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MSH6 recombinant protein :: DNA mismatch repair protein Msh6 Recombinant Protein

Scan QR to view Datasheet Catalog #    MBS957892
SDS-Page
Unit / Price
0.05 mg (E-Coli)  /  $190 +1 FREE 8GB USB
0.2 mg (E-Coli)  /  $460 +1 FREE 8GB USB
0.5 mg (E-Coli)  /  $750 +1 FREE 8GB USB
0.05 mg (Baculovirus)  /  $950 +1 FREE 8GB USB
0.5 mg (Yeast)  /  $950 +1 FREE 8GB USB
0.05 mg (Mammalian-Cell)  /  $1,170 +1 FREE 8GB USB
1 mg (E-Coli)  /  $1,180 +1 FREE 8GB USB
0.1 mg (Baculovirus)  /  $1,390 +1 FREE 8GB USB
1 mg (Yeast)  /  $1,390 +1 FREE 8GB USB
0.1 mg (Mammalian-Cell)  /  $1,850 +2 FREE 8GB USB
 
 Go to:   rightarrow  Product Names   rightarrow Product Info   rightarrow Accession #s   rightarrow Product Desc   rightarrow Diseases/Tissues/Pathways   rightarrow Applications   rightarrow References 
 Product Name   

DNA mismatch repair protein Msh6, Recombinant Protein

 Also Known As   

Recombinant Human DNA mismatch repair protein Msh6

 Product Synonym Names    G/T mismatch-binding protein; GTBP; GTMBP; MutS-alpha 160 kDa subunit; p160
 Product Gene Name   

MSH6 recombinant protein

[Similar Products]
 Research Use Only    For Research Use Only. Not for use in diagnostic procedures.
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 Sequence Positions    1-400
 Sequence    MSRQSTLYSF FPKSPALSDA NKASARASRE GGRAAAAPGA SPSPGGDAAW SEAGPGPRPL ARSASPPKAK NLNGGLRRSV APAAPTSCDF SPGDLVWAKM EGYPWWPCLV YNHPFDGTFI REKGKSVRVH VQFFDDSPTR GWVSKRLLKP YTGSKSKEAQ KGGHFYSAKP EILRAMQRAD EALNKDKIKR LELAVCDEPS EPEEEEEMEV GTTYVTDKSE EDNEIESEEE VQPKTQGSRR SSRQIKKRRV ISDSE
 OMIM    276300
 3D Structure    ModBase 3D Structure for P52701
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 Host    E Coli or Yeast or Baculovirus or Mammalian Cell
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 Purity/Purification    Greater than 90% as determined by SDS-PAGE.
 Form/Format    Liquid containing glycerol; lyophilization may be available upon request.
 Tag Information    This protein contains an N-terminal tag and may also contain a C-terminal Myc-tag. N-terminal host tags may vary (His, His-SUMO, His-B2M, GST). Tag types are determined by various factors including tag-protein stability and, therefore, are subject to change; please inquire for tag information. Additional charge for Tag removal. Tag removal service standardly refers to removal of N-terminal Tag. Any C-terminal Myc-tag may remain intact unless removal of the C-terminal Myc-tag is specifically requested. In most cases tags can be successfully removed. If the lab concludes the protein is no longer stable after tag removal then your protein will be supplied with the tag intact, and you will not be charged for tag removal service.
 Sterility    Sterile filter available upon request.
 Endotoxin    Low endotoxin available upon request.
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 Preparation and Storage    Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.
 ISO Certification    Manufactured in an ISO 9001:2008 Certified Laboratory.
 Other Notes    Small volumes of MSH6 recombinant protein vial(s) may occasionally become entrapped in the seal of the product vial during shipment and storage. If necessary, briefly centrifuge the vial on a tabletop centrifuge to dislodge any liquid in the container`s cap. Certain products may require to ship with dry ice and additional dry ice fee may apply.
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Product Description specifically for MSH6 recombinant protein

   Component of the post-replicative DNA mismatch repair system (MMR). Heterodimerizes with MSH2 to form MutS alpha, which binds to DNA mismatches thereby initiating DNA repair. When bound, MutS alpha bends the DNA helix and shields approximately 20 base pairs, and recognizes single base mismatches and dinucleotide insertion-deletion loops (IDL) in the DNA. After mismatch binding, 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. Recruited on chromatin in G1 and early S phase via its PWWP domain that specifically binds trimethylated 'Lys-36' of histone H3 (H3K36me3): early recruitment to chromatin to be replicated allowing a quick identification of mismatch repair to initiate the DNA mismatch repair reaction
 Product Categories/Family for MSH6 recombinant protein    Epigenetics and Nuclear Signaling
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 SDS-Page of MSH6 recombinant protein    MSH6 recombinant protein SDS-Page image
(Note: Representative image, actual molecular weight may vary depending on Tag type and expression host)
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NCBI/Uniprot data below describe general gene information for MSH6. It may not necessarily be applicable to this product.
 NCBI GI #    4504191
 NCBI GeneID    2956
 NCBI Accession #    NP_000170.1 [Other Products]
 NCBI GenBank Nucleotide #    NM_000179.2 [Other Products]
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 UniProt Primary Accession #    P52701 [Other Products]
 UniProt Secondary Accession #    O43706; O43917; Q8TCX4; Q9BTB5; B4DF41; B4E3I4; F5H2F9 [Other Products]
 UniProt Related Accession #    P52701 [Other Products]
 Molecular Weight    60.03kD
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 NCBI Official Full Name    DNA mismatch repair protein Msh6 isoform 1
 NCBI Official Synonym Full Names    mutS homolog 6
 NCBI Official Symbol    MSH6 [Similar Products]
 NCBI Official Synonym Symbols   
GTBP; HSAP; p160; GTMBP; HNPCC5
[Similar Products]
 NCBI Protein Information    DNA mismatch repair protein Msh6
 UniProt Protein Name    DNA mismatch repair protein Msh6
 UniProt Synonym Protein Names   
G/T mismatch-binding protein; GTBP; GTMBP; MutS-alpha 160 kDa subunit; p160
 Protein Family    DNA mismatch repair protein
 UniProt Gene Name    MSH6 [Similar Products]
 UniProt Synonym Gene Names    GTBP; hMSH6; GTBP; GTMBP; p160 [Similar Products]
 UniProt Entry Name    MSH6_HUMAN
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 NCBI Summary for MSH6    This gene encodes a member of the DNA mismatch repair MutS family. In E. coli, the MutS protein helps in the recognition of mismatched nucleotides prior to their repair. A highly conserved region of approximately 150 aa, called the Walker-A adenine nucleotide binding motif, exists in MutS homologs. The encoded protein heterodimerizes with MSH2 to form a mismatch recognition complex that functions as a bidirectional molecular switch that exchanges ADP and ATP as DNA mismatches are bound and dissociated. Mutations in this gene may be associated with hereditary nonpolyposis colon cancer, colorectal cancer, and endometrial cancer. Transcripts variants encoding different isoforms have been described. [provided by RefSeq, Jul 2013]
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 UniProt Comments for MSH6    MSH6: Component of the post-replicative DNA mismatch repair system (MMR). Heterodimerizes with MSH2 to form MutS alpha, which binds to DNA mismatches thereby initiating DNA repair. When bound, MutS alpha bends the DNA helix and shields approximately 20 base pairs, and recognizes single base mismatches and dinucleotide insertion-deletion loops (IDL) in the DNA. After mismatch binding, 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. Heterodimer consisting of MSH2-MSH6 (MutS alpha). Forms 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. Belongs to the DNA mismatch repair MutS family. 2 isoforms of the human protein are produced by alternative splicing.

Protein type: DNA-binding

Chromosomal Location of Human Ortholog: 2p16

Cellular Component: cytoplasm; Golgi apparatus; intracellular membrane-bound organelle; MutSalpha complex; nuclear chromatin; nucleoplasm; plasma membrane

Molecular Function: ADP binding; ATP binding; ATPase activity; chromatin binding; double-stranded DNA binding; four-way junction DNA binding; guanine/thymine mispair binding; magnesium ion binding; methylated histone residue binding; mismatched DNA binding; MutLalpha complex binding; oxidized purine DNA binding; protein binding; protein homodimerization activity; single guanine insertion binding; single thymine insertion binding

Biological Process: determination of adult life span; DNA damage response, signal transduction resulting in induction of apoptosis; DNA repair; isotype switching; maintenance of DNA repeat elements; meiotic mismatch repair; mismatch repair; negative regulation of DNA recombination; positive regulation of helicase activity; positive regulation of isotype switching; response to UV; somatic hypermutation of immunoglobulin genes; somatic recombination of immunoglobulin gene segments; viral reproduction

Disease: Colorectal Cancer, Hereditary Nonpolyposis, Type 5; Endometrial Cancer; Mismatch Repair Cancer Syndrome
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Product References and Citations for MSH6 recombinant protein

   hMSH2 forms specific mispair-binding complexes with hMSH3 and hMSH6.Acharya S., Wilson T., Gradia S., Kane M.F., Guerrette S., Marsischky G.T., Kolodner R.D., Fishel R.Proc. Natl. Acad. Sci. U.S.A. 93:13629-13634(1996) Alternative splicing of GTBP in normal human tissues.Shiwaku H.O., Wakatsuki S., Mori Y., Fukushige S., Horii A.DNA Res. 4:359-362(1997) Complete sequencing and characterization of 21,243 full-length human cDNAs.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.Nat. Genet. 36:40-45(2004) NIEHS SNPs programGeneration and annotation of the DNA sequences of human chromosomes 2 and 4.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.Nature 434:724-731(2005) GTBP, a 160-kilodalton protein essential for mismatch-binding activity in human cells.Palombo F., Gallinari P., Iaccarino I., Lettieri T., Hughes M., D'Arrigo A., Truong O., Hsuan J.J., Jiricny J.Science 268:1912-1914(1995) Molecular cloning of the N-terminus of GTBP.Nicolaides N.C., Palombo F., Kinzler K.W., Vogelstein B., Jiricny J.Genomics 31:395-397(1996) Isolation of an hMSH2-p160 heterodimer that restores DNA mismatch repair to tumor cells.Drummond J.T., Li G.-M., Longley M.J., Modrich P.Science 268:1909-1912(1995) Nucleotide-promoted release of hMutSalpha from heteroduplex DNA is consistent with an ATP-dependent translocation mechanism.Blackwell L.J., Martik D., Bjornson K.P., Bjornson E.S., Modrich P.J. Biol. Chem. 273:32055-32062(1998) DNA-dependent activation of the hMutSalpha ATPase.Blackwell L.J., Bjornson K.P., Modrich P.J. Biol. Chem. 273:32049-32054(1998) hMSH2 and hMSH6 play distinct roles in mismatch binding and contribute differently to the ATPase activity of hMutSalpha.Iaccarino I., Marra G., Palombo F., Jiricny J.EMBO J. 17:2677-2686(1998) Functional analysis of human MutSalpha and MutSbeta complexes in yeast.Clark A.B., Cook M.E., Tran H.T., Gordenin D.A., Resnick M.A., Kunkel T.A.Nucleic Acids Res. 27:736-742(1999) hMSH2-hMSH6 forms a hydrolysis-independent sliding clamp on mismatched DNA.Gradia S., Subramanian D., Wilson T., Acharya S., Makhov A., Griffith J., Fishel R.Mol. Cell 3:255-261(1999) The role of mismatched nucleotides in activating the hMSH2-hMSH6 molecular switch.Gradia S., Acharya S., Fishel R.J. Biol. Chem. 275:3922-3930(2000) The mismatch DNA repair heterodimer, hMSH2/6, regulates BLM helicase.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.Oncogene 23:3749-3756(2004) hMutS alpha is protected from ubiquitin-proteasome-dependent degradation by atypical protein kinase C zeta phosphorylation.Hernandez-Pigeon H., Quillet-Mary A., Louat T., Schambourg A., Humbert O., Selves J., Salles B., Laurent G., Lautier D.J. Mol. Biol. 348:63-74(2005) BASC, a super complex of BRCA1-associated proteins involved in the recognition and repair of aberrant DNA structures.Wang Y., Cortez D., Yazdi P., Neff N., Elledge S.J., Qin J.Genes Dev. 14:927-939(2000) Germline mutation of MSH6 as the cause of hereditary nonpolyposis colorectal cancer.Miyaki M., Konishi M., Tanaka K., Kikuchi-Yanoshita R., Muraoka M., Yasuno M., Igari T., Koike M., Chiba M., Mori T.Nat. Genet. 17:271-272(1997) Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.Cell 127:635-648(2006) A probability-based approach for high-throughput protein phosphorylation analysis and site localization.Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.Nat. Biotechnol. 24:1285-1292(2006) Novel biallelic mutations in MSH6 and PMS2 genes gene conversion as a likely cause of PMS2 gene inactivation.Auclair J., Leroux D., Desseigne F., Lasset C., Saurin J.C., Joly M.O., Pinson S., Xu X.L., Montmain G., Ruano E., Navarro C., Puisieux A., Wang Q.Hum. Mutat. 