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P28563 (DUS1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 132. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:Dusp1
Synonyms:3ch134, Mkp1, Ptpn10, Ptpn16
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length367 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 activity

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.

[a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate.

Subcellular location

Nucleus By similarity.

Induction

By growth factors.

Post-translational modification

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

Sequence similarities

Belongs to the protein-tyrosine phosphatase family. Non-receptor class dual specificity subfamily.

Contains 1 rhodanese domain.

Contains 1 tyrosine-protein phosphatase domain.

Ontologies

Keywords
   Biological processCell cycle
   Cellular componentNucleus
   Molecular functionHydrolase
Protein phosphatase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcellular response to hormone stimulus

Inferred from electronic annotation. Source: Ensembl

endoderm formation

Inferred from Biological aspect of Ancestor. Source: RefGenome

inactivation of MAPK activity

Inferred from sequence or structural similarity. Source: UniProtKB

intracellular signal transduction

Inferred from electronic annotation. Source: Ensembl

mitotic cell cycle arrest

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of MAP kinase activity

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of MAPK cascade

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of apoptotic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of meiotic cell cycle

Inferred from sequence or structural similarity. Source: UniProtKB

peptidyl-threonine dephosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

peptidyl-tyrosine dephosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of apoptotic process

Inferred from electronic annotation. Source: Ensembl

protein dephosphorylation

Inferred from Biological aspect of Ancestor. Source: RefGenome

regulation of apoptotic process

Inferred from Biological aspect of Ancestor. Source: RefGenome

regulation of mitotic cell cycle spindle assembly checkpoint

Inferred from sequence or structural similarity. Source: UniProtKB

response to cAMP

Inferred from electronic annotation. Source: Ensembl

response to calcium ion

Inferred from electronic annotation. Source: Ensembl

response to estradiol

Inferred from electronic annotation. Source: Ensembl

response to glucocorticoid

Inferred from electronic annotation. Source: Ensembl

response to hydrogen peroxide

Inferred from electronic annotation. Source: Ensembl

response to light stimulus

Inferred from electronic annotation. Source: Ensembl

response to retinoic acid

Inferred from electronic annotation. Source: Ensembl

response to testosterone

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

nucleoplasm

Inferred from Biological aspect of Ancestor. Source: RefGenome

nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionMAP kinase tyrosine/serine/threonine phosphatase activity

Inferred from sequence or structural similarity. Source: UniProtKB

protein tyrosine phosphatase activity

Inferred from electronic annotation. Source: UniProtKB-EC

protein tyrosine/threonine phosphatase activity

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 367367Dual specificity protein phosphatase 1
PRO_0000094791

Regions

Domain20 – 137118Rhodanese
Domain175 – 367193Tyrosine-protein phosphatase

Sites

Active site2581Phosphocysteine intermediate

Amino acid modifications

Modified residue3591Phosphoserine; by MAPK1 and MAPK3 Ref.5
Modified residue3641Phosphoserine; by MAPK1 and MAPK3 Ref.5

Experimental info

Mutagenesis2581C → S: Loss of activity.

Sequences

Sequence LengthMass (Da)Tools
P28563 [UniParc].

Last modified December 1, 1992. Version 1.
Checksum: 50B5F90FEBBD19AB

FASTA36739,370
        10         20         30         40         50         60 
MVMEVGILDA GGLRALLREG AAQCLLLDCR SFFAFNAGHI AGSVNVRFST IVRRRAKGAM 

        70         80         90        100        110        120 
GLEHIVPNAE LRGRLLAGAY HAVVLLDERS ASLDGAKRDG TLALAAGALC REARSTQVFF 

       130        140        150        160        170        180 
LQGGYEAFSA SCPELCSKQS TPTGLSLPLS TSVPDSAESG CSSCSTPLYD QGGPVEILSF 

       190        200        210        220        230        240 
LYLGSAYHAS RKDMLDALGI TALINVSANC PNHFEGHYQY KSIPVEDNHK ADISSWFNEA 

       250        260        270        280        290        300 
IDFIDSIKDA GGRVFVHCQA GISRSATICL AYLMRTNRVK LDEAFEFVKQ RRSIISPNFS 

       310        320        330        340        350        360 
FMGQLLQFES QVLAPHCSAE AGSPAMAVLD RGTSTTTVFN FPVSIPVHPT NSALNYLKSP 


ITTSPSC 

« Hide

References

« Hide 'large scale' references
[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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X61940 mRNA. Translation: CAA43944.1.
S64851 Genomic DNA. Translation: AAB27882.1.
BC006967 mRNA. Translation: AAH06967.1.
PIRS24411. A54681.
RefSeqNP_038670.1. NM_013642.3.
UniGeneMm.239041.

3D structure databases

ProteinModelPortalP28563.
SMRP28563. Positions 13-136, 172-314.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid202482. 3 interactions.
DIPDIP-29877N.
STRING10090.ENSMUSP00000025025.

Chemistry

BindingDBP28563.
ChEMBLCHEMBL5623.

PTM databases

PhosphoSiteP28563.

Proteomic databases

PRIDEP28563.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000025025; ENSMUSP00000025025; ENSMUSG00000024190.
GeneID19252.
KEGGmmu:19252.
UCSCuc008bee.2. mouse.

Organism-specific databases

CTD1843.
MGIMGI:105120. Dusp1.

Phylogenomic databases

eggNOGCOG2453.
HOGENOMHOG000294080.
HOVERGENHBG007347.
InParanoidP28563.
KOK04459.
OMASFNSSHI.
OrthoDBEOG75MVWD.
PhylomeDBP28563.
TreeFamTF105122.

Gene expression databases

ArrayExpressP28563.
BgeeP28563.
CleanExMM_DUSP1.
GenevestigatorP28563.

Family and domain databases

Gene3D3.40.250.10. 1 hit.
InterProIPR020417. Atypical_DUSP.
IPR020420. Atypical_DUSP_famB.
IPR000340. Dual-sp_phosphatase_cat-dom.
IPR020422. Dual-sp_phosphatase_subgr_cat.
IPR024950. DUSP.
IPR008343. MKP.
IPR001763. Rhodanese-like_dom.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
[Graphical view]
PANTHERPTHR10159. PTHR10159. 1 hit.
PfamPF00782. DSPc. 1 hit.
PF00581. Rhodanese. 1 hit.
[Graphical view]
PIRSFPIRSF000939. MAPK_Ptase. 1 hit.
PRINTSPR01908. ADSPHPHTASE.
PR01910. ADSPHPHTASEB.
PR01764. MAPKPHPHTASE.
SMARTSM00195. DSPc. 1 hit.
SM00450. RHOD. 1 hit.
[Graphical view]
SUPFAMSSF52821. SSF52821. 1 hit.
PROSITEPS50206. RHODANESE_3. 1 hit.
PS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50054. TYR_PHOSPHATASE_DUAL. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio296092.
PROP28563.
SOURCESearch...

Entry information

Entry nameDUS1_MOUSE
AccessionPrimary (citable) accession number: P28563
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: December 1, 1992
Last modified: April 16, 2014
This is version 132 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot