Serine/threonine-protein kinase US3 - Human herpesvirus 1 (strain 17) (HHV-1)

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P04413 (US03_HHV11) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 78. History...

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

Documents (1) |

Third-party data

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

Names and origin

Protein names

Recommended name:
Serine/threonine-protein kinase US3
EC=2.7.11.1

Gene names

Name:

US3

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	481 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Host-virus interaction Modulation of host cell apoptosis by virus Modulation of host chromatin by virus
Cellular component	Host cytoplasm Host nucleus
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	modulation by virus of host apoptotic process Inferred from electronic annotation. Source: UniProtKB-KW modulation by virus of host chromatin organization Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	host cell cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell host cell nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW protein serine/threonine kinase activity 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 – 481

481

Serine/threonine-protein kinase US3

PRO_0000086180

Regions

Domain

191 – 478

288

Protein kinase

Nucleotide binding

197 – 205

ATP By similarity

Sites

Active site

305

Proton acceptor By similarity

Binding site

220

ATP By similarity

Experimental info

Mutagenesis

147

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

Sequences

Sequence

Length

Mass (Da)

Tools

P04413 [UniParc].

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

481

52,835

        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

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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.
PIR	TVBE17. A00656.
RefSeq	NP_044665.1. NC_001806.1.
3D structure databases
ProteinModelPortal	P04413.
ModBase	Search...
Protein-protein interaction databases
IntAct	P04413. 29 interactions.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	2703401.
Phylogenomic databases
ProtClustDB	PHA3211.
Family and domain databases
InterPro	IPR011009. Kinase-like_dom. IPR000719. Prot_kinase_cat_dom. IPR008271. Ser/Thr_kinase_AS. [Graphical view]
Pfam	PF00069. Pkinase. 1 hit. [Graphical view]
SUPFAM	SSF56112. Kinase_like. 1 hit.
PROSITE	PS00107. PROTEIN_KINASE_ATP. False negative. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

US03_HHV11

Accession

Primary (citable) accession number: P04413

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 13, 1987
Last sequence update:	August 13, 1987
Last modified:	April 3, 2013
This is version 78 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Viral Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

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

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Experimental info

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

Relevant documents