Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P54278 (PMS2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 152. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Mismatch repair endonuclease PMS2

EC=3.1.-.-
Alternative name(s):
DNA mismatch repair protein PMS2
PMS1 protein homolog 2
Gene names
Name:PMS2
Synonyms:PMSL2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length862 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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-MSH6) 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. Ref.9 Ref.11

Subunit structure

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. Ref.15

Subcellular location

Nucleus.

Involvement in 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.8 Ref.10

Mismatch repair cancer syndrome (MMRCS) [MIM:276300]: Autosomal dominant disorder characterized by malignant tumors of the brain associated with multiple colorectal adenomas. Skin features include sebaceous cysts, hyperpigmented and cafe au lait spots.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.18 Ref.19 Ref.22 Ref.23

Sequence similarities

Belongs to the DNA mismatch repair MutL/HexB family.

Ontologies

Keywords
   Biological processDNA damage
DNA repair
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
Hereditary nonpolyposis colorectal cancer
Tumor suppressor
   Molecular functionEndonuclease
Hydrolase
Nuclease
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processATP catabolic process

Inferred from Biological aspect of Ancestor. Source: GOC

mismatch repair

Inferred from direct assay PubMed 10871409. Source: HGNC

response to drug

Inferred from electronic annotation. Source: Ensembl

somatic hypermutation of immunoglobulin genes

Inferred from Biological aspect of Ancestor. Source: RefGenome

somatic recombination of immunoglobulin gene segments

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentMutLalpha complex

Inferred from Biological aspect of Ancestor. Source: RefGenome

cytoplasm

Inferred from direct assay. Source: HPA

microtubule cytoskeleton

Inferred from direct assay. Source: HPA

nucleus

Inferred by curator PubMed 10871409. Source: HGNC

   Molecular_functionATP binding

Inferred from electronic annotation. Source: InterPro

ATPase activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

DNA binding

Inferred from direct assay PubMed 10871409. Source: HGNC

endonuclease activity

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction Ref.15. Source: UniProtKB

single base insertion or deletion binding

Inferred from direct assay PubMed 10871409. Source: HGNC

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

MLH1P406924EBI-1162561,EBI-744248

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P54278-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P54278-2)

The sequence of this isoform differs from the canonical sequence as follows:
     269-669: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: P54278-3)

The sequence of this isoform differs from the canonical sequence as follows:
     560-572: CKFRVLPQPTNLA → LKTGPSDPRTSMN
     573-862: Missing.
Note: No experimental confirmation available.
Isoform 4 (identifier: P54278-4)

The sequence of this isoform differs from the canonical sequence as follows:
     180-183: EYAK → QASV
     184-862: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 862862Mismatch repair endonuclease PMS2
PRO_0000178005

Amino acid modifications

Modified residue5971Phosphothreonine Ref.16

Natural variations

Alternative sequence180 – 1834EYAK → QASV in isoform 4.
VSP_029384
Alternative sequence184 – 862679Missing in isoform 4.
VSP_029385
Alternative sequence269 – 669401Missing in isoform 2.
VSP_029386
Alternative sequence560 – 57213CKFRV…PTNLA → LKTGPSDPRTSMN in isoform 3.
VSP_029387
Alternative sequence573 – 862290Missing in isoform 3.
VSP_029388
Natural variant201R → Q. Ref.1
Corresponds to variant rs10254120 [ dbSNP | Ensembl ].
VAR_004469
Natural variant461S → I in MMRCS. Ref.23
VAR_066838
Natural variant2771T → K.
Corresponds to variant rs1805322 [ dbSNP | Ensembl ].
VAR_016133
Natural variant4701P → S. Ref.3 Ref.4
Corresponds to variant rs1805321 [ dbSNP | Ensembl ].
VAR_016134
Natural variant4791H → Q. Ref.20
VAR_012969
Natural variant4851T → K. Ref.20
Corresponds to variant rs1805323 [ dbSNP | Ensembl ].
VAR_012970
Natural variant5111T → A. Ref.20
Corresponds to variant rs2228007 [ dbSNP | Ensembl ].
VAR_012971
Natural variant5411K → E. Ref.1 Ref.2 Ref.3 Ref.4 Ref.6
Corresponds to variant rs2228006 [ dbSNP | Ensembl ].
VAR_024541
Natural variant5971T → S May be associated with increased susceptibility to colorectal cancer; significantly reduced interaction with MLH1. Ref.20 Ref.21
Corresponds to variant rs1805318 [ dbSNP | Ensembl ].
VAR_012972
Natural variant6221M → I May be associated with increased susceptibility to colorectal cancer; significantly reduced interaction with MLH1. Ref.6 Ref.20 Ref.21
Corresponds to variant rs1805324 [ dbSNP | Ensembl ].
VAR_012973
Natural variant7051E → K in MMRCS; unknown pathological significance. Ref.19
VAR_012974
Natural variant7751N → S.
Corresponds to variant rs17420802 [ dbSNP | Ensembl ].
VAR_016135

