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Protein

Regulatory protein E2

Gene

E2

Organism
Human papillomavirus type 31
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 31
Taxonomic identifieri10585 [NCBI]
Taxonomic lineageiVirusesdsDNA viruses, no RNA stagePapillomaviridaeAlphapapillomavirus
Virus hostiHomo sapiens (Human) [TaxID: 9606]
Proteomesi
  • UP000009116 Componenti: Genome

Subcellular locationi

  • Host nucleus UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Host nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 372372Regulatory protein E2PRO_0000133211Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki299 – 299Glycyl 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
BRD4O608852EBI-7010529,EBI-723869From a different organism.

Protein-protein interaction databases

IntActiP17383. 1 interaction.
MINTiMINT-6732762.

Structurei

Secondary structure

1
372
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi292 – 3009Combined sources
Helixi302 – 31110Combined sources
Helixi312 – 3143Combined sources
Helixi316 – 3183Combined sources
Beta strandi331 – 3333Combined sources
Turni334 – 3374Combined sources
Beta strandi338 – 3436Combined sources
Helixi347 – 35610Combined sources
Beta strandi363 – 3719Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1A7GX-ray2.40E291-372[»]
1DHMNMR-A/B291-372[»]
ProteinModelPortaliP17383.
SMRiP17383. Positions 1-200, 291-372.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP17383.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 200200Transactivation domainUniRule annotationAdd
BLAST
Regioni292 – 37281DNA-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.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
IPR000427. Papillomavirus_E2_C.
IPR001866. Papillomavirus_E2_N.
[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.

P17383-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
METLSQRLNV CQDKILEHYE NDSKRLCDHI DYWKHIRLEC VLMYKAREMG
60 70 80 90 100
IHSINHQVVP ALSVSKAKAL QAIELQMMLE TLNNTEYKNE DWTMQQTSLE
110 120 130 140 150
LYLTAPTGCL KKHGYTVEVQ FDGDVHNTMH YTNWKFIYLC IDGQCTVVEG
160 170 180 190 200
QVNCKGIYYV HEGHITYFVN FTEEAKKYGT GKKWEVHAGG QVIVFPESVF
210 220 230 240 250
SSDEISFAGI VTKLPTANNT TTSNSKTCAL GTSEGVRRAT TSTKRPRTEP
260 270 280 290 300
EHRNTHHPNK LLRGDSVDSV NCGVISAAAC TNQTRAVSCP ATTPIIHLKG
310 320 330 340 350
DANILKCLRY RLSKYKQLYE QVSSTWHWTC TDGKHKNAIV TLTYISTSQR
360 370
DDFLNTVKIP NTVSVSTGYM TI
Length:372
Mass (Da):42,104
Last modified:August 1, 1990 - v1
Checksum:i4F387C5E3AFB9D1D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J04353 Genomic DNA. Translation: AAA46953.1.
PIRiD32444. W2WL31.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J04353 Genomic DNA. Translation: AAA46953.1.
PIRiD32444. W2WL31.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1A7GX-ray2.40E291-372[»]
1DHMNMR-A/B291-372[»]
ProteinModelPortaliP17383.
SMRiP17383. Positions 1-200, 291-372.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP17383. 1 interaction.
MINTiMINT-6732762.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP17383.

Family and domain databases

Gene3Di2.170.200.10. 1 hit.
3.30.70.330. 1 hit.
HAMAPiMF_04001. PPV_E2.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
IPR000427. Papillomavirus_E2_C.
IPR001866. Papillomavirus_E2_N.
[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...

Publicationsi

  1. "Nucleotide sequence of human papillomavirus type 31: a cervical neoplasia-associated virus."
    Goldsborough M.D., Disilvestre D., Temple G.F., Lorincz A.T.
    Virology 171:306-311(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Solution structure of the DNA-binding domain of a human papillomavirus E2 protein: evidence for flexible DNA-binding regions."
    Liang H., Petros A.M., Meadows R.P., Yoon H.S., Egan D.A., Walter K., Holzman T.F., Robins T., Fesik S.W.
    Biochemistry 35:2095-2103(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 291-372.

Entry informationi

Entry nameiVE2_HPV31
AccessioniPrimary (citable) accession number: P17383
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: August 1, 1990
Last modified: January 20, 2016
This is version 107 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

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.