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O43502 (RA51C_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 124. 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·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
DNA repair protein RAD51 homolog 3

Short name=R51H3
Alternative name(s):
RAD51 homolog C
RAD51-like protein 2
Gene names
Name:RAD51C
Synonyms:RAD51L2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length376 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Essential for the homologous recombination (HR) pathway of DNA repair. Involved in the homologous recombination repair (HRR) pathway of double-stranded DNA breaks arising during DNA replication or induced by DNA-damaging agents. Part of the RAD21 paralog protein complexes BCDX2 and CX3 which act at different stages of the BRCA1-BRCA2-dependent HR pathway. Upon DNA damage, BCDX2 seems to act downstream of BRCA2 recruitment and upstream of RAD51 recruitment; CX3 seems to act downstream of RAD51 recruitment; both complexes bind predominantly to the intersection of the four duplex arms of the Holliday junction (HJ) 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. The BCDX2 subcomplex RAD51B:RAD51C exhibits single-stranded DNA-dependent ATPase activity suggesting an involvement in early stages of the HR pathway. Involved in RAD51 foci formation in response to DNA damage suggesting an involvement in early stages of HR probably in the invasion step. Has an early function in DNA repair in facilitating phosphorylation of the checkpoint kinase CHEK2 and thereby transduction of the damage signal, leading to cell cycle arrest and HR activation. Participates in branch migration and HJ resolution and thus is important for processing HR intermediates late in the DNA repair process; the function may be linked to the CX3 complex. Part of a PALB2-scaffolded HR complex containing BRCA2 and which is thought to play a role in DNA repair by HR. Protects RAD51 from ubiquitin-mediated degradation that is enhanced following DNA damage. Plays a role in regulating mitochondrial DNA copy number under conditions of oxidative stress in the presence of RAD51 and XRCC3. Contributes to DNA cross-link resistance, sister chromatid cohesion and genomic stability. Involved in maintaining centrosome number in mitosis. Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.22 Ref.23

Subunit structure

Part of the Rad21 paralog protein complexes BCDX2 and CX3; the complexes have a ring-like structure arranged into a flat disc around a central channel. The BCDX2 complex consits of RAD51B, RAD51C, RAD51D and XRCC2; the CX3 complex consists of RAD51C and XRCC3. The BCDX2 subcomplex RAD51B:RAD51C interacts with RAD51. Interacts with SWSAP1; 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. Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.13 Ref.16 Ref.21 Ref.24

Subcellular location

Nucleus. Cytoplasm. Cytoplasmperinuclear region. Mitochondrion. Note: DNA damage induces an increase in nuclear levels. Accumulates in DNA damage induced nuclear foci or RAD51C foci which is formed during the S or G2 phase of cell cycle. Accumulation at DNA lesions requires the presence of NBN/NBS1, ATM and RPA. Ref.12 Ref.15 Ref.17 Ref.18 Ref.19

Tissue specificity

Expressed in a variety of tissues, with highest expression in testis, heart muscle, spleen and prostate.

Induction

Stress-induced increase in the mitochondrial levels is seen. Ref.19

Involvement in disease

Fanconi anemia complementation group O (FANCO) [MIM:613390]: A disorder affecting all bone marrow elements and resulting in anemia, leukopenia and thrombopenia. It is associated with cardiac, renal and limb malformations, dermal pigmentary changes, and a predisposition to the development of malignancies. At the cellular level it is associated with hypersensitivity to DNA-damaging agents, chromosomal instability (increased chromosome breakage) and defective DNA repair.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.24 Ref.26

Breast-ovarian cancer, familial, 3 (BROVCA3) [MIM:613399]: A condition associated with familial predisposition to cancer of the breast and ovaries. Characteristic features in affected families are an early age of onset of breast cancer (often before age 50), increased chance of bilateral cancers (cancer that develop in both breasts, or both ovaries, independently), frequent occurrence of breast cancer among men, increased incidence of tumors of other specific organs, such as the prostate.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.24 Ref.27 Ref.28

Sequence similarities

Belongs to the RecA family. RAD51 subfamily.

Ontologies

Keywords
   Biological processDNA damage
DNA recombination
DNA repair
   Cellular componentCytoplasm
Mitochondrion
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
Fanconi anemia
   LigandATP-binding
DNA-binding
Nucleotide-binding
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA catabolic process, endonucleolytic

Inferred from mutant phenotype Ref.14. Source: GOC

DNA recombination

Inferred from direct assay Ref.18. Source: UniProtKB

DNA repair

Inferred from direct assay Ref.18. Source: UniProtKB

blood coagulation

Traceable author statement. Source: Reactome

double-strand break repair via homologous recombination

Inferred from mutant phenotype Ref.23. Source: UniProtKB

female meiosis sister chromatid cohesion

Inferred from electronic annotation. Source: Ensembl

male meiosis I

Inferred from electronic annotation. Source: Ensembl

positive regulation of G2/M transition of mitotic cell cycle

Inferred from mutant phenotype Ref.22. Source: UniProtKB

reciprocal meiotic recombination

Inferred from electronic annotation. Source: Ensembl

sister chromatid cohesion

Inferred from sequence or structural similarity. Source: UniProtKB

spermatogenesis

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentRad51B-Rad51C-Rad51D-XRCC2 complex

Inferred from direct assay Ref.6. Source: UniProtKB

Rad51C-XRCC3 complex

Inferred from direct assay Ref.6. Source: UniProtKB

cytoplasm

Inferred from direct assay Ref.15. Source: UniProtKB

mitochondrion

Inferred from direct assay Ref.19. Source: UniProtKB

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay Ref.12Ref.15. Source: UniProtKB

perinuclear region of cytoplasm

Inferred from direct assay Ref.15. Source: UniProtKB

replication fork

Inferred from direct assay Ref.25. Source: UniProtKB

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

DNA binding

Traceable author statement Ref.1. Source: ProtInc

DNA-dependent ATPase activity

Inferred from electronic annotation. Source: InterPro

crossover junction endodeoxyribonuclease activity

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

RAD51Q066093EBI-2267048,EBI-297202
SWSAP1Q6NVH72EBI-2267048,EBI-5281637

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O43502-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: O43502-2)

The sequence of this isoform differs from the canonical sequence as follows:
     135-135: C → W
     136-376: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 376376DNA repair protein RAD51 homolog 3
PRO_0000122941

Regions

Nucleotide binding125 – 1328ATP Potential
Region1 – 126126Required for Holliday junction resolution activity
Region79 – 13658Interaction with RAD51B, RAD51D and XRCC3
Motif366 – 3705Nuclear localization signal Potential

Natural variations

Alternative sequence1351C → W in isoform 2.
VSP_043656
Alternative sequence136 – 376241Missing in isoform 2.
VSP_043657
Natural variant31G → R. Ref.27
VAR_063837
Natural variant521I → L. Ref.28
VAR_068014
Natural variant1031Missing. Ref.28
VAR_068015
Natural variant1141G → V. Ref.28
VAR_068016
Natural variant1251G → V in BROVCA3. Ref.27
VAR_063838
Natural variant1261A → T. Ref.27 Ref.28
Corresponds to variant rs61758784 [ dbSNP | Ensembl ].
VAR_063839
Natural variant1381L → F in BROVCA3; reduces interaction with BRCA2 and to a lesser extent with PALB2 and RAD51. Ref.24 Ref.27
VAR_063840
Natural variant1441I → T. Ref.2
Corresponds to variant rs28363307 [ dbSNP | Ensembl ].
VAR_020518
Natural variant1591D → N Reduces interaction with BRCA2 and to a lesser extent with PALB2 and RAD51. Ref.24 Ref.27
VAR_063841
Natural variant1621G → E in BROVCA3. Ref.28
Corresponds to variant rs35151472 [ dbSNP | Ensembl ].
VAR_068017
Natural variant1691V → A. Ref.27 Ref.28
VAR_063842
Natural variant1751A → T. Ref.28
VAR_068018
Natural variant1781Q → P in BROVCA3. Ref.28
VAR_068019
Natural variant2491R → C. Ref.2 Ref.28
Corresponds to variant rs28363311 [ dbSNP | Ensembl ].
VAR_020519
Natural variant2581R → H in FANCO; possibly hypomorphic allele; reduces interaction with BRCA2 and to a lesser extent with PALB2 and RAD51. Ref.24 Ref.26
VAR_064032
Natural variant2621L → V. Ref.28
Corresponds to variant rs149331537 [ dbSNP | Ensembl ].
VAR_068020
Natural variant2641G → S. Ref.27 Ref.28
Corresponds to variant rs147241704 [ dbSNP | Ensembl ].
VAR_063843
Natural variant2641G → V. Ref.27
VAR_063844
Natural variant2871T → A in BROVCA3. Ref.2 Ref.27 Ref.28
Corresponds to variant rs28363317 [ dbSNP | Ensembl ].
VAR_020520
Natural variant3661R → Q. Ref.27
VAR_063845

Experimental info

Mutagenesis1311K → A: Significant loss of function; abolishes Holliday junction resolution activity. Ref.12 Ref.14
Mutagenesis1311K → R: Partial loss of function. Ref.12 Ref.14

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified June 1, 1998. Version 1.
Checksum: 3AAADD3C1C0851E0

FASTA37642,190
        10         20         30         40         50         60 
MRGKTFRFEM QRDLVSFPLS PAVRVKLVSA GFQTAEELLE VKPSELSKEV GISKAEALET 

        70         80         90        100        110        120 
LQIIRRECLT NKPRYAGTSE SHKKCTALEL LEQEHTQGFI ITFCSALDDI LGGGVPLMKT 

       130        140        150        160        170        180 
TEICGAPGVG KTQLCMQLAV DVQIPECFGG VAGEAVFIDT EGSFMVDRVV DLATACIQHL 

       190        200        210        220        230        240 
QLIAEKHKGE EHRKALEDFT LDNILSHIYY FRCRDYTELL AQVYLLPDFL SEHSKVRLVI 

       250        260        270        280        290        300 
VDGIAFPFRH DLDDLSLRTR LLNGLAQQMI SLANNHRLAV ILTNQMTTKI DRNQALLVPA 

       310        320        330        340        350        360 
LGESWGHAAT IRLIFHWDRK QRLATLYKSP SQKECTVLFQ IKPQGFRDTV VTSACSLQTE 

       370 
GSLSTRKRSR DPEEEL 

« Hide

Isoform 2 [UniParc].

Checksum: 56657E563509D90F
Show »

