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MSH2_HUMAN
ID   MSH2_HUMAN              Reviewed;         934 AA.
AC   P43246; B4E2Z2; O75488;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 238.
DE   RecName: Full=DNA mismatch repair protein Msh2;
DE            Short=hMSH2;
DE   AltName: Full=MutS protein homolog 2;
GN   Name=MSH2;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   PubMed=8252616; DOI=10.1016/0092-8674(93)90546-3;
RA   Fishel R., Lescoe M., Rao M., Copeland N.G., Jenkins N.A., Garber J.,
RA   Kane M.F., Kolodner R.D.;
RT   "The human mutator gene homolog MSH2 and its association with hereditary
RT   nonpolyposis colon cancer.";
RL   Cell 75:1027-1038(1993).
RN   [2]
RP   ERRATUM OF PUBMED:8252616.
RX   PubMed=8156592;
RA   Fishel R., Lescoe M., Rao M., Copeland N.G., Jenkins N.A., Garber J.,
RA   Kane M.F., Kolodner R.D.;
RL   Cell 77:167-167(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS HNPCC1 LEU-622 AND
RP   TYR-639.
RX   PubMed=8261515; DOI=10.1016/0092-8674(93)90330-s;
RA   Leach F.S., Nicolaides N.C., Papadopoulos N., Liu B., Jen J., Parsons R.,
RA   Peltomaeki P., Sistonen P., Aaltonen L.A., Nystroem-Lahti M., Guan X.-Y.,
RA   Zhang J., Meltzer P.S., Yu J.-W., Kao F.-T., Chen D.J., Cerosaletti K.M.,
RA   Fournier R.E.K., Todd S., Lewis T., Leach R.J., Naylor S.L.,
RA   Weissenbach J., Mecklin J.-P., Jaervinen H., Petersen G.M., Hamilton S.R.,
RA   Green J., Jass J., Watson P., Lynch H.T., Trent J.M., de la Chapelle A.,
RA   Kinzler K.W., Vogelstein B.;
RT   "Mutations of a mutS homolog in hereditary nonpolyposis colorectal
RT   cancer.";
RL   Cell 75:1215-1225(1993).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INVOLVEMENT IN MRTES.
RX   PubMed=7713503; DOI=10.1006/geno.1994.1661;
RA   Kolodner R.D., Hall N.R., Lipford J., Kane M.F., Rao M.R.S., Morrison P.,
RA   Wirth L., Finan P.J., Burn J., Chapman P., Earabino C., Merchant E.,
RA   Bishop D.T.;
RT   "Structure of the human MSH2 locus and analysis of two Muir-Torre kindreds
RT   for msh2 mutations.";
RL   Genomics 24:516-526(1994).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT HIS-96.
RX   PubMed=7726159;
RA   Wijnen J., Vasen H., Khan P.M., Menko F.H., van der Klift H.,
RA   van Leeuwen C., van den Broek M., van Leeuwen-Cornelisse I., Nagengast F.,
RA   Meijers-Heijboer A., Lindhout D., Griffioen G., Cats A., Kleibeuker J.,
RA   Varesco L., Bertario L., Bisgaard M.-L., Mohr J., Fodde R.;
RT   "Seven new mutations in hMSH2, an HNPCC gene, identified by denaturing
RT   gradient-gel electrophoresis.";
RL   Am. J. Hum. Genet. 56:1060-1066(1995).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Uterus;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Testis;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA   Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA   Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15815621; DOI=10.1038/nature03466;
RA   Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA   Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA   Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA   Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA   Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA   Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA   Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA   Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA   Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA   McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA   Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA   Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA   Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA   Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA   Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA   Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA   Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA   Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA   Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA   Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA   Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA   Wilson R.K.;
RT   "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT   4.";
RL   Nature 434:724-731(2005).
RN   [9]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS MET-8; CYS-43; SER-127;
RP   ASP-322 AND PHE-390.
RG   NIEHS SNPs program;
RL   Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
RN   [10]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Muscle;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [11]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 375-425.
RC   TISSUE=Blood;
RA   Corvello C.M., Bevilacqua R.A.U., Rossi B.M., Simpson A.J.G.;
RT   "A novel germline mutation at exon 7 of the hMSH2 gene (417 del G) in a
RT   large HNPCC Brazilian kindred.";
RL   Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
RN   [12]
RP   DNA-BINDING.
RX   PubMed=7923193;
RA   Fishel R., Ewel A., Lescoe M.K.;
RT   "Purified human MSH2 protein binds to DNA containing mismatched
RT   nucleotides.";
RL   Cancer Res. 54:5539-5542(1994).
RN   [13]
RP   DNA-BINDING.
RX   PubMed=8769132; DOI=10.1006/bbrc.1996.1168;
RA   Whitehouse A., Taylor G.R., Deeble J., Phillips S.E., Meredith D.M.,
RA   Markham A.F.;
RT   "A carboxy terminal domain of the hMSH-2 gene product is sufficient for
RT   binding specific mismatched oligonucleotides.";
RL   Biochem. Biophys. Res. Commun. 225:289-295(1996).
RN   [14]
RP   INTERACTION WITH MSH3 AND MSH6.
RX   PubMed=8942985; DOI=10.1073/pnas.93.24.13629;
RA   Acharya S., Wilson T., Gradia S., Kane M.F., Guerrette S., Marsischky G.T.,
RA   Kolodner R.D., Fishel R.;
RT   "hMSH2 forms specific mispair-binding complexes with hMSH3 and hMSH6.";
RL   Proc. Natl. Acad. Sci. U.S.A. 93:13629-13634(1996).
RN   [15]
RP   INTERACTION WITH EXO1.
RX   PubMed=9788596;
RA   Schmutte C., Marinescu R.C., Sadoff M.M., Guerrette S., Overhauser J.,
RA   Fishel R.;
RT   "Human exonuclease I interacts with the mismatch repair protein hMSH2.";
RL   Cancer Res. 58:4537-4542(1998).
RN   [16]
RP   FUNCTION.
RX   PubMed=9822680; DOI=10.1074/jbc.273.48.32055;
RA   Blackwell L.J., Martik D., Bjornson K.P., Bjornson E.S., Modrich P.;
RT   "Nucleotide-promoted release of hMutSalpha from heteroduplex DNA is
RT   consistent with an ATP-dependent translocation mechanism.";
RL   J. Biol. Chem. 273:32055-32062(1998).
RN   [17]
RP   FUNCTION.
RX   PubMed=9822679; DOI=10.1074/jbc.273.48.32049;
RA   Blackwell L.J., Bjornson K.P., Modrich P.;
RT   "DNA-dependent activation of the hMutSalpha ATPase.";
RL   J. Biol. Chem. 273:32049-32054(1998).
RN   [18]
RP   FUNCTION, AND MUTAGENESIS OF LYS-675.
RX   PubMed=9564049; DOI=10.1093/emboj/17.9.2677;
RA   Iaccarino I., Marra G., Palombo F., Jiricny J.;
RT   "hMSH2 and hMSH6 play distinct roles in mismatch binding and contribute
RT   differently to the ATPase activity of hMutSalpha.";
RL   EMBO J. 17:2677-2686(1998).
RN   [19]
RP   MISMATCH-BINDING, AND CHARACTERIZATION OF VARIANT HNPCC1 PRO-524.
RX   PubMed=9889267; DOI=10.1093/nar/27.3.736;
RA   Clark A.B., Cook M.E., Tran H.T., Gordenin D.A., Resnick M.A., Kunkel T.A.;
RT   "Functional analysis of human MutSalpha and MutSbeta complexes in yeast.";
RL   Nucleic Acids Res. 27:736-742(1999).
RN   [20]
RP   FUNCTION.
RX   PubMed=10078208; DOI=10.1016/s1097-2765(00)80316-0;
RA   Gradia S., Subramanian D., Wilson T., Acharya S., Makhov A., Griffith J.,
RA   Fishel R.;
RT   "hMSH2-hMSH6 forms a hydrolysis-independent sliding clamp on mismatched
RT   DNA.";
RL   Mol. Cell 3:255-261(1999).
RN   [21]
RP   IDENTIFICATION OF MSH2 AS MEMBER OF BASC.
RX   PubMed=10783165;
RA   Wang Y., Cortez D., Yazdi P., Neff N., Elledge S.J., Qin J.;
RT   "BASC, a super complex of BRCA1-associated proteins involved in the
RT   recognition and repair of aberrant DNA structures.";
RL   Genes Dev. 14:927-939(2000).
RN   [22]
RP   INTERACTION WITH EXO1, AND TISSUE SPECIFICITY.
RX   PubMed=10856833; DOI=10.1016/s0921-8777(00)00012-4;
RA   Rasmussen L.J., Rasmussen M., Lee B.-I., Rasmussen A.K., Wilson D.M. III,
RA   Nielsen F.C., Bisgaard H.C.;
RT   "Identification of factors interacting with hMSH2 in the fetal liver
RT   utilizing the yeast two-hybrid system. In vivo interaction through the C-
RT   terminal domains of hEXO1 and hMSH2 and comparative expression analysis.";
RL   Mutat. Res. 460:41-52(2000).
RN   [23]
RP   FUNCTION.
RX   PubMed=10660545; DOI=10.1074/jbc.275.6.3922;
RA   Gradia S., Acharya S., Fishel R.;
RT   "The role of mismatched nucleotides in activating the hMSH2-hMSH6 molecular
RT   switch.";
RL   J. Biol. Chem. 275:3922-3930(2000).
RN   [24]
RP   POSSIBLE INVOLVEMENT IN ENDMC.
RX   PubMed=11306449;
RA   Schweizer P., Moisio A.L., Kuismanen S.A., Truninger K., Vierumaeki R.,
RA   Salovaara R., Arola J., Butzow R., Jiricny J., Peltomaeki P.,
RA   Nystroem-Lahti M.;
RT   "Lack of MSH2 and MSH6 characterizes endometrial but not colon carcinomas
RT   in hereditary nonpolyposis colorectal cancer.";
RL   Cancer Res. 61:2813-2815(2001).
RN   [25]
RP   INTERACTION WITH EXO1.
RX   PubMed=11427529; DOI=10.1074/jbc.m102670200;
RA   Schmutte C., Sadoff M.M., Shim K.-S., Acharya S., Fishel R.;
RT   "The interaction of DNA mismatch repair proteins with human exonuclease
RT   I.";
RL   J. Biol. Chem. 276:33011-33018(2001).
RN   [26]
RP   INTERACTION WITH EXO1.
RX   PubMed=11429708; DOI=10.1038/sj.onc.1204467;
RA   Jaeger A.C., Rasmussen M., Bisgaard H.C., Singh K.K., Nielsen F.C.,
RA   Rasmussen L.J.;
RT   "HNPCC mutations in the human DNA mismatch repair gene hMLH1 influence
RT   assembly of hMutLalpha and hMLH1-hEXO1 complexes.";
RL   Oncogene 20:3590-3595(2001).
RN   [27]
RP   INTERACTION WITH EXO1.
RX   PubMed=12414623;
RA   Sun X., Zheng L., Shen B.;
RT   "Functional alterations of human exonuclease 1 mutants identified in
RT   atypical hereditary nonpolyposis colorectal cancer syndrome.";
RL   Cancer Res. 62:6026-6030(2002).
RN   [28]
RP   INVOLVEMENT IN MMRCS2.
RX   PubMed=12549480; DOI=10.1086/345297;
RA   Bougeard G., Charbonnier F., Moerman A., Martin C., Ruchoux M.M.,
RA   Drouot N., Frebourg T.;
RT   "Early onset brain tumor and lymphoma in MSH2-deficient children.";
RL   Am. J. Hum. Genet. 72:213-216(2003).
RN   [29]
RP   INTERACTION WITH ATR, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=14657349; DOI=10.1073/pnas.2536810100;
RA   Wang Y., Qin J.;
RT   "MSH2 and ATR form a signaling module and regulate two branches of the
RT   damage response to DNA methylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:15387-15392(2003).
RN   [30]
RP   INTERACTION WITH EXO1.
RX   PubMed=14676842; DOI=10.1038/sj.onc.1207265;
RA   Nielsen F.C., Jaeger A.C., Luetzen A., Bundgaard J.R., Rasmussen L.J.;
RT   "Characterization of human exonuclease 1 in complex with mismatch repair
RT   proteins, subcellular localization and association with PCNA.";
RL   Oncogene 23:1457-1468(2004).
RN   [31]
RP   FUNCTION.
RX   PubMed=15064730; DOI=10.1038/sj.onc.1207462;
RA   Yang Q., Zhang R., Wang X.W., Linke S.P., Sengupta S., Hickson I.D.,
RA   Pedrazzi G., Perrera C., Stagljar I., Littman S.J., Modrich P.,
RA   Harris C.C.;
RT   "The mismatch DNA repair heterodimer, hMSH2/6, regulates BLM helicase.";
RL   Oncogene 23:3749-3756(2004).
RN   [32]
RP   PHOSPHORYLATION BY PRKCZ.
RX   PubMed=15808853; DOI=10.1016/j.jmb.2005.02.001;
RA   Hernandez-Pigeon H., Quillet-Mary A., Louat T., Schambourg A., Humbert O.,
RA   Selves J., Salles B., Laurent G., Lautier D.;
RT   "hMutS alpha is protected from ubiquitin-proteasome-dependent degradation
RT   by atypical protein kinase C zeta phosphorylation.";
RL   J. Mol. Biol. 348:63-74(2005).
RN   [33]
RP   INVOLVEMENT IN MMRCS2.
RX   PubMed=16372347; DOI=10.1002/ajmg.a.31070;
RA   Mueller A., Schackert H.K., Lange B., Rueschoff J., Fuezesi L., Willert J.,
RA   Burfeind P., Shah P., Becker H., Epplen J.T., Stemmler S.;
RT   "A novel MSH2 germline mutation in homozygous state in two brothers with
RT   colorectal cancers diagnosed at the age of 11 and 12 years.";
RL   Am. J. Med. Genet. A 140:195-199(2006).
RN   [34]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic kidney;
RX   PubMed=17525332; DOI=10.1126/science.1140321;
RA   Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA   Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA   Gygi S.P., Elledge S.J.;
RT   "ATM and ATR substrate analysis reveals extensive protein networks
RT   responsive to DNA damage.";
RL   Science 316:1160-1166(2007).
RN   [35]
RP   FUNCTION.
RX   PubMed=17611581; DOI=10.1038/sj.jid.5700941;
RA   Seifert M., Scherer S.J., Edelmann W., Bohm M., Meineke V., Lobrich M.,
RA   Tilgen W., Reichrath J.;
RT   "The DNA-mismatch repair enzyme hMSH2 modulates UV-B-induced cell cycle
RT   arrest and apoptosis in melanoma cells.";
RL   J. Invest. Dermatol. 128:203-213(2008).
RN   [36]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-555, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19608861; DOI=10.1126/science.1175371;
RA   Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA   Olsen J.V., Mann M.;
RT   "Lysine acetylation targets protein complexes and co-regulates major
RT   cellular functions.";
RL   Science 325:834-840(2009).
RN   [37]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [38]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN   [39]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-921, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [40]
RP   FUNCTION, IDENTIFICATION IN THE MMR COMPLEX, INTERACTION WITH MCM9 AND
RP   MCM8, AND SUBCELLULAR LOCATION.
RX   PubMed=26300262; DOI=10.1016/j.molcel.2015.07.010;
RA   Traver S., Coulombe P., Peiffer I., Hutchins J.R., Kitzmann M.,
RA   Latreille D., Mechali M.;
RT   "MCM9 Is Required for Mammalian DNA Mismatch Repair.";
RL   Mol. Cell 59:831-839(2015).
RN   [41]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-430, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=28112733; DOI=10.1038/nsmb.3366;
RA   Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA   Nielsen M.L.;
RT   "Site-specific mapping of the human SUMO proteome reveals co-modification
RT   with phosphorylation.";
RL   Nat. Struct. Mol. Biol. 24:325-336(2017).
RN   [42]
RP   CHARACTERIZATION OF VARIANTS HNPCC1 PRO-33; MET-44; VAL-45; SER-127;
RP   MET-145; ASP-161; ARG-162; ARG-164; PRO-173; ARG-187; PRO-187; VAL-272;
RP   TYR-333; LEU-519; ASN-603; PRO-636; ALA-674; VAL-688; PHE-697;
RP   745-ILE-ILE-746 DEL; LYS-749; THR-834; GLY-886 AND GLU-923,
RP   CHARACTERIZATION OF VARIANTS ASP-322 AND ILE-722, AND FUNCTION.
RX   PubMed=21120944; DOI=10.1002/humu.21409;
RA   Kansikas M., Kariola R., Nystroem M.;
RT   "Verification of the three-step model in assessing the pathogenicity of
RT   mismatch repair gene variants.";
RL   Hum. Mutat. 32:107-115(2011).
RN   [43]
RP   REVIEW.