Secondary structure

............................................................... 862
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 11, 2011. Version 2.
Checksum: B1B9547280ECAF9A

FASTA86295,797
        10         20         30         40         50         60 
MERAESSSTE PAKAIKPIDR KSVHQICSGQ VVLSLSTAVK ELVENSLDAG ATNIDLKLKD 

        70         80         90        100        110        120 
YGVDLIEVSD NGCGVEEENF EGLTLKHHTS KIQEFADLTQ VETFGFRGEA LSSLCALSDV 

       130        140        150        160        170        180 
TISTCHASAK VGTRLMFDHN GKIIQKTPYP RPRGTTVSVQ QLFSTLPVRH KEFQRNIKKE 

       190        200        210        220        230        240 
YAKMVQVLHA YCIISAGIRV SCTNQLGQGK RQPVVCTGGS PSIKENIGSV FGQKQLQSLI 

       250        260        270        280        290        300 
PFVQLPPSDS VCEEYGLSCS DALHNLFYIS GFISQCTHGV GRSSTDRQFF FINRRPCDPA 

       310        320        330        340        350        360 
KVCRLVNEVY HMYNRHQYPF VVLNISVDSE CVDINVTPDK RQILLQEEKL LLAVLKTSLI 

       370        380        390        400        410        420 
GMFDSDVNKL NVSQQPLLDV EGNLIKMHAA DLEKPMVEKQ DQSPSLRTGE EKKDVSISRL 

       430        440        450        460        470        480 
REAFSLRHTT ENKPHSPKTP EPRRSPLGQK RGMLSSSTSG AISDKGVLRP QKEAVSSSHG 

       490        500        510        520        530        540 
PSDPTDRAEV EKDSGHGSTS VDSEGFSIPD TGSHCSSEYA ASSPGDRGSQ EHVDSQEKAP 

       550        560        570        580        590        600 
KTDDSFSDVD CHSNQEDTGC KFRVLPQPTN LATPNTKRFK KEEILSSSDI CQKLVNTQDM 

       610        620        630        640        650        660 
SASQVDVAVK INKKVVPLDF SMSSLAKRIK QLHHEAQQSE GEQNYRKFRA KICPGENQAA 

       670        680        690        700        710        720 
EDELRKEISK TMFAEMEIIG QFNLGFIITK LNEDIFIVDQ HATDEKYNFE MLQQHTVLQG 

       730        740        750        760        770        780 
QRLIAPQTLN LTAVNEAVLI ENLEIFRKNG FDFVIDENAP VTERAKLISL PTSKNWTFGP 

       790        800        810        820        830        840 
QDVDELIFML SDSPGVMCRP SRVKQMFASR ACRKSVMIGT ALNTSEMKKL ITHMGEMDHP 

       850        860 
WNCPHGRPTM RHIANLGVIS QN 

« Hide

Isoform 2 [UniParc].

Checksum: 26A7DCBA84C6FEA5
Show »

FASTA46151,251
Isoform 3 [UniParc].

Checksum: 508F176091F469A4
Show »

FASTA57262,751
Isoform 4 [UniParc].

