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-APR-2013, entry version 94.
DE RecName: Full=Dual specificity protein phosphatase 10;
DE EC=3.1.3.16;
DE EC=3.1.3.48;
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;
OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC Muroidea; Muridae; Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6;
RX PubMed=11060451;
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.,
RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA 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.,
RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA 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
RT project: 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 (By similarity).
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 -!- SUBUNIT: Monomer. Interacts with MAPK14 (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By
CC similarity).
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.
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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 IPI; IPI00113513; -.
DR RefSeq; NP_071302.2; NM_022019.5.
DR UniGene; Mm.404024; -.
DR ProteinModelPortal; Q9ESS0; -.
DR SMR; Q9ESS0; 149-288, 322-468.
DR IntAct; Q9ESS0; 1.
DR STRING; 10090.ENSMUSP00000045838; -.
DR PaxDb; Q9ESS0; -.
DR PRIDE; Q9ESS0; -.
DR Ensembl; ENSMUST00000048655; ENSMUSP00000045838; ENSMUSG00000039384.
DR GeneID; 63953; -.
DR KEGG; mmu:63953; -.
DR CTD; 11221; -.
DR MGI; MGI:1927070; Dusp10.
DR eggNOG; COG2453; -.
DR GeneTree; ENSGT00700000104093; -.
DR HOGENOM; HOG000069871; -.
DR HOVERGEN; HBG102158; -.
DR InParanoid; Q8R3L3; -.
DR KO; K04459; -.
DR OMA; NEHDAQD; -.
DR OrthoDB; EOG4W0XD5; -.
DR NextBio; 319811; -.
DR ArrayExpress; Q9ESS0; -.
DR Bgee; Q9ESS0; -.
DR CleanEx; MM_DUSP10; -.
DR Genevestigator; Q9ESS0; -.
DR GermOnline; ENSMUSG00000039384; Mus musculus.
DR GO; GO:0005737; C:cytoplasm; IBA:RefGenome.
DR GO; GO:0005794; C:Golgi apparatus; IEA:Compara.
DR GO; GO:0005634; C:nucleus; IBA:RefGenome.
DR GO; GO:0017017; F:MAP kinase tyrosine/serine/threonine phosphatase activity; IBA:RefGenome.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:EC.
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:0060266; P:negative regulation of respiratory burst involved in inflammatory response; IMP:MGI.
DR GO; GO:0035335; P:peptidyl-tyrosine dephosphorylation; IEA:GOC.
DR GO; GO:0002819; P:regulation of adaptive immune response; IMP:MGI.
DR GO; GO:0032496; P:response to lipopolysaccharide; IMP:MGI.
DR Gene3D; 3.40.250.10; -; 1.
DR InterPro; IPR020417; Atypical_DUSP.
DR InterPro; IPR000340; Dual-sp_phosphatase_cat-dom.
DR InterPro; IPR020422; Dual-sp_phosphatase_subgr_cat.
DR InterPro; IPR024950; DUSP.
DR InterPro; IPR008343; MKP.
DR InterPro; IPR001763; Rhodanese-like_dom.
DR InterPro; IPR000387; Tyr/Dual-sp_Pase.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR PANTHER; PTHR10159; PTHR10159; 1.
DR Pfam; PF00782; DSPc; 1.
DR Pfam; PF00581; Rhodanese; 1.
DR PRINTS; PR01908; ADSPHPHTASE.
DR PRINTS; PR01764; MAPKPHPHTASE.
DR SMART; SM00195; DSPc; 1.
DR SMART; SM00450; RHOD; 1.
DR SUPFAM; SSF52821; Rhodanese-like; 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 Complete proteome; Cytoplasm; Hydrolase; Nucleus; Protein phosphatase;
KW Reference proteome.
FT CHAIN 1 483 Dual specificity protein phosphatase 10.
FT /FTId=PRO_0000094814.
FT DOMAIN 169 286 Rhodanese.
FT DOMAIN 386 456 Tyrosine-protein phosphatase.
FT REGION 200 216 Interaction with MAP kinases (By
FT similarity).
FT ACT_SITE 409 409 Phosphocysteine intermediate (By
FT similarity).
FT CONFLICT 48 48 T -> A (in Ref. 1; BAB17680).
FT CONFLICT 113 113 P -> S (in Ref. 2; BAB27966).
FT CONFLICT 386 386 Q -> R (in Ref. 1; BAB17680).
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
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