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Protein

Regulatory protein E2

Gene

E2

Organism
Human papillomavirus type 11
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Plays a role in the initiation of viral DNA replication. A dimer of E2 interacts with a dimer of E1 in order to improve specificity of E1 DNA binding activity. Once the complex recognizes and binds DNA at specific sites, the E2 dimer is removed from DNA. E2 also regulates viral transcription through binding to the E2RE response element (5'-ACCNNNNNNGGT-3') present in multiple copies in the regulatory regions of the viral genome. Activates or represses transcription depending on E2RE's position with regards to proximal promoter elements including the TATA-box. Repression occurs by sterically hindering the assembly of the transcription initiation complex.UniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Activator, Repressor

Keywords - Biological processi

DNA replication, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Regulatory protein E2UniRule annotation
Gene namesi
Name:E2UniRule annotation
OrganismiHuman papillomavirus type 11
Taxonomic identifieri10580 [NCBI]
Taxonomic lineageiVirusesdsDNA viruses, no RNA stagePapillomaviridaeAlphapapillomavirus
Virus hostiHomo sapiens (Human) [TaxID: 9606]
Proteomesi
  • UP000008222 Componenti: Genome

Subcellular locationi

  • Host nucleus UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Host nucleus

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL5830.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 367367Regulatory protein E2PRO_0000133190Add
BLAST

Post-translational modificationi

Phosphorylated.UniRule annotation

Keywords - PTMi

Phosphoprotein

Expressioni

Keywords - Developmental stagei

Early protein

Interactioni

Subunit structurei

Binds DNA as homodimer. Interacts with protein E1; this interaction greatly increases E1 DNA-binding activity. Interacts with protein L1; this interaction enhances E2-dependent replication and transcription activation. Interacts with protein L2; this interaction inhibits E2 transcriptional activity but not DNA replication function E2. Interacts with protein E7; this interaction inhibits E7 oncogenic activity. Interacts with host TAF1; this interaction modulates E2-dependent transcriptional regulation. Interacts with host BRD4; this interaction mediates E2 transcriptional activation function. Additionally, the interaction with host BRD4 on mitotic chromosomes mediates tethering of the viral genome. Interacts with host TOPBP1; this interaction is required for optimal viral DNA replication.UniRule annotation

Binary interactionsi

WithEntry#Exp.IntActNotes
BRD4O608852EBI-7010556,EBI-723869From a different organism.

Protein-protein interaction databases

IntActiP04015. 2 interactions.
MINTiMINT-95651.

Chemistry

BindingDBiP04015.

Structurei

Secondary structure

1
367
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 2118Combined sources
Helixi26 – 4823Combined sources
Beta strandi52 – 543Combined sources
Helixi62 – 8322Combined sources
Turni86 – 894Combined sources
Turni94 – 974Combined sources
Helixi99 – 1024Combined sources
Beta strandi104 – 1063Combined sources
Beta strandi109 – 12113Combined sources
Beta strandi128 – 14114Combined sources
Beta strandi144 – 1529Combined sources
Beta strandi154 – 1618Combined sources
Beta strandi164 – 1707Combined sources
Helixi171 – 1788Combined sources
Beta strandi180 – 1823Combined sources
Beta strandi184 – 1885Combined sources
Beta strandi191 – 1944Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1R6KX-ray2.50A2-201[»]
1R6NX-ray2.40A2-201[»]
ProteinModelPortaliP04015.
SMRiP04015. Positions 2-196, 281-367.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP04015.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 200200Transactivation domainUniRule annotationAdd
BLAST
Regioni283 – 36785DNA-binding domainUniRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the papillomaviridae E2 protein family.UniRule annotation

Family and domain databases

Gene3Di2.170.200.10. 1 hit.
3.30.70.330. 1 hit.
HAMAPiMF_04001. PPV_E2. 1 hit.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
IPR000427. Papillomavirus_E2_C.
IPR001866. Papillomavirus_E2_N.
IPR033668. Reg_prot_E2.
[Graphical view]
PfamiPF00511. PPV_E2_C. 1 hit.
PF00508. PPV_E2_N. 1 hit.
[Graphical view]
ProDomiPD000672. E2_early_recog_prot_C. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF51332. SSF51332. 1 hit.
SSF54957. SSF54957. 1 hit.

Sequencei

Sequence statusi: Complete.

P04015-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEAIAKRLDA CQDQLLELYE ENSIDIHKHI MHWKCIRLES VLLHKAKQMG
60 70 80 90 100
LSHIGLQVVP PLTVSETKGH NAIEMQMHLE SLAKTQYGVE PWTLQDTSYE
110 120 130 140 150
MWLTPPKRCF KKQGNTVEVK FDGCEDNVME YVVWTHIYLQ DNDSWVKVTS
160 170 180 190 200
SVDAKGIYYT CGQFKTYYVN FNKEAQKYGS TNHWEVCYGS TVICSPASVS
210 220 230 240 250
STVREVSIAE PTTYTPAQTT APTVSACTTE DGVSAPPRKR ARGPSTNNTL
260 270 280 290 300
CVANIRSVDS TINNIVTDNY NKHQRRNNCH SAATPIVQLQ GDSNCLKCFR
310 320 330 340 350
YRLNDKYKHL FELASSTWHW ASPEAPHKNA IVTLTYSSEE QRQQFLNSVK
360
IPPTIRHKVG FMSLHLL
Length:367
Mass (Da):41,709
Last modified:October 23, 1986 - v1
Checksum:iF7BAF74D336804F0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M14119 Genomic DNA. Translation: AAA46930.1.
PIRiA03668. W2WL11.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M14119 Genomic DNA. Translation: AAA46930.1.
PIRiA03668. W2WL11.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1R6KX-ray2.50A2-201[»]
1R6NX-ray2.40A2-201[»]
ProteinModelPortaliP04015.
SMRiP04015. Positions 2-196, 281-367.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP04015. 2 interactions.
MINTiMINT-95651.

Chemistry

BindingDBiP04015.
ChEMBLiCHEMBL5830.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP04015.

Family and domain databases

Gene3Di2.170.200.10. 1 hit.
3.30.70.330. 1 hit.
HAMAPiMF_04001. PPV_E2. 1 hit.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
IPR000427. Papillomavirus_E2_C.
IPR001866. Papillomavirus_E2_N.
IPR033668. Reg_prot_E2.
[Graphical view]
PfamiPF00511. PPV_E2_C. 1 hit.
PF00508. PPV_E2_N. 1 hit.
[Graphical view]
ProDomiPD000672. E2_early_recog_prot_C. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF51332. SSF51332. 1 hit.
SSF54957. SSF54957. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiVE2_HPV11
AccessioniPrimary (citable) accession number: P04015
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 23, 1986
Last sequence update: October 23, 1986
Last modified: September 7, 2016
This is version 109 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.