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Mismatch repair endonuclease PMS2 (EC 3.1.-.-) (DNA mismatch repair protein PMS2) (PMS1 protein homolog 2)

 PMS2_HUMAN              Reviewed;         862 AA.
P54278; B2R610; Q52LH6; Q5FBW9; Q5FBX1; Q5FBX2; Q75MR2;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
11-JAN-2011, sequence version 2.
18-JUL-2018, entry version 194.
RecName: Full=Mismatch repair endonuclease PMS2 {ECO:0000305};
EC=3.1.-.-;
AltName: Full=DNA mismatch repair protein PMS2;
AltName: Full=PMS1 protein homolog 2;
Name=PMS2 {ECO:0000312|HGNC:HGNC:9122};
Synonyms=PMSL2 {ECO:0000312|HGNC:HGNC:9122};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS GLN-20 AND GLU-541.
TISSUE=Endometrial tumor;
PubMed=8072530; DOI=10.1038/371075a0;
Nicolaides N.C., Papadopoulos N., Liu B., Wei Y.-F., Carter K.C.,
Ruben S.M., Rosen C.A., Haseltine W.H., Fleischmann R.D., Fraser C.M.,
Adams M.D., Venter J.C., Dunlop M.G., Hamilton S.R., Petersen G.M.,
de la Chapelle A., Vogelstein B., Kinzler K.W.;
"Mutations of two PMS homologues in hereditary nonpolyposis colon
cancer.";
Nature 371:75-80(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4), AND VARIANT
GLU-541.
Tabata Y., Sameshima E., Hayashi A., Iida K., Mitsuyama M., Kanai S.,
Furuya T., Saito T.;
"PMS2 mRNA, nirs splice variants.";
Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS SER-470 AND
GLU-541.
Bronner C.E., Baker S.M., Morrison P.T., Warren G., Smith L.G.,
Lescoe M.K., Kane M.F., Earibino C., Lipford J., Lindblom A.,
Tannergaard P., Bollag R.J., Godwin A.R., Ward D.C., Nordenskjoeld M.,
Fishel R., Kolodner R.D., Liskay R.M.;
Submitted (OCT-1994) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS
SER-470 AND GLU-541.
TISSUE=Amygdala;
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).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12853948; DOI=10.1038/nature01782;
Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R.,
Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E.,
Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H.,
Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A.,
Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J.,
Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A.,
Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S.,
Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M.,
Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C.,
Latreille P., Miller N., Johnson D., Murray J., Woessner J.P.,
Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J.,
Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L.,
Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R.,
Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K.,
Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S.,
Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M.,
Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R.,
Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D.,
Waterston R.H., Wilson R.K.;
"The DNA sequence of human chromosome 7.";
Nature 424:157-164(2003).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS
GLU-541 AND ILE-622.
TISSUE=Brain;
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).
[7]
IDENTIFICATION OF PMS2 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).
[8]
INVOLVEMENT IN HNPCC4.
PubMed=15887124; DOI=10.1053/j.gastro.2005.04.008;
Worthley D.L., Walsh M.D., Barker M., Ruszkiewicz A., Bennett G.,
Phillips K., Suthers G.;
"Familial mutations in PMS2 can cause autosomal dominant hereditary
nonpolyposis colorectal cancer.";
Gastroenterology 128:1431-1436(2005).
[9]
FUNCTION AS AN ENDONUCLEASE.
PubMed=16873062; DOI=10.1016/j.cell.2006.05.039;
Kadyrov F.A., Dzantiev L., Constantin N., Modrich P.;
"Endonucleolytic function of MutLalpha in human mismatch repair.";
Cell 126:297-308(2006).
[10]
INVOLVEMENT IN HNPCC4.
PubMed=18178629; DOI=10.1136/jmg.2007.056150;
Clendenning M., Senter L., Hampel H., Robinson K.L., Sun S.,
Buchanan D., Walsh M.D., Nilbert M., Green J., Potter J., Lindblom A.,
de la Chapelle A.;
"A frame-shift mutation of PMS2 is a widespread cause of Lynch
syndrome.";
J. Med. Genet. 45:340-345(2008).
[11]
FUNCTION.
PubMed=18206974; DOI=10.1016/j.molcel.2007.10.030;
Sacho E.J., Kadyrov F.A., Modrich P., Kunkel T.A., Erie D.A.;
"Direct visualization of asymmetric adenine nucleotide-induced
conformational changes in MutL alpha.";
Mol. Cell 29:112-121(2008).
[12]
REVIEW.
PubMed=16188885; DOI=10.1074/jbc.M509701200;
Constantin N., Dzantiev L., Kadyrov F.A., Modrich P.;
"Human mismatch repair: reconstitution of a nick-directed
bidirectional reaction.";
J. Biol. Chem. 280:39752-39761(2005).
[13]
REVIEW.
PubMed=16873053; DOI=10.1016/j.cell.2006.07.003;
Jiricny J.;
"MutLalpha: at the cutting edge of mismatch repair.";
Cell 126:239-241(2006).
[14]
REVIEW.
PubMed=18157157; DOI=10.1038/cr.2007.115;
Li G.M.;
"Mechanisms and functions of DNA mismatch repair.";
Cell Res. 18:85-98(2008).
[15]
INTERACTION WITH MTMR15.
PubMed=20603073; DOI=10.1016/j.molcel.2010.06.023;
Smogorzewska A., Desetty R., Saito T.T., Schlabach M., Lach F.P.,
Sowa M.E., Clark A.B., Kunkel T.A., Harper J.W., Colaiacovo M.P.,
Elledge S.J.;
"A genetic screen identifies FAN1, a Fanconi anemia-associated
nuclease necessary for DNA interstrand crosslink repair.";
Mol. Cell 39:36-47(2010).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-597, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
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.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-573, 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).
[18]
X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 1-364.
PubMed=11574484; DOI=10.1093/emboj/20.19.5521;
Guarne A., Junop M.S., Yang W.;
"Structure and function of the N-terminal 40 kDa fragment of human
PMS2: a monomeric GHL ATPase.";
EMBO J. 20:5521-5531(2001).
[19]
INVOLVEMENT IN MMRCS.
PubMed=7661930; DOI=10.1056/NEJM199503303321302;
Hamilton S.R., Liu B., Parsons R.E., Papadopoulos N., Jen J.,
Powell S.M., Krush A.J., Berk T., Cohen Z., Tetu B., Burger P.C.,
Wood P.A., Taqi F., Booker S.V., Petersen G.M., Offerhaus G.J.A.,
Tersmette A.C., Giardiello F.M., Vogelstein B., Kinzler K.W.;
"The molecular basis of Turcot's syndrome.";
N. Engl. J. Med. 332:839-847(1995).
[20]
VARIANT MMRCS LYS-705.
PubMed=9419979; DOI=10.1038/sj.onc.1201668;
Miyaki M., Nishio J., Konishi M., Kikuchi-Yanoshita R., Tanaka K.,
Muraoka M., Nagato M., Chong J.-M., Koike M., Terada T., Kawahara Y.,
Fukutome A., Tomiyama J., Chuganji Y., Momoi M., Utsunomiya J.;
"Drastic genetic instability of tumors and normal tissues in Turcot
syndrome.";
Oncogene 15:2877-2881(1997).
[21]
VARIANTS HNPCC4 GLN-479 AND ILE-622, AND VARIANTS LYS-485; ALA-511 AND
SER-597.
PubMed=10480359; DOI=10.1007/s004399900064;
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.;
"Prevalence of germline mutations of hMLH1, hMSH2, hPMS1, hPMS2, and
hMSH6 genes in 75 French kindreds with nonpolyposis colorectal
cancer.";
Hum. Genet. 105:79-85(1999).
[22]
CHARACTERIZATION OF VARIANT HNPCC4 ILE-622, AND CHARACTERIZATION OF
VARIANT SER-597.
PubMed=11793469; DOI=10.1002/humu.10040;
Yuan Z.Q., Gottlieb B., Beitel L.K., Wong N., Gordon P.H., Wang Q.,
Puisieux A., Foulkes W.D., Trifiro M.;
"Polymorphisms and HNPCC: PMS2-MLH1 protein interactions diminished by
single nucleotide polymorphisms.";
Hum. Mutat. 19:108-113(2002).
[23]
INVOLVEMENT IN MMRCS.
PubMed=15077197; DOI=10.1086/420796;
De Vos M., Hayward B.E., Picton S., Sheridan E., Bonthron D.T.;
"Novel PMS2 pseudogenes can conceal recessive mutations causing a
distinctive childhood cancer syndrome.";
Am. J. Hum. Genet. 74:954-964(2004).
[24]
VARIANTS HNPCC4 ILE-585 AND ILE-622, AND VARIANTS VAL-18; GLN-20;
SER-470; LYS-485; GLU-541; SER-597 AND ALA-857.
PubMed=16472587; DOI=10.1053/j.gastro.2005.10.052;
Hendriks Y.M., Jagmohan-Changur S., van der Klift H.M., Morreau H.,
van Puijenbroek M., Tops C., van Os T., Wagner A., Ausems M.G.,
Gomez E., Breuning M.H., Broecker-Vriends A.H., Vasen H.F.,
Wijnen J.T.;
"Heterozygous mutations in PMS2 cause hereditary nonpolyposis
colorectal carcinoma (Lynch syndrome).";
Gastroenterology 130:312-322(2006).
[25]
VARIANTS HNPCC4 THR-182 AND ARG-797, AND VARIANTS VAL-18 AND LEU-563.
PubMed=16619239; DOI=10.1002/humu.20318;
Clendenning M., Hampel H., LaJeunesse J., Lindblom A., Lockman J.,
Nilbert M., Senter L., Sotamaa K., de la Chapelle A.;
"Long-range PCR facilitates the identification of PMS2-specific
mutations.";
Hum. Mutat. 27:490-495(2006).
[26]
VARIANT MMRCS ILE-46.
PubMed=17557300; DOI=10.1002/humu.20569;
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.;
"Novel biallelic mutations in MSH6 and PMS2 genes: gene conversion as
a likely cause of PMS2 gene inactivation.";
Hum. Mutat. 28:1084-1090(2007).
[27]
VARIANTS HNPCC4 ASN-46; ILE-46; PRO-205; ILE-622; ALA-663; LYS-705;
ASP-750 AND TYR-843, AND VARIANT LEU-563.
PubMed=18602922; DOI=10.1053/j.gastro.2008.04.026;
Senter L., Clendenning M., Sotamaa K., Hampel H., Green J.,
Potter J.D., Lindblom A., Lagerstedt K., Thibodeau S.N., Lindor N.M.,
Young J., Winship I., Dowty J.G., White D.M., Hopper J.L.,
Baglietto L., Jenkins M.A., de la Chapelle A.;
"The clinical phenotype of Lynch syndrome due to germ-line PMS2
mutations.";
Gastroenterology 135:419-428(2008).
[28]
VARIANT HNPCC4 GLU-207.
