ID V9H019_HUMAN Unreviewed; 810 AA. AC V9H019; DT 19-FEB-2014, integrated into UniProtKB/TrEMBL. DT 19-FEB-2014, sequence version 1. DT 19-JAN-2022, entry version 48. DE RecName: Full=DNA mismatch repair protein Msh2 {ECO:0000256|ARBA:ARBA00019549}; DE AltName: Full=MutS protein homolog 2 {ECO:0000256|ARBA:ARBA00013441}; 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 PeptideAtlas; V9H019; -. DR PRIDE; V9H019; -. DR UCSC; uc061iyo.1; human. DR ChiTaRS; MSH2; human. DR Bgee; ENSG00000095002; Expressed in secondary oocyte and 227 other tissues. DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-KW. DR GO; GO:0032300; C:mismatch repair complex; IEA:InterPro. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0030983; F:mismatched DNA binding; IEA:InterPro. DR GO; GO:0006298; P:mismatch repair; IEA:InterPro. DR Gene3D; 3.30.420.110; -; 1. DR Gene3D; 3.40.1170.10; -; 1. DR Gene3D; 3.40.50.300; -; 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; IPR032642; Msh2. DR InterPro; IPR036678; MutS_con_dom_sf. DR InterPro; IPR045076; MutS_family. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR11361; PTHR11361; 1. DR PANTHER; PTHR11361:SF35; PTHR11361:SF35; 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; SSF48334; 1. DR SUPFAM; SSF52540; SSF52540; 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 Coiled coil {ECO:0000256|SAM:Coils}; 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_2" FT /evidence="ECO:0000259|PROSITE:PS00486" FT COILED 353..373 FT /evidence="ECO:0000256|SAM:Coils" FT COILED 478..498 FT /evidence="ECO:0000256|SAM:Coils" FT COILED 553..576 FT /evidence="ECO:0000256|SAM:Coils" 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 //