DUS10_HUMAN
ID DUS10_HUMAN Reviewed; 482 AA.
AC Q9Y6W6; D3DTB4; Q6GSI4; Q9H9Z5;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=Dual specificity protein phosphatase 10;
DE EC=3.1.3.16 {ECO:0000269|PubMed:16806267, ECO:0000269|PubMed:22375048};
DE EC=3.1.3.48 {ECO:0000269|PubMed:16806267, ECO:0000269|PubMed:22375048};
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 Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND FUNCTION.
RX PubMed=10391943; DOI=10.1074/jbc.274.28.19949;
RA Tanoue T., Moriguchi T., Nishida E.;
RT "Molecular cloning and characterization of a novel dual specificity
RT phosphatase, MKP-5.";
RL J. Biol. Chem. 274:19949-19956(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND FUNCTION.
RX PubMed=10597297; DOI=10.1038/sj.onc.1203185;
RA Theodosiou A., Smith A., Gillieron C., Arkinstall S., Ashworth A.;
RT "MKP5, a new member of the MAP kinase phosphatase family, which selectively
RT dephosphorylates stress-activated kinases.";
RL Oncogene 18:6981-6988(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, Lung, PNS, and Testis;
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 [7]
RP TISSUE SPECIFICITY.
RX PubMed=29043977; DOI=10.7554/elife.27356;
RA Mishra A., Oules B., Pisco A.O., Ly T., Liakath-Ali K., Walko G.,
RA Viswanathan P., Tihy M., Nijjher J., Dunn S.J., Lamond A.I., Watt F.M.;
RT "A protein phosphatase network controls the temporal and spatial dynamics
RT of differentiation commitment in human epidermis.";
RL Elife 6:0-0(2017).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 320-467, CATALYTIC ACTIVITY,
RP SUBUNIT, TISSUE SPECIFICITY, AND ACTIVE SITE.
RX PubMed=16806267; DOI=10.1016/j.jmb.2006.05.059;
RA Jeong D.G., Yoon T.S., Kim J.H., Shim M.Y., Jung S.K., Son J.H., Ryu S.E.,
RA Kim S.J.;
RT "Crystal structure of the catalytic domain of human MAP kinase phosphatase
RT 5: structural insight into constitutively active phosphatase.";
RL J. Mol. Biol. 360:946-955(2006).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 148-287, SUBUNIT, AND ACTIVE SITE.
RX PubMed=17400920; DOI=10.1110/ps.062712807;
RA Tao X., Tong L.;
RT "Crystal structure of the MAP kinase binding domain and the catalytic
RT domain of human MKP5.";
RL Protein Sci. 16:880-886(2007).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.71 ANGSTROMS) OF 139-288 IN COMPLEX WITH MAPK14,
RP FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH MAPK14, AND MUTAGENESIS OF
RP 180-PHE-MET-181 AND 203-ARG-ARG-204.
RX PubMed=22375048; DOI=10.1126/scisignal.2002241;
RA Zhang Y.Y., Wu J.W., Wang Z.X.;
RT "A distinct interaction mode revealed by the crystal structure of the
RT kinase p38alpha with the MAPK binding domain of the phosphatase MKP5.";
RL Sci. Signal. 4:RA88-RA88(2011).
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:0000269|PubMed:10391943, ECO:0000269|PubMed:10597297,
CC ECO:0000269|PubMed:22375048}.
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, ECO:0000269|PubMed:16806267,
CC ECO:0000269|PubMed:22375048};
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:0000269|PubMed:16806267, ECO:0000269|PubMed:22375048};
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:0000269|PubMed:16806267, ECO:0000269|PubMed:22375048};
CC -!- SUBUNIT: Monomer. Interacts with MAPK14. {ECO:0000269|PubMed:16806267,
CC ECO:0000269|PubMed:17400920, ECO:0000269|PubMed:22375048}.
