DUS1_MOUSE
ID DUS1_MOUSE Reviewed; 367 AA.
AC P28563;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=Dual specificity protein phosphatase 1 {ECO:0000305};
DE EC=3.1.3.16 {ECO:0000269|PubMed:8221888, ECO:0000269|PubMed:8355678};
DE EC=3.1.3.48 {ECO:0000269|PubMed:8221888, ECO:0000269|PubMed:8355678};
DE AltName: Full=Mitogen-activated protein kinase phosphatase 1 {ECO:0000303|PubMed:8221888};
DE Short=MAP kinase phosphatase 1 {ECO:0000303|PubMed:8221888};
DE Short=MKP-1 {ECO:0000303|PubMed:8221888};
DE AltName: Full=Protein-tyrosine phosphatase 3CH134 {ECO:0000303|PubMed:1741163};
DE AltName: Full=Protein-tyrosine phosphatase ERP {ECO:0000303|PubMed:8355678};
GN Name=Dusp1 {ECO:0000312|MGI:MGI:105120};
GN Synonyms=3ch134 {ECO:0000303|PubMed:1741163}, Mkp1, Ptpn10, Ptpn16;
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], AND INDUCTION.
RC STRAIN=BALB/cJ;
RX PubMed=1741163;
RA Charles C.H., Abler A.S., Lau L.F.;
RT "cDNA sequence of a growth factor-inducible immediate early gene and
RT characterization of its encoded protein.";
RL Oncogene 7:187-190(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], CATALYTIC ACTIVITY, DEVELOPMENTAL STAGE,
RP INDUCTION, AND MUTAGENESIS OF 257-HIS--ARG-264.
RC TISSUE=Liver;
RX PubMed=8355678; DOI=10.1128/mcb.13.9.5195-5205.1993;
RA Noguchi T., Metz R., Chen L., Mattei M.-G., Carrasco D., Bravo R.;
RT "Structure, mapping, and expression of erp, a growth factor-inducible gene
RT encoding a nontransmembrane protein tyrosine phosphatase, and effect of ERP
RT on cell growth.";
RL Mol. Cell. Biol. 13:5195-5205(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II; TISSUE=Mammary gland;
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 [4]
RP FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF CYS-258, AND ACTIVE SITE.
RX PubMed=8221888; DOI=10.1016/0092-8674(93)90383-2;
RA Sun H., Charles C.H., Lau L.F., Tonks N.K.;
RT "MKP-1 (3CH134), an immediate early gene product, is a dual specificity
RT phosphatase that dephosphorylates MAP kinase in vivo.";
RL Cell 75:487-493(1993).
RN [5]
RP PHOSPHORYLATION AT SER-359 AND SER-364.
RX PubMed=10617468; DOI=10.1126/science.286.5449.2514;
RA Brondello J.M., Pouyssegur J., McKenzie F.R.;
RT "Reduced MAP kinase phosphatase-1 degradation after p42/p44MAPK-dependent
RT phosphorylation.";
RL Science 286:2514-2517(1999).
CC -!- FUNCTION: Dual specificity phosphatase that dephosphorylates MAP kinase
CC MAPK1/ERK2 on both 'Thr-183' and 'Tyr-185', regulating its activity
CC during the meiotic cell cycle. {ECO:0000269|PubMed:8221888}.
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:8221888,
CC ECO:0000269|PubMed:8355678};
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; Evidence={ECO:0000269|PubMed:8221888,
CC ECO:0000269|PubMed:8355678};
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; Evidence={ECO:0000269|PubMed:8221888,
CC ECO:0000269|PubMed:8355678};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q91790}.
CC -!- DEVELOPMENTAL STAGE: Expression in lung increases after birth.
CC {ECO:0000269|PubMed:8355678}.
CC -!- INDUCTION: Up-regulated by growth factors and mitogens.
CC {ECO:0000269|PubMed:1741163, ECO:0000269|PubMed:8355678}.
CC -!- PTM: Phosphorylation at Ser-359 and Ser-364 by MAPK1/ERK2 and
CC MAPK3/ERK1 reduces its rate of degradation.
CC {ECO:0000269|PubMed:10617468}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class dual specificity subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X61940; CAA43944.1; -; mRNA.
DR EMBL; S64851; AAB27882.1; -; Genomic_DNA.
DR EMBL; BC006967; AAH06967.1; -; mRNA.
DR CCDS; CCDS28552.1; -.
DR PIR; A54681; S24411.
DR RefSeq; NP_038670.1; NM_013642.3.
DR AlphaFoldDB; P28563; -.
DR SMR; P28563; -.
DR BioGRID; 202482; 2.
DR DIP; DIP-29877N; -.
DR IntAct; P28563; 1.
DR STRING; 10090.ENSMUSP00000025025; -.
DR BindingDB; P28563; -.
DR ChEMBL; CHEMBL5623; -.
DR DrugCentral; P28563; -.
DR iPTMnet; P28563; -.
DR PhosphoSitePlus; P28563; -.
DR PaxDb; P28563; -.
DR PRIDE; P28563; -.
DR ProteomicsDB; 277609; -.
DR Antibodypedia; 4343; 597 antibodies from 39 providers.
DR DNASU; 19252; -.
DR Ensembl; ENSMUST00000025025; ENSMUSP00000025025; ENSMUSG00000024190.
DR GeneID; 19252; -.
DR KEGG; mmu:19252; -.
DR UCSC; uc008bee.2; mouse.
DR CTD; 1843; -.
DR MGI; MGI:105120; Dusp1.
DR VEuPathDB; HostDB:ENSMUSG00000024190; -.
DR eggNOG; KOG1716; Eukaryota.
DR GeneTree; ENSGT00940000159044; -.
DR HOGENOM; CLU_027074_0_2_1; -.
DR InParanoid; P28563; -.
DR OMA; PSCSPCN; -.
DR OrthoDB; 1576308at2759; -.
DR PhylomeDB; P28563; -.
DR TreeFam; TF105122; -.
DR Reactome; R-MMU-112409; RAF-independent MAPK1/3 activation.
DR Reactome; R-MMU-5675221; Negative regulation of MAPK pathway.
DR BioGRID-ORCS; 19252; 3 hits in 74 CRISPR screens.
DR ChiTaRS; Dusp1; mouse.
DR PRO; PR:P28563; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; P28563; protein.
DR Bgee; ENSMUSG00000024190; Expressed in granulocyte and 276 other tissues.
DR ExpressionAtlas; P28563; baseline and differential.
DR Genevisible; P28563; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0019838; F:growth factor binding; ISO:MGI.
DR GO; GO:0017017; F:MAP kinase tyrosine/serine/threonine phosphatase activity; IMP:UniProtKB.
DR GO; GO:0051019; F:mitogen-activated protein kinase binding; IDA:UniProtKB.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; IBA:GO_Central.
DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; IMP:UniProtKB.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IMP:UniProtKB.
DR GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; ISO:MGI.
DR GO; GO:0008330; F:protein tyrosine/threonine phosphatase activity; ISO:MGI.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:1990869; P:cellular response to chemokine; ISO:MGI.
DR GO; GO:0001706; P:endoderm formation; IBA:GO_Central.
DR GO; GO:0035556; P:intracellular signal transduction; ISO:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
DR GO; GO:0007162; P:negative regulation of cell adhesion; ISO:MGI.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IMP:UniProtKB.
DR GO; GO:2000279; P:negative regulation of DNA biosynthetic process; ISO:MGI.
DR GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; ISO:MGI.
DR GO; GO:0043407; P:negative regulation of MAP kinase activity; ISS:UniProtKB.
DR GO; GO:0043409; P:negative regulation of MAPK cascade; IMP:UniProtKB.
DR GO; GO:0051447; P:negative regulation of meiotic cell cycle; ISS:UniProtKB.
DR GO; GO:0090027; P:negative regulation of monocyte chemotaxis; ISO:MGI.
DR GO; GO:1903753; P:negative regulation of p38MAPK cascade; ISO:MGI.
DR GO; GO:0070262; P:peptidyl-serine dephosphorylation; IMP:UniProtKB.
DR GO; GO:0035970; P:peptidyl-threonine dephosphorylation; IMP:UniProtKB.
DR GO; GO:0035335; P:peptidyl-tyrosine dephosphorylation; IMP:UniProtKB.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISO:MGI.
DR GO; GO:0006470; P:protein dephosphorylation; ISO:MGI.
DR GO; GO:0090266; P:regulation of mitotic cell cycle spindle assembly checkpoint; ISS:UniProtKB.
DR Gene3D; 3.40.250.10; -; 1.
DR Gene3D; 3.90.190.10; -; 1.
DR InterPro; IPR020420; Atypical_DUSP_subfamB.
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; IPR003595; Tyr_Pase_cat.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR InterPro; IPR020422; TYR_PHOSPHATASE_DUAL_dom.
DR Pfam; PF00782; DSPc; 1.
DR Pfam; PF00581; Rhodanese; 1.
DR PIRSF; PIRSF000939; MAPK_Ptase; 1.
DR PRINTS; PR01910; ADSPHPHTASEB.
DR PRINTS; PR01764; MAPKPHPHTASE.
DR SMART; SM00195; DSPc; 1.
DR SMART; SM00404; PTPc_motif; 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 Cell cycle; Hydrolase; Nucleus; Phosphoprotein; Protein phosphatase;
KW Reference proteome.
FT CHAIN 1..367
FT /note="Dual specificity protein phosphatase 1"
FT /id="PRO_0000094791"
FT DOMAIN 20..137
FT /note="Rhodanese"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT DOMAIN 173..314
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT ACT_SITE 258
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160,
FT ECO:0000269|PubMed:8221888"
FT MOD_RES 359
FT /note="Phosphoserine; by MAPK1 and MAPK3"
FT /evidence="ECO:0000269|PubMed:10617468"
FT MOD_RES 364
FT /note="Phosphoserine; by MAPK1 and MAPK3"
FT /evidence="ECO:0000269|PubMed:10617468"
FT MUTAGEN 257..264
FT /note="Missing: Loss of phosphatase activity."
FT /evidence="ECO:0000269|PubMed:8355678"
FT MUTAGEN 258
FT /note="C->S: Loss of phosphatase activity."
FT /evidence="ECO:0000269|PubMed:8221888"
SQ SEQUENCE 367 AA; 39370 MW; 50B5F90FEBBD19AB CRC64;
MVMEVGILDA GGLRALLREG AAQCLLLDCR SFFAFNAGHI AGSVNVRFST IVRRRAKGAM
GLEHIVPNAE LRGRLLAGAY HAVVLLDERS ASLDGAKRDG TLALAAGALC REARSTQVFF
LQGGYEAFSA SCPELCSKQS TPTGLSLPLS TSVPDSAESG CSSCSTPLYD QGGPVEILSF
LYLGSAYHAS RKDMLDALGI TALINVSANC PNHFEGHYQY KSIPVEDNHK ADISSWFNEA
IDFIDSIKDA GGRVFVHCQA GISRSATICL AYLMRTNRVK LDEAFEFVKQ RRSIISPNFS
FMGQLLQFES QVLAPHCSAE AGSPAMAVLD RGTSTTTVFN FPVSIPVHPT NSALNYLKSP
ITTSPSC