FASTA13514,883

References

« Hide 'large scale' references
[1]"Isolation and characterization of RAD51C, a new human member of the RAD51 family of related genes."
Dosanjh M.K., Collins D.W., Fan W., Lennon G.G., Albala J.S., Shen Z., Schild D.
Nucleic Acids Res. 26:1179-1184(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
[2]NIEHS SNPs program
Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS THR-144; CYS-249 AND ALA-287.
[3]"DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L. expand/collapse author list , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]Mural R.J., Istrail S., Sutton 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].
[5]"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] (ISOFORM 1).
[6]"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: IDENTIFICATION IN THE BCDX2 COMPLEX WITH RAD51B; RAD51D AND XRCC2, IDENTIFICATION IN THE CX3 COMPLEX WITH XRCC3.
[7]"Mediator function of the human Rad51B-Rad51C complex in Rad51/RPA-catalyzed DNA strand exchange."
Sigurdsson S., Van Komen S., Bussen W., Schild D., Albala J.S., Sung P.
Genes Dev. 15:3308-3318(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FIUNCTION, INTERACTION WITH RAD51B.
[8]"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: INTERACTION WITH RAD51B, SUBUNIT.
[9]"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; RAD51D AND XRCC2.
[10]"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; RAD51D AND XRCC2, INTERACTION WITH XRCC3.
[11]"Complex formation by the human Rad51B and Rad51C DNA repair proteins and their activities in vitro."
Lio Y.-C., Mazin A.V., Kowalczykowski S.C., Chen D.J.
J. Biol. Chem. 278:2469-2478(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RAD51 AND RAD51B.
[12]"Identification of functional domains in the RAD51L2 (RAD51C) protein and its requirement for gene conversion."
French C.A., Tambini C.E., Thacker J.
J. Biol. Chem. 278:45445-45450(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-131.
[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 RAD51B; RAD51D AND XRCC3.
[14]"RAD51C is required for Holliday junction processing in mammalian cells."
Liu Y., Masson J.Y., Shah R., O'Regan P., West S.C.
Science 303:243-246(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF LYS-131.
[15]"Cellular localization of human Rad51C and regulation of ubiquitin-mediated proteolysis of Rad51."
Bennett B.T., Knight K.L.
J. Cell. Biochem. 96:1095-1109(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[16]"Interplay between human DNA repair proteins at a unique double-strand break in vivo."
Rodrigue A., Lafrance M., Gauthier M.C., McDonald D., Hendzel M., West S.C., Jasin M., Masson J.Y.
EMBO J. 25:222-231(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH RAD51.
[17]"Cellular redistribution of Rad51 in response to DNA damage: novel role for Rad51C."
Gildemeister O.S., Sage J.M., Knight K.L.
J. Biol. Chem. 284:31945-31952(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[18]"RAD51C facilitates checkpoint signaling by promoting CHK2 phosphorylation."
Badie S., Liao C., Thanasoula M., Barber P., Hill M.A., Tarsounas M.
J. Cell Biol. 185:587-600(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[19]"Discovery of a novel function for human Rad51: maintenance of the mitochondrial genome."
Sage J.M., Gildemeister O.S., Knight K.L.
J. Biol. Chem. 285:18984-18990(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INDUCTION.
[20]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[21]"hSWS1.SWSAP1 is an evolutionarily conserved complex required for efficient homologous recombination repair."
Liu T., Wan L., Wu Y., Chen J., Huang J.
J. Biol. Chem. 286:41758-41766(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SWSAP1.
[22]"The RAD51 paralogs ensure cellular protection against mitotic defects and aneuploidy."
Rodrigue A., Coulombe Y., Jacquet K., Gagne J.P., Roques C., Gobeil S., Poirier G., Masson J.Y.
J. Cell Sci. 126:348-359(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN MITOTIC CELL PROGRESSION.
[23]"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, FUNCTION OF THE CX3 COMPLEX.
[24]"Breast cancer-associated missense mutants of the PALB2 WD40 domain, which directly binds RAD51C, RAD51 and BRCA2, disrupt DNA repair."
Park J.Y., Singh T.R., Nassar N., Zhang F., Freund M., Hanenberg H., Meetei A.R., Andreassen P.R.
Oncogene 0:0-0(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH BRCA2; RAD51 AND PALB2, IDENTIFICATION IN A PALB2-CONTAINING HR COMPLEX, CHARACTERIZATION OF VARIANT BROVCA3 PHE-138, CHARACTERIZATION OF VARIANT ASN-159, CHARACTERIZATION OF VARIANT FANCO HIS-258.
[25]"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 AND CX3 COMPLEXES, DNA-BINDING OF THE BCDX2 AND CX3 COMPLEXES.
[26]"Mutation of the RAD51C gene in a Fanconi anemia-like disorder."
Vaz F., Hanenberg H., Schuster B., Barker K., Wiek C., Erven V., Neveling K., Endt D., Kesterton I., Autore F., Fraternali F., Freund M., Hartmann L., Grimwade D., Roberts R.G., Schaal H., Mohammed S., Rahman N., Schindler D., Mathew C.G.
Nat. Genet. 42:406-409(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT FANCO HIS-258, CHARACTERIZATION OF VARIANT FANCO HIS-258.
[27]"Germline mutations in breast and ovarian cancer pedigrees establish RAD51C as a human cancer susceptibility gene."
Meindl A., Hellebrand H., Wiek C., Erven V., Wappenschmidt B., Niederacher D., Freund M., Lichtner P., Hartmann L., Schaal H., Ramser J., Honisch E., Kubisch C., Wichmann H.E., Kast K., Deissler H., Engel C., Muller-Myhsok B. expand/collapse author list , Neveling K., Kiechle M., Mathew C.G., Schindler D., Schmutzler R.K., Hanenberg H.
Nat. Genet. 42:410-414(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ARG-3; THR-126; ASN-159; ALA-169; SER-264; VAL-264; ALA-287 AND GLN-366, VARIANTS BROVCA3 VAL-125 AND PHE-138.
[28]"Analysis of RAD51C germline mutations in high-risk breast and ovarian cancer families and ovarian cancer patients."
Kathleen Cuningham foundation consortium for research into familial breast cancer (kConFab)
Thompson E.R., Boyle S.E., Johnson J., Ryland G.L., Sawyer S., Choong D.Y., Chenevix-Trench G., Trainer A.H., Lindeman G.J., Mitchell G., James P.A., Campbell I.G.
Hum. Mutat. 33:95-99(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS LEU-52; PHE-103 DEL; VAL-114; THR-126; ALA-169; THR-175; CYS-249; VAL-262 AND SER-264, VARIANTS BROVCA3 GLU-162; PRO-178 AND ALA-287.
+Additional computationally mapped references.

Web resources

NIEHS-SNPs
RAD51 homolog C (S.cerevisiae) (RAD51C)

Leiden Open Variation Database (LOVD)

RAD51 homolog C (S.cerevisiae) (RAD51C)

ZJU-CGGM and BGI-Shenzhen

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF029669 mRNA. Translation: AAC39604.1.
AF029670 mRNA. Translation: AAC39605.1.
AY623112 Genomic DNA. Translation: AAT38108.1.
AC011195 Genomic DNA. No translation available.
AC025521 Genomic DNA. No translation available.
CH471109 Genomic DNA. Translation: EAW94432.1.
BC107753 mRNA. Translation: AAI07754.1.
RefSeqNP_002867.1. NM_002876.3.
NP_478123.1. NM_058216.2.
UniGeneHs.412587.

3D structure databases

ProteinModelPortalO43502.
SMRO43502. Positions 19-348.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111826. 10 interactions.
DIPDIP-41247N.
IntActO43502. 2 interactions.
MINTMINT-204767.
STRING9606.ENSP00000336701.

PTM databases

PhosphoSiteO43502.

Proteomic databases

PaxDbO43502.
PRIDEO43502.

Protocols and materials databases

DNASU5889.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000337432; ENSP00000336701; ENSG00000108384. [O43502-1]
ENST00000421782; ENSP00000391450; ENSG00000108384. [O43502-2]
GeneID5889.
KEGGhsa:5889.
UCSCuc002iwt.1. human. [O43502-2]
uc002iwu.3. human. [O43502-1]

Organism-specific databases

CTD5889.
GeneCardsGC17P056769.
HGNCHGNC:9820. RAD51C.
MIM602774. gene.
613390. phenotype.
613399. phenotype.
neXtProtNX_O43502.
Orphanet84. Fanconi anemia.
145. Hereditary breast and ovarian cancer syndrome.
PharmGKBPA34177.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0468.
HOGENOMHOG000227426.
HOVERGENHBG055764.
InParanoidO43502.
KOK10870.
OMATNQMTTR.
PhylomeDBO43502.
TreeFamTF101220.

Enzyme and pathway databases

ReactomeREACT_604. Hemostasis.

Gene expression databases

ArrayExpressO43502.
BgeeO43502.
CleanExHS_RAD51C.
GenevestigatorO43502.

Family and domain databases

Gene3D3.40.50.300. 1 hit.
InterProIPR003593. AAA+_ATPase.
IPR013632. 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.
SMARTSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
PROSITEPS50162. RECA_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiRAD51C.
GenomeRNAi5889.
NextBio22902.
PROO43502.
SOURCESearch...

Entry information

Entry nameRA51C_HUMAN
AccessionPrimary (citable) accession number: O43502
Secondary accession number(s): O43503, Q3B783
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: June 1, 1998
Last modified: April 16, 2014
This is version 124 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 17

Human chromosome 17: entries, gene names and cross-references to MIM