DUS19_MOUSE
ID DUS19_MOUSE Reviewed; 220 AA.
AC Q8K4T5;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Dual specificity protein phosphatase 19;
DE EC=3.1.3.16 {ECO:0000250|UniProtKB:Q8WTR2};
DE EC=3.1.3.48 {ECO:0000250|UniProtKB:Q8WTR2};
DE AltName: Full=Protein phosphatase SKRP1;
DE AltName: Full=Stress-activated protein kinase pathway-regulating phosphatase 1;
GN Name=Dusp19 {ECO:0000312|MGI:MGI:1915332}; Synonyms=Skrp1;
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].
RX PubMed=11959861; DOI=10.1074/jbc.m200837200;
RA Zama T., Aoki R., Kamimoto T., Inoue K., Ikeda Y., Hagiwara M.;
RT "A novel dual specificity phosphatase SKRP1 interacts with the MAPK kinase
RT MKK7 and inactivates the JNK MAPK pathway. Implication for the precise
RT regulation of the particular MAPK pathway.";
RL J. Biol. Chem. 277:23909-23918(2002).
CC -!- FUNCTION: Has a dual specificity toward Ser/Thr and Tyr-containing
CC proteins. {ECO:0000250|UniProtKB:Q8WTR2}.
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:Q8WTR2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10685;
CC Evidence={ECO:0000250|UniProtKB:Q8WTR2};
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:Q8WTR2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20630;
CC Evidence={ECO:0000250|UniProtKB:Q8WTR2};
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:Q8WTR2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47005;
CC Evidence={ECO:0000250|UniProtKB:Q8WTR2};
CC -!- ACTIVITY REGULATION: Phosphatase activity is enhanced by Ca(2+) and
CC Mn(2+). {ECO:0000250|UniProtKB:Q8WTR2}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class dual specificity subfamily. {ECO:0000305}.
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DR EMBL; AB051896; BAC01163.1; -; mRNA.
DR CCDS; CCDS16178.1; -.
DR AlphaFoldDB; Q8K4T5; -.
DR SMR; Q8K4T5; -.
DR STRING; 10090.ENSMUSP00000028384; -.
DR PhosphoSitePlus; Q8K4T5; -.
DR EPD; Q8K4T5; -.
DR MaxQB; Q8K4T5; -.
DR PaxDb; Q8K4T5; -.
DR PRIDE; Q8K4T5; -.
DR ProteomicsDB; 277414; -.
DR MGI; MGI:1915332; Dusp19.
DR eggNOG; KOG1716; Eukaryota.
DR InParanoid; Q8K4T5; -.
DR PhylomeDB; Q8K4T5; -.
DR ChiTaRS; Dusp19; mouse.
DR PRO; PR:Q8K4T5; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q8K4T5; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0008579; F:JUN kinase phosphatase activity; IDA:MGI.
DR GO; GO:0005078; F:MAP-kinase scaffold activity; IDA:BHF-UCL.
DR GO; GO:0031434; F:mitogen-activated protein kinase kinase binding; IPI:BHF-UCL.
DR GO; GO:0031435; F:mitogen-activated protein kinase kinase kinase binding; IPI:BHF-UCL.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0030295; F:protein kinase activator activity; IDA:BHF-UCL.
DR GO; GO:0004860; F:protein kinase inhibitor activity; IDA:BHF-UCL.
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:0008330; F:protein tyrosine/threonine phosphatase activity; IDA:MGI.
DR GO; GO:0007254; P:JNK cascade; IDA:MGI.
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; IDA:MGI.
DR GO; GO:0006469; P:negative regulation of protein kinase activity; IDA:BHF-UCL.
DR GO; GO:0046330; P:positive regulation of JNK cascade; IDA:BHF-UCL.
DR GO; GO:0043507; P:positive regulation of JUN kinase activity; IDA:BHF-UCL.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; IDA:BHF-UCL.
DR GO; GO:0045860; P:positive regulation of protein kinase activity; IDA:BHF-UCL.
DR GO; GO:0006470; P:protein dephosphorylation; IDA:MGI.
DR GO; GO:0043405; P:regulation of MAP kinase activity; IBA:GO_Central.
DR Gene3D; 3.90.190.10; -; 1.
DR InterPro; IPR000340; Dual-sp_phosphatase_cat-dom.
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 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; Hydrolase; Protein phosphatase; Reference proteome.
FT CHAIN 1..220
FT /note="Dual specificity protein phosphatase 19"
FT /id="PRO_0000094833"
FT DOMAIN 64..205
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT ACT_SITE 149
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q8WTR2"
SQ SEQUENCE 220 AA; 24181 MW; 5977D907CA7D3EDD CRC64;
MHSLNQKIKA FSRDNLRKQC TRVTTLTGKK LIETWEDATV HVVETEPSGG GGCGYVQDLT
LDLQVGVIKP WLLLGSQDAA HDLELLRKHK VTHILNVAYG VENAFLSEFT YKTISILDVP
ETNILSYFPE CFEFIEQAKL KDGVVLVHCN AGVSRAAAIV IGFLMSSEEA TFTTALSLVK
EARPSICPNP GFMEQLRTYQ VGKESNGGDK VPAEDTTHGL
