Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P07239

- DUSP_VACCW

UniProt

P07239 - DUSP_VACCW

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Dual specificity protein phosphatase H1

Gene

H1L

Organism
Vaccinia virus (strain Western Reserve) (VACV) (Vaccinia virus (strain WR))
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.5 Publications

Catalytic activityi

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.PROSITE-ProRule annotation
Protein serine phosphate + H2O = protein serine + phosphate.

Kineticsi

  1. KM=87 µM for 3-O-methylfluorescein phosphate1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei110 – 1101Phosphocysteine intermediate1 PublicationPROSITE-ProRule annotation

GO - Molecular functioni

  1. protein tyrosine/serine/threonine phosphatase activity Source: InterPro
  2. protein tyrosine phosphatase activity Source: UniProtKB-EC

GO - Biological processi

  1. suppression by virus of host STAT1 activity Source: UniProtKB-KW
  2. suppression by virus of host type I interferon-mediated signaling pathway Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Keywords - Biological processi

Host-virus interaction, Inhibition of host innate immune response by virus, Inhibition of host interferon signaling pathway by virus, Inhibition of host STAT1 by virus, Viral immunoevasion

Names & Taxonomyi

Protein namesi
Recommended name:
Dual specificity protein phosphatase H1 (EC:3.1.3.-, EC:3.1.3.48)
Alternative name(s):
Late protein H1
Gene namesi
ORF Names:H1L
OrganismiVaccinia virus (strain Western Reserve) (VACV) (Vaccinia virus (strain WR))
Taxonomic identifieri10254 [NCBI]
Taxonomic lineageiVirusesdsDNA viruses, no RNA stagePoxviridaeChordopoxvirinaeOrthopoxvirusVaccinia virus
Virus hostiBos taurus (Bovine) [TaxID: 9913]
ProteomesiUP000000344: Genome

Subcellular locationi

Virion 1 Publication. Host cytoplasm 1 Publication
Note: Approximately 200 molecules of H1 are packaged within the virion and are essential for the viability of the virus.

GO - Cellular componenti

  1. host cell cytoplasm Source: UniProtKB-KW
  2. virion Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Host cytoplasm, Virion

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi110 – 1101C → S: Loss of activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 171171Dual specificity protein phosphatase H1PRO_0000094868Add
BLAST

Expressioni

Inductioni

Expressed in the late phase of the viral replicative cycle.1 Publication

Keywords - Developmental stagei

Late protein

Interactioni

Subunit structurei

Homodimer.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
STAT1P422243EBI-7789600,EBI-1057697From a different organism.

Protein-protein interaction databases

IntActiP07239. 1 interaction.
MINTiMINT-8216572.

Structurei

Secondary structure

1
171
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi6 – 149Combined sources
Beta strandi31 – 377Combined sources
Helixi39 – 435Combined sources
Helixi45 – 473Combined sources
Beta strandi48 – 503Combined sources
Beta strandi53 – 575Combined sources
Beta strandi59 – 613Combined sources
Beta strandi71 – 744Combined sources
Beta strandi80 – 823Combined sources
Helixi86 – 883Combined sources
Helixi89 – 10214Combined sources
Beta strandi106 – 1094Combined sources
Beta strandi111 – 1155Combined sources
Helixi116 – 12813Combined sources
Helixi134 – 14916Combined sources
Helixi156 – 16611Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2Q05X-ray2.57A/B/C/D1-171[»]
2RF6X-ray1.95A1-171[»]
3CM3X-ray1.32A1-171[»]
ProteinModelPortaliP07239.
SMRiP07239. Positions 1-170.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP07239.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 2727DimerizationAdd
BLAST

Sequence similaritiesi

Family and domain databases

Gene3Di3.90.190.10. 1 hit.
InterProiIPR000340. 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]
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.

P07239-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MDKKSLYKYL LLRSTGDMHK AKSPTIMTRV TNNVYLGNYK NAMDAPSSEV
60 70 80 90 100
KFKYVLNLTM DKYTLPNSNI NIIHIPLVDD TTTDISKYFD DVTAFLSKCD
110 120 130 140 150
QRNEPVLVHC AAGVNRSGAM ILAYLMSKNK ESLPMLYFLY VYHSMRDLRG
160 170
AFVENPSFKR QIIEKYVIDK N
Length:171
Mass (Da):19,698
Last modified:April 1, 1988 - v1
Checksum:i65DE6E875C7AD47E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti20 – 201K → R in AAO89378. 1 PublicationCurated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M13209 Genomic DNA. Translation: AAB59836.1.
AY243312 Genomic DNA. Translation: AAO89378.1.
PIRiA24481. QQVZH1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M13209 Genomic DNA. Translation: AAB59836.1 .
AY243312 Genomic DNA. Translation: AAO89378.1 .
PIRi A24481. QQVZH1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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 [» ]
ProteinModelPortali P07239.
SMRi P07239. Positions 1-170.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P07239. 1 interaction.
MINTi MINT-8216572.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei P07239.

Family and domain databases

Gene3Di 3.90.190.10. 1 hit.
InterProi 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 ]
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. "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).

Entry informationi

Entry nameiDUSP_VACCW
AccessioniPrimary (citable) accession number: P07239
Secondary accession number(s): Q80HW5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: April 1, 1988
Last modified: November 26, 2014
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3