DUS14_MOUSE
ID DUS14_MOUSE Reviewed; 198 AA.
AC Q9JLY7; Q9D715;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2002, sequence version 2.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Dual specificity protein phosphatase 14;
DE EC=3.1.3.16;
DE EC=3.1.3.48;
DE AltName: Full=Mitogen-activated protein kinase phosphatase 6;
DE Short=MAP kinase phosphatase 6;
DE Short=MKP-6;
GN Name=Dusp14; Synonyms=Mkp6;
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=BALB/cJ;
RX PubMed=11123293; DOI=10.4049/jimmunol.166.1.197;
RA Marti F., Krause A., Post N.H., Lyddane C., Dupont B., Sadelain M.,
RA King P.D.;
RT "Negative-feedback regulation of CD28 costimulation by a novel mitogen-
RT activated protein kinase phosphatase, MKP6.";
RL J. Immunol. 166:197-206(2001).
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].
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: Involved in the inactivation of MAP kinases. Dephosphorylates
CC ERK, JNK and p38 MAP-kinases.
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 -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class dual specificity subfamily. {ECO:0000305}.
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DR EMBL; AF120113; AAF28862.1; -; mRNA.
DR EMBL; AK009744; BAB26474.1; -; mRNA.
DR EMBL; BC002130; AAH02130.1; -; mRNA.
DR CCDS; CCDS25182.1; -.
DR RefSeq; NP_062793.2; NM_019819.3.
DR RefSeq; XP_006533859.1; XM_006533796.3.
DR RefSeq; XP_006533860.1; XM_006533797.3.
DR RefSeq; XP_006533861.1; XM_006533798.3.
DR RefSeq; XP_006533862.1; XM_006533799.3.
DR AlphaFoldDB; Q9JLY7; -.
DR SMR; Q9JLY7; -.
DR BioGRID; 207957; 29.
DR STRING; 10090.ENSMUSP00000098271; -.
DR iPTMnet; Q9JLY7; -.
DR PhosphoSitePlus; Q9JLY7; -.
DR MaxQB; Q9JLY7; -.
DR PaxDb; Q9JLY7; -.
DR PRIDE; Q9JLY7; -.
DR ProteomicsDB; 275410; -.
DR Antibodypedia; 73139; 350 antibodies from 34 providers.
DR DNASU; 56405; -.
DR Ensembl; ENSMUST00000018792; ENSMUSP00000018792; ENSMUSG00000018648.
DR Ensembl; ENSMUST00000100705; ENSMUSP00000098271; ENSMUSG00000018648.
DR Ensembl; ENSMUST00000108101; ENSMUSP00000103736; ENSMUSG00000018648.
DR Ensembl; ENSMUST00000164891; ENSMUSP00000130624; ENSMUSG00000018648.
DR GeneID; 56405; -.
DR KEGG; mmu:56405; -.
DR UCSC; uc007kqc.1; mouse.
DR CTD; 11072; -.
DR MGI; MGI:1927168; Dusp14.
DR VEuPathDB; HostDB:ENSMUSG00000018648; -.
DR eggNOG; KOG1718; Eukaryota.
DR GeneTree; ENSGT00940000160675; -.
DR HOGENOM; CLU_027074_3_2_1; -.
DR InParanoid; Q9JLY7; -.
DR OMA; IPDVYDR; -.
DR OrthoDB; 1576308at2759; -.
DR PhylomeDB; Q9JLY7; -.
DR TreeFam; TF316009; -.
DR BioGRID-ORCS; 56405; 3 hits in 74 CRISPR screens.
DR ChiTaRS; Dusp14; mouse.
DR PRO; PR:Q9JLY7; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q9JLY7; protein.
DR Bgee; ENSMUSG00000018648; Expressed in animal zygote and 206 other tissues.
DR ExpressionAtlas; Q9JLY7; baseline and differential.
DR Genevisible; Q9JLY7; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:MGI.
DR GO; GO:0005634; C:nucleus; ISS:MGI.
DR GO; GO:0017017; F:MAP kinase tyrosine/serine/threonine phosphatase activity; IEA:InterPro.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0006470; P:protein dephosphorylation; IEA:InterPro.
DR Gene3D; 3.90.190.10; -; 1.
DR InterPro; IPR020420; Atypical_DUSP_subfamB.
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 Pfam; PF00782; DSPc; 1.
DR PRINTS; PR01910; ADSPHPHTASEB.
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 Hydrolase; Protein phosphatase; Reference proteome.
FT CHAIN 1..198
FT /note="Dual specificity protein phosphatase 14"
FT /id="PRO_0000094823"
FT DOMAIN 26..167
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT ACT_SITE 111
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT CONFLICT 38
FT /note="R -> K (in Ref. 1; AAF28862)"
FT /evidence="ECO:0000305"
FT CONFLICT 150
FT /note="P -> H (in Ref. 1; AAF28862)"
FT /evidence="ECO:0000305"
FT CONFLICT 160
FT /note="D -> E (in Ref. 1; AAF28862)"
FT /evidence="ECO:0000305"
FT CONFLICT 163
FT /note="S -> R (in Ref. 1; AAF28862)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 198 AA; 22311 MW; 5C2B4210E886DFCF CRC64;
MSSRGHSTLP RTLMAPRMIS EGDIGGIAQI TSSLFLGRAS VASNWHLLQA RGITCVINAT
IEIPNFNWPQ FEYVKVPLAD IPHAPIRLYF DTVADKIHSV SKKHGATLVH CAAGVSRSAT
LCIAYLMKFH NLCLLEAYNW VKARRPVIRP NLGFWRQLID YESQLFGKSS VKMVQTPYGI
IPDVYEKESR HLMPYWGI
