Dual specificity protein phosphatase H1 - Vaccinia virus (strain Western Reserve) (VACV)

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P07239 (DUSP_VACCW) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 80. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

Organism

Vaccinia virus (strain Western Reserve) (VACV) (Vaccinia virus (strain WR)) [Reference proteome]

Taxonomic identifier

10254 [NCBI]

Taxonomic lineage

Viruses › dsDNA viruses, no RNA stage › Poxviridae › Chordopoxvirinae › Orthopoxvirus › Vaccinia virus

Virus host

Bos taurus (Bovine) [TaxID: 9913]

Protein attributes

Sequence length	171 AA.
Sequence status	Complete.
Protein existence	Evidence 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: K_M=87 µM for 3-O-methylfluorescein phosphate Ref.8

Ontologies

Keywords
Biological process	Host-virus interaction Inhibition of host STAT1 by virus Inhibition of host innate immune response by virus Inhibition of host interferon signaling pathway by virus Viral immunoevasion
Cellular component	Host cytoplasm Virion
Developmental stage	Late protein
Molecular function	Hydrolase Protein phosphatase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	peptidyl-tyrosine dephosphorylation Inferred from electronic annotation. Source: GOC suppression by virus of host STAT1 activity Inferred from electronic annotation. Source: UniProtKB-KW suppression by virus of host type I interferon-mediated signaling pathway Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	host cell cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell virion Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	protein tyrosine phosphatase activity Inferred from electronic annotation. Source: EC protein tyrosine/serine/threonine phosphatase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 171

171

Dual specificity protein phosphatase H1

PRO_0000094868

Regions

Region

1 – 27

Dimerization

Sites

Active site

110

Phosphocysteine intermediate Ref.4

Experimental info

Mutagenesis

110

C → S: Loss of activity. Ref.4

Sequence conflict

K → R in AAO89378. Ref.3

Secondary structure

171

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P07239 [UniParc].

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

171

19,698

        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' referencesShow '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.

PIR

QQVZH1. A24481.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2Q05	X-ray	2.57	A/B/C/D	1-171	[»]
2RF6	X-ray	1.95	A	1-171	[»]
3CM3	X-ray	1.32	A	1-171	[»]

ProteinModelPortal

P07239.

SMR

P07239. Positions 1-170.

ModBase

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Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Phylogenomic databases

ProtClustDB

CLSP2509785.

Family and domain databases

InterPro

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]

PANTHER

PTHR10159. PTHR10159. 1 hit.

Pfam

PF00782. DSPc. 1 hit.
[Graphical view]

SMART

SM00195. DSPc. 1 hit.
[Graphical view]

PROSITE

PS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50054. TYR_PHOSPHATASE_DUAL. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P07239.

Entry information

Entry name

DUSP_VACCW

Accession

Primary (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 3, 2013
This is version 80 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Viral Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protocols and materials databases

Phylogenomic databases

Family and domain databases

Other

Entry information

Relevant documents