Checksum: ECC6B3983021FF07
Show »

FASTA18320,073

References

« Hide 'large scale' references
[1]"Mutations of two PMS homologues in hereditary nonpolyposis colon cancer."
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.
Nature 371:75-80(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS GLN-20 AND GLU-541.
Tissue: Endometrial tumor.
[2]"PMS2 mRNA, nirs splice variants."
Tabata Y., Sameshima E., Hayashi A., Iida K., Mitsuyama M., Kanai S., Furuya T., Saito T.
Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4), VARIANT GLU-541.
[3]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
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS SER-470 AND GLU-541.
[4]"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. expand/collapse author list , 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) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANTS SER-470 AND GLU-541.
Tissue: Amygdala.
[5]"The DNA sequence of human chromosome 7."
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. expand/collapse author list , 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.
Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANTS GLU-541 AND ILE-622.
Tissue: Brain.
[7]"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) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION OF PMS2 AS MEMBER OF BASC.
[8]"Familial mutations in PMS2 can cause autosomal dominant hereditary nonpolyposis colorectal cancer."
Worthley D.L., Walsh M.D., Barker M., Ruszkiewicz A., Bennett G., Phillips K., Suthers G.
Gastroenterology 128:1431-1436(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN HNPCC4.
[9]"Endonucleolytic function of MutLalpha in human mismatch repair."
Kadyrov F.A., Dzantiev L., Constantin N., Modrich P.
Cell 126:297-308(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS AN ENDONUCLEASE.
[10]"A frame-shift mutation of PMS2 is a widespread cause of Lynch syndrome."
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.
J. Med. Genet. 45:340-345(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN HNPCC4.
[11]"Direct visualization of asymmetric adenine nucleotide-induced conformational changes in MutL alpha."
Sacho E.J., Kadyrov F.A., Modrich P., Kunkel T.A., Erie D.A.
Mol. Cell 29:112-121(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[12]"Human mismatch repair: reconstitution of a nick-directed bidirectional reaction."
Constantin N., Dzantiev L., Kadyrov F.A., Modrich P.
J. Biol. Chem. 280:39752-39761(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[13]"MutLalpha: at the cutting edge of mismatch repair."
Jiricny J.
Cell 126:239-241(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[14]"Mechanisms and functions of DNA mismatch repair."
Li G.M.
Cell Res. 18:85-98(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[15]"A genetic screen identifies FAN1, a Fanconi anemia-associated nuclease necessary for DNA interstrand crosslink repair."
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.
Mol. Cell 39:36-47(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MTMR15.
[16]"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) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-597, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[17]"Structure and function of the N-terminal 40 kDa fragment of human PMS2: a monomeric GHL ATPase."
Guarne A., Junop M.S., Yang W.
EMBO J. 20:5521-5531(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 1-364.
[18]"The molecular basis of Turcot's syndrome."
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.
N. Engl. J. Med. 332:839-847(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN MMRCS.
[19]"Drastic genetic instability of tumors and normal tissues in Turcot syndrome."
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.
Oncogene 15:2877-2881(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT MMRCS LYS-705.
[20]"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) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS GLN-479; LYS-485; ALA-511; SER-597 AND ILE-622.
[21]"Polymorphisms and HNPCC: PMS2-MLH1 protein interactions diminished by single nucleotide polymorphisms."
Yuan Z.Q., Gottlieb B., Beitel L.K., Wong N., Gordon P.H., Wang Q., Puisieux A., Foulkes W.D., Trifiro M.
Hum. Mutat. 19:108-113(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF VARIANTS SER-597 AND ILE-622.
[22]"Novel PMS2 pseudogenes can conceal recessive mutations causing a distinctive childhood cancer syndrome."
De Vos M., Hayward B.E., Picton S., Sheridan E., Bonthron D.T.
Am. J. Hum. Genet. 74:954-964(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN MMRCS.
[23]"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) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT MMRCS ILE-46.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U13696 Genomic DNA. Translation: AAA63923.1.
AB103082 mRNA. Translation: BAD89425.1.
AB103083 mRNA. Translation: BAD89426.1.
AB103085 mRNA. Translation: BAD89428.1.
U14658 mRNA. Translation: AAA50390.1.
AK312390 mRNA. Translation: BAG35307.1.
AC005995 Genomic DNA. Translation: AAS00390.1.
BC093921 mRNA. Translation: AAH93921.1.
CCDSCCDS5343.1. [P54278-1]
PIRS47598.
RefSeqNP_000526.1. NM_000535.5.
UniGeneHs.632637.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1EA6X-ray2.70A/B1-364[»]
1H7SX-ray1.95A/B1-365[»]
1H7UX-ray2.70A/B1-365[»]
ProteinModelPortalP54278.
SMRP54278. Positions 29-365, 658-856.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111404. 45 interactions.
DIPDIP-27602N.
IntActP54278. 3 interactions.
MINTMINT-2804140.
STRING9606.ENSP00000265849.

