DUS12_MOUSE
ID DUS12_MOUSE Reviewed; 339 AA.
AC Q9D0T2; Q9EQD3;
DT 09-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Dual specificity protein phosphatase 12;
DE EC=3.1.3.16 {ECO:0000250|UniProtKB:Q9JIM4};
DE EC=3.1.3.48 {ECO:0000250|UniProtKB:Q9JIM4};
DE AltName: Full=Dual specificity phosphatase T-DSP4;
DE AltName: Full=Dual specificity phosphatase VH1;
GN Name=Dusp12;
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 Aoyama K., Matsuda T., Aoki N.;
RT "Molecular cloning of putative dual specificity phosphatase T-DSP4.";
RL Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ;
RX PubMed=11130991; DOI=10.1007/s003350010198;
RA Zhang X.M., Dormady S.P., Chaung W., Basch R.S.;
RT "mVH1, a dual-specificity phosphatase whose expression is cell cycle
RT regulated.";
RL Mamm. Genome 11:1154-1156(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo;
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).
CC -!- FUNCTION: Dual specificity phosphatase; can dephosphorylate both
CC phosphotyrosine and phosphoserine or phosphothreonine residues. Can
CC dephosphorylate glucokinase (in vitro). Has phosphatase activity with
CC the synthetic substrate 6,8-difluoro-4-methylumbelliferyl phosphate and
CC other in vitro substrates. {ECO:0000250|UniProtKB:Q9JIM4}.
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:Q9JIM4};
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:Q9JIM4};
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:Q9JIM4};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250};
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q9UNI6}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9UNI6}.
CC Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9UNI6}. Note=Primarily
CC nuclear. Detected in a mesh-like pattern in the cytosol.
CC {ECO:0000250|UniProtKB:Q9UNI6}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class dual specificity subfamily. {ECO:0000305}.
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DR EMBL; AF280810; AAK69508.1; -; mRNA.
DR EMBL; AF268196; AAG44739.1; -; mRNA.
DR EMBL; AK004488; BAB23328.1; -; mRNA.
DR CCDS; CCDS15474.1; -.
DR RefSeq; NP_075662.2; NM_023173.2.
DR AlphaFoldDB; Q9D0T2; -.
DR SMR; Q9D0T2; -.
DR STRING; 10090.ENSMUSP00000027970; -.
DR PhosphoSitePlus; Q9D0T2; -.
DR EPD; Q9D0T2; -.
DR MaxQB; Q9D0T2; -.
DR PaxDb; Q9D0T2; -.
DR PRIDE; Q9D0T2; -.
DR ProteomicsDB; 277528; -.
DR Antibodypedia; 1653; 226 antibodies from 25 providers.
DR DNASU; 80915; -.
DR Ensembl; ENSMUST00000027970; ENSMUSP00000027970; ENSMUSG00000026659.
DR GeneID; 80915; -.
DR KEGG; mmu:80915; -.
DR UCSC; uc007dml.1; mouse.
DR CTD; 11266; -.
DR MGI; MGI:1890614; Dusp12.
DR VEuPathDB; HostDB:ENSMUSG00000026659; -.
DR eggNOG; KOG1716; Eukaryota.
DR GeneTree; ENSGT00930000151041; -.
DR HOGENOM; CLU_023312_1_0_1; -.
DR InParanoid; Q9D0T2; -.
DR OMA; RIMLNTQ; -.
DR OrthoDB; 1482182at2759; -.
DR PhylomeDB; Q9D0T2; -.
DR TreeFam; TF105123; -.
DR BioGRID-ORCS; 80915; 17 hits in 76 CRISPR screens.
DR ChiTaRS; Dusp12; mouse.
DR PRO; PR:Q9D0T2; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q9D0T2; protein.
DR Bgee; ENSMUSG00000026659; Expressed in primary oocyte and 254 other tissues.
DR ExpressionAtlas; Q9D0T2; baseline and differential.
DR Genevisible; Q9D0T2; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0019900; F:kinase 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; 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; IDA:MGI.
DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR GO; GO:0016311; P:dephosphorylation; ISO:MGI.
DR GO; GO:0033133; P:positive regulation of glucokinase activity; ISO:MGI.
DR GO; GO:0006470; P:protein dephosphorylation; ISO:MGI.
DR Gene3D; 3.90.190.10; -; 1.
DR InterPro; IPR000340; Dual-sp_phosphatase_cat-dom.
DR InterPro; IPR016278; DUSP12.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR InterPro; IPR020422; TYR_PHOSPHATASE_DUAL_dom.
DR Pfam; PF00782; DSPc; 1.
DR PIRSF; PIRSF000941; DUSP12; 1.
DR SMART; SM00195; DSPc; 1.
DR SUPFAM; SSF52799; SSF52799; 1.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR PROSITE; PS50054; TYR_PHOSPHATASE_DUAL; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Cytoplasm; Hydrolase; Metal-binding; Nucleus; Phosphoprotein;
KW Protein phosphatase; Reference proteome; Zinc.
FT CHAIN 1..339
FT /note="Dual specificity protein phosphatase 12"
FT /id="PRO_0000094819"
FT DOMAIN 26..170
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 114
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT BINDING 115..120
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9UNI6"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q9UNI6"
FT MOD_RES 334
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UNI6"
FT CONFLICT 7
FT /note="S -> T (in Ref. 2; AAG44739)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 339 AA; 37159 MW; B6A254D319BEC98F CRC64;
MLEAQGSNHG CERQAPTASP ASSAGHAVEV RPGLYLGGAA AVAEPGHLRE AGITAVLTVD
SEPAFPAGAG FEGLRSLFVP ALDKPETDLL SHLDRCVAFI GQARSEGRAV LVHCHAGVSR
SVAVVMAFIM KTDQLTFEKA YDILRTVKPE AKVNEGFEWQ LKLYEAMGYE VDTSSAFYKQ
YRLQKVTEKC PKLWNLPQEL FAVDPTTISQ GLKDDILYKC RKCRRSLFRH SSILGHSEGS
GPIAFAHKRT APSSVLTTGS QAQCTSYFIE PVQWMESTLL GVMDGQLLCP KCSAKLGSFN
WYGEQCSCGR WITPAFQIHK NRVDEMKMLP VLGSQTKKL
