[1]	NUCLEOTIDE SEQUENCE [MRNA]. DOI=10.1016/0092-8674(93)90546-3; PubMed=8252616 [NCBI, ExPASy, EBI, Israel, Japan] Fishel R., Lescoe M., Rao M., Copeland N.G., Jenkins N.A., Garber J., Kane M.F., Kolodner R.D.; "The human mutator gene homolog MSH2 and its association with hereditary nonpolyposis colon cancer."; Cell 75:1027-1038(1993).
[2]	ERRATUM. PubMed=8156592 [NCBI, ExPASy, EBI, Israel, Japan] Fishel R., Lescoe M., Rao M., Copeland N.G., Jenkins N.A., Garber J., Kane M.F., Kolodner R.D.; Cell 77:167-167(1994).
[3]	NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS HNPCC1 LEU-622 AND TYR-639. DOI=10.1016/0092-8674(93)90330-S; PubMed=8261515 [NCBI, ExPASy, EBI, Israel, Japan] Leach F.S., Nicolaides N.C., Papadopoulos N., Liu B., Jen J., Parsons R., Peltomaeki P., Sistonen P., Aaltonen L.A., Nystroem-Lahti M., Guan X.-Y., Zhang J., Meltzer P.S., Yu J.-W., Kao F.-T., Chen D.J., Cerosaletti K.M., Fournier R.E.K., Todd S., Lewis T., Leach R.J., Naylor S.L., Weissenbach J., Mecklin J.-P., Jaervinen H., Petersen G.M., Hamilton S.R., Green J., Jass J., Watson P., Lynch H.T., Trent J.M., de la Chapelle A., Kinzler K.W., Vogelstein B.; "Mutations of a mutS homolog in hereditary nonpolyposis colorectal cancer."; Cell 75:1215-1225(1993).
[4]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND DISEASE. DOI=10.1006/geno.1994.1661; PubMed=7713503 [NCBI, ExPASy, EBI, Israel, Japan] Kolodner R.D., Hall N.R., Lipford J., Kane M.F., Rao M.R.S., Morrison P., Wirth L., Finan P.J., Burn J., Chapman P., Earabino C., Merchant E., Bishop D.T.; "Structure of the human MSH2 locus and analysis of two Muir-Torre kindreds for msh2 mutations."; Genomics 24:516-526(1994).
[5]	NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT HIS-96. PubMed=7726159 [NCBI, ExPASy, EBI, Israel, Japan] Wijnen J., Vasen H., Khan P.M., Menko F.H., van der Klift H., van Leeuwen C., van den Broek M., van Leeuwen-Cornelisse I., Nagengast F., Meijers-Heijboer A., Lindhout D., Griffioen G., Cats A., Kleibeuker J., Varesco L., Bertario L., Bisgaard M.-L., Mohr J., Fodde R.; "Seven new mutations in hMSH2, an HNPCC gene, identified by denaturing gradient-gel electrophoresis."; Am. J. Hum. Genet. 56:1060-1066(1995).
[6]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS MET-8; CYS-43; SER-127; ASP-322 AND PHE-390. NIEHS SNPs program; Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
[7]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Muscle; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).
[8]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 375-425. TISSUE=Blood; Corvello C.M., Bevilacqua R.A.U., Rossi B.M., Simpson A.J.G.; "A novel germline mutation at exon 7 of the hMSH2 gene (417 del G) in a large HNPCC Brazilian kindred."; Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
[9]	DNA-BINDING. PubMed=7923193 [NCBI, ExPASy, EBI, Israel, Japan] Fishel R., Ewel A., Lescoe M.K.; "Purified human MSH2 protein binds to DNA containing mismatched nucleotides."; Cancer Res. 54:5539-5542(1994).
[10]	DNA-BINDING. DOI=10.1006/bbrc.1996.1168; PubMed=8769132 [NCBI, ExPASy, EBI, Israel, Japan] Whitehouse A., Taylor G.R., Deeble J., Phillips S.E., Meredith D.M., Markham A.F.; "A carboxy terminal domain of the hMSH-2 gene product is sufficient for binding specific mismatched oligonucleotides."; Biochem. Biophys. Res. Commun. 225:289-295(1996).
[11]	INTERACTION WITH MSH3 AND MSH6. DOI=10.1073/pnas.93.24.13629; PubMed=8942985 [NCBI, ExPASy, EBI, Israel, Japan] Acharya S., Wilson T., Gradia S., Kane M.F., Guerrette S., Marsischky G.T., Kolodner R.D., Fishel R.; "hMSH2 forms specific mispair-binding complexes with hMSH3 and hMSH6."; Proc. Natl. Acad. Sci. U.S.A. 93:13629-13634(1996).
[12]	INTERACTION WITH EXO1. PubMed=9788596 [NCBI, ExPASy, EBI, Israel, Japan] Schmutte C., Marinescu R.C., Sadoff M.M., Guerrette S., Overhauser J., Fishel R.; "Human exonuclease I interacts with the mismatch repair protein hMSH2."; Cancer Res. 58:4537-4542(1998).
[13]	FUNCTION. DOI=10.1074/jbc.273.48.32055; PubMed=9822680 [NCBI, ExPASy, EBI, Israel, Japan] Blackwell L.J., Martik D., Bjornson K.P., Bjornson E.S., Modrich P.; "Nucleotide-promoted release of hMutSalpha from heteroduplex DNA is consistent with an ATP-dependent translocation mechanism."; J. Biol. Chem. 273:32055-32062(1998).
[14]	FUNCTION. DOI=10.1074/jbc.273.48.32049; PubMed=9822679 [NCBI, ExPASy, EBI, Israel, Japan] Blackwell L.J., Bjornson K.P., Modrich P.; "DNA-dependent activation of the hMutSalpha ATPase."; J. Biol. Chem. 273:32049-32054(1998).
[15]	FUNCTION, AND MUTAGENESIS OF LYS-675. DOI=10.1093/emboj/17.9.2677; PubMed=9564049 [NCBI, ExPASy, EBI, Israel, Japan] Iaccarino I., Marra G., Palombo F., Jiricny J.; "hMSH2 and hMSH6 play distinct roles in mismatch binding and contribute differently to the ATPase activity of hMutSalpha."; EMBO J. 17:2677-2686(1998).
[16]	MISMATCH-BINDING, AND CHARACTERIZATION OF VARIANT HNPCC1 PRO-524. DOI=10.1093/nar/27.3.736; PubMed=9889267 [NCBI, ExPASy, EBI, Israel, Japan] Clark A.B., Cook M.E., Tran H.T., Gordenin D.A., Resnick M.A., Kunkel T.A.; "Functional analysis of human MutSalpha and MutSbeta complexes in yeast."; Nucleic Acids Res. 27:736-742(1999).
[17]	FUNCTION. DOI=10.1016/S1097-2765(00)80316-0; PubMed=10078208 [NCBI, ExPASy, EBI, Israel, Japan] Gradia S., Subramanian D., Wilson T., Acharya S., Makhov A., Griffith J., Fishel R.; "hMSH2-hMSH6 forms a hydrolysis-independent sliding clamp on mismatched DNA."; Mol. Cell 3:255-261(1999).
[18]	IDENTIFICATION OF MSH2 AS MEMBER OF BASC. DOI=10.1101/gad.827000; PubMed=10783165 [NCBI, ExPASy, EBI, Israel, Japan] Wang Y., Cortez D., Yazdi P., Neff N., Elledge S.J., Qin J.; "BASC, a super complex of BRCA1-associated proteins involved in the recognition and repair of aberrant DNA structures."; Genes Dev. 14:927-939(2000).
[19]	INTERACTION WITH EXO1, AND TISSUE SPECIFICITY. DOI=10.1016/S0921-8777(00)00012-4; PubMed=10856833 [NCBI, ExPASy, EBI, Israel, Japan] Rasmussen L.J., Rasmussen M., Lee B.-I., Rasmussen A.K., Wilson D.M. III, Nielsen F.C., Bisgaard H.C.; "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. 460:41-52(2000).
[20]	FUNCTION. DOI=10.1074/jbc.275.6.3922; PubMed=10660545 [NCBI, ExPASy, EBI, Israel, Japan] Gradia S., Acharya S., Fishel R.; "The role of mismatched nucleotides in activating the hMSH2-hMSH6 molecular switch."; J. Biol. Chem. 275:3922-3930(2000).
[21]	INTERACTION WITH EXO1. DOI=10.1074/jbc.M102670200; PubMed=11427529 [NCBI, ExPASy, EBI, Israel, Japan] Schmutte C., Sadoff M.M., Shim K.-S., Acharya S., Fishel R.; "The interaction of DNA mismatch repair proteins with human exonuclease I."; J. Biol. Chem. 276:33011-33018(2001).
[22]	INTERACTION WITH EXO1. DOI=10.1038/sj.onc.1204467; PubMed=11429708 [NCBI, ExPASy, EBI, Israel, Japan] Jaeger A.C., Rasmussen M., Bisgaard H.C., Singh K.K., Nielsen F.C., Rasmussen L.J.; "HNPCC mutations in the human DNA mismatch repair gene hMLH1 influence assembly of hMutLalpha and hMLH1-hEXO1 complexes."; Oncogene 20:3590-3595(2001).
[23]	INTERACTION WITH EXO1. PubMed=12414623 [NCBI, ExPASy, EBI, Israel, Japan] Sun X., Zheng L., Shen B.; "Functional alterations of human exonuclease 1 mutants identified in atypical hereditary nonpolyposis colorectal cancer syndrome."; Cancer Res. 62:6026-6030(2002).
[24]	INTERACTION WITH ATR, AND IDENTIFICATION BY MASS SPECTROMETRY. DOI=10.1073/pnas.2536810100; PubMed=14657349 [NCBI, ExPASy, EBI, Israel, Japan] Wang Y., Qin J.; "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. 100:15387-15392(2003).
[25]	INTERACTION WITH EXO1. DOI=10.1038/sj.onc.1207265; PubMed=14676842 [NCBI, ExPASy, EBI, Israel, Japan] Nielsen F.C., Jaeger A.C., Luetzen A., Bundgaard J.R., Rasmussen L.J.; "Characterization of human exonuclease 1 in complex with mismatch repair proteins, subcellular localization and association with PCNA."; Oncogene 23:1457-1468(2004).
[26]	FUNCTION. DOI=10.1038/sj.onc.1207462; PubMed=15064730 [NCBI, ExPASy, EBI, Israel, Japan] Yang Q., Zhang R., Wang X.W., Linke S.P., Sengupta S., Hickson I.D., Pedrazzi G., Perrera C., Stagljar I., Littman S.J., Modrich P., Harris C.C.; "The mismatch DNA repair heterodimer, hMSH2/6, regulates BLM helicase."; Oncogene 23:3749-3756(2004).
[27]	PHOSPHORYLATION BY PRKCZ. DOI=10.1016/j.jmb.2005.02.001; PubMed=15808853 [NCBI, ExPASy, EBI, Israel, Japan] Hernandez-Pigeon H., Quillet-Mary A., Louat T., Schambourg A., Humbert O., Selves J., Salles B., Laurent G., Lautier D.; "hMutS alpha is protected from ubiquitin-proteasome-dependent degradation by atypical protein kinase C zeta phosphorylation."; J. Mol. Biol. 348:63-74(2005).
[28]	FUNCTION. DOI=10.1038/sj.jid.5700941; PubMed=17611581 [NCBI, ExPASy, EBI, Israel, Japan] Seifert M., Scherer S.J., Edelmann W., Bohm M., Meineke V., Lobrich M., Tilgen W., Reichrath J.; "The DNA-mismatch repair enzyme hMSH2 modulates UV-B-induced cell cycle arrest and apoptosis in melanoma cells."; J. Invest. Dermatol. 128:203-213(2008).
[29]	REVIEW. DOI=10.1016/0168-9525(94)90093-0; PubMed=8036718 [NCBI, ExPASy, EBI, Israel, Japan] Jiricny J.; "Colon cancer and DNA repair: have mismatches met their match?"; Trends Genet. 10:164-168(1994).
