.

Family and domain databases

Gene3D2.60.120.260. 1 hit.
3.40.50.10190. 2 hits.
InterProIPR001357. BRCT_dom.
IPR008979. Galactose-bd-like.
IPR002706. Xrcc1_N.
[Graphical view]
PfamPF00533. BRCT. 2 hits.
PF01834. XRCC1_N. 1 hit.
[Graphical view]
SMARTSM00292. BRCT. 2 hits.
[Graphical view]
SUPFAMSSF49785. SSF49785. 1 hit.
SSF52113. SSF52113. 2 hits.
PROSITEPS50172. BRCT. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ60596.
NextBio302941.
PROQ60596.
SOURCESearch...

Entry information

Entry nameXRCC1_MOUSE
AccessionPrimary (citable) accession number: Q60596
Secondary accession number(s): Q3THC5, Q5U435, Q7TNQ5
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: December 20, 2005
Last modified: July 9, 2014
This is version 118 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot