Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi130 – 1301W → 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 Publication
Mutagenesisi340 – 3401C → A: 90% decrease in DNA-binding affinity. 1 Publication
Mutagenesisi340 – 3401C → G: <50% decrease in DNA-binding affinity. 1 Publication
Mutagenesisi340 – 3401C → S: 50% decrease in DNA-binding affinity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 410410Regulatory protein E2PRO_0000133172Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei298 – 2981Phosphoserine; by host1 Publication
Modified residuei301 – 3011Phosphoserine; by host1 Publication
Modified residuei340 – 3401Cysteine sulfenic acid (-SOH)1 Publication

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 interactions.
MINTiMINT-95676.

Structurei

Secondary structure

1
410
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
Helixi86 – 894Combined sources
Turni94 – 974Combined sources
Helixi99 – 1035Combined sources
Beta strandi104 – 12017Combined sources
Beta strandi127 – 14014Combined sources
Beta strandi142 – 15211Combined sources
Beta strandi157 – 1615Combined sources
Turni162 – 1654Combined sources
Beta strandi166 – 1705Combined sources
Helixi173 – 1808Combined sources
Beta strandi182 – 1843Combined sources
Beta strandi186 – 1927Combined sources
Beta strandi194 – 1974Combined sources
Beta strandi327 – 3337Combined sources
Helixi335 – 34814Combined sources
Helixi350 – 3523Combined sources
Beta strandi354 – 3563Combined sources
Beta strandi360 – 3634Combined sources
Beta strandi365 – 3684Combined sources
Beta strandi370 – 38213Combined sources
Helixi383 – 39210Combined sources
Beta strandi400 – 4056Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 3-199, 311-410.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP03122.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 202202Transactivation domainUniRule annotationAdd
BLAST
Regioni325 – 41086DNA-binding domainUniRule annotation1 PublicationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi293 – 2964Poly-Glu

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
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. Positions 3-199, 311-410.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-40866N.
IntActiP03122. 5 interactions.
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: September 7, 2016
This is version 127 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.