[30]	REVIEW ON VARIANTS. DOI=10.1002/(SICI)1098-1004(1997)10:2<89::AID-HUMU1>3.3.CO;2-K; PubMed=9259192 [NCBI, ExPASy, EBI, Israel, Japan] Papadopoulos N., Lindblom A.; "Molecular basis of HNPCC: mutations of MMR genes."; Hum. Mutat. 10:89-99(1997).
[31]	REVIEW. DOI=10.1007/s10735-006-9062-5; PubMed=17080293 [NCBI, ExPASy, EBI, Israel, Japan] Seifert M., Reichrath J.; "The role of the human DNA mismatch repair gene hMSH2 in DNA repair, cell cycle control and apoptosis: implications for pathogenesis, progression and therapy of cancer."; J. Mol. Histol. 37:301-307(2006).
[32]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-860, AND MASS SPECTROMETRY. DOI=10.1126/science.1140321; PubMed=17525332 [NCBI, ExPASy, EBI, Israel, Japan] Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.; "ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."; Science 316:1160-1166(2007).
[33]	IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY. Colinge J., Superti-Furga G., Bennett K.L.; Submitted (OCT-2008) to UniProtKB.
[34]	X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS). DOI=10.1016/j.molcel.2007.04.018; PubMed=17531815 [NCBI, ExPASy, EBI, Israel, Japan] Warren J.J., Pohlhaus T.J., Changela A., Iyer R.R., Modrich P.L., Beese L.S.; "Structure of the human MutSalpha DNA lesion recognition complex."; Mol. Cell 26:579-592(2007).
[35]	VARIANT HNPCC1 ASN-596 DEL. PubMed=7874129 [NCBI, ExPASy, EBI, Israel, Japan] Mary J.-L., Bishop T., Kolodner R.D., Lipford J.R., Kane M.F., Weber W., Torhorst J., Mueller H., Spycher M., Scott R.J.; "Mutational analysis of the hMSH2 gene reveals a three base pair deletion in a family predisposed to colorectal cancer development."; Hum. Mol. Genet. 3:2067-2069(1994).
[36]	VARIANTS PHE-390 AND LYS-419. PubMed=8690195 [NCBI, ExPASy, EBI, Israel, Japan] Konishi M., Kikuchi-Yanoshita R., Tanaka K., Muraoka M., Onda A., Okumura Y., Kishi N., Iwama T., Mori T., Koike M., Ushio K., Chiba M., Nomizu S., Konishi F., Utsunomiya J., Miyaki M.; "Molecular nature of colon tumors in hereditary nonpolyposis colon cancer, familial polyposis, and sporadic colon cancer."; Gastroenterology 111:307-317(1996).
[37]	VARIANT ASP-322. DOI=10.1007/BF02265276; PubMed=8566964 [NCBI, ExPASy, EBI, Israel, Japan] Maliaka Y.K., Chudina A.P., Belev N.F., Alday P., Bochkov N.P., Buerstedde J.-M.; "CpG dinucleotides in the hMSH2 and hMLH1 genes are hotspots for HNPCC mutations."; Hum. Genet. 97:251-255(1996).
[38]	VARIANT HNPCC1 ASN-596 DEL, AND VARIANT HIS-167. DOI=10.1093/hmg/5.9.1245; PubMed=8872463 [NCBI, ExPASy, EBI, Israel, Japan] Moslein G., Tester D.J., Lindor N.M., Honchel R., Cunningham J.M., French A.J., Halling K.C., Schwab M., Goretzki P., Thibodeau S.N.; "Microsatellite instability and mutation analysis of hMSH2 and hMLH1 in patients with sporadic, familial and hereditary colorectal cancer."; Hum. Mol. Genet. 5:1245-1252(1996).
[39]	VARIANT CRC TYR-506. DOI=10.1093/jnci/88.18.1317; PubMed=8797773 [NCBI, ExPASy, EBI, Israel, Japan] Han H.-J., Yuan Y., Ku J.-L., Oh J.-H., Won Y.-J., Kang K.J., Kim K.Y., Kim S., Kim C.Y., Kim J.-P., Oh N.-G., Lee K.H., Choe K.J., Nakamura Y., Park J.-G.; "Germline mutations of hMLH1 and hMSH2 genes in Korean hereditary nonpolyposis colorectal cancer."; J. Natl. Cancer Inst. 88:1317-1319(1996).
[40]	VARIANT HNPCC1 GLN-46. PubMed=8700523 [NCBI, ExPASy, EBI, Israel, Japan] Bubb V.J., Curtis L.J., Cunningham C., Dunlop M.G., Carothers A.D., Morris R.G., White S., Bird C.C., Wyllie A.H.; "Microsatellite instability and the role of hMSH2 in sporadic colorectalcancer."; Oncogene 12:2641-2649(1996).
[41]	VARIANTS HNPCC1 THR-305; ASN-596 DEL AND THR-834. PubMed=9311737 [NCBI, ExPASy, EBI, Israel, Japan] Wijnen J., Khan P.M., Vasen H., van der Klift H., Mulder A., van Leeuwen-Cornelisse I., Bakker B., Losekoot M., Moeller P., Fodde R.; "Hereditary nonpolyposis colorectal cancer families not complying with the Amsterdam criteria show extremely low frequency of mismatch-repair-gene mutations."; Am. J. Hum. Genet. 61:329-335(1997).
[42]	VARIANT HNPCC1 CYS-323. DOI=10.1006/bbrc.1997.6942; PubMed=9240418 [NCBI, ExPASy, EBI, Israel, Japan] Akiyama Y., Tsubouchi N., Yuasa Y.; "Frequent somatic mutations of hMSH3 with reference to microsatellite instability in hereditary nonpolyposis colorectal cancers."; Biochem. Biophys. Res. Commun. 236:248-252(1997).
[43]	VARIANTS HNPCC1 THR-110; ARG-639; LYS-647; HIS-656; THR-679; VAL-729 AND ILE-732. PubMed=9419403 [NCBI, ExPASy, EBI, Israel, Japan] Nakahara M., Yokozaki H., Yasui W., Dohi K., Tahara E.; "Identification of concurrent germ-line mutations in hMSH2 and/or hMLH1 in Japanese hereditary nonpolyposis colorectal cancer kindreds."; Cancer Epidemiol. Biomarkers Prev. 6:1057-1064(1997).
[44]	VARIANT SER-596. DOI=10.1002/(SICI)1098-2264(199701)18:1<8::AID-GCC2>3.0.CO;2-7; PubMed=8993976 [NCBI, ExPASy, EBI, Israel, Japan] Viel A., Genuardi M., Capozzi E., Leonardi F., Bellacosa A., Paravatou-Petsotas M., Pomponi M.G., Fornasarig M., Percesepe A., Roncucci L., Tamassia M.G., Benatti P., Ponz de Leon M., Valenti A., Covino M., Anti M., Foletto M., Boiocchi M., Neri G.; "Characterization of MSH2 and MLH1 mutations in Italian families with hereditary nonpolyposis colorectal cancer."; Genes Chromosomes Cancer 18:8-18(1997).
[45]	VARIANT ASP-322. DOI=10.1002/(SICI)1098-2264(199704)18:4<269::AID-GCC4>3.3.CO;2-9; PubMed=9087566 [NCBI, ExPASy, EBI, Israel, Japan] Wu Y., Nystroem-Lahti M., Osinga J., Looman M.W.G., Peltomaeki P., Aaltonen L.A., de la Chapelle A., Hofstra R.M.W., Buys C.H.C.M.; "MSH2 and MLH1 mutations in sporadic replication error-positive colorectal carcinoma as assessed by two-dimensional DNA electrophoresis."; Genes Chromosomes Cancer 18:269-278(1997).
[46]	VARIANT HNPCC1 VAL-562. DOI=10.1007/s004390050343; PubMed=9048925 [NCBI, ExPASy, EBI, Israel, Japan] Beck N.E., Tomlinson I.P.M., Homfray T., Frayling I., Hodgson S.V., Harocopos C.J., Bodmer W.F.; "Use of SSCP analysis to identify germline mutations in HNPCC families fulfilling the Amsterdam criteria."; Hum. Genet. 99:219-224(1997).
[47]	VARIANT HNPCC1 PHE-697, AND VARIANT ASP-322. DOI=10.1002/(SICI)1098-1004(1997)10:3<241::AID-HUMU12>3.3.CO;2-3; PubMed=9298827 [NCBI, ExPASy, EBI, Israel, Japan] Wehner M., Buschhausen L., Lamberti C., Kruse R., Caspari R., Propping P., Friedl W.; "Hereditary nonpolyposis colorectal cancer (HNPCC): eight novel germline mutations in hMSH2 or hMLH1 genes."; Hum. Mutat. 10:241-244(1997).
[48]	VARIANT HNPCC1 265-VAL--GLN-314 DEL, AND VARIANTS GLY-641 AND VAL-770. DOI=10.1086/301996; PubMed=9718327 [NCBI, ExPASy, EBI, Israel, Japan] Farrington S.M., Lin-Goerke J., Ling J., Wang Y., Burczak J.D., Robbins D.J., Dunlop M.G.; "Systematic analysis of hMSH2 and hMLH1 in young colon cancer patients and controls."; Am. J. Hum. Genet. 63:749-759(1998).
[49]	VARIANT GLIOMA ARG-199. PubMed=9777949 [NCBI, ExPASy, EBI, Israel, Japan] Leung S.Y., Chan T.L., Chung L.P., Chan A.S.Y., Fan Y.W., Hung K.N., Kwong W.K., Ho J.W.C., Yuen S.T.; "Microsatellite instability and mutation of DNA mismatch repair genes in gliomas."; Am. J. Pathol. 153:1181-1188(1998).
[50]	VARIANT CRC TYR-506, AND VARIANT HNPCC1 ILE-688. DOI=10.1007/BF02235756; PubMed=9559627 [NCBI, ExPASy, EBI, Israel, Japan] Yuan Y., Han H.-J., Zheng S., Park J.-G.; "Germline mutations of hMLH1 and hMSH2 genes in patients with suspected hereditary nonpolyposis colorectal cancer and sporadic early-onset colorectal cancer."; Dis. Colon Rectum 41:434-440(1998).
[51]	VARIANT ASP-322. DOI=10.1016/S0959-8049(98)00217-2; PubMed=10023327 [NCBI, ExPASy, EBI, Israel, Japan] Liu T., Stathopoulos P., Lindblom P., Rubio C., Wasteson Arver B., Iselius L., Holmberg E., Groenberg H., Lindblom A.; "MSH2 codon 322 Gly to Asp seems not to confer an increased risk for colorectal cancer susceptibility."; Eur. J. Cancer 34:1981-1981(1998).
[52]	VARIANT PHE-390. DOI=10.1007/s100380050057; PubMed=9621522 [NCBI, ExPASy, EBI, Israel, Japan] Okamura S., Koyama K., Miyoshi Y., Monden M., Takami M.; "Novel germline mutations of hMSH2 in a patient with hereditary nonpolyposis colorectal cancer 'HNPCC' and in a patient with six primary cancers."; J. Hum. Genet. 43:143-145(1998).
[53]	VARIANTS HNPCC1 SER-336 AND ASN-596 DEL. DOI=10.1002/(SICI)1097-0142(19990615)85:12<2512::AID-CNCR4>3.0.CO;2-G; PubMed=10375096 [NCBI, ExPASy, EBI, Israel, Japan] Heinimann K., Scott R.J., Buerstedde J.-M., Weber W., Siebold K., Attenhofer M., Mueller H., Dobbie Z.; "Influence of selection criteria on mutation detection in patients with hereditary nonpolyposis colorectal cancer."; Cancer 85:2512-2518(1999).
[54]	CHARACTERIZATION OF VARIANTS ASP-322; PHE-390; LYS-419; TYR-506; PRO-524; LEU-622 AND PHE-697. DOI=10.1016/S0960-9822(99)80396-0; PubMed=10469597 [NCBI, ExPASy, EBI, Israel, Japan] Drotschmann K., Clark A.B., Kunkel T.A.; "Mutator phenotypes of common polymorphisms and missense mutations in MSH2."; Curr. Biol. 9:907-910(1999).
[55]	VARIANTS HNPCC1 GLN-246; ASP-322; SER-596 AND THR-834. DOI=10.1038/sj.ejhg.5200363; PubMed=10573010 [NCBI, ExPASy, EBI, Israel, Japan] Genuardi M., Carrara S., Anti M., Ponz de Leon M., Viel A.; "Assessment of pathogenicity criteria for constitutional missense mutations of the hereditary nonpolyposis colorectal cancer genes MLH1 and MSH2."; Eur. J. Hum. Genet. 7:778-782(1999).
