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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: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Plays a role in the inhibition of host immune response. Participates in the inhibiton of host autophagy by interacting with and inhibiting host PKR/EIF2AK2. This interaction also prevents the interferon-induced shut down of protein synthesis following viral infection. Downmodulates the host RLR signaling pathway via direct interaction with host DDX58 and IFIH1. May also participate in nuclear egress of viral particles through interactions with host NCL and regulation of the viral UL34 mRNA.4 Publications

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Host-virus interaction, Inhibition of host autophagy by virus, Inhibition of host innate immune response by virus, Inhibition of host interferon signaling pathway by virus, Inhibition of host MDA5 by virus, Inhibition of host PKR by virus, Inhibition of host RIG-I by virus, Inhibition of host RLR pathway 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 Componenti: Genome

Subcellular locationi

  • Host nucleushost nucleolus 1 Publication
  • Host cytoplasm 1 Publication

  • Note: Following infection, it is released into the cell cytoplasm.

GO - Cellular componenti

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. Interacts with host DDX58; this interaction prevents DDX58 binding to host MAVS. Interacts with host IFIH1; this interaction prevents host IFH1 binding to MAVS.4 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.
KEGGivg:2703439.

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.
PIRiA03728. DNBE17.
RefSeqiNP_044674.1. NC_001806.1.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi2703439.
KEGGivg:2703439.

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]
ProtoNetiSearch...

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. "Molecular anatomy of subcellular localization of HSV-1 tegument protein US11 in living cells."
    Xing J., Wu F., Pan W., Zheng C.
    Virus Res. 153:71-81(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  10. "Herpes simplex virus 1 tegument protein US11 downmodulates the RLR signaling pathway via direct interaction with RIG-I and MDA-5."
    Xing J., Wang S., Lin R., Mossman K.L., Zheng C.
    J. Virol. 86:3528-3540(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH HOST DDX58 AND IFIH1.
  11. "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.
  12. "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, INTERACTION WITH HOST EIF2AK2.
  13. "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: April 29, 2015
This is version 79 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

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 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.