ID DUS2_HUMAN Reviewed; 314 AA. AC Q05923; DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1994, sequence version 1. DT 07-JUL-2009, entry version 99. DE RecName: Full=Dual specificity protein phosphatase 2; DE EC=3.1.3.48; DE EC=3.1.3.16; DE AltName: Full=Dual specificity protein phosphatase PAC-1; GN Name=DUSP2; Synonyms=PAC1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=93206122; PubMed=7681221; DOI=10.1126/science.7681221; RA Rohan P., Davis P., Moskaluk C.A., Kearns M., Krutzsch H., RA Siebenlist U., Kelly K.; RT "PAC-1: a mitogen-induced nuclear protein tyrosine phosphatase."; RL Science 259:1763-1766(1993). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=96070437; PubMed=7590752; DOI=10.1006/geno.1995.1110; RA Yi H., Morton C.C., Weremowicz S., McBride O.W., Kelly K.; RT "Genomic organization and chromosomal localization of the DUSP2 gene, RT encoding a MAP kinase phosphatase, to human 2p11.2-q11."; RL Genomics 28:92-96(1995). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=B-cell; 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP STRUCTURE BY NMR OF 170-314. RX PubMed=12575935; DOI=10.1016/S0969-2126(02)00943-7; RA Farooq A., Plotnikova O., Chaturvedi G., Yan S., Zeng L., Zhang Q., RA Zhou M.M.; RT "Solution structure of the MAPK phosphatase PAC-1 catalytic domain. RT Insights into substrate-induced enzymatic activation of MKP."; RL Structure 11:155-164(2003). CC -!- FUNCTION: Regulates mitogenic signal transduction by CC dephosphorylating both Thr and Tyr residues on MAP kinases ERK1 CC and ERK2. CC -!- CATALYTIC ACTIVITY: Protein tyrosine phosphate + H(2)O = protein CC tyrosine + phosphate. CC -!- CATALYTIC ACTIVITY: A phosphoprotein + H(2)O = a protein + CC phosphate. CC -!- SUBCELLULAR LOCATION: Nucleus. CC -!- TISSUE SPECIFICITY: In hematopoietic tissues. CC -!- INDUCTION: By mitogens. CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. CC Non-receptor class dual specificity subfamily. CC -!- SIMILARITY: Contains 1 rhodanese domain. CC -!- SIMILARITY: Contains 1 tyrosine-protein phosphatase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L11329; AAA50779.1; -; mRNA. DR EMBL; U23853; AAA86112.1; -; Genomic_DNA. DR EMBL; BC007771; AAH07771.1; -; mRNA. DR IPI; IPI00016729; -. DR PIR; A57126; A57126. DR RefSeq; NP_004409.1; -. DR UniGene; Hs.1183; -. DR PDB; 1M3G; NMR; -; A=170-314. DR PDBsum; 1M3G; -. DR PRIDE; Q05923; -. DR Ensembl; ENSG00000158050; Homo sapiens. DR GeneID; 1844; -. DR KEGG; hsa:1844; -. DR UCSC; uc002svk.2; human. DR GeneCards; GC02M096230; -. DR H-InvDB; HIX0002269; -. DR HGNC; HGNC:3068; DUSP2. DR MIM; 603068; gene. DR PharmGKB; PA27525; -. DR HOGENOM; Q05923; -. DR HOVERGEN; Q05923; -. DR OMA; Q05923; NQMVEIS. DR BRENDA; 3.1.3.16; 247. DR BRENDA; 3.1.3.48; 247. DR NextBio; 7551; -. DR ArrayExpress; Q05923; -. DR Bgee; Q05923; -. DR CleanEx; HS_DUSP2; -. DR GermOnline; ENSG00000158050; Homo sapiens. DR GO; GO:0005634; C:nucleus; TAS:ProtInc. DR GO; GO:0017017; F:MAP kinase tyrosine/serine/threonine phosph...; IEA:InterPro. DR GO; GO:0004725; F:protein tyrosine phosphatase activity; TAS:ProtInc. DR GO; GO:0008330; F:protein tyrosine/threonine phosphatase acti...; TAS:ProtInc. DR GO; GO:0000188; P:inactivation of MAPK activity; TAS:ProtInc. DR GO; GO:0006470; P:protein amino acid dephosphorylation; TAS:ProtInc. DR InterPro; IPR014393; Dual_MAP_Kinase_Phosphatase. DR InterPro; IPR008343; MAPK_phosph. DR InterPro; IPR001763; Rhodanese-like. DR InterPro; IPR000387; Tyr_Pase. DR InterPro; IPR016130; Tyr_Pase_AS. DR InterPro; IPR000340; Tyr_Pase_dual_specific. DR Gene3D; G3DSA:3.40.250.10; Rhodanese-like; 1. DR Pfam; PF00782; DSPc; 1. DR Pfam; PF00581; Rhodanese; 1. DR PIRSF; PIRSF000939; MAPK_Ptase; 1. DR PRINTS; PR01764; MAPKPHPHTASE. DR SMART; SM00195; DSPc; 1. DR SMART; SM00450; RHOD; 1. DR PROSITE; PS50206; RHODANESE_3; 1. DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1. DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1. DR PROSITE; PS50054; TYR_PHOSPHATASE_DUAL; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Hydrolase; Nucleus; KW Protein phosphatase. FT CHAIN 1 314 Dual specificity protein phosphatase 2. FT /FTId=PRO_0000094793. FT DOMAIN 23 144 Rhodanese. FT DOMAIN 237 302 Tyrosine-protein phosphatase. FT ACT_SITE 257 257 Phosphocysteine intermediate (By FT similarity). FT STRAND 174 176 FT TURN 177 179 FT STRAND 180 182 FT HELIX 188 197 FT STRAND 200 204 FT STRAND 206 213 FT STRAND 215 221 FT HELIX 236 248 FT STRAND 253 255 FT STRAND 258 262 FT HELIX 263 274 FT HELIX 279 287 FT HELIX 305 311 SQ SEQUENCE 314 AA; 34400 MW; FDD3543C6DE10CA5 CRC64; MGLEAARELE CAALGTLLRD PREAERTLLL DCRPFLAFCR RHVRAARPVP WNALLRRRAR GPPAAVLACL LPDRALRTRL VRGELARAVV LDEGSASVAE LRPDSPAHVL LAALLHETRA GPTAVYFLRG GFDGFQGCCP DLCSEAPAPA LPPTGDKTSR SDSRAPVYDQ GGPVEILPYL FLGSCSHSSD LQGLQACGIT AVLNVSASCP NHFEGLFRYK SIPVEDNQMV EISAWFQEAI GFIDWVKNSG GRVLVHCQAG ISRSATICLA YLMQSRRVRL DEAFDFVKQR RGVISPNFSF MGQLLQFETQ VLCH //