Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P03281

- CAP9_ADE05

UniProt

P03281 - CAP9_ADE05

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Hexon-interlacing protein

Gene

IX

Organism
Human adenovirus C serotype 5 (HAdV-5) (Human adenovirus 5)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli

Functioni

Structural component of the virion that presumably stabilizes the groups of hexons but is dispensable for assembly. During virus entry, recruits the anterograde motor kinesin-1 to the capsid docked at the nuclear pore complex thereby subjecting the docked capsid to a pulling force. The resulting tension leads to capsid disruption, dispersion of capsid fragments toward cell periphery and eventually viral DNA entry into the host nucleus.1 Publication

GO - Biological processi

  1. viral entry into host cell Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Host-virus interaction, Virus entry into host cell

Names & Taxonomyi

Protein namesi
Recommended name:
Hexon-interlacing protein
Alternative name(s):
Protein IX
Gene namesi
ORF Names:IX
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]
ProteomesiUP000004992: Genome

Subcellular locationi

Virion 1 Publication. Host nucleus 1 Publication
Note: Located in the canyons between the hexons on the outer surface of the capsid. Forms a sort of hairnet on the outer side of the virion. Present in 240 copies per virion.

GO - Cellular componenti

  1. host cell nucleus Source: UniProtKB-KW
  2. viral capsid Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Capsid protein, Host nucleus, Virion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 140140Hexon-interlacing proteinPRO_0000221846Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei135 – 1351Phosphoserine; by hostBy similarity

Keywords - PTMi

Phosphoprotein

Expressioni

Inductioni

Expressed in the intermediate phase of the viral replicative cycle.

Interactioni

Subunit structurei

Homotrimer. Interacts with hexon protein; this interaction tethers the hexons together. Self-interacts with adjacent proteins. Interacts with kinesin light chain KLC1; this interaction leads to capsid disruption at the nuclear pore complex during virus entry into host cell.1 Publication

Protein-protein interaction databases

DIPiDIP-29895N.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3IYNelectron microscopy-Q/R/S/T1-140[»]
4CWUX-ray3.80P/Q/R/S1-140[»]
ProteinModelPortaliP03281.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP03281.

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili97 – 13337Sequence AnalysisAdd
BLAST

Domaini

Three N-terminal domains of hexon-interlacing protein form triskelions between hexon capsomers.

Sequence similaritiesi

Keywords - Domaini

Coiled coil

Family and domain databases

InterProiIPR005641. Hexon_assoc_IX.
[Graphical view]
PfamiPF03955. Adeno_PIX. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P03281-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSTNSFDGSI VSSYLTTRMP PWAGVRQNVM GSSIDGRPVL PANSTTLTYE
60 70 80 90 100
TVSGTPLETA ASAAASAAAA TARGIVTDFA FLSPLASSAA SRSSARDDKL
110 120 130 140
TALLAQLDSL TRELNVVSQQ LLDLRQQVSA LKASSPPNAV
Length:140
Mass (Da):14,458
Last modified:July 21, 1986 - v1
Checksum:iDAFD4045CAB616FB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M73260 Genomic DNA. No translation available.
X02996 Genomic DNA. Translation: CAA26746.1.
PIRiA03853. SXAD95.
RefSeqiAP_000200.1. AC_000008.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M73260 Genomic DNA. No translation available.
X02996 Genomic DNA. Translation: CAA26746.1 .
PIRi A03853. SXAD95.
RefSeqi AP_000200.1. AC_000008.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3IYN electron microscopy - Q/R/S/T 1-140 [» ]
4CWU X-ray 3.80 P/Q/R/S 1-140 [» ]
ProteinModelPortali P03281.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-29895N.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei P03281.

Family and domain databases

InterProi IPR005641. Hexon_assoc_IX.
[Graphical view ]
Pfami PF03955. Adeno_PIX. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "The 2.2 kb E1b mRNA of human Ad12 and Ad5 codes for two tumor antigens starting at different AUG triplets."
    Bos J.L., Polder L.J., Bernards R., Schrier P.I., van den Elsen P.J., van der Eb A.J., van Ormondt H.
    Cell 27:121-131(1981) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The nucleotide sequence of adenovirus type 5 early region E1: the region between map positions 8.0 (HindIII site) and 11.8 (SmaI site)."
    Maat J., van Beveren C.P., van Ormondt H.
    Gene 10:27-38(1980) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "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].
  4. "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].
  5. "Atomic structure of human adenovirus by cryo-EM reveals interactions among protein networks."
    Liu H., Jin L., Koh S.B., Atanasov I., Schein S., Wu L., Zhou Z.H.
    Science 329:1038-1043(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY ELECTRON MICROSCOPY (3.6 ANGSTROMS) OF THE VIRAL PARTICLE, FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH HEXON PROTEIN.
  6. "Latest insights on adenovirus structure and assembly."
    San Martin C.
    Viruses 4:847-877(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.

Entry informationi

Entry nameiCAP9_ADE05
AccessioniPrimary (citable) accession number: P03281
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: October 29, 2014
This is version 55 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.

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

External Data

Dasty 3