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DNA mismatch repair protein Msh2 (hMSH2) (MutS protein homolog 2)

 MSH2_HUMAN              Reviewed;         934 AA.
P43246; B4E2Z2; O75488;
01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
01-NOV-1995, sequence version 1.
30-AUG-2017, entry version 201.
RecName: Full=DNA mismatch repair protein Msh2;
Short=hMSH2;
AltName: Full=MutS protein homolog 2;
Name=MSH2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=8252616; DOI=10.1016/0092-8674(93)90546-3;
Fishel R., Lescoe M., Rao M., Copeland N.G., Jenkins N.A., Garber J.,
Kane M.F., Kolodner R.D.;
"The human mutator gene homolog MSH2 and its association with
hereditary nonpolyposis colon cancer.";
Cell 75:1027-1038(1993).
[2]
ERRATUM.
PubMed=8156592;
Fishel R., Lescoe M., Rao M., Copeland N.G., Jenkins N.A., Garber J.,
Kane M.F., Kolodner R.D.;
Cell 77:167-167(1994).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS HNPCC1 LEU-622
AND TYR-639.
PubMed=8261515; DOI=10.1016/0092-8674(93)90330-S;
Leach F.S., Nicolaides N.C., Papadopoulos N., Liu B., Jen J.,
Parsons R., Peltomaeki P., Sistonen P., Aaltonen L.A.,
Nystroem-Lahti M., Guan X.-Y., Zhang J., Meltzer P.S., Yu J.-W.,
Kao F.-T., Chen D.J., Cerosaletti K.M., Fournier R.E.K., Todd S.,
Lewis T., Leach R.J., Naylor S.L., Weissenbach J., Mecklin J.-P.,
Jaervinen H., Petersen G.M., Hamilton S.R., Green J., Jass J.,
Watson P., Lynch H.T., Trent J.M., de la Chapelle A., Kinzler K.W.,
Vogelstein B.;
"Mutations of a mutS homolog in hereditary nonpolyposis colorectal
cancer.";
Cell 75:1215-1225(1993).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INVOLVEMENT IN MRTES.
PubMed=7713503; DOI=10.1006/geno.1994.1661;
Kolodner R.D., Hall N.R., Lipford J., Kane M.F., Rao M.R.S.,
Morrison P., Wirth L., Finan P.J., Burn J., Chapman P., Earabino C.,
Merchant E., Bishop D.T.;
"Structure of the human MSH2 locus and analysis of two Muir-Torre
kindreds for msh2 mutations.";
Genomics 24:516-526(1994).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT HIS-96.
PubMed=7726159;
Wijnen J., Vasen H., Khan P.M., Menko F.H., van der Klift H.,
van Leeuwen C., van den Broek M., van Leeuwen-Cornelisse I.,
Nagengast F., Meijers-Heijboer A., Lindhout D., Griffioen G., Cats A.,
Kleibeuker J., Varesco L., Bertario L., Bisgaard M.-L., Mohr J.,
Fodde R.;
"Seven new mutations in hMSH2, an HNPCC gene, identified by denaturing
gradient-gel electrophoresis.";
Am. J. Hum. Genet. 56:1060-1066(1995).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Uterus;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Testis;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[9]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS MET-8; CYS-43;
SER-127; ASP-322 AND PHE-390.
NIEHS SNPs program;
Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Muscle;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[11]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 375-425.
TISSUE=Blood;
Corvello C.M., Bevilacqua R.A.U., Rossi B.M., Simpson A.J.G.;
"A novel germline mutation at exon 7 of the hMSH2 gene (417 del G) in
a large HNPCC Brazilian kindred.";
Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
[12]
DNA-BINDING.
PubMed=7923193;
Fishel R., Ewel A., Lescoe M.K.;
"Purified human MSH2 protein binds to DNA containing mismatched
nucleotides.";
Cancer Res. 54:5539-5542(1994).
[13]
DNA-BINDING.
PubMed=8769132; DOI=10.1006/bbrc.1996.1168;
Whitehouse A., Taylor G.R., Deeble J., Phillips S.E., Meredith D.M.,
Markham A.F.;
"A carboxy terminal domain of the hMSH-2 gene product is sufficient
for binding specific mismatched oligonucleotides.";
Biochem. Biophys. Res. Commun. 225:289-295(1996).
[14]
INTERACTION WITH MSH3 AND MSH6.
PubMed=8942985; DOI=10.1073/pnas.93.24.13629;
Acharya S., Wilson T., Gradia S., Kane M.F., Guerrette S.,
Marsischky G.T., Kolodner R.D., Fishel R.;
"hMSH2 forms specific mispair-binding complexes with hMSH3 and
hMSH6.";
Proc. Natl. Acad. Sci. U.S.A. 93:13629-13634(1996).
[15]
INTERACTION WITH EXO1.
PubMed=9788596;
Schmutte C., Marinescu R.C., Sadoff M.M., Guerrette S., Overhauser J.,
Fishel R.;
"Human exonuclease I interacts with the mismatch repair protein
hMSH2.";
Cancer Res. 58:4537-4542(1998).
[16]
FUNCTION.
PubMed=9822680; DOI=10.1074/jbc.273.48.32055;
Blackwell L.J., Martik D., Bjornson K.P., Bjornson E.S., Modrich P.;
"Nucleotide-promoted release of hMutSalpha from heteroduplex DNA is
consistent with an ATP-dependent translocation mechanism.";
J. Biol. Chem. 273:32055-32062(1998).
[17]
FUNCTION.
PubMed=9822679; DOI=10.1074/jbc.273.48.32049;
Blackwell L.J., Bjornson K.P., Modrich P.;
"DNA-dependent activation of the hMutSalpha ATPase.";
J. Biol. Chem. 273:32049-32054(1998).
[18]
FUNCTION, AND MUTAGENESIS OF LYS-675.
PubMed=9564049; DOI=10.1093/emboj/17.9.2677;
Iaccarino I., Marra G., Palombo F., Jiricny J.;
"hMSH2 and hMSH6 play distinct roles in mismatch binding and
contribute differently to the ATPase activity of hMutSalpha.";
EMBO J. 17:2677-2686(1998).
[19]
MISMATCH-BINDING, AND CHARACTERIZATION OF VARIANT HNPCC1 PRO-524.
PubMed=9889267; DOI=10.1093/nar/27.3.736;
Clark A.B., Cook M.E., Tran H.T., Gordenin D.A., Resnick M.A.,
Kunkel T.A.;
"Functional analysis of human MutSalpha and MutSbeta complexes in
yeast.";
Nucleic Acids Res. 27:736-742(1999).
[20]
FUNCTION.
PubMed=10078208; DOI=10.1016/S1097-2765(00)80316-0;
Gradia S., Subramanian D., Wilson T., Acharya S., Makhov A.,
Griffith J., Fishel R.;
"hMSH2-hMSH6 forms a hydrolysis-independent sliding clamp on
mismatched DNA.";
Mol. Cell 3:255-261(1999).
[21]
IDENTIFICATION OF MSH2 AS MEMBER OF BASC.
PubMed=10783165;
Wang Y., Cortez D., Yazdi P., Neff N., Elledge S.J., Qin J.;
"BASC, a super complex of BRCA1-associated proteins involved in the
recognition and repair of aberrant DNA structures.";
Genes Dev. 14:927-939(2000).
[22]
INTERACTION WITH EXO1, AND TISSUE SPECIFICITY.
PubMed=10856833; DOI=10.1016/S0921-8777(00)00012-4;
Rasmussen L.J., Rasmussen M., Lee B.-I., Rasmussen A.K.,
Wilson D.M. III, Nielsen F.C., Bisgaard H.C.;
"Identification of factors interacting with hMSH2 in the fetal liver
utilizing the yeast two-hybrid system. In vivo interaction through the
C-terminal domains of hEXO1 and hMSH2 and comparative expression
analysis.";
Mutat. Res. 460:41-52(2000).
[23]
FUNCTION.
PubMed=10660545; DOI=10.1074/jbc.275.6.3922;
Gradia S., Acharya S., Fishel R.;
"The role of mismatched nucleotides in activating the hMSH2-hMSH6
molecular switch.";
J. Biol. Chem. 275:3922-3930(2000).
[24]
POSSIBLE INVOLVEMENT IN ENDMC.
PubMed=11306449;
Schweizer P., Moisio A.L., Kuismanen S.A., Truninger K.,
Vierumaeki R., Salovaara R., Arola J., Butzow R., Jiricny J.,
Peltomaeki P., Nystroem-Lahti M.;
"Lack of MSH2 and MSH6 characterizes endometrial but not colon
carcinomas in hereditary nonpolyposis colorectal cancer.";
Cancer Res. 61:2813-2815(2001).
[25]
INTERACTION WITH EXO1.
PubMed=11427529; DOI=10.1074/jbc.M102670200;
Schmutte C., Sadoff M.M., Shim K.-S., Acharya S., Fishel R.;
"The interaction of DNA mismatch repair proteins with human
exonuclease I.";
J. Biol. Chem. 276:33011-33018(2001).
[26]
INTERACTION WITH EXO1.
PubMed=11429708; DOI=10.1038/sj.onc.1204467;
Jaeger A.C., Rasmussen M., Bisgaard H.C., Singh K.K., Nielsen F.C.,
Rasmussen L.J.;
"HNPCC mutations in the human DNA mismatch repair gene hMLH1 influence
assembly of hMutLalpha and hMLH1-hEXO1 complexes.";
Oncogene 20:3590-3595(2001).
[27]
INTERACTION WITH EXO1.
PubMed=12414623;
Sun X., Zheng L., Shen B.;
"Functional alterations of human exonuclease 1 mutants identified in
atypical hereditary nonpolyposis colorectal cancer syndrome.";
Cancer Res. 62:6026-6030(2002).
[28]
INVOLVEMENT IN MMRCS.
PubMed=12549480; DOI=10.1086/345297;
Bougeard G., Charbonnier F., Moerman A., Martin C., Ruchoux M.M.,
Drouot N., Frebourg T.;
"Early onset brain tumor and lymphoma in MSH2-deficient children.";
Am. J. Hum. Genet. 72:213-216(2003).
[29]
INTERACTION WITH ATR, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=14657349; DOI=10.1073/pnas.2536810100;
Wang Y., Qin J.;
"MSH2 and ATR form a signaling module and regulate two branches of the
damage response to DNA methylation.";
Proc. Natl. Acad. Sci. U.S.A. 100:15387-15392(2003).
[30]
INTERACTION WITH EXO1.
PubMed=14676842; DOI=10.1038/sj.onc.1207265;
Nielsen F.C., Jaeger A.C., Luetzen A., Bundgaard J.R., Rasmussen L.J.;
"Characterization of human exonuclease 1 in complex with mismatch
repair proteins, subcellular localization and association with PCNA.";
Oncogene 23:1457-1468(2004).
[31]
FUNCTION.
PubMed=15064730; DOI=10.1038/sj.onc.1207462;
Yang Q., Zhang R., Wang X.W., Linke S.P., Sengupta S., Hickson I.D.,
Pedrazzi G., Perrera C., Stagljar I., Littman S.J., Modrich P.,
Harris C.C.;
"The mismatch DNA repair heterodimer, hMSH2/6, regulates BLM
helicase.";
Oncogene 23:3749-3756(2004).
[32]
PHOSPHORYLATION BY PRKCZ.
PubMed=15808853; DOI=10.1016/j.jmb.2005.02.001;
Hernandez-Pigeon H., Quillet-Mary A., Louat T., Schambourg A.,
Humbert O., Selves J., Salles B., Laurent G., Lautier D.;
"hMutS alpha is protected from ubiquitin-proteasome-dependent
degradation by atypical protein kinase C zeta phosphorylation.";
J. Mol. Biol. 348:63-74(2005).
[33]
INVOLVEMENT IN MMRCS.
PubMed=16372347; DOI=10.1002/ajmg.a.31070;
Mueller A., Schackert H.K., Lange B., Rueschoff J., Fuezesi L.,
Willert J., Burfeind P., Shah P., Becker H., Epplen J.T., Stemmler S.;
"A novel MSH2 germline mutation in homozygous state in two brothers
with colorectal cancers diagnosed at the age of 11 and 12 years.";
Am. J. Med. Genet. A 140:195-199(2006).
[34]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic kidney;
PubMed=17525332; DOI=10.1126/science.1140321;
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
"ATM and ATR substrate analysis reveals extensive protein networks
responsive to DNA damage.";
Science 316:1160-1166(2007).
[35]
FUNCTION.
PubMed=17611581; DOI=10.1038/sj.jid.5700941;
Seifert M., Scherer S.J., Edelmann W., Bohm M., Meineke V.,
Lobrich M., Tilgen W., Reichrath J.;
"The DNA-mismatch repair enzyme hMSH2 modulates UV-B-induced cell
cycle arrest and apoptosis in melanoma cells.";
J. Invest. Dermatol. 128:203-213(2008).
[36]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-555, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[37]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[38]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[39]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-921, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[40]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-430, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[41]
CHARACTERIZATION OF VARIANTS HNPCC1 PRO-33; MET-44; VAL-45; SER-127;
MET-145; ASP-161; ARG-162; ARG-164; PRO-173; ARG-187; PRO-187;
VAL-272; TYR-333; LEU-519; ASN-603; PRO-636; ALA-674; VAL-688;
PHE-697; 745-ILE-ILE-746 DEL; LYS-749; THR-834; GLY-886 AND GLU-923,
CHARACTERIZATION OF VARIANTS ASP-322 AND ILE-722, AND FUNCTION.
PubMed=21120944; DOI=10.1002/humu.21409;
Kansikas M., Kariola R., Nystroem M.;
"Verification of the three-step model in assessing the pathogenicity
of mismatch repair gene variants.";
Hum. Mutat. 32:107-115(2011).
[42]
REVIEW.
PubMed=8036718; DOI=10.1016/0168-9525(94)90093-0;
Jiricny J.;
"Colon cancer and DNA repair: have mismatches met their match?";
Trends Genet. 10:164-168(1994).
[43]
REVIEW ON VARIANTS.
PubMed=9259192;
DOI=10.1002/(SICI)1098-1004(1997)10:2<89::AID-HUMU1>3.3.CO;2-K;
Papadopoulos N., Lindblom A.;
"Molecular basis of HNPCC: mutations of MMR genes.";
Hum. Mutat. 10:89-99(1997).
