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P28562 (DUS1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 141. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·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):
Dual specificity protein phosphatase hVH1
Mitogen-activated protein kinase phosphatase 1
Short name=MAP kinase phosphatase 1
Short name=MKP-1
Protein-tyrosine phosphatase CL100
Gene names
Name:DUSP1
Synonyms:CL100, MKP1, PTPN10, VH1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

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

Expressed at high levels in the lung, liver placenta and pancreas. Moderate levels seen in the heart and skeletal muscle. Lower levels found in the brain and kidney. Ref.2

Induction

By oxidative stress and heat shock.

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
Stress response
   Cellular componentNucleus
   Coding sequence diversityPolymorphism
   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 direct assay PubMed 7593328. 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 oxidative stress

Traceable author statement Ref.1. Source: ProtInc

response to retinoic acid

Inferred from electronic annotation. Source: Ensembl

response to testosterone

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcytoplasm

Inferred from direct assay PubMed 7593328. Source: UniProtKB

nucleoplasm

Inferred from Biological aspect of Ancestor. Source: RefGenome

nucleus

Inferred from direct assay PubMed 7593328. Source: UniProtKB

   Molecular_functionMAP kinase tyrosine/serine/threonine phosphatase activity

Inferred from sequence or structural similarity. Source: UniProtKB

non-membrane spanning protein tyrosine phosphatase activity

Traceable author statement Ref.1. Source: ProtInc

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_0000094790

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

Natural variations

Natural variant561A → T. Ref.3
Corresponds to variant rs34013988 [ dbSNP | Ensembl ].
VAR_025201
Natural variant1871Y → H. Ref.3
Corresponds to variant rs34471628 [ dbSNP | Ensembl ].
VAR_025202

Sequences

Sequence LengthMass (Da)Tools
P28562 [UniParc].

Last modified February 1, 1996. Version 3.
Checksum: 11BD1D39A9FCD51F

FASTA36739,298
        10         20         30         40         50         60 
MVMEVGTLDA GGLRALLGER AAQCLLLDCR SFFAFNAGHI AGSVNVRFST IVRRRAKGAM 

        70         80         90        100        110        120 
GLEHIVPNAE LRGRLLAGAY HAVVLLDERS AALDGAKRDG TLALAAGALC REARAAQVFF 

       130        140        150        160        170        180 
LKGGYEAFSA SCPELCSKQS TPMGLSLPLS TSVPDSAESG CSSCSTPLYD QGGPVEILPF 

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

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

       310        320        330        340        350        360 
FMGQLLQFES QVLAPHCSAE AGSPAMAVLD RGTSTTTVFN FPVSIPVHST NSALSYLQSP 


ITTSPSC 

« Hide

References

« Hide 'large scale' references
[1]"Oxidative stress and heat shock induce a human gene encoding a protein-tyrosine phosphatase."
Keyes S.M., Emslie E.A.
Nature 359:644-647(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Foreskin.
[2]"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: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
[3]NIEHS SNPs program
Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS THR-56 AND HIS-187.
[4]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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].
Tissue: Brain.
[6]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X68277 mRNA. Translation: CAA48338.1.
DQ301957 Genomic DNA. Translation: ABB96250.1.
CH471062 Genomic DNA. Translation: EAW61425.1.
CH471062 Genomic DNA. Translation: EAW61426.1.
BC022463 mRNA. Translation: AAH22463.1.
PIRS29090.
RefSeqNP_004408.1. NM_004417.3.
UniGeneHs.171695.

3D structure databases

ProteinModelPortalP28562.
SMRP28562. Positions 13-136, 172-314.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108176. 16 interactions.
IntActP28562. 14 interactions.
MINTMINT-8217028.
STRING9606.ENSP00000239223.

Chemistry

BindingDBP28562.
ChEMBLCHEMBL6026.

PTM databases

PhosphoSiteP28562.

Polymorphism databases

DMDM1346900.

Proteomic databases

PaxDbP28562.
PRIDEP28562.

Protocols and materials databases

DNASU1843.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000239223; ENSP00000239223; ENSG00000120129.
GeneID1843.
KEGGhsa:1843.
UCSCuc003mbv.2. human.

Organism-specific databases

CTD1843.
GeneCardsGC05M172195.
HGNCHGNC:3064. DUSP1.
HPACAB018554.
MIM600714. gene.
neXtProtNX_P28562.
PharmGKBPA27519.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2453.
HOGENOMHOG000294080.
HOVERGENHBG007347.
InParanoidP28562.
KOK04459.
OMASFNSSHI.
OrthoDBEOG75MVWD.
PhylomeDBP28562.
TreeFamTF105122.

Enzyme and pathway databases

SABIO-RKP28562.
SignaLinkP28562.

Gene expression databases

ArrayExpressP28562.
BgeeP28562.
CleanExHS_DUSP1.
GenevestigatorP28562.

Family and domain databases

Gene3D3.40.250.10. 1 hit.
InterProIPR020417. Atypical_DUSP.
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.
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

ChiTaRSDUSP1. human.
GeneWikiDUSP1.
GenomeRNAi1843.
NextBio7547.
PROP28562.
SOURCESearch...

Entry information

Entry nameDUS1_HUMAN
AccessionPrimary (citable) accession number: P28562
Secondary accession number(s): D3DQL9, Q2V508
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: February 1, 1996
Last modified: April 16, 2014
This is version 141 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 5

Human chromosome 5: entries, gene names and cross-references to MIM