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P51452 (DUS3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 133. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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 3

EC=3.1.3.16
EC=3.1.3.48
Alternative name(s):
Dual specificity protein phosphatase VHR
Vaccinia H1-related phosphatase
Short name=VHR
Gene names
Name:DUSP3
Synonyms:VHR
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length185 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Shows activity both for tyrosine-protein phosphate and serine-protein phosphate, but displays a strong preference toward phosphotyrosines. Specifically dephosphorylates and inactivates ERK1 and ERK2. Ref.5 Ref.8

Catalytic activity

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.

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

Subunit structure

Interacts with VRK3, which seems to activate it's phosphatase activity By similarity.

Subcellular location

Nucleus Ref.5.

Sequence similarities

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

Contains 1 tyrosine-protein phosphatase domain.

Ontologies

Keywords
   Cellular componentNucleus
   Molecular functionHydrolase
Protein phosphatase
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processMyD88-dependent toll-like receptor signaling pathway

Traceable author statement. Source: Reactome

MyD88-independent toll-like receptor signaling pathway

Traceable author statement. Source: Reactome

TRIF-dependent toll-like receptor signaling pathway

Traceable author statement. Source: Reactome

in utero embryonic development

Inferred from electronic annotation. Source: Ensembl

inactivation of MAPK activity

Inferred from mutant phenotype PubMed 16604064. Source: UniProtKB

innate immune response

Traceable author statement. Source: Reactome

negative regulation of ERK1 and ERK2 cascade

Inferred from direct assay PubMed 11085983. Source: UniProtKB

negative regulation of JNK cascade

Inferred from direct assay PubMed 11085983. Source: UniProtKB

negative regulation of MAPK cascade

Inferred from mutant phenotype PubMed 16604064. Source: UniProtKB

negative regulation of T cell activation

Inferred from direct assay PubMed 12447358. Source: UniProtKB

negative regulation of T cell receptor signaling pathway

Inferred from direct assay PubMed 12447358. Source: UniProtKB

neurotrophin TRK receptor signaling pathway

Traceable author statement. Source: Reactome

peptidyl-tyrosine dephosphorylation

Inferred from direct assay Ref.8PubMed 7876121. Source: UniProtKB

positive regulation of mitotic cell cycle

Inferred from mutant phenotype PubMed 16604064. Source: UniProtKB

stress-activated MAPK cascade

Traceable author statement. Source: Reactome

toll-like receptor 10 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor 2 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor 3 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor 4 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor 5 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor 9 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor TLR1:TLR2 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor TLR6:TLR2 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor signaling pathway

Traceable author statement. Source: Reactome

   Cellular_componentcytosol

Inferred from direct assay PubMed 12447358PubMed 18505570. Source: UniProtKB

immunological synapse

Inferred from direct assay PubMed 12447358. Source: UniProtKB

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay PubMed 16604064. Source: UniProtKB

   Molecular_functionMAP kinase phosphatase activity

Inferred from mutant phenotype PubMed 16604064. Source: UniProtKB

protein tyrosine phosphatase activity

Inferred from direct assay Ref.8. Source: UniProtKB

protein tyrosine/serine/threonine phosphatase activity

Inferred from direct assay PubMed 7876121. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 185185Dual specificity protein phosphatase 3
PRO_0000094795

Regions

Domain99 – 16971Tyrosine-protein phosphatase

Sites

Active site1241Phosphocysteine intermediate

Secondary structure

................................... 185
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P51452 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: C1045DD9B226FD94

FASTA18520,478
        10         20         30         40         50         60 
MSGSFELSVQ DLNDLLSDGS GCYSLPSQPC NEVTPRIYVG NASVAQDIPK LQKLGITHVL 

        70         80         90        100        110        120 
NAAEGRSFMH VNTNANFYKD SGITYLGIKA NDTQEFNLSA YFERAADFID QALAQKNGRV 

       130        140        150        160        170        180 
LVHCREGYSR SPTLVIAYLM MRQKMDVKSA LSIVRQNREI GPNDGFLAQL CQLNDRLAKE 