28:1084-1090(2007) ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage.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.Science 316:1160-1166(2007) Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis.Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. IIIJ. Proteome Res. 7:1346-1351(2008) Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle.Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.Mol. Cell 31:438-448(2008) A quantitative atlas of mitotic phosphorylation.Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) Lysine acetylation targets protein complexes and co-regulates major cellular functions.Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.Science 325:834-840(2009) Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.Sci. Signal. 3:RA3-RA3(2010) Initial characterization of the human central proteome.Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.BMC Syst. Biol. 5:17-17(2011) DNA mismatch repair proteins are required for efficient herpes simplex virus 1 replication.Mohni K.N., Mastrocola A.S., Bai P., Weller S.K., Heinen C.D.J. Virol. 85:12241-12253(2011) System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation.Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.Sci. Signal. 4:RS3-RS3(2011) The histone mark H3K36me3 regulates human DNA mismatch repair through its interaction with MutSalpha.Li F., Mao G., Tong D., Huang J., Gu L., Yang W., Li G.M.Cell 153:590-600(2013) Structure of the human MutSalpha DNA lesion recognition complex.Warren J.J., Pohlhaus T.J., Changela A., Iyer R.R., Modrich P.L., Beese L.S.Mol. Cell 26:579-592(2007) Mutations of GTBP in genetically unstable cells.Papadopoulos N., Nicolaides N.C., Liu B., Parsons R., Lengauer C., Palombo F., D'Arrigo A., Markowitz S., Willson J.K.V., Kinzler K.W., Jiricny J., Vogelstein B.Science 268:1915-1917(1995) Association of hereditary nonpolyposis colorectal cancer-related tumors displaying low microsatellite instability with MSH6 germline mutations.Wu Y., Berends M.J.W., Mensink R.G.J., Kempinga C., Sijmons R.H., van Der Zee A.G.J., Hollema H., Kleibeuker J.H., Buys C.H.C.M., Hofstra R.M.W.Am. J. Hum. Genet. 65:1291-1298(1999) Germ-line msh6 mutations in colorectal cancer families.Kolodner R.D., Tytell J.D., Schmeits J.L., Kane M.F., Das Gupta R., Weger J., Wahlberg S., Fox E.A., Peel D., Ziogas A., Garber J.E., Syngal S., Anton-Culver H., Li F.P.Cancer Res. 59:5068-5074(1999) Prevalence of germline mutations of hMLH1, hMSH2, hPMS1, hPMS2, and hMSH6 genes in 75 French kindreds with nonpolyposis colorectal cancer.Wang Q., Lasset C., Desseigne F., Saurin J.-C., Maugard C., Navarro C., Ruano E., Descos L., Trillet-Lenoir V., Bosset J.-F., Puisieux A.Hum. Genet. 105:79-85(1999) Frequent microsatellite instability and mismatch repair gene mutations in young Chinese patients with colorectal cancer.Chan T.L., Yuen S.T., Chung L.P., Ho J.W.C., Kwan K.Y.M., Chan A.S.Y., Ho J.C.Y., Leung S.Y., Wyllie A.H.J. Natl. Cancer Inst. 91:1221-1226(1999) Do MSH6 mutations contribute to double primary cancers of the colorectum and endometrium?Charames G.S., Millar A.L., Pal T., Narod S., Bapat B.Hum. Genet. 107:623-629(2000) Sequence analysis of the mismatch repair gene hMSH6 in the germline of patients with familial and sporadic colorectal cancer.Plaschke J., Kruppa C., Tischler R., Bocker T., Pistorius S., Dralle H., Rueschoff J., Saeger H.D., Fishel R., Schackert H.K.3.0.CO;2-B>Int. J. Cancer 85:606-613(2000) Germline and somatic mutations in hMSH6 and hMSH3 in gastrointestinal cancers of the microsatellite mutator phenotype.Ohmiya N., Matsumoto S., Yamamoto H., Baranovskaya S., Malkhosyan S.R., Perucho M.Gene 272:301-313(2001) A role for MLH3 in hereditary nonpolyposis colorectal cancer.Wu Y., Berends M.J.W., Sijmons R.H., Mensink R.G.J., Verlind E., Kooi K.A., van der Sluis T., Kempinga C., van der Zee A.G.J., Hollema H., Buys C.H.C.M., Kleibeuker J.H., Hofstra R.M.W.Nat. Genet. 29:137-138(2001) Molecular and clinical characteristics of MSH6 variants an analysis of 25 index carriers of a germline variant.Berends M.J.W., Wu Y., Sijmons R.H., Mensink R.G.J., van der Sluis T., Hordijk-Hos J.M., de Vries E.G.E., Hollema H., Karrenbeld A., Buys C.H.C.M., van der Zee A.G.J., Hofstra R.M.W., Kleibeuker J.H.Am. J. Hum. Genet. 70:26-37(2002) Involvement of hMSH6 in the development of hereditary and sporadic colorectal cancer revealed by immunostaining is based on germline mutations, but rarely on somatic inactivation.Plaschke J., Krueger S., Pistorius S., Theissig F., Saeger H.D., Schackert H.K.Int. J. Cancer 97:643-648(2002) 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.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.Am. J. Hum. Genet. 72:1088-1100(2003) Two mismatch repair gene mutations found in a colon cancer patient - which one is pathogenic?Kariola R., Otway R., Loennqvist K.E., Raevaara T.E., Macrae F., Vos Y.J., Kohonen-Corish M., Hofstra R.M.W., Nystroem-Lahti M.Hum. Genet. 112:105-109(2003) MSH6 germline mutations are rare in colorectal cancer families.Peterlongo P., Nafa K., Lerman G.S., Glogowski E., Shia J., Ye T.Z., Markowitz A.J., Guillem J.G., Kolachana P., Boyd J.A., Offit K., Ellis N.A.Int. J. Cancer 107:571-579(2003) MSH6 missense mutations are often associated with no or low cancer susceptibility.Kariola R., Hampel H., Frankel W.L., Raevaara T.E., de la Chapelle A., Nystroem-Lahti M.Br. J. Cancer 91:1287-1292(2004) Eight novel MSH6 germline mutations in patients with familial and nonfamilial colorectal cancer selected by loss of protein expression in tumor tissue.The German HNPCC consortiumPlaschke J., Krueger S., Dietmaier W., Gebert J., Sutter C., Mangold E., Pagenstecher C., Holinski-Feder E., Schulmann K., Moeslein G., Rueschoff J., Engel C., Evans G., Schackert H.K.Hum. Mutat. 23:285-285(2004) Germline mutations in MLH1, MSH2 and MSH6 in Korean hereditary non-polyposis colorectal cancer families.Shin Y.-K., Heo S.-C., Shin J.-H., Hong S.-H., Ku J.-L., Yoo B.-C., Kim I.-J., Park J.-G.Hum. Mutat. 24:351-351(2004) Mutation analysis of the MLH1, MSH2 and MSH6 genes in patients with double primary cancers of the colorectum and the endometrium a population-based study in northern Sweden.Cederquist K., Emanuelsson M., Goeransson I., Holinski-Feder E., Mueller-Koch Y., Golovleva I., Groenberg H.Int. J. Cancer 109:370-376(2004) Lower incidence of colorectal cancer and later age of disease onset in 27 families with pathogenic MSH6 germline mutations compared with families with MLH1 or MSH2 mutations the German hereditary nonpolyposis colorectal cancer consortium.Plaschke J., Engel C., Krueger S., Holinski-Feder E., Pagenstecher C., Mangold E., Moeslein G., Schulmann K., Gebert J., von Knebel Doeberitz M., Rueschoff J., Loeffler M., Schackert H.K.J. Clin. Oncol. 22:4486-4494(2004) Patterns of somatic mutation in human cancer genomes.Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.Nature 446:153-158(2007) Classification of ambiguous mutations in DNA mismatch repair genes identified in a population-based study of colorectal cancer.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.Hum. Mutat. 29:367-374(2008) A rapid and cell-free assay to test the activity of lynch syndrome-associated MSH2 and MSH6 missense variants.Drost M., Zonneveld J.B., van Hees S., Rasmussen L.J., Hofstra R.M., de Wind N.Hum. Mutat. 33:488-494(2012) Mismatch repair analysis of inherited MSH2 and/or MSH6 variation pairs found in cancer patients.Kantelinen J., Kansikas M., Candelin S., Hampel H., Smith B., Holm L., Kariola R., Nystrom M.Hum. Mutat. 33:1294-1301(2012) +Additional computationally mapped references.<p>Provides general information on the entry.
