ID DUS26_RAT Reviewed; 211 AA. AC Q5FVI9; DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2005, sequence version 1. DT 27-MAR-2024, entry version 114. DE RecName: Full=Dual specificity protein phosphatase 26; DE EC=3.1.3.16; DE EC=3.1.3.48; GN Name=Dusp26; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; 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). CC -!- FUNCTION: Inactivates MAPK1 and MAPK3 which leads to dephosphorylation CC of heat shock factor protein 4 and a reduction in its DNA-binding CC activity. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + CC phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA- CC COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858, CC ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence={ECO:0000255|PROSITE- CC ProRule:PRU10044}; CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + CC phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA- CC COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474, CC ChEBI:CHEBI:83421; EC=3.1.3.16; CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] + CC phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA- CC COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474, CC ChEBI:CHEBI:61977; EC=3.1.3.16; CC -!- SUBUNIT: Interacts with HSF4. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. CC Golgi apparatus {ECO:0000250}. CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non- CC receptor class dual specificity subfamily. {ECO:0000305}. 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; BC089954; AAH89954.1; -; mRNA. DR RefSeq; NP_001012352.1; NM_001012352.1. DR RefSeq; XP_006253294.1; XM_006253232.3. DR RefSeq; XP_017455623.1; XM_017600134.1. DR AlphaFoldDB; Q5FVI9; -. DR SMR; Q5FVI9; -. DR STRING; 10116.ENSRNOP00000015725; -. DR PhosphoSitePlus; Q5FVI9; -. DR PaxDb; 10116-ENSRNOP00000015725; -. DR Ensembl; ENSRNOT00000015725.8; ENSRNOP00000015725.4; ENSRNOG00000011518.8. DR Ensembl; ENSRNOT00055020791; ENSRNOP00055016775; ENSRNOG00055012224. DR Ensembl; ENSRNOT00060020102; ENSRNOP00060015775; ENSRNOG00060011882. DR GeneID; 306527; -. DR KEGG; rno:306527; -. DR UCSC; RGD:1310090; rat. DR AGR; RGD:1310090; -. DR CTD; 78986; -. DR RGD; 1310090; Dusp26. DR eggNOG; KOG1716; Eukaryota. DR GeneTree; ENSGT00940000158107; -. DR HOGENOM; CLU_027074_11_3_1; -. DR InParanoid; Q5FVI9; -. DR OMA; MSIHFQA; -. DR OrthoDB; 1082488at2759; -. DR PhylomeDB; Q5FVI9; -. DR TreeFam; TF105128; -. DR PRO; PR:Q5FVI9; -. DR Proteomes; UP000002494; Chromosome 16. DR Bgee; ENSRNOG00000011518; Expressed in skeletal muscle tissue and 15 other cell types or tissues. DR GO; GO:0005737; C:cytoplasm; ISO:RGD. DR GO; GO:0005794; C:Golgi apparatus; ISO:RGD. DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl. DR GO; GO:0005634; C:nucleus; ISO:RGD. DR GO; GO:0033549; F:MAP kinase phosphatase activity; IBA:GO_Central. DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC. DR GO; GO:0002039; F:p53 binding; ISO:RGD. DR GO; GO:0004721; F:phosphoprotein phosphatase activity; ISO:RGD. DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC. DR GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; ISO:RGD. DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; ISO:RGD. DR GO; GO:0016311; P:dephosphorylation; IEA:InterPro. DR GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; ISO:RGD. DR GO; GO:0043409; P:negative regulation of MAPK cascade; IBA:GO_Central. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:RGD. DR GO; GO:0045785; P:positive regulation of cell adhesion; ISO:RGD. DR CDD; cd14578; DUSP26; 1. DR Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1. DR InterPro; IPR020405; Atypical_DUSP_subfamA. DR InterPro; IPR000340; Dual-sp_phosphatase_cat-dom. DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like. DR InterPro; IPR016130; Tyr_Pase_AS. DR InterPro; IPR000387; Tyr_Pase_dom. DR InterPro; IPR020422; TYR_PHOSPHATASE_DUAL_dom. DR PANTHER; PTHR45682; AGAP008228-PA; 1. DR PANTHER; PTHR45682:SF8; DUAL SPECIFICITY PROTEIN PHOSPHATASE 26; 1. DR Pfam; PF00782; DSPc; 1. DR PRINTS; PR01908; ADSPHPHTASE. DR PRINTS; PR01909; ADSPHPHTASEA. DR SMART; SM00195; DSPc; 1. DR SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1. DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1. DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1. DR PROSITE; PS50054; TYR_PHOSPHATASE_DUAL; 1. DR Genevisible; Q5FVI9; RN. PE 2: Evidence at transcript level; KW Cytoplasm; Golgi apparatus; Hydrolase; Nucleus; Protein phosphatase; KW Reference proteome. FT CHAIN 1..211 FT /note="Dual specificity protein phosphatase 26" FT /id="PRO_0000292222" FT DOMAIN 60..207 FT /note="Tyrosine-protein phosphatase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160" FT ACT_SITE 152 FT /note="Phosphocysteine intermediate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160" SQ SEQUENCE 211 AA; 23947 MW; 0209F0B9DF23A542 CRC64; MCPGNWLWAS MTFMARFSRS SSRSPVRTRG SLEEMPSVHH PFLNVFELER LLYTGKTACN HADEVWPGLY LGDQDMANNR RELRRLGITH VLNASHSRWR GTPEAYEGLG IRYLGVEAHD SPAFDMSVHF QTAADFIHRA LSQPGGKILV HCAVGVSRSA TLVLAYLMLY HHFTLVEAIK KVKDHRGIIP NRGFLRQLLA LDRRLRQGLE A //