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P54278

- PMS2_HUMAN

UniProt

P54278 - PMS2_HUMAN

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Protein

Mismatch repair endonuclease PMS2

Gene

PMS2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.2 Publications

GO - Molecular functioni

  1. ATPase activity Source: RefGenome
  2. ATP binding Source: InterPro
  3. DNA binding Source: HGNC
  4. endonuclease activity Source: UniProtKB-KW
  5. single base insertion or deletion binding Source: HGNC

GO - Biological processi

  1. ATP catabolic process Source: GOC
  2. mismatch repair Source: HGNC
  3. response to drug Source: Ensembl
  4. somatic hypermutation of immunoglobulin genes Source: RefGenome
  5. somatic recombination of immunoglobulin gene segments Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Endonuclease, Hydrolase, Nuclease

Keywords - Biological processi

DNA damage, DNA repair

Names & Taxonomyi

Protein namesi
Recommended name:
Mismatch repair endonuclease PMS2 (EC:3.1.-.-)
Alternative name(s):
DNA mismatch repair protein PMS2
PMS1 protein homolog 2
Gene namesi
Name:PMS2
Synonyms:PMSL2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 7

Organism-specific databases

HGNCiHGNC:9122. PMS2.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. microtubule cytoskeleton Source: HPA
  3. MutLalpha complex Source: RefGenome
  4. nucleus Source: HGNC
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

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.2 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
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.4 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti46 – 461S → I in MMRCS. 1 Publication
VAR_066838
Natural varianti705 – 7051E → K in MMRCS; unknown pathological significance. 1 Publication
VAR_012974

Keywords - Diseasei

Disease mutation, Hereditary nonpolyposis colorectal cancer, Tumor suppressor

Organism-specific databases

MIMi276300. phenotype.
614337. phenotype.
Orphaneti252202. Constitutional mismatch repair deficiency syndrome.
144. Hereditary nonpolyposis colon cancer.
99817. Non-polyposis Turcot syndrome.
PharmGKBiPA33448.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 862862Mismatch repair endonuclease PMS2PRO_0000178005Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei597 – 5971Phosphothreonine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP54278.
PRIDEiP54278.

2D gel databases

SWISS-2DPAGEP54278.

PTM databases

PhosphoSiteiP54278.

Expressioni

Gene expression databases

BgeeiP54278.
CleanExiHS_PMS2.
ExpressionAtlasiP54278. baseline.
GenevestigatoriP54278.

Organism-specific databases

HPAiCAB010235.
HPA043839.
HPA044400.

Interactioni

Subunit structurei

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/FAN1.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
MLH1P406924EBI-1162561,EBI-744248

Protein-protein interaction databases

BioGridi111404. 45 interactions.
DIPiDIP-27602N.
IntActiP54278. 3 interactions.
MINTiMINT-2804140.
STRINGi9606.ENSP00000265849.

Structurei

Secondary structure

1
862
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi30 – 323Combined sources
Helixi35 – 4814Combined sources
Beta strandi52 – 598Combined sources
Helixi60 – 623Combined sources
Beta strandi64 – 707Combined sources
Helixi77 – 793Combined sources
Helixi81 – 844Combined sources
Beta strandi101 – 1099Combined sources
Helixi110 – 1178Combined sources
Beta strandi118 – 1258Combined sources
Beta strandi133 – 1375Combined sources
Beta strandi143 – 1486Combined sources
Beta strandi153 – 1619Combined sources
Turni162 – 1654Combined sources
Helixi167 – 1759Combined sources
Helixi177 – 19418Combined sources
Beta strandi199 – 2057Combined sources
Beta strandi211 – 2166Combined sources
Helixi223 – 2319Combined sources
Helixi233 – 2375Combined sources
Beta strandi239 – 2413Combined sources
Helixi249 – 2557Combined sources
Turni259 – 2635Combined sources
Beta strandi268 – 2747Combined sources
Turni278 – 2803Combined sources
Beta strandi281 – 2855Combined sources
Beta strandi288 – 2925Combined sources
Beta strandi295 – 2973Combined sources
Helixi300 – 31112Combined sources
Beta strandi321 – 3266Combined sources
Helixi329 – 3313Combined sources
Beta strandi332 – 3343Combined sources
Beta strandi343 – 3453Combined sources
Helixi348 – 36316Combined sources

