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P07239 (DUSP_VACCW) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 84. 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·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Dual specificity protein phosphatase H1

EC=3.1.3.-
EC=3.1.3.48
Alternative name(s):
Late protein H1
Gene names
ORF Names:H1L
OrganismVaccinia virus (strain Western Reserve) (VACV) (Vaccinia virus (strain WR)) [Reference proteome]
Taxonomic identifier10254 [NCBI]
Taxonomic lineageVirusesdsDNA viruses, no RNA stagePoxviridaeChordopoxvirinaeOrthopoxvirusVaccinia virus
Virus hostBos taurus (Bovine) [TaxID: 9913]

Protein attributes

Sequence length171 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Serine/Tyrosine phosphatase which down-regulates cellular antiviral response by dephosphorylating activated host STAT1 and blocking interferon (IFN)-stimulated innate immune responses. Dephosphorylates the A17 protein. Ref.4 Ref.5 Ref.6 Ref.7 Ref.8

Catalytic activity

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.

Protein serine phosphate + H2O = protein serine + phosphate.

Subunit structure

Homodimer. Ref.8

Subcellular location

Virion. Host cytoplasm. Note: Approximately 200 molecules of H1 are packaged within the virion and are essential for the viability of the virus. Ref.8

Induction

Expressed in the late phase of the viral replicative cycle. Ref.7

Sequence similarities

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

Biophysicochemical properties

Kinetic parameters:

KM=87 µM for 3-O-methylfluorescein phosphate Ref.8

Binary interactions

With

Entry

#Exp.

IntAct

Notes

STAT1P422243EBI-7789600,EBI-1057697From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 171171Dual specificity protein phosphatase H1
PRO_0000094868

Regions

Region1 – 2727Dimerization

Sites

Active site1101Phosphocysteine intermediate Ref.4

Experimental info

Mutagenesis1101C → S: Loss of activity. Ref.4
Sequence conflict201K → R in AAO89378. Ref.3

Secondary structure

.............................. 171
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P07239 [UniParc].

Last modified April 1, 1988. Version 1.
Checksum: 65DE6E875C7AD47E

FASTA17119,698
        10         20         30         40         50         60 
MDKKSLYKYL LLRSTGDMHK AKSPTIMTRV TNNVYLGNYK NAMDAPSSEV KFKYVLNLTM 

        70         80         90        100        110        120 
DKYTLPNSNI NIIHIPLVDD TTTDISKYFD DVTAFLSKCD QRNEPVLVHC AAGVNRSGAM 

       130        140        150        160        170 
ILAYLMSKNK ESLPMLYFLY VYHSMRDLRG AFVENPSFKR QIIEKYVIDK N 

« Hide

References

« Hide 'large scale' references
[1]"Homology between RNA polymerases of poxviruses, prokaryotes, and eukaryotes: nucleotide sequence and transcriptional analysis of vaccinia virus genes encoding 147-kDa and 22-kDa subunits."
Broyles S.S., Moss B.
Proc. Natl. Acad. Sci. U.S.A. 83:3141-3145(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Conserved TAAATG sequence at the transcriptional and translational initiation sites of vaccinia virus late genes deduced by structural and functional analysis of the HindIII H genome fragment."
Rosel J.L., Earl P.L., Weir J.P., Moss B.
J. Virol. 60:436-449(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Sequencing of the coding region of Vaccinia-WR to an average 9-fold redundancy and an error rate of 0.16/10kb."
Esposito J.J., Frace A.M., Sammons S.A., Olsen-Rasmussen M., Osborne J., Wohlhueter R.
Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"A Tyr/Ser protein phosphatase encoded by vaccinia virus."
Guan K., Broyels S.S., Dixon J.E.
Nature 350:359-362(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, ACTIVE SITE, MUTAGENESIS OF CYS-110.
[5]"Tyrosine phosphorylation of A17 during vaccinia virus infection: involvement of the H1 phosphatase and the F10 kinase."
Derrien M., Punjabi A., Khanna M., Grubisha O., Traktman P.
J. Virol. 73:7287-7296(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH A17.
[6]"Vaccinia virus blocks gamma interferon signal transduction: viral VH1 phosphatase reverses Stat1 activation."
Najarro P., Traktman P., Lewis J.A.
J. Virol. 75:3185-3196(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[7]"Vaccinia virus blocks Stat1-dependent and Stat1-independent gene expression induced by type I and type II interferons."
Mann B.A., Huang J.H., Li P., Chang H.C., Slee R.B., O'Sullivan A., Anita M., Yeh N., Klemsz M.J., Brutkiewicz R.R., Blum J.S., Kaplan M.H.
J. Interferon Cytokine Res. 28:367-380(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INDUCTION.
[8]"Dimerization of Vaccinia virus VH1 is essential for dephosphorylation of STAT1 at tyrosine 701."
Koksal A.C., Cingolani G.
J. Biol. Chem. 286:14373-14382(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION.
[9]"Dimeric quaternary structure of the prototypical dual specificity phosphatase VH1."
Koksal A.C., Nardozzi J.D., Cingolani G.
J. Biol. Chem. 284:10129-10137(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.32 ANGSTROMS).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M13209 Genomic DNA. Translation: AAB59836.1.
AY243312 Genomic DNA. Translation: AAO89378.1.
PIRQQVZH1. A24481.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2Q05X-ray2.57A/B/C/D1-171[»]
2RF6X-ray1.95A1-171[»]
3CM3X-ray1.32A1-171[»]
ProteinModelPortalP07239.
SMRP07239. Positions 1-170.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP07239. 1 interaction.
MINTMINT-8216572.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

ProtClustDBCLSP2509785.

Family and domain databases

InterProIPR000340. 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]
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

EvolutionaryTraceP07239.

Entry information

Entry nameDUSP_VACCW
AccessionPrimary (citable) accession number: P07239
Secondary accession number(s): Q80HW5
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: April 1, 1988
Last modified: April 16, 2014
This is version 84 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references