[44]
REVIEW.
PubMed=17080293; DOI=10.1007/s10735-006-9062-5;
Seifert M., Reichrath J.;
"The role of the human DNA mismatch repair gene hMSH2 in DNA repair,
cell cycle control and apoptosis: implications for pathogenesis,
progression and therapy of cancer.";
J. Mol. Histol. 37:301-307(2006).
[45]
INTERACTION WITH SMARCAD1.
PubMed=18675275; DOI=10.1016/j.jmb.2008.07.031;
Okazaki N., Ikeda S., Ohara R., Shimada K., Yanagawa T., Nagase T.,
Ohara O., Koga H.;
"The novel protein complex with SMARCAD1/KIAA1122 binds to the
vicinity of TSS.";
J. Mol. Biol. 382:257-265(2008).
[46]
INTERACTION WITH SLX4.
PubMed=19596235; DOI=10.1016/j.cell.2009.06.030;
Svendsen J.M., Smogorzewska A., Sowa M.E., O'Connell B.C., Gygi S.P.,
Elledge S.J., Harper J.W.;
"Mammalian BTBD12/SLX4 assembles a Holliday junction resolvase and is
required for DNA repair.";
Cell 138:63-77(2009).
[47]
POSSIBLE INVOLVEMENT IN ENDMC.
PubMed=21642682; DOI=10.1001/jama.2011.743;
French Cancer Genetics Network;
Bonadona V., Bonaiti B., Olschwang S., Grandjouan S., Huiart L.,
Longy M., Guimbaud R., Buecher B., Bignon Y.J., Caron O., Colas C.,
Nogues C., Lejeune-Dumoulin S., Olivier-Faivre L., Polycarpe-Osaer F.,
Nguyen T.D., Desseigne F., Saurin J.C., Berthet P., Leroux D.,
Duffour J., Manouvrier S., Frebourg T., Sobol H., Lasset C.,
Bonaiti-Pellie C.;
"Cancer risks associated with germline mutations in MLH1, MSH2, and
MSH6 genes in Lynch syndrome.";
JAMA 305:2304-2310(2011).
[48]
X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS).
PubMed=17531815; DOI=10.1016/j.molcel.2007.04.018;
Warren J.J., Pohlhaus T.J., Changela A., Iyer R.R., Modrich P.L.,
Beese L.S.;
"Structure of the human MutSalpha DNA lesion recognition complex.";
Mol. Cell 26:579-592(2007).
[49]
VARIANT HNPCC1 ASN-596 DEL.
PubMed=7874129;
Mary J.-L., Bishop T., Kolodner R.D., Lipford J.R., Kane M.F.,
Weber W., Torhorst J., Mueller H., Spycher M., Scott R.J.;
"Mutational analysis of the hMSH2 gene reveals a three base pair
deletion in a family predisposed to colorectal cancer development.";
Hum. Mol. Genet. 3:2067-2069(1994).
[50]
VARIANTS PHE-390 AND LYS-419.
PubMed=8690195; DOI=10.1053/gast.1996.v111.pm8690195;
Konishi M., Kikuchi-Yanoshita R., Tanaka K., Muraoka M., Onda A.,
Okumura Y., Kishi N., Iwama T., Mori T., Koike M., Ushio K., Chiba M.,
Nomizu S., Konishi F., Utsunomiya J., Miyaki M.;
"Molecular nature of colon tumors in hereditary nonpolyposis colon
cancer, familial polyposis, and sporadic colon cancer.";
Gastroenterology 111:307-317(1996).
[51]
VARIANT ASP-322.
PubMed=8566964; DOI=10.1007/BF02265276;
Maliaka Y.K., Chudina A.P., Belev N.F., Alday P., Bochkov N.P.,
Buerstedde J.-M.;
"CpG dinucleotides in the hMSH2 and hMLH1 genes are hotspots for HNPCC
mutations.";
Hum. Genet. 97:251-255(1996).
[52]
VARIANT HNPCC1 ASN-596 DEL, AND VARIANT HIS-167.
PubMed=8872463; DOI=10.1093/hmg/5.9.1245;
Moslein G., Tester D.J., Lindor N.M., Honchel R., Cunningham J.M.,
French A.J., Halling K.C., Schwab M., Goretzki P., Thibodeau S.N.;
"Microsatellite instability and mutation analysis of hMSH2 and hMLH1
in patients with sporadic, familial and hereditary colorectal
cancer.";
Hum. Mol. Genet. 5:1245-1252(1996).
[53]
VARIANT HNPCC1 TYR-506.
PubMed=8797773; DOI=10.1093/jnci/88.18.1317;
Han H.-J., Yuan Y., Ku J.-L., Oh J.-H., Won Y.-J., Kang K.J.,
Kim K.Y., Kim S., Kim C.Y., Kim J.-P., Oh N.-G., Lee K.H., Choe K.J.,
Nakamura Y., Park J.-G.;
"Germline mutations of hMLH1 and hMSH2 genes in Korean hereditary
nonpolyposis colorectal cancer.";
J. Natl. Cancer Inst. 88:1317-1319(1996).
[54]
VARIANT HNPCC1 GLN-46.
PubMed=8700523;
Bubb V.J., Curtis L.J., Cunningham C., Dunlop M.G., Carothers A.D.,
Morris R.G., White S., Bird C.C., Wyllie A.H.;
"Microsatellite instability and the role of hMSH2 in sporadic
colorectal cancer.";
Oncogene 12:2641-2649(1996).
[55]
VARIANTS HNPCC1 THR-305; ASN-596 DEL AND THR-834.
PubMed=9311737; DOI=10.1086/514847;
Wijnen J., Khan P.M., Vasen H., van der Klift H., Mulder A.,
van Leeuwen-Cornelisse I., Bakker B., Losekoot M., Moeller P.,
Fodde R.;
"Hereditary nonpolyposis colorectal cancer families not complying with
the Amsterdam criteria show extremely low frequency of mismatch-
repair-gene mutations.";
Am. J. Hum. Genet. 61:329-335(1997).
[56]
VARIANT HNPCC1 CYS-323.
PubMed=9240418; DOI=10.1006/bbrc.1997.6942;
Akiyama Y., Tsubouchi N., Yuasa Y.;
"Frequent somatic mutations of hMSH3 with reference to microsatellite
instability in hereditary nonpolyposis colorectal cancers.";
Biochem. Biophys. Res. Commun. 236:248-252(1997).
[57]
VARIANTS HNPCC1 THR-110; ARG-639; LYS-647; HIS-656; THR-679; VAL-729
AND ILE-732.
PubMed=9419403;
Nakahara M., Yokozaki H., Yasui W., Dohi K., Tahara E.;
"Identification of concurrent germ-line mutations in hMSH2 and/or
hMLH1 in Japanese hereditary nonpolyposis colorectal cancer
kindreds.";
Cancer Epidemiol. Biomarkers Prev. 6:1057-1064(1997).
[58]
VARIANT SER-596.
PubMed=8993976;
DOI=10.1002/(SICI)1098-2264(199701)18:1<8::AID-GCC2>3.0.CO;2-7;
Viel A., Genuardi M., Capozzi E., Leonardi F., Bellacosa A.,
Paravatou-Petsotas M., Pomponi M.G., Fornasarig M., Percesepe A.,
Roncucci L., Tamassia M.G., Benatti P., Ponz de Leon M., Valenti A.,
Covino M., Anti M., Foletto M., Boiocchi M., Neri G.;
"Characterization of MSH2 and MLH1 mutations in Italian families with
hereditary nonpolyposis colorectal cancer.";
Genes Chromosomes Cancer 18:8-18(1997).
[59]
VARIANT ASP-322.
PubMed=9087566;
DOI=10.1002/(SICI)1098-2264(199704)18:4<269::AID-GCC4>3.3.CO;2-9;
Wu Y., Nystroem-Lahti M., Osinga J., Looman M.W.G., Peltomaeki P.,
Aaltonen L.A., de la Chapelle A., Hofstra R.M.W., Buys C.H.C.M.;
"MSH2 and MLH1 mutations in sporadic replication error-positive
colorectal carcinoma as assessed by two-dimensional DNA
electrophoresis.";
Genes Chromosomes Cancer 18:269-278(1997).
[60]
VARIANT HNPCC1 VAL-562.
PubMed=9048925; DOI=10.1007/s004390050343;
Beck N.E., Tomlinson I.P.M., Homfray T., Frayling I., Hodgson S.V.,
Harocopos C.J., Bodmer W.F.;
"Use of SSCP analysis to identify germline mutations in HNPCC families
fulfilling the Amsterdam criteria.";
Hum. Genet. 99:219-224(1997).
[61]
VARIANT HNPCC1 PHE-697, AND VARIANT ASP-322.
PubMed=9298827;
DOI=10.1002/(SICI)1098-1004(1997)10:3<241::AID-HUMU12>3.0.CO;2-#;
Wehner M., Buschhausen L., Lamberti C., Kruse R., Caspari R.,
Propping P., Friedl W.;
"Hereditary nonpolyposis colorectal cancer (HNPCC): eight novel
germline mutations in hMSH2 or hMLH1 genes.";
Hum. Mutat. 10:241-244(1997).
[62]
VARIANT HNPCC1 265-VAL--GLN-314 DEL, AND VARIANTS GLY-641 AND VAL-770.
PubMed=9718327; DOI=10.1086/301996;
Farrington S.M., Lin-Goerke J., Ling J., Wang Y., Burczak J.D.,
Robbins D.J., Dunlop M.G.;
"Systematic analysis of hMSH2 and hMLH1 in young colon cancer patients
and controls.";
Am. J. Hum. Genet. 63:749-759(1998).
[63]
VARIANT GLIOMA ARG-199.
PubMed=9777949; DOI=10.1016/S0002-9440(10)65662-3;
Leung S.Y., Chan T.L., Chung L.P., Chan A.S.Y., Fan Y.W., Hung K.N.,
Kwong W.K., Ho J.W.C., Yuen S.T.;
"Microsatellite instability and mutation of DNA mismatch repair genes
in gliomas.";
Am. J. Pathol. 153:1181-1188(1998).
[64]
VARIANT CRC TYR-506, AND VARIANT HNPCC1 ILE-688.
PubMed=9559627; DOI=10.1007/BF02235756;
Yuan Y., Han H.-J., Zheng S., Park J.-G.;
"Germline mutations of hMLH1 and hMSH2 genes in patients with
suspected hereditary nonpolyposis colorectal cancer and sporadic
early-onset colorectal cancer.";
Dis. Colon Rectum 41:434-440(1998).
[65]
VARIANT ASP-322.
PubMed=10023327; DOI=10.1016/S0959-8049(98)00217-2;
Liu T., Stathopoulos P., Lindblom P., Rubio C., Wasteson Arver B.,
Iselius L., Holmberg E., Groenberg H., Lindblom A.;
"MSH2 codon 322 Gly to Asp seems not to confer an increased risk for
colorectal cancer susceptibility.";
Eur. J. Cancer 34:1981-1981(1998).
[66]
VARIANT HNPCC1 PHE-390.
PubMed=9621522; DOI=10.1007/s100380050057;
Okamura S., Koyama K., Miyoshi Y., Monden M., Takami M.;
"Novel germline mutations of hMSH2 in a patient with hereditary
nonpolyposis colorectal cancer 'HNPCC' and in a patient with six
primary cancers.";
J. Hum. Genet. 43:143-145(1998).
[67]
VARIANTS HNPCC1 SER-336 AND ASN-596 DEL.
PubMed=10375096;
DOI=10.1002/(SICI)1097-0142(19990615)85:12<2512::AID-CNCR4>3.0.CO;2-G;
Heinimann K., Scott R.J., Buerstedde J.-M., Weber W., Siebold K.,
Attenhofer M., Mueller H., Dobbie Z.;
"Influence of selection criteria on mutation detection in patients
with hereditary nonpolyposis colorectal cancer.";
Cancer 85:2512-2518(1999).
[68]
CHARACTERIZATION OF VARIANTS ASP-322; PHE-390; LYS-419; TYR-506;
PRO-524; LEU-622 AND PHE-697.
PubMed=10469597; DOI=10.1016/S0960-9822(99)80396-0;
Drotschmann K., Clark A.B., Kunkel T.A.;
"Mutator phenotypes of common polymorphisms and missense mutations in
MSH2.";
Curr. Biol. 9:907-910(1999).
[69]
VARIANTS HNPCC1 GLN-246; SER-596 AND THR-834, AND VARIANT ASP-322.
PubMed=10573010; DOI=10.1038/sj.ejhg.5200363;
Genuardi M., Carrara S., Anti M., Ponz de Leon M., Viel A.;
"Assessment of pathogenicity criteria for constitutional missense
mutations of the hereditary nonpolyposis colorectal cancer genes MLH1
and MSH2.";
Eur. J. Hum. Genet. 7:778-782(1999).
[70]
VARIANT HNPCC1 PHE-390.
PubMed=10386556; DOI=10.1001/jama.281.24.2316;
Weber T.K., Chin H.-M., Rodriguez-Bigas M., Keitz B., Gilligan R.,
O'Malley L., Urf E., Diba N., Pazik J., Petrelli N.J.;
"Novel hMLH1 and hMSH2 germline mutations in African Americans with
colorectal cancer.";
JAMA 281:2316-2320(1999).
[71]
VARIANT HNPCC1 PRO-636.
PubMed=10528862; DOI=10.1136/jmg.36.10.792;
Yuan Z.Q., Wong N., Foulkes W.D., Alpert L., Manganaro F.,
Andreutti-Zaugg C., Iggo R., Anthony K., Hsieh E., Redston M.,
Pinsky L., Trifiro M., Gordon P.H., Lasko D.;
"A missense mutation in both hMSH2 and APC in an Ashkenazi Jewish
HNPCC kindred: implications for clinical screening.";
J. Med. Genet. 36:790-793(1999).
[72]
VARIANTS HNPCC1 ILE-688 AND GLU-845, AND VARIANT MET-8.