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EA6X-ray2.70A/B1-364[»]
1H7SX-ray1.95A/B1-365[»]
1H7UX-ray2.70A/B1-365[»]
ProteinModelPortaliP54278.
SMRiP54278. Positions 29-365, 658-856.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP54278.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

GeneTreeiENSGT00530000063289.
HOGENOMiHOG000165474.
HOVERGENiHBG008219.
InParanoidiP54278.
KOiK10858.
OMAiSIEVRFR.
OrthoDBiEOG76QFGS.
PhylomeDBiP54278.
TreeFamiTF300711.

Family and domain databases

Gene3Di3.30.230.10. 1 hit.
3.30.565.10. 1 hit.
InterProiIPR013507. DNA_mismatch_repair_C.
IPR014762. DNA_mismatch_repair_CS.
IPR002099. DNA_mismatch_repair_fam.
IPR003594. HATPase_C.
IPR014790. MutL_C.
IPR028831. Pms1/Pms2/PMS2L.
IPR020568. Ribosomal_S5_D2-typ_fold.
IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
[Graphical view]
PANTHERiPTHR10073:SF9. PTHR10073:SF9. 1 hit.
PfamiPF01119. DNA_mis_repair. 1 hit.
PF08676. MutL_C. 1 hit.
[Graphical view]
SMARTiSM00387. HATPase_c. 1 hit.
SM00853. MutL_C. 1 hit.
[Graphical view]
SUPFAMiSSF54211. SSF54211. 1 hit.
SSF55874. SSF55874. 1 hit.
TIGRFAMsiTIGR00585. mutl. 1 hit.
PROSITEiPS00058. DNA_MISMATCH_REPAIR_1. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P54278-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MERAESSSTE PAKAIKPIDR KSVHQICSGQ VVLSLSTAVK ELVENSLDAG
60 70 80 90 100
ATNIDLKLKD YGVDLIEVSD NGCGVEEENF EGLTLKHHTS KIQEFADLTQ
110 120 130 140 150
VETFGFRGEA LSSLCALSDV TISTCHASAK VGTRLMFDHN GKIIQKTPYP
160 170 180 190 200
RPRGTTVSVQ QLFSTLPVRH KEFQRNIKKE YAKMVQVLHA YCIISAGIRV
210 220 230 240 250
SCTNQLGQGK RQPVVCTGGS PSIKENIGSV FGQKQLQSLI PFVQLPPSDS
260 270 280 290 300
VCEEYGLSCS DALHNLFYIS GFISQCTHGV GRSSTDRQFF FINRRPCDPA
310 320 330 340 350
KVCRLVNEVY HMYNRHQYPF VVLNISVDSE CVDINVTPDK RQILLQEEKL
360 370 380 390 400
LLAVLKTSLI GMFDSDVNKL NVSQQPLLDV EGNLIKMHAA DLEKPMVEKQ
410 420 430 440 450
DQSPSLRTGE EKKDVSISRL REAFSLRHTT ENKPHSPKTP EPRRSPLGQK
460 470 480 490 500
RGMLSSSTSG AISDKGVLRP QKEAVSSSHG PSDPTDRAEV EKDSGHGSTS
510 520 530 540 550
VDSEGFSIPD TGSHCSSEYA ASSPGDRGSQ EHVDSQEKAP KTDDSFSDVD
560 570 580 590 600
CHSNQEDTGC KFRVLPQPTN LATPNTKRFK KEEILSSSDI CQKLVNTQDM
610 620 630 640 650
SASQVDVAVK INKKVVPLDF SMSSLAKRIK QLHHEAQQSE GEQNYRKFRA
660 670 680 690 700
KICPGENQAA EDELRKEISK TMFAEMEIIG QFNLGFIITK LNEDIFIVDQ
710 720 730 740 750
HATDEKYNFE MLQQHTVLQG QRLIAPQTLN LTAVNEAVLI ENLEIFRKNG
760 770 780 790 800
FDFVIDENAP VTERAKLISL PTSKNWTFGP QDVDELIFML SDSPGVMCRP
810 820 830 840 850
SRVKQMFASR ACRKSVMIGT ALNTSEMKKL ITHMGEMDHP WNCPHGRPTM
860
RHIANLGVIS QN
Length:862
Mass (Da):95,797
Last modified:January 11, 2011 - v2
Checksum:iB1B9547280ECAF9A
GO
Isoform 2 (identifier: P54278-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     269-669: Missing.