RX   PubMed=8036718; DOI=10.1016/0168-9525(94)90093-0;
RA   Jiricny J.;
RT   "Colon cancer and DNA repair: have mismatches met their match?";
RL   Trends Genet. 10:164-168(1994).
RN   [44]
RP   REVIEW ON VARIANTS.
RX   PubMed=9259192;
RX   DOI=10.1002/(sici)1098-1004(1997)10:2<89::aid-humu1>3.0.co;2-h;
RA   Papadopoulos N., Lindblom A.;
RT   "Molecular basis of HNPCC: mutations of MMR genes.";
RL   Hum. Mutat. 10:89-99(1997).
RN   [45]
RP   REVIEW.
RX   PubMed=17080293; DOI=10.1007/s10735-006-9062-5;
RA   Seifert M., Reichrath J.;
RT   "The role of the human DNA mismatch repair gene hMSH2 in DNA repair, cell
RT   cycle control and apoptosis: implications for pathogenesis, progression and
RT   therapy of cancer.";
RL   J. Mol. Histol. 37:301-307(2006).
RN   [46]
RP   INTERACTION WITH SMARCAD1.
RX   PubMed=18675275; DOI=10.1016/j.jmb.2008.07.031;
RA   Okazaki N., Ikeda S., Ohara R., Shimada K., Yanagawa T., Nagase T.,
RA   Ohara O., Koga H.;
RT   "The novel protein complex with SMARCAD1/KIAA1122 binds to the vicinity of
RT   TSS.";
RL   J. Mol. Biol. 382:257-265(2008).
RN   [47]
RP   INTERACTION WITH SLX4.
RX   PubMed=19596235; DOI=10.1016/j.cell.2009.06.030;
RA   Svendsen J.M., Smogorzewska A., Sowa M.E., O'Connell B.C., Gygi S.P.,
RA   Elledge S.J., Harper J.W.;
RT   "Mammalian BTBD12/SLX4 assembles a Holliday junction resolvase and is
RT   required for DNA repair.";
RL   Cell 138:63-77(2009).
RN   [48]
RP   POSSIBLE INVOLVEMENT IN ENDMC.
RX   PubMed=21642682; DOI=10.1001/jama.2011.743;
RG   French Cancer Genetics Network;
RA   Bonadona V., Bonaiti B., Olschwang S., Grandjouan S., Huiart L., Longy M.,
RA   Guimbaud R., Buecher B., Bignon Y.J., Caron O., Colas C., Nogues C.,
RA   Lejeune-Dumoulin S., Olivier-Faivre L., Polycarpe-Osaer F., Nguyen T.D.,
RA   Desseigne F., Saurin J.C., Berthet P., Leroux D., Duffour J.,
RA   Manouvrier S., Frebourg T., Sobol H., Lasset C., Bonaiti-Pellie C.;
RT   "Cancer risks associated with germline mutations in MLH1, MSH2, and MSH6
RT   genes in Lynch syndrome.";
RL   JAMA 305:2304-2310(2011).
RN   [49]
RP   X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS).
RX   PubMed=17531815; DOI=10.1016/j.molcel.2007.04.018;
RA   Warren J.J., Pohlhaus T.J., Changela A., Iyer R.R., Modrich P.L.,
RA   Beese L.S.;
RT   "Structure of the human MutSalpha DNA lesion recognition complex.";
RL   Mol. Cell 26:579-592(2007).
RN   [50]
RP   VARIANT HNPCC1 ASN-596 DEL.
RX   PubMed=7874129;
RA   Mary J.-L., Bishop T., Kolodner R.D., Lipford J.R., Kane M.F., Weber W.,
RA   Torhorst J., Mueller H., Spycher M., Scott R.J.;
RT   "Mutational analysis of the hMSH2 gene reveals a three base pair deletion
RT   in a family predisposed to colorectal cancer development.";
RL   Hum. Mol. Genet. 3:2067-2069(1994).
RN   [51]
RP   VARIANTS PHE-390 AND LYS-419.
RX   PubMed=8690195; DOI=10.1053/gast.1996.v111.pm8690195;
RA   Konishi M., Kikuchi-Yanoshita R., Tanaka K., Muraoka M., Onda A.,
RA   Okumura Y., Kishi N., Iwama T., Mori T., Koike M., Ushio K., Chiba M.,
RA   Nomizu S., Konishi F., Utsunomiya J., Miyaki M.;
RT   "Molecular nature of colon tumors in hereditary nonpolyposis colon cancer,
RT   familial polyposis, and sporadic colon cancer.";
RL   Gastroenterology 111:307-317(1996).
RN   [52]
RP   VARIANT ASP-322.
RX   PubMed=8566964; DOI=10.1007/bf02265276;
RA   Maliaka Y.K., Chudina A.P., Belev N.F., Alday P., Bochkov N.P.,
RA   Buerstedde J.-M.;
RT   "CpG dinucleotides in the hMSH2 and hMLH1 genes are hotspots for HNPCC
RT   mutations.";
RL   Hum. Genet. 97:251-255(1996).
RN   [53]
RP   VARIANT HNPCC1 ASN-596 DEL, AND VARIANT HIS-167.
RX   PubMed=8872463; DOI=10.1093/hmg/5.9.1245;
RA   Moslein G., Tester D.J., Lindor N.M., Honchel R., Cunningham J.M.,
RA   French A.J., Halling K.C., Schwab M., Goretzki P., Thibodeau S.N.;
RT   "Microsatellite instability and mutation analysis of hMSH2 and hMLH1 in
RT   patients with sporadic, familial and hereditary colorectal cancer.";
RL   Hum. Mol. Genet. 5:1245-1252(1996).
RN   [54]
RP   VARIANT HNPCC1 TYR-506.
RX   PubMed=8797773; DOI=10.1093/jnci/88.18.1317;
RA   Han H.-J., Yuan Y., Ku J.-L., Oh J.-H., Won Y.-J., Kang K.J., Kim K.Y.,
RA   Kim S., Kim C.Y., Kim J.-P., Oh N.-G., Lee K.H., Choe K.J., Nakamura Y.,
RA   Park J.-G.;
RT   "Germline mutations of hMLH1 and hMSH2 genes in Korean hereditary
RT   nonpolyposis colorectal cancer.";
RL   J. Natl. Cancer Inst. 88:1317-1319(1996).
RN   [55]
RP   VARIANT HNPCC1 GLN-46.
RX   PubMed=8700523;
RA   Bubb V.J., Curtis L.J., Cunningham C., Dunlop M.G., Carothers A.D.,
RA   Morris R.G., White S., Bird C.C., Wyllie A.H.;
RT   "Microsatellite instability and the role of hMSH2 in sporadic colorectal
RT   cancer.";
RL   Oncogene 12:2641-2649(1996).
RN   [56]
RP   VARIANTS HNPCC1 THR-305; ASN-596 DEL AND THR-834.
RX   PubMed=9311737; DOI=10.1086/514847;
RA   Wijnen J., Khan P.M., Vasen H., van der Klift H., Mulder A.,
RA   van Leeuwen-Cornelisse I., Bakker B., Losekoot M., Moeller P., Fodde R.;
RT   "Hereditary nonpolyposis colorectal cancer families not complying with the
RT   Amsterdam criteria show extremely low frequency of mismatch-repair-gene
RT   mutations.";
RL   Am. J. Hum. Genet. 61:329-335(1997).
RN   [57]
RP   VARIANT HNPCC1 CYS-323.
RX   PubMed=9240418; DOI=10.1006/bbrc.1997.6942;
RA   Akiyama Y., Tsubouchi N., Yuasa Y.;
RT   "Frequent somatic mutations of hMSH3 with reference to microsatellite
RT   instability in hereditary nonpolyposis colorectal cancers.";
RL   Biochem. Biophys. Res. Commun. 236:248-252(1997).
RN   [58]
RP   VARIANTS HNPCC1 THR-110; ARG-639; LYS-647; HIS-656; THR-679; VAL-729 AND
RP   ILE-732.
RX   PubMed=9419403;
RA   Nakahara M., Yokozaki H., Yasui W., Dohi K., Tahara E.;
RT   "Identification of concurrent germ-line mutations in hMSH2 and/or hMLH1 in
RT   Japanese hereditary nonpolyposis colorectal cancer kindreds.";
RL   Cancer Epidemiol. Biomarkers Prev. 6:1057-1064(1997).
RN   [59]
RP   VARIANT SER-596.
RX   PubMed=8993976;
RX   DOI=10.1002/(sici)1098-2264(199701)18:1<8::aid-gcc2>3.0.co;2-7;
RA   Viel A., Genuardi M., Capozzi E., Leonardi F., Bellacosa A.,
RA   Paravatou-Petsotas M., Pomponi M.G., Fornasarig M., Percesepe A.,
RA   Roncucci L., Tamassia M.G., Benatti P., Ponz de Leon M., Valenti A.,
RA   Covino M., Anti M., Foletto M., Boiocchi M., Neri G.;
RT   "Characterization of MSH2 and MLH1 mutations in Italian families with
RT   hereditary nonpolyposis colorectal cancer.";
RL   Genes Chromosomes Cancer 18:8-18(1997).
RN   [60]
RP   VARIANT ASP-322.
RX   PubMed=9087566;
RX   DOI=10.1002/(sici)1098-2264(199704)18:4<269::aid-gcc4>3.0.co;2-z;
RA   Wu Y., Nystroem-Lahti M., Osinga J., Looman M.W.G., Peltomaeki P.,
RA   Aaltonen L.A., de la Chapelle A., Hofstra R.M.W., Buys C.H.C.M.;
RT   "MSH2 and MLH1 mutations in sporadic replication error-positive colorectal
RT   carcinoma as assessed by two-dimensional DNA electrophoresis.";
RL   Genes Chromosomes Cancer 18:269-278(1997).
RN   [61]
RP   VARIANT HNPCC1 VAL-562.
RX   PubMed=9048925; DOI=10.1007/s004390050343;
RA   Beck N.E., Tomlinson I.P.M., Homfray T., Frayling I., Hodgson S.V.,
RA   Harocopos C.J., Bodmer W.F.;
RT   "Use of SSCP analysis to identify germline mutations in HNPCC families
RT   fulfilling the Amsterdam criteria.";
RL   Hum. Genet. 99:219-224(1997).
RN   [62]
RP   VARIANT HNPCC1 PHE-697, AND VARIANT ASP-322.
RX   PubMed=9298827;
RX   DOI=10.1002/(sici)1098-1004(1997)10:3<241::aid-humu12>3.0.co;2-#;
RA   Wehner M., Buschhausen L., Lamberti C., Kruse R., Caspari R., Propping P.,
RA   Friedl W.;
RT   "Hereditary nonpolyposis colorectal cancer (HNPCC): eight novel germline
RT   mutations in hMSH2 or hMLH1 genes.";
RL   Hum. Mutat. 10:241-244(1997).
RN   [63]
RP   VARIANT HNPCC1 265-VAL--GLN-314 DEL, AND VARIANTS GLY-641 AND VAL-770.
RX   PubMed=9718327; DOI=10.1086/301996;
RA   Farrington S.M., Lin-Goerke J., Ling J., Wang Y., Burczak J.D.,
RA   Robbins D.J., Dunlop M.G.;
RT   "Systematic analysis of hMSH2 and hMLH1 in young colon cancer patients and
RT   controls.";
RL   Am. J. Hum. Genet. 63:749-759(1998).
RN   [64]
RP   VARIANT GLIOMA ARG-199.
RX   PubMed=9777949; DOI=10.1016/s0002-9440(10)65662-3;
RA   Leung S.Y., Chan T.L., Chung L.P., Chan A.S.Y., Fan Y.W., Hung K.N.,
RA   Kwong W.K., Ho J.W.C., Yuen S.T.;
RT   "Microsatellite instability and mutation of DNA mismatch repair genes in
RT   gliomas.";
RL   Am. J. Pathol. 153:1181-1188(1998).
RN   [65]
RP   VARIANT CRC TYR-506, AND VARIANT HNPCC1 ILE-688.
RX   PubMed=9559627; DOI=10.1007/bf02235756;
RA   Yuan Y., Han H.-J., Zheng S., Park J.-G.;
RT   "Germline mutations of hMLH1 and hMSH2 genes in patients with suspected
RT   hereditary nonpolyposis colorectal cancer and sporadic early-onset
RT   colorectal cancer.";
RL   Dis. Colon Rectum 41:434-440(1998).
RN   [66]
RP   VARIANT ASP-322.
RX   PubMed=10023327; DOI=10.1016/s0959-8049(98)00217-2;
RA   Liu T., Stathopoulos P., Lindblom P., Rubio C., Wasteson Arver B.,
RA   Iselius L., Holmberg E., Groenberg H., Lindblom A.;
RT   "MSH2 codon 322 Gly to Asp seems not to confer an increased risk for
RT   colorectal cancer susceptibility.";
RL   Eur. J. Cancer 34:1981-1981(1998).
RN   [67]
RP   VARIANT HNPCC1 PHE-390.
RX   PubMed=9621522; DOI=10.1007/s100380050057;
RA   Okamura S., Koyama K., Miyoshi Y., Monden M., Takami M.;
RT   "Novel germline mutations of hMSH2 in a patient with hereditary
RT   nonpolyposis colorectal cancer 'HNPCC' and in a patient with six primary
RT   cancers.";
RL   J. Hum. Genet. 43:143-145(1998).
RN   [68]
RP   VARIANTS HNPCC1 SER-336 AND ASN-596 DEL.
RX   PubMed=10375096;
RX   DOI=10.1002/(sici)1097-0142(19990615)85:12<2512::aid-cncr4>3.0.co;2-g;
RA   Heinimann K., Scott R.J., Buerstedde J.-M., Weber W., Siebold K.,
RA   Attenhofer M., Mueller H., Dobbie Z.;
RT   "Influence of selection criteria on mutation detection in patients with
RT   hereditary nonpolyposis colorectal cancer.";
RL   Cancer 85:2512-2518(1999).
RN   [69]
RP   CHARACTERIZATION OF VARIANTS ASP-322; PHE-390; LYS-419; TYR-506; PRO-524;
RP   LEU-622 AND PHE-697.
RX   PubMed=10469597; DOI=10.1016/s0960-9822(99)80396-0;
RA   Drotschmann K., Clark A.B., Kunkel T.A.;
RT   "Mutator phenotypes of common polymorphisms and missense mutations in
RT   MSH2.";
RL   Curr. Biol. 9:907-910(1999).
RN   [70]
RP   VARIANTS HNPCC1 GLN-246; SER-596 AND THR-834, AND VARIANT ASP-322.
RX   PubMed=10573010; DOI=10.1038/sj.ejhg.5200363;
RA   Genuardi M., Carrara S., Anti M., Ponz de Leon M., Viel A.;
RT   "Assessment of pathogenicity criteria for constitutional missense mutations
RT   of the hereditary nonpolyposis colorectal cancer genes MLH1 and MSH2.";
RL   Eur. J. Hum. Genet. 7:778-782(1999).
RN   [71]
RP   VARIANT HNPCC1 PHE-390.
RX   PubMed=10386556; DOI=10.1001/jama.281.24.2316;
RA   Weber T.K., Chin H.-M., Rodriguez-Bigas M., Keitz B., Gilligan R.,
RA   O'Malley L., Urf E., Diba N., Pazik J., Petrelli N.J.;
RT   "Novel hMLH1 and hMSH2 germline mutations in African Americans with
RT   colorectal cancer.";
RL   JAMA 281:2316-2320(1999).
RN   [72]
RP   VARIANT HNPCC1 PRO-636.
RX   PubMed=10528862; DOI=10.1136/jmg.36.10.792;
RA   Yuan Z.Q., Wong N., Foulkes W.D., Alpert L., Manganaro F.,
RA   Andreutti-Zaugg C., Iggo R., Anthony K., Hsieh E., Redston M., Pinsky L.,
RA   Trifiro M., Gordon P.H., Lasko D.;
RT   "A missense mutation in both hMSH2 and APC in an Ashkenazi Jewish HNPCC
RT   kindred: implications for clinical screening.";
RL   J. Med. Genet. 36:790-793(1999).
RN   [73]
RP   VARIANTS HNPCC1 ILE-688 AND GLU-845, AND VARIANT MET-8.
RX   PubMed=10777691; DOI=10.1006/bbrc.2000.2547;
RA   Nomura S., Sugano K., Kashiwabara H., Taniguchi T., Fukayama N., Fujita S.,
RA   Akasu T., Moriya Y., Ohhigashi S., Kakizoe T., Sekiya T.;
RT   "Enhanced detection of deleterious and other germline mutations of hMSH2
RT   and hMLH1 in Japanese hereditary nonpolyposis colorectal cancer kindreds.";
RL   Biochem. Biophys. Res. Commun. 271:120-129(2000).
RN   [74]
RP   VARIANT ASP-322.