[56]	VARIANT HNPCC1 PHE-390. DOI=10.1001/jama.281.24.2316; PubMed=10386556 [NCBI, ExPASy, EBI, Israel, Japan] Weber T.K., Chin H.-M., Rodriguez-Bigas M., Keitz B., Gilligan R., O'Malley L., Urf E., Diba N., Pazik J., Petrelli N.J.; "Novel hMLH1 and hMSH2 germline mutations in African Americans with colorectal cancer."; JAMA 281:2316-2320(1999).
[57]	VARIANT HNPCC1 PRO-636. PubMed=10528862 [NCBI, ExPASy, EBI, Israel, Japan] Yuan Z.Q., Wong N., Foulkes W.D., Alpert L., Manganaro F., Andreutti-Zaugg C., Iggo R., Anthony K., Hsieh E., Redston M., Pinsky L., Trifiro M., Gordon P.H., Lasko D.; "A missense mutation in both hMSH2 and APC in an Ashkenazi Jewish HNPCC kindred: implications for clinical screening."; J. Med. Genet. 36:792-793(1999).
[58]	VARIANTS HNPCC1 ILE-688 AND GLU-845, AND VARIANT MET-8. DOI=10.1006/bbrc.2000.2547; PubMed=10777691 [NCBI, ExPASy, EBI, Israel, Japan] Nomura S., Sugano K., Kashiwabara H., Taniguchi T., Fukayama N., Fujita S., Akasu T., Moriya Y., Ohhigashi S., Kakizoe T., Sekiya T.; "Enhanced detection of deleterious and other germline mutations of hMSH2 and hMLH1 in Japanese hereditary nonpolyposis colorectal cancer kindreds."; Biochem. Biophys. Res. Commun. 271:120-129(2000).
[59]	VARIANT ASP-322. DOI=10.1038/sj.ejhg.5200393; PubMed=10713887 [NCBI, ExPASy, EBI, Israel, Japan] Fidalgo P., Almeida M.R., West S., Gaspar C., Maia L., Wijnen J., Albuquerque C., Curtis A., Cravo M., Fodde R., Leitao C.N., Burn J.; "Detection of mutations in mismatch repair genes in Portuguese families with hereditary non-polyposis colorectal cancer (HNPCC) by a multi-method approach."; Eur. J. Hum. Genet. 8:49-53(2000).
[60]	VARIANTS HNPCC1 ARG-692 AND ARG-697. DOI=10.1002/(SICI)1098-1004(200001)15:1<116::AID-HUMU24>3.0.CO;2-Q; PubMed=10612836 [NCBI, ExPASy, EBI, Israel, Japan] Isidro G., Veiga I., Matos P., Almeida S., Bizarro S., Marshall B., Baptista M., Leite J., Regateiro F., Soares J., Castedo S., Boavida M.G.; "Four novel MSH2 / MLH1 gene mutations in Portuguese HNPCC families."; Hum. Mutat. 15:116-116(2000).
[61]	VARIANT HNPCC1 ASN-603, AND VARIANT ASP-322. PubMed=10829038 [NCBI, ExPASy, EBI, Israel, Japan] Salovaara R., Loukola A., Kristo P., Kaeaeriaeinen H., Ahtola H., Eskelinen M., Haerkoenen N., Julkunen R., Kangas E., Ojala S., Tulikoura J., Valkamo E., Jaervinen H., Mecklin J.-P., Aaltonen L.A., de la Chapelle A.; "Population-based molecular detection of hereditary nonpolyposis colorectal cancer."; J. Clin. Oncol. 18:2193-2200(2000).
[62]	ERRATUM. Salovaara R., Loukola A., Kristo P., Kaeaeriaeinen H., Ahtola H., Eskelinen M., Haerkoenen N., Julkunen R., Kangas E., Ojala S., Tulikoura J., Valkamo E., Jaervinen H., Mecklin J.-P., Aaltonen L.A., de la Chapelle A.; J. Clin. Oncol. 18:3456-3456(2000).
[63]	VARIANTS GASTRIC CANCER PHE-17; GLU-824; ALA-868; GLY-870 AND GLY-873, AND VARIANTS HNPCC1 CYS-98; TYR-323; ILE-335; ARG-629 AND VAL-714. PubMed=12132870 [NCBI, ExPASy, EBI, Israel, Japan] Kim J.C., Kim H.C., Roh S.A., Koo K.H., Lee D.H., Yu C.S., Lee J.H., Kim T.W., Lee H.I., Beck N.E., Bodmer W.F.; "hMLH1 and hMSH2 mutations in families with familial clustering of gastric cancer and hereditary non-polyposis colorectal cancer."; Cancer Detect. Prev. 25:503-510(2001).
[64]	VARIANTS HNPCC1 ASP-161; VAL-216 AND ARG-554. PubMed=11726306 [NCBI, ExPASy, EBI, Israel, Japan] Mueller-Koch Y., Kopp R., Lohse P., Baretton G., Stoetzer A., Aust D., Daum J., Kerker B., Gross M., Dietmeier W., Holinski-Feder E.; "Sixteen rare sequence variants of the hMLH1 and hMSH2 genes found in a cohort of 254 suspected HNPCC (hereditary non-polyposis colorectal cancer) patients: mutations or polymorphisms?"; Eur. J. Med. Res. 6:473-482(2001).
[65]	CHARACTERIZATION OF VARIANTS ASP-322; LEU-622 AND TYR-639. DOI=10.1093/hmg/10.18.1889; PubMed=11555625 [NCBI, ExPASy, EBI, Israel, Japan] Ellison A.R., Lofing J., Bitter G.A.; "Functional analysis of human MLH1 and MSH2 missense variants and hybrid human-yeast MLH1 proteins in Saccharomyces cerevisiae."; Hum. Mol. Genet. 10:1889-1900(2001).
[66]	VARIANT HNPCC1 VAL-813. DOI=10.1038/sj.bjc.6600565; PubMed=12373605 [NCBI, ExPASy, EBI, Israel, Japan] Gille J.J.P., Hogervorst F.B.L., Pals G., Wijnen J.T., van Schooten R.J., Dommering C.J., Meijer G.A., Craanen M.E., Nederlof P.M., de Jong D., McElgunn C.J., Schouten J.P., Menko F.H.; "Genomic deletions of MSH2 and MLH1 in colorectal cancer families detected by a novel mutation detection approach."; Br. J. Cancer 87:892-897(2002).
[67]	VARIANTS HNPCC1 VAL-600 AND PHE-723. DOI=10.1002/cncr.10332.abs; PubMed=11920458 [NCBI, ExPASy, EBI, Israel, Japan] Furukawa T., Konishi F., Shitoh K., Kojima M., Nagai H., Tsukamoto T.; "Evaluation of screening strategy for detecting hereditary nonpolyposis colorectal carcinoma."; Cancer 94:911-920(2002).
[68]	VARIANTS HNPCC1 HIS-167; MET-393; PRO-524; ASN-596 DEL; LEU-622; SER-674 AND ARG-905, AND CHARACTERIZATION OF VARIANTS HNPCC1 HIS-167; MET-393; PRO-524; ASN-596 DEL; LEU-622; SER-674 AND ARG-905. DOI=10.1016/S1535-6108(02)00073-9; PubMed=12124176 [NCBI, ExPASy, EBI, Israel, Japan] Heinen C.D., Wilson T., Mazurek A., Berardini M., Butz C., Fishel R.; "HNPCC mutations in hMSH2 result in reduced hMSH2-hMSH6 molecular switch functions."; Cancer Cell 1:469-478(2002).
[69]	INVOLVEMENT IN MULTIPLE CAFE-AU-LAIT SPOTS WITH LEUKEMIA. PubMed=11809679 [NCBI, ExPASy, EBI, Israel, Japan] Whiteside D., McLeod R., Graham G., Steckley J.L., Booth K., Somerville M.J., Andrew S.E.; "A homozygous germ-line mutation in the human MSH2 gene predisposes to hematological malignancy and multiple cafe-au-lait spots."; Cancer Res. 62:359-362(2002).
[70]	VARIANT ASP-322. DOI=10.1136/gut.50.3.405; PubMed=11839723 [NCBI, ExPASy, EBI, Israel, Japan] Cravo M., Afonso A.J., Lage P., Albuquerque C., Maia L., Lacerda C., Fidalgo P., Chaves P., Cruz C., Nobre-Leitao C.; "Pathogenicity of missense and splice site mutations in hMSH2 and hMLH1 mismatch repair genes: implications for genetic testing."; Gut 50:405-412(2002).
[71]	VARIANTS HNPCC1 MET-44; VAL-45; ASN-596 DEL; GLY-886 AND GLU-923. DOI=10.1002/humu.10083; PubMed=12112654 [NCBI, ExPASy, EBI, Israel, Japan] Bisgaard M.L., Jaeger A.C., Myrhoej T., Bernstein I., Nielsen F.C.; "Hereditary non-polyposis colorectal cancer (HNPCC): phenotype-genotype correlation between patients with and without identified mutation."; Hum. Mutat. 20:20-27(2002).
[72]	VARIANTS HNPCC1 ILE-102; ASP-163 AND ALA-564, AND VARIANT ASP-322. DOI=10.1007/s00432-002-0361-2; PubMed=12200596 [NCBI, ExPASy, EBI, Israel, Japan] Ward R., Meldrum C., Williams R., Mokany E., Scott R., Turner J., Hawkins N., Burgess B., Groombridge C., Spigelman A.; "Impact of microsatellite testing and mismatch repair protein expression on the clinical interpretation of genetic testing in hereditary non-polyposis colorectal cancer."; J. Cancer Res. Clin. Oncol. 128:403-411(2002).
[73]	VARIANTS HNPCC1 HIS-167 AND SER-359. PubMed=11870161 [NCBI, ExPASy, EBI, Israel, Japan] Scartozzi M., Bianchi F., Rosati S., Galizia E., Antolini A., Loretelli C., Piga A., Bearzi I., Cellerino R., Porfiri E.; "Mutations of hMLH1 and hMSH2 in patients with suspected hereditary nonpolyposis colorectal cancer: correlation with microsatellite instability and abnormalities of mismatch repair protein expression."; J. Clin. Oncol. 20:1203-1208(2002).
[74]	VARIANTS HNPCC1 LEU-92 DEL AND ALA-853, AND VARIANT ASP-322. DOI=10.1136/jmg.39.10.e65; PubMed=12362047 [NCBI, ExPASy, EBI, Israel, Japan] Kurzawski G., Suchy J., Kladny J., Safranow K., Jakubowska A., Elsakov P., Kucinskas V., Gardovski J., Irmejs A., Sibul H., Huzarski T., Byrski T., Debniak T., Cybulski C., Gronwald J., Oszurek O., Clark J., Gozdz S., Niepsuj S., Slomski R., Plawski A., Lacka-Wojciechowska A., Rozmiarek A., Fiszer-Maliszewska L., Bebenek M., Sorokin D., Stawicka M., Godlewski D., Richter P., Brozek I., Wysocka B., Jawien A., Banaszkiewicz Z., Kowalczyk J., Czudowska D., Goretzki P.E., Moeslein G., Lubinski J.; "Germline MSH2 and MLH1 mutational spectrum in HNPCC families from Poland and the Baltic States."; J. Med. Genet. 39:E65-E65(2002).
[75]	VARIANTS HNPCC1 PRO-552; SER-583 AND PRO-636. DOI=10.1086/373963; PubMed=12658575 [NCBI, ExPASy, EBI, Israel, Japan] Wagner A., Barrows A., Wijnen J.T., van der Klift H., Franken P.F., Verkuijlen P., Nakagawa H., Geugien M., Jaghmohan-Changur S., Breukel C., Meijers-Heijboer H., Morreau H., van Puijenbroek M., Burn J., Coronel S., Kinarski Y., Okimoto R., Watson P., Lynch J.F., de la Chapelle A., Lynch H.T., Fodde R.; "Molecular analysis of hereditary nonpolyposis colorectal cancer in the United States: high mutation detection rate among clinically selected families and characterization of an American founder genomic deletion of the MSH2 gene."; Am. J. Hum. Genet. 72:1088-1100(2003).
