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Protein

DNA repair protein XRCC3

Gene

Xrcc3

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

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).By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi107 – 1148ATPSequence Analysis

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. crossover junction endodeoxyribonuclease activity Source: Ensembl
  3. DNA-dependent ATPase activity Source: InterPro
  4. four-way junction DNA binding Source: Ensembl

GO - Biological processi

  1. DNA catabolic process, endonucleolytic Source: MGI
  2. DNA repair Source: MGI
  3. double-strand break repair via homologous recombination Source: UniProtKB
  4. positive regulation of mitotic cell cycle spindle assembly checkpoint Source: UniProtKB
  5. regulation of centrosome duplication Source: UniProtKB
  6. resolution of mitotic recombination intermediates Source: UniProtKB
  7. response to organic substance Source: Ensembl
Complete GO annotation...

Keywords - Biological processi

DNA damage, DNA recombination, DNA repair

Keywords - Ligandi

ATP-binding, DNA-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
DNA repair protein XRCC3
Alternative name(s):
X-ray repair cross-complementing protein 3
Gene namesi
Name:Xrcc3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 12

Organism-specific databases

MGIiMGI:1921585. Xrcc3.

Subcellular locationi

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

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. mitochondrial matrix Source: UniProtKB-SubCell
  3. mitochondrion Source: MGI
  4. nucleus Source: UniProtKB
  5. perinuclear region of cytoplasm Source: UniProtKB
  6. Rad51C-XRCC3 complex Source: UniProtKB
  7. replication fork Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Mitochondrion, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 349349DNA repair protein XRCC3PRO_0000122952Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiQ9CXE6.
PRIDEiQ9CXE6.

PTM databases

PhosphoSiteiQ9CXE6.

Expressioni

Gene expression databases

BgeeiQ9CXE6.
ExpressionAtlasiQ9CXE6. baseline and differential.
GenevestigatoriQ9CXE6.

Interactioni

Subunit structurei

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).By similarity

Protein-protein interaction databases

IntActiQ9CXE6. 1 interaction.
MINTiMINT-4140445.

Structurei

3D structure databases

ProteinModelPortaliQ9CXE6.
SMRiQ9CXE6. Positions 26-341.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the RecA family. RAD51 subfamily.Curated

Phylogenomic databases

eggNOGiCOG0468.
GeneTreeiENSGT00770000120668.
HOGENOMiHOG000239162.
HOVERGENiHBG054179.
InParanoidiQ9CXE6.
KOiK10880.
OMAiLLMRLMV.
PhylomeDBiQ9CXE6.
TreeFamiTF101203.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR013632. DNA_recomb/repair_Rad51_C.
IPR016467. DNA_recomb/repair_RecA-like.
IPR027417. P-loop_NTPase.
IPR020588. RecA_ATP-bd.
[Graphical view]
PfamiPF08423. Rad51. 1 hit.
[Graphical view]
PIRSFiPIRSF005856. Rad51. 1 hit.
SUPFAMiSSF52540. SSF52540. 1 hit.
PROSITEiPS50162. RECA_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9CXE6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDLDQLDLNP RITAAVKRGR LKSVKEILCY SGPDLQRLTG LPSHDVQCLL
60 70 80 90 100
RAASLHLRGS RVLSALHLFQ QKESFPEQHQ RLSLGCPVLD QFLGGGLPLE
110 120 130 140 150
GITGLAGCSS AGKTQLALQL CLAVQFPRQY GGLEAGAVYI CTEDAFPSKR
160 170 180 190 200
LWQLIAQQRR LRTDAPEELI EKIRFSNHIF IEHAADVDTL LECVSKKVPI
210 220 230 240 250
LLSRGMARLV VVDSIAAPFR CEFHLQASAI RAKLLLSLGA TLRRLSSTFR
260 270 280 290 300
SPVLCINQVT DMVEDQQSVS RSLGASEERL SPALGITWAN QLLMRLMVDR
310 320 330 340
THEDDVTTGL PRSPVRTLRV LFAPHLPLSS CCYTVSGEGI RGMPGTQSY
Length:349
Mass (Da):38,446
Last modified:May 31, 2001 - v1
Checksum:i15E5AFBBDEB9AAEB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK014491 mRNA. Translation: BAB29391.1.
CCDSiCCDS26187.1.
RefSeqiNP_083151.1. NM_028875.2.
XP_006516362.1. XM_006516299.1.
UniGeneiMm.19082.

Genome annotation databases

EnsembliENSMUST00000021715; ENSMUSP00000021715; ENSMUSG00000021287.
GeneIDi74335.
KEGGimmu:74335.
UCSCiuc007pdz.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK014491 mRNA. Translation: BAB29391.1.
CCDSiCCDS26187.1.
RefSeqiNP_083151.1. NM_028875.2.
XP_006516362.1. XM_006516299.1.
UniGeneiMm.19082.

3D structure databases

ProteinModelPortaliQ9CXE6.
SMRiQ9CXE6. Positions 26-341.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9CXE6. 1 interaction.
MINTiMINT-4140445.

PTM databases

PhosphoSiteiQ9CXE6.

Proteomic databases

PaxDbiQ9CXE6.
PRIDEiQ9CXE6.

Protocols and materials databases

DNASUi74335.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000021715; ENSMUSP00000021715; ENSMUSG00000021287.
GeneIDi74335.
KEGGimmu:74335.
UCSCiuc007pdz.1. mouse.

Organism-specific databases

CTDi7517.
MGIiMGI:1921585. Xrcc3.

Phylogenomic databases

eggNOGiCOG0468.
GeneTreeiENSGT00770000120668.
HOGENOMiHOG000239162.
HOVERGENiHBG054179.
InParanoidiQ9CXE6.
KOiK10880.
OMAiLLMRLMV.
PhylomeDBiQ9CXE6.
TreeFamiTF101203.

Miscellaneous databases

NextBioi340475.
PROiQ9CXE6.
SOURCEiSearch...

Gene expression databases

BgeeiQ9CXE6.
ExpressionAtlasiQ9CXE6. baseline and differential.
GenevestigatoriQ9CXE6.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR013632. DNA_recomb/repair_Rad51_C.
IPR016467. DNA_recomb/repair_RecA-like.
IPR027417. P-loop_NTPase.
IPR020588. RecA_ATP-bd.
[Graphical view]
PfamiPF08423. Rad51. 1 hit.
[Graphical view]
PIRSFiPIRSF005856. Rad51. 1 hit.
SUPFAMiSSF52540. SSF52540. 1 hit.
PROSITEiPS50162. RECA_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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.
    , 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: C57BL/6J.
    Tissue: Embryonic liver.

Entry informationi

Entry nameiXRCC3_MOUSE
AccessioniPrimary (citable) accession number: Q9CXE6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 2, 2002
Last sequence update: May 31, 2001
Last modified: March 3, 2015
This is version 97 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.