PubMed=10777691; DOI=10.1006/bbrc.2000.2547;
Nomura S., Sugano K., Kashiwabara H., Taniguchi T., Fukayama N.,
Fujita S., Akasu T., Moriya Y., Ohhigashi S., Kakizoe T., Sekiya T.;
"Enhanced detection of deleterious and other germline mutations of
hMSH2 and hMLH1 in Japanese hereditary nonpolyposis colorectal cancer
kindreds.";
Biochem. Biophys. Res. Commun. 271:120-129(2000).
[73]
VARIANT ASP-322.
PubMed=10713887; DOI=10.1038/sj.ejhg.5200393;
Fidalgo P., Almeida M.R., West S., Gaspar C., Maia L., Wijnen J.,
Albuquerque C., Curtis A., Cravo M., Fodde R., Leitao C.N., Burn J.;
"Detection of mutations in mismatch repair genes in Portuguese
families with hereditary non-polyposis colorectal cancer (HNPCC) by a
multi-method approach.";
Eur. J. Hum. Genet. 8:49-53(2000).
[74]
VARIANTS HNPCC1 ARG-692 AND ARG-697.
PubMed=10612836;
DOI=10.1002/(SICI)1098-1004(200001)15:1<116::AID-HUMU24>3.0.CO;2-Q;
Isidro G., Veiga I., Matos P., Almeida S., Bizarro S., Marshall B.,
Baptista M., Leite J., Regateiro F., Soares J., Castedo S.,
Boavida M.G.;
"Four novel MSH2 / MLH1 gene mutations in Portuguese HNPCC families.";
Hum. Mutat. 15:116-116(2000).
[75]
VARIANT HNPCC1 ASN-603, AND VARIANT ASP-322.
PubMed=10829038;
Salovaara R., Loukola A., Kristo P., Kaeaeriaeinen H., Ahtola H.,
Eskelinen M., Haerkoenen N., Julkunen R., Kangas E., Ojala S.,
Tulikoura J., Valkamo E., Jaervinen H., Mecklin J.-P., Aaltonen L.A.,
de la Chapelle A.;
"Population-based molecular detection of hereditary nonpolyposis
colorectal cancer.";
J. Clin. Oncol. 18:2193-2200(2000).
[76]
ERRATUM.
Salovaara R., Loukola A., Kristo P., Kaeaeriaeinen H., Ahtola H.,
Eskelinen M., Haerkoenen N., Julkunen R., Kangas E., Ojala S.,
Tulikoura J., Valkamo E., Jaervinen H., Mecklin J.-P., Aaltonen L.A.,
de la Chapelle A.;
J. Clin. Oncol. 18:3456-3456(2000).
[77]
VARIANTS GASTRIC CANCER PHE-17; GLU-824; ALA-868; GLY-870 AND GLY-873,
AND VARIANTS HNPCC1 CYS-98; TYR-323; ILE-335; ARG-629 AND VAL-714.
PubMed=12132870;
Kim J.C., Kim H.C., Roh S.A., Koo K.H., Lee D.H., Yu C.S., Lee J.H.,
Kim T.W., Lee H.I., Beck N.E., Bodmer W.F.;
"hMLH1 and hMSH2 mutations in families with familial clustering of
gastric cancer and hereditary non-polyposis colorectal cancer.";
Cancer Detect. Prev. 25:503-510(2001).
[78]
VARIANTS HNPCC1 ASP-161; VAL-216 AND ARG-554.
PubMed=11726306;
Mueller-Koch Y., Kopp R., Lohse P., Baretton G., Stoetzer A., Aust D.,
Daum J., Kerker B., Gross M., Dietmeier W., Holinski-Feder E.;
"Sixteen rare sequence variants of the hMLH1 and hMSH2 genes found in
a cohort of 254 suspected HNPCC (hereditary non-polyposis colorectal
cancer) patients: mutations or polymorphisms?";
Eur. J. Med. Res. 6:473-482(2001).
[79]
CHARACTERIZATION OF VARIANTS ASP-322; LEU-622 AND TYR-639.
PubMed=11555625; DOI=10.1093/hmg/10.18.1889;
Ellison A.R., Lofing J., Bitter G.A.;
"Functional analysis of human MLH1 and MSH2 missense variants and
hybrid human-yeast MLH1 proteins in Saccharomyces cerevisiae.";
Hum. Mol. Genet. 10:1889-1900(2001).
[80]
VARIANT HNPCC1 VAL-813.
PubMed=12373605; DOI=10.1038/sj.bjc.6600565;
Gille J.J.P., Hogervorst F.B.L., Pals G., Wijnen J.T.,
van Schooten R.J., Dommering C.J., Meijer G.A., Craanen M.E.,
Nederlof P.M., de Jong D., McElgunn C.J., Schouten J.P., Menko F.H.;
"Genomic deletions of MSH2 and MLH1 in colorectal cancer families
detected by a novel mutation detection approach.";
Br. J. Cancer 87:892-897(2002).
[81]
VARIANTS HNPCC1 VAL-600 AND PHE-723.
PubMed=11920458; DOI=10.1002/cncr.10332.abs;
Furukawa T., Konishi F., Shitoh K., Kojima M., Nagai H., Tsukamoto T.;
"Evaluation of screening strategy for detecting hereditary
nonpolyposis colorectal carcinoma.";
Cancer 94:911-920(2002).
[82]
VARIANTS HNPCC1 HIS-167; MET-393; PRO-524; ASN-596 DEL; LEU-622;
SER-674 AND ARG-905, AND CHARACTERIZATION OF VARIANTS HNPCC1 HIS-167;
MET-393; PRO-524; ASN-596 DEL; LEU-622; SER-674 AND ARG-905.
PubMed=12124176; DOI=10.1016/S1535-6108(02)00073-9;
Heinen C.D., Wilson T., Mazurek A., Berardini M., Butz C., Fishel R.;
"HNPCC mutations in hMSH2 result in reduced hMSH2-hMSH6 molecular
switch functions.";
Cancer Cell 1:469-478(2002).
[83]
INVOLVEMENT IN MULTIPLE CAFE-AU-LAIT SPOTS WITH LEUKEMIA.
PubMed=11809679;
Whiteside D., McLeod R., Graham G., Steckley J.L., Booth K.,
Somerville M.J., Andrew S.E.;
"A homozygous germ-line mutation in the human MSH2 gene predisposes to
hematological malignancy and multiple cafe-au-lait spots.";
Cancer Res. 62:359-362(2002).
[84]
VARIANT ASP-322.
PubMed=11839723; DOI=10.1136/gut.50.3.405;
Cravo M., Afonso A.J., Lage P., Albuquerque C., Maia L., Lacerda C.,
Fidalgo P., Chaves P., Cruz C., Nobre-Leitao C.;
"Pathogenicity of missense and splice site mutations in hMSH2 and
hMLH1 mismatch repair genes: implications for genetic testing.";
Gut 50:405-412(2002).
[85]
VARIANTS HNPCC1 MET-44; VAL-45; ASN-596 DEL; GLY-886 AND GLU-923.
PubMed=12112654; DOI=10.1002/humu.10083;
Bisgaard M.L., Jaeger A.C., Myrhoej T., Bernstein I., Nielsen F.C.;
"Hereditary non-polyposis colorectal cancer (HNPCC): phenotype-
genotype correlation between patients with and without identified
mutation.";
Hum. Mutat. 20:20-27(2002).
[86]
VARIANTS HNPCC1 ILE-102; ASP-163 AND ALA-564, AND VARIANT ASP-322.
PubMed=12200596; DOI=10.1007/s00432-002-0361-2;
Ward R., Meldrum C., Williams R., Mokany E., Scott R., Turner J.,
Hawkins N., Burgess B., Groombridge C., Spigelman A.;
"Impact of microsatellite testing and mismatch repair protein
expression on the clinical interpretation of genetic testing in
hereditary non-polyposis colorectal cancer.";
J. Cancer Res. Clin. Oncol. 128:403-411(2002).
[87]
VARIANTS HNPCC1 HIS-167 AND SER-359.
PubMed=11870161; DOI=10.1200/JCO.20.5.1203;
Scartozzi M., Bianchi F., Rosati S., Galizia E., Antolini A.,
Loretelli C., Piga A., Bearzi I., Cellerino R., Porfiri E.;
"Mutations of hMLH1 and hMSH2 in patients with suspected hereditary
nonpolyposis colorectal cancer: correlation with microsatellite
instability and abnormalities of mismatch repair protein expression.";
J. Clin. Oncol. 20:1203-1208(2002).
[88]
VARIANTS HNPCC1 LEU-92 DEL AND ALA-853, AND VARIANT ASP-322.
PubMed=12362047; DOI=10.1136/jmg.39.10.e65;
Kurzawski G., Suchy J., Kladny J., Safranow K., Jakubowska A.,
Elsakov P., Kucinskas V., Gardovski J., Irmejs A., Sibul H.,
Huzarski T., Byrski T., Debniak T., Cybulski C., Gronwald J.,
Oszurek O., Clark J., Gozdz S., Niepsuj S., Slomski R., Plawski A.,
Lacka-Wojciechowska A., Rozmiarek A., Fiszer-Maliszewska L.,
Bebenek M., Sorokin D., Stawicka M., Godlewski D., Richter P.,
Brozek I., Wysocka B., Jawien A., Banaszkiewicz Z., Kowalczyk J.,
Czudowska D., Goretzki P.E., Moeslein G., Lubinski J.;
"Germline MSH2 and MLH1 mutational spectrum in HNPCC families from
Poland and the Baltic States.";
J. Med. Genet. 39:E65-E65(2002).
[89]
VARIANTS HNPCC1 PRO-552; SER-583 AND PRO-636.
PubMed=12658575; DOI=10.1086/373963;
Wagner A., Barrows A., Wijnen J.T., van der Klift H., Franken P.F.,
Verkuijlen P., Nakagawa H., Geugien M., Jaghmohan-Changur S.,
Breukel C., Meijers-Heijboer H., Morreau H., van Puijenbroek M.,
Burn J., Coronel S., Kinarski Y., Okimoto R., Watson P., Lynch J.F.,
de la Chapelle A., Lynch H.T., Fodde R.;
"Molecular analysis of hereditary nonpolyposis colorectal cancer in
the United States: high mutation detection rate among clinically
selected families and characterization of an American founder genomic
deletion of the MSH2 gene.";
Am. J. Hum. Genet. 72:1088-1100(2003).
[90]
VARIANTS CRC ILE-13 AND ILE-342, AND VARIANT ASP-322.
PubMed=14504054; DOI=10.1093/annonc/mdg402;
Colombino M., Cossu A., Arba A., Manca A., Curci A., Avallone A.,
Comella G., Botti G., Scintu F., Amoruso M., D'Abbicco D.,
d'Agnessa M.R., Spanu A., Tanda F., Palmieri G.;
"Microsatellite instability and mutation analysis among southern
Italian patients with colorectal carcinoma: detection of different
alterations accounting for MLH1 and MSH2 inactivation in familial
cases.";
Ann. Oncol. 14:1530-1536(2003).
[91]
VARIANT HNPCC1 SER-127.
PubMed=12655564; DOI=10.1002/humu.9123;
Chen-Shtoyerman R., Theodor L., Harmati E., Friedman E., Dacka S.,
Kopelman Y., Sternberg A., Zarivach R., Bar-Meir S., Fireman Z.;
"Genetic analysis of familial colorectal cancer in Israeli Arabs.";
Hum. Mutat. 21:446-447(2003).
[92]
VARIANT HNPCC1 PRO-175.
PubMed=12655568; DOI=10.1002/humu.9127;
Bartosova Z., Fridrichova I., Bujalkova M., Wolf B., Ilencikova D.,
Krizan P., Hlavcak P., Palaj J., Lukac L., Lukacova M., Boeoer A.,
Haider R., Jiricny J., Nystroem-Lahti M., Marra G.;
"Novel MLH1 and MSH2 germline mutations in the first HNPCC families
identified in Slovakia.";
Hum. Mutat. 21:449-449(2003).
[93]
VARIANTS HNPCC1 GLY-163 AND GLY-660.
PubMed=14635101; DOI=10.1002/humu.10291;
Taylor C.F., Charlton R.S., Burn J., Sheridan E., Taylor G.R.;
"Genomic deletions in MSH2 or MLH1 are a frequent cause of hereditary
non-polyposis colorectal cancer: identification of novel and recurrent
deletions by MLPA.";
Hum. Mutat. 22:428-433(2003).
[94]
VARIANTS CRC SER-40; VAL-169; ARG-203; PHE-390; LYS-419; CYS-619 AND
ARG-629, AND VARIANT MET-8.
PubMed=12792735;
Yamada K., Zhong X., Kanazawa S., Koike J., Tsujita K., Hemmi H.;
"Oncogenic pathway of sporadic colorectal cancer with novel germline
missense mutations in the hMSH2 gene.";
Oncol. Rep. 10:859-866(2003).
[95]
VARIANT HNPCC1 THR-931.
PubMed=15046096;
Sun M.H., Cai Q., Fu G., Ren S., Mo S., Xu Y., Ding C., Zhang T.,
Zhu X., Xu X., Min D., Cai S., Luo D., Shi Y., Shi D.;
"Gene symbol: hMSH2. Disease: hereditary nonpolyposis colorectal
cancer.";
Hum. Genet. 114:409-409(2004).
[96]
VARIANT HNPCC1 TYR-671.
PubMed=15300854; DOI=10.1002/humu.9267;
Sharp A., Pichert G., Lucassen A., Eccles D.;
"RNA analysis reveals splicing mutations and loss of expression
defects in MLH1 and BRCA1.";
Hum. Mutat. 24:272-272(2004).
[97]
VARIANTS HNPCC1 LEU-440 DEL; TYR-506; ARG-629 AND ILE-688.
PubMed=15365995; DOI=10.1002/humu.9277;
Shin Y.-K., Heo S.-C., Shin J.-H., Hong S.-H., Ku J.-L., Yoo B.-C.,
Kim I.-J., Park J.-G.;
"Germline mutations in MLH1, MSH2 and MSH6 in Korean hereditary non-
polyposis colorectal cancer families.";
Hum. Mutat. 24:351-351(2004).
[98]
VARIANT HNPCC1 ARG-839, AND VARIANT ARG-629.