GKLKP 

« Hide

References

« Hide 'large scale' references
[1]"Expression cloning of a human dual-specificity phosphatase."
Ishibashi T., Bottaro D.P., Chan A., Miki T., Aaronson S.A.
Proc. Natl. Acad. Sci. U.S.A. 89:12170-12174(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]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].
[4]"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: Uterus.
[5]"Extracellular regulated kinases (ERK) 1 and ERK2 are authentic substrates for the dual-specificity protein-tyrosine phosphatase VHR. A novel role in down-regulating the ERK pathway."
Todd J.L., Tanner K.G., Denu J.M.
J. Biol. Chem. 274:13271-13280(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[6]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[7]"Crystal structure of the dual specificity protein phosphatase VHR."
Yuvaniyama J., Denu J.M., Dixon J.E., Saper M.A.
Science 272:1328-1331(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
[8]"Structural basis for the recognition of a bisphosphorylated MAP kinase peptide by human VHR protein Phosphatase."
Schumacher M.A., Todd J.L., Rice A.E., Tanner K.G., Denu J.M.
Biochemistry 41:3009-3017(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF 2-185, FUNCTION.
[9]"Multidentate small-molecule inhibitors of vaccinia H1-related (VHR) phosphatase decrease proliferation of cervix cancer cells."
Wu S., Vossius S., Rahmouni S., Miletic A.V., Vang T., Vazquez-Rodriguez J., Cerignoli F., Arimura Y., Williams S., Hayes T., Moutschen M., Vasile S., Pellecchia M., Mustelin T., Tautz L.
J. Med. Chem. 52:6716-6723(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 3-185.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L05147 mRNA. Translation: AAA35777.1.
BT019522 mRNA. Translation: AAV38329.1.
CH471178 Genomic DNA. Translation: EAW51667.1.
CH471178 Genomic DNA. Translation: EAW51668.1.
BC002682 mRNA. Translation: AAH02682.1.
PIRA47196.
RefSeqNP_004081.1. NM_004090.3.
UniGeneHs.181046.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1J4XX-ray2.75A2-185[»]
1VHRX-ray2.10A/B2-185[»]
3F81X-ray1.90A/B3-185[»]
ProteinModelPortalP51452.
SMRP51452. Positions 7-185.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108178. 9 interactions.
IntActP51452. 5 interactions.
MINTMINT-5001069.
STRING9606.ENSP00000226004.

Chemistry

BindingDBP51452.
ChEMBLCHEMBL2635.

PTM databases

PhosphoSiteP51452.

Polymorphism databases

DMDM1718191.

2D gel databases

UCD-2DPAGEP51452.

Proteomic databases

PaxDbP51452.
PRIDEP51452.

Protocols and materials databases

DNASU1845.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000226004; ENSP00000226004; ENSG00000108861.
GeneID1845.
KEGGhsa:1845.
UCSCuc002ied.4. human.

Organism-specific databases

CTD1845.
GeneCardsGC17M041856.
H-InvDBHIX0013868.
HGNCHGNC:3069. DUSP3.
HPACAB025265.
MIM600183. gene.
neXtProtNX_P51452.
PharmGKBPA27526.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2453.
HOGENOMHOG000233767.
HOVERGENHBG001524.
InParanoidP51452.
KOK17614.
OMATSANFYK.
OrthoDBEOG7CZK7N.
PhylomeDBP51452.
TreeFamTF105128.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_6782. TRAF6 Mediated Induction of proinflammatory cytokines.
REACT_6900. Immune System.
SignaLinkP51452.

Gene expression databases

ArrayExpressP51452.
BgeeP51452.
CleanExHS_DUSP3.
GenevestigatorP51452.

Family and domain databases

InterProIPR020417. Atypical_DUSP.
IPR020405. Atypical_DUSP_famA.
IPR000340. Dual-sp_phosphatase_cat-dom.
IPR020422. Dual-sp_phosphatase_subgr_cat.
IPR024950. DUSP.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
[Graphical view]
PANTHERPTHR10159. PTHR10159. 1 hit.
PfamPF00782. DSPc. 1 hit.
[Graphical view]
PRINTSPR01908. ADSPHPHTASE.
PR01909. ADSPHPHTASEA.
SMARTSM00195. DSPc. 1 hit.
[Graphical view]
PROSITEPS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50054. TYR_PHOSPHATASE_DUAL. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSDUSP3. human.
EvolutionaryTraceP51452.
GeneWikiDUSP3.
GenomeRNAi1845.
NextBio7555.
PROP51452.
SOURCESearch...

Entry information

Entry nameDUS3_HUMAN
AccessionPrimary (citable) accession number: P51452
Secondary accession number(s): D3DX45, Q5U0J1
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: April 16, 2014
This is version 133 of the entry and version 1 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM