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Protein

Regulatory protein E2

Gene

E2

Organism
Human papillomavirus type 18
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 18
Taxonomic identifieri333761 [NCBI]
Taxonomic lineageiVirusesdsDNA viruses, no RNA stagePapillomaviridaeAlphapapillomavirus
Virus hostiHomo sapiens (Human) [TaxID: 9606]
Proteomesi
  • UP000009109 Componenti: Genome

Subcellular locationi

  • Host nucleus UniRule annotation

GO - Cellular componenti

  • host cell nucleus Source: UniProtKB-SubCell
  • host cytoskeleton Source: CACAO
Complete GO annotation...

Keywords - Cellular componenti

Host nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 365365Regulatory protein E2PRO_0000133197Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki293 – 293Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)UniRule annotation

Post-translational modificationi

Phosphorylated.UniRule annotation
Sumoylation plays a regulatory role in E2 transcriptional activity.UniRule annotation

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

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
CEBPBP176764EBI-7010629,EBI-969696From a different organism.
EP300Q094726EBI-7010629,EBI-447295From a different organism.

Protein-protein interaction databases

IntActiP06790. 4 interactions.
MINTiMINT-95532.

Structurei

Secondary structure

1
365
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 2522Combined sources
Helixi30 – 5223Combined sources
Beta strandi56 – 583Combined sources
Helixi72 – 8817Combined sources
Turni90 – 934Combined sources
Turni98 – 1014Combined sources
Helixi103 – 1064Combined sources
Beta strandi108 – 1103Combined sources
Beta strandi113 – 12513Combined sources
Beta strandi129 – 14416Combined sources
Beta strandi150 – 1534Combined sources
Beta strandi155 – 1573Combined sources
Beta strandi159 – 1668Combined sources
Beta strandi169 – 1757Combined sources
Helixi176 – 1805Combined sources
Beta strandi189 – 1935Combined sources
Beta strandi287 – 2959Combined sources
Helixi296 – 30914Combined sources
Beta strandi314 – 3174Combined sources
Turni325 – 3273Combined sources
Beta strandi330 – 3367Combined sources
Helixi340 – 34910Combined sources
Beta strandi356 – 3649Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1F9FX-ray1.90A/B/C/D287-365[»]
1JJ4X-ray2.40A/B287-365[»]
1QQHX-ray2.10A70-213[»]
1TUEX-ray2.10B/E/G/J/L/Q1-215[»]
ProteinModelPortaliP06790.
SMRiP06790. Positions 4-213, 287-365.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP06790.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 205205Transactivation domainUniRule annotationAdd
BLAST
Regioni286 – 36580DNA-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.

P06790-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQTPKETLSE RLSCVQDKII DHYENDSKDI DSQIQYWQLI RWENAIFFAA
60 70 80 90 100
REHGIQTLNH QVVPAYNISK SKAHKAIELQ MALQGLAQSA YKTEDWTLQD
110 120 130 140 150
TCEELWNTEP THCFKKGGQT VQVYFDGNKD NCMTYVAWDS VYYMTDAGTW
160 170 180 190 200
DKTATCVSHR GLYYVKEGYN TFYIEFKSEC EKYGNTGTWE VHFGNNVIDC
210 220 230 240 250
NDSMCSTSDD TVSATQLVKQ LQHTPSPYSS TVSVGTAKTY GQTSAATRPG
260 270 280 290 300
HCGLAEKQHC GPVNPLLGAA TPTGNNKRRK LCSGNTTPII HLKGDRNSLK
310 320 330 340 350
CLRYRLRKHS DHYRDISSTW HWTGAGNEKT GILTVTYHSE TQRTKFLNTV
360
AIPDSVQILV GYMTM
Length:365
Mass (Da):41,294
Last modified:April 1, 1993 - v2
Checksum:i7871AD816A457ACB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X05015 Genomic DNA. Translation: CAA28667.1. Sequence problems.
PIRiD26251. W2WL18.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X05015 Genomic DNA. Translation: CAA28667.1. Sequence problems.
PIRiD26251. W2WL18.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1F9FX-ray1.90A/B/C/D287-365[»]
1JJ4X-ray2.40A/B287-365[»]
1QQHX-ray2.10A70-213[»]
1TUEX-ray2.10B/E/G/J/L/Q1-215[»]
ProteinModelPortaliP06790.
SMRiP06790. Positions 4-213, 287-365.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP06790. 4 interactions.
MINTiMINT-95532.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP06790.

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_HPV18
AccessioniPrimary (citable) accession number: P06790
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: April 1, 1993
Last modified: September 7, 2016
This is version 123 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete 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.