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Protein

Minor capsid protein L2

Gene

L2

Organism
Human papillomavirus type 16
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Minor protein of the capsid that localizes along the inner surface of the virion, within the central cavities beneath the L1 pentamers. Plays a role in capsid stabilization through interaction with the major capsid protein L1. Once the virion enters the host cell, L2 escorts the genomic DNA into the nucleus by promoting escape from the endosomal compartments and traffic through the host Golgi network. Plays a role through its interaction with host dynein in the intracellular microtubule-dependent transport of viral capsid toward the nucleus. Mediates the viral genome import into the nucleus through binding to host importins. Once within the nucleus, L2 localizes viral genomes to host PML bodies in order to activate early gene expression for establishment of infection. Later on, promotes late gene expression by interacting with the viral E2 protein and by inhibiting its transcriptional activation functions. During virion assembly, encapsidates the genome by direct interaction with the viral DNA.UniRule annotation4 Publications

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Cytoplasmic inwards viral transport, Host-virus interaction, Microtubular inwards viral transport, Viral penetration into host nucleus, Virus entry into host cell

Keywords - Ligandi

DNA-binding

Protein family/group databases

TCDBi1.A.86.1.1. the human papilloma virus type 16 (hpv16) l2 viroporin (l2 viroporin) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Minor capsid protein L2UniRule annotation
Gene namesi
Name:L2UniRule annotation
OrganismiHuman papillomavirus type 16
Taxonomic identifieri333760 [NCBI]
Taxonomic lineageiVirusesdsDNA viruses, no RNA stagePapillomaviridaeAlphapapillomavirus
Virus hostiHomo sapiens (Human) [TaxID: 9606]
Proteomesi
  • UP000009251 Componenti: Genome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Capsid protein, Host nucleus, Virion

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi22 – 221C → S: Complete loss of infectivity. 1 Publication
Mutagenesisi28 – 281C → S: Complete loss of infectivity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 473473Minor capsid protein L2PRO_0000133583Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi22 ↔ 28UniRule annotation1 Publication

Post-translational modificationi

Highly phosphorylated.UniRule annotation1 Publication

Keywords - PTMi

Disulfide bond, Phosphoprotein

Expressioni

Keywords - Developmental stagei

Late protein

Interactioni

Subunit structurei

Interacts with major capsid protein L1. Interacts with E2; this interaction inhibits E2 transcriptional activity but not the DNA replication function E2. Interacts with host GADD45GIP1. Interacts with host HSPA8; this interaction is required for L2 nuclear translocation. Interacts with host importins KPNB2 and KPNB3. Forms a complex with importin alpha2-beta1 heterodimers via interaction with the importin alpha2 adapter. Interacts with host DYNLT1; this interaction is essential for virus intracellular transport during entry.UniRule annotation6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
KPNA2P522923EBI-7362531,EBI-349938From a different organism.
KPNB1Q149742EBI-7362531,EBI-286758From a different organism.

Protein-protein interaction databases

IntActiP03107. 4 interactions.
MINTiMINT-253565.

Structurei

3D structure databases

ProteinModelPortaliP03107.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi1 – 1313Nuclear localization signalUniRule annotation1 PublicationAdd
BLAST
Motifi454 – 4629Nuclear localization signalUniRule annotation1 Publication

Sequence similaritiesi

Belongs to the papillomaviridae L2 protein family.UniRule annotation

Family and domain databases

HAMAPiMF_04003. PPV_L2.
InterProiIPR000784. Late_L2.
[Graphical view]
PfamiPF00513. Late_protein_L2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P03107-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRHKRSAKRT KRASATQLYK TCKQAGTCPP DIIPKVEGKT IAEQILQYGS
60 70 80 90 100
MGVFFGGLGI GTGSGTGGRT GYIPLGTRPP TATDTLAPVR PPLTVDPVGP
110 120 130 140 150
SDPSIVSLVE ETSFIDAGAP TSVPSIPPDV SGFSITTSTD TTPAILDINN
160 170 180 190 200
TVTTVTTHNN PTFTDPSVLQ PPTPAETGGH FTLSSSTIST HNYEEIPMDT
210 220 230 240 250
FIVSTNPNTV TSSTPIPGSR PVARLGLYSR TTQQVKVVDP AFVTTPTKLI
260 270 280 290 300
TYDNPAYEGI DVDNTLYFSS NDNSINIAPD PDFLDIVALH RPALTSRRTG
310 320 330 340 350
IRYSRIGNKQ TLRTRSGKSI GAKVHYYYDL STIDPAEEIE LQTITPSTYT
360 370 380 390 400
TTSHAASPTS INNGLYDIYA DDFITDTSTT PVPSVPSTSL SGYIPANTTI
410 420 430 440 450
PFGGAYNIPL VSGPDIPINI TDQAPSLIPI VPGSPQYTII ADAGDFYLHP
460 470
SYYMLRKRRK RLPYFFSDVS LAA
Length:473
Mass (Da):50,688
Last modified:July 21, 1986 - v1
Checksum:i18E64E793D760744
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti43 – 431E → D in AAQ10718 (Ref. 2) Curated
Sequence conflicti269 – 2691S → P in AAQ10718 (Ref. 2) Curated
Sequence conflicti353 – 3531S → L in AAQ10718 (Ref. 2) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K02718 Genomic DNA. Translation: AAA46942.1.
AF536179 Genomic DNA. Translation: AAQ10718.1.
PIRiA03649. P2WLHS.
RefSeqiNP_041331.1. NC_001526.2.