[76]	VARIANTS COLORECTAL CANCER ILE-13 AND ILE-342, AND VARIANT ASP-322. DOI=10.1093/annonc/mdg402; PubMed=14504054 [NCBI, ExPASy, EBI, Israel, Japan] Colombino M., Cossu A., Arba A., Manca A., Curci A., Avallone A., Comella G., Botti G., Scintu F., Amoruso M., D'Abbicco D., d'Agnessa M.R., Spanu A., Tanda F., Palmieri G.; "Microsatellite instability and mutation analysis among southern Italian patients with colorectal carcinoma: detection of different alterations accounting for MLH1 and MSH2 inactivation in familial cases."; Ann. Oncol. 14:1530-1536(2003).
[77]	VARIANT HNPCC1 SER-127. DOI=10.1002/humu.9123; PubMed=12655564 [NCBI, ExPASy, EBI, Israel, Japan] Chen-Shtoyerman R., Theodor L., Harmati E., Friedman E., Dacka S., Kopelman Y., Sternberg A., Zarivach R., Bar-Meir S., Fireman Z.; "Genetic analysis of familial colorectal cancer in Israeli Arabs."; Hum. Mutat. 21:446-447(2003).
[78]	VARIANT HNPCC1 PRO-175. DOI=10.1002/humu.9127; PubMed=12655568 [NCBI, ExPASy, EBI, Israel, Japan] Bartosova Z., Fridrichova I., Bujalkova M., Wolf B., Ilencikova D., Krizan P., Hlavcak P., Palaj J., Lukac L., Lukacova M., Boeoer A., Haider R., Jiricny J., Nystroem-Lahti M., Marra G.; "Novel MLH1 and MSH2 germline mutations in the first HNPCC families identified in Slovakia."; Hum. Mutat. 21:449-449(2003).
[79]	VARIANTS HNPCC1 GLY-163 AND GLY-660. DOI=10.1002/humu.10291; PubMed=14635101 [NCBI, ExPASy, EBI, Israel, Japan] Taylor C.F., Charlton R.S., Burn J., Sheridan E., Taylor G.R.; "Genomic deletions in MSH2 or MLH1 are a frequent cause of hereditary non-polyposis colorectal cancer: identification of novel and recurrent deletions by MLPA."; Hum. Mutat. 22:428-433(2003).
[80]	VARIANTS CRC MET-8; SER-40; VAL-169; ARG-203; PHE-390; LYS-419; CYS-619 AND ARG-629. PubMed=12792735 [NCBI, ExPASy, EBI, Israel, Japan] Yamada K., Zhong X., Kanazawa S., Koike J., Tsujita K., Hemmi H.; "Oncogenic pathway of sporadic colorectal cancer with novel germline missense mutations in the hMSH2 gene."; Oncol. Rep. 10:859-866(2003).
[81]	VARIANT HNPCC1 THR-931. PubMed=15046096 [NCBI, ExPASy, EBI, Israel, Japan] Sun M.H., Cai Q., Fu G., Ren S., Mo S., Xu Y., Ding C., Zhang T., Zhu X., Xu X., Min D., Cai S., Luo D., Shi Y., Shi D.; "Gene symbol: hMSH2. Disease: hereditary nonpolyposis colorectal cancer."; Hum. Genet. 114:409-409(2004).
[82]	VARIANT HNPCC1 TYR-671. DOI=10.1002/humu.9267; PubMed=15300854 [NCBI, ExPASy, EBI, Israel, Japan] Sharp A., Pichert G., Lucassen A., Eccles D.; "RNA analysis reveals splicing mutations and loss of expression defects in MLH1 and BRCA1."; Hum. Mutat. 24:272-272(2004).
[83]	VARIANTS HNPCC1 LEU-440 DEL; TYR-506; ARG-629 AND ILE-688. DOI=10.1002/humu.9277; PubMed=15365995 [NCBI, ExPASy, EBI, Israel, Japan] Shin Y.-K., Heo S.-C., Shin J.-H., Hong S.-H., Ku J.-L., Yoo B.-C., Kim I.-J., Park J.-G.; "Germline mutations in MLH1, MSH2 and MSH6 in Korean hereditary non-polyposis colorectal cancer families."; Hum. Mutat. 24:351-351(2004).
[84]	VARIANT HNPCC1 ARG-839, AND VARIANT ARG-629. DOI=10.1093/jjco/hyh121; PubMed=15613555 [NCBI, ExPASy, EBI, Israel, Japan] Yuan Y., Huang Y.-Q., Cai S.-R., Song Y.-M., Zheng S., Zhang S.-Z.; "Genetic characterization of Chinese hereditary non-polyposis colorectal cancer by DHPLC and multiplex PCR."; Jpn. J. Clin. Oncol. 34:660-666(2004).
[85]	VARIANTS HNPCC1 LEU-349 AND ASN-596 DEL. DOI=10.1136/jmg.2004.020651; PubMed=15342696 [NCBI, ExPASy, EBI, Israel, Japan] Domingo E., Laiho P., Ollikainen M., Pinto M., Wang L., French A.J., Westra J., Frebourg T., Espin E., Armengol M., Hamelin R., Yamamoto H., Hofstra R.M.W., Seruca R., Lindblom A., Peltomaeki P., Thibodeau S.N., Aaltonen L.A., Schwartz S. Jr.; "BRAF screening as a low-cost effective strategy for simplifying HNPCC genetic testing."; J. Med. Genet. 41:664-668(2004).
[86]	VARIANT HNPCC1 PHE-93. DOI=10.1016/j.canlet.2004.09.051; PubMed=15896463 [NCBI, ExPASy, EBI, Israel, Japan] Baudi F., Fersini G., Lavecchia A., Terracciano R., Leone F., Quaresima B., Faniello M.C., De Paola L., Doldo P., Cuda G., Costanzo F., Venuta S.; "A novel missense germline mutation in exon 2 of the hMSH2 gene in a HNPCC family from Southern Italy."; Cancer Lett. 223:285-291(2005).
[87]	VARIANTS HNPCC1 VAL-169; PHE-390; ALA-564 AND ARG-629, AND VARIANT CRC LYS-419. DOI=10.1111/j.1399-0004.2005.00469.x; PubMed=15996210 [NCBI, ExPASy, EBI, Israel, Japan] Lee S.-C., Guo J.-Y., Lim R., Soo R., Koay E., Salto-Tellez M., Leong A., Goh B.-C.; "Clinical and molecular characteristics of hereditary non-polyposis colorectal cancer families in Southeast Asia."; Clin. Genet. 68:137-145(2005).
[88]	VARIANT HNPCC1 TYR-283. DOI=10.1038/sj.ejhg.5201421; PubMed=15870828 [NCBI, ExPASy, EBI, Israel, Japan] Wehner M., Mangold E., Sengteller M., Friedrichs N., Aretz S., Friedl W., Propping P., Pagenstecher C.; "Hereditary nonpolyposis colorectal cancer: pitfalls in deletion screening in MSH2 and MLH1 genes."; Eur. J. Hum. Genet. 13:983-986(2005).
[89]	VARIANT HNPCC1 ARG-162. PubMed=15991316 [NCBI, ExPASy, EBI, Israel, Japan] Kohonen-Corish M.R.J., Otway R., Tetlow N., Hornby J., Doe W.F.; "Gene symbol: MSH2. Disease: hereditary nonpolyposis colorectal cancer."; Hum. Genet. 116:539-539(2005).
[90]	VARIANTS HNPCC1 THR-2; LEU-92 DEL; MET-145; PHE-390 AND ALA-853, AND VARIANT ASP-322. DOI=10.1111/j.1399-0004.2006.00550.x; PubMed=16451135 [NCBI, ExPASy, EBI, Israel, Japan] Kurzawski G., Suchy J., Lener M., Klujszo-Grabowska E., Kladny J., Safranow K., Jakubowska K., Jakubowska A., Huzarski T., Byrski T., Debniak T., Cybulski C., Gronwald J., Oszurek O., Oszutowska D., Kowalska E., Gozdz S., Niepsuj S., Slomski R., Plawski A., Lacka-Wojciechowska A., Rozmiarek A., Fiszer-Maliszewska L., Bebenek M., Sorokin D., Sasiadek M.M., Stembalska A., Grzebieniak Z., Kilar E., Stawicka M., Godlewski D., Richter P., Brozek I., Wysocka B., Limon J., Jawien A., Banaszkiewicz Z., Janiszewska H., Kowalczyk J., Czudowska D., Scott R.J., Lubinski J.; "Germline MSH2 and MLH1 mutational spectrum including large rearrangements in HNPCC families from Poland (update study)."; Clin. Genet. 69:40-47(2006).
[91]	VARIANTS HNPCC1 PRO-33; ASP-161; ARG-162; ARG-164; PRO-173; PRO-187; TYR-333; ASN-603; PRO-636; PHE-697; 745-ILE-ILE-746 DEL AND LYS-749, VARIANTS VAL-272; THR-834 AND GLU-923, CHARACTERIZATION OF VARIANTS HNPCC1 PRO-33; ASP-161; ARG-162; ARG-164; PRO-173; PRO-187; TYR-333; ASN-603; PRO-636; PHE-697; 745-ILE-ILE-746 DEL AND LYS-749, AND CHARACTERIZATION OF VARIANTS VAL-272; THR-834 AND GLU-923. DOI=10.1053/j.gastro.2006.08.044; PubMed=17101317 [NCBI, ExPASy, EBI, Israel, Japan] Ollila S., Sarantaus L., Kariola R., Chan P., Hampel H., Holinski-Feder E., Macrae F., Kohonen-Corish M., Gerdes A.-M., Peltomaeki P., Mangold E., de la Chapelle A., Greenblatt M., Nystroem M.; "Pathogenicity of MSH2 missense mutations is typically associated with impaired repair capability of the mutated protein."; Gastroenterology 131:1408-1417(2006).
[92]	VARIANT HNPCC1 ALA-162. PubMed=17128465 [NCBI, ExPASy, EBI, Israel, Japan] Leonardis D.; "Gene symbol: msh2. Disease: hereditary nonpolyposis colorectal cancer."; Hum. Genet. 119:675-675(2006).
[93]	VARIANTS GLN-46; LYS-106; ASP-322; SER-596; LEU-670; ILE-779; SER-807; HIS-835 AND ARG-911. DOI=10.1002/humu.20635; PubMed=18033691 [NCBI, ExPASy, EBI, Israel, Japan] Barnetson R.A., Cartwright N., van Vliet A., Haq N., Drew K., Farrington S., Williams N., Warner J., Campbell H., Porteous M.E., Dunlop M.G.; "Classification of ambiguous mutations in DNA mismatch repair genes identified in a population-based study of colorectal cancer."; Hum. Mutat. 29:367-374(2008).
[94]	MUTAGENESIS OF GLY-674, CHARACTERIZATION OF VARIANTS HNPCC1 PRO-33; SER-127; ASP-161; ARG-162; ARG-164; PRO-173; PRO-187; TYR-333; ASN-603; PRO-636; PHE-697; 745-ILE-ILE-746 DEL; LYS-749; THR-834 AND GLU-923, AND CHARACTERIZATION OF VARIANTS VAL-272 AND ASP-322. DOI=10.1002/humu.20893; PubMed=18951462 [NCBI, ExPASy, EBI, Israel, Japan] Ollila S., Dermadi Bebek D., Jiricny J., Nystroem M.; "Mechanisms of pathogenicity in human MSH2 missense mutants."; Hum. Mutat. 29:1355-1363(2008).
[95]	VARIANTS HNPCC1 LEU-92 DEL AND ARG-199, VARIANTS VAL-272; ASP-331; GLU-470; ASN-596 DEL; ASN-610; GLY-638; GLU-645; TYR-671; LEU-696; ARG-697; PHE-723; TYR-748 AND GLN-839, CHARACTERIZATION OF VARIANTS HNPCC1 LEU-92 DEL AND ARG-199, AND CHARACTERIZATION OF VARIANTS VAL-272; ASP-331; GLU-470; ASN-596 DEL; ASN-610; GLY-638; GLU-645; TYR-671; LEU-696; ARG-697; PHE-723; TYR-748 AND GLN-839. DOI=10.1002/humu.20796; PubMed=18561205 [NCBI, ExPASy, EBI, Israel, Japan] Tournier I., Vezain M., Martins A., Charbonnier F., Baert-Desurmont S., Olschwang S., Wang Q., Buisine M.P., Soret J., Tazi J., Frebourg T., Tosi M.; "A large fraction of unclassified variants of the mismatch repair genes MLH1 and MSH2 is associated with splicing defects."; Hum. Mutat. 29:1412-1424(2008).
[96]	CHARACTERIZATION OF VARIANTS HNPCC1 ARG-162; HIS-167 AND SER-359. DOI=10.1002/humu.20875; PubMed=18781619 [NCBI, ExPASy, EBI, Israel, Japan] Belvederesi L., Bianchi F., Galizia E., Loretelli C., Bracci R., Catalani R., Amati M., Cellerino R.; "MSH2 missense mutations and HNPCC syndrome: pathogenicity assessment in a human expression system."; Hum. Mutat. 29:E296-E309(2008).

