Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P04487 (RNB_HHV11) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 73. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
RNA-binding protein
Alternative name(s):
Vmw21
Gene names
Name:US11
OrganismHuman herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1) [Reference proteome]
Taxonomic identifier10299 [NCBI]
Taxonomic lineageVirusesdsDNA viruses, no RNA stageHerpesviralesHerpesviridaeAlphaherpesvirinaeSimplexvirus
Virus hostHomo sapiens (Human) [TaxID: 9606]

Protein attributes

Sequence length161 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.9 Ref.10 Ref.11

Subunit structure

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. Ref.8 Ref.9

Subcellular location

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

Domain

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.

Post-translational modification

May be phosphorylated on Ser residues by host kinases. Ref.5

Sequence similarities

Belongs to the simplex virus US11 protein family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

DDX58O957864EBI-6150681,EBI-995350From a different organism.
EIF2AK2P195253EBI-6150681,EBI-640775From a different organism.
IFIH1Q9BYX44EBI-6150681,EBI-6115771From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 161161RNA-binding protein
PRO_0000115740

Regions

Repeat85 – 9061
Repeat91 – 9662
Repeat97 – 10263
Repeat103 – 10864
Repeat109 – 11465
Repeat115 – 12066
Repeat121 – 12667
Repeat127 – 13268
Repeat133 – 13869
Repeat139 – 144610
Repeat145 – 150611
Repeat151 – 156612
Region85 – 1567212 X 6 AA approximate tandem repeats

Sequences

Sequence LengthMass (Da)Tools
P04487 [UniParc].

Last modified August 13, 1987. Version 1.
Checksum: 1CECA86CF1B9F2FF

FASTA16117,757
        10         20         30         40         50         60 
MSQTQPPAPV GPGDPDVYLK GVPSAGMHPR GVHAPRGHPR MISGPPQRGD NDQAAGQCGD 

        70         80         90        100        110        120 
SGLLRVGADT TISKPSEAVR PPTIPRTPRV PREPRVPRPP REPREPRVPR APRDPRVPRD 

       130        140        150        160 
PRDPRQPRSP REPRSPREPR SPREPRTPRT PREPRTARGS V 

« Hide

References

[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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L00036 Genomic DNA. Translation: AAA96677.1.
X14112 Genomic DNA. Translation: CAA32276.1.
X02138 Genomic DNA. Translation: CAA26065.1.
X00428 Genomic RNA. Translation: CAA25125.1.
PIRDNBE17. A03728.
RefSeqNP_044674.1. NC_001806.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid971460. 1 interaction.
IntActP04487. 145 interactions.
MINTMINT-6732702.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2703439.

Family and domain databases

InterProIPR020124. Herpes_US11_RNA-bd_N.
[Graphical view]
ProDomPD028529. Herpes_US11_RNA-bd_N. 1 hit.
[Graphical view] [Entries sharing at least one domain]
ProtoNetSearch...

Entry information

Entry nameRNB_HHV11
AccessionPrimary (citable) accession number: P04487
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: August 13, 1987
Last modified: June 11, 2014
This is version 73 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families