PubMed=15613555; DOI=10.1093/jjco/hyh121;
Yuan Y., Huang Y.-Q., Cai S.-R., Song Y.-M., Zheng S., Zhang S.-Z.;
"Genetic characterization of Chinese hereditary non-polyposis
colorectal cancer by DHPLC and multiplex PCR.";
Jpn. J. Clin. Oncol. 34:660-666(2004).
[99]
VARIANTS HNPCC1 LEU-349 AND ASN-596 DEL.
PubMed=15342696; DOI=10.1136/jmg.2004.020651;
Domingo E., Laiho P., Ollikainen M., Pinto M., Wang L., French A.J.,
Westra J., Frebourg T., Espin E., Armengol M., Hamelin R.,
Yamamoto H., Hofstra R.M.W., Seruca R., Lindblom A., Peltomaeki P.,
Thibodeau S.N., Aaltonen L.A., Schwartz S. Jr.;
"BRAF screening as a low-cost effective strategy for simplifying HNPCC
genetic testing.";
J. Med. Genet. 41:664-668(2004).
[100]
VARIANT HNPCC1 PHE-93.
PubMed=15896463; DOI=10.1016/j.canlet.2004.09.051;
Baudi F., Fersini G., Lavecchia A., Terracciano R., Leone F.,
Quaresima B., Faniello M.C., De Paola L., Doldo P., Cuda G.,
Costanzo F., Venuta S.;
"A novel missense germline mutation in exon 2 of the hMSH2 gene in a
HNPCC family from Southern Italy.";
Cancer Lett. 223:285-291(2005).
[101]
VARIANTS HNPCC1 VAL-169; PHE-390; ALA-564 AND ARG-629, AND VARIANT CRC
LYS-419.
PubMed=15996210; DOI=10.1111/j.1399-0004.2005.00469.x;
Lee S.-C., Guo J.-Y., Lim R., Soo R., Koay E., Salto-Tellez M.,
Leong A., Goh B.-C.;
"Clinical and molecular characteristics of hereditary non-polyposis
colorectal cancer families in Southeast Asia.";
Clin. Genet. 68:137-145(2005).
[102]
VARIANT HNPCC1 TYR-283.
PubMed=15870828; DOI=10.1038/sj.ejhg.5201421;
Wehner M., Mangold E., Sengteller M., Friedrichs N., Aretz S.,
Friedl W., Propping P., Pagenstecher C.;
"Hereditary nonpolyposis colorectal cancer: pitfalls in deletion
screening in MSH2 and MLH1 genes.";
Eur. J. Hum. Genet. 13:983-986(2005).
[103]
VARIANT HNPCC1 ARG-162.
PubMed=15991316;
Kohonen-Corish M.R.J., Otway R., Tetlow N., Hornby J., Doe W.F.;
"Gene symbol: MSH2. Disease: hereditary nonpolyposis colorectal
cancer.";
Hum. Genet. 116:539-539(2005).
[104]
VARIANTS HNPCC1 THR-2; LEU-92 DEL; MET-145; PHE-390 AND ALA-853, AND
VARIANT ASP-322.
PubMed=16451135; DOI=10.1111/j.1399-0004.2006.00550.x;
Kurzawski G., Suchy J., Lener M., Klujszo-Grabowska E., Kladny J.,
Safranow K., Jakubowska K., Jakubowska A., Huzarski T., Byrski T.,
Debniak T., Cybulski C., Gronwald J., Oszurek O., Oszutowska D.,
Kowalska E., Gozdz S., Niepsuj S., Slomski R., Plawski A.,
Lacka-Wojciechowska A., Rozmiarek A., Fiszer-Maliszewska L.,
Bebenek M., Sorokin D., Sasiadek M.M., Stembalska A., Grzebieniak Z.,
Kilar E., Stawicka M., Godlewski D., Richter P., Brozek I.,
Wysocka B., Limon J., Jawien A., Banaszkiewicz Z., Janiszewska H.,
Kowalczyk J., Czudowska D., Scott R.J., Lubinski J.;
"Germline MSH2 and MLH1 mutational spectrum including large
rearrangements in HNPCC families from Poland (update study).";
Clin. Genet. 69:40-47(2006).
[105]
VARIANTS HNPCC1 PRO-33; ASP-161; ARG-162; ARG-164; PRO-173; PRO-187;
TYR-333; ASN-603; PRO-636; PHE-697; 745-ILE-ILE-746 DEL AND LYS-749,
VARIANTS VAL-272; THR-834 AND GLU-923, CHARACTERIZATION OF VARIANTS
HNPCC1 PRO-33; ASP-161; ARG-162; ARG-164; PRO-173; PRO-187; TYR-333;
ASN-603; PRO-636; PHE-697; 745-ILE-ILE-746 DEL AND LYS-749, AND
CHARACTERIZATION OF VARIANTS VAL-272; THR-834 AND GLU-923.
PubMed=17101317; DOI=10.1053/j.gastro.2006.08.044;
Ollila S., Sarantaus L., Kariola R., Chan P., Hampel H.,
Holinski-Feder E., Macrae F., Kohonen-Corish M., Gerdes A.-M.,
Peltomaeki P., Mangold E., de la Chapelle A., Greenblatt M.,
Nystroem M.;
"Pathogenicity of MSH2 missense mutations is typically associated with
impaired repair capability of the mutated protein.";
Gastroenterology 131:1408-1417(2006).
[106]
VARIANT HNPCC1 ALA-162.
PubMed=17128465;
Leonardis D.;
"Gene symbol: msh2. Disease: hereditary nonpolyposis colorectal
cancer.";
Hum. Genet. 119:675-675(2006).
[107]
VARIANT HNPCC1 ARG-674.
PubMed=18625694; DOI=10.1136/gut.2008.156695;
Ramsoekh D., Wagner A., van Leerdam M.E., Dinjens W.N.,
Steyerberg E.W., Halley D.J., Kuipers E.J., Dooijes D.;
"A high incidence of MSH6 mutations in Amsterdam criteria II-negative
families tested in a diagnostic setting.";
Gut 57:1539-1544(2008).
[108]
VARIANTS GLN-46; LYS-106; ASP-322; SER-596; LEU-670; ILE-779; SER-807;
HIS-835 AND ARG-911.
PubMed=18033691; DOI=10.1002/humu.20635;
Barnetson R.A., Cartwright N., van Vliet A., Haq N., Drew K.,
Farrington S., Williams N., Warner J., Campbell H., Porteous M.E.,
Dunlop M.G.;
"Classification of ambiguous mutations in DNA mismatch repair genes
identified in a population-based study of colorectal cancer.";
Hum. Mutat. 29:367-374(2008).
[109]
CHARACTERIZATION OF VARIANTS HNPCC1 PRO-33; SER-127; ASP-161; ARG-162;
ARG-164; PRO-173; PRO-187; VAL-272; TYR-333; ASN-603; PRO-636;
ALA-674; PHE-697; 745-ILE-ILE-746 DEL; LYS-749; THR-834 AND GLU-923,
AND CHARACTERIZATION OF VARIANT ASP-322.
PubMed=18951462; DOI=10.1002/humu.20893;
Ollila S., Dermadi Bebek D., Jiricny J., Nystroem M.;
"Mechanisms of pathogenicity in human MSH2 missense mutants.";
Hum. Mutat. 29:1355-1363(2008).
[110]
VARIANTS HNPCC1 LEU-92 DEL; ARG-199; ASP-331; GLU-470; ASN-610;
GLY-638; GLU-645; LEU-696; TYR-748 AND GLN-839, VARIANTS VAL-272;
ASN-596 DEL; TYR-671; ARG-697 AND PHE-723, CHARACTERIZATION OF
VARIANTS HNPCC1 LEU-92 DEL; ARG-199; ASP-331; GLU-470; ASN-610;
GLY-638; GLU-645; LEU-696; TYR-748 AND GLN-839, AND CHARACTERIZATION
OF VARIANTS VAL-272; ASN-596 DEL; TYR-671; ARG-697 AND PHE-723.
PubMed=18561205; DOI=10.1002/humu.20796;
Tournier I., Vezain M., Martins A., Charbonnier F.,
Baert-Desurmont S., Olschwang S., Wang Q., Buisine M.P., Soret J.,
Tazi J., Frebourg T., Tosi M.;
"A large fraction of unclassified variants of the mismatch repair
genes MLH1 and MSH2 is associated with splicing defects.";
Hum. Mutat. 29:1412-1424(2008).
[111]
CHARACTERIZATION OF VARIANTS HNPCC1 ARG-162; HIS-167 AND SER-359.
PubMed=18781619; DOI=10.1002/humu.20875;
Belvederesi L., Bianchi F., Galizia E., Loretelli C., Bracci R.,
Catalani R., Amati M., Cellerino R.;
"MSH2 missense mutations and HNPCC syndrome: pathogenicity assessment
in a human expression system.";
Hum. Mutat. 29:E296-E309(2008).
[112]
CHARACTERIZATION OF VARIANTS HNPCC1 HIS-167; THR-305: LEU-622;
ARG-639; ARG-674; PHE-697 AND THR-834.
PubMed=18822302; DOI=10.1016/j.mrfmmm.2008.08.015;
Lutzen A., de Wind N., Georgijevic D., Nielsen F.C., Rasmussen L.J.;
"Functional analysis of HNPCC-related missense mutations in MSH2.";
Mutat. Res. 645:44-55(2008).
[113]
CHARACTERIZATION OF VARIANTS HNPCC1 MET-44; VAL-45; HIS-167; THR-305;
PHE-390; ASN-596 DEL; ARG-639; ARG-674; PHE-697; PHE-723 AND GLY-886,
AND CHARACTERIZATION OF VARIANTS ASP-165; HIS-177; VAL-272; LEU-385;
LEU-519; ALA-675; GLU-759; VAL-805; GLY-843 AND LEU-860.
PubMed=22102614; DOI=10.1002/humu.22000;
Drost M., Zonneveld J.B., van Hees S., Rasmussen L.J., Hofstra R.M.,
de Wind N.;
"A rapid and cell-free assay to test the activity of lynch syndrome-
associated MSH2 and MSH6 missense variants.";
Hum. Mutat. 33:488-494(2012).
[114]
CHARACTERIZATION OF VARIANTS SER-127; MET-145; GLN-205; ASP-322;
PRO-328; ILE-367; GLU-487 AND ILE-909.
PubMed=22581703; DOI=10.1002/humu.22119;
Kantelinen J., Kansikas M., Candelin S., Hampel H., Smith B., Holm L.,
Kariola R., Nystrom M.;
"Mismatch repair analysis of inherited MSH2 and/or MSH6 variation
pairs found in cancer patients.";
Hum. Mutat. 33:1294-1301(2012).
[115]
VARIANT HNPCC1 ARG-669.
PubMed=22371642; DOI=10.3748/wjg.v18.i8.814;
Zahary M.N., Kaur G., Abu Hassan M.R., Singh H., Naik V.R.,
Ankathil R.;
"Germline mutation analysis of MLH1 and MSH2 in Malaysian Lynch
syndrome patients.";
World J. Gastroenterol. 18:814-820(2012).
-!- FUNCTION: Component of the post-replicative DNA mismatch repair
system (MMR). Forms two different heterodimers: MutS alpha (MSH2-
MSH6 heterodimer) and MutS beta (MSH2-MSH3 heterodimer) which
binds to DNA mismatches thereby initiating DNA repair. When bound,
heterodimers bend the DNA helix and shields approximately 20 base
pairs. MutS alpha recognizes single base mismatches and
dinucleotide insertion-deletion loops (IDL) in the DNA. MutS beta
recognizes larger insertion-deletion loops up to 13 nucleotides
long. After mismatch binding, MutS alpha or beta forms a ternary
complex with the MutL alpha heterodimer, which is thought to be
responsible for directing the downstream MMR events, including
strand discrimination, excision, and resynthesis. ATP binding and
hydrolysis play a pivotal role in mismatch repair functions. The
ATPase activity associated with MutS alpha regulates binding
similar to a molecular switch: mismatched DNA provokes ADP-->ATP
exchange, resulting in a discernible conformational transition
that converts MutS alpha into a sliding clamp capable of
hydrolysis-independent diffusion along the DNA backbone. This
transition is crucial for mismatch repair. MutS alpha may also
play a role in DNA homologous recombination repair. In melanocytes
may modulate both UV-B-induced cell cycle regulation and
apoptosis. {ECO:0000269|PubMed:10078208,
ECO:0000269|PubMed:10660545, ECO:0000269|PubMed:15064730,
ECO:0000269|PubMed:17611581, ECO:0000269|PubMed:21120944,
ECO:0000269|PubMed:9564049, ECO:0000269|PubMed:9822679,
ECO:0000269|PubMed:9822680}.
-!- SUBUNIT: Heterodimer consisting of MSH2-MSH6 (MutS alpha) or MSH2-
MSH3 (MutS beta). Both heterodimer form a ternary complex with
MutL alpha (MLH1-PMS1). Interacts with EXO1. Part of the BRCA1-
associated genome surveillance complex (BASC), which contains
BRCA1, MSH2, MSH6, MLH1, ATM, BLM, PMS2 and the RAD50-MRE11-NBS1
protein complex. This association could be a dynamic process
changing throughout the cell cycle and within subnuclear domains.
Interacts with ATR. Interacts with SLX4/BTBD12; this interaction
is direct and links MutS beta to SLX4, a subunit of different
structure-specific endonucleases. Interacts with SMARCAD1.
{ECO:0000269|PubMed:10856833, ECO:0000269|PubMed:11427529,
ECO:0000269|PubMed:11429708, ECO:0000269|PubMed:12414623,
ECO:0000269|PubMed:14657349, ECO:0000269|PubMed:14676842,
ECO:0000269|PubMed:18675275, ECO:0000269|PubMed:19596235,
ECO:0000269|PubMed:8942985, ECO:0000269|PubMed:9788596}.
-!- INTERACTION:
O00716:E2F3; NbExp=2; IntAct=EBI-355888, EBI-765551;
P39875:EXO1 (xeno); NbExp=2; IntAct=EBI-355888, EBI-6738;
Q9UQ84-1:EXO1; NbExp=3; IntAct=EBI-355888, EBI-944694;
P09429:HMGB1; NbExp=2; IntAct=EBI-355888, EBI-389432;
P20585:MSH3; NbExp=4; IntAct=EBI-355888, EBI-1164205;
P52701:MSH6; NbExp=6; IntAct=EBI-355888, EBI-395529;
Q8IY92:SLX4; NbExp=5; IntAct=EBI-355888, EBI-2370740;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P43246-1; Sequence=Displayed;
Name=2;
IsoId=P43246-2; Sequence=VSP_045536;
-!- TISSUE SPECIFICITY: Ubiquitously expressed.
