P33064 (DUSP_VAR67) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 73.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames 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 |
| ||
| Organism | Variola virus (isolate Human/India/Ind3/1967) (VARV) (Smallpox virus) [Reference proteome] | ||
| Taxonomic identifier | 587200 [NCBI] | ||
| Taxonomic lineage | Viruses › dsDNA viruses, no RNA stage › Poxviridae › Chordopoxvirinae › Orthopoxvirus › ![]() | ||
| Virus host | Homo sapiens (Human) [TaxID: 9606] |
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 By similarity. |
| Catalytic activity | Protein tyrosine phosphate + H2O = protein tyrosine + phosphate. Protein serine phosphate + H2O = protein serine + phosphate. |
| Subunit structure | Homodimer By similarity. |
| Subcellular location | Virion By similarity. Host cytoplasm By similarity. Note: Approximately 200 molecules of H1 are packaged within the virion and are essential for the viability of the virus By similarity. |
| Induction | Expressed in the late phase of the viral replicative cycle. |
| Sequence similarities | Belongs to the protein-tyrosine phosphatase family. Non-receptor class dual specificity subfamily. |
Ontologies
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_0000094869 | ||||||||||||||||||||||||||||||||
Sites | ||||||||||||||||||||||||||||||||||||
| Active site | 110 | 1 | Phosphocysteine intermediate By similarity | |||||||||||||||||||||||||||||||||
Secondary structure | ||||||||||||||||||||||||||||||||||||
Helix Strand Turn | ||||||||||||||||||||||||||||||||||||
| Helix | 6 – 14 | 9 | ||||||||||||||||||||||||||||||||||
| Beta strand | 31 – 37 | 7 | ||||||||||||||||||||||||||||||||||
| Helix | 39 – 44 | 6 | ||||||||||||||||||||||||||||||||||
| Helix | 45 – 47 | 3 | ||||||||||||||||||||||||||||||||||
| Beta strand | 53 – 57 | 5 | ||||||||||||||||||||||||||||||||||
| Beta strand | 59 – 61 | 3 | ||||||||||||||||||||||||||||||||||
| Beta strand | 71 – 74 | 4 | ||||||||||||||||||||||||||||||||||
| Beta strand | 80 – 83 | 4 | ||||||||||||||||||||||||||||||||||
| Helix | 86 – 88 | 3 | ||||||||||||||||||||||||||||||||||
| Helix | 89 – 102 | 14 | ||||||||||||||||||||||||||||||||||
| Beta strand | 106 – 109 | 4 | ||||||||||||||||||||||||||||||||||
| Beta strand | 111 – 115 | 5 | ||||||||||||||||||||||||||||||||||
| Helix | 116 – 128 | 13 | ||||||||||||||||||||||||||||||||||
| Helix | 134 – 149 | 16 | ||||||||||||||||||||||||||||||||||
| Helix | 156 – 166 | 11 | ||||||||||||||||||||||||||||||||||
Sequences
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References
Cross-references
Sequence databases | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | X67119 Genomic DNA. Translation: CAA47583.1. S55844 Genomic DNA. Translation: AAB24680.1. X69198 Genomic DNA. Translation: CAA49025.1. L22579 Genomic DNA. Translation: AAA60832.1. X76264 Genomic DNA. Translation: CAA53838.1. | ||||||||||||
| PIR | B72161. I36845. T28522. | ||||||||||||
| RefSeq | NP_042128.1. NC_001611.1. | ||||||||||||
3D structure databases | |||||||||||||
| PDBe RCSB PDB PDBj |
| ||||||||||||
| ProteinModelPortal | P33064. | ||||||||||||
| SMR | P33064. Positions 5-167. | ||||||||||||
| ModBase | Search... | ||||||||||||
Protocols and materials databases | |||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||
Genome annotation databases | |||||||||||||
| GeneID | 1486439. | ||||||||||||
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 | P33064. | ||||||||||||
Entry information
| Entry name | DUSP_VAR67 | ||||||||
| Accession | Primary (citable) accession number: P33064 | ||||||||
| Entry history |
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| 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 |

Clusters with
