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P54278

- PMS2_HUMAN

UniProt

P54278 - PMS2_HUMAN

Protein

Mismatch repair endonuclease PMS2

Gene

PMS2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 153 (01 Oct 2014)
      Sequence version 2 (11 Jan 2011)
      Previous versions | rss
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    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. protein binding Source: UniProtKB
    6. 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

    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

    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

    ArrayExpressiP54278.
    BgeeiP54278.
    CleanExiHS_PMS2.
    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 – 323
    Helixi35 – 4814
    Beta strandi52 – 598
    Helixi60 – 623
    Beta strandi64 – 707
    Helixi77 – 793
    Helixi81 – 844
    Beta strandi101 – 1099
    Helixi110 – 1178
    Beta strandi118 – 1258
    Beta strandi133 – 1375
    Beta strandi143 – 1486
    Beta strandi153 – 1619
    Turni162 – 1654
    Helixi167 – 1759
    Helixi177 – 19418
    Beta strandi199 – 2057
    Beta strandi211 – 2166
    Helixi223 – 2319
    Helixi233 – 2375
    Beta strandi239 – 2413
    Helixi249 – 2557
    Turni259 – 2635
    Beta strandi268 – 2747
    Turni278 – 2803
    Beta strandi281 – 2855
    Beta strandi288 – 2925
    Beta strandi295 – 2973
    Helixi300 – 31112
    Beta strandi321 – 3266
    Helixi329 – 3313
    Beta strandi332 – 3343
    Beta strandi343 – 3453
    Helixi348 – 36316

    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

    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_ATP-bd.
    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

    MERAESSSTE PAKAIKPIDR KSVHQICSGQ VVLSLSTAVK ELVENSLDAG    50
    ATNIDLKLKD YGVDLIEVSD NGCGVEEENF EGLTLKHHTS KIQEFADLTQ 100
    VETFGFRGEA LSSLCALSDV TISTCHASAK VGTRLMFDHN GKIIQKTPYP 150
    RPRGTTVSVQ QLFSTLPVRH KEFQRNIKKE YAKMVQVLHA YCIISAGIRV 200
    SCTNQLGQGK RQPVVCTGGS PSIKENIGSV FGQKQLQSLI PFVQLPPSDS 250
    VCEEYGLSCS DALHNLFYIS GFISQCTHGV GRSSTDRQFF FINRRPCDPA 300
    KVCRLVNEVY HMYNRHQYPF VVLNISVDSE CVDINVTPDK RQILLQEEKL 350
    LLAVLKTSLI GMFDSDVNKL NVSQQPLLDV EGNLIKMHAA DLEKPMVEKQ 400
    DQSPSLRTGE EKKDVSISRL REAFSLRHTT ENKPHSPKTP EPRRSPLGQK 450
    RGMLSSSTSG AISDKGVLRP QKEAVSSSHG PSDPTDRAEV EKDSGHGSTS 500
    VDSEGFSIPD TGSHCSSEYA ASSPGDRGSQ EHVDSQEKAP KTDDSFSDVD 550
    CHSNQEDTGC KFRVLPQPTN LATPNTKRFK KEEILSSSDI CQKLVNTQDM 600
    SASQVDVAVK INKKVVPLDF SMSSLAKRIK QLHHEAQQSE GEQNYRKFRA 650
    KICPGENQAA EDELRKEISK TMFAEMEIIG QFNLGFIITK LNEDIFIVDQ 700
    HATDEKYNFE MLQQHTVLQG QRLIAPQTLN LTAVNEAVLI ENLEIFRKNG 750
    FDFVIDENAP VTERAKLISL PTSKNWTFGP QDVDELIFML SDSPGVMCRP 800
    SRVKQMFASR ACRKSVMIGT ALNTSEMKKL ITHMGEMDHP WNCPHGRPTM 850
    RHIANLGVIS QN 862
    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 GC07M005979.
    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

    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

    ArrayExpressi P54278.
    Bgeei P54278.
    CleanExi HS_PMS2.
    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_ATP-bd.
    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

    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 1, 2014
    This is version 153 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