[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. DOI=10.1016/0042-6822(85)90214-4; PubMed=2990099 [NCBI, ExPASy, EBI, Israel, Japan] Seedorf K., Krammer G., Durst M., Suhai S., Rowekamp W.G.; "Human papillomavirus type 16 DNA sequence."; Virology 145:181-185(1985).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=Isolate European German 131; Terai M., Fu L., Ma Z., Burk R.D.; "Cloning and sequencing of non-European human papillomavirus (HPV) variant complete genomes from cervicovaginal cells by an overlapping PCR method."; Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases.
[3]	FUNCTION. PubMed=3033289 [NCBI, ExPASy, EBI, Israel, Japan] Phelps W.C., Howley P.M.; "Transcriptional trans-activation by the human papillomavirus type 16 E2 gene product."; J. Virol. 61:1630-1638(1987).
[4]	X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1-201. DOI=10.1107/S0907444998010889; PubMed=10089541 [NCBI, ExPASy, EBI, Israel, Japan] Burns J.E., Moroz O.V., Antson A.A., Sanders C.M., Wilson K.S., Maitland N.J.; "Expression, crystallization and preliminary X-ray analysis of the E2 transactivation domain from papillomavirus type 16."; Acta Crystallogr. D 54:1471-1474(1998).

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.
SUBUNIT: Binds DNA as a dimer.
INTERACTION:
O60885:BRD4 (xeno); NbExp=2; IntAct=EBI-1779322, EBI-723869;
Q9H0C5:BTBD1 (xeno); NbExp=2; IntAct=EBI-1779322, EBI-935503;
Q9BX70:BTBD2 (xeno); NbExp=2; IntAct=EBI-1779322, EBI-710091;
Q8TD31:CCHCR1 (xeno); NbExp=2; IntAct=EBI-1779322, EBI-949834;
P31274:HOXC9 (xeno); NbExp=2; IntAct=EBI-1779322, EBI-1779423;
P22736:NR4A1 (xeno); NbExp=2; IntAct=EBI-1779322, EBI-721550;
Q15637:SF1 (xeno); NbExp=2; IntAct=EBI-1779322, EBI-744603;
P21675-2:TAF1 (xeno); NbExp=2; IntAct=EBI-1779322, EBI-491313;
P82094:TMF1 (xeno); NbExp=2; IntAct=EBI-1779322, EBI-949763;
SUBCELLULAR LOCATION: Nucleus.
MISCELLANEOUS: HPV16, in comparison to HPV types 6 and 11, is more often associated with malignant genital cancers in humans.
SIMILARITY: Belongs to the papillomaviridae E2 protein family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

K02718; AAA46941.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF536179; AAQ10715.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A03669; W2WLHS.

RefSeq

NP_041328.1; -.

3D structure databases

PDB

1BY9; X-ray; 2.20 A; A=285-365.	[ExPASy / RCSB / EBI]
1DTO; X-ray; 1.90 A; A=1-201.	[ExPASy / RCSB / EBI]
1R8P; NMR; -; A/B=286-365.	[ExPASy / RCSB / EBI]
1ZZF; NMR; -; A/B=286-365.	[ExPASy / RCSB / EBI]
2NNU; X-ray; 1.59 A; A=1-201.	[ExPASy / RCSB / EBI]
2Q79; X-ray; 1.80 A; A=285-365.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1BY9; -.
1DTO; -.
1R8P; -.
1ZZF; -.
2NNU; -.
2Q79; -.

ModBase

P03120.

Protein-protein interaction databases

IntAct

P03120; -.

Ontologies

GO:0005515;	Molecular function: protein binding (inferred from physical interaction from IntAct).
QuickGo view.

Family and domain databases

InterPro

IPR012677; a_b_plait_nuc_bd.
IPR000427; E2_C.
IPR001866; E2_N.
Graphical view of domain structure.

Gene3D

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

Pfam

PF00511; PPV_E2_C; 1.
PF00508; PPV_E2_N; 1.
Pfam graphical view of domain structure.

ProDom

PD000672; E2_C; 1.
PD000678; E2_N; 1.
[Domain structure / List of seq. sharing at least 1 domain]

Genome annotation databases

GeneID

1489080; -.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Activator; DNA replication; DNA-binding; Early protein; Nucleus; Repressor; Transcription; Transcription regulation.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 365`	`365`	`Regulatory protein E2.`	`PRO_0000133195`
`CONFLICT`	`77 77`		`L -> P (in Ref. 2; AAQ10715).`
`CONFLICT`	`210 210`		`I -> T (in Ref. 2; AAQ10715).`
`CONFLICT`	`219 219`		`P -> S (in Ref. 2; AAQ10715).`
`CONFLICT`	`310 310`		`T -> K (in Ref. 2; AAQ10715).`
`HELIX`	`1 21`	`21`
`HELIX`	`26 48`	`23`
`STRAND`	`52 54`	`3`
`HELIX`	`62 83`	`22`
`TURN`	`86 89`	`4`
`TURN`	`94 97`	`4`
`HELIX`	`99 102`	`4`
`STRAND`	`104 106`	`3`
`STRAND`	`111 122`	`12`
`STRAND`	`128 141`	`14`
`STRAND`	`144 148`	`5`
`STRAND`	`154 161`	`8`
`STRAND`	`164 170`	`7`
`HELIX`	`171 178`	`8`
`STRAND`	`180 182`	`3`
`STRAND`	`185 191`	`7`
`STRAND`	`286 293`	`8`
`HELIX`	`295 305`	`11`
`HELIX`	`306 311`	`6`
`STRAND`	`313 316`	`4`
`STRAND`	`331 336`	`6`
`HELIX`	`340 349`	`10`
`STRAND`	`356 363`	`8`

Sequence information

Length: 365 AA [This is the length of the unprocessed precursor]

Molecular weight: 41825 Da [This is the MW of the unprocessed precursor]

CRC64: 27581F82B246E112 [This is a checksum on the sequence]

        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

P03120 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools