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HPV11:VE1

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Species (Taxon ID) Human papillomavirus type 11. (10580)
Gene Name(s) E1
Protein Name(s) Replication protein E1

ATP-dependent helicase E1

External Links
UniProt P04014
EMBL M14119
PIR A03659
ProteinModelPortal P04014
SMR P04014
IntAct P04014
MINT MINT-95113
BindingDB P04014
ChEMBL CHEMBL4953
Proteomes UP000008222
GO GO:0042025
GO:0005524
GO:0004003
GO:0003677
GO:0030911
GO:0006260
Gene3D 3.40.50.300
InterPro IPR001177
IPR014000
IPR014015
IPR027417
IPR016393
Pfam PF00519
PF00524
PIRSF PIRSF003383
SUPFAM SSF52540
PROSITE PS51206

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:0030911

TPR domain binding

PMID:19008854[1]

ECO:0000021

UniProtKB:P09914


F

Figure S1 and S2. Co-immunoprecipitation assays confirm the binding of ATPase HPV11 E1 to the TPR2 domain of P56 (IFIT1) protein.

complete

GO:0042025

host cell nucleus

PMID:19008854[1]

ECO:0000314

C

Figure 1E, panel 1 (middle). Immunofluorescence confirms the location of HPV11 E1 in host cell nucleus.

complete

GO:0019079

viral genome replication

PMID:19008854[1]

ECO:0000314

P

Figure 6A. In vitro DNA replication assay confirms that HPV11 E1 is needed for de novo viral DNA synthesis.

complete

GO:0004003

ATP-dependent DNA helicase activity

PMID:19008854[1]

ECO:0000314

F

Figure 7A. The release of 32P-labelled oligonucleotide annealed to M13mp18 single-stranded DNA comfirms the ATP-dependent DNA helicase activity of E1.

complete

GO:0016887

ATPase activity

PMID:19008854[1]

ECO:0000314

F

Figure 7C shows ATPase activity of E1.

complete

enables

GO:0003677

DNA binding

PMID:9804845[2]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0032508

DNA duplex unwinding

PMID:12192057[3]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0039686

bidirectional double-stranded viral DNA replication

PMID:12192057[3]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0003678

DNA helicase activity

PMID:12192057[3]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0034214

protein hexamerization

PMID:12192057[3]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0003677

DNA binding

PMID:7592989[4]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0039693

viral DNA genome replication

PMID:7592989[4]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0030911

TPR domain binding

PMID:19008854[1]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P09914

F

Seeded From UniProt

complete

enables

GO:0003677

DNA binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR001177

F

Seeded From UniProt

complete

enables

GO:0004003

ATP-dependent DNA helicase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR001177

F

Seeded From UniProt

complete

enables

GO:0005524

ATP binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR001177

F

Seeded From UniProt

complete

involved_in

GO:0006260

DNA replication

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR001177

P

Seeded From UniProt

complete

enables

GO:0016817

hydrolase activity, acting on acid anhydrides

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR014000
InterPro:IPR016393

F

Seeded From UniProt

complete

enables

GO:0005524

ATP binding

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000242300

F

Seeded From UniProt

complete

part_of

GO:0042025

host cell nucleus

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000242300

C

Seeded From UniProt

complete

enables

GO:0004003

ATP-dependent DNA helicase activity

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000242300

F

Seeded From UniProt

complete

enables

GO:0003677

DNA binding

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000242300

F

Seeded From UniProt

complete

involved_in

GO:0006260

DNA replication

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000242300

P

Seeded From UniProt

complete

involved_in

GO:0006260

DNA replication

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0235

P

Seeded From UniProt

complete

enables

GO:0016787

hydrolase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0378

F

Seeded From UniProt

complete

enables

GO:0004386

helicase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0347

F

Seeded From UniProt

complete

enables

GO:0005524

ATP binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0067

F

Seeded From UniProt

complete

part_of

GO:0042025

host cell nucleus

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-1048
UniProtKB-SubCell:SL-0414

C

Seeded From UniProt

complete

enables

GO:0003677

DNA binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0238

F

Seeded From UniProt

complete

enables

GO:0000166

nucleotide binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0547

F

Seeded From UniProt

complete

Notes

References

See Help:References for how to manage references in GONUTS.

  1. 1.0 1.1 1.2 1.3 1.4 1.5 Terenzi, F et al. (2008) Interferon-inducible protein, P56, inhibits HPV DNA replication by binding to the viral protein E1. EMBO J. 27 3311-21 PubMed GONUTS page
  2. Liu, JS et al. (1998) Human Hsp70 and Hsp40 chaperone proteins facilitate human papillomavirus-11 E1 protein binding to the origin and stimulate cell-free DNA replication. J. Biol. Chem. 273 30704-12 PubMed GONUTS page
  3. 3.0 3.1 3.2 3.3 Lin, BY et al. (2002) Chaperone proteins abrogate inhibition of the human papillomavirus (HPV) E1 replicative helicase by the HPV E2 protein. Mol. Cell. Biol. 22 6592-604 PubMed GONUTS page
  4. 4.0 4.1 Liu, JS et al. (1995) The functions of human papillomavirus type 11 E1, E2, and E2C proteins in cell-free DNA replication. J. Biol. Chem. 270 27283-91 PubMed GONUTS page