DUS10_MOUSE
ID DUS10_MOUSE Reviewed; 483 AA.
AC Q9ESS0; Q8R3L3; Q9CZY9;
DT 09-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Dual specificity protein phosphatase 10;
DE EC=3.1.3.16 {ECO:0000250|UniProtKB:Q9Y6W6};
DE EC=3.1.3.48 {ECO:0000250|UniProtKB:Q9Y6W6};
DE AltName: Full=Mitogen-activated protein kinase phosphatase 5;
DE Short=MAP kinase phosphatase 5;
DE Short=MKP-5;
GN Name=Dusp10; Synonyms=Mkp5;
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].
RC STRAIN=C57BL/6J;
RX PubMed=11060451; DOI=10.1159/000015666;
RA Masuda K., Shima H., Kikuchi K., Watanabe Y., Matsuda Y.;
RT "Expression and comparative chromosomal mapping of MKP-5 genes
RT DUSP10/Dusp10.";
RL Cytogenet. Cell Genet. 90:71-74(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD;
RC TISSUE=Embryo, Kidney, Pancreas, Thymus, and Urinary bladder;
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 STRAIN=Czech II; 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).
CC -!- FUNCTION: Protein phosphatase involved in the inactivation of MAP
CC kinases. Has a specificity for the MAPK11/MAPK12/MAPK13/MAPK14
CC subfamily. It preferably dephosphorylates p38.
CC {ECO:0000250|UniProtKB:Q9Y6W6}.
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;
CC Evidence={ECO:0000250|UniProtKB:Q9Y6W6, 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 Evidence={ECO:0000250|UniProtKB:Q9Y6W6};
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 Evidence={ECO:0000250|UniProtKB:Q9Y6W6};
CC -!- SUBUNIT: Monomer. Interacts with MAPK14.
CC {ECO:0000250|UniProtKB:Q9Y6W6}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9Y6W6}. Nucleus
CC {ECO:0000250|UniProtKB:Q9Y6W6}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class dual specificity subfamily. {ECO:0000305}.
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DR EMBL; AB037908; BAB17680.1; -; mRNA.
DR EMBL; AK011995; BAB27966.1; -; mRNA.
DR EMBL; AK035293; BAC29019.1; -; mRNA.
DR EMBL; AK050528; BAC34308.1; -; mRNA.
DR EMBL; AK088024; BAC40102.1; -; mRNA.
DR EMBL; AK088186; BAC40196.1; -; mRNA.
DR EMBL; AK088357; BAC40300.1; -; mRNA.
DR EMBL; AK142568; BAE25109.1; -; mRNA.
DR EMBL; BC025066; AAH25066.1; -; mRNA.
DR CCDS; CCDS15591.1; -.
DR RefSeq; NP_071302.2; NM_022019.5.
DR RefSeq; XP_006497251.1; XM_006497188.2.
DR RefSeq; XP_006497252.1; XM_006497189.1.
DR AlphaFoldDB; Q9ESS0; -.
DR SMR; Q9ESS0; -.
DR BioGRID; 211005; 1.
DR IntAct; Q9ESS0; 1.
DR STRING; 10090.ENSMUSP00000045838; -.
DR iPTMnet; Q9ESS0; -.
DR PhosphoSitePlus; Q9ESS0; -.
DR MaxQB; Q9ESS0; -.
DR PaxDb; Q9ESS0; -.
DR PeptideAtlas; Q9ESS0; -.
DR PRIDE; Q9ESS0; -.
DR ProteomicsDB; 279488; -.
DR Antibodypedia; 20739; 373 antibodies from 36 providers.
DR DNASU; 63953; -.
DR Ensembl; ENSMUST00000048655; ENSMUSP00000045838; ENSMUSG00000039384.
DR GeneID; 63953; -.
DR KEGG; mmu:63953; -.
DR UCSC; uc007dym.1; mouse.
DR CTD; 11221; -.
DR MGI; MGI:1927070; Dusp10.
DR VEuPathDB; HostDB:ENSMUSG00000039384; -.
DR eggNOG; KOG1716; Eukaryota.
DR GeneTree; ENSGT00940000157671; -.
DR HOGENOM; CLU_027074_0_1_1; -.
DR InParanoid; Q9ESS0; -.
DR OMA; FIYKRLP; -.
DR OrthoDB; 1576308at2759; -.
DR PhylomeDB; Q9ESS0; -.
DR TreeFam; TF105122; -.
DR Reactome; R-MMU-112409; RAF-independent MAPK1/3 activation.
DR Reactome; R-MMU-5675221; Negative regulation of MAPK pathway.
DR BioGRID-ORCS; 63953; 3 hits in 72 CRISPR screens.
DR PRO; PR:Q9ESS0; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q9ESS0; protein.
DR Bgee; ENSMUSG00000039384; Expressed in temporalis muscle and 197 other tissues.
DR ExpressionAtlas; Q9ESS0; baseline and differential.
DR Genevisible; Q9ESS0; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0016607; C:nuclear speck; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0008432; F:JUN kinase binding; ISO:MGI.
DR GO; GO:0033549; F:MAP kinase phosphatase activity; IDA:BHF-UCL.
DR GO; GO:0017017; F:MAP kinase tyrosine/serine/threonine phosphatase activity; IBA:GO_Central.
DR GO; GO:0048273; F:mitogen-activated protein kinase p38 binding; ISO:MGI.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0016791; F:phosphatase activity; ISO:MGI.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; IBA:GO_Central.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0008330; F:protein tyrosine/threonine phosphatase activity; ISO:MGI.
DR GO; GO:0016311; P:dephosphorylation; ISO:MGI.
DR GO; GO:0010633; P:negative regulation of epithelial cell migration; IMP:BHF-UCL.
DR GO; GO:0050680; P:negative regulation of epithelial cell proliferation; IMP:BHF-UCL.
DR GO; GO:1905042; P:negative regulation of epithelium regeneration; IDA:BHF-UCL.
DR GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; IMP:BHF-UCL.
DR GO; GO:0046329; P:negative regulation of JNK cascade; IMP:MGI.
DR GO; GO:0043508; P:negative regulation of JUN kinase activity; IMP:MGI.
DR GO; GO:0043409; P:negative regulation of MAPK cascade; IBA:GO_Central.
DR GO; GO:0048715; P:negative regulation of oligodendrocyte differentiation; ISO:MGI.
DR GO; GO:1903753; P:negative regulation of p38MAPK cascade; ISO:MGI.
DR GO; GO:0044387; P:negative regulation of protein kinase activity by regulation of protein phosphorylation; IDA:MGI.
DR GO; GO:0060266; P:negative regulation of respiratory burst involved in inflammatory response; IMP:MGI.
DR GO; GO:0032873; P:negative regulation of stress-activated MAPK cascade; IMP:MGI.
DR GO; GO:0048709; P:oligodendrocyte differentiation; IMP:MGI.
DR GO; GO:0035970; P:peptidyl-threonine dephosphorylation; ISO:MGI.
DR GO; GO:1990264; P:peptidyl-tyrosine dephosphorylation involved in inactivation of protein kinase activity; ISO:MGI.
DR GO; GO:0045591; P:positive regulation of regulatory T cell differentiation; ISO:MGI.
DR GO; GO:0006470; P:protein dephosphorylation; IDA:BHF-UCL.
DR GO; GO:0002819; P:regulation of adaptive immune response; IMP:MGI.
DR GO; GO:0090335; P:regulation of brown fat cell differentiation; IDA:MGI.
DR GO; GO:0045088; P:regulation of innate immune response; IMP:MGI.
DR GO; GO:0032496; P:response to lipopolysaccharide; IMP:MGI.
DR GO; GO:0051403; P:stress-activated MAPK cascade; IMP:MGI.
DR Gene3D; 3.40.250.10; -; 1.
DR Gene3D; 3.90.190.10; -; 1.
DR InterPro; IPR000340; Dual-sp_phosphatase_cat-dom.
DR InterPro; IPR008343; MKP.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR001763; Rhodanese-like_dom.
DR InterPro; IPR036873; Rhodanese-like_dom_sf.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR InterPro; IPR020422; TYR_PHOSPHATASE_DUAL_dom.
DR Pfam; PF00782; DSPc; 1.
DR Pfam; PF00581; Rhodanese; 1.
DR PRINTS; PR01764; MAPKPHPHTASE.
DR SMART; SM00195; DSPc; 1.
DR SMART; SM00450; RHOD; 1.
DR SUPFAM; SSF52799; SSF52799; 1.
DR SUPFAM; SSF52821; SSF52821; 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 2: Evidence at transcript level;
KW Cytoplasm; Hydrolase; Nucleus; Protein phosphatase; Reference proteome.
FT CHAIN 1..483
FT /note="Dual specificity protein phosphatase 10"
FT /id="PRO_0000094814"
FT DOMAIN 169..286
FT /note="Rhodanese"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT DOMAIN 322..465
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT REGION 200..216
FT /note="Interaction with MAP kinases"
FT /evidence="ECO:0000250"
FT ACT_SITE 409
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT CONFLICT 48
FT /note="T -> A (in Ref. 1; BAB17680)"
FT /evidence="ECO:0000305"
FT CONFLICT 113
FT /note="P -> S (in Ref. 2; BAB27966)"
FT /evidence="ECO:0000305"
FT CONFLICT 386
FT /note="Q -> R (in Ref. 1; BAB17680)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 483 AA; 52532 MW; 7797A1877D986AA8 CRC64;
MPPSPLDDRV VVALSRPVRP QDLNLCLDSS YLGSASPGSG SHAPVLATAV VTLKAANLTY
MPSSSGSARS LNCGCSSTSC CTVATYDKDH QAQTQAIAAG TATTAIGTST TCPANQMVNN
NENTGSVLSP SGGVGSPVSG TPKQLASIKI IYPNDLAKKM TKCSKSHLPS QGPVIIDCRP
FMEYNKSHIQ GAVHINCADK ISRRRLQQGK ITVLDLISCR EGKDSFKRIF SKEIIVYDEN
TNEPSRVTPS QPLHIVLESL KREGKEPLVL KGGLSSFKQN HGNLCDNSLQ LQECREVGGG
ASAASSMLPQ SVPTTPDIEN AELTPILPFL FLGNEQDAQD LDTMQRLNIG YVINVTTHLP
LYHYEKGLFN YKRLPATDSN KQNLRQYFEE AFEFIEEAHQ CGKGLLIHCQ AGVSRSATIV
IAYLMKHTRM TMTDAYKFVK GKRPIISPNL NFMGQLLEFE EDLNNGVTPR ILTPKLMGME
TVV