PubMed=19479271; DOI=10.1007/s00384-009-0731-1;
Montazer Haghighi M., Radpour R., Aghajani K., Zali N., Molaei M.,
Zali M.R.;
"Four novel germline mutations in the MLH1 and PMS2 mismatch repair
genes in patients with hereditary nonpolyposis colorectal cancer.";
Int. J. Colorectal Dis. 24:885-893(2009).
[29]
VARIANTS THR-423; MET-511 AND PRO-511.
PubMed=20186689; DOI=10.1002/humu.21223;
Ganster C., Wernstedt A., Kehrer-Sawatzki H., Messiaen L., Schmidt K.,
Rahner N., Heinimann K., Fonatsch C., Zschocke J., Wimmer K.;
"Functional PMS2 hybrid alleles containing a pseudogene-specific
missense variant trace back to a single ancient intrachromosomal
recombination event.";
Hum. Mutat. 31:552-560(2010).
[30]
CHARACTERIZATION OF VARIANTS VAL-18; GLN-20; ALA-41; GLU-60; THR-423;
LYS-485; ALA-511; MET-511; GLU-541; LEU-563; ILE-571; SER-597 AND
ALA-857, CHARACTERIZATION OF VARIANTS HNPCC4 ASN-46; ILE-46; PRO-205;
GLU-207; VAL-263; GLN-479; ILE-622; ALA-663; LYS-705; ASP-750; ARG-797
AND TYR-843, AND MUTAGENESIS OF GLU-41 AND TYR-519.
PubMed=24027009; DOI=10.1002/humu.22426;
Drost M., Koppejan H., de Wind N.;
"Inactivation of DNA mismatch repair by variants of uncertain
significance in the PMS2 gene.";
Hum. Mutat. 34:1477-1480(2013).
[31]
VARIANT HNPCC4 ILE-46, VARIANTS GLN-20; SER-470; SER-597 AND SER-775,
CHARACTERIZATION OF VARIANT HNPCC4 ILE-46, CHARACTERIZATION OF
VARIANTS GLN-20 AND SER-470, MUTAGENESIS OF ASP-70, FUNCTION, AND
SUBCELLULAR LOCATION.
PubMed=23709753; DOI=10.1136/jmedgenet-2012-101511;
Borras E., Pineda M., Cadinanos J., Del Valle J., Brieger A.,
Hinrichsen I., Cabanillas R., Navarro M., Brunet J., Sanjuan X.,
Musulen E., van der Klift H., Lazaro C., Plotz G., Blanco I.,
Capella G.;
"Refining the role of PMS2 in Lynch syndrome: germline mutational
analysis improved by comprehensive assessment of variants.";
J. Med. Genet. 50:552-563(2013).
[32]
VARIANTS MMRCS ILE-46; THR-66; TRP-107; GLY-115; PRO-205; VAL-263;
LYS-307; SER-437; GLN-479; VAL-488; GLN-504; ILE-585 AND LEU-815,
CHARACTERIZATION OF VARIANTS MMRCS ILE-46; THR-66; TRP-107; GLY-115;
LYS-307; SER-437; VAL-488; GLN-504 AND LEU-815, VARIANTS VAL-18;
GLU-60; SER-470; LEU-563; ILE-571 AND SER-775, AND CHARACTERIZATION OF
VARIANTS SER-470 AND SER-775.
PubMed=27435373; DOI=10.1002/humu.23052;
van der Klift H.M., Mensenkamp A.R., Drost M., Bik E.C., Vos Y.J.,
Gille H.J., Redeker B.E., Tiersma Y., Zonneveld J.B., Garcia E.G.,
Letteboer T.G., Olderode-Berends M.J., van Hest L.P., van Os T.A.,
Verhoef S., Wagner A., van Asperen C.J., Ten Broeke S.W., Hes F.J.,
de Wind N., Nielsen M., Devilee P., Ligtenberg M.J., Wijnen J.T.,
Tops C.M.;
"Comprehensive mutation analysis of PMS2 in a large cohort of probands
suspected of lynch syndrome or constitutional mismatch repair
deficiency syndrome.";
Hum. Mutat. 37:1162-1179(2016).
[33]
VARIANTS ARG-36; GLU-475; HIS-699; ASN-792 AND MET-853, AND
CHARACTERIZATION OF VARIANTS ARG-36; GLU-475; HIS-699; ASN-792 AND
MET-853.
PubMed=28494185; DOI=10.1080/15384047.2017.1326439;
Arora S., Huwe P.J., Sikder R., Shah M., Browne A.J., Lesh R.,
Nicolas E., Deshpande S., Hall M.J., Dunbrack R.L. Jr., Golemis E.A.;
"Functional analysis of rare variants in mismatch repair proteins
augments results from computation-based predictive methods.";
Cancer Biol. Ther. 18:519-533(2017).
-!- FUNCTION: Component of the post-replicative DNA mismatch repair
system (MMR). Heterodimerizes with MLH1 to form MutL alpha. DNA
repair is initiated by MutS alpha (MSH2-MSH6) or MutS beta (MSH2-
MSH3) binding to a dsDNA mismatch, then MutL alpha is recruited to
the heteroduplex. Assembly of the MutL-MutS-heteroduplex ternary
complex in presence of RFC and PCNA is sufficient to activate
endonuclease activity of PMS2. It introduces single-strand breaks
near the mismatch and thus generates new entry points for the
exonuclease EXO1 to degrade the strand containing the mismatch.
