DUS26_MOUSE
ID DUS26_MOUSE Reviewed; 211 AA.
AC Q9D700; Q8VCZ5;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 2.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Dual specificity protein phosphatase 26;
DE EC=3.1.3.16;
DE EC=3.1.3.48;
DE AltName: Full=Dual specificity phosphatase SKRP3;
GN Name=Dusp26; Synonyms=Skrp3;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Zama T., Aoki R., Murata M., Ikeda Y.;
RT "Identification of a novel dual specificity phosphatase, SKRP3.";
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Tongue;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Mammary tumor;
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 [4]
RP TISSUE SPECIFICITY.
RX PubMed=16581800; DOI=10.1128/mcb.26.8.3282-3294.2006;
RA Hu Y., Mivechi N.F.;
RT "Association and regulation of heat shock transcription factor 4b with both
RT extracellular signal-regulated kinase mitogen-activated protein kinase and
RT dual-specificity tyrosine phosphatase DUSP26.";
RL Mol. Cell. Biol. 26:3282-3294(2006).
RN [5]
RP TISSUE SPECIFICITY.
RX PubMed=17001450; DOI=10.1007/s11010-006-9313-5;
RA Takagaki K., Shima H., Tanuma N., Nomura M., Satoh T., Watanabe M.,
RA Kikuchi K.;
RT "Characterization of a novel low-molecular-mass dual specificity
RT phosphatase-4 (LDP-4) expressed in brain.";
RL Mol. Cell. Biochem. 296:177-184(2007).
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 -!- TISSUE SPECIFICITY: Brain and skeletal muscle. In the brain it is
CC expressed ubiquitously except in the hippocampus.
CC {ECO:0000269|PubMed:16581800, ECO:0000269|PubMed:17001450}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class dual specificity subfamily. {ECO:0000305}.
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DR EMBL; AB104416; BAD91016.1; -; mRNA.
DR EMBL; AK009781; BAB26501.2; -; mRNA.
DR EMBL; BC018204; AAH18204.1; -; mRNA.
DR CCDS; CCDS22219.1; -.
DR RefSeq; NP_080145.1; NM_025869.3.
DR RefSeq; XP_017168431.1; XM_017312942.1.
DR AlphaFoldDB; Q9D700; -.
DR SMR; Q9D700; -.
DR STRING; 10090.ENSMUSP00000046794; -.
DR PhosphoSitePlus; Q9D700; -.
DR PaxDb; Q9D700; -.
DR PRIDE; Q9D700; -.
DR ProteomicsDB; 277610; -.
DR Antibodypedia; 10741; 232 antibodies from 31 providers.
DR DNASU; 66959; -.
DR Ensembl; ENSMUST00000036631; ENSMUSP00000046794; ENSMUSG00000039661.
DR Ensembl; ENSMUST00000161713; ENSMUSP00000124949; ENSMUSG00000039661.
DR Ensembl; ENSMUST00000170204; ENSMUSP00000126397; ENSMUSG00000039661.
DR GeneID; 66959; -.
DR KEGG; mmu:66959; -.
DR UCSC; uc009ljb.1; mouse.
DR CTD; 78986; -.
DR MGI; MGI:1914209; Dusp26.
DR VEuPathDB; HostDB:ENSMUSG00000039661; -.
DR eggNOG; KOG1716; Eukaryota.
DR GeneTree; ENSGT00940000158107; -.
DR HOGENOM; CLU_027074_11_3_1; -.
DR InParanoid; Q9D700; -.
DR OMA; TVYFDEC; -.
DR OrthoDB; 1576308at2759; -.
DR PhylomeDB; Q9D700; -.
DR TreeFam; TF105128; -.
DR BioGRID-ORCS; 66959; 4 hits in 72 CRISPR screens.
DR ChiTaRS; Dusp26; mouse.
DR PRO; PR:Q9D700; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q9D700; protein.
DR Bgee; ENSMUSG00000039661; Expressed in superior cervical ganglion and 200 other tissues.
DR Genevisible; Q9D700; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:MGI.
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:MGI.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; ISO:MGI.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; ISO:MGI.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; ISO:MGI.
DR GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; ISO:MGI.
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:MGI.
DR GO; GO:0045785; P:positive regulation of cell adhesion; ISO:MGI.
DR GO; GO:0006470; P:protein dephosphorylation; ISO:MGI.
DR Gene3D; 3.90.190.10; -; 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; PTHR45682; 1.
DR Pfam; PF00782; DSPc; 1.
DR PRINTS; PR01909; ADSPHPHTASEA.
DR SMART; SM00195; DSPc; 1.
DR SUPFAM; SSF52799; SSF52799; 1.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR PROSITE; PS50054; TYR_PHOSPHATASE_DUAL; 1.
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_0000292220"
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; 23946 MW; 952A6C7561E9B046 CRC64;
MCPGNWLWAS MTFMARFSRG SSRSPVRTRG SLEEMPSVHH PFLNVFELER LLYTGKTACN
HADEVWPGLY LGDQDMANNR RELRRLGITH VLNASHNRWR GTPEAYEGLG IRYLGVEAHD
SPAFDMSIHF QTAADFIHRA LSQPGGKILV HCAVGVSRSA TLVLAYLMLY HHFTLVEAIK
KVKDHRGITP NRGFLRQLLA LDRRLRQGLE A
