MSH2

MutS homolog 2, colon cancer, nonpolyposis type 1 (E. coli)

PDB rendering based on 2o8b.
Identifiers
Symbols MSH2; COCA1; FCC1; HNPCC; HNPCC1; LCFS2
External IDs OMIM: 609309 MGI: 101816 HomoloGene: 210 GeneCards: MSH2 Gene
RNA expression pattern
More reference expression data
Orthologs
Species Human Mouse
Entrez 4436 17685
Ensembl ENSG00000095002 ENSMUSG00000024151
UniProt P43246 Q3TZI5
RefSeq (mRNA) NM_000251.1 NM_008628.2
RefSeq (protein) NP_000242.1 NP_032654.1
Location (UCSC) Chr 2:
47.63 – 47.79 Mb		 Chr 17:
88.07 – 88.12 Mb
PubMed search [1] [2]

MSH2 is a gene commonly associated with Hereditary nonpolyposis colorectal cancer.

MSH2 was identified as a locus frequently mutated in hereditary nonpolyposis colon cancer (HNPCC). When cloned, it was discovered to be a human homolog of the E. coli mismatch repair gene mutS, consistent with the characteristic alterations in microsatellite sequences (RER+ phenotype) found in HNPCC.[1] It is also associated with some endometrial cancers.

Contents

Interactions

MSH2 has been shown to interact with Exonuclease 1,[2][3][4] MSH3,[5][6][7][8] MSH6,[5][6][7][8][9] CHEK2,[10][11] MAX,[12] Ataxia telangiectasia and Rad3 related[5] and BRCA1.[9][13]

See also

References

  1. ^ "Entrez Gene: MSH2 mutS homolog 2, colon cancer, nonpolyposis type 1 (E. coli)". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4436. 
  2. ^ Rasmussen, L J; Rasmussen M, Lee B, Rasmussen A K, Wilson D M, Nielsen F C, Bisgaard H C (Jun. 2000). "Identification of factors interacting with hMSH2 in the fetal liver utilizing the yeast two-hybrid system. In vivo interaction through the C-terminal domains of hEXO1 and hMSH2 and comparative expression analysis". Mutat. Res. (NETHERLANDS) 460 (1): 41–52. doi:10.1016/S0921-8777(00)00012-4. ISSN 0027-5107. PMID 10856833. 
  3. ^ Schmutte, C; Marinescu R C, Sadoff M M, Guerrette S, Overhauser J, Fishel R (Oct. 1998). "Human exonuclease I interacts with the mismatch repair protein hMSH2". Cancer Res. (UNITED STATES) 58 (20): 4537–42. ISSN 0008-5472. PMID 9788596. 
  4. ^ Schmutte, C; Sadoff M M, Shim K S, Acharya S, Fishel R (Aug. 2001). "The interaction of DNA mismatch repair proteins with human exonuclease I". J. Biol. Chem. (United States) 276 (35): 33011–8. doi:10.1074/jbc.M102670200. ISSN 0021-9258. PMID 11427529. 
  5. ^ a b c 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. 
  6. ^ a b 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. 
  7. ^ a b 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. 
  8. ^ a b 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. 
  9. ^ a b Wang, Y; Cortez D, Yazdi P, Neff N, Elledge S J, Qin J (Apr. 2000). "BASC, a super complex of BRCA1-associated proteins involved in the recognition and repair of aberrant DNA structures". Genes Dev. (UNITED STATES) 14 (8): 927–39. ISSN 0890-9369. PMC 316544. PMID 10783165. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=316544. 
  10. ^ Adamson, Aaron W; Beardsley Dillon I, Kim Wan-Ju, Gao Yajuan, Baskaran R, Brown Kevin D (Mar. 2005). "Methylator-induced, mismatch repair-dependent G2 arrest is activated through Chk1 and Chk2". Mol. Biol. Cell (United States) 16 (3): 1513–26. doi:10.1091/mbc.E04-02-0089. ISSN 1059-1524. PMC 551512. PMID 15647386. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=551512. 
  11. ^ Brown, Kevin D; Rathi Abhilasha, Kamath Ravindra, Beardsley Dillon I, Zhan Qimin, Mannino Jennifer L, Baskaran R (Jan. 2003). "The mismatch repair system is required for S-phase checkpoint activation". Nat. Genet. (United States) 33 (1): 80–4. doi:10.1038/ng1052. ISSN 1061-4036. PMID 12447371. 
  12. ^ Mac Partlin, Mary; Homer Elizabeth, Robinson Helen, McCormick Carol J, Crouch Dorothy H, Durant Stephen T, Matheson Elizabeth C, Hall Andrew G, Gillespie David A F, Brown Robert (Feb. 2003). "Interactions of the DNA mismatch repair proteins MLH1 and MSH2 with c-MYC and MAX". Oncogene (England) 22 (6): 819–25. doi:10.1038/sj.onc.1206252. ISSN 0950-9232. PMID 12584560. 
  13. ^ 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

External links

Excision repair
Other forms of repair
Other/ungrouped proteins
Regulation
Other/ungrouped
see also DNA repair-deficiency disorder
B bsyn: dna (repl, cycl, reco, repr) · tscr (fact, tcrg, nucl, rnat, rept, ptts) · tltn (risu, pttl, nexn) · dnab, rnab/runp · stru (domn, 1°, 2°, 3°, 4°)