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 Research Articles on MSH6    1. MutSalpha, proliferating cell nuclear antigen, and replication factor C activate MutLalpha endonuclease to remove the 1-nucleotide Okazaki fragment flaps
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Products associated with MSH6 recombinant proteinPathways associated with MSH6 recombinant protein
 Reference Product  PubMed Publications
 MSH2 recombinant protein  >1085 publications with MSH6 and MSH2
 MLH1 recombinant protein  >880 publications with MSH6 and MLH1
 MSH3 recombinant protein  >202 publications with MSH6 and MSH3
 PMS1 recombinant protein  >93 publications with MSH6 and PMS1
 MLH3 recombinant protein  >46 publications with MSH6 and MLH3
 PCNA recombinant protein  >41 publications with MSH6 and PCNA
 POLE recombinant protein  >7 publications with MSH6 and POLE
 PRKDC recombinant protein  >2 publications with MSH6 and PRKDC
 XRCC6 recombinant protein  >1 publications with MSH6 and XRCC6
 Products by Pathway  Pathway Diagram
 BRCA1-associated Genome Surveillance Complex (BASC) Pathway antibodies  BRCA1-associated Genome Surveillance Complex (BASC) Pathway Diagram
 BRCA1-associated Genome Surveillance Complex (BASC) Pathway antibodies  BRCA1-associated Genome Surveillance Complex (BASC) Pathway Diagram
 Colorectal Cancer Pathway antibodies  Colorectal Cancer Pathway Diagram
 Colorectal Cancer Pathway antibodies  Colorectal Cancer Pathway Diagram
 DNA Repair Pathway antibodies  DNA Repair Pathway Diagram
 Integrated Breast Cancer Pathway antibodies  Integrated Breast Cancer Pathway Diagram
 Integrated Cancer Pathway antibodies  Integrated Cancer Pathway Diagram
 Mismatch Repair Pathway antibodies  Mismatch Repair Pathway Diagram
 Mismatch Repair Pathway antibodies  Mismatch Repair Pathway Diagram
 Mismatch Repair Pathway antibodies  Mismatch Repair Pathway Diagram
Diseases associated with MSH6 recombinant proteinOrgans/Tissues associated with MSH6 recombinant protein
 Disease Name  Pubmed Publications
 Colorectal Neoplasms, Hereditary Nonpolyposis Antibodies  >476 publications with MSH6 and Colorectal Neoplasms, Hereditary Nonpolyposis
 Microsatellite Instability Antibodies  >466 publications with MSH6 and Microsatellite Instability
 Endometrial Neoplasms Antibodies  >204 publications with MSH6 and Endometrial Neoplasms
 Nervous System Diseases Antibodies  >66 publications with MSH6 and Nervous System Diseases
 Neoplasms, Experimental Antibodies  >34 publications with MSH6 and Neoplasms, Experimental
 Chromosome Aberrations Antibodies  >31 publications with MSH6 and Chromosome Aberrations
 Kidney Diseases Antibodies  >18 publications with MSH6 and Kidney Diseases
 Hyperplasia Antibodies  >16 publications with MSH6 and Hyperplasia
 Liver Diseases Antibodies  >14 publications with MSH6 and Liver Diseases
 Cell Transformation, Neoplastic Antibodies  >12 publications with MSH6 and Cell Transformation, Neoplastic
 Organ/Tissue Name  Pubmed Publications
 Blood Antibodies  >83 publications with MSH6 and Blood
 Brain Antibodies  >70 publications with MSH6 and Brain
 Skin Antibodies  >47 publications with MSH6 and Skin
 Intestine Antibodies  >45 publications with MSH6 and Intestine
 Stomach Antibodies  >39 publications with MSH6 and Stomach
 Lymph Node Antibodies  >28 publications with MSH6 and Lymph Node
 Liver Antibodies  >27 publications with MSH6 and Liver
 Kidney Antibodies  >25 publications with MSH6 and Kidney
 Bladder Antibodies  >21 publications with MSH6 and Bladder
 Prostate Antibodies  >20 publications with MSH6 and Prostate
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