Regulatory protein E2 - Human papillomavirus type 16

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P03120 (VE2_HPV16) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 101. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Regulatory protein E2

Gene names

Name:

Organism

Human papillomavirus type 16

Taxonomic identifier

333760 [NCBI]

Taxonomic lineage

Viruses › dsDNA viruses, no RNA stage › Papillomaviridae › Alphapapillomavirus

Virus host

Homo sapiens (Human) [TaxID: 9606]

Protein attributes

Sequence length	365 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Plays an accessory role in initiation of 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. Ref.3 Ref.4 Ref.5
Subunit structure	Interacts with the E1 protein; this interaction greatly increases E1 DNA-binding specificity. Interacts with L2; this interaction inhibits E2 transcriptional activity but not the DNA replication function E2. Interacts with E7; this interaction inhibits E7 oncogenic activity. Interacts with host TAF1; this interaction modulates E2-dependent transcriptional regulation. Ref.5 Ref.6 Ref.7
Subcellular location	Host nucleus.
Miscellaneous	HPV16, in comparison to HPV types 6 and 11, is more often associated with malignant genital cancers in humans.
Sequence similarities	Belongs to the papillomaviridae E2 protein family.

Ontologies

Keywords
Biological process	DNA replication Transcription Transcription regulation
Cellular component	Host nucleus
Developmental stage	Early protein
Ligand	DNA-binding
Molecular function	Activator Repressor
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	DNA replication Inferred from electronic annotation. Source: UniProtKB-KW regulation of DNA replication Inferred from electronic annotation. Source: InterPro transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW viral reproduction Inferred from electronic annotation. Source: InterPro
Cellular component	host cell nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	DNA binding Inferred from electronic annotation. Source: UniProtKB-KW nucleotide binding Inferred from electronic annotation. Source: InterPro sequence-specific DNA binding transcription factor activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 365

365

Regulatory protein E2

PRO_0000133195

Experimental info

Sequence conflict

L → P in AAQ10715. Ref.2

Sequence conflict

210

I → T in AAQ10715. Ref.2

Sequence conflict

219

P → S in AAQ10715. Ref.2

Sequence conflict

310

T → K in AAQ10715. Ref.2

Secondary structure

365

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P03120 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: 27581F82B246E112
Show »

FASTA

365

41,825

        10         20         30         40         50         60 
METLCQRLNV CQDKILTHYE NDSTDLRDHI DYWKHMRLEC AIYYKAREMG FKHINHQVVP 

        70         80         90        100        110        120 
TLAVSKNKAL QAIELQLTLE TIYNSQYSNE KWTLQDVSLE VYLTAPTGCI KKHGYTVEVQ 

       130        140        150        160        170        180 
FDGDICNTMH YTNWTHIYIC EEASVTVVEG QVDYYGLYYV HEGIRTYFVQ FKDDAEKYSK 

       190        200        210        220        230        240 
NKVWEVHAGG QVILCPTSVF SSNEVSSPEI IRQHLANHPA ATHTKAVALG TEETQTTIQR 

       250        260        270        280        290        300 
PRSEPDTGNP CHTTKLLHRD SVDSAPILTA FNSSHKGRIN CNSNTTPIVH LKGDANTLKC 

       310        320        330        340        350        360 
LRYRFKKHCT LYTAVSSTWH WTGHNVKHKS AIVTLTYDSE WQRDQFLSQV KIPKTITVST 


GFMSI

« Hide

References

[1]	"Human papillomavirus type 16 DNA sequence." Seedorf K., Krammer G., Durst M., Suhai S., Rowekamp W.G. Virology 145:181-185(1985) [PubMed: 2990099] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Cloning and sequencing of non-European human papillomavirus (HPV) variant complete genomes from cervicovaginal cells by an overlapping PCR method." Terai M., Fu L., Ma Z., Burk R.D. Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: Isolate European German 131.
[3]	"Transcriptional trans-activation by the human papillomavirus type 16 E2 gene product." Phelps W.C., Howley P.M. J. Virol. 61:1630-1638(1987) [PubMed: 3033289] [Abstract] Cited for: FUNCTION.
[4]	"Transient replication of human papillomavirus DNAs." Del Vecchio A.M., Romanczuk H., Howley P.M., Baker C.C. J. Virol. 66:5949-5958(1992) [PubMed: 1326651] [Abstract] Cited for: FUNCTION.
[5]	"Human papillomavirus 16 L2 inhibits the transcriptional activation function, but not the DNA replication function, of HPV-16 E2." Okoye A., Cordano P., Taylor E.R., Morgan I.M., Everett R., Campo M.S. Virus Res. 108:1-14(2005) [PubMed: 15681049] [Abstract] Cited for: FUNCTION, INTERACTION WITH L2.
[6]	"Regulation of human papillomavirus type 16 E7 activity through direct protein interaction with the E2 transcriptional activator." Gammoh N., Grm H.S., Massimi P., Banks L. J. Virol. 80:1787-1797(2006) [PubMed: 16439535] [Abstract] Cited for: INTERACTION WITH E7.
[7]	"TAF1 interacts with and modulates human papillomavirus 16 E2-dependent transcriptional regulation." Centeno F., Ramirez-Salazar E., Garcia-Villa E., Gariglio P., Garrido E. Intervirology 51:137-143(2008) [PubMed: 18580066] [Abstract] Cited for: INTERACTION WITH HOST TAF1.
[8]	"Expression, crystallization and preliminary X-ray analysis of the E2 transactivation domain from papillomavirus type 16." Burns J.E., Moroz O.V., Antson A.A., Sanders C.M., Wilson K.S., Maitland N.J. Acta Crystallogr. D 54:1471-1474(1998) [PubMed: 10089541] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1-201.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

K02718 Genomic DNA. Translation: AAA46941.1.
AF536179 Genomic DNA. Translation: AAQ10715.1.

PIR

W2WLHS. A03669.

RefSeq

NP_041328.1. NC_001526.2.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1BY9	X-ray	2.20	A	285-365	[»]
1DTO	X-ray	1.90	A	1-201	[»]
1R8P	NMR	-	A/B	286-365	[»]
1ZZF	NMR	-	A/B	286-365	[»]
2NNU	X-ray	1.59	A	1-201	[»]
2Q79	X-ray	1.80	A	285-365	[»]
3MI7	X-ray	2.20	X	283-365	[»]

ProteinModelPortal

P03120.

SMR

P03120. Positions 1-200, 286-365.

ModBase

Search...

Protein-protein interaction databases

IntAct

P03120. 9 interactions.

MINT

MINT-95621.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

1489080.

Family and domain databases

InterPro

IPR012677. Nucleotide-bd_a/b_plait.
IPR000427. Papillomavirus_E2_C.
IPR001866. Papillomavirus_E2_N.
[Graphical view]

Gene3D

G3DSA:3.30.70.330. a_b_plait_nuc_bd. 1 hit.
G3DSA:2.170.200.10. E2_N. 1 hit.

Pfam

PF00511. PPV_E2_C. 1 hit.
PF00508. PPV_E2_N. 1 hit.
[Graphical view]

ProDom

PD000672. E2_early_recog_prot_C. 1 hit.
[Graphical view] [Entries sharing at least one domain]

SUPFAM

SSF51332. E2_N. 1 hit.
SSF54957. Viral_DNA_bd. 1 hit.

ProtoNet

Search...

Entry information

Entry name

VE2_HPV16

Accession

Primary (citable) accession number: P03120
Secondary accession number(s): Q71BI4

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 21, 1986
Last modified:	December 14, 2011
This is version 101 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Viral Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Family and domain databases

Entry information

Relevant documents