CC -!- INTERACTION:
CC Q9Y6W6; Q86V38: ATN1; NbExp=3; IntAct=EBI-3443946, EBI-11954292;
CC Q9Y6W6; Q9Y5Z0: BACE2; NbExp=3; IntAct=EBI-3443946, EBI-11282723;
CC Q9Y6W6; P02489: CRYAA; NbExp=3; IntAct=EBI-3443946, EBI-6875961;
CC Q9Y6W6; Q14204: DYNC1H1; NbExp=3; IntAct=EBI-3443946, EBI-356015;
CC Q9Y6W6; P22607: FGFR3; NbExp=3; IntAct=EBI-3443946, EBI-348399;
CC Q9Y6W6; Q53EP0-3: FNDC3B; NbExp=3; IntAct=EBI-3443946, EBI-10242151;
CC Q9Y6W6; Q14957: GRIN2C; NbExp=3; IntAct=EBI-3443946, EBI-8285963;
CC Q9Y6W6; P06396: GSN; NbExp=3; IntAct=EBI-3443946, EBI-351506;
CC Q9Y6W6; P49639: HOXA1; NbExp=5; IntAct=EBI-3443946, EBI-740785;
CC Q9Y6W6; P01112: HRAS; NbExp=3; IntAct=EBI-3443946, EBI-350145;
CC Q9Y6W6; Q9BYR7: KRTAP3-2; NbExp=3; IntAct=EBI-3443946, EBI-751260;
CC Q9Y6W6; P45983-4: MAPK8; NbExp=3; IntAct=EBI-3443946, EBI-18121963;
CC Q9Y6W6; P45984: MAPK9; NbExp=5; IntAct=EBI-3443946, EBI-713568;
CC Q9Y6W6; Q9UMX0: UBQLN1; NbExp=3; IntAct=EBI-3443946, EBI-741480;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9Y6W6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Y6W6-2; Sequence=VSP_036549;
CC -!- TISSUE SPECIFICITY: Expressed in keratinocytes (at protein level)
CC (PubMed:29043977). Detected in brain (PubMed:16806267).
CC {ECO:0000269|PubMed:16806267, ECO:0000269|PubMed:29043977}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class dual specificity subfamily. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/DUSP10ID49913ch1q41.html";
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DR EMBL; AB026436; BAA81668.1; -; mRNA.
DR EMBL; AF179212; AAD51857.1; -; mRNA.
DR EMBL; AK022513; BAB14070.1; -; mRNA.
DR EMBL; AL590966; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471100; EAW93283.1; -; Genomic_DNA.
DR EMBL; CH471100; EAW93285.1; -; Genomic_DNA.
DR EMBL; CH471100; EAW93286.1; -; Genomic_DNA.
DR EMBL; CH471100; EAW93287.1; -; Genomic_DNA.
DR EMBL; BC020608; AAH20608.1; -; mRNA.
DR EMBL; BC031405; AAH31405.1; -; mRNA.
DR EMBL; BC063826; AAH63826.1; -; mRNA.
DR CCDS; CCDS1528.1; -. [Q9Y6W6-1]
DR RefSeq; NP_009138.1; NM_007207.5. [Q9Y6W6-1]
DR PDB; 1ZZW; X-ray; 1.60 A; A/B=320-467.
DR PDB; 2OUC; X-ray; 2.20 A; A/B=148-287.
DR PDB; 2OUD; X-ray; 2.80 A; A=315-482.
DR PDB; 3TG1; X-ray; 2.71 A; B=139-288.
DR PDB; 6MC1; X-ray; 2.70 A; A/B/C/D/E/F=320-467.
DR PDBsum; 1ZZW; -.
DR PDBsum; 2OUC; -.
DR PDBsum; 2OUD; -.
DR PDBsum; 3TG1; -.
DR PDBsum; 6MC1; -.
DR AlphaFoldDB; Q9Y6W6; -.
DR SMR; Q9Y6W6; -.
DR BioGRID; 116389; 69.
DR ELM; Q9Y6W6; -.
DR IntAct; Q9Y6W6; 33.
DR MINT; Q9Y6W6; -.
DR STRING; 9606.ENSP00000355866; -.
DR BindingDB; Q9Y6W6; -.
DR ChEMBL; CHEMBL2396511; -.
DR DEPOD; DUSP10; -.
DR iPTMnet; Q9Y6W6; -.
DR PhosphoSitePlus; Q9Y6W6; -.
DR BioMuta; DUSP10; -.
DR DMDM; 20138090; -.
DR MassIVE; Q9Y6W6; -.
DR PaxDb; Q9Y6W6; -.
DR PeptideAtlas; Q9Y6W6; -.
DR PRIDE; Q9Y6W6; -.
DR ProteomicsDB; 86803; -. [Q9Y6W6-1]
DR ProteomicsDB; 86804; -. [Q9Y6W6-2]
DR Antibodypedia; 20739; 373 antibodies from 36 providers.
DR DNASU; 11221; -.
DR Ensembl; ENST00000366899.4; ENSP00000355866.3; ENSG00000143507.18. [Q9Y6W6-1]
DR GeneID; 11221; -.
DR KEGG; hsa:11221; -.
DR MANE-Select; ENST00000366899.4; ENSP00000355866.3; NM_007207.6; NP_009138.1.
DR UCSC; uc001hmy.3; human. [Q9Y6W6-1]
DR CTD; 11221; -.
DR DisGeNET; 11221; -.
DR GeneCards; DUSP10; -.
DR HGNC; HGNC:3065; DUSP10.
DR HPA; ENSG00000143507; Tissue enhanced (liver).
DR MIM; 608867; gene.
DR neXtProt; NX_Q9Y6W6; -.
