Regulatory protein E2 - Human papillomavirus type 16

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Reviewed, UniProtKB/Swiss-Prot P03120 (VE2_HPV16)

Last modified June 16, 2009. Version 82. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein names

Recommended name:
Regulatory protein E2

Gene names

Name:

E2

Organism

Human papillomavirus type 16

Taxonomic identifier

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.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	E2 regulates viral transcription and DNA replication. It binds to the E2RE response element (5'-ACCNNNNNNGGT-3') present in multiple copies in the regulatory region. It can either activate or repress transcription depending on E2RE's position with regards to proximal promoter elements. Repression occurs by sterically hindering the assembly of the transcription initiation complex. The E1-E2 complex binds to the origin of DNA replication. Ref.3
Subunit structure	Binds DNA as a dimer.
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	Nucleus
Developmental stage	Early protein
Ligand	DNA-binding
Molecular function	Activator Repressor
Technical term	3D-structure
Gene Ontology (GO)
Biological process	DNA replication Inferred from electronic annotation. Source: UniProtKB-KW regulation of DNA replication Inferred from electronic annotation. Source: InterPro regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW transcription 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 nucleus Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	nucleotide binding Inferred from electronic annotation. Source: InterPro protein binding Inferred from physical interaction. Source: IntAct transcription factor activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
BRD4	O60885	2	EBI-1779322,EBI-723869	From a different organism.
BTBD1	Q9H0C5	2	EBI-1779322,EBI-935503	From a different organism.
BTBD2	Q9BX70	2	EBI-1779322,EBI-710091	From a different organism.
CCHCR1	Q8TD31	2	EBI-1779322,EBI-949834	From a different organism.
HOXC9	P31274	2	EBI-1779322,EBI-1779423	From a different organism.
NR4A1	P22736	2	EBI-1779322,EBI-721550	From a different organism.
SF1	Q15637	2	EBI-1779322,EBI-744603	From a different organism.
TAF1	P21675-2	2	EBI-1779322,EBI-491313	From a different organism.
TMF1	P82094	2	EBI-1779322,EBI-949763	From a different organism.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

365

Regulatory protein E2

PRO_0000133195

Experimental info

Sequence conflict

1

L → P in AAQ10715. Ref.2

Sequence conflict

1

I → T in AAQ10715. Ref.2

Sequence conflict

1

P → S in AAQ10715. Ref.2

Sequence conflict

1

T → K in AAQ10715. Ref.2

Secondary structure

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365

Helix Strand Turn

Sequences

Sequence

Length

Mass (Da)

Tools

P03120-1 [UniParc].

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

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

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]	"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

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

PIR

W2WLHS. A03669.

RefSeq

3D structure databases

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	[»]

ModBase

Protein-protein interaction databases

IntAct

P03120. 11 interactions.

Genome annotation databases

GeneID

Family and domain databases

InterPro

IPR012677. a_b_plait_nuc_bd.
IPR000427. E2_early_recog_prot_C.
IPR001866. 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_C. 1 hit.
PD000678. E2_N. 1 hit.
[Graphical view] [Entries sharing at least one domain]

ProtoNet

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:	June 16, 2009
This is version 82 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Virus (Virus annotation project)

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents