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Q64623 (DUS1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 118. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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 CL100
Protein-tyrosine phosphatase non-receptor type 16
Gene names
Name:Dusp1
Synonyms:Cl100, Mkp1, Ptpn16
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

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 By similarity.

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.

Tissue specificity

Brain. High level expression seen in the cingulate gyrus within the retrospinal cortex, ventral and medial divisions of the anterior thalamus and the medial geniculate nucleus. Expressed at moderate levels in the parietal and temporal cortex. Expressed in the cerebellum. Ref.3 Ref.4 Ref.5

Induction

Exhibits night/day variations with a 100-fold increased expression at night in the pineal gland (at protein level). Up-regulation is due to a large degree to the release of norepinephrine from nerve terminals in the pineal gland and cAMP signaling pathway. Ref.4 Ref.5

Post-translational modification

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

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 expression pattern PubMed 15358679. Source: RGD

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 direct assay Ref.2. Source: RGD

mitotic cell cycle arrest

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of DNA biosynthetic process

Inferred from direct assay PubMed 10446064. Source: RGD

negative regulation of ERK1 and ERK2 cascade

Inferred from mutant phenotype PubMed 17437549. Source: RGD

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 mutant phenotype PubMed 15059639. Source: RGD

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 mutant phenotype PubMed 9228085. Source: RGD

protein dephosphorylation

Inferred from direct assay PubMed 12435803. Source: RGD

regulation of mitotic cell cycle spindle assembly checkpoint

Inferred from sequence or structural similarity. Source: UniProtKB

response to cAMP

Inferred from expression pattern PubMed 15358679. Source: RGD

response to calcium ion

Inferred from expression pattern Ref.2. Source: RGD

response to estradiol

Inferred from expression pattern PubMed 8804359. Source: RGD

response to glucocorticoid

Inferred from expression pattern PubMed 17403137. Source: RGD

response to hydrogen peroxide

Inferred from expression pattern PubMed 7540516. Source: RGD

response to light stimulus

Inferred from expression pattern Ref.4. Source: RGD

response to organic substance

Inferred from expression pattern PubMed 11027531. Source: RGD

response to retinoic acid

Inferred from expression pattern PubMed 15494319. Source: RGD

response to testosterone

Inferred from expression pattern PubMed 8804359. Source: RGD

   Cellular_componentcytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

nucleus

Inferred from direct assay PubMed 8883936. Source: RGD

   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/serine/threonine phosphatase activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

protein tyrosine/threonine phosphatase activity

Inferred from direct assay PubMed 12435803. Source: RGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 367367Dual specificity protein phosphatase 1
PRO_0000094792

Regions

Domain20 – 137118Rhodanese
Domain175 – 367193Tyrosine-protein phosphatase

Sites

Active site2581Phosphocysteine intermediate By similarity

Amino acid modifications

Modified residue3591Phosphoserine; by MAPK1 and MAPK3 By similarity
Modified residue3641Phosphoserine; by MAPK1 and MAPK3 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q64623 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 5112ADF290499139

FASTA36739,541
        10         20         30         40         50         60 
MVMEVGILDA GGLRALLRER AAQCLLLDCR SFFAFNAGHI VGSVNVRFST IVRRRAKGAM 

        70         80         90        100        110        120 
GLEHIVPNTE LRGRLLAGAY HAVVLLDERS AALDGAKRDG TLALAAGALC REARSTQVFF 

       130        140        150        160        170        180 
LQGGYEAFSA SCPELCSKQS TPMGLSLPLS 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 NSALNYLQSP 


ITTSPSC 

« Hide

References

[1]"Pathways regulating CL100 gene expression in pituitary cells."
Muda M., Schlegel W., Arkinstall S.
Submitted (JAN-1995) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Sprague-Dawley.
Tissue: Lung.
[2]"MAP kinase phosphatase-1 gene transcription in rat neuroendocrine cells is modulated by a calcium-sensitive block to elongation in the first exon."
Ryser S., Tortola S., van Haasteren G., Muda M., Li S., Schlegel W.
J. Biol. Chem. 276:33319-33327(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: Wistar Furth.
[3]"Isolation and characterization of a human dual specificity protein-tyrosine phosphatase gene."
Kwak S.P., Hakes D.J., Martell K.J., Dixon J.E.
J. Biol. Chem. 269:3596-3604(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[4]"Mitogen-activated protein kinase phosphatase-1 (MKP-1): >100-fold nocturnal and norepinephrine-induced changes in the rat pineal gland."
Price D.M., Chik C.L., Terriff D., Weller J., Humphries A., Carter D.A., Klein D.C., Ho A.K.
FEBS Lett. 577:220-226(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY, INDUCTION.
[5]"Night/day changes in pineal expression of >600 genes: central role of adrenergic/cAMP signaling."
Bailey M.J., Coon S.L., Carter D.A., Humphries A., Kim J.S., Shi Q., Gaildrat P., Morin F., Ganguly S., Hogenesch J.B., Weller J.L., Rath M.F., Moller M., Baler R., Sugden D., Rangel Z.G., Munson P.J., Klein D.C.
J. Biol. Chem. 284:7606-7622(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY, INDUCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X84004 mRNA. Translation: CAA58828.1.
AF357203 Genomic DNA. Translation: AAK55327.1.
PIRS52265.
RefSeqNP_446221.2. NM_053769.3.
UniGeneRn.98260.

3D structure databases

ProteinModelPortalQ64623.
SMRQ64623. Positions 171-313.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid250421. 1 interaction.

Proteomic databases

PRIDEQ64623.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000005383; ENSRNOP00000005383; ENSRNOG00000003977.
GeneID114856.
KEGGrno:114856.
UCSCRGD:620897. rat.

Organism-specific databases

CTD1843.
RGD620897. Dusp1.

Phylogenomic databases

eggNOGCOG2453.
GeneTreeENSGT00700000104321.
HOGENOMHOG000294080.
HOVERGENHBG007347.
InParanoidQ64623.
KOK04459.
OMASFNSSHI.
OrthoDBEOG75MVWD.
PhylomeDBQ64623.
TreeFamTF105122.

Gene expression databases

GenevestigatorQ64623.

Family and domain databases

Gene3D3.40.250.10. 1 hit.
3.90.190.10. 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.
IPR029021. Prot-tyrosine_phosphatase-like.
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]
SUPFAMSSF52799. SSF52799. 1 hit.
SSF52821. 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

NextBio618903.
PROQ64623.

Entry information

Entry nameDUS1_RAT
AccessionPrimary (citable) accession number: Q64623
Secondary accession number(s): Q548G6
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: July 9, 2014
This is version 118 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