DNA methylation would prevent cleavage and therefore assure that
only the newly mutated DNA strand is going to be corrected. MutL
alpha (MLH1-PMS2) interacts physically with the clamp loader
subunits of DNA polymerase III, suggesting that it may play a role
to recruit the DNA polymerase III to the site of the MMR. Also
implicated in DNA damage signaling, a process which induces cell
cycle arrest and can lead to apoptosis in case of major DNA
damages. {ECO:0000269|PubMed:16873062,
ECO:0000269|PubMed:18206974, ECO:0000269|PubMed:23709753}.
-!- SUBUNIT: Heterodimer of PMS2 and MLH1 (MutL alpha). Forms a
ternary complex with MutS alpha (MSH2-MSH6) or MutS beta (MSH2-
MSH3). 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 MTMR15/FAN1.
{ECO:0000269|PubMed:20603073}.
-!- INTERACTION:
P40692:MLH1; NbExp=5; IntAct=EBI-1162561, EBI-744248;
O15350:TP73; NbExp=3; IntAct=EBI-15726984, EBI-389606;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23709753}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1;
IsoId=P54278-1; Sequence=Displayed;
Name=2;
IsoId=P54278-2; Sequence=VSP_029386;
Note=No experimental confirmation available.;
Name=3;
IsoId=P54278-3; Sequence=VSP_029387, VSP_029388;
Note=No experimental confirmation available.;
Name=4;
IsoId=P54278-4; Sequence=VSP_029384, VSP_029385;
Note=No experimental confirmation available.;
-!- DISEASE: Hereditary non-polyposis colorectal cancer 4 (HNPCC4)
[MIM:614337]: 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:10480359, ECO:0000269|PubMed:11793469,
ECO:0000269|PubMed:15887124, ECO:0000269|PubMed:16472587,
ECO:0000269|PubMed:16619239, ECO:0000269|PubMed:18178629,
ECO:0000269|PubMed:18602922, ECO:0000269|PubMed:19479271,
ECO:0000269|PubMed:23709753, ECO:0000269|PubMed:24027009}.
Note=The disease is caused by mutations 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:15077197, ECO:0000269|PubMed:17557300,
ECO:0000269|PubMed:27435373, ECO:0000269|PubMed:7661930,
ECO:0000269|PubMed:9419979}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the DNA mismatch repair MutL/HexB family.
{ECO:0000305}.
-!- WEB RESOURCE: Name=Hereditary non-polyposis colorectal cancer db;
URL="http://www.nfdht.nl/";
-----------------------------------------------------------------------
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EMBL; U13696; AAA63923.1; -; Genomic_DNA.
EMBL; AB103082; BAD89425.1; -; mRNA.
EMBL; AB103083; BAD89426.1; -; mRNA.
EMBL; AB103085; BAD89428.1; -; mRNA.
EMBL; U14658; AAA50390.1; -; mRNA.
EMBL; AK312390; BAG35307.1; -; mRNA.
EMBL; AC005995; AAS00390.1; -; Genomic_DNA.
EMBL; BC093921; AAH93921.1; -; mRNA.
CCDS; CCDS5343.1; -. [P54278-1]
PIR; S47598; S47598.
RefSeq; NP_000526.2; NM_000535.6. [P54278-1]
RefSeq; NP_001308932.1; NM_001322003.1.
RefSeq; NP_001308933.1; NM_001322004.1.
RefSeq; NP_001308934.1; NM_001322005.1.
RefSeq; NP_001308935.1; NM_001322006.1.
RefSeq; NP_001308936.1; NM_001322007.1.
RefSeq; NP_001308937.1; NM_001322008.1.
RefSeq; NP_001308938.1; NM_001322009.1.
RefSeq; NP_001308939.1; NM_001322010.1.
RefSeq; NP_001308940.1; NM_001322011.1.
RefSeq; NP_001308941.1; NM_001322012.1.
RefSeq; NP_001308942.1; NM_001322013.1.
RefSeq; NP_001308943.1; NM_001322014.1.
RefSeq; NP_001308944.1; NM_001322015.1.
RefSeq; XP_016885888.1; XM_017030399.1.
UniGene; Hs.632637; -.
UniGene; Hs.715590; -.
PDB; 1EA6; X-ray; 2.70 A; A/B=1-364.
PDB; 1H7S; X-ray; 1.95 A; A/B=1-365.
PDB; 1H7U; X-ray; 2.70 A; A/B=1-365.
PDB; 5U5R; X-ray; 2.10 A; B=573-583.
PDBsum; 1EA6; -.
PDBsum; 1H7S; -.
PDBsum; 1H7U; -.
PDBsum; 5U5R; -.
ProteinModelPortal; P54278; -.
SMR; P54278; -.
BioGrid; 111404; 55.
CORUM; P54278; -.
DIP; DIP-46295N; -.
IntAct; P54278; 26.
MINT; P54278; -.
STRING; 9606.ENSP00000265849; -.
DrugBank; DB02930; Phosphothiophosphoric Acid-Adenylate Ester.
iPTMnet; P54278; -.
PhosphoSitePlus; P54278; -.
BioMuta; PMS2; -.
DMDM; 317373266; -.
SWISS-2DPAGE; P54278; -.
EPD; P54278; -.
MaxQB; P54278; -.
PaxDb; P54278; -.
PeptideAtlas; P54278; -.
PRIDE; P54278; -.
ProteomicsDB; 56669; -.
ProteomicsDB; 56670; -. [P54278-2]
ProteomicsDB; 56671; -. [P54278-3]
ProteomicsDB; 56672; -. [P54278-4]
Ensembl; ENST00000265849; ENSP00000265849; ENSG00000122512. [P54278-1]
Ensembl; ENST00000382321; ENSP00000371758; ENSG00000122512. [P54278-2]
Ensembl; ENST00000643595; ENSP00000494497; ENSG00000122512. [P54278-4]
GeneID; 5395; -.
KEGG; hsa:107984056; -.
KEGG; hsa:5395; -.
UCSC; uc003spl.4; human. [P54278-1]
CTD; 5395; -.
DisGeNET; 107984056; -.
DisGeNET; 5395; -.
EuPathDB; HostDB:ENSG00000122512.14; -.
GeneCards; PMS2; -.
GeneReviews; PMS2; -.
HGNC; HGNC:9122; PMS2.
HPA; CAB010235; -.
HPA; HPA044400; -.
HPA; HPA066490; -.
HPA; HPA070310; -.
MalaCards; PMS2; -.
MIM; 276300; phenotype.
MIM; 600259; gene.
MIM; 614337; phenotype.
neXtProt; NX_P54278; -.
OpenTargets; ENSG00000122512; -.
Orphanet; 252202; Constitutional mismatch repair deficiency syndrome.
Orphanet; 144; Hereditary nonpolyposis colon cancer.
Orphanet; 99817; Non-polyposis Turcot syndrome.
PharmGKB; PA33448; -.
eggNOG; KOG1978; Eukaryota.
eggNOG; COG0323; LUCA.
GeneTree; ENSGT00530000063289; -.
HOGENOM; HOG000165474; -.
HOVERGEN; HBG008219; -.
InParanoid; P54278; -.
KO; K10858; -.
OMA; FFFINQR; -.
OrthoDB; EOG091G07MF; -.
PhylomeDB; P54278; -.
TreeFam; TF300711; -.
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-5545483; Defective Mismatch Repair Associated With MLH1.
Reactome; R-HSA-5632987; Defective Mismatch Repair Associated With PMS2.
Reactome; R-HSA-6796648; TP53 Regulates Transcription of DNA Repair Genes.
SIGNOR; P54278; -.
ChiTaRS; PMS2; human.
EvolutionaryTrace; P54278; -.
GeneWiki; PMS2; -.
GenomeRNAi; 5395; -.
PRO; PR:P54278; -.
Proteomes; UP000005640; Chromosome 7.
Bgee; ENSG00000122512; -.
CleanEx; HS_PMS2; -.
ExpressionAtlas; P54278; baseline and differential.
Genevisible; P54278; HS.
GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; IDA:HPA.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0015630; C:microtubule cytoskeleton; IDA:HPA.
GO; GO:0032389; C:MutLalpha complex; IBA:GO_Central.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:HPA.
GO; GO:0005524; F:ATP binding; IEA:InterPro.
GO; GO:0016887; F:ATPase activity; IBA:GO_Central.
GO; GO:0003677; F:DNA binding; IDA:HGNC.
GO; GO:0004519; F:endonuclease activity; TAS:Reactome.
GO; GO:0032138; F:single base insertion or deletion binding; IDA:HGNC.
GO; GO:0006298; P:mismatch repair; IDA:UniProtKB.
GO; GO:0042493; P:response to drug; IEA:Ensembl.
GO; GO:0016446; P:somatic hypermutation of immunoglobulin genes; IBA:GO_Central.
CDD; cd00075; HATPase_c; 1.
Gene3D; 3.30.230.10; -; 1.
Gene3D; 3.30.565.10; -; 1.
InterPro; IPR014762; DNA_mismatch_repair_CS.
InterPro; IPR002099; DNA_mismatch_repair_N.
InterPro; IPR013507; DNA_mismatch_S5_2-like.
InterPro; IPR003594; HATPase_C.
InterPro; IPR036890; HATPase_C_sf.
InterPro; IPR038973; MutL/Mlh/Pms.
InterPro; IPR014790; MutL_C.
InterPro; IPR037198; MutL_C_sf.
InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
PANTHER; PTHR10073; PTHR10073; 1.
Pfam; PF01119; DNA_mis_repair; 1.
Pfam; PF08676; MutL_C; 1.
SMART; SM01340; DNA_mis_repair; 1.
SMART; SM00853; MutL_C; 1.
SUPFAM; SSF118116; SSF118116; 1.
SUPFAM; SSF54211; SSF54211; 1.
SUPFAM; SSF55874; SSF55874; 1.
TIGRFAMs; TIGR00585; mutl; 1.
PROSITE; PS00058; DNA_MISMATCH_REPAIR_1; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome;
Disease mutation; DNA damage; DNA repair; Endonuclease;
Hereditary nonpolyposis colorectal cancer; Hydrolase; Nuclease;
Nucleus; Phosphoprotein; Polymorphism; Reference proteome;
Tumor suppressor.
CHAIN 1 862 Mismatch repair endonuclease PMS2.
/FTId=PRO_0000178005.
MOD_RES 573 573 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 597 597 Phosphothreonine.
{ECO:0000244|PubMed:20068231}.
VAR_SEQ 180 183 EYAK -> QASV (in isoform 4).
{ECO:0000303|Ref.2}.
/FTId=VSP_029384.
VAR_SEQ 184 862 Missing (in isoform 4).
{ECO:0000303|Ref.2}.
/FTId=VSP_029385.
VAR_SEQ 269 669 Missing (in isoform 2).
{ECO:0000303|Ref.2}.
/FTId=VSP_029386.
VAR_SEQ 560 572 CKFRVLPQPTNLA -> LKTGPSDPRTSMN (in
isoform 3). {ECO:0000303|Ref.2}.
/FTId=VSP_029387.
VAR_SEQ 573 862 Missing (in isoform 3).
{ECO:0000303|Ref.2}.
/FTId=VSP_029388.
VARIANT 18 18 I -> V (polymorphism; normal DNA mismatch
repair activity; dbSNP:rs63750123).
{ECO:0000269|PubMed:16472587,
ECO:0000269|PubMed:16619239,
ECO:0000269|PubMed:24027009,
ECO:0000269|PubMed:27435373}.
/FTId=VAR_078517.
VARIANT 20 20 R -> Q (polymorphism; no effect on
protein abundance; no effect on
subcellular localization; normal DNA
mismatch repair activity;
dbSNP:rs10254120).
{ECO:0000269|PubMed:16472587,
ECO:0000269|PubMed:23709753,
ECO:0000269|PubMed:24027009,
ECO:0000269|PubMed:8072530}.
/FTId=VAR_004469.
VARIANT 36 36 S -> R (polymorphism; no effect on
protein levels; dbSNP:rs587781918).
{ECO:0000269|PubMed:28494185}.
/FTId=VAR_079817.
VARIANT 46 46 S -> I (in MMRCS and HNPCC4; strongly
decreased DNA mismatch repair activity;
no effect on protein abundance; no effect
on subcellular localization;
dbSNP:rs121434629).
{ECO:0000269|PubMed:17557300,
ECO:0000269|PubMed:18602922,
ECO:0000269|PubMed:23709753,
ECO:0000269|PubMed:24027009,
ECO:0000269|PubMed:27435373}.
/FTId=VAR_066838.
VARIANT 46 46 S -> N (in HNPCC4; strongly decreased DNA
mismatch repair activity;
dbSNP:rs121434629).
{ECO:0000269|PubMed:18602922,
ECO:0000269|PubMed:24027009}.
/FTId=VAR_078518.
VARIANT 60 60 D -> E (polymorphism; normal DNA mismatch
repair activity; dbSNP:rs200313585).
{ECO:0000269|PubMed:24027009,
ECO:0000269|PubMed:27435373}.
/FTId=VAR_078519.
VARIANT 66 66 I -> T (in MMRCS; unknown pathological
significance; normal DNA mismatch repair
activity; dbSNP:rs769554577).
{ECO:0000269|PubMed:27435373}.
/FTId=VAR_078520.
VARIANT 107 107 R -> W (in MMRCS; decreased DNA mismatch
repair activity; dbSNP:rs188006077).
{ECO:0000269|PubMed:27435373}.
/FTId=VAR_078521.
VARIANT 115 115 C -> G (in MMRCS; decreased DNA mismatch
repair activity).
{ECO:0000269|PubMed:27435373}.
/FTId=VAR_078522.
VARIANT 182 182 A -> T (in HNPCC4; unknown pathological
significance; dbSNP:rs587779341).
{ECO:0000269|PubMed:16619239}.
/FTId=VAR_078523.
VARIANT 205 205 Q -> P (in MMRCS and HNPCC4; unknown
pathological significance; normal DNA
mismatch repair activity;
dbSNP:rs587779342).
{ECO:0000269|PubMed:18602922,
ECO:0000269|PubMed:24027009,
ECO:0000269|PubMed:27435373}.
/FTId=VAR_078524.
VARIANT 207 207 G -> E (in HNPCC4; unknown pathological
significance; normal DNA mismatch repair
activity; dbSNP:rs374704824).
{ECO:0000269|PubMed:19479271,
ECO:0000269|PubMed:24027009}.
/FTId=VAR_078525.
VARIANT 263 263 L -> V (in MMRCS and HNPCC4; unknown
pathological significance; normal DNA
mismatch repair activity;
dbSNP:rs587779345).
{ECO:0000269|PubMed:24027009,
ECO:0000269|PubMed:27435373}.
/FTId=VAR_078526.
VARIANT 277 277 T -> K (in dbSNP:rs1805322).
/FTId=VAR_016133.
VARIANT 307 307 N -> K (in MMRCS; unknown pathological
significance; decreased DNA mismatch
repair activity; dbSNP:rs587779346).
{ECO:0000269|PubMed:27435373}.
/FTId=VAR_078527.
VARIANT 423 423 A -> T (polymorphism; normal DNA mismatch
repair activity; dbSNP:rs587778619).
{ECO:0000269|PubMed:20186689,
ECO:0000269|PubMed:24027009}.
/FTId=VAR_079012.
VARIANT 437 437 P -> S (in MMRCS; unknown pathological
significance; normal DNA mismatch repair
activity; dbSNP:rs200726484).
{ECO:0000269|PubMed:27435373}.
/FTId=VAR_078528.
VARIANT 470 470 P -> S (polymorphism; no effect on
protein abundance; no effect on
subcellular localization; normal DNA
mismatch repair activity;
dbSNP:rs1805321).
{ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:16472587,
ECO:0000269|PubMed:23709753,
ECO:0000269|PubMed:27435373,
ECO:0000269|Ref.3}.
/FTId=VAR_016134.
VARIANT 475 475 V -> E (polymorphism; no effect on
protein levels; dbSNP:rs587781827).
{ECO:0000269|PubMed:28494185}.
/FTId=VAR_079818.
VARIANT 479 479 H -> Q (in MMRCS and HNPCC4; unknown
pathological significance; normal DNA
mismatch repair activity;
dbSNP:rs63750685).
{ECO:0000269|PubMed:10480359,
ECO:0000269|PubMed:24027009,
ECO:0000269|PubMed:27435373}.
/FTId=VAR_012969.
VARIANT 485 485 T -> K (polymorphism; normal DNA mismatch
repair activity; dbSNP:rs1805323).
{ECO:0000269|PubMed:10480359,
ECO:0000269|PubMed:16472587,
ECO:0000269|PubMed:24027009}.
/FTId=VAR_012970.
VARIANT 488 488 A -> V (in MMRCS; unknown pathological
significance; normal DNA mismatch repair
activity; dbSNP:rs587779328).
{ECO:0000269|PubMed:27435373}.
/FTId=VAR_078529.
VARIANT 504 504 E -> Q (in MMRCS; unknown pathological
significance; normal DNA mismatch repair
activity; dbSNP:rs368516768).
{ECO:0000269|PubMed:27435373}.
/FTId=VAR_078530.
VARIANT 511 511 T -> A (polymorphism; normal DNA mismatch
repair activity; dbSNP:rs2228007).
{ECO:0000269|PubMed:10480359,
ECO:0000269|PubMed:24027009}.
/FTId=VAR_012971.
VARIANT 511 511 T -> M (polymorphism; normal DNA mismatch
repair activity; dbSNP:rs74902811).
{ECO:0000269|PubMed:20186689,
ECO:0000269|PubMed:24027009}.
/FTId=VAR_079013.
VARIANT 511 511 T -> P (in dbSNP:rs2228007).
{ECO:0000269|PubMed:20186689}.
/FTId=VAR_079014.
VARIANT 541 541 K -> E (polymorphism; normal DNA mismatch
repair activity; dbSNP:rs2228006).
{ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:16472587,
ECO:0000269|PubMed:24027009,
ECO:0000269|PubMed:8072530,
ECO:0000269|Ref.2, ECO:0000269|Ref.3}.
/FTId=VAR_024541.
VARIANT 563 563 R -> L (polymorphism; normal DNA mismatch
repair activity; dbSNP:rs63750668).
{ECO:0000269|PubMed:16619239,
ECO:0000269|PubMed:18602922,
ECO:0000269|PubMed:24027009,
ECO:0000269|PubMed:27435373}.
/FTId=VAR_078531.
VARIANT 571 571 L -> I (polymorphism; normal DNA mismatch
repair activity; dbSNP:rs63750055).
{ECO:0000269|PubMed:24027009,
ECO:0000269|PubMed:27435373}.
/FTId=VAR_078532.
VARIANT 585 585 L -> I (in MMRCS and HNPCC4; unknown
pathological significance; normal DNA
mismatch repair activity;
dbSNP:rs63750947).
{ECO:0000269|PubMed:16472587,
ECO:0000269|PubMed:24027009,
ECO:0000269|PubMed:27435373}.
/FTId=VAR_078533.
VARIANT 597 597 T -> S (polymorphism; normal DNA mismatch
repair activity; significantly reduced
interaction with MLH1; dbSNP:rs1805318).
{ECO:0000269|PubMed:10480359,
ECO:0000269|PubMed:11793469,
ECO:0000269|PubMed:16472587,
ECO:0000269|PubMed:23709753,
ECO:0000269|PubMed:24027009}.
/FTId=VAR_012972.
VARIANT 622 622 M -> I (in HNPCC4; unknown pathological
significance; significantly reduced
interaction with MLH1; normal DNA
mismatch repair activity;
dbSNP:rs1805324).
{ECO:0000269|PubMed:10480359,
ECO:0000269|PubMed:11793469,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:16472587,
ECO:0000269|PubMed:18602922,
ECO:0000269|PubMed:24027009}.
/FTId=VAR_012973.
VARIANT 663 663 E -> A (in HNPCC4; unknown pathological
significance; normal DNA mismatch repair
activity; dbSNP:rs587779332).
{ECO:0000269|PubMed:18602922,
ECO:0000269|PubMed:24027009}.
/FTId=VAR_078534.
VARIANT 699 699 D -> H (polymorphism; no effect on
protein levels; dbSNP:rs587781317).
{ECO:0000269|PubMed:28494185}.
/FTId=VAR_079819.
VARIANT 705 705 E -> K (in MMRCS and HNPCC4; decreases
DNA mismatch repair activity;
dbSNP:rs267608161).
{ECO:0000269|PubMed:18602922,
ECO:0000269|PubMed:24027009,
ECO:0000269|PubMed:9419979}.
/FTId=VAR_012974.
VARIANT 750 750 G -> D (in HNPCC4; unknown pathological
significance; decreased DNA mismatch
repair activity; dbSNP:rs587779337).
{ECO:0000269|PubMed:18602922,
ECO:0000269|PubMed:24027009}.
/FTId=VAR_078535.
VARIANT 775 775 N -> S (polymorphism; normal DNA mismatch
repair activity; dbSNP:rs17420802).
{ECO:0000269|PubMed:23709753,
ECO:0000269|PubMed:27435373}.
/FTId=VAR_016135.
VARIANT 792 792 D -> N (polymorphism; no effect on
protein levels; dbSNP:rs587781265).
{ECO:0000269|PubMed:28494185}.
/FTId=VAR_079820.
VARIANT 797 797 M -> R (in HNPCC4; unknown pathological
significance; normal DNA mismatch repair
activity; dbSNP:rs267608152).
{ECO:0000269|PubMed:16619239,
ECO:0000269|PubMed:24027009}.
/FTId=VAR_078536.
VARIANT 815 815 S -> L (in MMRCS; decreased DNA mismatch
repair activity; dbSNP:rs587779338).
{ECO:0000269|PubMed:27435373}.
/FTId=VAR_078537.
VARIANT 843 843 C -> Y (in HNPCC4; decreased DNA mismatch
repair activity; dbSNP:rs267608174).
{ECO:0000269|PubMed:18602922,
ECO:0000269|PubMed:24027009}.
/FTId=VAR_078538.
