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Protein

DNA repair protein XRCC1

Gene

Xrcc1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: 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
  2. enzyme binding Source: MGI

GO - Biological processi

  1. base-excision repair Source: GO_Central
  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
Complete GO annotation...

Keywords - Biological processi

DNA damage, DNA repair

Enzyme and pathway databases

ReactomeiREACT_352300. Resolution of AP sites via the single-nucleotide replacement pathway.

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 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:99137. Xrcc1.

Subcellular locationi

Nucleus Curated

GO - Cellular componenti

  1. nucleoplasm Source: MGI
  2. nucleus Source: MGI
Complete GO annotation...

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. 4 interactions.
IntActiQ60596. 3 interactions.
MINTiMINT-4140428.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
OMAiCNEKQKL.
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

        10         20         30         40         50
MPEISLRHVV SCSSQDSTHC AENLLKADTY RKWRAAKAGE KTISVVLQLE
60 70 80 90 100
KEEQIHSVDI GNDGSAFVEV LVGSSAGGAT AGEQDYEVLL VTSSFMSPSE
110 120 130 140 150
SRSGSNPNRV RIFGPDKLVR AAAEKRWDRV KIVCSQPYSK DSPYGLSFVK
160 170 180 190 200
FHSPPDKDEA EATSQKVTVT KLGQFRVKEE DDSANSLKPG ALFFSRINKT
210 220 230 240 250
SSASTSDPAG PSYAAATLQA SSAASSASPV PKVVGSSSKP QEPPKGKRKL
260 270 280 290 300
DLSLEDRKPP SKPSAGPSTL KRPKLSVPSR TPAAAPASTP AQRAVPGKPR
310 320 330 340 350
GEGTEPRGAR TGPQELGKIL QGVVVVLSGF QNPFRSELRD KALELGAKYR
360 370 380 390 400
PDWTPDSTHL ICAFANTPKY SQVLGLGGRI VRKEWVLDCH HMRRRLPSRR
410 420 430 440 450
YLMAGLGSSS EDEGDSHSES GEDEAPKLPQ KRPQPKAKTQ AAGPSSPPRP
460 470 480 490 500
PTPKETKAPS PGPQDNSDTE GEESEGRDNG AEDSGDTEDE LRRVAKQREQ
510 520 530 540 550
RQPPAPEENG EDPYAGSTDE NTDSETPSEA DLPIPELPDF FEGKHFFLYG
560 570 580 590 600
EFPGDERRRL IRYVTAFNGE LEDYMNERVQ FVITAQEWDP NFEEALMENP
610 620 630
SLAFVRPRWI YSCNEKQKLL PHQLYGVVPQ A
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:
EMBLi
GenBanki
DDBJi
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_006539737.2.
UniGeneiMm.4347.

Genome annotation databases

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

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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_006539737.2.
UniGeneiMm.4347.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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...

Protein-protein interaction databases

BioGridi204607. 4 interactions.
IntActiQ60596. 3 interactions.
MINTiMINT-4140428.

PTM databases

PhosphoSiteiQ60596.

Proteomic databases

MaxQBiQ60596.
PaxDbiQ60596.
PRIDEiQ60596.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi7515.
MGIiMGI:99137. Xrcc1.

Phylogenomic databases

eggNOGiNOG295271.
GeneTreeiENSGT00390000004140.
HOGENOMiHOG000111006.
HOVERGENiHBG052992.
InParanoidiQ60596.
KOiK10803.
OMAiCNEKQKL.
OrthoDBiEOG77WWD8.
PhylomeDBiQ60596.
TreeFamiTF101201.

Enzyme and pathway databases

ReactomeiREACT_352300. Resolution of AP sites via the single-nucleotide replacement pathway.

Miscellaneous databases

EvolutionaryTraceiQ60596.
NextBioi302941.
PROiQ60596.
SOURCEiSearch...

Gene expression databases

BgeeiQ60596.
GenevestigatoriQ60596.

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]
ProtoNetiSearch...

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(1993) [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(2004) [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(2003) [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(2008) [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: April 1, 2015
This is version 125 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.