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P51452

- DUS3_HUMAN

UniProt

P51452 - DUS3_HUMAN

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Protein
Dual specificity protein phosphatase 3
Gene
DUSP3, VHR
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Shows activity both for tyrosine-protein phosphate and serine-protein phosphate, but displays a strong preference toward phosphotyrosines. Specifically dephosphorylates and inactivates ERK1 and ERK2.2 Publications

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei124 – 1241Phosphocysteine intermediate

GO - Molecular functioni

  1. MAP kinase phosphatase activity Source: UniProtKB
  2. protein tyrosine phosphatase activity Source: UniProtKB
  3. protein tyrosine/serine/threonine phosphatase activity Source: UniProtKB

GO - Biological processi

  1. MyD88-dependent toll-like receptor signaling pathway Source: Reactome
  2. MyD88-independent toll-like receptor signaling pathway Source: Reactome
  3. TRIF-dependent toll-like receptor signaling pathway Source: Reactome
  4. in utero embryonic development Source: Ensembl
  5. inactivation of MAPK activity Source: UniProtKB
  6. innate immune response Source: Reactome
  7. negative regulation of ERK1 and ERK2 cascade Source: UniProtKB
  8. negative regulation of JNK cascade Source: UniProtKB
  9. negative regulation of MAPK cascade Source: UniProtKB
  10. negative regulation of T cell activation Source: UniProtKB
  11. negative regulation of T cell receptor signaling pathway Source: UniProtKB
  12. neurotrophin TRK receptor signaling pathway Source: Reactome
  13. peptidyl-tyrosine dephosphorylation Source: UniProtKB
  14. positive regulation of mitotic cell cycle Source: UniProtKB
  15. stress-activated MAPK cascade Source: Reactome
  16. toll-like receptor 10 signaling pathway Source: Reactome
  17. toll-like receptor 2 signaling pathway Source: Reactome
  18. toll-like receptor 3 signaling pathway Source: Reactome
  19. toll-like receptor 4 signaling pathway Source: Reactome
  20. toll-like receptor 5 signaling pathway Source: Reactome
  21. toll-like receptor 9 signaling pathway Source: Reactome
  22. toll-like receptor TLR1:TLR2 signaling pathway Source: Reactome
  23. toll-like receptor TLR6:TLR2 signaling pathway Source: Reactome
  24. toll-like receptor signaling pathway Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Enzyme and pathway databases

ReactomeiREACT_12436. ERKs are inactivated.
SignaLinkiP51452.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:DUSP3
Synonyms:VHR
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 17

Organism-specific databases

HGNCiHGNC:3069. DUSP3.

Subcellular locationi

Nucleus 1 Publication

GO - Cellular componenti

  1. cytosol Source: UniProtKB
  2. extracellular vesicular exosome Source: UniProt
  3. immunological synapse Source: UniProtKB
  4. nucleoplasm Source: Reactome
  5. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA27526.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 185185Dual specificity protein phosphatase 3
PRO_0000094795Add
BLAST

Proteomic databases

MaxQBiP51452.
PaxDbiP51452.
PRIDEiP51452.

2D gel databases

UCD-2DPAGEP51452.

PTM databases

PhosphoSiteiP51452.

Expressioni

Gene expression databases

ArrayExpressiP51452.
BgeeiP51452.
CleanExiHS_DUSP3.
GenevestigatoriP51452.

Organism-specific databases

HPAiCAB025265.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi108178. 9 interactions.
IntActiP51452. 5 interactions.
MINTiMINT-5001069.
STRINGi9606.ENSP00000226004.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi8 – 169
Beta strandi19 – 213
Beta strandi27 – 348
Beta strandi37 – 404
Helixi42 – 454
Helixi48 – 547
Beta strandi58 – 614
Beta strandi64 – 674
Helixi76 – 783
Turni79 – 824
Beta strandi84 – 874
Helixi98 – 1014
Helixi102 – 11413
Turni115 – 1173
Beta strandi120 – 1234
Beta strandi125 – 1295
Helixi130 – 14314
Helixi147 – 15711
Helixi164 – 17916

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1J4XX-ray2.75A2-185[»]
1VHRX-ray2.10A/B2-185[»]
3F81X-ray1.90A/B3-185[»]
ProteinModelPortaliP51452.
SMRiP51452. Positions 7-185.

Miscellaneous databases

EvolutionaryTraceiP51452.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini99 – 16971Tyrosine-protein phosphatase
Add
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG2453.
HOGENOMiHOG000233767.
HOVERGENiHBG001524.
InParanoidiP51452.
KOiK17614.
OMAiPCNEVIP.
OrthoDBiEOG7CZK7N.
PhylomeDBiP51452.
TreeFamiTF105128.

