ID V9H019_HUMAN Unreviewed; 810 AA. AC V9H019; DT 19-FEB-2014, integrated into UniProtKB/TrEMBL. DT 19-FEB-2014, sequence version 1. DT 29-MAY-2024, entry version 53. DE SubName: Full=MSH2 protein {ECO:0000313|EMBL:AAB59572.1}; GN Name=MSH2 {ECO:0000313|EMBL:AAB59572.1}; 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 {ECO:0000313|EMBL:AAB59572.1}; RN [1] {ECO:0000313|EMBL:AAB59572.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=7726159; RA Wijnen J., Vasen H., Khan P.M., Menko F.H., van der Klift H., RA van Leeuwen C., van den Broek M., van Leeuwen-Cornelisse I., Nagengast F., RA Meijers-Heijboer A., Lindhout D., Griffioen G., Cats A., Kleibeuker J., RA Varesco L., Bertario L., Bisgaard M.L., Mohr J., Fodde R.; RT "Seven new mutations in hMSH2, an HNPCC gene, identified by denaturing RT gradient-gel electrophoresis."; RL Am. J. Hum. Genet. 56:1060-1066(1995). RN [2] {ECO:0007829|PubMed:19608861} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., RA Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [3] {ECO:0007829|PubMed:21269460} 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., Burckstummer 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 [4] {ECO:0007829|PubMed:22814378} 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). CC -!- FUNCTION: Component of the post-replicative DNA mismatch repair system CC (MMR). {ECO:0000256|RuleBase:RU003756}. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}. CC -!- SIMILARITY: Belongs to the DNA mismatch repair MutS family. CC {ECO:0000256|ARBA:ARBA00006271, ECO:0000256|RuleBase:RU003756}. 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; L47580; AAB59572.1; -; mRNA. DR AlphaFoldDB; V9H019; -. DR PeptideAtlas; V9H019; -. DR UCSC; uc061iyo.1; human. DR ChiTaRS; MSH2; human. DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-KW. DR GO; GO:0032301; C:MutSalpha complex; IEA:TreeGrafter. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0140664; F:ATP-dependent DNA damage sensor activity; IEA:InterPro. DR GO; GO:0030983; F:mismatched DNA binding; IEA:InterPro. DR GO; GO:0006298; P:mismatch repair; IEA:InterPro. DR GO; GO:0006312; P:mitotic recombination; IEA:TreeGrafter. DR GO; GO:0002204; P:somatic recombination of immunoglobulin genes involved in immune response; IEA:TreeGrafter. DR Gene3D; 1.10.1420.10; -; 2. DR Gene3D; 3.40.1170.10; DNA repair protein MutS, domain I; 1. DR Gene3D; 3.30.420.110; MutS, connector domain; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR InterPro; IPR011184; DNA_mismatch_repair_Msh2. DR InterPro; IPR007695; DNA_mismatch_repair_MutS-lik_N. DR InterPro; IPR000432; DNA_mismatch_repair_MutS_C. DR InterPro; IPR007861; DNA_mismatch_repair_MutS_clamp. DR InterPro; IPR007696; DNA_mismatch_repair_MutS_core. DR InterPro; IPR016151; DNA_mismatch_repair_MutS_N. DR InterPro; IPR036187; DNA_mismatch_repair_MutS_sf. DR InterPro; IPR007860; DNA_mmatch_repair_MutS_con_dom. DR InterPro; IPR036678; MutS_con_dom_sf. DR InterPro; IPR045076; MutS_family. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR11361:SF35; DNA MISMATCH REPAIR PROTEIN MSH2; 1. DR PANTHER; PTHR11361; DNA MISMATCH REPAIR PROTEIN MUTS FAMILY MEMBER; 1. DR Pfam; PF01624; MutS_I; 1. DR Pfam; PF05188; MutS_II; 1. DR Pfam; PF05192; MutS_III; 1. DR Pfam; PF05190; MutS_IV; 1. DR Pfam; PF00488; MutS_V; 1. DR PIRSF; PIRSF005813; MSH2; 1. DR SMART; SM00534; MUTSac; 1. DR SMART; SM00533; MUTSd; 1. DR SUPFAM; SSF48334; DNA repair protein MutS, domain III; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR PROSITE; PS00486; DNA_MISMATCH_REPAIR_2; 1. PE 1: Evidence at protein level; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840}; KW Chromosome {ECO:0000256|ARBA:ARBA00022454}; KW DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|RuleBase:RU003756}; KW DNA repair {ECO:0000256|RuleBase:RU003756}; KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU003756}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, KW ECO:0000256|RuleBase:RU003756}; Nucleus {ECO:0000256|ARBA:ARBA00023242}. FT DOMAIN 743..759 FT /note="DNA mismatch repair proteins mutS family" FT /evidence="ECO:0000259|PROSITE:PS00486" SQ SEQUENCE 810 AA; 90855 MW; F8D3163FFF46AB3A CRC64; MAVQPKETLQ LESAAEVGFV RFFQGMPEKP TTTVRLFDRG DFYTAHGEDA LLAAREVFKT QGVIKYMGPA GAKNLQSVVL SKMNFESFVK DLLLVRQYRV EVYKNRAGNK ASKENDWYLA YKASPGNLSQ FEDILFGNND MSASIGVVGV KMSAVDGQRQ VGVGYVDSIQ RKLGLCEFPD NDQFSNLEAL LIQIGPKECV LPGGETAGDM GKLRQIIQRG GILITERKKA DFSTKDIYQD LNRLLKGKKG EQMNSAVLPE MENQVAVSSL SAVIKFLELL SDDSNFGQFE LTTFDFSQYM KLDIAAVRAL NLFQGSVEDT TGSQSLAALL NKCKTPQGQR LVNQWIKQPL MDKNRIEERL NLVEAFVEDA ELRQTLQEDL LRRFPDLNRL AKKFQRQAAN LQDCYRLYQG INQLPNVIQA LEKHEGKHQK LLLAVFVTPL TDLRSDFSKF QEMIETTLDM DQVENHEFLV KPSFDPNLSE LREIMNDLEK KMQSTLISAA RDLGLDPGKQ IKLDSSAQFG YYFRVTCKEE KVLRNNKNFS TVDIQKNGVK FTNSKLTSLN EEYTKNKTEY EEAQDAIVKE IVNISSGYVE PMQTLNDVLA QLDAVVSFAH VSNGAPVPYV RPAILEKGQG RIILKASRHA CVEVQDEIAF IPNDVYFEKD KQMFHIITGP NMGGKSTYIR QTGVIVLMAQ IGCFVPCESA EVSIVDCILA RVGAGDSQLK GVSTFMAEML ETASILRSAT KDSLIIIDEL GRGTSTYDGF GLAWAISEYI ATKIGAFCMF ATIFMNLLPW PIRYQLLIIY MSQHSPLKRP //