P28926 · US03_EHV1B

Function

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 protein 26 and 29, 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 (By similarity).

Catalytic activity

Features

Showing features for binding site, active site.

TypeIDPosition(s)Description
Binding site99-107ATP (UniProtKB | ChEBI)
Binding site122ATP (UniProtKB | ChEBI)
Active site207Proton acceptor

GO annotations

AspectTerm
Cellular Componenthost cell cytoplasm
Cellular Componenthost cell nucleus
Molecular FunctionATP binding
Molecular Functionprotein serine kinase activity
Molecular Functionprotein serine/threonine kinase activity
Biological Processmodulation by virus of host chromatin organization
Biological Processsymbiont-mediated perturbation of host apoptosis

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Serine/threonine-protein kinase US3 homolog
  • EC number

Gene names

    • Ordered locus names
      69

Organism names

Accessions

  • Primary accession
    P28926
  • Secondary accessions
    • Q6S6W2

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00000861771-382Serine/threonine-protein kinase US3 homolog

Post-translational modification

Phosphorylated by protein 49; this phosphorylation regulates subsequent phosphorylation of proteins 26 and 29 by US3 homolog. Autophosphorylated (By similarity).

Structure

3D structure databases

Family & Domains

Features

Showing features for region, compositional bias, domain.

TypeIDPosition(s)Description
Region1-75Disordered
Compositional bias8-24Polar residues
Compositional bias50-75Acidic residues
Domain93-379Protein kinase

Sequence similarities

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

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    382
  • Mass (Da)
    42,543
  • Last updated
    1992-12-01 v1
  • Checksum
    DFB3F4F1A75731C9
MENKQCDHLTDWFSTTSDASESMDTTPPLPPPTPSVDPSYSGAAADEDLYSDISEGDLEYSDCDSASESDEDDDDCLIPSKEKAREVAASFGYTVIKTLTPGSEGRVMVATKDGQPEPVVLKIGQKGTTLIEAMMLRNVNHPSVIQMKDTLVSGAITCMVLPHYSSDLYTFLTKESRRIPIDQALIIEKQILEGLRYLHAQRIIHRDVKTENIFINSVDQVCIADFGAAQFPVVEPADLGLAGTVETNAPEVLARAKYNSKADIWSAGIVLFEMLAYPSTLFEDPPSTPEEYVKSCHSQLLKIISTLKINPEEFPRDPGSRLVRGYIEYSRLERKPYTRYPCFQRVNLHIDGEFLVHKMLAFNAAMRPSAEELLSYPMFAQL

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias8-24Polar residues
Compositional bias50-75Acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AY665713
EMBL· GenBank· DDBJ
AAT67326.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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