PMS1_HUMAN
ID PMS1_HUMAN Reviewed; 932 AA.
AC P54277; D3DPI1; Q4VAL4; Q5FBZ3; Q5FBZ6; Q5FBZ8;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 198.
DE RecName: Full=PMS1 protein homolog 1;
DE AltName: Full=DNA mismatch repair protein PMS1;
GN Name=PMS1; Synonyms=PMSL1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Gall bladder;
RX PubMed=8072530; DOI=10.1038/371075a0;
RA Nicolaides N.C., Papadopoulos N., Liu B., Wei Y.-F., Carter K.C.,
RA Ruben S.M., Rosen C.A., Haseltine W.H., Fleischmann R.D., Fraser C.M.,
RA Adams M.D., Venter J.C., Dunlop M.G., Hamilton S.R., Petersen G.M.,
RA de la Chapelle A., Vogelstein B., Kinzler K.W.;
RT "Mutations of two PMS homologues in hereditary nonpolyposis colon cancer.";
RL Nature 371:75-80(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3 AND 4).
RA Hayashi A., Sameshima E., Tabata Y., Iida K., Mitsuyama M., Kanai S.,
RA Furuya T., Saito T.;
RT "PMS1 mRNA, nirs splice variants.";
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS GLN-27; LYS-202; ARG-501;
RP SER-632; ASP-720 AND HIS-793.
RG NIEHS SNPs program;
RL Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-920 (ISOFORM 1).
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP FUNCTION, SUBUNIT, AND INTERACTION WITH MLH1.
RX PubMed=10748105; DOI=10.1074/jbc.m908768199;
RA Leung W.K., Kim J.J., Wu L., Sepulveda J.L., Sepulveda A.R.;
RT "Identification of a second MutL DNA mismatch repair complex (hPMS1 and
RT hMLH1) in human epithelial cells.";
RL J. Biol. Chem. 275:15728-15732(2000).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [10]
RP IDENTIFICATION IN THE MMR COMPLEX, AND INTERACTION WITH MCM9.
RX PubMed=26300262; DOI=10.1016/j.molcel.2015.07.010;
RA Traver S., Coulombe P., Peiffer I., Hutchins J.R., Kitzmann M.,
RA Latreille D., Mechali M.;
RT "MCM9 Is Required for Mammalian DNA Mismatch Repair.";
RL Mol. Cell 59:831-839(2015).
RN [11]
RP STRUCTURE BY NMR OF 571-649.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the HMG domain of human DNA mismatch repair
RT protein.";
RL Submitted (NOV-2005) to the PDB data bank.
RN [12]
RP VARIANTS THR-394 AND ARG-501.
RX PubMed=10480359; DOI=10.1007/s004399900064;
RA Wang Q., Lasset C., Desseigne F., Saurin J.-C., Maugard C., Navarro C.,
RA Ruano E., Descos L., Trillet-Lenoir V., Bosset J.-F., Puisieux A.;
RT "Prevalence of germline mutations of hMLH1, hMSH2, hPMS1, hPMS2, and hMSH6
RT genes in 75 French kindreds with nonpolyposis colorectal cancer.";
RL Hum. Genet. 105:79-85(1999).
CC -!- FUNCTION: Probably involved in the repair of mismatches in DNA.
CC {ECO:0000269|PubMed:10748105}.
CC -!- SUBUNIT: Component of the DNA mismatch repair (MMR) complex composed at
CC least of MSH2, MSH3, MSH6, PMS1 and MLH1 (PubMed:26300262). The MutL-
CC beta complex is a heterodimer of PMS1 and MLH1 (PubMed:10748105).
CC Interacts with MCM9 (PubMed:26300262). {ECO:0000269|PubMed:10748105,
CC ECO:0000269|PubMed:26300262}.
