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Protein

Dual specificity protein phosphatase 1

Gene

Dusp1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Dual specificity phosphatase that dephosphorylates MAP kinase MAPK1/ERK2 on both 'Thr-183' and 'Tyr-185', regulating its activity during the meiotic cell cycle.

Catalytic activityi

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.PROSITE-ProRule annotation
[a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei258 – 2581Phosphocysteine intermediate

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Keywords - Biological processi

Cell cycle

Names & Taxonomyi

Protein namesi
Recommended name:
Dual specificity protein phosphatase 1 (EC:3.1.3.16, EC:3.1.3.48)
Alternative name(s):
Mitogen-activated protein kinase phosphatase 1
Short name:
MAP kinase phosphatase 1
Short name:
MKP-1
Protein-tyrosine phosphatase 3CH134
Protein-tyrosine phosphatase ERP
Gene namesi
Name:Dusp1
Synonyms:3ch134, Mkp1, Ptpn10, Ptpn16
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 17

Organism-specific databases

MGIiMGI:105120. Dusp1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi258 – 2581C → S: Loss of activity.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 367367Dual specificity protein phosphatase 1PRO_0000094791Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei359 – 3591Phosphoserine; by MAPK1 and MAPK31 Publication
Modified residuei364 – 3641Phosphoserine; by MAPK1 and MAPK31 Publication

Post-translational modificationi

Phosphorylation at Ser-359 and Ser-364 by MAPK1/ERK2 and MAPK3/ERK1 reduces its rate of degradation.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PRIDEiP28563.

PTM databases

PhosphoSiteiP28563.

Expressioni

Inductioni

By growth factors.

Gene expression databases

BgeeiP28563.
CleanExiMM_DUSP1.
ExpressionAtlasiP28563. baseline and differential.
GenevisibleiP28563. MM.

Interactioni

Protein-protein interaction databases

BioGridi202482. 3 interactions.
DIPiDIP-29877N.
STRINGi10090.ENSMUSP00000025025.

Structurei

3D structure databases

ProteinModelPortaliP28563.
SMRiP28563. Positions 13-136, 172-314.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini20 – 137118RhodanesePROSITE-ProRule annotationAdd
BLAST
Domaini175 – 367193Tyrosine-protein phosphataseAdd
BLAST

Sequence similaritiesi

Contains 1 rhodanese domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG2453.
GeneTreeiENSGT00760000118902.
HOGENOMiHOG000294080.
HOVERGENiHBG007347.
InParanoidiP28563.
KOiK04459.
OMAiMVIMEVP.
OrthoDBiEOG75MVWD.
PhylomeDBiP28563.
TreeFamiTF105122.

Family and domain databases

Gene3Di3.40.250.10. 1 hit.
3.90.190.10. 1 hit.
InterProiIPR020417. Atypical_DUSP.
IPR020420. Atypical_DUSP_famB.
IPR000340. Dual-sp_phosphatase_cat-dom.
IPR020422. Dual-sp_phosphatase_subgr_cat.
IPR024950. DUSP.
IPR008343. MKP.
IPR029021. Prot-tyrosine_phosphatase-like.
IPR001763. Rhodanese-like_dom.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
[Graphical view]
PANTHERiPTHR10159. PTHR10159. 1 hit.
PfamiPF00782. DSPc. 1 hit.
PF00581. Rhodanese. 1 hit.
[Graphical view]
PIRSFiPIRSF000939. MAPK_Ptase. 1 hit.
PRINTSiPR01908. ADSPHPHTASE.
PR01910. ADSPHPHTASEB.
PR01764. MAPKPHPHTASE.
SMARTiSM00195. DSPc. 1 hit.
SM00450. RHOD. 1 hit.
[Graphical view]
SUPFAMiSSF52799. SSF52799. 1 hit.
SSF52821. SSF52821. 1 hit.
PROSITEiPS50206. RHODANESE_3. 1 hit.
PS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50054. TYR_PHOSPHATASE_DUAL. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P28563-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVMEVGILDA GGLRALLREG AAQCLLLDCR SFFAFNAGHI AGSVNVRFST
60 70 80 90 100
IVRRRAKGAM GLEHIVPNAE LRGRLLAGAY HAVVLLDERS ASLDGAKRDG
110 120 130 140 150
TLALAAGALC REARSTQVFF LQGGYEAFSA SCPELCSKQS TPTGLSLPLS
160 170 180 190 200
TSVPDSAESG CSSCSTPLYD QGGPVEILSF LYLGSAYHAS RKDMLDALGI
210 220 230 240 250
TALINVSANC PNHFEGHYQY KSIPVEDNHK ADISSWFNEA IDFIDSIKDA
260 270 280 290 300
GGRVFVHCQA GISRSATICL AYLMRTNRVK LDEAFEFVKQ RRSIISPNFS
310 320 330 340 350
FMGQLLQFES QVLAPHCSAE AGSPAMAVLD RGTSTTTVFN FPVSIPVHPT
360
NSALNYLKSP ITTSPSC
Length:367
Mass (Da):39,370
Last modified:December 1, 1992 - v1
Checksum:i50B5F90FEBBD19AB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X61940 mRNA. Translation: CAA43944.1.
S64851 Genomic DNA. Translation: AAB27882.1.
BC006967 mRNA. Translation: AAH06967.1.
CCDSiCCDS28552.1.
PIRiA54681. S24411.
RefSeqiNP_038670.1. NM_013642.3.
UniGeneiMm.239041.

Genome annotation databases

EnsembliENSMUST00000025025; ENSMUSP00000025025; ENSMUSG00000024190.
GeneIDi19252.
KEGGimmu:19252.
UCSCiuc008bee.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X61940 mRNA. Translation: CAA43944.1.
S64851 Genomic DNA. Translation: AAB27882.1.
BC006967 mRNA. Translation: AAH06967.1.
CCDSiCCDS28552.1.
PIRiA54681. S24411.
RefSeqiNP_038670.1. NM_013642.3.
UniGeneiMm.239041.

3D structure databases

ProteinModelPortaliP28563.
SMRiP28563. Positions 13-136, 172-314.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi202482. 3 interactions.
DIPiDIP-29877N.
STRINGi10090.ENSMUSP00000025025.

Chemistry

BindingDBiP28563.
ChEMBLiCHEMBL5623.

PTM databases

PhosphoSiteiP28563.

Proteomic databases

PRIDEiP28563.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000025025; ENSMUSP00000025025; ENSMUSG00000024190.
GeneIDi19252.
KEGGimmu:19252.
UCSCiuc008bee.2. mouse.

Organism-specific databases

CTDi1843.
MGIiMGI:105120. Dusp1.

Phylogenomic databases

eggNOGiCOG2453.
GeneTreeiENSGT00760000118902.
HOGENOMiHOG000294080.
HOVERGENiHBG007347.
InParanoidiP28563.
KOiK04459.
OMAiMVIMEVP.
OrthoDBiEOG75MVWD.
PhylomeDBiP28563.
TreeFamiTF105122.

Miscellaneous databases

NextBioi296092.
PROiP28563.
SOURCEiSearch...

Gene expression databases

BgeeiP28563.
CleanExiMM_DUSP1.
ExpressionAtlasiP28563. baseline and differential.
GenevisibleiP28563. MM.

Family and domain databases

Gene3Di3.40.250.10. 1 hit.
3.90.190.10. 1 hit.
InterProiIPR020417. Atypical_DUSP.
IPR020420. Atypical_DUSP_famB.
IPR000340. Dual-sp_phosphatase_cat-dom.
IPR020422. Dual-sp_phosphatase_subgr_cat.
IPR024950. DUSP.
IPR008343. MKP.
IPR029021. Prot-tyrosine_phosphatase-like.
IPR001763. Rhodanese-like_dom.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
[Graphical view]
PANTHERiPTHR10159. PTHR10159. 1 hit.
PfamiPF00782. DSPc. 1 hit.
PF00581. Rhodanese. 1 hit.
[Graphical view]
PIRSFiPIRSF000939. MAPK_Ptase. 1 hit.
PRINTSiPR01908. ADSPHPHTASE.
PR01910. ADSPHPHTASEB.
PR01764. MAPKPHPHTASE.
SMARTiSM00195. DSPc. 1 hit.
SM00450. RHOD. 1 hit.
[Graphical view]
SUPFAMiSSF52799. SSF52799. 1 hit.
SSF52821. SSF52821. 1 hit.
PROSITEiPS50206. RHODANESE_3. 1 hit.
PS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50054. TYR_PHOSPHATASE_DUAL. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "cDNA sequence of a growth factor-inducible immediate early gene and characterization of its encoded protein."
    Charles C.H., Abler A.S., Lau L.F.
    Oncogene 7:187-190(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: BALB/c.
  2. "Structure, mapping, and expression of erp, a growth factor-inducible gene encoding a nontransmembrane protein tyrosine phosphatase, and effect of ERP on cell growth."
    Noguchi T., Metz R., Chen L., Mattei M.-G., Carrasco D., Bravo R.
    Mol. Cell. Biol. 13:5195-5205(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Tissue: Liver.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Czech II.
    Tissue: Mammary gland.
  4. "MKP-1 (3CH134), an immediate early gene product, is a dual specificity phosphatase that dephosphorylates MAP kinase in vivo."
    Sun H., Charles C.H., Lau L.F., Tonks N.K.
    Cell 75:487-493(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  5. "Reduced MAP kinase phosphatase-1 degradation after p42/p44MAPK-dependent phosphorylation."
    Brondello J.M., Pouyssegur J., McKenzie F.R.
    Science 286:2514-2517(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-359 AND SER-364.

Entry informationi

Entry nameiDUS1_MOUSE
AccessioniPrimary (citable) accession number: P28563
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: December 1, 1992
Last modified: July 22, 2015
This is version 141 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.