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P04487

- RNB_HHV11

UniProt

P04487 - RNB_HHV11

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Protein

RNA-binding protein

Gene

US11

Organism
Human herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

Plays a role in the inhibition of immune response by interacting with and inhibiting host PKR/EIF2AK2 thereby preventing the interferon-induced shut down of protein synthesis following viral infection. May also participate in nuclear egress of viral particles through interactions with host NCL and regulation of the viral UL34 mRNA.3 Publications

GO - Molecular functioni

  1. DNA binding Source: UniProtKB-KW
  2. RNA binding Source: UniProtKB-KW

GO - Biological processi

  1. modulation by virus of host morphology or physiology Source: UniProtKB
  2. suppression by virus of host cell cycle arrest Source: UniProtKB
  3. suppression by virus of host PKR activity Source: UniProtKB-KW
  4. suppression by virus of host type I interferon-mediated signaling pathway Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Host-virus interaction, Inhibition of host innate immune response by virus, Inhibition of host interferon signaling pathway by virus, Inhibition of host PKR by virus, Viral immunoevasion

Keywords - Ligandi

DNA-binding, RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
RNA-binding protein
Alternative name(s):
Vmw21
Gene namesi
Name:US11
OrganismiHuman herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1)
Taxonomic identifieri10299 [NCBI]
Taxonomic lineageiVirusesdsDNA viruses, no RNA stageHerpesviralesHerpesviridaeAlphaherpesvirinaeSimplexvirus
Virus hostiHomo sapiens (Human) [TaxID: 9606]
ProteomesiUP000009294: Genome

Subcellular locationi

Host nucleushost nucleolus. Host cytoplasm
Note: Following infection, it is released into the cell cytoplasm.

GO - Cellular componenti

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

Keywords - Cellular componenti

Host cytoplasm, Host nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 161161RNA-binding proteinPRO_0000115740Add
BLAST

Post-translational modificationi

May be phosphorylated on Ser residues by host kinases.1 Publication

Keywords - PTMi

Phosphoprotein

Expressioni

Keywords - Developmental stagei

Late protein

Interactioni

Subunit structurei

Associates with RNA derived from the 60S ribosomal subunits. Seems to form large heterogeneous polymers of up to 200 identical subunits in the cytoplasm. Interacts with host EIF2AK2. Interacts with host NCL.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
DDX58O957864EBI-6150681,EBI-995350From a different organism.
EIF2AK2P195253EBI-6150681,EBI-640775From a different organism.
IFIH1Q9BYX44EBI-6150681,EBI-6115771From a different organism.

Protein-protein interaction databases

BioGridi971460. 1 interaction.
IntActiP04487. 145 interactions.
MINTiMINT-6732702.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati85 – 9061
Repeati91 – 9662
Repeati97 – 10263
Repeati103 – 10864
Repeati109 – 11465
Repeati115 – 12066
Repeati121 – 12667
Repeati127 – 13268
Repeati133 – 13869
Repeati139 – 144610
Repeati145 – 150611
Repeati151 – 156612

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni85 – 1567212 X 6 AA approximate tandem repeatsAdd
BLAST

Domaini

The N-terminal tetrapeptide may be responsible for virion incorporation.
The C-terminal half, rich in Arg and Pro residues, seems to be responsible for the RNA-binding activity, and for the association with ribosomes and the localization to the nucleolus. This region may adopt a poly-L-proline II helix secondary structure.

Sequence similaritiesi

Belongs to the simplex virus US11 protein family.Curated

Keywords - Domaini

Repeat

Family and domain databases

InterProiIPR020124. Herpes_US11_RNA-bd_N.
[Graphical view]
ProDomiPD028529. Herpes_US11_RNA-bd_N. 1 hit.
[Graphical view] [Entries sharing at least one domain]

Sequencei

Sequence statusi: Complete.

P04487-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSQTQPPAPV GPGDPDVYLK GVPSAGMHPR GVHAPRGHPR MISGPPQRGD
60 70 80 90 100
NDQAAGQCGD SGLLRVGADT TISKPSEAVR PPTIPRTPRV PREPRVPRPP
110 120 130 140 150
REPREPRVPR APRDPRVPRD PRDPRQPRSP REPRSPREPR SPREPRTPRT
160
PREPRTARGS V
Length:161
Mass (Da):17,757
Last modified:August 13, 1987 - v1
Checksum:i1CECA86CF1B9F2FF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L00036 Genomic DNA. Translation: AAA96677.1.
X14112 Genomic DNA. Translation: CAA32276.1.
X02138 Genomic DNA. Translation: CAA26065.1.
X00428 Genomic RNA. Translation: CAA25125.1.
PIRiA03728. DNBE17.
RefSeqiNP_044674.1. NC_001806.1.

Genome annotation databases

GeneIDi2703439.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L00036 Genomic DNA. Translation: AAA96677.1 .
X14112 Genomic DNA. Translation: CAA32276.1 .
X02138 Genomic DNA. Translation: CAA26065.1 .
X00428 Genomic RNA. Translation: CAA25125.1 .
PIRi A03728. DNBE17.
RefSeqi NP_044674.1. NC_001806.1.

3D structure databases

ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 971460. 1 interaction.
IntActi P04487. 145 interactions.
MINTi MINT-6732702.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 2703439.

Family and domain databases

InterProi IPR020124. Herpes_US11_RNA-bd_N.
[Graphical view ]
ProDomi PD028529. Herpes_US11_RNA-bd_N. 1 hit.
[Graphical view ] [Entries sharing at least one domain ]
ProtoNeti Search...

Publicationsi

  1. "A 3' co-terminal family of mRNAs from the herpes simplex virus type 1 short region: two overlapping reading frames encode unrelated polypeptide one of which has highly reiterated amino acid sequence."
    Rixon F.J., McGeoch D.J.
    Nucleic Acids Res. 12:2473-2487(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Sequence determination and genetic content of the short unique region in the genome of herpes simplex virus type 1."
    McGeoch D.J., Dolan A., Donald S., Rixon F.J.
    J. Mol. Biol. 181:1-13(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "The products of gene US11 of herpes simplex virus type 1 are DNA-binding and localize to the nucleoli of infected cells."
    McLean C.A., Rixon F.J., Marsden H.S.
    J. Gen. Virol. 68:1921-1937(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  4. Erratum
    McLean C.A., Rixon F.J., Marsden H.S.
    J. Gen. Virol. 69:763-763(1988)
  5. "Phosphorylation of herpes simplex virus type 1 Us11 protein is independent of viral genome expression."
    Simonin D., Diaz J.-J., Kindbeiter K., Pernas P., Madjar J.-J.
    Electrophoresis 16:1317-1322(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION.
  6. "Structure and function in the herpes simplex virus 1 RNA-binding protein U(s)11: mapping of the domain required for ribosomal and nucleolar association and RNA binding in vitro."
    Roller R.J., Monk L.L., Stuart D., Roizman B.
    J. Virol. 70:2842-2851(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  7. "Distinct domains in herpes simplex virus type 1 US11 protein mediate post-transcriptional transactivation of human T-lymphotropic virus type I envelope glycoprotein gene expression and specific binding to the Rex responsive element."
    Schaerer-Uthurralt N., Erard M., Kindbeiter K., Madjar J.-J., Diaz J.-J.
    J. Gen. Virol. 79:1593-1602(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  8. "The herpes simplex virus type 1 U(S)11 protein interacts with protein kinase R in infected cells and requires a 30-amino-acid sequence adjacent to a kinase substrate domain."
    Cassady K.A., Gross M.
    J. Virol. 76:2029-2035(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HOST EIF2AK2.
  9. "Nucleolin interacts with US11 protein of herpes simplex virus 1 and is involved in its trafficking."
    Greco A., Arata L., Soler E., Gaume X., Coute Y., Hacot S., Calle A., Monier K., Epstein A.L., Sanchez J.C., Bouvet P., Diaz J.J.
    J. Virol. 86:1449-1457(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH HOST NCL.
  10. "The herpes simplex virus 1 Us11 protein inhibits autophagy through its interaction with the protein kinase PKR."
    Lussignol M., Queval C., Bernet-Camard M.F., Cotte-Laffitte J., Beau I., Codogno P., Esclatine A.
    J. Virol. 87:859-871(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  11. "Herpes simplex virus type 1 virion-derived US11 inhibits type 1 interferon-induced protein kinase R phosphorylation."
    Ishioka K., Ikuta K., Sato Y., Kaneko H., Sorimachi K., Fukushima E., Saijo M., Suzutani T.
    Microbiol. Immunol. 57:426-436(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.

Entry informationi

Entry nameiRNB_HHV11
AccessioniPrimary (citable) accession number: P04487
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: August 13, 1987
Last modified: October 29, 2014
This is version 75 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

External Data

Dasty 3