Comments

FUNCTION: Component of the post-replicative DNA mismatch repair system (MMR). Forms two different heterodimers: MutS alpha (MSH2-MSH6 heterodimer) and MutS beta (MSH2-MSH3 heterodimer) which binds to DNA mismatches thereby initiating DNA repair. When bound, heterodimers bend the DNA helix and shields approximately 20 base pairs. MutS alpha recognizes single base mismatches and dinucleotide insertion-deletion loops (IDL) in the DNA. MutS beta recognizes larger insertion-deletion loops up to 13 nucleotides long. After mismatch binding, MutS alpha or beta forms a ternary complex with the MutL alpha heterodimer, which is thought to be responsible for directing the downstream MMR events, including strand discrimination, excision, and resynthesis. ATP binding and hydrolysis play a pivotal role in mismatch repair functions. The ATPase activity associated with MutS alpha regulates binding similar to a molecular switch: mismatched DNA provokes ADP-->ATP exchange, resulting in a discernible conformational transition that converts MutS alpha into a sliding clamp capable of hydrolysis-independent diffusion along the DNA backbone. This transition is crucial for mismatch repair. MutS alpha may also play a role in DNA homologous recombination repair. In melanocytes may modulate both UV-B-induced cell cycle regulation and apoptosis.
SUBUNIT: Heterodimer consisting of MSH2-MSH6 (MutS alpha) or MSH2-MSH3 (MutS beta). Both heterodimer form a ternary complex with MutL alpha (MLH1-PMS1). Interacts with EXO1. Part of the BRCA1-associated genome surveillance complex (BASC), which contains BRCA1, MSH2, MSH6, MLH1, ATM, BLM, PMS2 and the RAD50-MRE11-NBS1 protein complex. This association could be a dynamic process changing throughout the cell cycle and within subnuclear domains. Interacts with ATR.
INTERACTION:
Self; NbExp=1; IntAct=EBI-355888, EBI-355888;
P39875:EXO1 (xeno); NbExp=1; IntAct=EBI-355888, EBI-6738;
Q9UQ84-1:EXO1; NbExp=2; IntAct=EBI-355888, EBI-944694;
P20585:MSH3; NbExp=1; IntAct=EBI-355888, EBI-1164205;
P52701:MSH6; NbExp=1; IntAct=EBI-355888, EBI-395529;
O75365:PTP4A3; NbExp=1; IntAct=EBI-355888, EBI-1043866;
SUBCELLULAR LOCATION: Nucleus (Potential).
TISSUE SPECIFICITY: Ubiquitously expressed.
PTM: Phosphorylated by PRKCZ, which may prevent MutS alpha degradation by the ubiquitin-proteasome pathway.
PTM: Phosphorylated upon DNA damage, probably by ATM or ATR.
DISEASE: Defects in MSH2 are the cause of hereditary non-polyposis colorectal cancer type 1 (HNPCC1) [MIM:120435]. Mutations in more than one gene locus can be involved alone or in combination in the production of the HNPCC phenotype (also called Lynch syndrome). Most families with clinically recognized HNPCC have mutations in either MLH1 or MSH2 genes. HNPCC is an autosomal, dominantly inherited disease associated with marked increase in cancer susceptibility. It is characterized by a familial predisposition to early onset colorectal carcinoma (CRC) and extra-colonic cancers of the gastrointestinal, urological and female reproductive tracts. HNPCC is reported to be the most common form of inherited colorectal cancer in the Western world. Cancers in HNPCC originate within benign neoplastic polyps termed adenomas. Clinically, HNPCC is often divided into two subgroups. Type I: hereditary predisposition to colorectal cancer, a young age of onset, and carcinoma observed in the proximal colon. Type II: patients have an increased risk for cancers in certain tissues such as the uterus, ovary, breast, stomach, small intestine, skin, and larynx in addition to the colon. Diagnosis of classical HNPCC is based on the Amsterdam criteria: 3 or more relatives affected by colorectal cancer, one a first degree relative of the other two; 2 or more generation affected; 1 or more colorectal cancers presenting before 50 years of age; exclusion of hereditary polyposis syndromes. The term "suspected HNPCC" or "incomplete HNPCC" can be used to describe families who do not or only partially fulfill the Amsterdam criteria, but in whom a genetic basis for colon cancer is strongly suspected. MSH2 mutations may predispose to hematological malignancies and multiple cafe-au-lait spots.
DISEASE: Defects in MSH2 are a cause of Muir-Torre syndrome (MTS) [MIM:158320]. MTS is a rare autosomal dominant disorder characterized by sebaceous neoplasms and visceral malignancy.
DISEASE: Defects in MSH2 are a cause of susceptibility to endometrial cancer [MIM:608089].
SIMILARITY: Belongs to the DNA mismatch repair mutS family.
SEQUENCE CAUTION:
- Sequence=AAC27930.1; Type=Frameshift; Positions=417; Note=The frameshift is caused by a single nucleotide deletion which is found in a HNPCC kindred
WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL="http://atlasgeneticsoncology.org/Genes/MSH2ID340ch2p22.html";.
WEB RESOURCE: Name=GeneReviews; URL="http://www.genetests.org/query?gene=MSH2";.
WEB RESOURCE: Name=Hereditary non-polyposis colorectal cancer db; URL="http://www.nfdht.nl/";.
WEB RESOURCE: Name=NIEHS-SNPs; URL="http://egp.gs.washington.edu/data/msh2/";.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

U03911; AAA18643.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U04045; AAA61870.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U41221; AAA82080.1; ALT_SEQ; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U41206; AAA82080.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U41207; AAA82080.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U41208; AAA82080.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U41210; AAA82080.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U41211; AAA82080.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U41212; AAA82080.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U41213; AAA82080.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U41214; AAA82080.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U41215; AAA82080.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U41216; AAA82080.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U41217; AAA82080.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U41218; AAA82080.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U41219; AAA82080.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U41220; AAA82080.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
L47583; AAB59564.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
L47582; AAB59565.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
L47581; AAA76858.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY601851; AAS99351.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC021566; AAH21566.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF066081; AAC27930.1; ALT_FRAME; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

IPI00017303; -.

I64819; I64819.

NP_000242.1; -.

3D structure databases

PDB

2O8B; X-ray; 2.75 A; A=1-934.	[ExPASy / RCSB / EBI]
2O8C; X-ray; 3.37 A; A=1-934.	[ExPASy / RCSB / EBI]
2O8D; X-ray; 3.00 A; A=1-934.	[ExPASy / RCSB / EBI]
2O8E; X-ray; 3.30 A; A=1-934.	[ExPASy / RCSB / EBI]
2O8F; X-ray; 3.25 A; A=1-934.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

2O8B; -.
2O8C; -.
2O8D; -.
2O8E; -.
2O8F; -.

ModBase

P43246.

Protein-protein interaction databases

IntAct

P43246; 15.

PTM databases

PhosphoSite

P43246; -.

Organism-specific databases

GC02P047541; -.

HIX0022211; -.

HGNC:7325; MSH2.

CAB009572; -.

120435; phenotype. [NCBI / EBI]
158320; phenotype. [NCBI / EBI]
608089; phenotype. [NCBI / EBI]
609309; gene. [NCBI / EBI]

Orphanet

144; Colon cancer, familial nonpolyposis.
587; Muir-Torre syndrome.

PharmGKB

PA31133; -.

Gene expression databases

P43246; -.

P43246; -.

HS_MSH2; -.

ENSG00000095002; Homo sapiens.

Ontologies

GO:0032301;	Cellular component: MutSalpha complex (inferred from direct assay from HGNC).
GO:0032302;	Cellular component: MutSbeta complex (inferred from direct assay from HGNC).
GO:0005524;	Molecular function: ATP binding (inferred from electronic annotation from UniProtKB-KW).
GO:0032137;	Molecular function: guanine/thymine mispair binding (inferred from mutant phenotype from MGI).
GO:0008022;	Molecular function: protein C-terminus binding (inferred from physical interaction from UniProtKB).
GO:0042803;	Molecular function: protein homodimerization activity (inferred from direct assay from HGNC).
GO:0030183;	Biological process: B cell differentiation (inferred from sequence or structural similarity from UniProtKB).
GO:0045190;	Biological process: isotype switching (inferred from sequence or structural similarity from UniProtKB).
GO:0043570;	Biological process: maintenance of DNA repeat elements (inferred from mutant phenotype from HGNC).
GO:0008584;	Biological process: male gonad development (inferred from sequence or structural similarity from UniProtKB).
GO:0006298;	Biological process: mismatch repair (inferred from direct assay from UniProtKB).
GO:0045786;	Biological process: negative regulation of cell cycle (inferred from electronic annotation from UniProtKB-KW).
GO:0045910;	Biological process: negative regulation of DNA recombination (inferred from direct assay from UniProtKB).
GO:0043524;	Biological process: negative regulation of neuron apoptosis (inferred from sequence or structural similarity from UniProtKB).
GO:0051096;	Biological process: positive regulation of helicase activity (inferred from direct assay from UniProtKB).
GO:0006301;	Biological process: postreplication repair (inferred from direct assay from UniProtKB).
GO:0010224;	Biological process: response to UV-B (inferred from sequence or structural similarity from UniProtKB).
GO:0010165;	Biological process: response to X-ray (inferred from sequence or structural similarity from UniProtKB).
QuickGo view.

Family and domain databases

InterPro

IPR011184; DNA_mismatch_repair_MSH2.
IPR007695; DNA_mismatch_repair_MutS-lik_N.
IPR000432; DNA_mismatch_repair_MutS_C.
IPR007861; DNA_mismatch_repair_MutS_clamp.
IPR007860; DNA_mismatch_repair_MutS_connt.
IPR007696; DNA_mismatch_repair_MutS_core.
Graphical view of domain structure.

PANTHER

PTHR11361; MutS_C; 1.

Pfam

PF01624; MutS_I; 1.
PF05188; MutS_II; 1.
PF05192; MutS_III; 1.
PF05190; MutS_IV; 1.
PF00488; MutS_V; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF005813; MSH2; 1.

ProDom

PD001263; MutS_C; 1.
[Domain structure / List of seq. sharing at least 1 domain]

SMART

SM00534; MUTSac; 1.
SM00533; MUTSd; 1.
SMART graphical view of domain structure.

PROSITE

PS00486; DNA_MISMATCH_REPAIR_2; 1.

Proteomic databases

PeptideAtlas

P43246; -.

PRIDE

P43246; -.

Genome annotation databases

Ensembl

ENSG00000095002; Homo sapiens. [Contig view]

GeneID

4436; -.

KEGG

hsa:4436; -.

Phylogenomic databases

HOGENOM

P43246; -.

HOVERGEN

P43246; -.

OMA

P43246; WAISEHI.

Other

17289; -.

MSH2; Homo sapiens.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Anti-oncogene; ATP-binding; Cell cycle; Disease mutation; DNA damage; DNA repair; DNA-binding; Hereditary nonpolyposis colorectal cancer; Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 934`	`934`	`DNA mismatch repair protein Msh2.`	`PRO_0000115183`
`NP_BIND`	`669 676`	`8`	`ATP (Potential).`
`REGION`	`601 671`	`71`	`Interaction with EXO1.`
`MOD_RES`	`860 860`		`Phosphoserine.`
`VARIANT`	`2 2`	`1`	`A -> T (in HNPCC1).`	`VAR_054511`
`VARIANT`	`8 8`	`1`	`T -> M (could be associated with increased colorectal cancer susceptibility; dbSNP:rs17217716 [NCBI]).`	`VAR_013171`
`VARIANT`	`13 13`	`1`	`S -> I (in colorectal cancer).`	`VAR_043736`
`VARIANT`	`17 17`	`1`	`V -> F (in gastric cancer; uncertain pathogenicity; cryptic acceptor splice site suppressed on ex vivo splicing assay).`	`VAR_043737`
`VARIANT`	`33 33`	`1`	`T -> P (in HNPCC1; shows slightly reduced mismatch binding or release efficiency).`	`VAR_043738`
`VARIANT`	`40 40`	`1`	`G -> S (in CRC).`	`VAR_043739`
`VARIANT`	`43 43`	`1`	`Y -> C (in dbSNP:rs17217723 [NCBI]).`	`VAR_019233`
`VARIANT`	`44 44`	`1`	`T -> M (in HNPCC1).`	`VAR_043740`
`VARIANT`	`45 45`	`1`	`A -> V (in HNPCC1).`	`VAR_043741`
`VARIANT`	`46 46`	`1`	`H -> Q (in HNPCC1; dbSNP:rs33946261 [NCBI]).`	`VAR_004470`
`VARIANT`	`92 92`	`1`	`Missing (in HNPCC1; uncertain pathogenicity; has no effect on ex vivo splicing assay).`	`VAR_043742`
`VARIANT`	`93 93`	`1`	`L -> F (in HNPCC1).`	`VAR_043743`
`VARIANT`	`96 96`	`1`	`R -> H.`	`VAR_004471`
`VARIANT`	`98 98`	`1`	`Y -> C (in HNPCC1; uncertain pathogenicity).`	`VAR_043744`
`VARIANT`	`102 102`	`1`	`V -> I (in HNPCC1).`	`VAR_043745`
`VARIANT`	`106 106`	`1`	`R -> K (in dbSNP:rs41295286 [NCBI]).`	`VAR_038026`
`VARIANT`	`110 110`	`1`	`K -> T (in HNPCC1; somatic mutation).`	`VAR_043746`
`VARIANT`	`127 127`	`1`	`N -> S (in HNPCC1; shows no defects; dbSNP:rs17217772 [NCBI]).`	`VAR_019234`
`VARIANT`	`139 139`	`1`	`N -> S (in HNPCC1).`	`VAR_004472`
`VARIANT`	`145 145`	`1`	`I -> M (in HNPCC1).`	`VAR_004473`
`VARIANT`	`161 161`	`1`	`V -> D (in HNPCC1; affects protein stability; associated with an absence of the protein in tumors).`	`VAR_012936`
`VARIANT`	`162 162`	`1`	`G -> A (in HNPCC1).`	`VAR_054512`
`VARIANT`	`162 162`	`1`	`G -> R (in HNPCC1; shows a decreased expression level of the MutS alpha complex and is associated with an abnormal subcellular localization pattern; affects protein stability; associated with an absence of the protein in tumors).`	`VAR_043747`
`VARIANT`	`163 163`	`1`	`V -> D (in HNPCC1).`	`VAR_043748`
`VARIANT`	`163 163`	`1`	`V -> G (in HNPCC1).`	`VAR_022670`
`VARIANT`	`164 164`	`1`	`G -> R (in HNPCC1; affects protein stability; associated with an absence of the protein in tumors).`	`VAR_043749`
`VARIANT`	`167 167`	`1`	`D -> H (in HNPCC1; does not show a decreased expression level of the MutS alpha complex and is not associated with an abnormal subcellular localization pattern; could be a polymorphism).`	`VAR_004474`
`VARIANT`	`169 169`	`1`	`I -> V (in HNPCC1; uncertain pathogenicity).`	`VAR_043750`
`VARIANT`	`173 173`	`1`	`L -> P (in HNPCC1; affects protein stability; associated with an absence of the protein in tumors).`	`VAR_043751`
`VARIANT`	`175 175`	`1`	`L -> P (in HNPCC1).`	`VAR_043752`
`VARIANT`	`187 187`	`1`	`L -> P (in HNPCC1; affects protein stability; associated with an absence of the protein in tumors).`	`VAR_043753`
`VARIANT`	`198 198`	`1`	`E -> G (in HNPCC1).`	`VAR_054513`
`VARIANT`	`199 199`	`1`	`C -> R (in glioma; also associated with HNPCC1; has no effect on ex vivo splicing assay).`	`VAR_012937`
`VARIANT`	`203 203`	`1`	`G -> R (in CRC; uncertain pathogenicity; somatic mutation).`	`VAR_043754`
`VARIANT`	`216 216`	`1`	`I -> V (in HNPCC1; could be a polymorphism; shows slightly reduced mismatch binding or release efficiency).`	`VAR_012938`
`VARIANT`	`246 246`	`1`	`K -> Q (in HNPCC1; uncertain pathogenicity).`	`VAR_043755`
`VARIANT`	`265 314`	`50`	`Missing (in HNPCC1).`	`VAR_004475`
`VARIANT`	`272 272`	`1`	`A -> V (associated wiht HNPCC1; shows slightly reduced mismatch binding or release efficiency; results in partial exon 5 skipping on ex vivo splicing assay; dbSNP:rs34136999 [NCBI]).`	`VAR_043756`
`VARIANT`	`283 283`	`1`	`D -> Y (in HNPCC1).`	`VAR_043757`
`VARIANT`	`305 305`	`1`	`A -> T (in HNPCC1).`	`VAR_004476`
`VARIANT`	`322 322`	`1`	`G -> D (common polymorphism; may be associated with increased colorectal cancer susceptibility; the equivalent substitution in yeast reduces the mismatch repair efficiency in vitro; shows slightly reduced mismatch binding or release efficiency; dbSNP:rs4987188 [NCBI]).`	`VAR_004477`
`VARIANT`	`323 323`	`1`	`S -> C (in HNPCC1; uncertain pathogenicity).`	`VAR_012939`
`VARIANT`	`323 323`	`1`	`S -> Y (in HNPCC1; uncertain pathogenicity).`	`VAR_043758`
`VARIANT`	`331 331`	`1`	`N -> D (associated with HNPCC1; has no effect on ex vivo splicing assay).`	`VAR_054514`
`VARIANT`	`333 333`	`1`	`C -> Y (in HNPCC1; affects protein stability; associated with an absence of the protein in tumors).`	`VAR_043759`
`VARIANT`	`335 335`	`1`	`T -> I (in HNPCC1; uncertain pathogenicity).`	`VAR_043760`
`VARIANT`	`336 336`	`1`	`P -> S (in HNPCC1).`	`VAR_043761`
`VARIANT`	`342 342`	`1`	`V -> I (in colorectal cancer).`	`VAR_043762`
`VARIANT`	`349 349`	`1`	`P -> L (in HNPCC1).`	`VAR_043763`
`VARIANT`	`359 359`	`1`	`R -> S (in HNPCC1; shows a decreased expression level of the MutS alpha comp lex and is associated with an abnormal subcellular localization pattern).`	`VAR_043764`
`VARIANT`	`390 390`	`1`	`L -> F (in HNPCC1; uncertain pathogenicity; the equivalent substitution in yeast partially affects mismatch repair in vitro; dbSNP:rs17224367 [NCBI]).`	`VAR_004478`
`VARIANT`	`393 393`	`1`	`K -> M (in HNPCC1).`	`VAR_043765`
`VARIANT`	`419 419`	`1`	`Q -> K (in CRC; uncertain pathogenicity; the equivalent substitution in yeast partially affects mismatch repair in vitro).`	`VAR_012940`
`VARIANT`	`440 440`	`1`	`Missing (in HNPCC1).`	`VAR_043766`
`VARIANT`	`470 470`	`1`	`V -> E (associated with HNPCC1; has no effect on ex vivo splicing assay).`	`VAR_054515`
`VARIANT`	`492 492`	`1`	`M -> V (in HNPCC1).`	`VAR_043767`
`VARIANT`	`506 506`	`1`	`D -> Y (in CRC; sporadic; early onset; the equivalent substitution in yeast partially affects mismatch repair in vitro).`	`VAR_012941`
`VARIANT`	`524 524`	`1`	`R -> P (in HNPCC1; defective in mismatch repair activity).`	`VAR_004479`
`VARIANT`	`552 552`	`1`	`T -> P (in HNPCC1).`	`VAR_043768`
`VARIANT`	`554 554`	`1`	`S -> R (in HNPCC1; could be a polymorphism).`	`VAR_012942`
`VARIANT`	`562 562`	`1`	`E -> V (in HNPCC1).`	`VAR_004480`