Family and domain databases

Gene3Di3.90.190.10. 1 hit.
InterProiIPR020417. Atypical_DUSP.
IPR020405. Atypical_DUSP_famA.
IPR000340. Dual-sp_phosphatase_cat-dom.
IPR020422. Dual-sp_phosphatase_subgr_cat.
IPR024950. DUSP.
IPR029021. Prot-tyrosine_phosphatase-like.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
[Graphical view]
PANTHERiPTHR10159. PTHR10159. 1 hit.
PfamiPF00782. DSPc. 1 hit.
[Graphical view]
PRINTSiPR01908. ADSPHPHTASE.
PR01909. ADSPHPHTASEA.
SMARTiSM00195. DSPc. 1 hit.
[Graphical view]
SUPFAMiSSF52799. SSF52799. 1 hit.
PROSITEiPS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50054. TYR_PHOSPHATASE_DUAL. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P51452-1 [UniParc]FASTAAdd to Basket

« Hide

MSGSFELSVQ DLNDLLSDGS GCYSLPSQPC NEVTPRIYVG NASVAQDIPK    50
LQKLGITHVL NAAEGRSFMH VNTNANFYKD SGITYLGIKA NDTQEFNLSA 100
YFERAADFID QALAQKNGRV LVHCREGYSR SPTLVIAYLM MRQKMDVKSA 150
LSIVRQNREI GPNDGFLAQL CQLNDRLAKE GKLKP 185
Length:185
Mass (Da):20,478
Last modified:October 1, 1996 - v1
Checksum:iC1045DD9B226FD94
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS11469.1.
PIRiA47196.
RefSeqiNP_004081.1. NM_004090.3.
UniGeneiHs.181046.

Genome annotation databases

EnsembliENST00000226004; ENSP00000226004; ENSG00000108861.
GeneIDi1845.
KEGGihsa:1845.
UCSCiuc002ied.4. human.

Polymorphism databases

DMDMi1718191.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS11469.1.
PIRi A47196.
RefSeqi NP_004081.1. NM_004090.3.
UniGenei Hs.181046.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1J4X X-ray 2.75 A 2-185 [» ]
1VHR X-ray 2.10 A/B 2-185 [» ]
3F81 X-ray 1.90 A/B 3-185 [» ]
ProteinModelPortali P51452.
SMRi P51452. Positions 7-185.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108178. 9 interactions.
IntActi P51452. 5 interactions.
MINTi MINT-5001069.
STRINGi 9606.ENSP00000226004.

Chemistry

BindingDBi P51452.
ChEMBLi CHEMBL2635.

PTM databases

PhosphoSitei P51452.

Polymorphism databases

DMDMi 1718191.

2D gel databases

UCD-2DPAGE P51452.

Proteomic databases

MaxQBi P51452.
PaxDbi P51452.
PRIDEi P51452.

Protocols and materials databases

DNASUi 1845.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000226004 ; ENSP00000226004 ; ENSG00000108861 .
GeneIDi 1845.
KEGGi hsa:1845.
UCSCi uc002ied.4. human.

Organism-specific databases

CTDi 1845.
GeneCardsi GC17M041856.
H-InvDB HIX0013868.
HGNCi HGNC:3069. DUSP3.
HPAi CAB025265.
MIMi 600183. gene.
neXtProti NX_P51452.
PharmGKBi PA27526.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG2453.
HOGENOMi HOG000233767.
HOVERGENi HBG001524.
InParanoidi P51452.
KOi K17614.
OMAi PCNEVIP.
OrthoDBi EOG7CZK7N.
PhylomeDBi P51452.
TreeFami TF105128.

Enzyme and pathway databases

Reactomei REACT_12436. ERKs are inactivated.
SignaLinki P51452.

Miscellaneous databases

ChiTaRSi DUSP3. human.
EvolutionaryTracei P51452.
GeneWikii DUSP3.
GenomeRNAii 1845.
NextBioi 7555.
PROi P51452.
SOURCEi Search...

Gene expression databases

ArrayExpressi P51452.
Bgeei P51452.
CleanExi HS_DUSP3.
Genevestigatori P51452.

Family and domain databases

Gene3Di 3.90.190.10. 1 hit.
InterProi IPR020417. Atypical_DUSP.
IPR020405. Atypical_DUSP_famA.
IPR000340. Dual-sp_phosphatase_cat-dom.
IPR020422. Dual-sp_phosphatase_subgr_cat.
IPR024950. DUSP.
IPR029021. Prot-tyrosine_phosphatase-like.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
[Graphical view ]
PANTHERi PTHR10159. PTHR10159. 1 hit.
Pfami PF00782. DSPc. 1 hit.
[Graphical view ]
PRINTSi PR01908. ADSPHPHTASE.
PR01909. ADSPHPHTASEA.
SMARTi SM00195. DSPc. 1 hit.
[Graphical view ]
SUPFAMi SSF52799. SSF52799. 1 hit.
PROSITEi PS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50054. TYR_PHOSPHATASE_DUAL. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. 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. 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. 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.

Entry informationi

Entry nameiDUS3_HUMAN
AccessioniPrimary (citable) accession number: P51452
Secondary accession number(s): D3DX45, Q5U0J1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: September 3, 2014
This is version 137 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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