PTM databases

PhosphoSiteP54278.

Polymorphism databases

DMDM317373266.

2D gel databases

SWISS-2DPAGEP54278.

Proteomic databases

MaxQBP54278.
PRIDEP54278.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000265849; ENSP00000265849; ENSG00000122512. [P54278-1]
ENST00000382321; ENSP00000371758; ENSG00000122512. [P54278-2]
ENST00000406569; ENSP00000384308; ENSG00000122512. [P54278-3]
GeneID5395.
KEGGhsa:5395.
UCSCuc003spk.3. human. [P54278-1]
uc010kte.3. human. [P54278-2]
uc010ktf.2. human. [P54278-3]

Organism-specific databases

CTD5395.
GeneCardsGC07M005979.
GeneReviewsPMS2.
HGNCHGNC:9122. PMS2.
HPACAB010235.
HPA043839.
HPA044400.
MIM276300. phenotype.
600259. gene.
614337. phenotype.
neXtProtNX_P54278.
Orphanet252202. Constitutional mismatch repair deficiency syndrome.
144. Hereditary nonpolyposis colon cancer.
99817. Non-polyposis Turcot syndrome.
PharmGKBPA33448.
GenAtlasSearch...

Phylogenomic databases

HOGENOMHOG000165474.
HOVERGENHBG008219.
InParanoidP54278.
KOK10858.
OMASIEVRFR.
OrthoDBEOG76QFGS.
PhylomeDBP54278.
TreeFamTF300711.

Gene expression databases

ArrayExpressP54278.
BgeeP54278.
CleanExHS_PMS2.
GenevestigatorP54278.

Family and domain databases

Gene3D3.30.230.10. 1 hit.
3.30.565.10. 1 hit.
InterProIPR013507. DNA_mismatch_repair_C.
IPR014762. DNA_mismatch_repair_CS.
IPR002099. DNA_mismatch_repair_fam.
IPR003594. HATPase_ATP-bd.
IPR014790. MutL_C.
IPR028831. Pms1/Pms2/PMS2L.
IPR020568. Ribosomal_S5_D2-typ_fold.
IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
[Graphical view]
PANTHERPTHR10073:SF9. PTHR10073:SF9. 1 hit.
PfamPF01119. DNA_mis_repair. 1 hit.
PF08676. MutL_C. 1 hit.
[Graphical view]
SMARTSM00387. HATPase_c. 1 hit.
SM00853. MutL_C. 1 hit.
[Graphical view]
SUPFAMSSF54211. SSF54211. 1 hit.
SSF55874. SSF55874. 1 hit.
TIGRFAMsTIGR00585. mutl. 1 hit.
PROSITEPS00058. DNA_MISMATCH_REPAIR_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP54278.
GeneWikiPMS2.
GenomeRNAi5395.
NextBio20918.
PROP54278.
SOURCESearch...

Entry information

Entry namePMS2_HUMAN
AccessionPrimary (citable) accession number: P54278
Secondary accession number(s): B2R610 expand/collapse secondary AC list , Q52LH6, Q5FBW9, Q5FBX1, Q5FBX2, Q75MR2
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 11, 2011
Last modified: July 9, 2014
This is version 152 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 7

Human chromosome 7: entries, gene names and cross-references to MIM