MSH3

From Wikipedia, the free encyclopedia

MutS homolog 3 (E. coli)

Identifiers

MSH3; MRP1; DUP; MGC163306; MGC163308

External IDs

OMIM: 600887 MGI: 109519 HomoloGene: 1829

Gene ontology
Molecular Function:	• nucleotide binding • purine-specific mismatch base pair DNA N-glycosylase activity • damaged DNA binding • single-stranded DNA binding • protein binding • ATP binding • mismatched DNA binding • guanine/thymine mispair binding • single guanine insertion binding • dinucleotide repeat insertion binding • oxidized purine DNA binding • protein homodimerization activity
Cellular Component:	• MutSbeta complex
Biological Process:	• base-excision repair • mismatch repair • maintenance of DNA repeat elements

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_002439 (mRNA)
NP_002430 (protein)

XM_983266 (mRNA)
XP_988360 (protein)

Location

Chr 5: 79.99 - 80.21 Mb

Chr 13: 93.31 - 93.46 Mb

Pubmed search

[1]

[2]

MutS homolog 3 (E. coli), also known as MSH3, is a human gene.^[1]

[edit] References

^ Entrez Gene: MSH3 mutS homolog 3 (E. coli).

[edit] 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. PMID 8029024.
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. 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. PMID 8942985.
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. PMID 9774676.
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. PMID 10871409.
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. 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. PMID 11274057.
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. PMID 11809883.
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.