MSH3

MutS homolog 3 (E. coli)

Identifiers

MSH3; DUP; MGC163306; MGC163308; MRP1

External IDs

OMIM: 600887 MGI: 109519 HomoloGene: 1829 GeneCards: MSH3 Gene

Gene Ontology
Molecular function	• nucleotide binding • Y-form DNA binding • loop DNA binding • double-strand/single-strand DNA junction binding • damaged DNA binding • single-stranded DNA binding • protein binding • ATP binding • DNA-dependent ATPase activity • centromeric DNA binding • enzyme binding • mismatched DNA binding • guanine/thymine mispair binding • dinucleotide insertion or deletion binding • single guanine insertion binding • dinucleotide repeat insertion binding • oxidized purine DNA binding • protein homodimerization activity
Cellular component	• nuclear chromosome • MutSbeta complex
Biological process	• meiotic mismatch repair • DNA repair • mismatch repair • reciprocal meiotic recombination • somatic recombination of immunoglobulin gene segments • maintenance of DNA repeat elements • negative regulation of DNA recombination • positive regulation of helicase activity
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

ENSG00000113318

ENSMUSG00000014850

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 5:
79.95 – 80.17 Mb

Chr 13:
92.98 – 93.12 Mb

PubMed search

DNA mismatch repair protein Msh3 is a protein that in humans is encoded by the MSH3 gene.^[1]

Interactions

MSH3 has been shown to interact with MSH2,^[2]^[3]^[4]^[5] PCNA^[6]^[7]^[8] and BRCA1.^[9]^[10]

References

^ "Entrez Gene: MSH3 mutS homolog 3 (E. coli)". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4437.
^ Wang, Yi; Qin Jun (Dec. 2003). "MSH2 and ATR form a signaling module and regulate two branches of the damage response to DNA methylation". Proc. Natl. Acad. Sci. U.S.A. (United States) 100 (26): 15387–92. doi:10.1073/pnas.2536810100. ISSN 0027-8424. PMC 307577. PMID 14657349. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=307577.
^ Guerrette, S; Wilson T, Gradia S, Fishel R (Nov. 1998). "Interactions of human hMSH2 with hMSH3 and hMSH2 with hMSH6: examination of mutations found in hereditary nonpolyposis colorectal cancer". Mol. Cell. Biol. (UNITED STATES) 18 (11): 6616–23. ISSN 0270-7306. PMC 109246. PMID 9774676. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=109246.
^ Bocker, T; Barusevicius A, Snowden T, Rasio D, Guerrette S, Robbins D, Schmidt C, Burczak J, Croce C M, Copeland T, Kovatich A J, Fishel R (Feb. 1999). "hMSH5: a human MutS homologue that forms a novel heterodimer with hMSH4 and is expressed during spermatogenesis". Cancer Res. (UNITED STATES) 59 (4): 816–22. ISSN 0008-5472. PMID 10029069.
^ Acharya, S; Wilson T, Gradia S, Kane M F, Guerrette S, Marsischky G T, Kolodner R, Fishel R (Nov. 1996). "hMSH2 forms specific mispair-binding complexes with hMSH3 and hMSH6". Proc. Natl. Acad. Sci. U.S.A. (UNITED STATES) 93 (24): 13629–34. doi:10.1073/pnas.93.24.13629. ISSN 0027-8424. PMC 19374. PMID 8942985. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=19374.
^ Kleczkowska, H E; Marra G, Lettieri T, Jiricny J (Mar. 2001). "hMSH3 and hMSH6 interact with PCNA and colocalize with it to replication foci". Genes Dev. (United States) 15 (6): 724–36. doi:10.1101/gad.191201. ISSN 0890-9369. PMC 312660. PMID 11274057. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=312660.
^ Clark, A B; Valle F, Drotschmann K, Gary R K, Kunkel T A (Nov. 2000). "Functional interaction of proliferating cell nuclear antigen with MSH2-MSH6 and MSH2-MSH3 complexes". J. Biol. Chem. (UNITED STATES) 275 (47): 36498–501. doi:10.1074/jbc.C000513200. ISSN 0021-9258. PMID 11005803.
^ Ohta, Satoshi; Shiomi Yasushi, Sugimoto Katsunori, Obuse Chikashi, Tsurimoto Toshiki (Oct. 2002). "A proteomics approach to identify proliferating cell nuclear antigen (PCNA)-binding proteins in human cell lysates. Identification of the human CHL12/RFCs2-5 complex as a novel PCNA-binding protein". J. Biol. Chem. (United States) 277 (43): 40362–7. doi:10.1074/jbc.M206194200. ISSN 0021-9258. PMID 12171929.
^ Rodriguez, Maria; Yu Xiaochun, Chen Junjie, Songyang Zhou (Dec. 2003). "Phosphopeptide binding specificities of BRCA1 COOH-terminal (BRCT) domains". J. Biol. Chem. (United States) 278 (52): 52914–8. doi:10.1074/jbc.C300407200. ISSN 0021-9258. PMID 14578343.
^ Wang, Q; Zhang H, Guerrette S, Chen J, Mazurek A, Wilson T, Slupianek A, Skorski T, Fishel R, Greene M I (Aug. 2001). "Adenosine nucleotide modulates the physical interaction between hMSH2 and BRCA1". Oncogene (England) 20 (34): 4640–9. doi:10.1038/sj.onc.1204625. ISSN 0950-9232. PMID 11498787.

Further reading

Marti TM, Kunz C, Fleck O (2002). "DNA mismatch repair and mutation avoidance pathways.". J. Cell. Physiol. 191 (1): 28–41. doi:10.1002/jcp.10077. PMID 11920679.
Fujii H, Shimada T (1989). "Isolation and characterization of cDNA clones derived from the divergently transcribed gene in the region upstream from the human dihydrofolate reductase gene.". J. Biol. Chem. 264 (17): 10057–64. PMID 2722860.
Chen MJ, Shimada T, Moulton AD, et al. (1984). "The functional human dihydrofolate reductase gene.". J. Biol. Chem. 259 (6): 3933–43. PMID 6323448.
Shinya E, Shimada T (1994). "Identification of two initiator elements in the bidirectional promoter of the human dihydrofolate reductase and mismatch repair protein 1 genes.". Nucleic Acids Res. 22 (11): 2143–9. doi:10.1093/nar/22.11.2143. PMC 308133. PMID 8029024. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=308133.
Risinger JI, Umar A, Boyd J, et al. (1996). "Mutation of MSH3 in endometrial cancer and evidence for its functional role in heteroduplex repair.". Nat. Genet. 14 (1): 102–5. doi:10.1038/ng0996-102. PMID 8782829.
Watanabe A, Ikejima M, Suzuki N, Shimada T (1997). "Genomic organization and expression of the human MSH3 gene.". Genomics 31 (3): 311–8. doi:10.1006/geno.1996.0053. PMID 8838312.
Nakajima E, Orimo H, Ikejima M, Shimada T (1996). "Nine-bp repeat polymorphism in exon 1 of the hMSH3 gene.". Jpn. J. Hum. Genet. 40 (4): 343–5. doi:10.1007/BF01900603. PMID 8851770.
Acharya S, Wilson T, Gradia S, et al. (1997). "hMSH2 forms specific mispair-binding complexes with hMSH3 and hMSH6.". Proc. Natl. Acad. Sci. U.S.A. 93 (24): 13629–34. doi:10.1073/pnas.93.24.13629. PMC 19374. PMID 8942985. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=19374.
Guerrette S, Wilson T, Gradia S, Fishel R (1998). "Interactions of human hMSH2 with hMSH3 and hMSH2 with hMSH6: examination of mutations found in hereditary nonpolyposis colorectal cancer.". Mol. Cell. Biol. 18 (11): 6616–23. PMC 109246. PMID 9774676. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=109246.
Ceccotti S, Ciotta C, Fronza G, et al. (2000). "Multiple mutations and frameshifts are the hallmark of defective hPMS2 in pZ189-transfected human tumor cells.". Nucleic Acids Res. 28 (13): 2577–84. doi:10.1093/nar/28.13.2577. PMC 102707. PMID 10871409. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=102707.
Orimo H, Nakajima E, Yamamoto M, et al. (2000). "Association between single nucleotide polymorphisms in the hMSH3 gene and sporadic colon cancer with microsatellite instability.". J. Hum. Genet. 45 (4): 228–30. doi:10.1007/s100380070031. PMID 10944853.
Clark AB, Valle F, Drotschmann K, et al. (2001). "Functional interaction of proliferating cell nuclear antigen with MSH2-MSH6 and MSH2-MSH3 complexes.". J. Biol. Chem. 275 (47): 36498–501. doi:10.1074/jbc.C000513200. PMID 11005803.
Kleczkowska HE, Marra G, Lettieri T, Jiricny J (2001). "hMSH3 and hMSH6 interact with PCNA and colocalize with it to replication foci.". Genes Dev. 15 (6): 724–36. doi:10.1101/gad.191201. PMC 312660. PMID 11274057. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=312660.
Schmutte C, Sadoff MM, Shim KS, et al. (2001). "The interaction of DNA mismatch repair proteins with human exonuclease I.". J. Biol. Chem. 276 (35): 33011–8. doi:10.1074/jbc.M102670200. PMID 11427529.
Wang Q, Zhang H, Guerrette S, et al. (2001). "Adenosine nucleotide modulates the physical interaction between hMSH2 and BRCA1.". Oncogene 20 (34): 4640–9. doi:10.1038/sj.onc.1204625. PMID 11498787.
Mazurek A, Berardini M, Fishel R (2002). "Activation of human MutS homologs by 8-oxo-guanine DNA damage.". J. Biol. Chem. 277 (10): 8260–6. doi:10.1074/jbc.M111269200. PMID 11756455.
Plotz G, Raedle J, Brieger A, et al. (2002). "hMutSalpha forms an ATP-dependent complex with hMutLalpha and hMutLbeta on DNA.". Nucleic Acids Res. 30 (3): 711–8. doi:10.1093/nar/30.3.711. PMC 100294. PMID 11809883. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=100294.
Arzimanoglou II, Hansen LL, Chong D, et al. (2002). "Frequent LOH at hMLH1, a highly variable SNP in hMSH3, and negligible coding instability in ovarian cancer.". Anticancer Res. 22 (2A): 969–75. PMID 12014680.
Ohta S, Shiomi Y, Sugimoto K, et al. (2002). "A proteomics approach to identify proliferating cell nuclear antigen (PCNA)-binding proteins in human cell lysates. Identification of the human CHL12/RFCs2-5 complex as a novel PCNA-binding protein.". J. Biol. Chem. 277 (43): 40362–7. doi:10.1074/jbc.M206194200. PMID 12171929.