RNA-binding protein - Human herpesvirus 1 (strain 17) (HHV-1)

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P04487 (RNB_HHV11) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 66. History...

Clusters with 100%, 90%, 50% identity |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info Customize order

Names and origin

Protein names

Recommended name:
RNA-binding protein

Alternative name(s):
Vmw21

Gene names

Name:

US11

Organism

Human herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1) [Reference proteome]

Taxonomic identifier

10299 [NCBI]

Taxonomic lineage

Viruses › dsDNA viruses, no RNA stage › Herpesvirales › Herpesviridae › Alphaherpesvirinae › Simplexvirus ›

Virus host

Homo sapiens (Human) [TaxID: 9606]

Protein attributes

Sequence length	161 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Binds DNA and RNA. Is one of the most abundant viral proteins present in cells late in infection. Not necessary for virus viability. Component of the HSV-1 virion, with approximately 600 to 1000 copies per virion. Binds specifically to UL34 mRNA (in vitro) and seems to regulate the expression of that gene.
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.
Subcellular location	Host nucleus › host nucleolus. Host cytoplasm. Note: Following infection, it is released into the cell cytoplasm.
Domain	The first 40 amino acids of the N-terminal region is an effector domain necessary for the transactivation of HTLV-1 env gene expression, which may interact with cellular proteins. 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

Ontologies

Keywords
Biological process	Host-virus interaction Inhibition of host PKR by virus Inhibition of host innate immune response by virus Inhibition of host interferon signaling pathway by virus Viral immunoevasion
Cellular component	Host cytoplasm Host nucleus
Developmental stage	Late protein
Domain	Repeat
Ligand	DNA-binding RNA-binding
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	suppression by virus of host PKR activity Inferred from electronic annotation. Source: UniProtKB-KW suppression by virus of host cell cycle arrest Non-traceable author statement PubMed 14990717. Source: UniProtKB suppression by virus of host type I interferon-mediated signaling pathway Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	host cell cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell host cell nucleolus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	DNA binding Inferred from electronic annotation. Source: UniProtKB-KW RNA binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 161

161

RNA-binding protein

PRO_0000115740

Regions

Repeat

Repeat

Repeat

Repeat

Repeat

Repeat

Repeat

Repeat

Repeat

Repeat

Repeat

Repeat

Region

12 X 6 AA approximate tandem repeats

Sequences

Sequence

Length

Mass (Da)

Tools

P04487 [UniParc].

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

161

17,757

        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.
+	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.
PIR	DNBE17. A03728.
RefSeq	NP_044674.1. NC_001806.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
IntAct	P04487. 141 interactions.
MINT	MINT-6732702.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	2703439.
Phylogenomic databases
ProtClustDB	CLSP2510185.
Family and domain databases
InterPro	IPR020124. Herpes_US11_RNA-bd_N. [Graphical view]
ProDom	PD028529. Herpes_US11_RNA-bd_N. 1 hit. [Graphical view] [Entries sharing at least one domain]
ProtoNet	Search...

Entry information

Entry name

RNB_HHV11

Accession

Primary (citable) accession number: P04487

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 13, 1987
Last sequence update:	August 13, 1987
Last modified:	April 3, 2013
This is version 66 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Viral Protein Annotation Program

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Family and domain databases

Entry information