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Protein

Regulatory protein E2

Gene

E2

Organism
Bovine papillomavirus type 1
Status
Reviewed-Annotation score: Annotation score: 5 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

Enzyme regulationi

Inactivated by oxidation of Cys-340 to a sulfenic acid.

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
OrganismiBovine papillomavirus type 1
Taxonomic identifieri10559 [NCBI]
Taxonomic lineageiVirusesdsDNA viruses, no RNA stagePapillomaviridaeDeltapapillomavirus
Virus hostiBos taurus (Bovine) [TaxID: 9913]
Proteomesi
  • UP000006567 Componenti: Genome

Subcellular locationi

  • Host nucleus UniRule annotation1 Publication

  • Note: Colocalizes with DDX11 at early stages of mitosis.

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Host nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi130W → R: Loss of ability to bind to DDX11, no effect on ability to bind BRD4, loss of attachment to mitotic chromosomes, and interference with the maintenance of replicating viral episomes. 1 Publication1
Mutagenesisi340C → A: 90% decrease in DNA-binding affinity. 1 Publication1
Mutagenesisi340C → G: <50% decrease in DNA-binding affinity. 1 Publication1
Mutagenesisi340C → S: 50% decrease in DNA-binding affinity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001331721 – 410Regulatory protein E2Add BLAST410

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei298Phosphoserine; by host1 Publication1
Modified residuei301Phosphoserine; by host1 Publication1
Modified residuei340Cysteine sulfenic acid (-SOH)1 Publication1

Post-translational modificationi

Oxidation of Cys-340 in response to redox signaling leads to the loss of DNA-binding activity and the inactivation of gene activator or repressor function.1 Publication
Phosphorylated.UniRule annotation

Keywords - PTMi

Oxidation, Phosphoprotein

PTM databases

iPTMnetiP03122.

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. Interacts with human DDX11.UniRule annotation1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
CEBPAP497152EBI-7028618,EBI-1172054From a different organism.
CEBPBP176763EBI-7028618,EBI-969696From a different organism.
EP300Q094723EBI-7028618,EBI-447295From a different organism.

Protein-protein interaction databases

DIPiDIP-40866N.
IntActiP03122. 5 interactors.
MINTiMINT-95676.

Structurei

Secondary structure

1410
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi4 – 21Combined sources18
Helixi26 – 48Combined sources23
Beta strandi52 – 54Combined sources3
Helixi62 – 83Combined sources22
Helixi86 – 89Combined sources4
Turni94 – 97Combined sources4
Helixi99 – 103Combined sources5
Beta strandi104 – 120Combined sources17
Beta strandi127 – 140Combined sources14
Beta strandi142 – 152Combined sources11
Beta strandi157 – 161Combined sources5
Turni162 – 165Combined sources4
Beta strandi166 – 170Combined sources5
Helixi173 – 180Combined sources8
Beta strandi182 – 184Combined sources3
Beta strandi186 – 192Combined sources7
Beta strandi194 – 197Combined sources4
Beta strandi327 – 333Combined sources7
Helixi335 – 348Combined sources14
Helixi350 – 352Combined sources3
Beta strandi354 – 356Combined sources3
Beta strandi360 – 363Combined sources4
Beta strandi365 – 368Combined sources4
Beta strandi370 – 382Combined sources13
Helixi383 – 392Combined sources10
Beta strandi400 – 405Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1DBDNMR-A/B311-410[»]
1JJHX-ray2.50A/B/C326-410[»]
2BOPX-ray1.70A326-410[»]
2JEUX-ray2.80A1-209[»]
2JEXX-ray2.35A1-209[»]
ProteinModelPortaliP03122.
SMRiP03122.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP03122.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 202Transactivation domainUniRule annotationAdd BLAST202
Regioni325 – 410DNA-binding domainUniRule annotation1 PublicationAdd BLAST86

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi293 – 296Poly-Glu4

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.

P03122-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
METACERLHV AQETQMQLIE KSSDKLQDHI LYWTAVRTEN TLLYAARKKG
60 70 80 90 100
VTVLGHCRVP HSVVCQERAK QAIEMQLSLQ ELSKTEFGDE PWSLLDTSWD
110 120 130 140 150
RYMSEPKRCF KKGARVVEVE FDGNASNTNW YTVYSNLYMR TEDGWQLAKA
160 170 180 190 200
GADGTGLYYC TMAGAGRIYY SRFGDEAARF STTGHYSVRD QDRVYAGVSS
210 220 230 240 250
TSSDFRDRPD GVWVASEGPE GDPAGKEAEP AQPVSSLLGS PACGPIRAGL
260 270 280 290 300
GWVRDGPRSH PYNFPAGSGG SILRSSSTPV QGTVPVDLAS RQEEEEQSPD
310 320 330 340 350
STEEEPVTLP RRTTNDGFHL LKAGGSCFAL ISGTANQVKC YRFRVKKNHR
360 370 380 390 400
HRYENCTTTW FTVADNGAER QGQAQILITF GSPSQRQDFL KHVPLPPGMN
410
ISGFTASLDF
Length:410
Mass (Da):45,450
Last modified:July 15, 1998 - v2
Checksum:iF45B0BB74E679045
GO

Sequence cautioni

The sequence CAB46512 differs from that shown. Reason: Frameshift at position 280.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X02346 Genomic DNA. Translation: CAB46512.1. Frameshift.
PIRiA03672. W2WLEB.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X02346 Genomic DNA. Translation: CAB46512.1. Frameshift.
PIRiA03672. W2WLEB.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1DBDNMR-A/B311-410[»]
1JJHX-ray2.50A/B/C326-410[»]
2BOPX-ray1.70A326-410[»]
2JEUX-ray2.80A1-209[»]
2JEXX-ray2.35A1-209[»]
ProteinModelPortaliP03122.
SMRiP03122.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-40866N.
IntActiP03122. 5 interactors.
MINTiMINT-95676.

PTM databases

iPTMnetiP03122.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP03122.

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_BPV1
AccessioniPrimary (citable) accession number: P03122
Secondary accession number(s): Q9WMH0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 15, 1998
Last modified: November 30, 2016
This is version 130 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, 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.