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Gene Review

UL13  -  tegument serine/threonine protein kinase

Human herpesvirus 1

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Disease relevance of UL13


High impact information on UL13

  • These results indicate that UL13 phosphorylates Us3 in infected cells and regulates UL34 and UL31 localization, either by phosphorylating Us3 or by a Us3-independent mechanism [6].
  • UL13 and Us3 are protein kinases encoded by herpes simplex virus 1 [6].
  • (i) The electrophoretic mobility, in denaturing gels, of Us3 isoforms from Vero cells infected with wild-type virus was slower than that of isoforms from cells infected with a UL13 deletion mutant virus (DeltaUL13) [6].
  • These experiments revealed that this interaction has biological activity; at early times of infection, US11 down-regulates UL13 protein kinase mRNA and protein [3].
  • US1.5 protein must be posttranslationally modified by the UL13 protein kinase to enable expression of a subset of late genes exemplified by UL38 and US11 [7].

Chemical compound and disease context of UL13


Biological context of UL13

  • In the present study, we investigated the role(s) of the protein kinase activity of UL13 in viral replication using a recombinant virus expressing enzymatically inactive UL13 after an amino acid substitution in the invariant lysine of UL13 [2].
  • We conclude that UL13 physically associates with gE and mediates the phosphorylation of gE and gI [8].
  • The two mutants were shown to be deficient in UL13 gene expression by Western blotting of infected cells [9].
  • A revertant virus, in which UL13 expression was restored to a near-normal level, was generated by recombination of one of the UL13-negative mutants with a plasmid carrying the wild-type UL13 gene [9].
  • The two novel mutations localized in EcoRI-d fragment were further finely mapped, and it was demonstrated that the mutations belonging to groups E and H were involved in the open reading frames UL10 and UL13, respectively [10].

Enzymatic interactions of UL13

  • However, the UL41 gene product could still be phosphorylated in lysates of UL13-negative virions [9].

Other interactions of UL13

  • Herpes simplex virus 1 encodes a Fc receptor consisting of glycoproteins E (gE) and I (gI) and two protein kinases specified by UL13 and US3, respectively [8].

Analytical, diagnostic and therapeutic context of UL13

  • These results indicate that the protein kinase activity of UL13 plays a role in viral replication in cell culture, but the activity is not essential for the optimal expression of UL41 and ICP0 [2].


  1. Phosphorylation of structural components promotes dissociation of the herpes simplex virus type 1 tegument. Morrison, E.E., Wang, Y.F., Meredith, D.M. J. Virol. (1998) [Pubmed]
  2. The role of protein kinase activity expressed by the UL13 gene of herpes simplex virus 1: the activity is not essential for optimal expression of UL41 and ICP0. Tanaka, M., Nishiyama, Y., Sata, T., Kawaguchi, Y. Virology (2005) [Pubmed]
  3. The herpes simplex virus type 1 US11 protein binds the coterminal UL12, UL13, and UL14 RNAs and regulates UL13 expression in vivo. Attrill, H.L., Cumming, S.A., Clements, J.B., Graham, S.V. J. Virol. (2002) [Pubmed]
  4. The ORF47 and ORF66 putative protein kinases of varicella-zoster virus determine tropism for human T cells and skin in the SCID-hu mouse. Moffat, J.F., Zerboni, L., Sommer, M.H., Heineman, T.C., Cohen, J.I., Kaneshima, H., Arvin, A.M. Proc. Natl. Acad. Sci. U.S.A. (1998) [Pubmed]
  5. Protein kinases conserved in herpesviruses potentially share a function mimicking the cellular protein kinase cdc2. Kawaguchi, Y., Kato, K. Rev. Med. Virol. (2003) [Pubmed]
  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. (2006) [Pubmed]
  7. Functional anatomy of herpes simplex virus 1 overlapping genes encoding infected-cell protein 22 and US1.5 protein. Ogle, W.O., Roizman, B. J. Virol. (1999) [Pubmed]
  8. UL13 protein kinase of herpes simplex virus 1 complexes with glycoprotein E and mediates the phosphorylation of the viral Fc receptor: glycoproteins E and I. Ng, T.I., Ogle, W.O., Roizman, B. Virology (1998) [Pubmed]
  9. Production of host shutoff-defective mutants of herpes simplex virus type 1 by inactivation of the UL13 gene. Overton, H., McMillan, D., Hope, L., Wong-Kai-In, P. Virology (1994) [Pubmed]
  10. Two novel genes of herpes simplex virus type 1 involved in cell fusion. Yamamoto, S., Hamada, N., Shingu, M. The Kurume medical journal. (1993) [Pubmed]
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