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P04413 (US03_HHV11) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 82. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Serine/threonine-protein kinase US3

EC=2.7.11.1
Gene names
Name:US3
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 length481 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Multifunctional serine/threonine kinase that plays a role in several processes including egress of virus particles from the nucleus, modulation of the actin cytoskeleton and inhibition of apoptosis. Phosphorylates UL31 and UL34, two critical regulators of capsid budding from nucleus to endoplasmic reticulum, thereby facilitating virion egress. Modulates and redistributes host components of the nuclear envelope, including LMNA, emerin/EMD and the nuclear matrix protein MATR3. Phosphorylates envelope glycoprotein B (gB), probably to direct it to the cell surface. Promotes virus intracellular spread by restructuring host cell cytoskeleton. Blocks host apoptosis to extend cell survival and allow efficient viral replication. Promotes viral gene expression by phosphorylating host HDAC2 to reduce viral genome silencing. Ref.3 Ref.4 Ref.5 Ref.7 Ref.9 Ref.11 Ref.12 Ref.13

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Subcellular location

Host cytoplasm By similarity. Host nucleus By similarity.

Post-translational modification

Phosphorylated by UL13; this phosphorylation regulates subsequent phosphorylation of UL31 and UL34 by US3. Autophosphorylated. Ref.6 Ref.8

Sequence similarities

Belongs to the protein kinase superfamily. Ser/Thr protein kinase family.

Contains 1 protein kinase domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 481481Serine/threonine-protein kinase US3
PRO_0000086180

Regions

Domain191 – 478288Protein kinase
Nucleotide binding197 – 2059ATP By similarity

Sites

Active site3051Proton acceptor By similarity
Binding site2201ATP By similarity

Experimental info

Mutagenesis1471S → A: Complete loss of autophosphorylation. Ref.10

Sequences

Sequence LengthMass (Da)Tools
P04413 [UniParc].

Last modified August 13, 1987. Version 1.
Checksum: 71838AB0483BE055

FASTA48152,835
        10         20         30         40         50         60 
MACRKFCRVY GGQGRRKEEA VPPETKPSRV FPHGPFYTPA EDACLDSPPP ETPKPSHTTP 

        70         80         90        100        110        120 
PSEAERLCHL QEILAQMYGN QDYPIEDDPS ADAADDVDED APDDVAYPEE YAEELFLPGD 

       130        140        150        160        170        180 
ATGPLIGAND HIPPPCGASP PGIRRRSRDE IGATGFTAEE LDAMDREAAR AISRGGKPPS 

       190        200        210        220        230        240 
TMAKLVTGMG FTIHGALTPG SEGCVFDSSH PDYPQRVIVK AGWYTSTSHE ARLLRRLDHP 

       250        260        270        280        290        300 
AILPLLDLHV VSGVTCLVLP KYQADLYTYL SRRLNPLGRP QIAAVSRQLL SAVDYIHRQG 

       310        320        330        340        350        360 
IIHRDIKTEN IFINTPEDIC LGDFGAACFV QGSRSSPFPY GIAGTIDTNA PEVLAGDPYT 

       370        380        390        400        410        420 
TTVDIWSAGL VIFETAVHNA SLFSAPRGPK RGPCDSQITR IIRQAQVHVD EFSPHPESRL 

       430        440        450        460        470        480 
TSRYRSRAAG NNRPPYTRPA WTRYYKMDID VEYLVCKALT FDGALRPSAA ELLCLPLFQQ 


K 

« Hide

References

[1]"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].
[2]"The herpesvirus protein kinase: a new departure in protein phosphorylation?"
Leader D.P., Purves F.C.
Trends Biochem. Sci. 13:244-246(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[3]"The herpes simplex virus 1 protein kinase encoded by the US3 gene mediates posttranslational modification of the phosphoprotein encoded by the UL34 gene."
Purves F.C., Spector D., Roizman B.
J. Virol. 65:5757-5764(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PHOSPHORYLATION OF UL34.
Strain: F.
[4]"The herpes simplex virus 1 protein kinase US3 is required for protection from apoptosis induced by the virus."
Leopardi R., Van Sant C., Roizman B.
Proc. Natl. Acad. Sci. U.S.A. 94:7891-7896(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
Strain: F.
[5]"Identification of proteins phosphorylated directly by the Us3 protein kinase encoded by herpes simplex virus 1."
Kato A., Yamamoto M., Ohno T., Kodaira H., Nishiyama Y., Kawaguchi Y.
J. Virol. 79:9325-9331(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PHOSPHORYLATION OF UL31; ICP22 AND US9.
Strain: F.
[6]"Herpes simplex virus 1-encoded protein kinase UL13 phosphorylates viral Us3 protein kinase and regulates nuclear localization of viral envelopment factors UL34 and UL31."
Kato A., Yamamoto M., Ohno T., Tanaka M., Sata T., Nishiyama Y., Kawaguchi Y.
J. Virol. 80:1476-1486(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION BY UL13.
Strain: F.
[7]"Emerin is hyperphosphorylated and redistributed in herpes simplex virus type 1-infected cells in a manner dependent on both UL34 and US3."
Leach N., Bjerke S.L., Christensen D.K., Bouchard J.M., Mou F., Park R., Baines J., Haraguchi T., Roller R.J.
J. Virol. 81:10792-10803(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[8]"Identification of a physiological phosphorylation site of the herpes simplex virus 1-encoded protein kinase Us3 which regulates its optimal catalytic activity in vitro and influences its function in infected cells."
Kato A., Tanaka M., Yamamoto M., Asai R., Sata T., Nishiyama Y., Kawaguchi Y.
J. Virol. 82:6172-6189(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: AUTOPHOSPHORYLATION.
Strain: F.
[9]"Phosphorylation of the UL31 protein of herpes simplex virus 1 by the US3-encoded kinase regulates localization of the nuclear envelopment complex and egress of nucleocapsids."
Mou F., Wills E., Baines J.D.
J. Virol. 83:5181-5191(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
Strain: F.
[10]"Regulation of the catalytic activity of herpes simplex virus 1 protein kinase Us3 by autophosphorylation and its role in pathogenesis."
Sagou K., Imai T., Sagara H., Uema M., Kawaguchi Y.
J. Virol. 83:5773-5783(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF SER-147.
[11]"Effects of phosphorylation of herpes simplex virus 1 envelope glycoprotein B by Us3 kinase in vivo and in vitro."
Imai T., Sagou K., Arii J., Kawaguchi Y.
J. Virol. 84:153-162(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PHOSPHORYLATION OF GLYCOPROTEIN B.
[12]"Hyperphosphorylation of histone deacetylase 2 by alphaherpesvirus US3 kinases."
Walters M.S., Kinchington P.R., Banfield B.W., Silverstein S.
J. Virol. 84:9666-9676(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PHOSPHORYLATION OF HOST HDAC2.
[13]"The alphaherpesvirus US3/ORF66 protein kinases direct phosphorylation of the nuclear matrix protein matrin 3."
Erazo A., Yee M.B., Banfield B.W., Kinchington P.R.
J. Virol. 85:568-581(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PHOSPHORYLATION OF HOST MATR3.
Strain: RC.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L00036 Genomic DNA. Translation: AAA96685.1.
X14112 Genomic DNA. Translation: CAA32280.1.
X02138 Genomic DNA. Translation: CAA26057.1.
PIRTVBE17. A00656.
RefSeqNP_044665.1. NC_001806.1.

3D structure databases

ProteinModelPortalP04413.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP04413. 29 interactions.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2703401.

Phylogenomic databases

ProtClustDBPHA3211.

Family and domain databases

InterProIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameUS03_HHV11
AccessionPrimary (citable) accession number: P04413
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: August 13, 1987
Last modified: February 19, 2014
This is version 82 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