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P04413

- US03_HHV11

UniProt

P04413 - US03_HHV11

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Protein
Serine/threonine-protein kinase US3
Gene
US3
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

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.8 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei220 – 2201ATP By similarity
Active sitei305 – 3051Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi197 – 2059ATP By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. protein serine/threonine kinase activity Source: UniProtKB-KW
Complete GO annotation...

GO - Biological processi

  1. modulation by virus of host apoptotic process Source: UniProtKB-KW
  2. modulation by virus of host chromatin organization Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Host-virus interaction, Modulation of host cell apoptosis by virus, Modulation of host chromatin by virus

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein kinase US3 (EC:2.7.11.1)
Gene namesi
Name:US3
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 cytoplasm By similarity. Host nucleus By similarity

GO - Cellular componenti

  1. host cell cytoplasm Source: UniProtKB-SubCell
  2. host cell nucleus Source: UniProtKB-SubCell
  3. viral tegument Source: CACAO
Complete GO annotation...

Keywords - Cellular componenti

Host cytoplasm, Host nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi147 – 1471S → A: Complete loss of autophosphorylation. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 481481Serine/threonine-protein kinase US3
PRO_0000086180Add
BLAST

Post-translational modificationi

Phosphorylated by UL13; this phosphorylation regulates subsequent phosphorylation of UL31 and UL34 by US3. Autophosphorylated.2 Publications

Keywords - PTMi

Phosphoprotein

Interactioni

Protein-protein interaction databases

IntActiP04413. 29 interactions.

Structurei

3D structure databases

ProteinModelPortaliP04413.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini191 – 478288Protein kinase
Add
BLAST

Sequence similaritiesi

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P04413-1 [UniParc]FASTAAdd to Basket

« Hide

MACRKFCRVY GGQGRRKEEA VPPETKPSRV FPHGPFYTPA EDACLDSPPP    50
ETPKPSHTTP PSEAERLCHL QEILAQMYGN QDYPIEDDPS ADAADDVDED 100
APDDVAYPEE YAEELFLPGD ATGPLIGAND HIPPPCGASP PGIRRRSRDE 150
IGATGFTAEE LDAMDREAAR AISRGGKPPS TMAKLVTGMG FTIHGALTPG 200
SEGCVFDSSH PDYPQRVIVK AGWYTSTSHE ARLLRRLDHP AILPLLDLHV 250
VSGVTCLVLP KYQADLYTYL SRRLNPLGRP QIAAVSRQLL SAVDYIHRQG 300
IIHRDIKTEN IFINTPEDIC LGDFGAACFV QGSRSSPFPY GIAGTIDTNA 350
PEVLAGDPYT TTVDIWSAGL VIFETAVHNA SLFSAPRGPK RGPCDSQITR 400
IIRQAQVHVD EFSPHPESRL TSRYRSRAAG NNRPPYTRPA WTRYYKMDID 450
VEYLVCKALT FDGALRPSAA ELLCLPLFQQ K 481
Length:481
Mass (Da):52,835
Last modified:August 13, 1987 - v1
Checksum:i71838AB0483BE055
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L00036 Genomic DNA. Translation: AAA96685.1.
X14112 Genomic DNA. Translation: CAA32280.1.
X02138 Genomic DNA. Translation: CAA26057.1.
PIRiA00656. TVBE17.
RefSeqiNP_044665.1. NC_001806.1.

Genome annotation databases

GeneIDi2703401.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L00036 Genomic DNA. Translation: AAA96685.1 .
X14112 Genomic DNA. Translation: CAA32280.1 .
X02138 Genomic DNA. Translation: CAA26057.1 .
PIRi A00656. TVBE17.
RefSeqi NP_044665.1. NC_001806.1.

3D structure databases

ProteinModelPortali P04413.
ModBasei Search...

Protein-protein interaction databases

IntActi P04413. 29 interactions.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 2703401.

Family and domain databases

InterProi IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view ]
Pfami PF00069. Pkinase. 1 hit.
[Graphical view ]
SUPFAMi SSF56112. SSF56112. 1 hit.
PROSITEi PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiUS03_HHV11
AccessioniPrimary (citable) accession number: P04413
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: August 13, 1987
Last modified: May 14, 2014
This is version 83 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

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