DR OpenTargets; ENSG00000143507; -.
DR PharmGKB; PA27520; -.
DR VEuPathDB; HostDB:ENSG00000143507; -.
DR eggNOG; KOG1716; Eukaryota.
DR GeneTree; ENSGT00940000157671; -.
DR HOGENOM; CLU_027074_0_1_1; -.
DR InParanoid; Q9Y6W6; -.
DR OMA; FIYKRLP; -.
DR OrthoDB; 1576308at2759; -.
DR PhylomeDB; Q9Y6W6; -.
DR TreeFam; TF105122; -.
DR BRENDA; 3.1.3.16; 2681.
DR BRENDA; 3.1.3.48; 2681.
DR PathwayCommons; Q9Y6W6; -.
DR Reactome; R-HSA-112409; RAF-independent MAPK1/3 activation.
DR Reactome; R-HSA-5675221; Negative regulation of MAPK pathway.
DR Reactome; R-HSA-9652817; Signaling by MAPK mutants.
DR SABIO-RK; Q9Y6W6; -.
DR SignaLink; Q9Y6W6; -.
DR SIGNOR; Q9Y6W6; -.
DR BioGRID-ORCS; 11221; 25 hits in 1088 CRISPR screens.
DR EvolutionaryTrace; Q9Y6W6; -.
DR GeneWiki; DUSP10; -.
DR GenomeRNAi; 11221; -.
DR Pharos; Q9Y6W6; Tbio.
DR PRO; PR:Q9Y6W6; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9Y6W6; protein.
DR Bgee; ENSG00000143507; Expressed in skeletal muscle tissue of rectus abdominis and 188 other tissues.
DR ExpressionAtlas; Q9Y6W6; baseline and differential.
DR Genevisible; Q9Y6W6; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0016607; C:nuclear speck; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
DR GO; GO:0008432; F:JUN kinase binding; IDA:BHF-UCL.
DR GO; GO:0033549; F:MAP kinase phosphatase activity; IDA:UniProtKB.
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; IPI:BHF-UCL.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0016791; F:phosphatase activity; IDA:UniProtKB.
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; IDA:BHF-UCL.
DR GO; GO:0016311; P:dephosphorylation; IDA:UniProtKB.
DR GO; GO:0030336; P:negative regulation of cell migration; NAS:BHF-UCL.
DR GO; GO:0010633; P:negative regulation of epithelial cell migration; ISS:BHF-UCL.
DR GO; GO:0050680; P:negative regulation of epithelial cell proliferation; ISS:BHF-UCL.
DR GO; GO:1905042; P:negative regulation of epithelium regeneration; ISS:BHF-UCL.
DR GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; ISS:BHF-UCL.
DR GO; GO:0046329; P:negative regulation of JNK cascade; IDA:BHF-UCL.
DR GO; GO:0043508; P:negative regulation of JUN kinase activity; IDA:BHF-UCL.
DR GO; GO:0043409; P:negative regulation of MAPK cascade; IBA:GO_Central.
DR GO; GO:0048715; P:negative regulation of oligodendrocyte differentiation; IEA:Ensembl.
DR GO; GO:1903753; P:negative regulation of p38MAPK cascade; IDA:BHF-UCL.
DR GO; GO:0044387; P:negative regulation of protein kinase activity by regulation of protein phosphorylation; IEA:Ensembl.
DR GO; GO:0060266; P:negative regulation of respiratory burst involved in inflammatory response; IEA:Ensembl.
DR GO; GO:0048709; P:oligodendrocyte differentiation; IEA:Ensembl.
DR GO; GO:0035970; P:peptidyl-threonine dephosphorylation; IDA:BHF-UCL.
DR GO; GO:1990264; P:peptidyl-tyrosine dephosphorylation involved in inactivation of protein kinase activity; IDA:BHF-UCL.
DR GO; GO:0045591; P:positive regulation of regulatory T cell differentiation; IMP:BHF-UCL.
DR GO; GO:0002819; P:regulation of adaptive immune response; IEA:Ensembl.
DR GO; GO:0090335; P:regulation of brown fat cell differentiation; IEA:Ensembl.
DR GO; GO:0032496; P:response to lipopolysaccharide; IEA:Ensembl.
DR GO; GO:0051403; P:stress-activated MAPK cascade; IEA:Ensembl.
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 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Hydrolase; Nucleus;
KW Protein phosphatase; Reference proteome.
FT CHAIN 1..482
FT /note="Dual specificity protein phosphatase 10"
FT /id="PRO_0000094813"
FT DOMAIN 168..285
FT /note="Rhodanese"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT DOMAIN 321..464
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT REGION 199..215
FT /note="Interaction with MAP kinases"
FT ACT_SITE 408
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160,
FT ECO:0000305|PubMed:16806267, ECO:0000305|PubMed:17400920"
FT VAR_SEQ 1..342
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_036549"
FT MUTAGEN 180..181
FT /note="FM->DD: Reduced enzyme activity with MAPK14."