Note: No experimental confirmation available.

Show »
Length:461
Mass (Da):51,251
Checksum:i26A7DCBA84C6FEA5
GO
Isoform 3 (identifier: P54278-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     560-572: CKFRVLPQPTNLA → LKTGPSDPRTSMN
     573-862: Missing.

Note: No experimental confirmation available.

Show »
Length:572
Mass (Da):62,751
Checksum:i508F176091F469A4
GO
Isoform 4 (identifier: P54278-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     180-183: EYAK → QASV
     184-862: Missing.

Note: No experimental confirmation available.

Show »
Length:183
Mass (Da):20,073
Checksum:iECC6B3983021FF07
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti20 – 201R → Q.1 Publication
Corresponds to variant rs10254120 [ dbSNP | Ensembl ].
VAR_004469
Natural varianti46 – 461S → I in MMRCS. 1 Publication
VAR_066838
Natural varianti277 – 2771T → K.
Corresponds to variant rs1805322 [ dbSNP | Ensembl ].
VAR_016133
Natural varianti470 – 4701P → S.2 Publications
Corresponds to variant rs1805321 [ dbSNP | Ensembl ].
VAR_016134
Natural varianti479 – 4791H → Q.1 Publication
VAR_012969
Natural varianti485 – 4851T → K.1 Publication
Corresponds to variant rs1805323 [ dbSNP | Ensembl ].
VAR_012970
Natural varianti511 – 5111T → A.1 Publication
Corresponds to variant rs2228007 [ dbSNP | Ensembl ].
VAR_012971
Natural varianti541 – 5411K → E.5 Publications
Corresponds to variant rs2228006 [ dbSNP | Ensembl ].
VAR_024541
Natural varianti597 – 5971T → S May be associated with increased susceptibility to colorectal cancer; significantly reduced interaction with MLH1. 1 Publication
Corresponds to variant rs1805318 [ dbSNP | Ensembl ].
VAR_012972
Natural varianti622 – 6221M → I May be associated with increased susceptibility to colorectal cancer; significantly reduced interaction with MLH1. 2 Publications
Corresponds to variant rs1805324 [ dbSNP | Ensembl ].
VAR_012973
Natural varianti705 – 7051E → K in MMRCS; unknown pathological significance. 1 Publication
VAR_012974
Natural varianti775 – 7751N → S.
Corresponds to variant rs17420802 [ dbSNP | Ensembl ].
VAR_016135

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei180 – 1834EYAK → QASV in isoform 4. 1 PublicationVSP_029384
Alternative sequencei184 – 862679Missing in isoform 4. 1 PublicationVSP_029385Add
BLAST
Alternative sequencei269 – 669401Missing in isoform 2. 1 PublicationVSP_029386Add
BLAST
Alternative sequencei560 – 57213CKFRV…PTNLA → LKTGPSDPRTSMN in isoform 3. 1 PublicationVSP_029387Add
BLAST
Alternative sequencei573 – 862290Missing in isoform 3. 1 PublicationVSP_029388Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS5343.1. [P54278-1]
PIRiS47598.
RefSeqiNP_000526.1. NM_000535.5.
UniGeneiHs.632637.

