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Protein

Core-capsid bridging protein

Gene

L2

Organism
Human adenovirus C serotype 5 (HAdV-5) (Human adenovirus 5)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Associates loosely with the viral dsDNA to form an outer shell around the nucleoprotein-DNA complex and links it with the capsid by binding the endosome lysis protein (PubMed:7175505, PubMed:24899200, PubMed:25071205). Dissociates from the viral genome during entry (By similarity). Might be involved in nuclear capsid assembly of the viral particles through its association with NPM1/nucleophosmin (By similarity).By similarity3 Publications

GO - Molecular functioni

  • DNA binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Viral capsid assembly, Virus exit from host cell

Keywords - Ligandi

DNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Core-capsid bridging protein
Alternative name(s):
Core protein V
Gene namesi
ORF Names:L2
OrganismiHuman adenovirus C serotype 5 (HAdV-5) (Human adenovirus 5)
Taxonomic identifieri28285 [NCBI]
Taxonomic lineageiVirusesdsDNA viruses, no RNA stageAdenoviridaeMastadenovirus
Virus hostiHomo sapiens (Human) [TaxID: 9606]
Proteomesi
  • UP000004992 Componenti: Genome

Subcellular locationi

  • Virion 1 Publication
  • Host nucleushost nucleolus By similarity

  • Note: Located inside the capsid (core) (PubMed:25071205). Present in 157 copies per virion. Localizes in the nucleoli during infection, then translocates from the nucleoli to the nucleoplasm as the infection progresses and is finally incorporated into the viral particles (By similarity).By similarity1 Publication

GO - Cellular componenti

  • host cell nucleolus Source: UniProtKB-SubCell
  • viral capsid Source: CACAO
  • virion Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Host nucleus, Virion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 368368Core-capsid bridging proteinPRO_0000221904Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei84 – 841Phosphothreonine; by hostBy similarity
Modified residuei165 – 1651Phosphoserine; by hostBy similarity

Keywords - PTMi

Phosphoprotein

Expressioni

Inductioni

Expressed in the late phase of the viral replicative cycle.

Keywords - Developmental stagei

Late protein

Interactioni

Subunit structurei

Monomer (PubMed:24899200). Homodimer (PubMed:24899200). Exists in equilibrium between monomers and dimers in solution (PubMed:24899200). Interacts with the histone-like nucleoprotein; this interactions bridge the virus core to the capsid (By similarity). Interacts with core protein X; this interactions bridge the virus core to the capsid (By similarity). Part of a complex composed of the core-capsid bridging protein, the endosome lysis protein VI and the hexon-linking protein VIII; these interactions bridge the virus core to the capsid (PubMed:25071205). Interacts with the peripentonal hexons (PubMed:25071205). Interacts with host NPM1; this interaction might play a role in virus assembly (By similarity).By similarity2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
NPM1P067484EBI-7481199,EBI-78579From a different organism.

Protein-protein interaction databases

IntActiP24938. 2 interactions.
MINTiMINT-4981252.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4CWUX-ray3.80T1-368[»]
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi23 – 4220Lys-richAdd
BLAST
Compositional biasi43 – 464Poly-Asp
Compositional biasi309 – 35446Arg-richAdd
BLAST

Sequence similaritiesi

Family and domain databases

InterProiIPR005608. Adeno_PV.
[Graphical view]
PfamiPF03910. Adeno_PV. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P24938-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSKRKIKEEM LQVIAPEIYG PPKKEEQDYK PRKLKRVKKK KKDDDDELDD
60 70 80 90 100
EVELLHATAP RRRVQWKGRR VKRVLRPGTT VVFTPGERST RTYKRVYDEV
110 120 130 140 150
YGDEDLLEQA NERLGEFAYG KRHKDMLALP LDEGNPTPSL KPVTLQQVLP
160 170 180 190 200
ALAPSEEKRG LKRESGDLAP TVQLMVPKRQ RLEDVLEKMT VEPGLEPEVR
210 220 230 240 250
VRPIKQVAPG LGVQTVDVQI PTTSSTSIAT ATEGMETQTS PVASAVADAA
260 270 280 290 300
VQAVAAAASK TSTEVQTDPW MFRVSAPRRP RGSRKYGAAS ALLPEYALHP
310 320 330 340 350
SIAPTPGYRG YTYRPRRRAT TRRRTTTGTR RRRRRRQPVL APISVRRVAR
360
EGGRTLVLPT ARYHPSIV
Length:368
Mass (Da):41,447
Last modified:March 1, 1992 - v1
Checksum:i722E6C6D22C692A4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M73260 Genomic DNA. Translation: AAA96409.1.
PIRiC39449. FOADM5.
RefSeqiAP_000208.1. AC_000008.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M73260 Genomic DNA. Translation: AAA96409.1.
PIRiC39449. FOADM5.
RefSeqiAP_000208.1. AC_000008.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4CWUX-ray3.80T1-368[»]
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP24938. 2 interactions.
MINTiMINT-4981252.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

InterProiIPR005608. Adeno_PV.
[Graphical view]
PfamiPF03910. Adeno_PV. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The sequence of the genome of adenovirus type 5 and its comparison with the genome of adenovirus type 2."
    Chroboczek J., Bieber F., Jacrot B.
    Virology 186:280-285(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "De novo derivation of proteomes from transcriptomes for transcript and protein identification."
    Evans V.C., Barker G., Heesom K.J., Fan J., Bessant C., Matthews D.A.
    Nat. Methods 9:1207-1211(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "Nucleic acid-binding properties of adenovirus structural polypeptides."
    Russell W.C., Precious B.
    J. Gen. Virol. 63:69-79(1982) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DNA-BINDING.
  4. "Latest insights on adenovirus structure and assembly."
    San Martin C.
    Viruses 4:847-877(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  5. "Chromatin structure of adenovirus DNA throughout infection."
    Giberson A.N., Davidson A.R., Parks R.J.
    Nucleic Acids Res. 40:2369-2376(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  6. "Isolation and characterization of the DNA and protein binding activities of adenovirus core protein V."
    Perez-Vargas J., Vaughan R.C., Houser C., Hastie K.M., Kao C.C., Nemerow G.R.
    J. Virol. 88:9287-9296(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH THE ENDOSOME LYSIS PROTEIN VI, DNA-BINDING, SUBUNIT.
  7. "Structures and organization of adenovirus cement proteins provide insights into the role of capsid maturation in virus entry and infection."
    Reddy V.S., Nemerow G.R.
    Proc. Natl. Acad. Sci. U.S.A. 111:11715-11720(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.80 ANGSTROMS), IDENTIFICATION IN A COMPLEX WITH ENDOSOME LYSIS PROTEIN VI AND HEXON-LINKING PROTEIN VIII, INTERACTION WITH THE HEXON PROTEIN, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiCORE5_ADE05
AccessioniPrimary (citable) accession number: P24938
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: March 1, 1992
Last modified: June 8, 2016
This is version 49 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Miscellaneous

This protein is only encoded by mastadenoviruses, and may therefore play a role in mammals tropism.
All late proteins expressed from the major late promoter are produced by alternative splicing and alternative polyadenylation of the same gene giving rise to non-overlapping ORFs. A leader sequence is present in the N-terminus of all these mRNAs and is recognized by the viral shutoff protein to provide expression although conventional translation via ribosome scanning from the cap has been shut off in the host cell (By similarity).By similarity

Keywords - Technical termi

3D-structure, Complete proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.