Genome annotation databases

GeneIDi1489081.
KEGGivg:1489081.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K02718 Genomic DNA. Translation: AAA46942.1.
AF536179 Genomic DNA. Translation: AAQ10718.1.
PIRiA03649. P2WLHS.
RefSeqiNP_041331.1. NC_001526.2.

3D structure databases

ProteinModelPortaliP03107.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP03107. 4 interactions.
MINTiMINT-253565.

Protein family/group databases

TCDBi1.A.86.1.1. the human papilloma virus type 16 (hpv16) l2 viroporin (l2 viroporin) family.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi1489081.
KEGGivg:1489081.

Family and domain databases

HAMAPiMF_04003. PPV_L2.
InterProiIPR000784. Late_L2.
[Graphical view]
PfamiPF00513. Late_protein_L2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. 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. "Baculovirus expression of the human papillomavirus type 16 capsid proteins: detection of L1-L2 protein complexes."
    Xi S.Z., Banks L.M.
    J. Gen. Virol. 72:2981-2988(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PROTEIN L1, PHOSPHORYLATION.
  4. "Interaction of human papillomavirus type 16 L2 with cellular proteins: identification of novel nuclear body-associated proteins."
    Goernemann J., Hofmann T.G., Will H., Mueller M.
    Virology 303:69-78(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HUMAN GADD45GIP1.
    Tissue: Keratinocyte.
  5. "Interaction of human papillomavirus (HPV) type 16 capsid proteins with HPV DNA requires an intact L2 N-terminal sequence."
    Zhou J., Sun X.Y., Louis K., Frazer I.H.
    J. Virol. 68:619-625(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: DNA-BINDING.
  6. "Human papillomavirus type 16 capsid proteins produced from recombinant Semliki Forest virus assemble into virus-like particles."
    Heino P., Dillner J., Schwartz S.
    Virology 214:349-359(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. "Nuclear translocation of papillomavirus minor capsid protein L2 requires Hsc70."
    Florin L., Becker K.A., Sapp C., Lambert C., Sirma H., Muller M., Streeck R.E., Sapp M.
    J. Virol. 78:5546-5553(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HOST HSPA8.
  8. "The l2 minor capsid protein of human papillomavirus type 16 interacts with a network of nuclear import receptors."
    Darshan M.S., Lucchi J., Harding E., Moroianu J.
    J. Virol. 78:12179-12188(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH IMPORTINS KPNB2 AND KPNB3, NUCLEAR LOCALIZATION SIGNALS.
  9. "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] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH E2.
  10. "Expression pattern and subcellular localization of human papillomavirus minor capsid protein L2."
    Lin Z., Yemelyanova A.V., Gambhira R., Jagu S., Meyers C., Kirnbauer R., Ronnett B.M., Gravitt P.E., Roden R.B.
    Am. J. Pathol. 174:136-143(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  11. "Two highly conserved cysteine residues in HPV16 L2 form an intramolecular disulfide bond and are critical for infectivity in human keratinocytes."
    Campos S.K., Ozbun M.A.
    PLoS ONE 4:E4463-E4463(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF CYS-22 AND CYS-28, DISULFIDE BOND.
  12. "Identification of the dynein light chains required for human papillomavirus infection."
    Schneider M.A., Spoden G.A., Florin L., Lambert C.
    Cell. Microbiol. 13:32-46(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH HUMAN DYNLT1.
  13. "Cleavage of the HPV16 minor capsid protein L2 during virion morphogenesis ablates the requirement for cellular furin during De Novo infection."
    Cruz L., Biryukov J., Conway M.J., Meyers C.
    Viruses 7:5813-5830(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: CLEAVAGE BY HOST FURIN.

Entry informationi

Entry nameiVL2_HPV16
AccessioniPrimary (citable) accession number: P03107
Secondary accession number(s): Q71BI1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: June 8, 2016
This is version 78 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Miscellaneous

HPV16, in comparison to HPV types 6 and 11, is more often associated with malignant genital cancers in humans.

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.