CC -!- INTERACTION:
CC P54277; P40692: MLH1; NbExp=4; IntAct=EBI-2893308, EBI-744248;
CC P54277-2; P51808: DYNLT3; NbExp=3; IntAct=EBI-12402645, EBI-743027;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00267}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=P54277-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P54277-2; Sequence=VSP_042676, VSP_042677;
CC Name=3;
CC IsoId=P54277-3; Sequence=VSP_043371;
CC Name=4;
CC IsoId=P54277-4; Sequence=VSP_047692, VSP_043371, VSP_042676,
CC VSP_042677;
CC -!- SIMILARITY: Belongs to the DNA mismatch repair MutL/HexB family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/PMS1ID345ch2q31.html";
CC -!- WEB RESOURCE: Name=Hereditary non-polyposis colorectal cancer db;
CC URL="http://www.nfdht.nl/";
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/pms1/";
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U13695; AAA63922.1; -; Genomic_DNA.
DR EMBL; AB102870; BAD89399.1; -; mRNA.
DR EMBL; AB102872; BAD89401.1; -; mRNA.
DR EMBL; AB102875; BAD89404.1; -; mRNA.
DR EMBL; AY267352; AAO89079.1; -; Genomic_DNA.
DR EMBL; AC008122; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC013468; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471058; EAX10883.1; -; Genomic_DNA.
DR EMBL; CH471058; EAX10885.1; -; Genomic_DNA.
DR EMBL; BC096330; AAH96330.1; -; mRNA.
DR EMBL; BC096332; AAH96332.1; -; mRNA.
DR CCDS; CCDS2302.1; -. [P54277-1]
DR CCDS; CCDS46473.1; -. [P54277-2]
DR CCDS; CCDS46474.1; -. [P54277-3]
DR PIR; S47597; S47597.
DR RefSeq; NP_000525.1; NM_000534.4. [P54277-1]
DR RefSeq; NP_001121615.1; NM_001128143.1. [P54277-3]
DR RefSeq; NP_001121616.1; NM_001128144.1. [P54277-2]
DR RefSeq; NP_001276337.1; NM_001289408.1.
DR RefSeq; NP_001307974.1; NM_001321045.1. [P54277-1]
DR RefSeq; NP_001307975.1; NM_001321046.1.
DR RefSeq; NP_001307976.1; NM_001321047.1. [P54277-1]
DR RefSeq; NP_001307977.1; NM_001321048.1. [P54277-1]
DR RefSeq; XP_016859833.1; XM_017004344.1. [P54277-3]
DR RefSeq; XP_016859837.1; XM_017004348.1. [P54277-2]
DR PDB; 2CS1; NMR; -; A=571-649.
DR PDBsum; 2CS1; -.
DR AlphaFoldDB; P54277; -.
DR SMR; P54277; -.
DR BioGRID; 111391; 100.
DR CORUM; P54277; -.
DR IntAct; P54277; 20.
DR MINT; P54277; -.
DR STRING; 9606.ENSP00000406490; -.
DR GlyGen; P54277; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P54277; -.
DR MetOSite; P54277; -.
DR PhosphoSitePlus; P54277; -.
DR BioMuta; PMS1; -.
DR DMDM; 1709683; -.
DR EPD; P54277; -.
DR jPOST; P54277; -.
DR MassIVE; P54277; -.
DR MaxQB; P54277; -.
DR PaxDb; P54277; -.
DR PeptideAtlas; P54277; -.
DR PRIDE; P54277; -.
DR ProteomicsDB; 56666; -. [P54277-1]
DR ProteomicsDB; 56667; -. [P54277-2]
DR ProteomicsDB; 56668; -. [P54277-3]
DR ProteomicsDB; 62795; -.
DR Antibodypedia; 4133; 343 antibodies from 32 providers.
DR CPTC; P54277; 1 antibody.
DR DNASU; 5378; -.
DR Ensembl; ENST00000409593.5; ENSP00000387169.1; ENSG00000064933.19. [P54277-4]
DR Ensembl; ENST00000409823.7; ENSP00000387125.3; ENSG00000064933.19. [P54277-3]
DR Ensembl; ENST00000441310.7; ENSP00000406490.3; ENSG00000064933.19. [P54277-1]
DR Ensembl; ENST00000447232.6; ENSP00000401064.2; ENSG00000064933.19. [P54277-2]
DR GeneID; 5378; -.
DR KEGG; hsa:5378; -.
DR MANE-Select; ENST00000441310.7; ENSP00000406490.3; NM_000534.5; NP_000525.1.
DR UCSC; uc002urh.5; human. [P54277-1]
DR CTD; 5378; -.
DR DisGeNET; 5378; -.
DR GeneCards; PMS1; -.
DR HGNC; HGNC:9121; PMS1.
DR HPA; ENSG00000064933; Tissue enhanced (testis).
DR MalaCards; PMS1; -.
DR MIM; 600258; gene.
DR neXtProt; NX_P54277; -.
DR OpenTargets; ENSG00000064933; -.
DR Orphanet; 144; Lynch syndrome.
DR PharmGKB; PA33447; -.
DR VEuPathDB; HostDB:ENSG00000064933; -.
DR eggNOG; KOG1978; Eukaryota.
DR GeneTree; ENSGT00940000157085; -.
DR HOGENOM; CLU_015755_0_0_1; -.
DR InParanoid; P54277; -.
DR OMA; KEIYECR; -.
DR PhylomeDB; P54277; -.
DR TreeFam; TF300711; -.
DR PathwayCommons; P54277; -.
DR SignaLink; P54277; -.
DR SIGNOR; P54277; -.
DR BioGRID-ORCS; 5378; 20 hits in 1100 CRISPR screens.
DR ChiTaRS; PMS1; human.
DR EvolutionaryTrace; P54277; -.
DR GeneWiki; PMS1; -.
DR GenomeRNAi; 5378; -.
DR Pharos; P54277; Tbio.
DR PRO; PR:P54277; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; P54277; protein.
DR Bgee; ENSG00000064933; Expressed in sperm and 201 other tissues.
DR ExpressionAtlas; P54277; baseline and differential.
DR Genevisible; P54277; HS.
DR GO; GO:0032300; C:mismatch repair complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0140664; F:ATP-dependent DNA damage sensor activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; TAS:ProtInc.
DR GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
DR GO; GO:0030983; F:mismatched DNA binding; IEA:InterPro.
DR GO; GO:0006298; P:mismatch repair; IBA:GO_Central.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
DR Gene3D; 1.10.30.10; -; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.30.565.10; -; 1.
DR InterPro; IPR014762; DNA_mismatch_repair_CS.
DR InterPro; IPR002099; DNA_mismatch_repair_N.
DR InterPro; IPR013507; DNA_mismatch_S5_2-like.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR009071; HMG_box_dom.
DR InterPro; IPR036910; HMG_box_dom_sf.
DR InterPro; IPR038973; MutL/Mlh/Pms.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR PANTHER; PTHR10073; PTHR10073; 1.
DR Pfam; PF01119; DNA_mis_repair; 1.
DR Pfam; PF00505; HMG_box; 1.
DR SMART; SM01340; DNA_mis_repair; 1.
DR SMART; SM00398; HMG; 1.
DR SUPFAM; SSF47095; SSF47095; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
DR TIGRFAMs; TIGR00585; mutl; 1.
DR PROSITE; PS00058; DNA_MISMATCH_REPAIR_1; 1.
DR PROSITE; PS50118; HMG_BOX_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; DNA damage; DNA repair; DNA-binding;
KW Hereditary nonpolyposis colorectal cancer; Nucleus; Reference proteome;
KW Tumor suppressor.