RX   PubMed=10713887; DOI=10.1038/sj.ejhg.5200393;
RA   Fidalgo P., Almeida M.R., West S., Gaspar C., Maia L., Wijnen J.,
RA   Albuquerque C., Curtis A., Cravo M., Fodde R., Leitao C.N., Burn J.;
RT   "Detection of mutations in mismatch repair genes in Portuguese families
RT   with hereditary non-polyposis colorectal cancer (HNPCC) by a multi-method
RT   approach.";
RL   Eur. J. Hum. Genet. 8:49-53(2000).
RN   [75]
RP   VARIANTS HNPCC1 ARG-692 AND ARG-697.
RX   PubMed=10612836;
RX   DOI=10.1002/(sici)1098-1004(200001)15:1<116::aid-humu24>3.0.co;2-q;
RA   Isidro G., Veiga I., Matos P., Almeida S., Bizarro S., Marshall B.,
RA   Baptista M., Leite J., Regateiro F., Soares J., Castedo S., Boavida M.G.;
RT   "Four novel MSH2 / MLH1 gene mutations in Portuguese HNPCC families.";
RL   Hum. Mutat. 15:116-116(2000).
RN   [76]
RP   VARIANT HNPCC1 ASN-603, AND VARIANT ASP-322.
RX   PubMed=10829038; DOI=10.1200/jco.2000.18.11.2193;
RA   Salovaara R., Loukola A., Kristo P., Kaeaeriaeinen H., Ahtola H.,
RA   Eskelinen M., Haerkoenen N., Julkunen R., Kangas E., Ojala S.,
RA   Tulikoura J., Valkamo E., Jaervinen H., Mecklin J.-P., Aaltonen L.A.,
RA   de la Chapelle A.;
RT   "Population-based molecular detection of hereditary nonpolyposis colorectal
RT   cancer.";
RL   J. Clin. Oncol. 18:2193-2200(2000).
RN   [77]
RP   ERRATUM OF PUBMED:10829038.
RA   Salovaara R., Loukola A., Kristo P., Kaeaeriaeinen H., Ahtola H.,
RA   Eskelinen M., Haerkoenen N., Julkunen R., Kangas E., Ojala S.,
RA   Tulikoura J., Valkamo E., Jaervinen H., Mecklin J.-P., Aaltonen L.A.,
RA   de la Chapelle A.;
RL   J. Clin. Oncol. 18:3456-3456(2000).
RN   [78]
RP   VARIANTS GASTRIC CANCER PHE-17; GLU-824; ALA-868; GLY-870 AND GLY-873, AND
RP   VARIANTS HNPCC1 CYS-98; TYR-323; ILE-335; ARG-629 AND VAL-714.
RX   PubMed=12132870;
RA   Kim J.C., Kim H.C., Roh S.A., Koo K.H., Lee D.H., Yu C.S., Lee J.H.,
RA   Kim T.W., Lee H.I., Beck N.E., Bodmer W.F.;
RT   "hMLH1 and hMSH2 mutations in families with familial clustering of gastric
RT   cancer and hereditary non-polyposis colorectal cancer.";
RL   Cancer Detect. Prev. 25:503-510(2001).
RN   [79]
RP   VARIANTS HNPCC1 ASP-161; VAL-216 AND ARG-554.
RX   PubMed=11726306;
RA   Mueller-Koch Y., Kopp R., Lohse P., Baretton G., Stoetzer A., Aust D.,
RA   Daum J., Kerker B., Gross M., Dietmeier W., Holinski-Feder E.;
RT   "Sixteen rare sequence variants of the hMLH1 and hMSH2 genes found in a
RT   cohort of 254 suspected HNPCC (hereditary non-polyposis colorectal cancer)
RT   patients: mutations or polymorphisms?";
RL   Eur. J. Med. Res. 6:473-482(2001).
RN   [80]
RP   CHARACTERIZATION OF VARIANTS ASP-322; LEU-622 AND TYR-639.
RX   PubMed=11555625; DOI=10.1093/hmg/10.18.1889;
RA   Ellison A.R., Lofing J., Bitter G.A.;
RT   "Functional analysis of human MLH1 and MSH2 missense variants and hybrid
RT   human-yeast MLH1 proteins in Saccharomyces cerevisiae.";
RL   Hum. Mol. Genet. 10:1889-1900(2001).
RN   [81]
RP   VARIANT HNPCC1 VAL-813.
RX   PubMed=12373605; DOI=10.1038/sj.bjc.6600565;
RA   Gille J.J.P., Hogervorst F.B.L., Pals G., Wijnen J.T., van Schooten R.J.,
RA   Dommering C.J., Meijer G.A., Craanen M.E., Nederlof P.M., de Jong D.,
RA   McElgunn C.J., Schouten J.P., Menko F.H.;
RT   "Genomic deletions of MSH2 and MLH1 in colorectal cancer families detected
RT   by a novel mutation detection approach.";
RL   Br. J. Cancer 87:892-897(2002).
RN   [82]
RP   VARIANTS HNPCC1 VAL-600 AND PHE-723.
RX   PubMed=11920458; DOI=10.1002/cncr.10332.abs;
RA   Furukawa T., Konishi F., Shitoh K., Kojima M., Nagai H., Tsukamoto T.;
RT   "Evaluation of screening strategy for detecting hereditary nonpolyposis
RT   colorectal carcinoma.";
RL   Cancer 94:911-920(2002).
RN   [83]
RP   VARIANTS HNPCC1 HIS-167; MET-393; PRO-524; ASN-596 DEL; LEU-622; SER-674
RP   AND ARG-905, AND CHARACTERIZATION OF VARIANTS HNPCC1 HIS-167; MET-393;
RP   PRO-524; ASN-596 DEL; LEU-622; SER-674 AND ARG-905.
RX   PubMed=12124176; DOI=10.1016/s1535-6108(02)00073-9;
RA   Heinen C.D., Wilson T., Mazurek A., Berardini M., Butz C., Fishel R.;
RT   "HNPCC mutations in hMSH2 result in reduced hMSH2-hMSH6 molecular switch
RT   functions.";
RL   Cancer Cell 1:469-478(2002).
RN   [84]
RP   INVOLVEMENT IN MULTIPLE CAFE-AU-LAIT SPOTS WITH LEUKEMIA.
RX   PubMed=11809679;
RA   Whiteside D., McLeod R., Graham G., Steckley J.L., Booth K.,
RA   Somerville M.J., Andrew S.E.;
RT   "A homozygous germ-line mutation in the human MSH2 gene predisposes to
RT   hematological malignancy and multiple cafe-au-lait spots.";
RL   Cancer Res. 62:359-362(2002).
RN   [85]
RP   VARIANT ASP-322.
RX   PubMed=11839723; DOI=10.1136/gut.50.3.405;
RA   Cravo M., Afonso A.J., Lage P., Albuquerque C., Maia L., Lacerda C.,
RA   Fidalgo P., Chaves P., Cruz C., Nobre-Leitao C.;
RT   "Pathogenicity of missense and splice site mutations in hMSH2 and hMLH1
RT   mismatch repair genes: implications for genetic testing.";
RL   Gut 50:405-412(2002).
RN   [86]
RP   VARIANTS HNPCC1 MET-44; VAL-45; ASN-596 DEL; GLY-886 AND GLU-923.
RX   PubMed=12112654; DOI=10.1002/humu.10083;
RA   Bisgaard M.L., Jaeger A.C., Myrhoej T., Bernstein I., Nielsen F.C.;
RT   "Hereditary non-polyposis colorectal cancer (HNPCC): phenotype-genotype
RT   correlation between patients with and without identified mutation.";
RL   Hum. Mutat. 20:20-27(2002).
RN   [87]
RP   VARIANTS HNPCC1 ILE-102; ASP-163 AND ALA-564, AND VARIANT ASP-322.
RX   PubMed=12200596; DOI=10.1007/s00432-002-0361-2;
RA   Ward R., Meldrum C., Williams R., Mokany E., Scott R., Turner J.,
RA   Hawkins N., Burgess B., Groombridge C., Spigelman A.;
RT   "Impact of microsatellite testing and mismatch repair protein expression on
RT   the clinical interpretation of genetic testing in hereditary non-polyposis
RT   colorectal cancer.";
RL   J. Cancer Res. Clin. Oncol. 128:403-411(2002).
RN   [88]
RP   VARIANTS HNPCC1 HIS-167 AND SER-359.
RX   PubMed=11870161; DOI=10.1200/jco.2002.20.5.1203;
RA   Scartozzi M., Bianchi F., Rosati S., Galizia E., Antolini A., Loretelli C.,
RA   Piga A., Bearzi I., Cellerino R., Porfiri E.;
RT   "Mutations of hMLH1 and hMSH2 in patients with suspected hereditary
RT   nonpolyposis colorectal cancer: correlation with microsatellite instability
RT   and abnormalities of mismatch repair protein expression.";
RL   J. Clin. Oncol. 20:1203-1208(2002).
RN   [89]
RP   VARIANTS HNPCC1 LEU-92 DEL AND ALA-853, AND VARIANT ASP-322.
RX   PubMed=12362047; DOI=10.1136/jmg.39.10.e65;
RA   Kurzawski G., Suchy J., Kladny J., Safranow K., Jakubowska A., Elsakov P.,
RA   Kucinskas V., Gardovski J., Irmejs A., Sibul H., Huzarski T., Byrski T.,
RA   Debniak T., Cybulski C., Gronwald J., Oszurek O., Clark J., Gozdz S.,
RA   Niepsuj S., Slomski R., Plawski A., Lacka-Wojciechowska A., Rozmiarek A.,
RA   Fiszer-Maliszewska L., Bebenek M., Sorokin D., Stawicka M., Godlewski D.,
RA   Richter P., Brozek I., Wysocka B., Jawien A., Banaszkiewicz Z.,
RA   Kowalczyk J., Czudowska D., Goretzki P.E., Moeslein G., Lubinski J.;
RT   "Germline MSH2 and MLH1 mutational spectrum in HNPCC families from Poland
RT   and the Baltic States.";
RL   J. Med. Genet. 39:E65-E65(2002).
RN   [90]
RP   VARIANTS HNPCC1 PRO-552; SER-583 AND PRO-636.
RX   PubMed=12658575; DOI=10.1086/373963;
RA   Wagner A., Barrows A., Wijnen J.T., van der Klift H., Franken P.F.,
RA   Verkuijlen P., Nakagawa H., Geugien M., Jaghmohan-Changur S., Breukel C.,
RA   Meijers-Heijboer H., Morreau H., van Puijenbroek M., Burn J., Coronel S.,
RA   Kinarski Y., Okimoto R., Watson P., Lynch J.F., de la Chapelle A.,
RA   Lynch H.T., Fodde R.;
RT   "Molecular analysis of hereditary nonpolyposis colorectal cancer in the
RT   United States: high mutation detection rate among clinically selected
RT   families and characterization of an American founder genomic deletion of
RT   the MSH2 gene.";
RL   Am. J. Hum. Genet. 72:1088-1100(2003).
RN   [91]
RP   VARIANTS CRC ILE-13 AND ILE-342, AND VARIANT ASP-322.
RX   PubMed=14504054; DOI=10.1093/annonc/mdg402;
RA   Colombino M., Cossu A., Arba A., Manca A., Curci A., Avallone A.,
RA   Comella G., Botti G., Scintu F., Amoruso M., D'Abbicco D., d'Agnessa M.R.,
RA   Spanu A., Tanda F., Palmieri G.;
RT   "Microsatellite instability and mutation analysis among southern Italian
RT   patients with colorectal carcinoma: detection of different alterations
RT   accounting for MLH1 and MSH2 inactivation in familial cases.";
RL   Ann. Oncol. 14:1530-1536(2003).
RN   [92]
RP   VARIANT HNPCC1 SER-127.
RX   PubMed=12655564; DOI=10.1002/humu.9123;
RA   Chen-Shtoyerman R., Theodor L., Harmati E., Friedman E., Dacka S.,
RA   Kopelman Y., Sternberg A., Zarivach R., Bar-Meir S., Fireman Z.;
RT   "Genetic analysis of familial colorectal cancer in Israeli Arabs.";
RL   Hum. Mutat. 21:446-447(2003).
RN   [93]
RP   VARIANT HNPCC1 PRO-175.
RX   PubMed=12655568; DOI=10.1002/humu.9127;
RA   Bartosova Z., Fridrichova I., Bujalkova M., Wolf B., Ilencikova D.,
RA   Krizan P., Hlavcak P., Palaj J., Lukac L., Lukacova M., Boeoer A.,
RA   Haider R., Jiricny J., Nystroem-Lahti M., Marra G.;
RT   "Novel MLH1 and MSH2 germline mutations in the first HNPCC families
RT   identified in Slovakia.";
RL   Hum. Mutat. 21:449-449(2003).
RN   [94]
RP   VARIANTS HNPCC1 GLY-163 AND GLY-660.
RX   PubMed=14635101; DOI=10.1002/humu.10291;
RA   Taylor C.F., Charlton R.S., Burn J., Sheridan E., Taylor G.R.;
RT   "Genomic deletions in MSH2 or MLH1 are a frequent cause of hereditary non-
RT   polyposis colorectal cancer: identification of novel and recurrent
RT   deletions by MLPA.";
RL   Hum. Mutat. 22:428-433(2003).
RN   [95]
RP   VARIANTS CRC SER-40; VAL-169; ARG-203; PHE-390; LYS-419; CYS-619 AND
RP   ARG-629, AND VARIANT MET-8.
RX   PubMed=12792735;
RA   Yamada K., Zhong X., Kanazawa S., Koike J., Tsujita K., Hemmi H.;
RT   "Oncogenic pathway of sporadic colorectal cancer with novel germline
RT   missense mutations in the hMSH2 gene.";
RL   Oncol. Rep. 10:859-866(2003).
RN   [96]
RP   VARIANT HNPCC1 THR-931.
RX   PubMed=15046096;
RA   Sun M.H., Cai Q., Fu G., Ren S., Mo S., Xu Y., Ding C., Zhang T., Zhu X.,
RA   Xu X., Min D., Cai S., Luo D., Shi Y., Shi D.;
RT   "Gene symbol: hMSH2. Disease: hereditary nonpolyposis colorectal cancer.";
RL   Hum. Genet. 114:409-409(2004).
RN   [97]
RP   VARIANT HNPCC1 TYR-671.
RX   PubMed=15300854; DOI=10.1002/humu.9267;
RA   Sharp A., Pichert G., Lucassen A., Eccles D.;
RT   "RNA analysis reveals splicing mutations and loss of expression defects in
RT   MLH1 and BRCA1.";
RL   Hum. Mutat. 24:272-272(2004).
RN   [98]
RP   VARIANTS HNPCC1 LEU-440 DEL; TYR-506; ARG-629 AND ILE-688.
RX   PubMed=15365995; DOI=10.1002/humu.9277;
RA   Shin Y.-K., Heo S.-C., Shin J.-H., Hong S.-H., Ku J.-L., Yoo B.-C.,
RA   Kim I.-J., Park J.-G.;
RT   "Germline mutations in MLH1, MSH2 and MSH6 in Korean hereditary non-
RT   polyposis colorectal cancer families.";
RL   Hum. Mutat. 24:351-351(2004).
RN   [99]
RP   VARIANT HNPCC1 ARG-839, AND VARIANT ARG-629.
RX   PubMed=15613555; DOI=10.1093/jjco/hyh121;
RA   Yuan Y., Huang Y.-Q., Cai S.-R., Song Y.-M., Zheng S., Zhang S.-Z.;
RT   "Genetic characterization of Chinese hereditary non-polyposis colorectal
RT   cancer by DHPLC and multiplex PCR.";
RL   Jpn. J. Clin. Oncol. 34:660-666(2004).
RN   [100]
RP   VARIANTS HNPCC1 LEU-349 AND ASN-596 DEL.
RX   PubMed=15342696; DOI=10.1136/jmg.2004.020651;
RA   Domingo E., Laiho P., Ollikainen M., Pinto M., Wang L., French A.J.,
RA   Westra J., Frebourg T., Espin E., Armengol M., Hamelin R., Yamamoto H.,
RA   Hofstra R.M.W., Seruca R., Lindblom A., Peltomaeki P., Thibodeau S.N.,
RA   Aaltonen L.A., Schwartz S. Jr.;
RT   "BRAF screening as a low-cost effective strategy for simplifying HNPCC
RT   genetic testing.";
RL   J. Med. Genet. 41:664-668(2004).
RN   [101]
RP   VARIANT HNPCC1 PHE-93.
RX   PubMed=15896463; DOI=10.1016/j.canlet.2004.09.051;
RA   Baudi F., Fersini G., Lavecchia A., Terracciano R., Leone F., Quaresima B.,
RA   Faniello M.C., De Paola L., Doldo P., Cuda G., Costanzo F., Venuta S.;
RT   "A novel missense germline mutation in exon 2 of the hMSH2 gene in a HNPCC
RT   family from Southern Italy.";
RL   Cancer Lett. 223:285-291(2005).
RN   [102]
RP   VARIANTS HNPCC1 VAL-169; PHE-390; ALA-564 AND ARG-629, AND VARIANT CRC
RP   LYS-419.
RX   PubMed=15996210; DOI=10.1111/j.1399-0004.2005.00469.x;
RA   Lee S.-C., Guo J.-Y., Lim R., Soo R., Koay E., Salto-Tellez M., Leong A.,
RA   Goh B.-C.;
RT   "Clinical and molecular characteristics of hereditary non-polyposis
RT   colorectal cancer families in Southeast Asia.";
RL   Clin. Genet. 68:137-145(2005).
RN   [103]
RP   VARIANT HNPCC1 TYR-283.
RX   PubMed=15870828; DOI=10.1038/sj.ejhg.5201421;
RA   Wehner M., Mangold E., Sengteller M., Friedrichs N., Aretz S., Friedl W.,
RA   Propping P., Pagenstecher C.;
RT   "Hereditary nonpolyposis colorectal cancer: pitfalls in deletion screening
RT   in MSH2 and MLH1 genes.";
RL   Eur. J. Hum. Genet. 13:983-986(2005).
RN   [104]
RP   VARIANT HNPCC1 ARG-162.
RX   PubMed=15991316;
RA   Kohonen-Corish M.R.J., Otway R., Tetlow N., Hornby J., Doe W.F.;
RT   "Gene symbol: MSH2. Disease: hereditary nonpolyposis colorectal cancer.";
RL   Hum. Genet. 116:539-539(2005).
RN   [105]
RP   VARIANTS HNPCC1 THR-2; LEU-92 DEL; MET-145; PHE-390 AND ALA-853, AND
RP   VARIANT ASP-322.
RX   PubMed=16451135; DOI=10.1111/j.1399-0004.2006.00550.x;
RA   Kurzawski G., Suchy J., Lener M., Klujszo-Grabowska E., Kladny J.,
RA   Safranow K., Jakubowska K., Jakubowska A., Huzarski T., Byrski T.,
RA   Debniak T., Cybulski C., Gronwald J., Oszurek O., Oszutowska D.,
RA   Kowalska E., Gozdz S., Niepsuj S., Slomski R., Plawski A.,
RA   Lacka-Wojciechowska A., Rozmiarek A., Fiszer-Maliszewska L., Bebenek M.,
RA   Sorokin D., Sasiadek M.M., Stembalska A., Grzebieniak Z., Kilar E.,
RA   Stawicka M., Godlewski D., Richter P., Brozek I., Wysocka B., Limon J.,
RA   Jawien A., Banaszkiewicz Z., Janiszewska H., Kowalczyk J., Czudowska D.,
RA   Scott R.J., Lubinski J.;
RT   "Germline MSH2 and MLH1 mutational spectrum including large rearrangements
RT   in HNPCC families from Poland (update study).";
RL   Clin. Genet. 69:40-47(2006).
RN   [106]
RP   VARIANTS HNPCC1 PRO-33; ASP-161; ARG-162; ARG-164; PRO-173; PRO-187;
RP   TYR-333; ASN-603; PRO-636; PHE-697; 745-ILE-ILE-746 DEL AND LYS-749,
RP   VARIANTS VAL-272; THR-834 AND GLU-923, CHARACTERIZATION OF VARIANTS HNPCC1
RP   PRO-33; ASP-161; ARG-162; ARG-164; PRO-173; PRO-187; TYR-333; ASN-603;
RP   PRO-636; PHE-697; 745-ILE-ILE-746 DEL AND LYS-749, AND CHARACTERIZATION OF
RP   VARIANTS VAL-272; THR-834 AND GLU-923.
RX   PubMed=17101317; DOI=10.1053/j.gastro.2006.08.044;
RA   Ollila S., Sarantaus L., Kariola R., Chan P., Hampel H., Holinski-Feder E.,
RA   Macrae F., Kohonen-Corish M., Gerdes A.-M., Peltomaeki P., Mangold E.,
RA   de la Chapelle A., Greenblatt M., Nystroem M.;
RT   "Pathogenicity of MSH2 missense mutations is typically associated with
RT   impaired repair capability of the mutated protein.";
RL   Gastroenterology 131:1408-1417(2006).
RN   [107]
RP   VARIANT HNPCC1 ALA-162.
RX   PubMed=17128465;
RA   Leonardis D.;
RT   "Gene symbol: msh2. Disease: hereditary nonpolyposis colorectal cancer.";
RL   Hum. Genet. 119:675-675(2006).
RN   [108]
RP   VARIANT HNPCC1 ARG-674.
RX   PubMed=18625694; DOI=10.1136/gut.2008.156695;
RA   Ramsoekh D., Wagner A., van Leerdam M.E., Dinjens W.N., Steyerberg E.W.,
RA   Halley D.J., Kuipers E.J., Dooijes D.;
RT   "A high incidence of MSH6 mutations in Amsterdam criteria II-negative
RT   families tested in a diagnostic setting.";
RL   Gut 57:1539-1544(2008).
RN   [109]
RP   VARIANTS GLN-46; LYS-106; ASP-322; SER-596; LEU-670; ILE-779; SER-807;
RP   HIS-835 AND ARG-911.
RX   PubMed=18033691; DOI=10.1002/humu.20635;
RA   Barnetson R.A., Cartwright N., van Vliet A., Haq N., Drew K.,
RA   Farrington S., Williams N., Warner J., Campbell H., Porteous M.E.,
RA   Dunlop M.G.;
RT   "Classification of ambiguous mutations in DNA mismatch repair genes
RT   identified in a population-based study of colorectal cancer.";
RL   Hum. Mutat. 29:367-374(2008).
RN   [110]
RP   CHARACTERIZATION OF VARIANTS HNPCC1 PRO-33; SER-127; ASP-161; ARG-162;
RP   ARG-164; PRO-173; PRO-187; VAL-272; TYR-333; ASN-603; PRO-636; ALA-674;
RP   PHE-697; 745-ILE-ILE-746 DEL; LYS-749; THR-834 AND GLU-923, AND
RP   CHARACTERIZATION OF VARIANT ASP-322.
RX   PubMed=18951462; DOI=10.1002/humu.20893;
RA   Ollila S., Dermadi Bebek D., Jiricny J., Nystroem M.;
RT   "Mechanisms of pathogenicity in human MSH2 missense mutants.";
RL   Hum. Mutat. 29:1355-1363(2008).
RN   [111]
RP   VARIANTS HNPCC1 LEU-92 DEL; ARG-199; ASP-331; GLU-470; ASN-610; GLY-638;
RP   GLU-645; LEU-696; TYR-748 AND GLN-839, VARIANTS VAL-272; ASN-596 DEL;
RP   TYR-671; ARG-697 AND PHE-723, CHARACTERIZATION OF VARIANTS HNPCC1 LEU-92
RP   DEL; ARG-199; ASP-331; GLU-470; ASN-610; GLY-638; GLU-645; LEU-696; TYR-748
RP   AND GLN-839, AND CHARACTERIZATION OF VARIANTS VAL-272; ASN-596 DEL;
RP   TYR-671; ARG-697 AND PHE-723.
RX   PubMed=18561205; DOI=10.1002/humu.20796;
RA   Tournier I., Vezain M., Martins A., Charbonnier F., Baert-Desurmont S.,
RA   Olschwang S., Wang Q., Buisine M.P., Soret J., Tazi J., Frebourg T.,
RA   Tosi M.;
RT   "A large fraction of unclassified variants of the mismatch repair genes
RT   MLH1 and MSH2 is associated with splicing defects.";
RL   Hum. Mutat. 29:1412-1424(2008).
RN   [112]
RP   CHARACTERIZATION OF VARIANTS HNPCC1 ARG-162; HIS-167 AND SER-359.
RX   PubMed=18781619; DOI=10.1002/humu.20875;
RA   Belvederesi L., Bianchi F., Galizia E., Loretelli C., Bracci R.,
RA   Catalani R., Amati M., Cellerino R.;
RT   "MSH2 missense mutations and HNPCC syndrome: pathogenicity assessment in a
RT   human expression system.";
RL   Hum. Mutat. 29:E296-E309(2008).
RN   [113]
RP   CHARACTERIZATION OF VARIANTS HNPCC1 HIS-167; THR-305: LEU-622; ARG-639;
RP   ARG-674; PHE-697 AND THR-834.
RX   PubMed=18822302; DOI=10.1016/j.mrfmmm.2008.08.015;
RA   Lutzen A., de Wind N., Georgijevic D., Nielsen F.C., Rasmussen L.J.;
RT   "Functional analysis of HNPCC-related missense mutations in MSH2.";
RL   Mutat. Res. 645:44-55(2008).
RN   [114]
RP   CHARACTERIZATION OF VARIANTS HNPCC1 MET-44; VAL-45; HIS-167; THR-305;
RP   PHE-390; ASN-596 DEL; ARG-639; ARG-674; PHE-697; PHE-723 AND GLY-886, AND
RP   CHARACTERIZATION OF VARIANTS ASP-165; HIS-177; VAL-272; LEU-385; LEU-519;
RP   ALA-675; GLU-759; VAL-805; GLY-843 AND LEU-860.
RX   PubMed=22102614; DOI=10.1002/humu.22000;
RA   Drost M., Zonneveld J.B., van Hees S., Rasmussen L.J., Hofstra R.M.,
RA   de Wind N.;
RT   "A rapid and cell-free assay to test the activity of lynch syndrome-
RT   associated MSH2 and MSH6 missense variants.";
RL   Hum. Mutat. 33:488-494(2012).
RN   [115]
RP   CHARACTERIZATION OF VARIANTS SER-127; MET-145; GLN-205; ASP-322; PRO-328;
RP   ILE-367; GLU-487 AND ILE-909.
RX   PubMed=22581703; DOI=10.1002/humu.22119;
RA   Kantelinen J., Kansikas M., Candelin S., Hampel H., Smith B., Holm L.,
RA   Kariola R., Nystrom M.;
RT   "Mismatch repair analysis of inherited MSH2 and/or MSH6 variation pairs
RT   found in cancer patients.";
RL   Hum. Mutat. 33:1294-1301(2012).
RN   [116]
RP   VARIANT HNPCC1 ARG-669.
RX   PubMed=22371642; DOI=10.3748/wjg.v18.i8.814;
RA   Zahary M.N., Kaur G., Abu Hassan M.R., Singh H., Naik V.R., Ankathil R.;
RT   "Germline mutation analysis of MLH1 and MSH2 in Malaysian Lynch syndrome
RT   patients.";
RL   World J. Gastroenterol. 18:814-820(2012).
RN   [117]
RP   VARIANTS GLN-5; GLY-55; PRO-534; ILE-813 AND ARG-839, AND CHARACTERIZATION
RP   OF VARIANTS GLN-5; GLY-55; PRO-534; ILE-813 AND ARG-839.
RX   PubMed=28494185; DOI=10.1080/15384047.2017.1326439;
RA   Arora S., Huwe P.J., Sikder R., Shah M., Browne A.J., Lesh R., Nicolas E.,
RA   Deshpande S., Hall M.J., Dunbrack R.L. Jr., Golemis E.A.;
RT   "Functional analysis of rare variants in mismatch repair proteins augments
RT   results from computation-based predictive methods.";
RL   Cancer Biol. Ther. 18:519-533(2017).
CC   -!- FUNCTION: Component of the post-replicative DNA mismatch repair system
CC       (MMR). Forms two different heterodimers: MutS alpha (MSH2-MSH6
CC       heterodimer) and MutS beta (MSH2-MSH3 heterodimer) which binds to DNA
CC       mismatches thereby initiating DNA repair. When bound, heterodimers bend
CC       the DNA helix and shields approximately 20 base pairs. MutS alpha
CC       recognizes single base mismatches and dinucleotide insertion-deletion
CC       loops (IDL) in the DNA. MutS beta recognizes larger insertion-deletion
CC       loops up to 13 nucleotides long. After mismatch binding, MutS alpha or
CC       beta forms a ternary complex with the MutL alpha heterodimer, which is
CC       thought to be responsible for directing the downstream MMR events,
CC       including strand discrimination, excision, and resynthesis. Recruits
CC       DNA helicase MCM9 to chromatin which unwinds the mismatch containing
CC       DNA strand (PubMed:26300262). ATP binding and hydrolysis play a pivotal
CC       role in mismatch repair functions. The ATPase activity associated with
CC       MutS alpha regulates binding similar to a molecular switch: mismatched
CC       DNA provokes ADP-->ATP exchange, resulting in a discernible
CC       conformational transition that converts MutS alpha into a sliding clamp
CC       capable of hydrolysis-independent diffusion along the DNA backbone.
CC       This transition is crucial for mismatch repair. MutS alpha may also
CC       play a role in DNA homologous recombination repair. In melanocytes may
CC       modulate both UV-B-induced cell cycle regulation and apoptosis.
CC       {ECO:0000269|PubMed:10078208, ECO:0000269|PubMed:10660545,
CC       ECO:0000269|PubMed:15064730, ECO:0000269|PubMed:17611581,
CC       ECO:0000269|PubMed:21120944, ECO:0000269|PubMed:26300262,
CC       ECO:0000269|PubMed:9564049, ECO:0000269|PubMed:9822679,
CC       ECO:0000269|PubMed:9822680}.
CC   -!- SUBUNIT: Component of the DNA mismatch repair (MMR) complex composed at
CC       least of MSH2, MSH3, MSH6, PMS1 and MLH1 (PubMed:26300262). Heterodimer
CC       consisting of MSH2-MSH6 (MutS alpha) or MSH2-MSH3 (MutS beta)
CC       (PubMed:8942985). Both heterodimers form a ternary complex with MutL
CC       alpha (MLH1-PMS1) (PubMed:9788596, PubMed:10856833, PubMed:11427529,
CC       PubMed:11429708, PubMed:12414623, PubMed:14676842). Interacts with
CC       MCM9; the interaction recruits MCM9 to chromatin (PubMed:26300262).
CC       Interacts with MCM8 (PubMed:26300262). Interacts with EXO1
CC       (PubMed:9788596, PubMed:10856833, PubMed:11427529, PubMed:11429708,
CC       PubMed:12414623, PubMed:14676842). Part of the BRCA1-associated genome
CC       surveillance complex (BASC), which contains BRCA1, MSH2, MSH6, MLH1,
CC       ATM, BLM, PMS2 and the RAD50-MRE11-NBS1 protein complex
CC       (PubMed:10783165). This association could be a dynamic process changing
CC       throughout the cell cycle and within subnuclear domains
CC       (PubMed:10783165). Interacts with ATR (PubMed:14657349). Interacts with
CC       SLX4/BTBD12; this interaction is direct and links MutS beta to SLX4, a
CC       subunit of different structure-specific endonucleases
CC       (PubMed:19596235). Interacts with SMARCAD1 (PubMed:18675275).
CC       {ECO:0000269|PubMed:10783165, ECO:0000269|PubMed:10856833,
CC       ECO:0000269|PubMed:11427529, ECO:0000269|PubMed:11429708,
CC       ECO:0000269|PubMed:12414623, ECO:0000269|PubMed:14657349,
CC       ECO:0000269|PubMed:14676842, ECO:0000269|PubMed:18675275,
CC       ECO:0000269|PubMed:19596235, ECO:0000269|PubMed:26300262,
CC       ECO:0000269|PubMed:8942985, ECO:0000269|PubMed:9788596}.
CC   -!- INTERACTION:
CC       P43246; Q92624: APPBP2; NbExp=3; IntAct=EBI-355888, EBI-743771;
CC       P43246; Q9UQ84-1: EXO1; NbExp=3; IntAct=EBI-355888, EBI-944694;
CC       P43246; P09429: HMGB1; NbExp=2; IntAct=EBI-355888, EBI-389432;
CC       P43246; P20585: MSH3; NbExp=10; IntAct=EBI-355888, EBI-1164205;
CC       P43246; P52701: MSH6; NbExp=7; IntAct=EBI-355888, EBI-395529;
CC       P43246; Q8IY92: SLX4; NbExp=5; IntAct=EBI-355888, EBI-2370740;
CC       P43246; P39875: EXO1; Xeno; NbExp=2; IntAct=EBI-355888, EBI-6738;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:26300262}. Chromosome
CC       {ECO:0000269|PubMed:26300262}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P43246-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P43246-2; Sequence=VSP_045536;
CC   -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC       {ECO:0000269|PubMed:10856833}.
CC   -!- PTM: Phosphorylated by PRKCZ, which may prevent MutS alpha degradation
CC       by the ubiquitin-proteasome pathway. {ECO:0000269|PubMed:15808853}.
