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O43543 (XRCC2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 110. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
DNA repair protein XRCC2
Alternative name(s):
X-ray repair cross-complementing protein 2
Gene names
Name:XRCC2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length280 AA.
Sequence statusComplete.
Protein existenceEvidence at protein 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 BCDX2 which acts in the BRCA1-BRCA2-dependent HR pathway. Upon DNA damage, BCDX2 acts downstream of BRCA2 recruitment and upstream of RAD51 recruitment. BCDX2 binds predominantly to the intersection of the four duplex arms of the Holliday junction and to junction of replication forks. The BCDX2 complex was originally reported to bind single-stranded DNA, single-stranded gaps in duplex DNA and specifically to nicks in duplex DNA. Ref.8 Ref.10 Ref.14 Ref.15

Subunit structure

Interacts with RAD51D. Part of the BCDX2 complex consisting of RAD51B, RAD51C, RAD51D and XRCC2; the complex has a ring-like structure arranged into a flat disc around a central channel. In the absence of DNA, the BCDX2 subcomplex XRCC2:RAD51D formed a multimeric ring structure; in the presence of single-stranded DNA it formed a filamentous structure with the ssDNA. Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13

Subcellular location

Nucleus. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome Ref.14.

Sequence similarities

Belongs to the RecA family. RAD51 subfamily.

Ontologies

Keywords
   Biological processDNA damage
DNA recombination
DNA repair
   Cellular componentCytoplasm
Cytoskeleton
Nucleus
   Coding sequence diversityPolymorphism
   LigandDNA-binding
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA repair

Inferred from genetic interaction PubMed 10422536. Source: BHF-UCL

centrosome organization

Inferred from mutant phenotype Ref.14. Source: UniProtKB

double-strand break repair via homologous recombination

Inferred from mutant phenotype Ref.15. Source: UniProtKB

in utero embryonic development

Inferred from electronic annotation. Source: Ensembl

meiotic nuclear division

Traceable author statement Ref.3. Source: ProtInc

mitotic cell cycle

Inferred from mutant phenotype Ref.14. Source: UniProtKB

negative regulation of neuron apoptotic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of neurogenesis

Inferred from electronic annotation. Source: Ensembl

response to X-ray

Inferred from electronic annotation. Source: Ensembl

response to gamma radiation

Inferred from electronic annotation. Source: Ensembl

strand invasion

Inferred from direct assay Ref.10. Source: UniProtKB

   Cellular_componentRad51B-Rad51C-Rad51D-XRCC2 complex

Inferred from direct assay Ref.8. Source: UniProtKB

centrosome

Inferred from direct assay Ref.14. Source: UniProtKB

replication fork

Inferred from direct assay Ref.16. Source: UniProtKB

   Molecular_functionATP binding

Inferred from electronic annotation. Source: InterPro

DNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

DNA-dependent ATPase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

RAD51DO757712EBI-3918457,EBI-1055693

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 280280DNA repair protein XRCC2
PRO_0000122948

Natural variations

Natural variant161A → S.
Corresponds to variant rs4987090 [ dbSNP | Ensembl ].
VAR_020403
Natural variant1881R → H. Ref.4
Corresponds to variant rs3218536 [ dbSNP | Ensembl ].
VAR_020404
Natural variant2211I → T. Ref.4
Corresponds to variant rs3218537 [ dbSNP | Ensembl ].
VAR_029294

Sequences

Sequence LengthMass (Da)Tools
O43543 [UniParc].

Last modified June 1, 1998. Version 1.
Checksum: 5656277E74C06074

FASTA28031,956
        10         20         30         40         50         60 
MCSAFHRAES GTELLARLEG RSSLKEIEPN LFADEDSPVH GDILEFHGPE GTGKTEMLYH 

        70         80         90        100        110        120 
LTARCILPKS EGGLEVEVLF IDTDYHFDML RLVTILEHRL SQSSEEIIKY CLGRFFLVYC 

       130        140        150        160        170        180 
SSSTHLLLTL YSLESMFCSH PSLCLLILDS LSAFYWIDRV NGGESVNLQE STLRKCSQCL 

       190        200        210        220        230        240 
EKLVNDYRLV LFATTQTIMQ KASSSSEEPS HASRRLCDVD IDYRPYLCKA WQQLVKHRMF 