VARIANT 853 853 I -> M (polymorphism; no effect on
protein levels; dbSNP:rs371673459).
{ECO:0000269|PubMed:28494185}.
/FTId=VAR_079821.
VARIANT 857 857 G -> A (polymorphism; normal DNA mismatch
repair activity; dbSNP:rs1802683).
{ECO:0000269|PubMed:16472587,
ECO:0000269|PubMed:24027009}.
/FTId=VAR_078539.
MUTAGEN 41 41 E->A: Decreased DNA mismatch repair
activity. {ECO:0000269|PubMed:24027009}.
MUTAGEN 70 70 D->N: No effect on protein abundance, no
effect on subcellular localization and
loss of DNA mismatch repair activity.
{ECO:0000269|PubMed:23709753}.
MUTAGEN 519 519 Y->C: No effect on DNA mismatch repair
activity. {ECO:0000269|PubMed:24027009}.
STRAND 30 32 {ECO:0000244|PDB:1H7S}.
HELIX 35 48 {ECO:0000244|PDB:1H7S}.
STRAND 52 59 {ECO:0000244|PDB:1H7S}.
HELIX 60 62 {ECO:0000244|PDB:1H7S}.
STRAND 64 70 {ECO:0000244|PDB:1H7S}.
HELIX 77 79 {ECO:0000244|PDB:1H7S}.
HELIX 81 84 {ECO:0000244|PDB:1H7S}.
STRAND 101 109 {ECO:0000244|PDB:1H7S}.
HELIX 110 117 {ECO:0000244|PDB:1H7S}.
STRAND 118 125 {ECO:0000244|PDB:1H7S}.
STRAND 133 137 {ECO:0000244|PDB:1H7S}.
STRAND 143 148 {ECO:0000244|PDB:1H7S}.
STRAND 153 161 {ECO:0000244|PDB:1H7S}.
TURN 162 165 {ECO:0000244|PDB:1H7S}.
HELIX 167 175 {ECO:0000244|PDB:1H7S}.
HELIX 177 194 {ECO:0000244|PDB:1H7S}.
STRAND 199 205 {ECO:0000244|PDB:1H7S}.
STRAND 211 216 {ECO:0000244|PDB:1H7S}.
HELIX 223 231 {ECO:0000244|PDB:1H7S}.
HELIX 233 237 {ECO:0000244|PDB:1H7S}.
STRAND 239 241 {ECO:0000244|PDB:1H7S}.
HELIX 249 255 {ECO:0000244|PDB:1H7S}.
TURN 259 263 {ECO:0000244|PDB:1H7S}.
STRAND 268 274 {ECO:0000244|PDB:1H7S}.
TURN 278 280 {ECO:0000244|PDB:1H7S}.
STRAND 281 285 {ECO:0000244|PDB:1H7S}.
STRAND 288 292 {ECO:0000244|PDB:1H7S}.
STRAND 295 297 {ECO:0000244|PDB:1H7S}.
HELIX 300 311 {ECO:0000244|PDB:1H7S}.
STRAND 321 326 {ECO:0000244|PDB:1H7S}.
HELIX 329 331 {ECO:0000244|PDB:1H7S}.
STRAND 332 334 {ECO:0000244|PDB:1H7S}.
STRAND 343 345 {ECO:0000244|PDB:1H7S}.
HELIX 348 363 {ECO:0000244|PDB:1H7S}.
SEQUENCE 862 AA; 95797 MW; B1B9547280ECAF9A CRC64;
MERAESSSTE PAKAIKPIDR KSVHQICSGQ VVLSLSTAVK ELVENSLDAG ATNIDLKLKD
YGVDLIEVSD NGCGVEEENF EGLTLKHHTS KIQEFADLTQ VETFGFRGEA LSSLCALSDV
TISTCHASAK VGTRLMFDHN GKIIQKTPYP RPRGTTVSVQ QLFSTLPVRH KEFQRNIKKE
YAKMVQVLHA YCIISAGIRV SCTNQLGQGK RQPVVCTGGS PSIKENIGSV FGQKQLQSLI
PFVQLPPSDS VCEEYGLSCS DALHNLFYIS GFISQCTHGV GRSSTDRQFF FINRRPCDPA
KVCRLVNEVY HMYNRHQYPF VVLNISVDSE CVDINVTPDK RQILLQEEKL LLAVLKTSLI
GMFDSDVNKL NVSQQPLLDV EGNLIKMHAA DLEKPMVEKQ DQSPSLRTGE EKKDVSISRL
REAFSLRHTT ENKPHSPKTP EPRRSPLGQK RGMLSSSTSG AISDKGVLRP QKEAVSSSHG
PSDPTDRAEV EKDSGHGSTS VDSEGFSIPD TGSHCSSEYA ASSPGDRGSQ EHVDSQEKAP
KTDDSFSDVD CHSNQEDTGC KFRVLPQPTN LATPNTKRFK KEEILSSSDI CQKLVNTQDM
SASQVDVAVK INKKVVPLDF SMSSLAKRIK QLHHEAQQSE GEQNYRKFRA KICPGENQAA
EDELRKEISK TMFAEMEIIG QFNLGFIITK LNEDIFIVDQ HATDEKYNFE MLQQHTVLQG
QRLIAPQTLN LTAVNEAVLI ENLEIFRKNG FDFVIDENAP VTERAKLISL PTSKNWTFGP
QDVDELIFML SDSPGVMCRP SRVKQMFASR ACRKSVMIGT ALNTSEMKKL ITHMGEMDHP
WNCPHGRPTM RHIANLGVIS QN


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