CC   -!- DISEASE: Hereditary non-polyposis colorectal cancer 1 (HNPCC1)
CC       [MIM:120435]: An autosomal dominant disease associated with marked
CC       increase in cancer susceptibility. It is characterized by a familial
CC       predisposition to early-onset colorectal carcinoma (CRC) and extra-
CC       colonic tumors of the gastrointestinal, urological and female
CC       reproductive tracts. HNPCC is reported to be the most common form of
CC       inherited colorectal cancer in the Western world. Clinically, HNPCC is
CC       often divided into two subgroups. Type I is characterized by hereditary
CC       predisposition to colorectal cancer, a young age of onset, and
CC       carcinoma observed in the proximal colon. Type II is characterized by
CC       increased risk for cancers in certain tissues such as the uterus,
CC       ovary, breast, stomach, small intestine, skin, and larynx in addition
CC       to the colon. Diagnosis of classical HNPCC is based on the Amsterdam
CC       criteria: 3 or more relatives affected by colorectal cancer, one a
CC       first degree relative of the other two; 2 or more generation affected;
CC       1 or more colorectal cancers presenting before 50 years of age;
CC       exclusion of hereditary polyposis syndromes. The term 'suspected HNPCC'
CC       or 'incomplete HNPCC' can be used to describe families who do not or
CC       only partially fulfill the Amsterdam criteria, but in whom a genetic
CC       basis for colon cancer is strongly suspected.
CC       {ECO:0000269|PubMed:10375096, ECO:0000269|PubMed:10386556,
CC       ECO:0000269|PubMed:10528862, ECO:0000269|PubMed:10573010,
CC       ECO:0000269|PubMed:10612836, ECO:0000269|PubMed:10777691,
CC       ECO:0000269|PubMed:10829038, ECO:0000269|PubMed:11726306,
CC       ECO:0000269|PubMed:11870161, ECO:0000269|PubMed:11920458,
CC       ECO:0000269|PubMed:12112654, ECO:0000269|PubMed:12124176,
CC       ECO:0000269|PubMed:12132870, ECO:0000269|PubMed:12200596,
CC       ECO:0000269|PubMed:12362047, ECO:0000269|PubMed:12373605,
CC       ECO:0000269|PubMed:12655564, ECO:0000269|PubMed:12655568,
CC       ECO:0000269|PubMed:12658575, ECO:0000269|PubMed:14635101,
CC       ECO:0000269|PubMed:15046096, ECO:0000269|PubMed:15300854,
CC       ECO:0000269|PubMed:15342696, ECO:0000269|PubMed:15365995,
CC       ECO:0000269|PubMed:15613555, ECO:0000269|PubMed:15870828,
CC       ECO:0000269|PubMed:15896463, ECO:0000269|PubMed:15991316,
CC       ECO:0000269|PubMed:15996210, ECO:0000269|PubMed:16451135,
CC       ECO:0000269|PubMed:17101317, ECO:0000269|PubMed:17128465,
CC       ECO:0000269|PubMed:18561205, ECO:0000269|PubMed:18625694,
CC       ECO:0000269|PubMed:18781619, ECO:0000269|PubMed:18822302,
CC       ECO:0000269|PubMed:18951462, ECO:0000269|PubMed:21120944,
CC       ECO:0000269|PubMed:22102614, ECO:0000269|PubMed:22371642,
CC       ECO:0000269|PubMed:7874129, ECO:0000269|PubMed:8261515,
CC       ECO:0000269|PubMed:8700523, ECO:0000269|PubMed:8797773,
CC       ECO:0000269|PubMed:8872463, ECO:0000269|PubMed:9048925,
CC       ECO:0000269|PubMed:9240418, ECO:0000269|PubMed:9298827,
CC       ECO:0000269|PubMed:9311737, ECO:0000269|PubMed:9419403,
CC       ECO:0000269|PubMed:9559627, ECO:0000269|PubMed:9621522,
CC       ECO:0000269|PubMed:9718327, ECO:0000269|PubMed:9889267}. Note=The
CC       disease is caused by variants affecting the gene represented in this
CC       entry.
CC   -!- DISEASE: Muir-Torre syndrome (MRTES) [MIM:158320]: Rare autosomal
CC       dominant disorder characterized by sebaceous neoplasms and visceral
CC       malignancy. {ECO:0000269|PubMed:7713503}. Note=The disease is caused by
CC       variants affecting the gene represented in this entry.
CC   -!- DISEASE: Endometrial cancer (ENDMC) [MIM:608089]: A malignancy of
CC       endometrium, the mucous lining of the uterus. Most endometrial cancers
CC       are adenocarcinomas, cancers that begin in cells that make and release
CC       mucus and other fluids. {ECO:0000305|PubMed:11306449,
CC       ECO:0000305|PubMed:21642682}. Note=Disease susceptibility is associated
CC       with variants affecting the gene represented in this entry.
CC   -!- DISEASE: Mismatch repair cancer syndrome 2 (MMRCS2) [MIM:619096]: An
CC       autosomal recessive form of mismatch repair cancer syndrome, a
CC       childhood cancer predisposition syndrome encompassing a broad tumor
CC       spectrum. This includes hematological malignancies, central nervous
CC       system tumors, Lynch syndrome-associated malignancies such as
CC       colorectal tumors as well as multiple intestinal polyps, embryonic
CC       tumors and rhabdomyosarcoma. Multiple cafe-au-lait macules, a feature
CC       reminiscent of neurofibromatosis type 1, are often found as first
CC       manifestation of the underlying cancer. {ECO:0000269|PubMed:12549480,
CC       ECO:0000269|PubMed:16372347}. Note=The disease is caused by variants
CC       affecting the gene represented in this entry.
CC   -!- DISEASE: Colorectal cancer (CRC) [MIM:114500]: A complex disease
CC       characterized by malignant lesions arising from the inner wall of the
CC       large intestine (the colon) and the rectum. Genetic alterations are
CC       often associated with progression from premalignant lesion (adenoma) to
CC       invasive adenocarcinoma. Risk factors for cancer of the colon and
CC       rectum include colon polyps, long-standing ulcerative colitis, and
CC       genetic family history. {ECO:0000269|PubMed:12792735,
CC       ECO:0000269|PubMed:14504054, ECO:0000269|PubMed:15996210,
CC       ECO:0000269|PubMed:9559627}. Note=Disease susceptibility may be
CC       associated with variants affecting the gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the DNA mismatch repair MutS family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC27930.1; Type=Frameshift; Note=The frameshift is caused by a single nucleotide deletion which is found in a HNPCC kindred.; Evidence={ECO:0000305};
CC   -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC       Haematology;
CC       URL="http://atlasgeneticsoncology.org/Genes/MSH2ID340ch2p22.html";
CC   -!- WEB RESOURCE: Name=Hereditary non-polyposis colorectal cancer db;
CC       URL="http://www.nfdht.nl/";
CC   -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC       URL="http://egp.gs.washington.edu/data/msh2/";
CC   ---------------------------------------------------------------------------
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CC   ---------------------------------------------------------------------------
DR   EMBL; U03911; AAA18643.1; -; mRNA.
DR   EMBL; U04045; AAA61870.1; -; mRNA.
DR   EMBL; U41221; AAA82080.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; U41206; AAA82080.1; JOINED; Genomic_DNA.
DR   EMBL; U41207; AAA82080.1; JOINED; Genomic_DNA.
DR   EMBL; U41208; AAA82080.1; JOINED; Genomic_DNA.
DR   EMBL; U41210; AAA82080.1; JOINED; Genomic_DNA.
DR   EMBL; U41211; AAA82080.1; JOINED; Genomic_DNA.
DR   EMBL; U41212; AAA82080.1; JOINED; Genomic_DNA.
DR   EMBL; U41213; AAA82080.1; JOINED; Genomic_DNA.
DR   EMBL; U41214; AAA82080.1; JOINED; Genomic_DNA.
DR   EMBL; U41215; AAA82080.1; JOINED; Genomic_DNA.
DR   EMBL; U41216; AAA82080.1; JOINED; Genomic_DNA.
DR   EMBL; U41217; AAA82080.1; JOINED; Genomic_DNA.
DR   EMBL; U41218; AAA82080.1; JOINED; Genomic_DNA.
DR   EMBL; U41219; AAA82080.1; JOINED; Genomic_DNA.
DR   EMBL; U41220; AAA82080.1; JOINED; Genomic_DNA.
DR   EMBL; L47583; AAB59564.1; -; mRNA.
DR   EMBL; L47582; AAB59565.1; -; mRNA.
DR   EMBL; L47581; AAA76858.1; -; mRNA.
DR   EMBL; AY601851; AAS99351.1; -; Genomic_DNA.
DR   EMBL; AK304496; BAG65304.1; -; mRNA.
DR   EMBL; BX649122; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AC079775; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC138655; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC021566; AAH21566.1; -; mRNA.
DR   EMBL; AF066081; AAC27930.1; ALT_FRAME; Genomic_DNA.
DR   CCDS; CCDS1834.1; -. [P43246-1]
DR   CCDS; CCDS58709.1; -. [P43246-2]
DR   PIR; I64819; I64819.
DR   RefSeq; NP_000242.1; NM_000251.2. [P43246-1]
DR   RefSeq; NP_001245210.1; NM_001258281.1. [P43246-2]
DR   PDB; 2O8B; X-ray; 2.75 A; A=1-934.
DR   PDB; 2O8C; X-ray; 3.37 A; A=1-934.
DR   PDB; 2O8D; X-ray; 3.00 A; A=1-934.
DR   PDB; 2O8E; X-ray; 3.30 A; A=1-934.
DR   PDB; 2O8F; X-ray; 3.25 A; A=1-934.
DR   PDB; 3THW; X-ray; 3.09 A; A=1-934.
DR   PDB; 3THX; X-ray; 2.70 A; A=1-934.
DR   PDB; 3THY; X-ray; 2.89 A; A=1-934.
DR   PDB; 3THZ; X-ray; 4.30 A; A=1-934.
DR   PDBsum; 2O8B; -.
DR   PDBsum; 2O8C; -.
DR   PDBsum; 2O8D; -.
DR   PDBsum; 2O8E; -.
DR   PDBsum; 2O8F; -.
DR   PDBsum; 3THW; -.
DR   PDBsum; 3THX; -.
DR   PDBsum; 3THY; -.
DR   PDBsum; 3THZ; -.
DR   AlphaFoldDB; P43246; -.
DR   SMR; P43246; -.
DR   BioGRID; 110573; 229.
DR   ComplexPortal; CPX-77; DNA mismatch repair MutSbeta complex.
DR   ComplexPortal; CPX-80; DNA mismatch repair MutSalpha complex.
DR   CORUM; P43246; -.
DR   DIP; DIP-35054N; -.
DR   IntAct; P43246; 68.
DR   MINT; P43246; -.
DR   STRING; 9606.ENSP00000233146; -.
DR   ChEMBL; CHEMBL4296019; -.
DR   GlyGen; P43246; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P43246; -.
DR   PhosphoSitePlus; P43246; -.
DR   SwissPalm; P43246; -.
DR   BioMuta; MSH2; -.
DR   DMDM; 1171032; -.
DR   EPD; P43246; -.
DR   jPOST; P43246; -.
DR   MassIVE; P43246; -.
DR   MaxQB; P43246; -.
DR   PaxDb; P43246; -.
DR   PeptideAtlas; P43246; -.
DR   PRIDE; P43246; -.
DR   ProteomicsDB; 55601; -. [P43246-1]
DR   ProteomicsDB; 5866; -.
DR   Antibodypedia; 4037; 736 antibodies from 49 providers.
DR   CPTC; P43246; 1 antibody.
DR   DNASU; 4436; -.
DR   Ensembl; ENST00000233146.7; ENSP00000233146.2; ENSG00000095002.15. [P43246-1]
DR   Ensembl; ENST00000543555.6; ENSP00000442697.1; ENSG00000095002.15. [P43246-2]
DR   GeneID; 4436; -.
DR   KEGG; hsa:4436; -.
DR   MANE-Select; ENST00000233146.7; ENSP00000233146.2; NM_000251.3; NP_000242.1.
DR   UCSC; uc002rvy.3; human. [P43246-1]
DR   CTD; 4436; -.
DR   DisGeNET; 4436; -.
DR   GeneCards; MSH2; -.
DR   GeneReviews; MSH2; -.
DR   HGNC; HGNC:7325; MSH2.
DR   HPA; ENSG00000095002; Low tissue specificity.
DR   MalaCards; MSH2; -.
DR   MIM; 114500; phenotype.
DR   MIM; 120435; phenotype.
DR   MIM; 158320; phenotype.
DR   MIM; 608089; phenotype.
DR   MIM; 609309; gene.
DR   MIM; 619096; phenotype.
DR   neXtProt; NX_P43246; -.
DR   OpenTargets; ENSG00000095002; -.
DR   Orphanet; 252202; Constitutional mismatch repair deficiency syndrome.
DR   Orphanet; 144; Lynch syndrome.
DR   Orphanet; 587; Muir-Torre syndrome.
DR   PharmGKB; PA31133; -.
DR   VEuPathDB; HostDB:ENSG00000095002; -.
DR   eggNOG; KOG0219; Eukaryota.
DR   GeneTree; ENSGT00550000074867; -.
DR   HOGENOM; CLU_002472_10_0_1; -.
DR   InParanoid; P43246; -.
DR   OMA; LFRIYQV; -.
DR   PhylomeDB; P43246; -.
DR   TreeFam; TF351780; -.
DR   PathwayCommons; P43246; -.
DR   Reactome; R-HSA-5358565; Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha).
DR   Reactome; R-HSA-5358606; Mismatch repair (MMR) directed by MSH2:MSH3 (MutSbeta).
DR   Reactome; R-HSA-5632927; Defective Mismatch Repair Associated With MSH3.
DR   Reactome; R-HSA-5632928; Defective Mismatch Repair Associated With MSH2.
DR   Reactome; R-HSA-5632968; Defective Mismatch Repair Associated With MSH6.
DR   Reactome; R-HSA-6796648; TP53 Regulates Transcription of DNA Repair Genes.
DR   SignaLink; P43246; -.
DR   SIGNOR; P43246; -.
DR   BioGRID-ORCS; 4436; 25 hits in 1082 CRISPR screens.
DR   ChiTaRS; MSH2; human.
DR   EvolutionaryTrace; P43246; -.
DR   GeneWiki; MSH2; -.
DR   GenomeRNAi; 4436; -.
DR   Pharos; P43246; Tbio.
DR   PRO; PR:P43246; -.
DR   Proteomes; UP000005640; Chromosome 2.
DR   RNAct; P43246; protein.
DR   Bgee; ENSG00000095002; Expressed in secondary oocyte and 192 other tissues.
DR   ExpressionAtlas; P43246; baseline and differential.
DR   Genevisible; P43246; HS.
DR   GO; GO:0000781; C:chromosome, telomeric region; HDA:BHF-UCL.
DR   GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR   GO; GO:0032301; C:MutSalpha complex; IDA:UniProtKB.
DR   GO; GO:0032302; C:MutSbeta complex; IDA:HGNC-UCL.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:Ensembl.
DR   GO; GO:0008094; F:ATP-dependent activity, acting on DNA; IDA:HGNC-UCL.
DR   GO; GO:0140664; F:ATP-dependent DNA damage sensor activity; IEA:InterPro.
DR   GO; GO:0019237; F:centromeric DNA binding; IEA:Ensembl.
DR   GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
DR   GO; GO:0003684; F:damaged DNA binding; IEA:Ensembl.
DR   GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR   GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
DR   GO; GO:0032137; F:guanine/thymine mispair binding; IMP:MGI.
DR   GO; GO:0008022; F:protein C-terminus binding; IPI:UniProtKB.
DR   GO; GO:0042803; F:protein homodimerization activity; IDA:HGNC-UCL.
DR   GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR   GO; GO:0030183; P:B cell differentiation; ISS:BHF-UCL.
DR   GO; GO:0019724; P:B cell mediated immunity; ISS:BHF-UCL.
DR   GO; GO:0008340; P:determination of adult lifespan; IEA:Ensembl.
DR   GO; GO:0006281; P:DNA repair; IDA:BHF-UCL.
DR   GO; GO:0006302; P:double-strand break repair; IEA:Ensembl.
DR   GO; GO:0007281; P:germ cell development; IEA:Ensembl.
DR   GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR   GO; GO:0042771; P:intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator; IEA:Ensembl.
DR   GO; GO:0045190; P:isotype switching; ISS:BHF-UCL.
DR   GO; GO:0043570; P:maintenance of DNA repeat elements; IMP:HGNC-UCL.
DR   GO; GO:0008584; P:male gonad development; ISS:BHF-UCL.
DR   GO; GO:0006298; P:mismatch repair; IDA:UniProtKB.
DR   GO; GO:0031573; P:mitotic intra-S DNA damage checkpoint signaling; IEA:Ensembl.
DR   GO; GO:0006312; P:mitotic recombination; IBA:GO_Central.
DR   GO; GO:0045910; P:negative regulation of DNA recombination; IDA:BHF-UCL.
DR   GO; GO:0043524; P:negative regulation of neuron apoptotic process; ISS:BHF-UCL.
DR   GO; GO:0006119; P:oxidative phosphorylation; IEA:Ensembl.
DR   GO; GO:0051096; P:positive regulation of helicase activity; IDA:BHF-UCL.
DR   GO; GO:0048298; P:positive regulation of isotype switching to IgA isotypes; IEA:Ensembl.
DR   GO; GO:0048304; P:positive regulation of isotype switching to IgG isotypes; IEA:Ensembl.
DR   GO; GO:0006301; P:postreplication repair; IDA:UniProtKB.
DR   GO; GO:0071168; P:protein localization to chromatin; IMP:UniProtKB.
DR   GO; GO:0010224; P:response to UV-B; ISS:BHF-UCL.
DR   GO; GO:0010165; P:response to X-ray; ISS:BHF-UCL.
DR   GO; GO:0016446; P:somatic hypermutation of immunoglobulin genes; IEA:Ensembl.
DR   GO; GO:0016447; P:somatic recombination of immunoglobulin gene segments; ISS:BHF-UCL.
DR   GO; GO:0002204; P:somatic recombination of immunoglobulin genes involved in immune response; IBA:GO_Central.
DR   Gene3D; 3.30.420.110; -; 1.
DR   Gene3D; 3.40.1170.10; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   IDEAL; IID00048; -.
DR   InterPro; IPR011184; DNA_mismatch_repair_Msh2.
DR   InterPro; IPR007695; DNA_mismatch_repair_MutS-lik_N.
DR   InterPro; IPR000432; DNA_mismatch_repair_MutS_C.
DR   InterPro; IPR007861; DNA_mismatch_repair_MutS_clamp.
DR   InterPro; IPR007696; DNA_mismatch_repair_MutS_core.
DR   InterPro; IPR016151; DNA_mismatch_repair_MutS_N.
DR   InterPro; IPR036187; DNA_mismatch_repair_MutS_sf.
DR   InterPro; IPR007860; DNA_mmatch_repair_MutS_con_dom.
DR   InterPro; IPR032642; Msh2.
DR   InterPro; IPR036678; MutS_con_dom_sf.
DR   InterPro; IPR045076; MutS_family.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR11361; PTHR11361; 1.
DR   PANTHER; PTHR11361:SF35; PTHR11361:SF35; 1.
DR   Pfam; PF01624; MutS_I; 1.
DR   Pfam; PF05188; MutS_II; 1.
DR   Pfam; PF05192; MutS_III; 1.
DR   Pfam; PF05190; MutS_IV; 1.
DR   Pfam; PF00488; MutS_V; 1.
DR   PIRSF; PIRSF005813; MSH2; 1.
DR   SMART; SM00534; MUTSac; 1.
DR   SMART; SM00533; MUTSd; 1.
DR   SUPFAM; SSF48334; SSF48334; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS00486; DNA_MISMATCH_REPAIR_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative splicing; ATP-binding; Chromosome;
KW   Disease variant; DNA damage; DNA repair; DNA-binding;
KW   Hereditary nonpolyposis colorectal cancer; Isopeptide bond;
KW   Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW   Tumor suppressor; Ubl conjugation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:22814378"
FT   CHAIN           2..934
FT                   /note="DNA mismatch repair protein Msh2"
FT                   /id="PRO_0000115183"
FT   REGION          601..671
FT                   /note="Interaction with EXO1"
FT   BINDING         669..676
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0007744|PubMed:22814378"
FT   MOD_RES         555
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   MOD_RES         567
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P43247"
FT   MOD_RES         921
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   CROSSLNK        430
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   VAR_SEQ         1..66
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039,
FT                   ECO:0000303|PubMed:17974005"
FT                   /id="VSP_045536"
FT   VARIANT         2
FT                   /note="A -> T (in HNPCC1; dbSNP:rs63750466)"
FT                   /evidence="ECO:0000269|PubMed:16451135"
FT                   /id="VAR_054511"
FT   VARIANT         5
FT                   /note="P -> Q (decreases protein levels; dbSNP:rs56170584)"
FT                   /evidence="ECO:0000269|PubMed:28494185"
FT                   /id="VAR_079822"
FT   VARIANT         8
FT                   /note="T -> M (in dbSNP:rs17217716)"
FT                   /evidence="ECO:0000269|PubMed:10777691,
FT                   ECO:0000269|PubMed:12792735, ECO:0000269|Ref.9"
FT                   /id="VAR_013171"
FT   VARIANT         13
FT                   /note="S -> I (in CRC; unknown pathological significance;
FT                   dbSNP:rs63749907)"
FT                   /evidence="ECO:0000269|PubMed:14504054"
FT                   /id="VAR_043736"
FT   VARIANT         17
FT                   /note="V -> F (in gastric cancer; unknown pathological
FT                   significance; cryptic acceptor splice site suppressed on ex
FT                   vivo splicing assay; dbSNP:rs63750966)"
FT                   /evidence="ECO:0000269|PubMed:12132870"
FT                   /id="VAR_043737"
FT   VARIANT         33
FT                   /note="T -> P (in HNPCC1; decreased mismatch repair
FT                   activity; dbSNP:rs63751107)"
FT                   /evidence="ECO:0000269|PubMed:17101317,
FT                   ECO:0000269|PubMed:18951462, ECO:0000269|PubMed:21120944"
FT                   /id="VAR_043738"
FT   VARIANT         40
FT                   /note="G -> S (in CRC; unknown pathological significance;
FT                   dbSNP:rs63751260)"
FT                   /evidence="ECO:0000269|PubMed:12792735"
FT                   /id="VAR_043739"
FT   VARIANT         43
FT                   /note="Y -> C (in dbSNP:rs17217723)"
FT                   /evidence="ECO:0000269|Ref.9"
FT                   /id="VAR_019233"
FT   VARIANT         44
FT                   /note="T -> M (in HNPCC1; unknown pathological
FT                   significance; no decrease in mismatch repair activity;
FT                   dbSNP:rs587779085)"
FT                   /evidence="ECO:0000269|PubMed:12112654,
FT                   ECO:0000269|PubMed:21120944, ECO:0000269|PubMed:22102614"
FT                   /id="VAR_043740"
FT   VARIANT         45
FT                   /note="A -> V (in HNPCC1; unknown pathological
FT                   significance; no decrease in mismatch repair activity;
FT                   dbSNP:rs63750285)"
FT                   /evidence="ECO:0000269|PubMed:12112654,
FT                   ECO:0000269|PubMed:21120944, ECO:0000269|PubMed:22102614"
FT                   /id="VAR_043741"
FT   VARIANT         46
FT                   /note="H -> Q (in HNPCC1; dbSNP:rs33946261)"
FT                   /evidence="ECO:0000269|PubMed:18033691,
FT                   ECO:0000269|PubMed:8700523"
FT                   /id="VAR_004470"
FT   VARIANT         55
FT                   /note="R -> G (decreases protein levels;
FT                   dbSNP:rs587782354)"
FT                   /evidence="ECO:0000269|PubMed:28494185"
FT                   /id="VAR_079823"
FT   VARIANT         92
FT                   /note="Missing (in HNPCC1; unknown pathological
FT                   significance)"
FT                   /evidence="ECO:0000269|PubMed:12362047,
FT                   ECO:0000269|PubMed:16451135, ECO:0000269|PubMed:18561205"
FT                   /id="VAR_043742"
FT   VARIANT         93
FT                   /note="L -> F (in HNPCC1; dbSNP:rs63751429)"
FT                   /evidence="ECO:0000269|PubMed:15896463"
FT                   /id="VAR_043743"
FT   VARIANT         96
FT                   /note="R -> H (in dbSNP:rs63750002)"
FT                   /evidence="ECO:0000269|PubMed:7726159"
FT                   /id="VAR_004471"
FT   VARIANT         98
FT                   /note="Y -> C (in HNPCC1; unknown pathological
FT                   significance; dbSNP:rs63750887)"
FT                   /evidence="ECO:0000269|PubMed:12132870"
FT                   /id="VAR_043744"
FT   VARIANT         102
FT                   /note="V -> I (in HNPCC1; dbSNP:rs193922373)"
FT                   /evidence="ECO:0000269|PubMed:12200596"
FT                   /id="VAR_043745"
FT   VARIANT         106
FT                   /note="R -> K (in dbSNP:rs41295286)"
FT                   /evidence="ECO:0000269|PubMed:18033691"
FT                   /id="VAR_038026"
FT   VARIANT         110
FT                   /note="K -> T (in HNPCC1; somatic mutation)"
FT                   /evidence="ECO:0000269|PubMed:9419403"
FT                   /id="VAR_043746"
FT   VARIANT         127
FT                   /note="N -> S (in HNPCC1; presumed to enhance cancer risk
FT                   considerably when associated with P-328; shows
FT                   significantly decreased repair efficiency when associated
FT                   with variant P-328; dbSNP:rs17217772)"
FT                   /evidence="ECO:0000269|PubMed:12655564,
FT                   ECO:0000269|PubMed:18951462, ECO:0000269|PubMed:21120944,
FT                   ECO:0000269|PubMed:22581703, ECO:0000269|Ref.9"
FT                   /id="VAR_019234"
FT   VARIANT         139
FT                   /note="N -> S (in HNPCC1; dbSNP:rs1553350676)"
FT                   /id="VAR_004472"
FT   VARIANT         145
FT                   /note="I -> M (in HNPCC1; unknown pathological
FT                   significance; normal mismatch repair activity;
FT                   dbSNP:rs63750124)"
FT                   /evidence="ECO:0000269|PubMed:16451135,
FT                   ECO:0000269|PubMed:21120944, ECO:0000269|PubMed:22581703"
FT                   /id="VAR_004473"
FT   VARIANT         161
FT                   /note="V -> D (in HNPCC1; decreased mismatch repair
FT                   activity; affects protein stability; loss of protein
FT                   expression; dbSNP:rs63750126)"
FT                   /evidence="ECO:0000269|PubMed:11726306,
FT                   ECO:0000269|PubMed:17101317, ECO:0000269|PubMed:18951462,
FT                   ECO:0000269|PubMed:21120944"
FT                   /id="VAR_012936"
FT   VARIANT         162
FT                   /note="G -> A (in HNPCC1; dbSNP:rs63750773)"
FT                   /evidence="ECO:0000269|PubMed:17128465"
FT                   /id="VAR_054512"
FT   VARIANT         162
FT                   /note="G -> R (in HNPCC1; decreased mismatch repair
FT                   activity; associated with an abnormal subcellular
FT                   localization pattern; affects protein stability; loss of
FT                   protein expression; dbSNP:rs63750624)"
FT                   /evidence="ECO:0000269|PubMed:15991316,
FT                   ECO:0000269|PubMed:17101317, ECO:0000269|PubMed:18781619,
FT                   ECO:0000269|PubMed:18951462, ECO:0000269|PubMed:21120944"
FT                   /id="VAR_043747"
FT   VARIANT         163
FT                   /note="V -> D (in HNPCC1; dbSNP:rs63750214)"
FT                   /evidence="ECO:0000269|PubMed:12200596"
FT                   /id="VAR_043748"
FT   VARIANT         163
FT                   /note="V -> G (in HNPCC1; dbSNP:rs63750214)"
FT                   /evidence="ECO:0000269|PubMed:14635101"
FT                   /id="VAR_022670"
FT   VARIANT         164
FT                   /note="G -> R (in HNPCC1; decreased mismatch repair
FT                   activity; affects protein stability; loss of protein
FT                   expression; dbSNP:rs63750582)"
FT                   /evidence="ECO:0000269|PubMed:17101317,
FT                   ECO:0000269|PubMed:18951462, ECO:0000269|PubMed:21120944"
FT                   /id="VAR_043749"
FT   VARIANT         165
FT                   /note="Y -> D (in HNPCC1; unknown pathological
FT                   significance; decreased mismatch repair activity;
FT                   dbSNP:rs587779163)"
FT                   /evidence="ECO:0000269|PubMed:22102614"
FT                   /id="VAR_067284"
FT   VARIANT         167
FT                   /note="D -> H (in HNPCC1; shows reduced mismatch binding;
FT                   does not show a decreased expression level of the MutS
FT                   alpha complex; not associated with an abnormal subcellular
FT                   localization pattern; normal mismatch repair activity;
FT                   dbSNP:rs63750255)"
FT                   /evidence="ECO:0000269|PubMed:11870161,
FT                   ECO:0000269|PubMed:12124176, ECO:0000269|PubMed:18781619,
FT                   ECO:0000269|PubMed:18822302, ECO:0000269|PubMed:22102614,
FT                   ECO:0000269|PubMed:8872463"
FT                   /id="VAR_004474"
FT   VARIANT         169
FT                   /note="I -> V (in HNPCC1 and CRC; unknown pathological
FT                   significance; dbSNP:rs63750716)"
FT                   /evidence="ECO:0000269|PubMed:12792735,
FT                   ECO:0000269|PubMed:15996210"
FT                   /id="VAR_043750"
FT   VARIANT         173
FT                   /note="L -> P (in HNPCC1; decreased mismatch repair
FT                   activity; affects protein stability; loss of protein
FT                   expression; dbSNP:rs63750070)"
FT                   /evidence="ECO:0000269|PubMed:17101317,
FT                   ECO:0000269|PubMed:18951462, ECO:0000269|PubMed:21120944"
FT                   /id="VAR_043751"
FT   VARIANT         175
FT                   /note="L -> P (in HNPCC1; dbSNP:rs63751291)"
FT                   /evidence="ECO:0000269|PubMed:12655568"
FT                   /id="VAR_043752"
FT   VARIANT         177
FT                   /note="E -> H (in HNPCC1; requires 2 nucleotide
FT                   substitutions; unknown pathological significance; normal
FT                   mismatch repair activity)"
FT                   /evidence="ECO:0000269|PubMed:22102614"
FT                   /id="VAR_067285"
FT   VARIANT         187
FT                   /note="L -> P (in HNPCC1; decreased mismatch repair
FT                   activity; affects protein stability; loss of protein
FT                   expression; dbSNP:rs63751444)"
FT                   /evidence="ECO:0000269|PubMed:17101317,
FT                   ECO:0000269|PubMed:18951462, ECO:0000269|PubMed:21120944"
FT                   /id="VAR_043753"
FT   VARIANT         187
FT                   /note="L -> R (in HNPCC1; decreased mismatch repair
FT                   activity; loss of protein expression; dbSNP:rs63751444)"
FT                   /evidence="ECO:0000269|PubMed:21120944"
FT                   /id="VAR_076352"
FT   VARIANT         198
FT                   /note="E -> G (in HNPCC1; dbSNP:rs63750327)"
FT                   /id="VAR_054513"
FT   VARIANT         199
FT                   /note="C -> R (in glioma; also associated with HNPCC1; no
FT                   effect on MSH2 splicing; dbSNP:rs63751110)"
FT                   /evidence="ECO:0000269|PubMed:18561205,
FT                   ECO:0000269|PubMed:9777949"
FT                   /id="VAR_012937"
FT   VARIANT         203
FT                   /note="G -> R (in CRC; unknown pathological significance;
FT                   somatic mutation; dbSNP:rs587779973)"
FT                   /evidence="ECO:0000269|PubMed:12792735"
FT                   /id="VAR_043754"
FT   VARIANT         205
FT                   /note="E -> Q (shows no defects; normal mismatch repair
FT                   activity; dbSNP:rs63749984)"
FT                   /evidence="ECO:0000269|PubMed:22581703"
FT                   /id="VAR_068705"
FT   VARIANT         216
FT                   /note="I -> V (in HNPCC1; unknown pathological
FT                   significance; shows slightly reduced mismatch binding or
FT                   release efficiency; dbSNP:rs63749936)"
FT                   /evidence="ECO:0000269|PubMed:11726306"
FT                   /id="VAR_012938"
FT   VARIANT         246
FT                   /note="K -> Q (in HNPCC1; unknown pathological
FT                   significance; dbSNP:rs63750881)"
FT                   /evidence="ECO:0000269|PubMed:10573010"
FT                   /id="VAR_043755"
FT   VARIANT         265..314
FT                   /note="Missing (in HNPCC1)"
FT                   /evidence="ECO:0000269|PubMed:9718327"
FT                   /id="VAR_004475"
FT   VARIANT         272
FT                   /note="A -> V (in HNPCC1; unknown pathological
FT                   significance; shows slightly reduced mismatch binding or
FT                   release efficiency; results in partial MSH2 exon 5
FT                   skipping; normal mismatch repair activity;
FT                   dbSNP:rs34136999)"
FT                   /evidence="ECO:0000269|PubMed:17101317,
FT                   ECO:0000269|PubMed:18561205, ECO:0000269|PubMed:18951462,
FT                   ECO:0000269|PubMed:21120944, ECO:0000269|PubMed:22102614"
FT                   /id="VAR_043756"
FT   VARIANT         283
FT                   /note="D -> Y (in HNPCC1; dbSNP:rs63750381)"
FT                   /evidence="ECO:0000269|PubMed:15870828"
FT                   /id="VAR_043757"
FT   VARIANT         305
FT                   /note="A -> T (in HNPCC1; normal mismatch repair activity;
FT                   dbSNP:rs63751454)"
FT                   /evidence="ECO:0000269|PubMed:22102614,
FT                   ECO:0000269|PubMed:9311737"
FT                   /id="VAR_004476"
FT   VARIANT         322
FT                   /note="G -> D (may be associated with increased colorectal
FT                   cancer susceptibility; shows significantly decreased repair
FT                   efficiency when associated with variant E-487;
FT                   dbSNP:rs4987188)"
FT                   /evidence="ECO:0000269|PubMed:10023327,
FT                   ECO:0000269|PubMed:10469597, ECO:0000269|PubMed:10573010,
FT                   ECO:0000269|PubMed:10713887, ECO:0000269|PubMed:10829038,
FT                   ECO:0000269|PubMed:11555625, ECO:0000269|PubMed:11839723,
FT                   ECO:0000269|PubMed:12200596, ECO:0000269|PubMed:12362047,
FT                   ECO:0000269|PubMed:14504054, ECO:0000269|PubMed:16451135,