       250        260        270        280 
FSKQDDSQSS NQFSLVSRCL KSNSLKKHFF IIGESGVEFC 

« Hide

References

« Hide 'large scale' references
[1]"XRCC2 and XRCC3, new human Rad51-family members, promote chromosome stability and protect against DNA cross-links and other damages."
Liu N., Lamerdin J.E., Tebbs R.S., Schild D., Tucker J.D., Shen M.R., Brookman K.W., Siciliano M.J., Walter C.A., Fan W., Narayana L.S., Zhou Z.-Q., Adamson A.W., Sorensen K.J., Chen D.J., Jones N.J., Thompson L.H.
Mol. Cell 1:783-793(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
Tissue: Cervix carcinoma.
[2]"The XRCC2 DNA repair gene: identification of a positional candidate."
Tambini C.E., George A.M., Rommens J.M., Tsui L.-C., Scherer S.W., Thacker J.
Genomics 41:84-92(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"The XRCC2 DNA repair gene from human and mouse encodes a novel member of the recA/RAD51 family."
Cartwright R., Tambini C.E., Simpson P.J., Thacker J.
Nucleic Acids Res. 26:3084-3089(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
Tissue: Cervix carcinoma.
[4]NIEHS SNPs program
Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS HIS-188 AND THR-221.
[5]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Testis.
[6]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"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].
Tissue: Brain.
[8]"Identification and purification of two distinct complexes containing the five RAD51 paralogs."
Masson J.Y., Tarsounas M.C., Stasiak A.Z., Stasiak A., Shah R., McIlwraith M.J., Benson F.E., West S.C.
Genes Dev. 15:3296-3307(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, IDENTIFICATION IN THE BCDX2 COMPLEX WITH RAD51C; RAD51D AND XRCC2.
[9]"RAD51C interacts with RAD51B and is central to a larger protein complex in vivo exclusive of RAD51."
Miller K.A., Yoshikawa D.M., McConnell I.R., Clark R., Schild D., Albala J.S.
J. Biol. Chem. 277:8406-8411(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT.
[10]"Homologous pairing and ring and filament structure formation activities of the human Xrcc2*Rad51D complex."
Kurumizaka H., Ikawa S., Nakada M., Enomoto R., Kagawa W., Kinebuchi T., Yamazoe M., Yokoyama S., Shibata T.
J. Biol. Chem. 277:14315-14320(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBUNIT.
[11]"Interactions involving the Rad51 paralogs Rad51C and XRCC3 in human cells."
Wiese C., Collins D.W., Albala J.S., Thompson L.H., Kronenberg A., Schild D.
Nucleic Acids Res. 30:1001-1008(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A COMPLEX WITH RAD51B; RAD51C AND RAD51D.
[12]"Involvement of Rad51C in two distinct protein complexes of Rad51 paralogs in human cells."
Liu N., Schild D., Thelen M.P., Thompson L.H.
Nucleic Acids Res. 30:1009-1015(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A COMPLEX WITH RAD51B; RAD51C AND RAD51D.
[13]"Domain mapping of the Rad51 paralog protein complexes."
Miller K.A., Sawicka D., Barsky D., Albala J.S.
Nucleic Acids Res. 32:169-178(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RAD51D.
[14]"Homologous recombination proteins are associated with centrosomes and are required for mitotic stability."
Cappelli E., Townsend S., Griffin C., Thacker J.
Exp. Cell Res. 317:1203-1213(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[15]"Rad51 paralog complexes BCDX2 and CX3 act at different stages in the BRCA1-BRCA2-dependent homologous recombination pathway."
Chun J., Buechelmaier E.S., Powell S.N.
Mol. Cell. Biol. 33:387-395(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION OF THE BCDX2 COMPLEX.
[16]"Ring-shaped Rad51 paralog protein complexes bind Holliday junctions and replication forks as visualized by electron microscopy."
Compton S.A., Ozgur S., Griffith J.D.
J. Biol. Chem. 285:13349-13356(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: ELECTRON MICROSCOPY OF THE BCDX2 COMPLEX, DNA-BINDING OF THE BCDX2 COMPLEX.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF035587 mRNA. Translation: AAC05369.1.
AC003109 Genomic DNA. Translation: AAC05802.1.
Y08837 mRNA. Translation: CAA70065.1.
Y17033 Genomic DNA. Translation: CAA76597.1.
AF520762 Genomic DNA. Translation: AAM55241.1.
AK313607 mRNA. Translation: BAG36372.1.
CH471173 Genomic DNA. Translation: EAW53968.1.
BC042137 mRNA. Translation: AAH42137.1.
RefSeqNP_005422.1. NM_005431.1.
UniGeneHs.647093.

3D structure databases

ProteinModelPortalO43543.
SMRO43543. Positions 9-196.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113350. 9 interactions.
DIPDIP-24242N.
IntActO43543. 5 interactions.
MINTMINT-137755.
STRING9606.ENSP00000352271.

PTM databases

PhosphoSiteO43543.

Proteomic databases

PaxDbO43543.
PRIDEO43543.

Protocols and materials databases

DNASU7516.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000359321; ENSP00000352271; ENSG00000196584.
GeneID7516.
KEGGhsa:7516.
UCSCuc003wld.3. human.

Organism-specific databases

CTD7516.
GeneCardsGC07M152341.
HGNCHGNC:12829. XRCC2.
MIM600375. gene.
neXtProtNX_O43543.
Orphanet227535. Hereditary breast cancer.
PharmGKBPA37421.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG279678.
HOGENOMHOG000004802.
HOVERGENHBG079347.
InParanoidO43543.
KOK10879.
OMADTDYHFD.
OrthoDBEOG7K9K4C.
PhylomeDBO43543.
TreeFamTF101202.

Gene expression databases

BgeeO43543.
CleanExHS_XRCC2.
GenevestigatorO43543.

Family and domain databases

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

Other

ChiTaRSXRCC2. human.
GeneWikiXRCC2.
GenomeRNAi7516.
NextBio29411.
PROO43543.
SOURCESearch...

Entry information

Entry nameXRCC2_HUMAN
AccessionPrimary (citable) accession number: O43543
Secondary accession number(s): B2R925
Entry history
Integrated into UniProtKB/Swiss-Prot: April 3, 2002
Last sequence update: June 1, 1998
Last modified: April 16, 2014
This is version 110 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 7

Human chromosome 7: entries, gene names and cross-references to MIM