{ECO:0000269|PubMed:10856833}.
-!- PTM: Phosphorylated by PRKCZ, which may prevent MutS alpha
degradation by the ubiquitin-proteasome pathway.
{ECO:0000269|PubMed:15808853}.
-!- DISEASE: Hereditary non-polyposis colorectal cancer 1 (HNPCC1)
[MIM:120435]: An autosomal dominant disease associated with marked
increase in cancer susceptibility. It is characterized by a
familial predisposition to early-onset colorectal carcinoma (CRC)
and extra-colonic tumors of the gastrointestinal, urological and
female reproductive tracts. HNPCC is reported to be the most
common form of inherited colorectal cancer in the Western world.
Clinically, HNPCC is often divided into two subgroups. Type I is
characterized by hereditary predisposition to colorectal cancer, a
young age of onset, and carcinoma observed in the proximal colon.
Type II is characterized by increased risk for cancers in certain
tissues such as the uterus, ovary, breast, stomach, small
intestine, skin, and larynx in addition to the colon. Diagnosis of
classical HNPCC is based on the Amsterdam criteria: 3 or more
relatives affected by colorectal cancer, one a first degree
relative of the other two; 2 or more generation affected; 1 or
more colorectal cancers presenting before 50 years of age;
exclusion of hereditary polyposis syndromes. The term 'suspected
HNPCC' or 'incomplete HNPCC' can be used to describe families who
do not or only partially fulfill the Amsterdam criteria, but in
whom a genetic basis for colon cancer is strongly suspected.
{ECO:0000269|PubMed:10375096, ECO:0000269|PubMed:10386556,
ECO:0000269|PubMed:10528862, ECO:0000269|PubMed:10573010,
ECO:0000269|PubMed:10612836, ECO:0000269|PubMed:10777691,
ECO:0000269|PubMed:10829038, ECO:0000269|PubMed:11726306,
ECO:0000269|PubMed:11870161, ECO:0000269|PubMed:11920458,
ECO:0000269|PubMed:12112654, ECO:0000269|PubMed:12124176,
ECO:0000269|PubMed:12132870, ECO:0000269|PubMed:12200596,
ECO:0000269|PubMed:12362047, ECO:0000269|PubMed:12373605,
ECO:0000269|PubMed:12655564, ECO:0000269|PubMed:12655568,
ECO:0000269|PubMed:12658575, ECO:0000269|PubMed:14635101,
ECO:0000269|PubMed:15046096, ECO:0000269|PubMed:15300854,
ECO:0000269|PubMed:15342696, ECO:0000269|PubMed:15365995,
ECO:0000269|PubMed:15613555, ECO:0000269|PubMed:15870828,
ECO:0000269|PubMed:15896463, ECO:0000269|PubMed:15991316,
ECO:0000269|PubMed:15996210, ECO:0000269|PubMed:16451135,
ECO:0000269|PubMed:17101317, ECO:0000269|PubMed:17128465,
ECO:0000269|PubMed:18561205, ECO:0000269|PubMed:18625694,
ECO:0000269|PubMed:18781619, ECO:0000269|PubMed:18822302,
ECO:0000269|PubMed:18951462, ECO:0000269|PubMed:21120944,
ECO:0000269|PubMed:22102614, ECO:0000269|PubMed:22371642,
ECO:0000269|PubMed:7874129, ECO:0000269|PubMed:8261515,
ECO:0000269|PubMed:8700523, ECO:0000269|PubMed:8797773,
ECO:0000269|PubMed:8872463, ECO:0000269|PubMed:9048925,
ECO:0000269|PubMed:9240418, ECO:0000269|PubMed:9298827,
ECO:0000269|PubMed:9311737, ECO:0000269|PubMed:9419403,
ECO:0000269|PubMed:9559627, ECO:0000269|PubMed:9621522,
ECO:0000269|PubMed:9718327, ECO:0000269|PubMed:9889267}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- DISEASE: Muir-Torre syndrome (MRTES) [MIM:158320]: Rare autosomal
dominant disorder characterized by sebaceous neoplasms and
visceral malignancy. {ECO:0000269|PubMed:7713503}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- DISEASE: Endometrial cancer (ENDMC) [MIM:608089]: A malignancy of
endometrium, the mucous lining of the uterus. Most endometrial
cancers are adenocarcinomas, cancers that begin in cells that make
and release mucus and other fluids. {ECO:0000305|PubMed:11306449,
ECO:0000305|PubMed:21642682}. Note=Disease susceptibility is
associated with variations affecting the gene represented in this
entry.
-!- DISEASE: Mismatch repair cancer syndrome (MMRCS) [MIM:276300]: An
autosomal recessive, rare, childhood cancer predisposition
syndrome encompassing a broad tumor spectrum. This includes
hematological malignancies, central nervous system tumors, Lynch
syndrome-associated malignancies such as colorectal tumors as well
as multiple intestinal polyps, embryonic tumors and
rhabdomyosarcoma. Multiple cafe-au-lait macules, a feature
reminiscent of neurofibromatosis type 1, are often found as first
manifestation of the underlying cancer. Areas of skin
hypopigmentation have also been reported in MMRCS patients.
{ECO:0000269|PubMed:12549480, ECO:0000269|PubMed:16372347}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: Colorectal cancer (CRC) [MIM:114500]: A complex disease
characterized by malignant lesions arising from the inner wall of
the large intestine (the colon) and the rectum. Genetic
alterations are often associated with progression from
premalignant lesion (adenoma) to invasive adenocarcinoma. Risk
factors for cancer of the colon and rectum include colon polyps,
long-standing ulcerative colitis, and genetic family history.
{ECO:0000269|PubMed:12792735, ECO:0000269|PubMed:14504054,
ECO:0000269|PubMed:15996210, ECO:0000269|PubMed:9559627}.
Note=Disease susceptibility may be associated with variations
affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the DNA mismatch repair MutS family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAC27930.1; Type=Frameshift; Positions=417; Note=The frameshift is caused by a single nucleotide deletion which is found in a HNPCC kindred.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/MSH2ID340ch2p22.html";
-!- WEB RESOURCE: Name=Hereditary non-polyposis colorectal cancer db;
URL="http://www.nfdht.nl/";
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/msh2/";
-----------------------------------------------------------------------
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EMBL; U03911; AAA18643.1; -; mRNA.
EMBL; U04045; AAA61870.1; -; mRNA.
EMBL; U41221; AAA82080.1; ALT_SEQ; Genomic_DNA.
EMBL; U41206; AAA82080.1; JOINED; Genomic_DNA.
EMBL; U41207; AAA82080.1; JOINED; Genomic_DNA.
EMBL; U41208; AAA82080.1; JOINED; Genomic_DNA.
EMBL; U41210; AAA82080.1; JOINED; Genomic_DNA.
EMBL; U41211; AAA82080.1; JOINED; Genomic_DNA.
EMBL; U41212; AAA82080.1; JOINED; Genomic_DNA.
EMBL; U41213; AAA82080.1; JOINED; Genomic_DNA.
EMBL; U41214; AAA82080.1; JOINED; Genomic_DNA.
EMBL; U41215; AAA82080.1; JOINED; Genomic_DNA.
EMBL; U41216; AAA82080.1; JOINED; Genomic_DNA.
EMBL; U41217; AAA82080.1; JOINED; Genomic_DNA.
EMBL; U41218; AAA82080.1; JOINED; Genomic_DNA.
EMBL; U41219; AAA82080.1; JOINED; Genomic_DNA.
EMBL; U41220; AAA82080.1; JOINED; Genomic_DNA.
EMBL; L47583; AAB59564.1; -; mRNA.
EMBL; L47582; AAB59565.1; -; mRNA.
EMBL; L47581; AAA76858.1; -; mRNA.
EMBL; AY601851; AAS99351.1; -; Genomic_DNA.
EMBL; AK304496; BAG65304.1; -; mRNA.
EMBL; BX649122; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; AC079775; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC138655; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC021566; AAH21566.1; -; mRNA.
EMBL; AF066081; AAC27930.1; ALT_FRAME; Genomic_DNA.
CCDS; CCDS1834.1; -. [P43246-1]
CCDS; CCDS58709.1; -. [P43246-2]
PIR; I64819; I64819.
RefSeq; NP_000242.1; NM_000251.2. [P43246-1]
RefSeq; NP_001245210.1; NM_001258281.1. [P43246-2]
UniGene; Hs.597656; -.
PDB; 2O8B; X-ray; 2.75 A; A=1-934.
PDB; 2O8C; X-ray; 3.37 A; A=1-934.
PDB; 2O8D; X-ray; 3.00 A; A=1-934.
PDB; 2O8E; X-ray; 3.30 A; A=1-934.
PDB; 2O8F; X-ray; 3.25 A; A=1-934.
PDB; 3THW; X-ray; 3.09 A; A=1-934.
PDB; 3THX; X-ray; 2.70 A; A=1-934.
PDB; 3THY; X-ray; 2.89 A; A=1-934.
PDB; 3THZ; X-ray; 4.30 A; A=1-934.
PDBsum; 2O8B; -.
PDBsum; 2O8C; -.
PDBsum; 2O8D; -.
PDBsum; 2O8E; -.
PDBsum; 2O8F; -.
PDBsum; 3THW; -.
PDBsum; 3THX; -.
PDBsum; 3THY; -.
PDBsum; 3THZ; -.
ProteinModelPortal; P43246; -.
SMR; P43246; -.
BioGrid; 110573; 124.
DIP; DIP-35054N; -.
IntAct; P43246; 48.
MINT; MINT-84789; -.
STRING; 9606.ENSP00000233146; -.
iPTMnet; P43246; -.
PhosphoSitePlus; P43246; -.
BioMuta; MSH2; -.
DMDM; 1171032; -.
EPD; P43246; -.
MaxQB; P43246; -.
PaxDb; P43246; -.
PeptideAtlas; P43246; -.
PRIDE; P43246; -.
DNASU; 4436; -.
Ensembl; ENST00000233146; ENSP00000233146; ENSG00000095002. [P43246-1]
Ensembl; ENST00000543555; ENSP00000442697; ENSG00000095002. [P43246-2]
GeneID; 4436; -.
KEGG; hsa:4436; -.
UCSC; uc002rvy.3; human. [P43246-1]
CTD; 4436; -.
DisGeNET; 4436; -.
GeneCards; MSH2; -.
GeneReviews; MSH2; -.
HGNC; HGNC:7325; MSH2.
HPA; CAB009572; -.
HPA; CAB070867; -.
MalaCards; MSH2; -.
MIM; 114500; phenotype.
MIM; 120435; phenotype.
MIM; 158320; phenotype.
MIM; 276300; phenotype.
MIM; 608089; phenotype.
MIM; 609309; gene.
neXtProt; NX_P43246; -.
OpenTargets; ENSG00000095002; -.
Orphanet; 252202; Constitutional mismatch repair deficiency syndrome.
Orphanet; 144; Hereditary nonpolyposis colon cancer.
Orphanet; 587; Muir-Torre syndrome.
Orphanet; 99817; Non-polyposis Turcot syndrome.
PharmGKB; PA31133; -.
eggNOG; KOG0219; Eukaryota.
eggNOG; COG0249; LUCA.
GeneTree; ENSGT00550000074867; -.
HOGENOM; HOG000196498; -.
HOVERGEN; HBG006399; -.
InParanoid; P43246; -.
KO; K08735; -.
OMA; GDFYTAH; -.
OrthoDB; EOG091G03SA; -.
PhylomeDB; P43246; -.
TreeFam; TF351780; -.
Reactome; R-HSA-5358565; Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha).
Reactome; R-HSA-5358606; Mismatch repair (MMR) directed by MSH2:MSH3 (MutSbeta).
Reactome; R-HSA-5632927; Defective Mismatch Repair Associated With MSH3.
Reactome; R-HSA-5632928; Defective Mismatch Repair Associated With MSH2.
Reactome; R-HSA-5632968; Defective Mismatch Repair Associated With MSH6.
Reactome; R-HSA-6796648; TP53 Regulates Transcription of DNA Repair Genes.
SIGNOR; P43246; -.
ChiTaRS; MSH2; human.
EvolutionaryTrace; P43246; -.
GeneWiki; MSH2; -.
GenomeRNAi; 4436; -.
PRO; PR:P43246; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000095002; -.
CleanEx; HS_MSH2; -.
ExpressionAtlas; P43246; baseline and differential.
Genevisible; P43246; HS.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0032301; C:MutSalpha complex; IDA:UniProtKB.
GO; GO:0032302; C:MutSbeta complex; IDA:HGNC.
GO; GO:0000784; C:nuclear chromosome, telomeric region; IDA:BHF-UCL.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0019237; F:centromeric DNA binding; IEA:Ensembl.
GO; GO:0003684; F:damaged DNA binding; IEA:Ensembl.
GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
GO; GO:0008094; F:DNA-dependent ATPase activity; IBA:GO_Central.
GO; GO:0000406; F:double-strand/single-strand DNA junction binding; IBA:GO_Central.
GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
GO; GO:0032137; F:guanine/thymine mispair binding; IMP:MGI.
GO; GO:0000404; F:heteroduplex DNA loop binding; IBA:GO_Central.
GO; GO:0008022; F:protein C-terminus binding; IPI:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IDA:HGNC.
GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
GO; GO:0000403; F:Y-form DNA binding; IBA:GO_Central.
GO; GO:0030183; P:B cell differentiation; ISS:BHF-UCL.
GO; GO:0019724; P:B cell mediated immunity; ISS:BHF-UCL.
GO; GO:0007050; P:cell cycle arrest; IEA:Ensembl.
GO; GO:0008340; P:determination of adult lifespan; IEA:Ensembl.
GO; GO:0006281; P:DNA repair; IDA:BHF-UCL.
GO; GO:0006302; P:double-strand break repair; IBA:GO_Central.
GO; GO:0007281; P:germ cell development; IEA:Ensembl.
GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
GO; GO:0031573; P:intra-S DNA damage checkpoint; IBA:GO_Central.