FT                   ECO:0000269|PubMed:18033691, ECO:0000269|PubMed:18951462,
FT                   ECO:0000269|PubMed:21120944, ECO:0000269|PubMed:22581703,
FT                   ECO:0000269|PubMed:8566964, ECO:0000269|PubMed:9087566,
FT                   ECO:0000269|PubMed:9298827, ECO:0000269|Ref.9"
FT                   /id="VAR_004477"
FT   VARIANT         323
FT                   /note="S -> C (in HNPCC1; unknown pathological
FT                   significance; dbSNP:rs63750732)"
FT                   /evidence="ECO:0000269|PubMed:9240418"
FT                   /id="VAR_012939"
FT   VARIANT         323
FT                   /note="S -> Y (in HNPCC1; unknown pathological
FT                   significance; dbSNP:rs63750732)"
FT                   /evidence="ECO:0000269|PubMed:12132870"
FT                   /id="VAR_043758"
FT   VARIANT         328
FT                   /note="A -> P (shows significantly decreased repair
FT                   efficiency when associated with variant S-127; presumed to
FT                   enhance cancer risk considerably when associated with
FT                   variant S-127; dbSNP:rs753237286)"
FT                   /evidence="ECO:0000269|PubMed:22581703"
FT                   /id="VAR_068706"
FT   VARIANT         331
FT                   /note="N -> D (in HNPCC1; no effect on MSH2 splicing;
FT                   dbSNP:rs267607938)"
FT                   /evidence="ECO:0000269|PubMed:18561205"
FT                   /id="VAR_054514"
FT   VARIANT         333
FT                   /note="C -> Y (in HNPCC1; decreased mismatch repair
FT                   activity; affects protein stability; loss of protein
FT                   expression; dbSNP:rs63750828)"
FT                   /evidence="ECO:0000269|PubMed:17101317,
FT                   ECO:0000269|PubMed:18951462, ECO:0000269|PubMed:21120944"
FT                   /id="VAR_043759"
FT   VARIANT         335
FT                   /note="T -> I (in HNPCC1; unknown pathological
FT                   significance; dbSNP:rs63750602)"
FT                   /evidence="ECO:0000269|PubMed:12132870"
FT                   /id="VAR_043760"
FT   VARIANT         336
FT                   /note="P -> S (in HNPCC1; dbSNP:rs63751062)"
FT                   /evidence="ECO:0000269|PubMed:10375096"
FT                   /id="VAR_043761"
FT   VARIANT         342
FT                   /note="V -> I (in CRC; unknown pathological significance;
FT                   dbSNP:rs63749879)"
FT                   /evidence="ECO:0000269|PubMed:14504054"
FT                   /id="VAR_043762"
FT   VARIANT         349
FT                   /note="P -> L (in HNPCC1; dbSNP:rs587779067)"
FT                   /evidence="ECO:0000269|PubMed:15342696"
FT                   /id="VAR_043763"
FT   VARIANT         359
FT                   /note="R -> S (in HNPCC1; shows a decreased expression
FT                   level of the MutS alpha complex; associated with an
FT                   abnormal subcellular localization pattern;
FT                   dbSNP:rs63751617)"
FT                   /evidence="ECO:0000269|PubMed:11870161,
FT                   ECO:0000269|PubMed:18781619"
FT                   /id="VAR_043764"
FT   VARIANT         367
FT                   /note="V -> I (shows no defects; normal mismatch repair
FT                   activity; dbSNP:rs80285180)"
FT                   /evidence="ECO:0000269|PubMed:22581703"
FT                   /id="VAR_068707"
FT   VARIANT         385
FT                   /note="P -> L (in HNPCC1; unknown pathological
FT                   significance; normal mismatch repair activity;
FT                   dbSNP:rs564736113)"
FT                   /evidence="ECO:0000269|PubMed:22102614"
FT                   /id="VAR_067286"
FT   VARIANT         390
FT                   /note="L -> F (in HNPCC1 and CRC; unknown pathological
FT                   significance; may decrease mismatch repair activity;
FT                   dbSNP:rs17224367)"
FT                   /evidence="ECO:0000269|PubMed:10386556,
FT                   ECO:0000269|PubMed:10469597, ECO:0000269|PubMed:12792735,
FT                   ECO:0000269|PubMed:15996210, ECO:0000269|PubMed:16451135,
FT                   ECO:0000269|PubMed:22102614, ECO:0000269|PubMed:8690195,
FT                   ECO:0000269|PubMed:9621522, ECO:0000269|Ref.9"
FT                   /id="VAR_004478"
FT   VARIANT         393
FT                   /note="K -> M (in HNPCC1; dbSNP:rs1558478490)"
FT                   /evidence="ECO:0000269|PubMed:12124176"
FT                   /id="VAR_043765"
FT   VARIANT         419
FT                   /note="Q -> K (in CRC; unknown pathological significance;
FT                   decreased mismatch repair activity; dbSNP:rs63750006)"
FT                   /evidence="ECO:0000269|PubMed:10469597,
FT                   ECO:0000269|PubMed:12792735, ECO:0000269|PubMed:15996210,
FT                   ECO:0000269|PubMed:8690195"
FT                   /id="VAR_012940"
FT   VARIANT         440
FT                   /note="Missing (in HNPCC1)"
FT                   /evidence="ECO:0000269|PubMed:15365995"
FT                   /id="VAR_043766"
FT   VARIANT         470
FT                   /note="V -> E (in HNPCC1; has no effect on ex vivo splicing
FT                   assay; dbSNP:rs267607959)"
FT                   /evidence="ECO:0000269|PubMed:18561205"
FT                   /id="VAR_054515"
FT   VARIANT         487
FT                   /note="D -> E (decreased mismatch repair activity; shows
FT                   significantly decreased repair efficiency when associated
FT                   with variant D-322; dbSNP:rs35107951)"
FT                   /evidence="ECO:0000269|PubMed:22581703"
FT                   /id="VAR_068708"
FT   VARIANT         492
FT                   /note="M -> V (in HNPCC1)"
FT                   /id="VAR_043767"
FT   VARIANT         506
FT                   /note="D -> Y (in HNPCC1 and CRC; sporadic early-onset CRC;
FT                   decreased mismatch repair activity; dbSNP:rs63750492)"
FT                   /evidence="ECO:0000269|PubMed:10469597,
FT                   ECO:0000269|PubMed:15365995, ECO:0000269|PubMed:8797773,
FT                   ECO:0000269|PubMed:9559627"
FT                   /id="VAR_012941"
FT   VARIANT         519
FT                   /note="F -> L (in HNPCC1; unknown pathological
FT                   significance; normal mismatch repair activity;
FT                   dbSNP:rs1371291280)"
FT                   /evidence="ECO:0000269|PubMed:21120944,
FT                   ECO:0000269|PubMed:22102614"
FT                   /id="VAR_067287"
FT   VARIANT         524
FT                   /note="R -> P (in HNPCC1; decreased mismatch repair
FT                   activity; dbSNP:rs63751207)"
FT                   /evidence="ECO:0000269|PubMed:10469597,
FT                   ECO:0000269|PubMed:12124176, ECO:0000269|PubMed:9889267"
FT                   /id="VAR_004479"
FT   VARIANT         534
FT                   /note="R -> P (no effect on protein levels;
FT                   dbSNP:rs587778523)"
FT                   /evidence="ECO:0000269|PubMed:28494185"
FT                   /id="VAR_079824"
FT   VARIANT         552
FT                   /note="T -> P (in HNPCC1; dbSNP:rs63750838)"
FT                   /evidence="ECO:0000269|PubMed:12658575"
FT                   /id="VAR_043768"
FT   VARIANT         554
FT                   /note="S -> R (in HNPCC1; unknown pathological
FT                   significance; dbSNP:rs63751656)"
FT                   /evidence="ECO:0000269|PubMed:11726306"
FT                   /id="VAR_012942"
FT   VARIANT         562
FT                   /note="E -> V (in HNPCC1; dbSNP:rs63750997)"
FT                   /evidence="ECO:0000269|PubMed:9048925"
FT                   /id="VAR_004480"
FT   VARIANT         564
FT                   /note="T -> A (in HNPCC1; unknown pathological
FT                   significance; dbSNP:rs55778204)"
FT                   /evidence="ECO:0000269|PubMed:12200596,
FT                   ECO:0000269|PubMed:15996210"
FT                   /id="VAR_043769"
FT   VARIANT         583
FT                   /note="N -> S (in HNPCC1; dbSNP:rs201118107)"
FT                   /evidence="ECO:0000269|PubMed:12658575"
FT                   /id="VAR_043770"
FT   VARIANT         596
FT                   /note="N -> S (in HNPCC1; unknown pathological
FT                   significance; dbSNP:rs41295288)"
FT                   /evidence="ECO:0000269|PubMed:10573010,
FT                   ECO:0000269|PubMed:18033691, ECO:0000269|PubMed:8993976"
FT                   /id="VAR_012943"
FT   VARIANT         596
FT                   /note="Missing (in HNPCC1; decreased mismatch repair
FT                   activity; has no effect on MSH2 splicing;
FT                   dbSNP:rs63749831)"
FT                   /evidence="ECO:0000269|PubMed:10375096,
FT                   ECO:0000269|PubMed:12112654, ECO:0000269|PubMed:12124176,
FT                   ECO:0000269|PubMed:15342696, ECO:0000269|PubMed:18561205,
FT                   ECO:0000269|PubMed:22102614, ECO:0000269|PubMed:7874129,
FT                   ECO:0000269|PubMed:8872463, ECO:0000269|PubMed:9311737"
FT                   /id="VAR_004481"
FT   VARIANT         600
FT                   /note="A -> V (in HNPCC1; dbSNP:rs63751236)"
FT                   /evidence="ECO:0000269|PubMed:11920458"
FT                   /id="VAR_043771"
FT   VARIANT         603
FT                   /note="D -> N (in HNPCC1; decreased mismatch repair
FT                   activity; affects protein stability; loss of protein
FT                   expression; dbSNP:rs63750657)"
FT                   /evidence="ECO:0000269|PubMed:10829038,
FT                   ECO:0000269|PubMed:17101317, ECO:0000269|PubMed:18951462,
FT                   ECO:0000269|PubMed:21120944"
FT                   /id="VAR_043772"
FT   VARIANT         610
FT                   /note="H -> N (in HNPCC1; has no effect on MSH2 splicing;
FT                   dbSNP:rs267607980)"
FT                   /evidence="ECO:0000269|PubMed:18561205"
FT                   /id="VAR_054516"
FT   VARIANT         619
FT                   /note="Y -> C (in CRC; unknown pathological significance;
FT                   dbSNP:rs63749982)"
FT                   /evidence="ECO:0000269|PubMed:12792735"
FT                   /id="VAR_043773"
FT   VARIANT         622
FT                   /note="P -> L (in HNPCC1; decreased mismatch repair
FT                   activity; confers multiple biochemical defects;
FT                   dbSNP:rs28929483)"
FT                   /evidence="ECO:0000269|PubMed:10469597,
FT                   ECO:0000269|PubMed:11555625, ECO:0000269|PubMed:12124176,
FT                   ECO:0000269|PubMed:18822302, ECO:0000269|PubMed:8261515"
FT                   /id="VAR_004482"
FT   VARIANT         629
FT                   /note="Q -> R (in HNPCC1; unknown pathological
FT                   significance; dbSNP:rs61756468)"
FT                   /evidence="ECO:0000269|PubMed:12132870,
FT                   ECO:0000269|PubMed:12792735, ECO:0000269|PubMed:15365995,
FT                   ECO:0000269|PubMed:15613555, ECO:0000269|PubMed:15996210"
FT                   /id="VAR_043774"
FT   VARIANT         636
FT                   /note="A -> P (in HNPCC1; decreased mismatch binding
FT                   activity; dbSNP:rs63750875)"
FT                   /evidence="ECO:0000269|PubMed:10528862,
FT                   ECO:0000269|PubMed:12658575, ECO:0000269|PubMed:17101317,
FT                   ECO:0000269|PubMed:18951462, ECO:0000269|PubMed:21120944"
FT                   /id="VAR_012944"
FT   VARIANT         638
FT                   /note="R -> G (in HNPCC1; has no effect on MSH2 splicing;
FT                   dbSNP:rs267607981)"
FT                   /evidence="ECO:0000269|PubMed:18561205"
FT                   /id="VAR_054517"
FT   VARIANT         639
FT                   /note="H -> R (in HNPCC1; decreased mismatch repair
FT                   activity; dbSNP:rs587779116)"
FT                   /evidence="ECO:0000269|PubMed:18822302,
FT                   ECO:0000269|PubMed:22102614, ECO:0000269|PubMed:9419403"
FT                   /id="VAR_043775"
FT   VARIANT         639
FT                   /note="H -> Y (in HNPCC1; the equivalent substitution in
FT                   yeast does not affect mismatch repair efficiency in vitro;
FT                   dbSNP:rs28929484)"
FT                   /evidence="ECO:0000269|PubMed:11555625,
FT                   ECO:0000269|PubMed:8261515"
FT                   /id="VAR_004483"
FT   VARIANT         641
FT                   /note="C -> G (in dbSNP:rs63749946)"
FT                   /evidence="ECO:0000269|PubMed:9718327"
FT                   /id="VAR_004484"
FT   VARIANT         645
FT                   /note="Q -> E (in HNPCC1; has no effect on MSH2 splicing;
FT                   dbSNP:rs267607982)"
FT                   /evidence="ECO:0000269|PubMed:18561205"
FT                   /id="VAR_054518"
FT   VARIANT         647
FT                   /note="E -> K (in HNPCC1)"
FT                   /evidence="ECO:0000269|PubMed:9419403"
FT                   /id="VAR_043776"
FT   VARIANT         656
FT                   /note="Y -> H (in HNPCC1; somatic mutation;
FT                   dbSNP:rs1573567393)"
FT                   /evidence="ECO:0000269|PubMed:9419403"
FT                   /id="VAR_043777"
FT   VARIANT         660
FT                   /note="D -> G (in HNPCC1; dbSNP:rs1085308057)"
FT                   /evidence="ECO:0000269|PubMed:14635101"
FT                   /id="VAR_022671"
FT   VARIANT         669
FT                   /note="G -> R (in HNPCC1; dbSNP:rs63751668)"
FT                   /evidence="ECO:0000269|PubMed:22371642"
FT                   /id="VAR_067761"
FT   VARIANT         670
FT                   /note="P -> L (in dbSNP:rs41294982)"
FT                   /evidence="ECO:0000269|PubMed:18033691"
FT                   /id="VAR_038027"
FT   VARIANT         671
FT                   /note="N -> Y (in HNPCC1; unknown pathological
FT                   significance; dbSNP:rs63751232)"
FT                   /evidence="ECO:0000269|PubMed:15300854,
FT                   ECO:0000269|PubMed:18561205"
FT                   /id="VAR_043778"
FT   VARIANT         674
FT                   /note="G -> A (in HNPCC1; decreased mismatch repair
FT                   activity; dbSNP:rs267607996)"
FT                   /evidence="ECO:0000269|PubMed:18951462,
FT                   ECO:0000269|PubMed:21120944"
FT                   /id="VAR_076353"
FT   VARIANT         674
FT                   /note="G -> R (in HNPCC1; decreased mismatch repair
FT                   activity; dbSNP:rs63750234)"
FT                   /evidence="ECO:0000269|PubMed:18625694,
FT                   ECO:0000269|PubMed:18822302, ECO:0000269|PubMed:22102614"
FT                   /id="VAR_067288"
FT   VARIANT         674
FT                   /note="G -> S (in HNPCC1; somatic mutation;
FT                   dbSNP:rs63750234)"
FT                   /evidence="ECO:0000269|PubMed:12124176"
FT                   /id="VAR_004485"
FT   VARIANT         675
FT                   /note="K -> A (in HNPCC1; requires 2 nucleotide
FT                   substitutions; unknown pathological significance; decreased
FT                   mismatch repair activity; dbSNP:rs587779128)"
FT                   /evidence="ECO:0000269|PubMed:22102614"
FT                   /id="VAR_067289"
FT   VARIANT         679
FT                   /note="I -> T (in HNPCC1; somatic mutation)"
FT                   /evidence="ECO:0000269|PubMed:9419403"
FT                   /id="VAR_043779"
FT   VARIANT         688
FT                   /note="M -> I (in HNPCC1; dbSNP:rs63750790)"
FT                   /evidence="ECO:0000269|PubMed:10777691,
FT                   ECO:0000269|PubMed:15365995, ECO:0000269|PubMed:9559627"
FT                   /id="VAR_012945"
FT   VARIANT         688
FT                   /note="M -> V (in HNPCC1; loss of protein expression)"
FT                   /evidence="ECO:0000269|PubMed:21120944"
FT                   /id="VAR_076354"
FT   VARIANT         692
FT                   /note="G -> R (in HNPCC1; dbSNP:rs63750232)"
FT                   /evidence="ECO:0000269|PubMed:10612836"
FT                   /id="VAR_009250"
FT   VARIANT         696
FT                   /note="P -> L (in HNPCC1; has no effect on ex vivo splicing
FT                   assay; dbSNP:rs267607994)"
FT                   /evidence="ECO:0000269|PubMed:18561205"
FT                   /id="VAR_054519"
FT   VARIANT         697
FT                   /note="C -> F (in HNPCC1; decreased mismatch repair
FT                   activity; loss of protein expression; confers multiple
FT                   biochemical defects; dbSNP:rs63750398)"
FT                   /evidence="ECO:0000269|PubMed:10469597,
FT                   ECO:0000269|PubMed:17101317, ECO:0000269|PubMed:18822302,
FT                   ECO:0000269|PubMed:18951462, ECO:0000269|PubMed:21120944,
FT                   ECO:0000269|PubMed:22102614, ECO:0000269|PubMed:9298827"
FT                   /id="VAR_004486"
FT   VARIANT         697
FT                   /note="C -> R (in HNPCC1; has no effect on MSH2 splicing;
FT                   dbSNP:rs63750961)"
FT                   /evidence="ECO:0000269|PubMed:10612836,
FT                   ECO:0000269|PubMed:18561205"
FT                   /id="VAR_009251"
FT   VARIANT         714
FT                   /note="A -> V (in HNPCC1; unknown pathological
FT                   significance; dbSNP:rs63751224)"
FT                   /evidence="ECO:0000269|PubMed:12132870"
FT                   /id="VAR_043780"
FT   VARIANT         722
FT                   /note="V -> I (associated with HNPCC1; dbSNP:rs587781996)"
FT                   /evidence="ECO:0000269|PubMed:21120944"
FT                   /id="VAR_076355"
FT   VARIANT         723
FT                   /note="S -> F (in HNPCC1; decreased mismatch repair
FT                   activity; has no effect on MSH2 splicing;
FT                   dbSNP:rs63750794)"
FT                   /evidence="ECO:0000269|PubMed:11920458,
FT                   ECO:0000269|PubMed:18561205, ECO:0000269|PubMed:22102614"
FT                   /id="VAR_043781"
FT   VARIANT         729
FT                   /note="M -> V (in HNPCC1; somatic mutation;
FT                   dbSNP:rs1558520059)"
FT                   /evidence="ECO:0000269|PubMed:9419403"
FT                   /id="VAR_043782"
FT   VARIANT         732
FT                   /note="T -> I (in HNPCC1; somatic mutation;
FT                   dbSNP:rs730881765)"
FT                   /evidence="ECO:0000269|PubMed:9419403"
FT                   /id="VAR_043783"
FT   VARIANT         745..746
FT                   /note="Missing (in HNPCC1; decreased mismatch repair
FT                   activity)"
FT                   /evidence="ECO:0000269|PubMed:17101317,
FT                   ECO:0000269|PubMed:18951462, ECO:0000269|PubMed:21120944"
FT                   /id="VAR_043784"
FT   VARIANT         748
FT                   /note="D -> Y (in HNPCC1; has no effect on MSH2 splicing;
FT                   dbSNP:rs267608007)"
FT                   /evidence="ECO:0000269|PubMed:18561205"
FT                   /id="VAR_054520"
FT   VARIANT         749
FT                   /note="E -> K (in HNPCC1; decreased mismatch repair
FT                   activity; no loss of protein expression; dbSNP:rs63751477)"
FT                   /evidence="ECO:0000269|PubMed:17101317,
FT                   ECO:0000269|PubMed:18951462, ECO:0000269|PubMed:21120944"
FT                   /id="VAR_043785"
FT   VARIANT         759
FT                   /note="G -> E (in HNPCC1; unknown pathological
FT                   significance; decreased mismatch repair activity;
FT                   dbSNP:rs386833406)"
FT                   /evidence="ECO:0000269|PubMed:22102614"
FT                   /id="VAR_067290"
FT   VARIANT         770
FT                   /note="I -> V (in dbSNP:rs63750684)"
FT                   /evidence="ECO:0000269|PubMed:9718327"
FT                   /id="VAR_004487"
FT   VARIANT         779
FT                   /note="M -> I (in dbSNP:rs41295292)"
FT                   /evidence="ECO:0000269|PubMed:18033691"
FT                   /id="VAR_038028"
FT   VARIANT         805
FT                   /note="L -> V (in HNPCC1; unknown pathological
FT                   significance; normal mismatch repair activity)"
FT                   /evidence="ECO:0000269|PubMed:22102614"
FT                   /id="VAR_067291"
FT   VARIANT         807
FT                   /note="T -> S (in dbSNP:rs41295294)"
FT                   /evidence="ECO:0000269|PubMed:18033691"
FT                   /id="VAR_038029"
FT   VARIANT         813
FT                   /note="M -> I (no effect on protein levels;
FT                   dbSNP:rs587781678)"
FT                   /evidence="ECO:0000269|PubMed:28494185"
FT                   /id="VAR_079825"
FT   VARIANT         813
FT                   /note="M -> V (in HNPCC1; dbSNP:rs63749841)"
FT                   /evidence="ECO:0000269|PubMed:12373605"
FT                   /id="VAR_043786"
FT   VARIANT         824
FT                   /note="Q -> E (in gastric cancer; unknown pathological
FT                   significance; dbSNP:rs63750623)"
FT                   /evidence="ECO:0000269|PubMed:12132870"
FT                   /id="VAR_043787"
FT   VARIANT         834
FT                   /note="A -> T (in HNPCC1; decreased mismatch repair
FT                   activity; shows no functional defects in gel shift assay;
FT                   dbSNP:rs63750757)"
FT                   /evidence="ECO:0000269|PubMed:10573010,
FT                   ECO:0000269|PubMed:17101317, ECO:0000269|PubMed:18822302,
FT                   ECO:0000269|PubMed:18951462, ECO:0000269|PubMed:21120944,
FT                   ECO:0000269|PubMed:9311737"
FT                   /id="VAR_004488"
FT   VARIANT         835
FT                   /note="N -> H (in dbSNP:rs41295296)"
FT                   /evidence="ECO:0000269|PubMed:18033691"
FT                   /id="VAR_038030"
FT   VARIANT         839
FT                   /note="H -> Q (in HNPCC1; has no effect on MSH2 splicing;
FT                   dbSNP:rs267608016)"
FT                   /evidence="ECO:0000269|PubMed:18561205"
FT                   /id="VAR_054521"
FT   VARIANT         839
FT                   /note="H -> R (in HNPCC1; decreases protein levels;
FT                   dbSNP:rs63750027)"
FT                   /evidence="ECO:0000269|PubMed:15613555,
FT                   ECO:0000269|PubMed:28494185"
FT                   /id="VAR_043788"
FT   VARIANT         843
FT                   /note="C -> G (in HNPCC1; unknown pathological
FT                   significance; normal mismatch repair activity)"
FT                   /evidence="ECO:0000269|PubMed:22102614"
FT                   /id="VAR_067292"
FT   VARIANT         845
FT                   /note="K -> E (in HNPCC1; dbSNP:rs63750571)"
FT                   /evidence="ECO:0000269|PubMed:10777691"
FT                   /id="VAR_013172"
FT   VARIANT         853
FT                   /note="E -> A (in HNPCC1; unknown pathological
FT                   significance; dbSNP:rs63750797)"
FT                   /evidence="ECO:0000269|PubMed:12362047,
FT                   ECO:0000269|PubMed:16451135"
FT                   /id="VAR_043789"
FT   VARIANT         860
FT                   /note="S -> L (in HNPCC1; unknown pathological
FT                   significance; normal mismatch repair activity;
FT                   dbSNP:rs63750849)"
FT                   /evidence="ECO:0000269|PubMed:22102614"
FT                   /id="VAR_067293"
FT   VARIANT         868
FT                   /note="P -> A (in gastric cancer; unknown pathological
FT                   significance; dbSNP:rs63751400)"
FT                   /evidence="ECO:0000269|PubMed:12132870"
FT                   /id="VAR_043790"
FT   VARIANT         870
FT                   /note="A -> G (in gastric cancer; unknown pathological
FT                   significance; dbSNP:rs63750709)"
FT                   /evidence="ECO:0000269|PubMed:12132870"
FT                   /id="VAR_043791"
FT   VARIANT         873
FT                   /note="C -> G (in gastric cancer; unknown pathological
FT                   significance; dbSNP:rs63750795)"
FT                   /evidence="ECO:0000269|PubMed:12132870"
FT                   /id="VAR_043792"
FT   VARIANT         886
FT                   /note="E -> G (in HNPCC1; unknown pathological
FT                   significance; normal mismatch repair activity;
FT                   dbSNP:rs63750350)"
FT                   /evidence="ECO:0000269|PubMed:12112654,
FT                   ECO:0000269|PubMed:21120944, ECO:0000269|PubMed:22102614"
FT                   /id="VAR_043793"
FT   VARIANT         905
FT                   /note="T -> R (in HNPCC1; unknown pathological
FT                   significance; dbSNP:rs267608022)"
FT                   /evidence="ECO:0000269|PubMed:12124176"
FT                   /id="VAR_004489"
FT   VARIANT         909
FT                   /note="K -> I (found in a colorectal cancer sample; normal
FT                   mismatch repair activity; dbSNP:rs34319539)"
FT                   /evidence="ECO:0000269|PubMed:22581703"
FT                   /id="VAR_068709"
FT   VARIANT         911
FT                   /note="L -> R (in dbSNP:rs41295182)"
FT                   /evidence="ECO:0000269|PubMed:18033691"
FT                   /id="VAR_038031"
FT   VARIANT         923
FT                   /note="V -> E (in HNPCC1; unknown pathological
FT                   significance; dbSNP:rs146421227)"
FT                   /evidence="ECO:0000269|PubMed:12112654,
FT                   ECO:0000269|PubMed:17101317, ECO:0000269|PubMed:18951462,
FT                   ECO:0000269|PubMed:21120944"
FT                   /id="VAR_043794"
FT   VARIANT         931
FT                   /note="K -> T (in HNPCC1; dbSNP:rs267608023)"
FT                   /evidence="ECO:0000269|PubMed:15046096"
FT                   /id="VAR_043795"
FT   MUTAGEN         675
FT                   /note="K->R: No effect on mismatch binding, complete loss
FT                   of DNA repair function when associated with MSH6 mutant R-
FT                   1140."
FT                   /evidence="ECO:0000269|PubMed:9564049"
FT   CONFLICT        784
FT                   /note="F -> I (in Ref. 7; BX649122)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        836
FT                   /note="F -> S (in Ref. 7; BX649122)"
FT                   /evidence="ECO:0000305"
FT   HELIX           14..24
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   STRAND          33..38
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   STRAND          40..46
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   HELIX           48..56
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   STRAND          59..61
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   STRAND          65..71
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   STRAND          75..81
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   HELIX           82..94
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   STRAND          99..105
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   STRAND          117..124
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   HELIX           129..131
FT                   /evidence="ECO:0007829|PDB:2O8B"
FT   HELIX           132..135
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   STRAND          147..152
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   STRAND          155..158
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   STRAND          160..167
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   TURN            168..171
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   STRAND          172..179
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   HELIX           185..194
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   STRAND          197..204
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   HELIX           208..220
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   STRAND          223..227
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   HELIX           229..232
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   HELIX           237..244
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   TURN            252..254
FT                   /evidence="ECO:0007829|PDB:2O8E"
FT   HELIX           255..257
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   HELIX           259..262
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   HELIX           264..277
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   HELIX           279..281
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   HELIX           283..285
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   STRAND          289..293
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   HELIX           296..298
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   HELIX           304..309
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   HELIX           326..330
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   HELIX           336..347
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   HELIX           353..367
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   HELIX           370..377
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   TURN            378..380
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   HELIX           381..383
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   HELIX           387..395
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   HELIX           401..411
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   HELIX           414..423
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   STRAND          424..426
FT                   /evidence="ECO:0007829|PDB:2O8F"
FT   STRAND          427..429
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   HELIX           432..435
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   HELIX           437..455
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   HELIX           462..464
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   TURN            472..474
FT                   /evidence="ECO:0007829|PDB:2O8B"
FT   HELIX           476..502
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   TURN            507..509
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   STRAND          512..515
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   TURN            517..519
FT                   /evidence="ECO:0007829|PDB:2O8B"
FT   STRAND          521..525
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   HELIX           527..530
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   TURN            531..535
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   STRAND          540..544
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   STRAND          549..552
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   HELIX           556..563
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   TURN            564..567
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   HELIX           568..585
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   HELIX           586..588
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   HELIX           589..613
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   STRAND          615..617
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   STRAND          623..625
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   STRAND          631..637
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   TURN            640..644
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   STRAND          653..658
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   TURN            659..661
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   STRAND          664..668
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   HELIX           675..691
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   STRAND          695..703
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   STRAND          706..711
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   HELIX           724..738
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   STRAND          744..749
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   HELIX           756..772
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   STRAND          777..783
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   HELIX           785..792
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   STRAND          797..807
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   STRAND          810..820
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   HELIX           827..833
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   HELIX           838..850
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   TURN            851..855
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   HELIX           875..892
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   HELIX           896..898
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   HELIX           901..917
FT                   /evidence="ECO:0007829|PDB:3THX"
FT   HELIX           921..928
FT                   /evidence="ECO:0007829|PDB:3THX"
SQ   SEQUENCE   934 AA;  104743 MW;  664A058C78242E05 CRC64;
     MAVQPKETLQ LESAAEVGFV RFFQGMPEKP TTTVRLFDRG DFYTAHGEDA LLAAREVFKT
     QGVIKYMGPA GAKNLQSVVL SKMNFESFVK DLLLVRQYRV EVYKNRAGNK ASKENDWYLA
     YKASPGNLSQ FEDILFGNND MSASIGVVGV KMSAVDGQRQ VGVGYVDSIQ RKLGLCEFPD
     NDQFSNLEAL LIQIGPKECV LPGGETAGDM GKLRQIIQRG GILITERKKA DFSTKDIYQD
     LNRLLKGKKG EQMNSAVLPE MENQVAVSSL SAVIKFLELL SDDSNFGQFE LTTFDFSQYM
     KLDIAAVRAL NLFQGSVEDT TGSQSLAALL NKCKTPQGQR LVNQWIKQPL MDKNRIEERL
     NLVEAFVEDA ELRQTLQEDL LRRFPDLNRL AKKFQRQAAN LQDCYRLYQG INQLPNVIQA
     LEKHEGKHQK LLLAVFVTPL TDLRSDFSKF QEMIETTLDM DQVENHEFLV KPSFDPNLSE
     LREIMNDLEK KMQSTLISAA RDLGLDPGKQ IKLDSSAQFG YYFRVTCKEE KVLRNNKNFS
     TVDIQKNGVK FTNSKLTSLN EEYTKNKTEY EEAQDAIVKE IVNISSGYVE PMQTLNDVLA
     QLDAVVSFAH VSNGAPVPYV RPAILEKGQG RIILKASRHA CVEVQDEIAF IPNDVYFEKD
     KQMFHIITGP NMGGKSTYIR QTGVIVLMAQ IGCFVPCESA EVSIVDCILA RVGAGDSQLK
     GVSTFMAEML ETASILRSAT KDSLIIIDEL GRGTSTYDGF GLAWAISEYI ATKIGAFCMF
     ATHFHELTAL ANQIPTVNNL HVTALTTEET LTMLYQVKKG VCDQSFGIHV AELANFPKHV
     IECAKQKALE LEEFQYIGES QGYDIMEPAA KKCYLEREQG EKIIQEFLSK VKQMPFTEMS
     EENITIKLKQ LKAEVIAKNN SFVNEIISRI KVTT
 
 
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