Genome annotation databases

EnsembliENST00000265849; ENSP00000265849; ENSG00000122512. [P54278-1]
ENST00000382321; ENSP00000371758; ENSG00000122512. [P54278-2]
GeneIDi5395.
KEGGihsa:5395.
UCSCiuc003spk.3. human. [P54278-1]
uc010kte.3. human. [P54278-2]
uc010ktf.2. human. [P54278-3]

Polymorphism databases

DMDMi317373266.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Hereditary non-polyposis colorectal cancer db

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS5343.1. [P54278-1 ]
PIRi S47598.
RefSeqi NP_000526.1. NM_000535.5.
UniGenei Hs.632637.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1EA6 X-ray 2.70 A/B 1-364 [» ]
1H7S X-ray 1.95 A/B 1-365 [» ]
1H7U X-ray 2.70 A/B 1-365 [» ]
ProteinModelPortali P54278.
SMRi P54278. Positions 29-365, 658-856.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111404. 45 interactions.
DIPi DIP-27602N.
IntActi P54278. 3 interactions.
MINTi MINT-2804140.
STRINGi 9606.ENSP00000265849.

PTM databases

PhosphoSitei P54278.

Polymorphism databases

DMDMi 317373266.

2D gel databases

SWISS-2DPAGE P54278.

Proteomic databases

MaxQBi P54278.
PRIDEi P54278.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000265849 ; ENSP00000265849 ; ENSG00000122512 . [P54278-1 ]
ENST00000382321 ; ENSP00000371758 ; ENSG00000122512 . [P54278-2 ]
GeneIDi 5395.
KEGGi hsa:5395.
UCSCi uc003spk.3. human. [P54278-1 ]
uc010kte.3. human. [P54278-2 ]
uc010ktf.2. human. [P54278-3 ]

Organism-specific databases

CTDi 5395.
GeneCardsi GC07M006016.
GeneReviewsi PMS2.
HGNCi HGNC:9122. PMS2.
HPAi CAB010235.
HPA043839.
HPA044400.
MIMi 276300. phenotype.
600259. gene.
614337. phenotype.
neXtProti NX_P54278.
Orphaneti 252202. Constitutional mismatch repair deficiency syndrome.
144. Hereditary nonpolyposis colon cancer.
99817. Non-polyposis Turcot syndrome.
PharmGKBi PA33448.
GenAtlasi Search...

Phylogenomic databases

GeneTreei ENSGT00530000063289.
HOGENOMi HOG000165474.
HOVERGENi HBG008219.
InParanoidi P54278.
KOi K10858.
OMAi SIEVRFR.
OrthoDBi EOG76QFGS.
PhylomeDBi P54278.
TreeFami TF300711.

Miscellaneous databases

EvolutionaryTracei P54278.
GeneWikii PMS2.
GenomeRNAii 5395.
NextBioi 20918.
PROi P54278.
SOURCEi Search...

Gene expression databases

Bgeei P54278.
CleanExi HS_PMS2.
ExpressionAtlasi P54278. baseline.
Genevestigatori P54278.

Family and domain databases

Gene3Di 3.30.230.10. 1 hit.
3.30.565.10. 1 hit.
InterProi IPR013507. DNA_mismatch_repair_C.
IPR014762. DNA_mismatch_repair_CS.
IPR002099. DNA_mismatch_repair_fam.
IPR003594. HATPase_C.
IPR014790. MutL_C.
IPR028831. Pms1/Pms2/PMS2L.
IPR020568. Ribosomal_S5_D2-typ_fold.
IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
[Graphical view ]
PANTHERi PTHR10073:SF9. PTHR10073:SF9. 1 hit.
Pfami PF01119. DNA_mis_repair. 1 hit.
PF08676. MutL_C. 1 hit.
[Graphical view ]
SMARTi SM00387. HATPase_c. 1 hit.
SM00853. MutL_C. 1 hit.
[Graphical view ]
SUPFAMi SSF54211. SSF54211. 1 hit.
SSF55874. SSF55874. 1 hit.
TIGRFAMsi TIGR00585. mutl. 1 hit.
PROSITEi PS00058. DNA_MISMATCH_REPAIR_1. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. 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. 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.
    , 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.
    , 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. 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. Cited for: INVOLVEMENT IN MMRCS.
  19. 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.

Entry informationi

Entry nameiPMS2_HUMAN
AccessioniPrimary (citable) accession number: P54278
Secondary accession number(s): B2R610
, Q52LH6, Q5FBW9, Q5FBX1, Q5FBX2, Q75MR2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 11, 2011
Last modified: October 29, 2014
This is version 154 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 7
    Human chromosome 7: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3