GO; GO:0042771; P:intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator; IBA:GO_Central.
GO; GO:0045190; P:isotype switching; ISS:BHF-UCL.
GO; GO:0043570; P:maintenance of DNA repeat elements; IMP:HGNC.
GO; GO:0008584; P:male gonad development; ISS:BHF-UCL.
GO; GO:0006311; P:meiotic gene conversion; IBA:GO_Central.
GO; GO:0006298; P:mismatch repair; IDA:UniProtKB.
GO; GO:0045910; P:negative regulation of DNA recombination; IDA:BHF-UCL.
GO; GO:0043524; P:negative regulation of neuron apoptotic process; ISS:BHF-UCL.
GO; GO:0045128; P:negative regulation of reciprocal meiotic recombination; IBA:GO_Central.
GO; GO:0006119; P:oxidative phosphorylation; IEA:Ensembl.
GO; GO:0051096; P:positive regulation of helicase activity; IDA:BHF-UCL.
GO; GO:0048298; P:positive regulation of isotype switching to IgA isotypes; IEA:Ensembl.
GO; GO:0048304; P:positive regulation of isotype switching to IgG isotypes; IEA:Ensembl.
GO; GO:0006301; P:postreplication repair; IDA:UniProtKB.
GO; GO:0010224; P:response to UV-B; ISS:BHF-UCL.
GO; GO:0010165; P:response to X-ray; ISS:BHF-UCL.
GO; GO:0016446; P:somatic hypermutation of immunoglobulin genes; IBA:GO_Central.
GO; GO:0016447; P:somatic recombination of immunoglobulin gene segments; ISS:BHF-UCL.
Gene3D; 3.30.420.110; -; 1.
Gene3D; 3.40.1170.10; -; 1.
InterPro; IPR011184; DNA_mismatch_repair_Msh2.
InterPro; IPR007695; DNA_mismatch_repair_MutS-lik_N.
InterPro; IPR000432; DNA_mismatch_repair_MutS_C.
InterPro; IPR007861; DNA_mismatch_repair_MutS_clamp.
InterPro; IPR007696; DNA_mismatch_repair_MutS_core.
InterPro; IPR016151; DNA_mismatch_repair_MutS_N.
InterPro; IPR007860; DNA_mmatch_repair_MutS_con_dom.
InterPro; IPR032642; Msh2.
InterPro; IPR027417; P-loop_NTPase.
PANTHER; PTHR11361:SF118; PTHR11361:SF118; 1.
Pfam; PF01624; MutS_I; 1.
Pfam; PF05188; MutS_II; 1.
Pfam; PF05192; MutS_III; 1.
Pfam; PF05190; MutS_IV; 1.
Pfam; PF00488; MutS_V; 1.
PIRSF; PIRSF005813; MSH2; 1.
SMART; SM00534; MUTSac; 1.
SMART; SM00533; MUTSd; 1.
SUPFAM; SSF48334; SSF48334; 1.
SUPFAM; SSF52540; SSF52540; 1.
PROSITE; PS00486; DNA_MISMATCH_REPAIR_2; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; ATP-binding;
Complete proteome; Disease mutation; DNA damage; DNA repair;
DNA-binding; Hereditary nonpolyposis colorectal cancer;
Isopeptide bond; Nucleotide-binding; Nucleus; Phosphoprotein;
Polymorphism; Reference proteome; Tumor suppressor; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:22814378}.
CHAIN 2 934 DNA mismatch repair protein Msh2.
/FTId=PRO_0000115183.
NP_BIND 669 676 ATP. {ECO:0000255}.
REGION 601 671 Interaction with EXO1.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:22814378}.
MOD_RES 555 555 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 567 567 N6-acetyllysine.
{ECO:0000250|UniProtKB:P43247}.
MOD_RES 921 921 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
CROSSLNK 430 430 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VAR_SEQ 1 66 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:17974005}.
/FTId=VSP_045536.
VARIANT 2 2 A -> T (in HNPCC1; dbSNP:rs63750466).
{ECO:0000269|PubMed:16451135}.
/FTId=VAR_054511.
VARIANT 8 8 T -> M (in dbSNP:rs17217716).
{ECO:0000269|PubMed:10777691,
ECO:0000269|PubMed:12792735,
ECO:0000269|Ref.9}.
/FTId=VAR_013171.
VARIANT 13 13 S -> I (in CRC; unknown pathological
significance; dbSNP:rs63749907).
{ECO:0000269|PubMed:14504054}.
/FTId=VAR_043736.
VARIANT 17 17 V -> F (in gastric cancer; unknown
pathological significance; cryptic
acceptor splice site suppressed on ex
vivo splicing assay; dbSNP:rs63750966).
{ECO:0000269|PubMed:12132870}.
/FTId=VAR_043737.
VARIANT 33 33 T -> P (in HNPCC1; decreased mismatch
repair activity; dbSNP:rs63751107).
{ECO:0000269|PubMed:17101317,
ECO:0000269|PubMed:18951462,
ECO:0000269|PubMed:21120944}.
/FTId=VAR_043738.
VARIANT 40 40 G -> S (in CRC; unknown pathological
significance; dbSNP:rs63751260).
{ECO:0000269|PubMed:12792735}.
/FTId=VAR_043739.
VARIANT 43 43 Y -> C (in dbSNP:rs17217723).
{ECO:0000269|Ref.9}.
/FTId=VAR_019233.
VARIANT 44 44 T -> M (in HNPCC1; unknown pathological
significance; no decrease in mismatch
repair activity; dbSNP:rs587779085).
{ECO:0000269|PubMed:12112654,
ECO:0000269|PubMed:21120944,
ECO:0000269|PubMed:22102614}.
/FTId=VAR_043740.
VARIANT 45 45 A -> V (in HNPCC1; unknown pathological
significance; no decrease in mismatch
repair activity; dbSNP:rs63750285).
{ECO:0000269|PubMed:12112654,
ECO:0000269|PubMed:21120944,
ECO:0000269|PubMed:22102614}.
/FTId=VAR_043741.
VARIANT 46 46 H -> Q (in HNPCC1; dbSNP:rs33946261).
{ECO:0000269|PubMed:18033691,
ECO:0000269|PubMed:8700523}.
/FTId=VAR_004470.
VARIANT 92 92 Missing (in HNPCC1; unknown pathological
significance).
{ECO:0000269|PubMed:12362047,
ECO:0000269|PubMed:16451135,
ECO:0000269|PubMed:18561205}.
/FTId=VAR_043742.
VARIANT 93 93 L -> F (in HNPCC1; dbSNP:rs63751429).
{ECO:0000269|PubMed:15896463}.
/FTId=VAR_043743.
VARIANT 96 96 R -> H (in dbSNP:rs63750002).
{ECO:0000269|PubMed:7726159}.
/FTId=VAR_004471.
VARIANT 98 98 Y -> C (in HNPCC1; unknown pathological
significance; dbSNP:rs63750887).
{ECO:0000269|PubMed:12132870}.
/FTId=VAR_043744.
VARIANT 102 102 V -> I (in HNPCC1; dbSNP:rs193922373).
{ECO:0000269|PubMed:12200596}.
/FTId=VAR_043745.
VARIANT 106 106 R -> K (in dbSNP:rs41295286).
{ECO:0000269|PubMed:18033691}.
/FTId=VAR_038026.
VARIANT 110 110 K -> T (in HNPCC1; somatic mutation).
{ECO:0000269|PubMed:9419403}.
/FTId=VAR_043746.
VARIANT 127 127 N -> S (in HNPCC1; presumed to enhance
cancer risk considerably when associated
with P-328; shows significantly decreased
repair efficiency when associated with
variant P-328; dbSNP:rs17217772).
{ECO:0000269|PubMed:12655564,
ECO:0000269|PubMed:18951462,
ECO:0000269|PubMed:21120944,
ECO:0000269|PubMed:22581703,
ECO:0000269|Ref.9}.
/FTId=VAR_019234.
VARIANT 139 139 N -> S (in HNPCC1).
/FTId=VAR_004472.
VARIANT 145 145 I -> M (in HNPCC1; unknown pathological
significance; normal mismatch repair
activity; dbSNP:rs63750124).
{ECO:0000269|PubMed:16451135,
ECO:0000269|PubMed:21120944,
ECO:0000269|PubMed:22581703}.
/FTId=VAR_004473.
VARIANT 161 161 V -> D (in HNPCC1; decreased mismatch
repair activity; affects protein
stability; loss of protein expression;
dbSNP:rs63750126).
{ECO:0000269|PubMed:11726306,
ECO:0000269|PubMed:17101317,
ECO:0000269|PubMed:18951462,
ECO:0000269|PubMed:21120944}.
/FTId=VAR_012936.
VARIANT 162 162 G -> A (in HNPCC1; dbSNP:rs63750773).
{ECO:0000269|PubMed:17128465}.
/FTId=VAR_054512.
VARIANT 162 162 G -> R (in HNPCC1; decreased mismatch
repair activity; associated with an
abnormal subcellular localization
pattern; affects protein stability; loss
of protein expression; dbSNP:rs63750624).
{ECO:0000269|PubMed:15991316,
ECO:0000269|PubMed:17101317,
ECO:0000269|PubMed:18781619,
ECO:0000269|PubMed:18951462,
ECO:0000269|PubMed:21120944}.
/FTId=VAR_043747.
VARIANT 163 163 V -> D (in HNPCC1; dbSNP:rs63750214).
{ECO:0000269|PubMed:12200596}.
/FTId=VAR_043748.
VARIANT 163 163 V -> G (in HNPCC1; dbSNP:rs63750214).
{ECO:0000269|PubMed:14635101}.
/FTId=VAR_022670.
VARIANT 164 164 G -> R (in HNPCC1; decreased mismatch
repair activity; affects protein
stability; loss of protein expression;
dbSNP:rs63750582).
{ECO:0000269|PubMed:17101317,
ECO:0000269|PubMed:18951462,
ECO:0000269|PubMed:21120944}.
/FTId=VAR_043749.
VARIANT 165 165 Y -> D (in HNPCC1; unknown pathological
significance; decreased mismatch repair
activity; dbSNP:rs587779163).
{ECO:0000269|PubMed:22102614}.
/FTId=VAR_067284.
VARIANT 167 167 D -> H (in HNPCC1; shows reduced mismatch
binding; does not show a decreased
expression level of the MutS alpha
complex; not associated with an abnormal
subcellular localization pattern; normal
mismatch repair activity;
dbSNP:rs63750255).
{ECO:0000269|PubMed:11870161,
ECO:0000269|PubMed:12124176,
ECO:0000269|PubMed:18781619,
ECO:0000269|PubMed:18822302,
ECO:0000269|PubMed:22102614,
ECO:0000269|PubMed:8872463}.
/FTId=VAR_004474.
VARIANT 169 169 I -> V (in HNPCC1 and CRC; unknown
pathological significance;
dbSNP:rs63750716).
{ECO:0000269|PubMed:12792735,
ECO:0000269|PubMed:15996210}.
/FTId=VAR_043750.
VARIANT 173 173 L -> P (in HNPCC1; decreased mismatch
repair activity; affects protein
stability; loss of protein expression;
dbSNP:rs63750070).
{ECO:0000269|PubMed:17101317,
ECO:0000269|PubMed:18951462,
ECO:0000269|PubMed:21120944}.
/FTId=VAR_043751.
VARIANT 175 175 L -> P (in HNPCC1; dbSNP:rs63751291).
{ECO:0000269|PubMed:12655568}.
/FTId=VAR_043752.
VARIANT 177 177 E -> H (in HNPCC1; requires 2 nucleotide
substitutions; unknown pathological
significance; normal mismatch repair
activity). {ECO:0000269|PubMed:22102614}.
/FTId=VAR_067285.
VARIANT 187 187 L -> P (in HNPCC1; decreased mismatch
repair activity; affects protein
stability; loss of protein expression;
dbSNP:rs63751444).
{ECO:0000269|PubMed:17101317,
ECO:0000269|PubMed:18951462,
ECO:0000269|PubMed:21120944}.
/FTId=VAR_043753.
VARIANT 187 187 L -> R (in HNPCC1; decreased mismatch
repair activity; loss of protein
expression; dbSNP:rs63751444).
{ECO:0000269|PubMed:21120944}.
/FTId=VAR_076352.
VARIANT 198 198 E -> G (in HNPCC1; dbSNP:rs63750327).
/FTId=VAR_054513.
VARIANT 199 199 C -> R (in glioma; also associated with
HNPCC1; no effect on MSH2 splicing;
dbSNP:rs63751110).
{ECO:0000269|PubMed:18561205,
ECO:0000269|PubMed:9777949}.
/FTId=VAR_012937.
VARIANT 203 203 G -> R (in CRC; unknown pathological
significance; somatic mutation;
dbSNP:rs587779973).
{ECO:0000269|PubMed:12792735}.
/FTId=VAR_043754.
VARIANT 205 205 E -> Q (shows no defects; normal mismatch
repair activity; dbSNP:rs63749984).
{ECO:0000269|PubMed:22581703}.
/FTId=VAR_068705.
VARIANT 216 216 I -> V (in HNPCC1; unknown pathological
significance; shows slightly reduced
mismatch binding or release efficiency;
dbSNP:rs63749936).
{ECO:0000269|PubMed:11726306}.
/FTId=VAR_012938.
VARIANT 246 246 K -> Q (in HNPCC1; unknown pathological
significance; dbSNP:rs63750881).
{ECO:0000269|PubMed:10573010}.
/FTId=VAR_043755.
VARIANT 265 314 Missing (in HNPCC1).
{ECO:0000269|PubMed:9718327}.
/FTId=VAR_004475.
VARIANT 272 272 A -> V (in HNPCC1; unknown pathological
significance; shows slightly reduced
mismatch binding or release efficiency;
results in partial MSH2 exon 5 skipping;
normal mismatch repair activity;
dbSNP:rs34136999).
{ECO:0000269|PubMed:17101317,
ECO:0000269|PubMed:18561205,
ECO:0000269|PubMed:18951462,
ECO:0000269|PubMed:21120944,
ECO:0000269|PubMed:22102614}.
/FTId=VAR_043756.
VARIANT 283 283 D -> Y (in HNPCC1; dbSNP:rs63750381).