FT CHAIN 1..932
FT /note="PMS1 protein homolog 1"
FT /id="PRO_0000178004"
FT DNA_BIND 571..639
FT /note="HMG box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00267"
FT REGION 465..493
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..176
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_047692"
FT VAR_SEQ 195..233
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_043371"
FT VAR_SEQ 619
FT /note="K -> N (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_042676"
FT VAR_SEQ 620..781
FT /note="Missing (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_042677"
FT VARIANT 27
FT /note="E -> Q (in dbSNP:rs5742973)"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_019166"
FT VARIANT 202
FT /note="R -> K (in dbSNP:rs2066459)"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_014877"
FT VARIANT 394
FT /note="M -> T (in dbSNP:rs1145231)"
FT /evidence="ECO:0000269|PubMed:10480359"
FT /id="VAR_012967"
FT VARIANT 501
FT /note="G -> R (in dbSNP:rs1145232)"
FT /evidence="ECO:0000269|PubMed:10480359, ECO:0000269|Ref.3"
FT /id="VAR_012968"
FT VARIANT 632
FT /note="N -> S (in dbSNP:rs2066456)"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_014878"
FT VARIANT 720
FT /note="E -> D (in dbSNP:rs2066455)"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_014879"
FT VARIANT 793
FT /note="Y -> H (in dbSNP:rs1145234)"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_014880"
FT HELIX 577..592
FT /evidence="ECO:0007829|PDB:2CS1"
FT HELIX 598..610
FT /evidence="ECO:0007829|PDB:2CS1"
FT HELIX 614..625
FT /evidence="ECO:0007829|PDB:2CS1"
FT TURN 626..628
FT /evidence="ECO:0007829|PDB:2CS1"
FT HELIX 629..638
FT /evidence="ECO:0007829|PDB:2CS1"
SQ SEQUENCE 932 AA; 105830 MW; EC4F402937B616DF CRC64;
MKQLPAATVR LLSSSQIITS VVSVVKELIE NSLDAGATSV DVKLENYGFD KIEVRDNGEG
IKAVDAPVMA MKYYTSKINS HEDLENLTTY GFRGEALGSI CCIAEVLITT RTAADNFSTQ
YVLDGSGHIL SQKPSHLGQG TTVTALRLFK NLPVRKQFYS TAKKCKDEIK KIQDLLMSFG
ILKPDLRIVF VHNKAVIWQK SRVSDHKMAL MSVLGTAVMN NMESFQYHSE ESQIYLSGFL
PKCDADHSFT SLSTPERSFI FINSRPVHQK DILKLIRHHY NLKCLKESTR LYPVFFLKID
VPTADVDVNL TPDKSQVLLQ NKESVLIALE NLMTTCYGPL PSTNSYENNK TDVSAADIVL
SKTAETDVLF NKVESSGKNY SNVDTSVIPF QNDMHNDESG KNTDDCLNHQ ISIGDFGYGH
CSSEISNIDK NTKNAFQDIS MSNVSWENSQ TEYSKTCFIS SVKHTQSENG NKDHIDESGE
NEEEAGLENS SEISADEWSR GNILKNSVGE NIEPVKILVP EKSLPCKVSN NNYPIPEQMN
LNEDSCNKKS NVIDNKSGKV TAYDLLSNRV IKKPMSASAL FVQDHRPQFL IENPKTSLED
ATLQIEELWK TLSEEEKLKY EEKATKDLER YNSQMKRAIE QESQMSLKDG RKKIKPTSAW
NLAQKHKLKT SLSNQPKLDE LLQSQIEKRR SQNIKMVQIP FSMKNLKINF KKQNKVDLEE
KDEPCLIHNL RFPDAWLMTS KTEVMLLNPY RVEEALLFKR LLENHKLPAE PLEKPIMLTE
SLFNGSHYLD VLYKMTADDQ RYSGSTYLSD PRLTANGFKI KLIPGVSITE NYLEIEGMAN
CLPFYGVADL KEILNAILNR NAKEVYECRP RKVISYLEGE AVRLSRQLPM YLSKEDIQDI
IYRMKHQFGN EIKECVHGRP FFHHLTYLPE TT
