Reviewed,
UniProtKB/Swiss-Prot P03126 (VE6_HPV16)
Last modified
January 19, 2010.
Version 75.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Protein E6 | ||
| Gene names |
| ||
| Organism | Human papillomavirus type 16 | ||
| Taxonomic identifier | 333760 [NCBI] | ||
| Taxonomic lineage | Viruses › dsDNA viruses, no RNA stage › Papillomaviridae › Alphapapillomavirus | ||
| Virus host | Homo sapiens (Human) [TaxID: 9606] |
Protein attributes
| Sequence length | 158 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Transcriptional transactivator. Binds double stranded DNA. Has transforming activity. Inactivates, with E6-AP ubiquitin-protein ligase, the human TP53/p53 tumor suppressor protein by targeting it to degradation. Binds and targets human MUPP1/MPDZ protein to degradation. Those two functions presumably contribute to transforming activity By similarity. Interaction with human FBLN1 protein also seems to be linked to cell transformation. |
| Subunit structure | Forms a complex with E6-AP ubiquitin-protein ligase which interacts with human P53. Binds to human FBLN1 and MPDZ By similarity. Interacts with human NFX1 and MAGI3. Ref.4 Ref.5 Ref.6 Ref.7 Ref.8 |
| Subcellular location | |
| Miscellaneous | HPV16, in comparison to HPV types 6 and 11, is more often associated with malignant genital cancers in humans. |
| Sequence similarities | Belongs to the papillomaviridae E6 protein family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Host-virus interaction Transcription Transcription regulation |
| Cellular component | Host nucleus |
| Developmental stage | Early protein |
| Disease | Oncogene |
| Domain | Zinc-finger |
| Ligand | DNA-binding Metal-binding Zinc |
| Molecular function | Activator |
| Technical term | 3D-structure |
| Gene Ontology (GO) | |
| Biological process | interspecies interaction between organisms Inferred from electronic annotation. Source: UniProtKB-KW regulation of transcriptionInferred from electronic annotation. Source: UniProtKB-KW transcriptionInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | host cell nuclear matrix Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | DNA binding Inferred from electronic annotation. Source: UniProtKB-KW protein bindingInferred from physical interaction. Source: IntAct zinc ion bindingInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Binary interactions
With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| TP73 | O15350-1 | 1 | EBI-1177242,EBI-389619 | From a different organism. |
| TP73 | O15350-2 | 1 | EBI-1177242,EBI-389623 | From a different organism. |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||||||||||||||
Molecule processing | |||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 158 | 158 | Protein E6 | PRO_0000133336 | |||||||||||||||||||
Regions | |||||||||||||||||||||||
| Zinc finger | 37 – 73 | 37 | Potential | ||||||||||||||||||||
| Zinc finger | 110 – 146 | 37 | Potential | ||||||||||||||||||||
| Motif | 155 – 158 | 4 | PDZ-binding By similarity | ||||||||||||||||||||
Experimental info | |||||||||||||||||||||||
| Sequence conflict | 17 | 1 | R → G in AAQ10712. Ref.2 | ||||||||||||||||||||
| Sequence conflict | 90 | 1 | L → V in AAQ10712. Ref.2 | ||||||||||||||||||||
Secondary structure | |||||||||||||||||||||||
Helix Strand Turn | |||||||||||||||||||||||
| Beta strand | 87 – 90 | 4 | |||||||||||||||||||||
| Helix | 93 – 100 | 8 | |||||||||||||||||||||
| Turn | 101 – 105 | 5 | |||||||||||||||||||||
| Beta strand | 111 – 113 | 3 | |||||||||||||||||||||
| Helix | 119 – 128 | 10 | |||||||||||||||||||||
| Beta strand | 132 – 135 | 4 | |||||||||||||||||||||
| Beta strand | 138 – 141 | 4 | |||||||||||||||||||||
| Helix | 142 – 146 | 5 | |||||||||||||||||||||
Sequences
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References
| [1] | "Human papillomavirus type 16 DNA sequence." Seedorf K., Krammer G., Durst M., Suhai S., Rowekamp W.G. Virology 145:181-185(1985) [PubMed: 2990099] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [2] | "Cloning and sequencing of non-European human papillomavirus (HPV) variant complete genomes from cervicovaginal cells by an overlapping PCR method." Terai M., Fu L., Ma Z., Burk R.D. Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: Isolate European German 131. |
| [3] | "Expression of the human papillomavirus type 16 genome in SK-v cells, a line derived from a vulvar intraepithelial neoplasia." Schneider-Maunoury S., Pehau-Arnaudet G., Breitburd F., Orth G. J. Gen. Virol. 71:809-817(1990) [PubMed: 2157796] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 31-50. |
| [4] | "Interaction of oncogenic papillomavirus E6 proteins with fibulin-1." Du M., Fan X., Hong E., Chen J.J. Biochem. Biophys. Res. Commun. 296:962-969(2002) [PubMed: 12200142] [Abstract] Cited for: INTERACTION WITH HUMAN FBLN1, INHIBITION OF E6-MEDIATED TRANSFORMATION. |
| [5] | "Identification of a novel telomerase repressor that interacts with the human papillomavirus type-16 E6/E6-AP complex." Gewin L., Myers H., Kiyono T., Galloway D.A. Genes Dev. 18:2269-2282(2004) [PubMed: 15371341] [Abstract] Cited for: INTERACTION WITH HUMAN NFX1. |
| [6] | "Oncogenic human papillomavirus E6 proteins target the MAGI-2 and MAGI-3 proteins for degradation." Thomas M., Laura R., Hepner K., Guccione E., Sawyers C., Lasky L., Banks L. Oncogene 21:5088-5096(2002) [PubMed: 12140759] [Abstract] Cited for: INTERACTION WITH HUMAN MAGI3. |
| [7] | "Role of the PDZ domain-binding motif of the oncoprotein E6 in the pathogenesis of human papillomavirus type 31." Lee C., Laimins L.A. J. Virol. 78:12366-12377(2004) [PubMed: 15507623] [Abstract] Cited for: INTERACTION WITH HUMAN MAGI3. |
| [8] | "HPV E6 specifically targets different cellular pools of its PDZ domain-containing tumour suppressor substrates for proteasome-mediated degradation." Massimi P., Gammoh N., Thomas M., Banks L. Oncogene 23:8033-8039(2004) [PubMed: 15378012] [Abstract] Cited for: INTERACTION WITH HUMAN MAGI3. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | K02718 Genomic DNA. Translation: AAA46939.1. AF536179 Genomic DNA. Translation: AAQ10712.1. D00735 Genomic DNA. Translation: BAA00632.1. | ||||||||||||||||||
| PIR | W6WLHS. A03682. | ||||||||||||||||||
| RefSeq | NP_041325.1. | ||||||||||||||||||
3D structure databases | |||||||||||||||||||
| PDBe RCSB PDB PDBj |
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| ModBase | Search... | ||||||||||||||||||
Protein-protein interaction databases | |||||||||||||||||||
| IntAct | P03126. 5 interactions. | ||||||||||||||||||
Genome annotation databases | |||||||||||||||||||
| GeneID | 1489078. | ||||||||||||||||||
Family and domain databases | |||||||||||||||||||
| InterPro | IPR001334. E6. [Graphical view] | ||||||||||||||||||
| Pfam | PF00518. E6. 1 hit. [Graphical view] | ||||||||||||||||||
| ProtoNet | Search... | ||||||||||||||||||
Entry information
| Entry name | VE6_HPV16 | ||||||||
| Accession | Primary (citable) accession number: P03126 Secondary accession number(s): Q71BI7 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | Virus (Virus annotation project) | ||||||||
Relevant documents
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with