{ECO:0000269|PubMed:15870828}.
/FTId=VAR_043757.
VARIANT 305 305 A -> T (in HNPCC1; normal mismatch repair
activity; dbSNP:rs63751454).
{ECO:0000269|PubMed:22102614,
ECO:0000269|PubMed:9311737}.
/FTId=VAR_004476.
VARIANT 322 322 G -> D (common polymorphism; may be
associated with increased colorectal
cancer susceptibility; shows
significantly decreased repair efficiency
when associated with variant E-487;
dbSNP:rs4987188).
{ECO:0000269|PubMed:10023327,
ECO:0000269|PubMed:10469597,
ECO:0000269|PubMed:10573010,
ECO:0000269|PubMed:10713887,
ECO:0000269|PubMed:10829038,
ECO:0000269|PubMed:11555625,
ECO:0000269|PubMed:11839723,
ECO:0000269|PubMed:12200596,
ECO:0000269|PubMed:12362047,
ECO:0000269|PubMed:14504054,
ECO:0000269|PubMed:16451135,
ECO:0000269|PubMed:18033691,
ECO:0000269|PubMed:18951462,
ECO:0000269|PubMed:21120944,
ECO:0000269|PubMed:22581703,
ECO:0000269|PubMed:8566964,
ECO:0000269|PubMed:9087566,
ECO:0000269|PubMed:9298827,
ECO:0000269|Ref.9}.
/FTId=VAR_004477.
VARIANT 323 323 S -> C (in HNPCC1; unknown pathological
significance; dbSNP:rs63750732).
{ECO:0000269|PubMed:9240418}.
/FTId=VAR_012939.
VARIANT 323 323 S -> Y (in HNPCC1; unknown pathological
significance; dbSNP:rs63750732).
{ECO:0000269|PubMed:12132870}.
/FTId=VAR_043758.
VARIANT 328 328 A -> P (shows significantly decreased
repair efficiency when associated with
variant S-127; presumed to enhance cancer
risk considerably when associated with
variant S-127; dbSNP:rs753237286).
{ECO:0000269|PubMed:22581703}.
/FTId=VAR_068706.
VARIANT 331 331 N -> D (in HNPCC1; no effect on MSH2
splicing; dbSNP:rs267607938).
{ECO:0000269|PubMed:18561205}.
/FTId=VAR_054514.
VARIANT 333 333 C -> Y (in HNPCC1; decreased mismatch
repair activity; affects protein
stability; loss of protein expression;
dbSNP:rs63750828).
{ECO:0000269|PubMed:17101317,
ECO:0000269|PubMed:18951462,
ECO:0000269|PubMed:21120944}.
/FTId=VAR_043759.
VARIANT 335 335 T -> I (in HNPCC1; unknown pathological
significance; dbSNP:rs63750602).
{ECO:0000269|PubMed:12132870}.
/FTId=VAR_043760.
VARIANT 336 336 P -> S (in HNPCC1; dbSNP:rs63751062).
{ECO:0000269|PubMed:10375096}.
/FTId=VAR_043761.
VARIANT 342 342 V -> I (in CRC; unknown pathological
significance; dbSNP:rs63749879).
{ECO:0000269|PubMed:14504054}.
/FTId=VAR_043762.
VARIANT 349 349 P -> L (in HNPCC1; dbSNP:rs587779067).
{ECO:0000269|PubMed:15342696}.
/FTId=VAR_043763.
VARIANT 359 359 R -> S (in HNPCC1; shows a decreased
expression level of the MutS alpha
complex; associated with an abnormal
subcellular localization pattern;
dbSNP:rs63751617).
{ECO:0000269|PubMed:11870161,
ECO:0000269|PubMed:18781619}.
/FTId=VAR_043764.
VARIANT 367 367 V -> I (shows no defects; normal mismatch
repair activity; dbSNP:rs80285180).
{ECO:0000269|PubMed:22581703}.
/FTId=VAR_068707.
VARIANT 385 385 P -> L (in HNPCC1; unknown pathological
significance; normal mismatch repair
activity; dbSNP:rs564736113).
{ECO:0000269|PubMed:22102614}.
/FTId=VAR_067286.
VARIANT 390 390 L -> F (in HNPCC1 and CRC; unknown
pathological significance; may decrease
mismatch repair activity;
dbSNP:rs17224367).
{ECO:0000269|PubMed:10386556,
ECO:0000269|PubMed:10469597,
ECO:0000269|PubMed:12792735,
ECO:0000269|PubMed:15996210,
ECO:0000269|PubMed:16451135,
ECO:0000269|PubMed:22102614,
ECO:0000269|PubMed:8690195,
ECO:0000269|PubMed:9621522,
ECO:0000269|Ref.9}.
/FTId=VAR_004478.
VARIANT 393 393 K -> M (in HNPCC1).
{ECO:0000269|PubMed:12124176}.
/FTId=VAR_043765.
VARIANT 419 419 Q -> K (in CRC; unknown pathological
significance; decreased mismatch repair
activity; dbSNP:rs63750006).
{ECO:0000269|PubMed:10469597,
ECO:0000269|PubMed:12792735,
ECO:0000269|PubMed:15996210,
ECO:0000269|PubMed:8690195}.
/FTId=VAR_012940.
VARIANT 440 440 Missing (in HNPCC1).
{ECO:0000269|PubMed:15365995}.
/FTId=VAR_043766.
VARIANT 470 470 V -> E (in HNPCC1; has no effect on ex
vivo splicing assay; dbSNP:rs267607959).
{ECO:0000269|PubMed:18561205}.
/FTId=VAR_054515.
VARIANT 487 487 D -> E (decreased mismatch repair
activity; shows significantly decreased
repair efficiency when associated with
variant D-322; dbSNP:rs35107951).
{ECO:0000269|PubMed:22581703}.
/FTId=VAR_068708.
VARIANT 492 492 M -> V (in HNPCC1).
/FTId=VAR_043767.
VARIANT 506 506 D -> Y (in HNPCC1 and CRC; sporadic
early-onset CRC; decreased mismatch
repair activity; dbSNP:rs63750492).
{ECO:0000269|PubMed:10469597,
ECO:0000269|PubMed:15365995,
ECO:0000269|PubMed:8797773,
ECO:0000269|PubMed:9559627}.
/FTId=VAR_012941.
VARIANT 519 519 F -> L (in HNPCC1; unknown pathological
significance; normal mismatch repair
activity). {ECO:0000269|PubMed:21120944,
ECO:0000269|PubMed:22102614}.
/FTId=VAR_067287.
VARIANT 524 524 R -> P (in HNPCC1; decreased mismatch
repair activity; dbSNP:rs63751207).
{ECO:0000269|PubMed:10469597,
ECO:0000269|PubMed:12124176,
ECO:0000269|PubMed:9889267}.
/FTId=VAR_004479.
VARIANT 552 552 T -> P (in HNPCC1; dbSNP:rs63750838).
{ECO:0000269|PubMed:12658575}.
/FTId=VAR_043768.
VARIANT 554 554 S -> R (in HNPCC1; unknown pathological
significance; dbSNP:rs63751656).
{ECO:0000269|PubMed:11726306}.
/FTId=VAR_012942.
VARIANT 562 562 E -> V (in HNPCC1; dbSNP:rs63750997).
{ECO:0000269|PubMed:9048925}.
/FTId=VAR_004480.
VARIANT 564 564 T -> A (in HNPCC1; unknown pathological
significance; dbSNP:rs55778204).
{ECO:0000269|PubMed:12200596,
ECO:0000269|PubMed:15996210}.
/FTId=VAR_043769.
VARIANT 583 583 N -> S (in HNPCC1; dbSNP:rs201118107).
{ECO:0000269|PubMed:12658575}.
/FTId=VAR_043770.
VARIANT 596 596 N -> S (in HNPCC1; unknown pathological
significance; dbSNP:rs41295288).
{ECO:0000269|PubMed:10573010,
ECO:0000269|PubMed:18033691,
ECO:0000269|PubMed:8993976}.
/FTId=VAR_012943.
VARIANT 596 596 Missing (in HNPCC1; decreased mismatch
repair activity; has no effect on MSH2
splicing). {ECO:0000269|PubMed:10375096,
ECO:0000269|PubMed:12112654,
ECO:0000269|PubMed:12124176,
ECO:0000269|PubMed:15342696,
ECO:0000269|PubMed:18561205,
ECO:0000269|PubMed:22102614,
ECO:0000269|PubMed:7874129,
ECO:0000269|PubMed:8872463,
ECO:0000269|PubMed:9311737}.
/FTId=VAR_004481.
VARIANT 600 600 A -> V (in HNPCC1; dbSNP:rs63751236).
{ECO:0000269|PubMed:11920458}.
/FTId=VAR_043771.
VARIANT 603 603 D -> N (in HNPCC1; decreased mismatch
repair activity; affects protein
stability; loss of protein expression;
dbSNP:rs63750657).
{ECO:0000269|PubMed:10829038,
ECO:0000269|PubMed:17101317,
ECO:0000269|PubMed:18951462,
ECO:0000269|PubMed:21120944}.
/FTId=VAR_043772.
VARIANT 610 610 H -> N (in HNPCC1; has no effect on MSH2
splicing; dbSNP:rs267607980).
{ECO:0000269|PubMed:18561205}.
/FTId=VAR_054516.
VARIANT 619 619 Y -> C (in CRC; unknown pathological
significance; dbSNP:rs63749982).
{ECO:0000269|PubMed:12792735}.
/FTId=VAR_043773.
VARIANT 622 622 P -> L (in HNPCC1; decreased mismatch
repair activity; confers multiple
biochemical defects; dbSNP:rs28929483).
{ECO:0000269|PubMed:10469597,
ECO:0000269|PubMed:11555625,
ECO:0000269|PubMed:12124176,
ECO:0000269|PubMed:18822302,
ECO:0000269|PubMed:8261515}.
/FTId=VAR_004482.
VARIANT 629 629 Q -> R (in HNPCC1; unknown pathological
significance; dbSNP:rs61756468).
{ECO:0000269|PubMed:12132870,
ECO:0000269|PubMed:12792735,
ECO:0000269|PubMed:15365995,
ECO:0000269|PubMed:15613555,
ECO:0000269|PubMed:15996210}.
/FTId=VAR_043774.
VARIANT 636 636 A -> P (in HNPCC1; decreased mismatch
binding activity; dbSNP:rs63750875).
{ECO:0000269|PubMed:10528862,
ECO:0000269|PubMed:12658575,
ECO:0000269|PubMed:17101317,
ECO:0000269|PubMed:18951462,
ECO:0000269|PubMed:21120944}.
/FTId=VAR_012944.
VARIANT 638 638 R -> G (in HNPCC1; has no effect on MSH2
splicing; dbSNP:rs267607981).
{ECO:0000269|PubMed:18561205}.
/FTId=VAR_054517.
VARIANT 639 639 H -> R (in HNPCC1; decreased mismatch
repair activity; dbSNP:rs587779116).
{ECO:0000269|PubMed:18822302,
ECO:0000269|PubMed:22102614,
ECO:0000269|PubMed:9419403}.
/FTId=VAR_043775.
VARIANT 639 639 H -> Y (in HNPCC1; the equivalent
substitution in yeast does not affect
mismatch repair efficiency in vitro;
dbSNP:rs28929484).
{ECO:0000269|PubMed:11555625,
ECO:0000269|PubMed:8261515}.
/FTId=VAR_004483.
VARIANT 641 641 C -> G (in dbSNP:rs63749946).
{ECO:0000269|PubMed:9718327}.
/FTId=VAR_004484.
VARIANT 645 645 Q -> E (in HNPCC1; has no effect on MSH2
splicing; dbSNP:rs267607982).
{ECO:0000269|PubMed:18561205}.
/FTId=VAR_054518.
VARIANT 647 647 E -> K (in HNPCC1).
{ECO:0000269|PubMed:9419403}.
/FTId=VAR_043776.
VARIANT 656 656 Y -> H (in HNPCC1; somatic mutation).
{ECO:0000269|PubMed:9419403}.
/FTId=VAR_043777.
VARIANT 660 660 D -> G (in HNPCC1).
{ECO:0000269|PubMed:14635101}.
/FTId=VAR_022671.
VARIANT 669 669 G -> R (in HNPCC1; dbSNP:rs63751668).
{ECO:0000269|PubMed:22371642}.
/FTId=VAR_067761.
VARIANT 670 670 P -> L (in dbSNP:rs41294982).
{ECO:0000269|PubMed:18033691}.
/FTId=VAR_038027.
VARIANT 671 671 N -> Y (in HNPCC1; unknown pathological
significance; dbSNP:rs63751232).
{ECO:0000269|PubMed:15300854,
ECO:0000269|PubMed:18561205}.
/FTId=VAR_043778.
VARIANT 674 674 G -> A (in HNPCC1; decreased mismatch
repair activity; dbSNP:rs267607996).
{ECO:0000269|PubMed:18951462,
ECO:0000269|PubMed:21120944}.
/FTId=VAR_076353.
VARIANT 674 674 G -> R (in HNPCC1; decreased mismatch
repair activity; dbSNP:rs63750234).
{ECO:0000269|PubMed:18625694,
ECO:0000269|PubMed:18822302,
ECO:0000269|PubMed:22102614}.
/FTId=VAR_067288.
VARIANT 674 674 G -> S (in HNPCC1; somatic mutation;
dbSNP:rs63750234).
{ECO:0000269|PubMed:12124176}.
/FTId=VAR_004485.
VARIANT 675 675 K -> A (in HNPCC1; requires 2 nucleotide
substitutions; unknown pathological
significance; decreased mismatch repair
activity; dbSNP:rs587779128).
{ECO:0000269|PubMed:22102614}.
/FTId=VAR_067289.
VARIANT 679 679 I -> T (in HNPCC1; somatic mutation).
{ECO:0000269|PubMed:9419403}.
/FTId=VAR_043779.
VARIANT 688 688 M -> I (in HNPCC1; dbSNP:rs63750790).
{ECO:0000269|PubMed:10777691,
ECO:0000269|PubMed:15365995,
ECO:0000269|PubMed:9559627}.
/FTId=VAR_012945.
VARIANT 688 688 M -> V (in HNPCC1; loss of protein
expression).
{ECO:0000269|PubMed:21120944}.
/FTId=VAR_076354.
VARIANT 692 692 G -> R (in HNPCC1; dbSNP:rs63750232).
{ECO:0000269|PubMed:10612836}.
/FTId=VAR_009250.
VARIANT 696 696 P -> L (in HNPCC1; has no effect on ex
vivo splicing assay; dbSNP:rs267607994).
{ECO:0000269|PubMed:18561205}.
/FTId=VAR_054519.
VARIANT 697 697 C -> F (in HNPCC1; decreased mismatch
repair activity; loss of protein
expression; confers multiple biochemical
defects; dbSNP:rs63750398).
{ECO:0000269|PubMed:10469597,
ECO:0000269|PubMed:17101317,
ECO:0000269|PubMed:18822302,
ECO:0000269|PubMed:18951462,
ECO:0000269|PubMed:21120944,
ECO:0000269|PubMed:22102614,
ECO:0000269|PubMed:9298827}.
/FTId=VAR_004486.
VARIANT 697 697 C -> R (in HNPCC1; has no effect on MSH2
splicing; dbSNP:rs63750961).
{ECO:0000269|PubMed:10612836,
ECO:0000269|PubMed:18561205}.
/FTId=VAR_009251.
VARIANT 714 714 A -> V (in HNPCC1; unknown pathological
significance; dbSNP:rs63751224).
{ECO:0000269|PubMed:12132870}.
/FTId=VAR_043780.
VARIANT 722 722 V -> I (common polymorphism associated
with HNPCC1; dbSNP:rs587781996).
{ECO:0000269|PubMed:21120944}.
/FTId=VAR_076355.
VARIANT 723 723 S -> F (in HNPCC1; decreased mismatch
repair activity; has no effect on MSH2
splicing; dbSNP:rs63750794).
{ECO:0000269|PubMed:11920458,
ECO:0000269|PubMed:18561205,
ECO:0000269|PubMed:22102614}.
/FTId=VAR_043781.
VARIANT 729 729 M -> V (in HNPCC1; somatic mutation).
{ECO:0000269|PubMed:9419403}.
/FTId=VAR_043782.
VARIANT 732 732 T -> I (in HNPCC1; somatic mutation).
{ECO:0000269|PubMed:9419403}.
/FTId=VAR_043783.
VARIANT 745 746 Missing (in HNPCC1; decreased mismatch
repair activity).
{ECO:0000269|PubMed:17101317,
ECO:0000269|PubMed:18951462,
ECO:0000269|PubMed:21120944}.
/FTId=VAR_043784.
VARIANT 748 748 D -> Y (in HNPCC1; has no effect on MSH2
splicing; dbSNP:rs267608007).
{ECO:0000269|PubMed:18561205}.
/FTId=VAR_054520.
VARIANT 749 749 E -> K (in HNPCC1; decreased mismatch
repair activity; no loss of protein
expression; dbSNP:rs63751477).
{ECO:0000269|PubMed:17101317,
ECO:0000269|PubMed:18951462,
ECO:0000269|PubMed:21120944}.
/FTId=VAR_043785.
VARIANT 759 759 G -> E (in HNPCC1; unknown pathological
significance; decreased mismatch repair
activity; dbSNP:rs386833406).
{ECO:0000269|PubMed:22102614}.
/FTId=VAR_067290.
VARIANT 770 770 I -> V (in dbSNP:rs63750684).
{ECO:0000269|PubMed:9718327}.
/FTId=VAR_004487.
VARIANT 779 779 M -> I (in dbSNP:rs41295292).
{ECO:0000269|PubMed:18033691}.
/FTId=VAR_038028.
VARIANT 805 805 L -> V (in HNPCC1; unknown pathological
significance; normal mismatch repair
activity). {ECO:0000269|PubMed:22102614}.
/FTId=VAR_067291.
VARIANT 807 807 T -> S (in dbSNP:rs41295294).
{ECO:0000269|PubMed:18033691}.
/FTId=VAR_038029.
VARIANT 813 813 M -> V (in HNPCC1; dbSNP:rs63749841).
{ECO:0000269|PubMed:12373605}.
/FTId=VAR_043786.
VARIANT 824 824 Q -> E (in gastric cancer; unknown
pathological significance;
dbSNP:rs63750623).
{ECO:0000269|PubMed:12132870}.
/FTId=VAR_043787.
VARIANT 834 834 A -> T (in HNPCC1; decreased mismatch
repair activity; shows no functional
defects in gel shift assay;
dbSNP:rs63750757).
{ECO:0000269|PubMed:10573010,
ECO:0000269|PubMed:17101317,
ECO:0000269|PubMed:18822302,
ECO:0000269|PubMed:18951462,
ECO:0000269|PubMed:21120944,
ECO:0000269|PubMed:9311737}.
/FTId=VAR_004488.
VARIANT 835 835 N -> H (in dbSNP:rs41295296).
{ECO:0000269|PubMed:18033691}.
/FTId=VAR_038030.
VARIANT 839 839 H -> Q (in HNPCC1; has no effect on MSH2
splicing; dbSNP:rs267608016).
{ECO:0000269|PubMed:18561205}.
/FTId=VAR_054521.
VARIANT 839 839 H -> R (in HNPCC1; dbSNP:rs63750027).
{ECO:0000269|PubMed:15613555}.
/FTId=VAR_043788.
VARIANT 843 843 C -> G (in HNPCC1; unknown pathological
significance; normal mismatch repair
activity). {ECO:0000269|PubMed:22102614}.
/FTId=VAR_067292.
VARIANT 845 845 K -> E (in HNPCC1; dbSNP:rs63750571).
{ECO:0000269|PubMed:10777691}.
/FTId=VAR_013172.
VARIANT 853 853 E -> A (in HNPCC1; unknown pathological
significance; dbSNP:rs63750797).
{ECO:0000269|PubMed:12362047,
ECO:0000269|PubMed:16451135}.
/FTId=VAR_043789.
VARIANT 860 860 S -> L (in HNPCC1; unknown pathological
significance; normal mismatch repair
activity; dbSNP:rs63750849).
{ECO:0000269|PubMed:22102614}.
/FTId=VAR_067293.
VARIANT 868 868 P -> A (in gastric cancer; unknown
pathological significance;
dbSNP:rs63751400).
{ECO:0000269|PubMed:12132870}.
/FTId=VAR_043790.
VARIANT 870 870 A -> G (in gastric cancer; unknown
pathological significance;
dbSNP:rs63750709).
{ECO:0000269|PubMed:12132870}.
/FTId=VAR_043791.
VARIANT 873 873 C -> G (in gastric cancer; unknown
pathological significance;
dbSNP:rs63750795).
{ECO:0000269|PubMed:12132870}.
/FTId=VAR_043792.
VARIANT 886 886 E -> G (in HNPCC1; unknown pathological
significance; normal mismatch repair
activity; dbSNP:rs63750350).
{ECO:0000269|PubMed:12112654,
ECO:0000269|PubMed:21120944,
ECO:0000269|PubMed:22102614}.
/FTId=VAR_043793.
VARIANT 905 905 T -> R (in HNPCC1; unknown pathological
significance; dbSNP:rs267608022).
{ECO:0000269|PubMed:12124176}.
/FTId=VAR_004489.
VARIANT 909 909 K -> I (found in a colorectal cancer
sample; normal mismatch repair activity;
dbSNP:rs34319539).
{ECO:0000269|PubMed:22581703}.
/FTId=VAR_068709.
VARIANT 911 911 L -> R (in dbSNP:rs41295182).
{ECO:0000269|PubMed:18033691}.
/FTId=VAR_038031.
VARIANT 923 923 V -> E (in HNPCC1; unknown pathological
significance; dbSNP:rs146421227).
{ECO:0000269|PubMed:12112654,
ECO:0000269|PubMed:17101317,
ECO:0000269|PubMed:18951462,
ECO:0000269|PubMed:21120944}.
/FTId=VAR_043794.
VARIANT 931 931 K -> T (in HNPCC1; dbSNP:rs267608023).
{ECO:0000269|PubMed:15046096}.
/FTId=VAR_043795.
MUTAGEN 675 675 K->R: No effect on mismatch binding,
complete loss of DNA repair function when
associated with MSH6 mutant R-1140.
{ECO:0000269|PubMed:9564049}.
CONFLICT 784 784 F -> I (in Ref. 7; BX649122).
{ECO:0000305}.
CONFLICT 836 836 F -> S (in Ref. 7; BX649122).
{ECO:0000305}.
HELIX 14 24 {ECO:0000244|PDB:3THX}.
STRAND 33 38 {ECO:0000244|PDB:3THX}.
STRAND 40 46 {ECO:0000244|PDB:3THX}.
HELIX 48 56 {ECO:0000244|PDB:3THX}.
STRAND 59 61 {ECO:0000244|PDB:3THX}.
STRAND 65 71 {ECO:0000244|PDB:3THX}.
STRAND 75 81 {ECO:0000244|PDB:3THX}.
HELIX 82 94 {ECO:0000244|PDB:3THX}.
STRAND 99 105 {ECO:0000244|PDB:3THX}.
STRAND 117 124 {ECO:0000244|PDB:3THX}.
HELIX 129 131 {ECO:0000244|PDB:2O8B}.
HELIX 132 135 {ECO:0000244|PDB:3THX}.
STRAND 147 152 {ECO:0000244|PDB:3THX}.
STRAND 155 158 {ECO:0000244|PDB:3THX}.
STRAND 160 167 {ECO:0000244|PDB:3THX}.
TURN 168 171 {ECO:0000244|PDB:3THX}.
STRAND 172 179 {ECO:0000244|PDB:3THX}.
HELIX 185 194 {ECO:0000244|PDB:3THX}.
STRAND 197 204 {ECO:0000244|PDB:3THX}.
HELIX 208 220 {ECO:0000244|PDB:3THX}.
STRAND 223 227 {ECO:0000244|PDB:3THX}.
HELIX 229 232 {ECO:0000244|PDB:3THX}.
HELIX 237 244 {ECO:0000244|PDB:3THX}.
TURN 252 254 {ECO:0000244|PDB:2O8E}.
HELIX 255 257 {ECO:0000244|PDB:3THX}.
HELIX 259 262 {ECO:0000244|PDB:3THX}.
HELIX 264 277 {ECO:0000244|PDB:3THX}.
HELIX 279 281 {ECO:0000244|PDB:3THX}.
HELIX 283 285 {ECO:0000244|PDB:3THX}.
STRAND 289 293 {ECO:0000244|PDB:3THX}.
HELIX 296 298 {ECO:0000244|PDB:3THX}.
HELIX 304 309 {ECO:0000244|PDB:3THX}.
HELIX 326 330 {ECO:0000244|PDB:3THX}.
HELIX 336 347 {ECO:0000244|PDB:3THX}.
HELIX 353 367 {ECO:0000244|PDB:3THX}.
HELIX 370 377 {ECO:0000244|PDB:3THX}.
TURN 378 380 {ECO:0000244|PDB:3THX}.
HELIX 381 383 {ECO:0000244|PDB:3THX}.
HELIX 387 395 {ECO:0000244|PDB:3THX}.
HELIX 401 411 {ECO:0000244|PDB:3THX}.
HELIX 414 423 {ECO:0000244|PDB:3THX}.
STRAND 424 426 {ECO:0000244|PDB:2O8F}.
STRAND 427 429 {ECO:0000244|PDB:3THX}.
HELIX 432 435 {ECO:0000244|PDB:3THX}.
HELIX 437 455 {ECO:0000244|PDB:3THX}.
HELIX 462 464 {ECO:0000244|PDB:3THX}.
TURN 472 474 {ECO:0000244|PDB:2O8B}.
HELIX 476 502 {ECO:0000244|PDB:3THX}.
TURN 507 509 {ECO:0000244|PDB:3THX}.
STRAND 512 515 {ECO:0000244|PDB:3THX}.
TURN 517 519 {ECO:0000244|PDB:2O8B}.
STRAND 521 525 {ECO:0000244|PDB:3THX}.
HELIX 527 530 {ECO:0000244|PDB:3THX}.
TURN 531 535 {ECO:0000244|PDB:3THX}.
STRAND 540 544 {ECO:0000244|PDB:3THX}.
STRAND 549 552 {ECO:0000244|PDB:3THX}.
HELIX 556 563 {ECO:0000244|PDB:3THX}.
TURN 564 567 {ECO:0000244|PDB:3THX}.
HELIX 568 585 {ECO:0000244|PDB:3THX}.
HELIX 586 588 {ECO:0000244|PDB:3THX}.
HELIX 589 613 {ECO:0000244|PDB:3THX}.
STRAND 615 617 {ECO:0000244|PDB:3THX}.
STRAND 623 625 {ECO:0000244|PDB:3THX}.
STRAND 631 637 {ECO:0000244|PDB:3THX}.
TURN 640 644 {ECO:0000244|PDB:3THX}.
STRAND 653 658 {ECO:0000244|PDB:3THX}.
TURN 659 661 {ECO:0000244|PDB:3THX}.
STRAND 664 668 {ECO:0000244|PDB:3THX}.
HELIX 675 691 {ECO:0000244|PDB:3THX}.
STRAND 695 703 {ECO:0000244|PDB:3THX}.
STRAND 706 711 {ECO:0000244|PDB:3THX}.
HELIX 724 738 {ECO:0000244|PDB:3THX}.
STRAND 744 749 {ECO:0000244|PDB:3THX}.
HELIX 756 772 {ECO:0000244|PDB:3THX}.
STRAND 777 783 {ECO:0000244|PDB:3THX}.
HELIX 785 792 {ECO:0000244|PDB:3THX}.
STRAND 797 807 {ECO:0000244|PDB:3THX}.
STRAND 810 820 {ECO:0000244|PDB:3THX}.
HELIX 827 833 {ECO:0000244|PDB:3THX}.
HELIX 838 850 {ECO:0000244|PDB:3THX}.
TURN 851 855 {ECO:0000244|PDB:3THX}.
HELIX 875 892 {ECO:0000244|PDB:3THX}.
HELIX 896 898 {ECO:0000244|PDB:3THX}.
HELIX 901 917 {ECO:0000244|PDB:3THX}.
HELIX 921 928 {ECO:0000244|PDB:3THX}.
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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