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Protein

Replication protein E1

Gene

E1

Organism
Human papillomavirus type 11
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

ATP-dependent DNA helicase required for initiation of viral DNA replication. It forms a complex with the viral E2 protein. The E1-E2 complex binds to the replication origin which contains binding sites for both proteins. During the initial step, a dimer of E1 interacts with a dimer of protein E2 leading to a complex that binds the viral origin of replication with high specificity. Then, a second dimer of E1 displaces the E2 dimer in an ATP-dependent manner to form the E1 tetramer. Following this, two E1 monomers are added to each half of the site, which results in the formation of two E1 trimers on the viral ori. Subsequently, two hexamers will be created. The double hexamer acts as a bi-directional helicase machinery and unwinds the viral DNA and then recruits the host DNA polymerase to start replication.UniRule annotation

Catalytic activityi

ATP + H2O = ADP + phosphate.UniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi478 – 4858ATPUniRule annotation

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • ATP-dependent DNA helicase activity Source: InterPro
  • DNA binding Source: UniProtKB
  • DNA helicase activity Source: UniProtKB
  • TPR domain binding Source: BHF-UCL

GO - Biological processi

  • bidirectional double-stranded viral DNA replication Source: UniProtKB
  • DNA duplex unwinding Source: UniProtKB
  • protein hexamerization Source: UniProtKB
  • viral DNA genome replication Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Helicase, Hydrolase

Keywords - Biological processi

DNA replication

Keywords - Ligandi

ATP-binding, DNA-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi3.6.4.12. 10313.

Names & Taxonomyi

Protein namesi
Recommended name:
Replication protein E1UniRule annotation (EC:3.6.4.12UniRule annotation)
Alternative name(s):
ATP-dependent helicase E1UniRule annotation
Gene namesi
Name:E1UniRule annotation
OrganismiHuman papillomavirus type 11
Taxonomic identifieri10580 [NCBI]
Taxonomic lineageiVirusesdsDNA viruses, no RNA stagePapillomaviridaeAlphapapillomavirus
Virus hostiHomo sapiens (Human) [TaxID: 9606]
Proteomesi
  • UP000008222 Componenti: Genome

Subcellular locationi

  • Host nucleus UniRule annotation1 Publication

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Host nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi89 – 891S → A: About 60% loss of nuclear localization. 1 Publication
Mutagenesisi93 – 931S → A: About 60% loss of nuclear localization. 1 Publication
Mutagenesisi107 – 1071S → A: More than 80% loss of nuclear localization. 1 Publication

Chemistry

ChEMBLiCHEMBL4953.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 649649Replication protein E1PRO_0000133109Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei89 – 891Phosphoserine; by hostUniRule annotation
Modified residuei93 – 931Phosphoserine; by hostUniRule annotation
Modified residuei107 – 1071Phosphoserine; by hostUniRule annotation
Cross-linki559 – 559Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)UniRule annotation

Post-translational modificationi

Phosphorylated.UniRule annotation
Sumoylated.UniRule annotation

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Expressioni

Keywords - Developmental stagei

Early protein

Interactioni

Subunit structurei

Can form hexamers. Interacts with E2 protein; this interaction increases E1 DNA binding specificity. Interacts with host DNA polymerase subunit POLA2. Interacts with host single stranded DNA-binding protein RPA1. Interacts with host TOP1; this interaction stimulates the enzymatic activity of TOP1.UniRule annotation

Binary interactionsi

WithEntry#Exp.IntActNotes
H1F0P073052EBI-7014446,EBI-725224From a different organism.
POLA1P098842EBI-7014446,EBI-850026From a different organism.

GO - Molecular functioni

  • TPR domain binding Source: BHF-UCL

Protein-protein interaction databases

IntActiP04014. 5 interactions.
MINTiMINT-95113.

Chemistry

BindingDBiP04014.

Structurei

3D structure databases

ProteinModelPortaliP04014.
SMRiP04014. Positions 205-348, 354-623.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini452 – 602151SF3 helicaseUniRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni187 – 353167DNA-binding regionUniRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi83 – 853Nuclear localization signalUniRule annotation
Motifi106 – 11510Nuclear export signalUniRule annotation1 Publication

Sequence similaritiesi

Belongs to the papillomaviridae E1 protein family.UniRule annotation
Contains 1 SF3 helicase domain.UniRule annotation

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
HAMAPiMF_04000. PPV_E1.
InterProiIPR001177. DNA_helicase_E1_C_Papillomavir.
IPR014000. DNA_helicase_E1_N_Papillomavir.
IPR014015. Helicase_SF3_DNA-vir.
IPR027417. P-loop_NTPase.
IPR016393. Rep_E1_papillomaV.
[Graphical view]
PfamiPF00519. PPV_E1_C. 1 hit.
PF00524. PPV_E1_N. 1 hit.
[Graphical view]
PIRSFiPIRSF003383. Rep_E1_papillomaV. 1 hit.
SUPFAMiSSF52540. SSF52540. 1 hit.
PROSITEiPS51206. SF3_HELICASE_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P04014-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MADDSGTENE GSGCTGWFMV EAIVEHTTGT QISEDEEEEV EDSGYDMVDF
60 70 80 90 100
IDDRHITQNS VEAQALFNRQ EADAHYATVQ DLKRKYLGSP YVSPISNVAN
110 120 130 140 150
AVESEISPRL DAIKLTTQPK KVKRRLFETR ELTDSGYGYS EVEAATQVEK
160 170 180 190 200
HGDPENGGDG QERDTGRDIE GEGVEHREAE AVDDSTREHA DTSGILELLK
210 220 230 240 250
CKDIRSTLHG KFKDCFGLSF VDLIRPFKSD RTTCADWVVA GFGIHHSIAD
260 270 280 290 300
AFQKLIEPLS LYAHIQWLTN AWGMVLLVLI RFKVNKSRCT VARTLGTLLN
310 320 330 340 350
IPENHMLIEP PKIQSGVRAL YWFRTGISNA STVIGEAPEW ITRQTVIEHS
360 370 380 390 400
LADSQFKLTE MVQWAYDNDI CEESEIAFEY AQRGDFDSNA RAFLNSNMQA
410 420 430 440 450
KYVKDCAIMC RHYKHAEMKK MSIKQWIKYR GTKVDSVGNW KPIVQFLRHQ
460 470 480 490 500
NIEFIPFLSK LKLWLHGTPK KNCIAIVGPP DTGKSCFCMS LIKFLGGTVI
510 520 530 540 550
SYVNSCSHFW LQPLTDAKVA LLDDATQPCW TYMDTYMRNL LDGNPMSIDR
560 570 580 590 600
KHRALTLIKC PPLLVTSNID ISKEEKYKYL HSRVTTFTFP NPFPFDRNGN
610 620 630 640
AVYELSDANW KCFFERLSSS LDIEDSEDEE DGSNSQAFRC VPGSVVRTL
Length:649
Mass (Da):73,530
Last modified:October 23, 1986 - v1
Checksum:i6665BE1E55B265A8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M14119 Genomic DNA. Translation: AAA46929.1.
PIRiA03659. W1WL11.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M14119 Genomic DNA. Translation: AAA46929.1.
PIRiA03659. W1WL11.

3D structure databases

ProteinModelPortaliP04014.
SMRiP04014. Positions 205-348, 354-623.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP04014. 5 interactions.
MINTiMINT-95113.

Chemistry

BindingDBiP04014.
ChEMBLiCHEMBL4953.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi3.6.4.12. 10313.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
HAMAPiMF_04000. PPV_E1.
InterProiIPR001177. DNA_helicase_E1_C_Papillomavir.
IPR014000. DNA_helicase_E1_N_Papillomavir.
IPR014015. Helicase_SF3_DNA-vir.
IPR027417. P-loop_NTPase.
IPR016393. Rep_E1_papillomaV.
[Graphical view]
PfamiPF00519. PPV_E1_C. 1 hit.
PF00524. PPV_E1_N. 1 hit.
[Graphical view]
PIRSFiPIRSF003383. Rep_E1_papillomaV. 1 hit.
SUPFAMiSSF52540. SSF52540. 1 hit.
PROSITEiPS51206. SF3_HELICASE_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The nucleotide sequence and genome organization of human papilloma virus type 11."
    Dartmann K., Schwarz E., Gissmann L., zur Hausen H.
    Virology 151:124-130(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Cyclin/CDK regulates the nucleocytoplasmic localization of the human papillomavirus E1 DNA helicase."
    Deng W., Lin B.Y., Jin G., Wheeler C.G., Ma T., Harper J.W., Broker T.R., Chow L.T.
    J. Virol. 78:13954-13965(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEAR EXPORT SIGNAL, SUBCELLULAR LOCATION, MUTAGENESIS OF SER-89; SER-93 AND SER-107.

Entry informationi

Entry nameiVE1_HPV11
AccessioniPrimary (citable) accession number: P04014
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 23, 1986
Last sequence update: October 23, 1986
Last modified: May 11, 2016
This is version 84 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

Complete proteome, Reference proteome

Documents

  1. 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.