FT /evidence="ECO:0000269|PubMed:22375048"
FT MUTAGEN 203..204
FT /note="RR->AA: Strongly reduced affinity for MAPK14. Almost
FT abolishes enzyme activity with MAPK14."
FT /evidence="ECO:0000269|PubMed:22375048"
FT HELIX 152..160
FT /evidence="ECO:0007829|PDB:2OUC"
FT STRAND 173..176
FT /evidence="ECO:0007829|PDB:2OUC"
FT HELIX 180..185
FT /evidence="ECO:0007829|PDB:2OUC"
FT STRAND 186..188
FT /evidence="ECO:0007829|PDB:2OUC"
FT HELIX 199..206
FT /evidence="ECO:0007829|PDB:2OUC"
FT HELIX 212..217
FT /evidence="ECO:0007829|PDB:2OUC"
FT HELIX 224..230
FT /evidence="ECO:0007829|PDB:2OUC"
FT STRAND 233..236
FT /evidence="ECO:0007829|PDB:2OUC"
FT HELIX 243..245
FT /evidence="ECO:0007829|PDB:2OUC"
FT STRAND 248..250
FT /evidence="ECO:0007829|PDB:3TG1"
FT HELIX 251..261
FT /evidence="ECO:0007829|PDB:2OUC"
FT STRAND 267..269
FT /evidence="ECO:0007829|PDB:2OUC"
FT HELIX 272..276
FT /evidence="ECO:0007829|PDB:2OUC"
FT TURN 277..279
FT /evidence="ECO:0007829|PDB:2OUC"
FT HELIX 281..283
FT /evidence="ECO:0007829|PDB:2OUC"
FT STRAND 284..286
FT /evidence="ECO:0007829|PDB:2OUC"
FT STRAND 323..326
FT /evidence="ECO:0007829|PDB:1ZZW"
FT STRAND 329..332
FT /evidence="ECO:0007829|PDB:1ZZW"
FT HELIX 336..338
FT /evidence="ECO:0007829|PDB:1ZZW"
FT HELIX 340..345
FT /evidence="ECO:0007829|PDB:1ZZW"
FT STRAND 348..353
FT /evidence="ECO:0007829|PDB:1ZZW"
FT STRAND 356..358
FT /evidence="ECO:0007829|PDB:1ZZW"
FT HELIX 363..365
FT /evidence="ECO:0007829|PDB:1ZZW"
FT STRAND 368..372
FT /evidence="ECO:0007829|PDB:1ZZW"
FT STRAND 378..380
FT /evidence="ECO:0007829|PDB:1ZZW"
FT HELIX 384..386
FT /evidence="ECO:0007829|PDB:1ZZW"
FT HELIX 387..399
FT /evidence="ECO:0007829|PDB:1ZZW"
FT STRAND 403..407
FT /evidence="ECO:0007829|PDB:1ZZW"
FT STRAND 409..413
FT /evidence="ECO:0007829|PDB:1ZZW"
FT HELIX 414..426
FT /evidence="ECO:0007829|PDB:1ZZW"
FT HELIX 431..441
FT /evidence="ECO:0007829|PDB:1ZZW"
FT HELIX 449..463
FT /evidence="ECO:0007829|PDB:1ZZW"
FT HELIX 478..482
FT /evidence="ECO:0007829|PDB:2OUD"
SQ SEQUENCE 482 AA; 52642 MW; A8CB74ABF9498CD4 CRC64;
MPPSPLDDRV VVALSRPVRP QDLNLCLDSS YLGSANPGSN SHPPVIATTV VSLKAANLTY
MPSSSGSARS LNCGCSSASC CTVATYDKDN QAQTQAIAAG TTTTAIGTST TCPANQMVNN
NENTGSLSPS SGVGSPVSGT PKQLASIKII YPNDLAKKMT KCSKSHLPSQ GPVIIDCRPF
MEYNKSHIQG AVHINCADKI SRRRLQQGKI TVLDLISCRE GKDSFKRIFS KEIIVYDENT
NEPSRVMPSQ PLHIVLESLK REGKEPLVLK GGLSSFKQNH ENLCDNSLQL QECREVGGGA
SAASSLLPQP IPTTPDIENA ELTPILPFLF LGNEQDAQDL DTMQRLNIGY VINVTTHLPL
YHYEKGLFNY KRLPATDSNK QNLRQYFEEA FEFIEEAHQC GKGLLIHCQA GVSRSATIVI
AYLMKHTRMT MTDAYKFVKG KRPIISPNLN FMGQLLEFEE DLNNGVTPRI LTPKLMGVET
VV
