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   04-NOV-2026, entry version 206.
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=O-phospho-L-tyrosyl-[protein] + H2O = L-tyrosyl-[protein] +
CC         phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC         COMP:20101, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858,
CC         ChEBI:CHEBI:61978; 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=O-phospho-L-seryl-[protein] + H2O = 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=O-phospho-L-threonyl-[protein] + H2O = 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   -!- PTM: 'Lys-48'-linked polyubiquitinated by NEURL3, leading to
CC       proteasomal degradation. {ECO:0000250|UniProtKB:Q91790}.
CC   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC       receptor class dual specificity subfamily. {ECO:0000305}.
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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   SMR; P28563; -.
DR   BioGRID; 202482; 3.
DR   DIP; DIP-29877N; -.
DR   IntAct; P28563; 1.
DR   STRING; 10090.ENSMUSP00000025025; -.
DR   BindingDB; P28563; -.
DR   ChEMBL; CHEMBL5623; -.
DR   iPTMnet; P28563; -.
DR   PhosphoSitePlus; P28563; -.
DR   PaxDb; 10090-ENSMUSP00000025025; -.
DR   ProteomicsDB; 277609; -.
DR   DNASU; 19252; -.
DR   Ensembl; ENSMPUT00000012855; ENSMPUP00000012651; ENSMPUG00000012746.
DR   Ensembl; ENSMUST00000025025.7; ENSMUSP00000025025.7; ENSMUSG00000024190.8.
DR   GeneID; 19252; -.
DR   KEGG; mmu:19252; -.
DR   UCSC; uc008bee.2; mouse.
DR   CTD; 1843; -.
DR   VEuPathDB; HostDB:ENSMUSG00000024190; -.
DR   AGR; MGI:105120; -.
DR   MGI; MGI:105120; Dusp1.
DR   eggNOG; KOG1716; Eukaryota.
DR   GeneTree; ENSGT00940000159044; -.
DR   HOGENOM; CLU_027074_0_2_1; -.
DR   InParanoid; P28563; -.
DR   OMA; AACSEFC; -.
DR   OrthoDB; 165342at2759; -.
DR   PhylomeDB; P28563; -.
DR   Reactome; R-MMU-112409; RAF-independent MAPK1/3 activation.
DR   Reactome; R-MMU-5675221; Negative regulation of MAPK pathway.
DR   PRO; PR:P28563; -.
DR   Bgee; ENSMUSG00000024190; Expressed in granulocyte and 280 other cell types or tissues.
DR   ExpressionAtlas; P28563; baseline and differential.
DR   CDD; cd14638; DSP_DUSP1; 1.
DR   CDD; cd01446; DSP_MapKP; 1.
DR   FunFam; 3.90.190.10:FF:000015; Dual specificity phosphatase 4; 1.
DR   FunFam; 3.40.250.10:FF:000026; Dual specificity protein phosphatase; 1.
DR   Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1.
DR   Gene3D; 3.40.250.10; Rhodanese-like domain; 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   PANTHER; PTHR10159; DUAL SPECIFICITY PROTEIN PHOSPHATASE; 1.
DR   PANTHER; PTHR10159:SF309; DUAL SPECIFICITY PROTEIN PHOSPHATASE 1; 1.
DR   Pfam; PF00782; DSPc; 1.
DR   Pfam; PF00581; Rhodanese; 1.
DR   PIRSF; PIRSF000939; MAPK_Ptase; 1.
DR   PRINTS; PR01908; ADSPHPHTASE.
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; (Phosphotyrosine protein) phosphatases II; 1.
DR   SUPFAM; SSF52821; Rhodanese/Cell cycle control phosphatase; 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.
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:GO_Central.
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: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:GO_Central.
DR   GO; GO:1990869; P:cellular response to chemokine; ISO:GO_Central.
DR   GO; GO:0032870; P:cellular response to hormone stimulus; IEA:Ensembl.
DR   GO; GO:0001706; P:endoderm formation; IBA:GO_Central.
DR   GO; GO:0070371; P:ERK1 and ERK2 cascade; ISO:GO_Central.
DR   GO; GO:0035556; P:intracellular signal transduction; ISO:GO_Central.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; ISO:GO_Central.
DR   GO; GO:0007162; P:negative regulation of cell adhesion; ISO:GO_Central.
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:GO_Central.
DR   GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; ISO:GO_Central.
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:GO_Central.
DR   GO; GO:1903753; P:negative regulation of p38MAPK cascade; ISO:GO_Central.
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:GO_Central.
DR   GO; GO:0006470; P:protein dephosphorylation; ISO:GO_Central.
DR   GO; GO:0090266; P:regulation of mitotic cell cycle spindle assembly checkpoint; ISS:UniProtKB.
DR   GO; GO:0051592; P:response to calcium ion; IEA:Ensembl.
DR   GO; GO:0051591; P:response to cAMP; IEA:Ensembl.
DR   GO; GO:0032355; P:response to estradiol; IEA:Ensembl.
DR   GO; GO:0051384; P:response to glucocorticoid; IEA:Ensembl.
DR   GO; GO:0042542; P:response to hydrogen peroxide; IEA:Ensembl.
DR   GO; GO:0009416; P:response to light stimulus; IEA:Ensembl.
DR   GO; GO:0032526; P:response to retinoic acid; IEA:Ensembl.
DR   GO; GO:0033574; P:response to testosterone; IEA:Ensembl.
DR   GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR   Proteomes; UP000000589; Chromosome 17.
DR   DrugCentral; P28563; -.
DR   Antibodypedia; 4343; 631 antibodies from 42 providers.
DR   RNAct; P28563; protein.
DR   BioGRID-ORCS; 19252; 3 hits in 79 CRISPR screens.
DR   AlphaFoldDB; P28563; -.
DR   FunCoup; P28563; 1689.
PE   1: Evidence at protein level;
KW   Cell cycle; Hydrolase; Nucleus; Phosphoprotein; Protein phosphatase;
KW   Reference proteome; Ubl conjugation.
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
//