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Protein

Regulatory protein E2

Gene

E2

Organism
Human papillomavirus type 16
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 annotation6 Publications

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 16
Taxonomic identifieri333760 [NCBI]
Taxonomic lineageiVirusesdsDNA viruses, no RNA stagePapillomaviridaeAlphapapillomavirus
Virus hostiHomo sapiens (Human) [TaxID: 9606]
Proteomesi
  • UP000009251 Componenti: Genome

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Host nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi292K → R: Complete loss of sumoylation. 1 Publication1

Chemistry databases

ChEMBLiCHEMBL4656.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001331951 – 365Regulatory protein E2Add BLAST365

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei243Phosphoserine; by host1 Publication1
Cross-linki292Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)UniRule annotation1 Publication

Post-translational modificationi

Phosphorylated. Phosphorylation at Ser-243 mediates binding to host Brd4 and is required for host chromosome binding.UniRule annotation2 Publications
Sumoylation plays a regulatory role in E2 transcriptional activity.UniRule annotation1 Publication

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

PRIDEiP03120.

PTM databases

iPTMnetiP03120.

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 annotation9 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
BRD4O608853EBI-1779322,EBI-723869From a different organism.
CEBPBP176762EBI-1779322,EBI-969696From a different organism.
CPSF3P791012EBI-1779322,EBI-7894416From a different organism.
CPSF4O191373EBI-1779322,EBI-7894441From a different organism.
E1P031143EBI-1779322,EBI-7387308
Rep68P031322EBI-1779322,EBI-7387242From a different organism.
TOPBP1Q925472EBI-1779322,EBI-308302From a different organism.

Protein-protein interaction databases

DIPiDIP-44574N.
IntActiP03120. 19 interactors.
MINTiMINT-95621.

Chemistry databases

BindingDBiP03120.

Structurei

Secondary structure

1365
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi1 – 21Combined sources21
Helixi26 – 48Combined sources23
Beta strandi52 – 54Combined sources3
Helixi62 – 83Combined sources22
Turni86 – 89Combined sources4
Turni94 – 97Combined sources4
Helixi99 – 103Combined sources5
Beta strandi104 – 106Combined sources3
Beta strandi110 – 121Combined sources12
Beta strandi127 – 141Combined sources15
Beta strandi144 – 148Combined sources5
Beta strandi154 – 161Combined sources8
Beta strandi164 – 170Combined sources7
Helixi171 – 178Combined sources8
Beta strandi180 – 182Combined sources3
Beta strandi184 – 190Combined sources7
Beta strandi286 – 293Combined sources8
Helixi295 – 305Combined sources11
Helixi306 – 311Combined sources6
Beta strandi313 – 315Combined sources3
Beta strandi331 – 336Combined sources6
Helixi340 – 349Combined sources10
Beta strandi356 – 363Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1BY9X-ray2.20A285-365[»]
1DTOX-ray1.90A1-201[»]
1R8PNMR-A/B286-365[»]
1ZZFNMR-A/B286-365[»]
2NNUX-ray1.59A1-201[»]
2Q79X-ray1.80A285-365[»]
3MI7X-ray2.20X283-365[»]
ProteinModelPortaliP03120.
SMRiP03120.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP03120.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 200Transactivation domainUniRule annotation1 PublicationAdd BLAST200
Regioni285 – 365DNA-binding domainUniRule annotation1 PublicationAdd BLAST81

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.

P03120-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
METLCQRLNV CQDKILTHYE NDSTDLRDHI DYWKHMRLEC AIYYKAREMG
60 70 80 90 100
FKHINHQVVP TLAVSKNKAL QAIELQLTLE TIYNSQYSNE KWTLQDVSLE
110 120 130 140 150
VYLTAPTGCI KKHGYTVEVQ FDGDICNTMH YTNWTHIYIC EEASVTVVEG
160 170 180 190 200
QVDYYGLYYV HEGIRTYFVQ FKDDAEKYSK NKVWEVHAGG QVILCPTSVF
210 220 230 240 250
SSNEVSSPEI IRQHLANHPA ATHTKAVALG TEETQTTIQR PRSEPDTGNP
260 270 280 290 300
CHTTKLLHRD SVDSAPILTA FNSSHKGRIN CNSNTTPIVH LKGDANTLKC
310 320 330 340 350
LRYRFKKHCT LYTAVSSTWH WTGHNVKHKS AIVTLTYDSE WQRDQFLSQV
360
KIPKTITVST GFMSI
Length:365
Mass (Da):41,825
Last modified:July 21, 1986 - v1
Checksum:i27581F82B246E112
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti77L → P in AAQ10715 (Ref. 2) Curated1
Sequence conflicti210I → T in AAQ10715 (Ref. 2) Curated1
Sequence conflicti219P → S in AAQ10715 (Ref. 2) Curated1
Sequence conflicti310T → K in AAQ10715 (Ref. 2) Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K02718 Genomic DNA. Translation: AAA46941.1.
AF536179 Genomic DNA. Translation: AAQ10715.1.
PIRiA03669. W2WLHS.
RefSeqiNP_041328.1. NC_001526.4.

Genome annotation databases

GeneIDi1489080.
KEGGivg:1489080.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K02718 Genomic DNA. Translation: AAA46941.1.
AF536179 Genomic DNA. Translation: AAQ10715.1.
PIRiA03669. W2WLHS.
RefSeqiNP_041328.1. NC_001526.4.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1BY9X-ray2.20A285-365[»]
1DTOX-ray1.90A1-201[»]
1R8PNMR-A/B286-365[»]
1ZZFNMR-A/B286-365[»]
2NNUX-ray1.59A1-201[»]
2Q79X-ray1.80A285-365[»]
3MI7X-ray2.20X283-365[»]
ProteinModelPortaliP03120.
SMRiP03120.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-44574N.
IntActiP03120. 19 interactors.
MINTiMINT-95621.

Chemistry databases

BindingDBiP03120.
ChEMBLiCHEMBL4656.

PTM databases

iPTMnetiP03120.

Proteomic databases

PRIDEiP03120.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi1489080.
KEGGivg:1489080.

Miscellaneous databases

EvolutionaryTraceiP03120.
PROiP03120.

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_HPV16
AccessioniPrimary (citable) accession number: P03120
Secondary accession number(s): Q71BI4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: November 2, 2016
This is version 137 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Miscellaneous

HPV16, in comparison to HPV types 6 and 11, is more often associated with malignant genital cancers in humans.

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.