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Q9CXE6 (XRCC3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 91. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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 XRCC3
Alternative name(s):
X-ray repair cross-complementing protein 3
Gene names
Name:Xrcc3
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length349 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Involved in the homologous recombination repair (HRR) pathway of double-stranded DNA, thought to repair chromosomal fragmentation, translocations and deletions. Part of the RAD21 paralog protein complex CX3 which acts in the BRCA1-BRCA2-dependent HR pathway. Upon DNA damage, CX3 acts downstream of RAD51 recruitment; the complex binds predominantly to the intersection of the four duplex arms of the Holliday junction (HJ) and to junctions of replication forks. Involved in HJ resolution and thus in processing HR intermediates late in the DNA repair process; the function may be linked to the CX3 complex and seems to involve GEN1 during mitotic cell cycle progression. Part of a PALB2-scaffolded HR complex containing BRCA2 and RAD51C and which is thought to play a role in DNA repair by HR. Plays a role in regulating mitochondrial DNA copy number under conditions of oxidative stress in the presence of RAD51 and RAD51C By similarity.

Subunit structure

Interacts with RAD51C and RAD51. Part of the CX3 complex consisting of RAD51C and XRCC3; the complex has a ring-like structure arranged into a flat disc around a central channel; CX3 can interact with RAD51 in vitro. Forms a complex with FANCD2, BRCA2 and phosphorylated FANCG. Interacts with SWSAP1 and ZSWIM7; involved in homologous recombination repair. Interacts directly with PALB2 which may serve as a scaffold for a HR complex containing PALB2, BRCA2, RAD51C, RAD51 and XRCC3 By similarity.

Subcellular location

Nucleus By similarity. Cytoplasm By similarity. Cytoplasmperinuclear region By similarity. Mitochondrion matrix By similarity. Note: Accumulates in discrete nuclear foci prior to DNA damage, and these foci persist throughout the time course of DNA repair By similarity.

Sequence similarities

Belongs to the RecA family. RAD51 subfamily.

Ontologies

Keywords
   Biological processDNA damage
DNA recombination
DNA repair
   Cellular componentCytoplasm
Mitochondrion
Nucleus
   LigandATP-binding
DNA-binding
Nucleotide-binding
   PTMAcetylation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processdouble-strand break repair via homologous recombination

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of mitotic cell cycle spindle assembly checkpoint

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of centrosome duplication

Inferred from sequence or structural similarity. Source: UniProtKB

resolution of mitotic recombination intermediates

Inferred from sequence or structural similarity. Source: UniProtKB

response to organic substance

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentRad51C-XRCC3 complex

Inferred from sequence or structural similarity. Source: UniProtKB

cytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

mitochondrial matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

perinuclear region of cytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

replication fork

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

DNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

DNA-dependent ATPase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 349349DNA repair protein XRCC3
PRO_0000122952

Regions

Nucleotide binding107 – 1148ATP Potential

Amino acid modifications

Modified residue11N-acetylmethionine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9CXE6 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 15E5AFBBDEB9AAEB

FASTA34938,446
        10         20         30         40         50         60 
MDLDQLDLNP RITAAVKRGR LKSVKEILCY SGPDLQRLTG LPSHDVQCLL RAASLHLRGS 

        70         80         90        100        110        120 
RVLSALHLFQ QKESFPEQHQ RLSLGCPVLD QFLGGGLPLE GITGLAGCSS AGKTQLALQL 

       130        140        150        160        170        180 
CLAVQFPRQY GGLEAGAVYI CTEDAFPSKR LWQLIAQQRR LRTDAPEELI EKIRFSNHIF 

       190        200        210        220        230        240 
IEHAADVDTL LECVSKKVPI LLSRGMARLV VVDSIAAPFR CEFHLQASAI RAKLLLSLGA 

       250        260        270        280        290        300 
TLRRLSSTFR SPVLCINQVT DMVEDQQSVS RSLGASEERL SPALGITWAN QLLMRLMVDR 

       310        320        330        340 
THEDDVTTGL PRSPVRTLRV LFAPHLPLSS CCYTVSGEGI RGMPGTQSY 

« Hide

References

[1]"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: C57BL/6J.
Tissue: Embryonic liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK014491 mRNA. Translation: BAB29391.1.
CCDSCCDS26187.1.
RefSeqNP_083151.1. NM_028875.2.
XP_006516362.1. XM_006516299.1.
UniGeneMm.19082.

3D structure databases

ProteinModelPortalQ9CXE6.
SMRQ9CXE6. Positions 26-341.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ9CXE6. 1 interaction.
MINTMINT-4140445.

PTM databases

PhosphoSiteQ9CXE6.

Proteomic databases

PaxDbQ9CXE6.
PRIDEQ9CXE6.

Protocols and materials databases

DNASU74335.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000021715; ENSMUSP00000021715; ENSMUSG00000021287.
GeneID74335.
KEGGmmu:74335.
UCSCuc007pdz.1. mouse.

Organism-specific databases

CTD7517.
MGIMGI:1921585. Xrcc3.

Phylogenomic databases

eggNOGCOG0468.
GeneTreeENSGT00710000106840.
HOGENOMHOG000239162.
HOVERGENHBG054179.
InParanoidQ9CXE6.
KOK10880.
OMALLMRLMV.
PhylomeDBQ9CXE6.
TreeFamTF101203.

Gene expression databases

BgeeQ9CXE6.
GenevestigatorQ9CXE6.

Family and domain databases

Gene3D3.40.50.300. 1 hit.
InterProIPR013632. DNA_recomb/repair_Rad51_C.
IPR016467. DNA_recomb/repair_RecA-like.
IPR027417. P-loop_NTPase.
IPR020588. RecA_ATP-bd.
[Graphical view]
PfamPF08423. Rad51. 1 hit.
[Graphical view]
PIRSFPIRSF005856. Rad51. 1 hit.
SUPFAMSSF52540. SSF52540. 1 hit.
PROSITEPS50162. RECA_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio340475.
PROQ9CXE6.
SOURCESearch...

Entry information

Entry nameXRCC3_MOUSE
AccessionPrimary (citable) accession number: Q9CXE6
Entry history
Integrated into UniProtKB/Swiss-Prot: April 3, 2002
Last sequence update: June 1, 2001
Last modified: July 9, 2014
This is version 91 of the entry and version 1 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

MGD cross-references

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