`VARIANT`	`564 564`	`1`	`T -> A (in HNPCC1; uncertain pathogenicity; dbSNP:rs55778204 [NCBI]).`	`VAR_043769`
`VARIANT`	`583 583`	`1`	`N -> S (in HNPCC1).`	`VAR_043770`
`VARIANT`	`596 596`	`1`	`N -> S (in HNPCC1; could be a polymorphism; dbSNP:rs41295288 [NCBI]).`	`VAR_012943`
`VARIANT`	`596 596`	`1`	`Missing (in HNPCC1; has no effect on ex vivo splicing assay).`	`VAR_004481`
`VARIANT`	`600 600`	`1`	`A -> V (in HNPCC1).`	`VAR_043771`
`VARIANT`	`603 603`	`1`	`D -> N (in HNPCC1; affects protein stability; associated with an absence of the protein in tumors).`	`VAR_043772`
`VARIANT`	`610 610`	`1`	`H -> N (associated with HNPCC1; has no effect on ex vivo splicing assay).`	`VAR_054516`
`VARIANT`	`619 619`	`1`	`Y -> C (in CRC).`	`VAR_043773`
`VARIANT`	`622 622`	`1`	`P -> L (in HNPCC1; the equivalent substitution in yeast causes loss of function in a mismatch repair assay).`	`VAR_004482`
`VARIANT`	`629 629`	`1`	`Q -> R (in HNPCC1; uncertain pathogenicity).`	`VAR_043774`
`VARIANT`	`636 636`	`1`	`A -> P (in HNPCC1; partial functional loss; mainly causes defects in mismatch binding or release efficiency).`	`VAR_012944`
`VARIANT`	`638 638`	`1`	`R -> G (associated with HNPCC1; has no effect on ex vivo splicing assay).`	`VAR_054517`
`VARIANT`	`639 639`	`1`	`H -> R (in HNPCC1).`	`VAR_043775`
`VARIANT`	`639 639`	`1`	`H -> Y (in HNPCC1; the equivalent substitution in yeast does not affect mismatch repair efficiency in vitro).`	`VAR_004483`
`VARIANT`	`641 641`	`1`	`C -> G.`	`VAR_004484`
`VARIANT`	`645 645`	`1`	`Q -> E (associated with HNPCC1; has no effect on ex vivo splicing assay).`	`VAR_054518`
`VARIANT`	`647 647`	`1`	`E -> K (in HNPCC1).`	`VAR_043776`
`VARIANT`	`656 656`	`1`	`Y -> H (in HNPCC1; somatic mutation).`	`VAR_043777`
`VARIANT`	`660 660`	`1`	`D -> G (in HNPCC1).`	`VAR_022671`
`VARIANT`	`670 670`	`1`	`P -> L (in dbSNP:rs41294982 [NCBI]).`	`VAR_038027`
`VARIANT`	`671 671`	`1`	`N -> Y (in HNPCC1; uncertain pathogenicity).`	`VAR_043778`
`VARIANT`	`674 674`	`1`	`G -> S (in HNPCC1; somatic mutation).`	`VAR_004485`
`VARIANT`	`679 679`	`1`	`I -> T (in HNPCC1; somatic mutation).`	`VAR_043779`
`VARIANT`	`688 688`	`1`	`M -> I (in HNPCC1).`	`VAR_012945`
`VARIANT`	`692 692`	`1`	`G -> R (in HNPCC1).`	`VAR_009250`
`VARIANT`	`696 696`	`1`	`P -> L (associated with HNPCC1; has no effect on ex vivo splicing assay).`	`VAR_054519`
`VARIANT`	`697 697`	`1`	`C -> F (in HNPCC1; the equivalent substitution in yeast causes loss of function in a mismatch repair assay; mainly causes defects in mismatch binding or release efficiency).`	`VAR_004486`
`VARIANT`	`697 697`	`1`	`C -> R (in HNPCC1; has no effect on ex vivo splicing assay).`	`VAR_009251`
`VARIANT`	`714 714`	`1`	`A -> V (in HNPCC1; uncertain pathogenicity).`	`VAR_043780`
`VARIANT`	`723 723`	`1`	`S -> F (in HNPCC1; has no effect on ex vivo splicing assay).`	`VAR_043781`
`VARIANT`	`729 729`	`1`	`M -> V (in HNPCC1; somatic mutation).`	`VAR_043782`
`VARIANT`	`732 732`	`1`	`T -> I (in HNPCC1; somatic mutation).`	`VAR_043783`
`VARIANT`	`745 746`	`2`	`Missing (in HNPCC1; mainly causes defects in mismatch binding or release efficiency).`	`VAR_043784`
`VARIANT`	`748 748`	`1`	`D -> Y (associated with HNPCC1; has no effect on ex vivo splicing assay).`	`VAR_054520`
`VARIANT`	`749 749`	`1`	`E -> K (in HNPCC1; mainly causes defects in mismatch binding or release efficiency; the mutant protein is well expressed in tumors).`	`VAR_043785`
`VARIANT`	`770 770`	`1`	`I -> V.`	`VAR_004487`
`VARIANT`	`779 779`	`1`	`M -> I (in dbSNP:rs41295292 [NCBI]).`	`VAR_038028`
`VARIANT`	`807 807`	`1`	`T -> S (in dbSNP:rs41295294 [NCBI]).`	`VAR_038029`
`VARIANT`	`813 813`	`1`	`M -> V (in HNPCC1).`	`VAR_043786`
`VARIANT`	`824 824`	`1`	`Q -> E (in gastric cancer; uncertain pathogenicity).`	`VAR_043787`
`VARIANT`	`834 834`	`1`	`A -> T (in HNPCC1; shows no defects; could be a polymorphism).`	`VAR_004488`
`VARIANT`	`835 835`	`1`	`N -> H (in dbSNP:rs41295296 [NCBI]).`	`VAR_038030`
`VARIANT`	`839 839`	`1`	`H -> Q (associated with HNPCC1; has no effect on ex vivo splicing assay).`	`VAR_054521`
`VARIANT`	`839 839`	`1`	`H -> R (in HNPCC1).`	`VAR_043788`
`VARIANT`	`845 845`	`1`	`K -> E (in HNPCC1).`	`VAR_013172`
`VARIANT`	`853 853`	`1`	`E -> A (in HNPCC1; uncertain pathogenicity).`	`VAR_043789`
`VARIANT`	`868 868`	`1`	`P -> A (in gastric cancer; uncertain pathogenicity).`	`VAR_043790`
`VARIANT`	`870 870`	`1`	`A -> G (in gastric cancer; uncertain pathogenicity).`	`VAR_043791`
`VARIANT`	`873 873`	`1`	`C -> G (in gastric cancer; uncertain pathogenicity).`	`VAR_043792`
`VARIANT`	`886 886`	`1`	`E -> G (in HNPCC1).`	`VAR_043793`
`VARIANT`	`905 905`	`1`	`T -> R (in HNPCC1; could be a polymorphism).`	`VAR_004489`
`VARIANT`	`911 911`	`1`	`L -> R (in dbSNP:rs41295182 [NCBI]).`	`VAR_038031`
`VARIANT`	`923 923`	`1`	`V -> E (in HNPCC1; could be a polymorphism).`	`VAR_043794`
`VARIANT`	`931 931`	`1`	`K -> T (in HNPCC1).`	`VAR_043795`
`MUTAGEN`	`674 674`		`G->A: Mainly causes defects in mismatch binding or release efficiency.`
`MUTAGEN`	`675 675`		`K->R: No effect on mismatch binding, complete loss of DNA repair function when associated with MSH6 mutant R-1140.`
`HELIX`	`13 24`	`12`
`STRAND`	`33 38`	`6`
`STRAND`	`40 46`	`7`
`HELIX`	`47 56`	`10`
`STRAND`	`65 68`	`4`
`STRAND`	`75 80`	`6`
`HELIX`	`82 94`	`13`
`STRAND`	`99 105`	`7`
`STRAND`	`117 124`	`8`
`HELIX`	`129 131`	`3`
`TURN`	`132 134`	`3`
`STRAND`	`147 151`	`5`
`STRAND`	`154 158`	`5`
`STRAND`	`160 167`	`8`
`TURN`	`168 171`	`4`
`STRAND`	`172 179`	`8`
`HELIX`	`185 194`	`10`
`STRAND`	`197 201`	`5`
`STRAND`	`206 208`	`3`
`HELIX`	`209 218`	`10`
`TURN`	`219 221`	`3`
`STRAND`	`223 226`	`4`
`HELIX`	`237 240`	`4`
`TURN`	`252 256`	`5`
`HELIX`	`259 262`	`4`
`HELIX`	`264 276`	`13`
`HELIX`	`304 309`	`6`
`HELIX`	`326 330`	`5`
`HELIX`	`336 347`	`12`
`HELIX`	`353 369`	`17`
`HELIX`	`371 377`	`7`
`TURN`	`378 380`	`3`
`HELIX`	`381 383`	`3`
`HELIX`	`387 395`	`9`
`HELIX`	`401 412`	`12`
`HELIX`	`415 421`	`7`
`STRAND`	`424 427`	`4`
`HELIX`	`437 446`	`10`
`HELIX`	`448 457`	`10`
`HELIX`	`460 463`	`4`
`STRAND`	`464 466`	`3`
`TURN`	`472 474`	`3`
`HELIX`	`476 503`	`28`
`TURN`	`508 510`	`3`
`TURN`	`517 519`	`3`
`STRAND`	`523 525`	`3`
`TURN`	`531 534`	`4`
`STRAND`	`537 545`	`9`
`STRAND`	`548 553`	`6`
`HELIX`	`554 585`	`32`
`HELIX`	`586 588`	`3`
`HELIX`	`589 614`	`26`
`STRAND`	`615 617`	`3`
`STRAND`	`623 625`	`3`
`STRAND`	`630 637`	`8`
`TURN`	`640 644`	`5`
`STRAND`	`653 658`	`6`
`STRAND`	`664 668`	`5`
`HELIX`	`675 690`	`16`
`STRAND`	`695 703`	`9`
`STRAND`	`706 712`	`7`
`HELIX`	`724 736`	`13`
`STRAND`	`743 749`	`7`
`HELIX`	`756 772`	`17`
`STRAND`	`777 781`	`5`
`HELIX`	`790 793`	`4`
`STRAND`	`794 806`	`13`
`STRAND`	`811 820`	`10`
`HELIX`	`827 833`	`7`
`HELIX`	`838 852`	`15`

Sequence information

Length: 934 AA [This is the length of the unprocessed precursor]

Molecular weight: 104743 Da [This is the MW of the unprocessed precursor]

CRC64: 664A058C78242E05 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAVQPKETLQ LESAAEVGFV RFFQGMPEKP TTTVRLFDRG DFYTAHGEDA LLAAREVFKT 

        70         80         90        100        110        120 
QGVIKYMGPA GAKNLQSVVL SKMNFESFVK DLLLVRQYRV EVYKNRAGNK ASKENDWYLA 

       130        140        150        160        170        180 
YKASPGNLSQ FEDILFGNND MSASIGVVGV KMSAVDGQRQ VGVGYVDSIQ RKLGLCEFPD 

       190        200        210        220        230        240 
NDQFSNLEAL LIQIGPKECV LPGGETAGDM GKLRQIIQRG GILITERKKA DFSTKDIYQD 

       250        260        270        280        290        300 
LNRLLKGKKG EQMNSAVLPE MENQVAVSSL SAVIKFLELL SDDSNFGQFE LTTFDFSQYM 

       310        320        330        340        350        360 
KLDIAAVRAL NLFQGSVEDT TGSQSLAALL NKCKTPQGQR LVNQWIKQPL MDKNRIEERL 

       370        380        390        400        410        420 
NLVEAFVEDA ELRQTLQEDL LRRFPDLNRL AKKFQRQAAN LQDCYRLYQG INQLPNVIQA 

       430        440        450        460        470        480 
LEKHEGKHQK LLLAVFVTPL TDLRSDFSKF QEMIETTLDM DQVENHEFLV KPSFDPNLSE 

       490        500        510        520        530        540 
LREIMNDLEK KMQSTLISAA RDLGLDPGKQ IKLDSSAQFG YYFRVTCKEE KVLRNNKNFS 

       550        560        570        580        590        600 
TVDIQKNGVK FTNSKLTSLN EEYTKNKTEY EEAQDAIVKE IVNISSGYVE PMQTLNDVLA 

       610        620        630        640        650        660 
QLDAVVSFAH VSNGAPVPYV RPAILEKGQG RIILKASRHA CVEVQDEIAF IPNDVYFEKD 

       670        680        690        700        710        720 
KQMFHIITGP NMGGKSTYIR QTGVIVLMAQ IGCFVPCESA EVSIVDCILA RVGAGDSQLK 

       730        740        750        760        770        780 
GVSTFMAEML ETASILRSAT KDSLIIIDEL GRGTSTYDGF GLAWAISEYI ATKIGAFCMF 

       790        800        810        820        830        840 
ATHFHELTAL ANQIPTVNNL HVTALTTEET LTMLYQVKKG VCDQSFGIHV AELANFPKHV 

       850        860        870        880        890        900 
IECAKQKALE LEEFQYIGES QGYDIMEPAA KKCYLEREQG EKIIQEFLSK VKQMPFTEMS 

       910        920        930 
EENITIKLKQ LKAEVIAKNN SFVNEIISRI KVTT

P43246 in FASTA format

View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools