E1BK52 · STK10_BOVIN

  • Protein
    Serine/threonine-protein kinase 10
  • Gene
    STK10
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    5/5

Function

function

Serine/threonine-protein kinase involved in regulation of lymphocyte migration. Phosphorylates MSN, and possibly PLK1. Involved in regulation of lymphocyte migration by mediating phosphorylation of ERM proteins such as MSN. Acts as a negative regulator of MAP3K1/MEKK1. May also act as a cell cycle regulator by acting as a polo kinase kinase: mediates phosphorylation of PLK1 in vitro; however such data require additional evidences in vivo (By similarity).

Catalytic activity

Activity regulation

Inhibited by the pyrrole-indolinone inhibitor SU11274 (K00593): intercalates between the ATP-binding Lys-65 and alpha-C glutamate (Glu-81), resulting in a partial disordering of the lysine side chain. Also specifically inhibited by erlotinib. Slightly inhibited by gefitinib (By similarity).

Features

Showing features for binding site, active site.

Type
IDPosition(s)Description
Binding site42-50ATP (UniProtKB | ChEBI)
Binding site65ATP (UniProtKB | ChEBI)
Active site157Proton acceptor

GO annotations

AspectTerm
Cellular Componentplasma membrane
Molecular Function3-phosphoinositide-dependent protein kinase activity
Molecular FunctionAMP-activated protein kinase activity
Molecular FunctionATP binding
Molecular FunctionDNA-dependent protein kinase activity
Molecular Functioneukaryotic translation initiation factor 2alpha kinase activity
Molecular Functionhistone H2AS1 kinase activity
Molecular Functionhistone H2AS121 kinase activity
Molecular Functionhistone H2AT120 kinase activity
Molecular Functionhistone H2AXS139 kinase activity
Molecular Functionhistone H2BS14 kinase activity
Molecular Functionhistone H2BS36 kinase activity
Molecular Functionhistone H3S10 kinase activity
Molecular Functionhistone H3S28 kinase activity
Molecular Functionhistone H3S57 kinase activity
Molecular Functionhistone H3T11 kinase activity
Molecular Functionhistone H3T3 kinase activity
Molecular Functionhistone H3T45 kinase activity
Molecular Functionhistone H3T6 kinase activity
Molecular Functionhistone H4S1 kinase activity
Molecular Functionprotein homodimerization activity
Molecular Functionprotein serine kinase activity
Molecular Functionprotein serine/threonine kinase activity
Molecular FunctionRho-dependent protein serine/threonine kinase activity
Molecular Functionribosomal protein S6 kinase activity
Biological Processprotein autophosphorylation
Biological Processregulation of lymphocyte migration

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Serine/threonine-protein kinase 10
  • EC number

Gene names

    • Name
      STK10

Organism names

  • Taxonomic identifier
  • Strain
    • Hereford
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Laurasiatheria > Artiodactyla > Ruminantia > Pecora > Bovidae > Bovinae > Bos

Accessions

  • Primary accession
    E1BK52

Proteomes

Subcellular Location

Cell membrane
; Peripheral membrane protein

Keywords

PTM/Processing

Features

Showing features for chain, modified residue.

Type
IDPosition(s)Description
ChainPRO_00004147101-966Serine/threonine-protein kinase 10
Modified residue13Phosphoserine
Modified residue20Phosphoserine
Modified residue185Phosphothreonine; by autocatalysis
Modified residue191Phosphoserine; by autocatalysis
Modified residue437Phosphoserine
Modified residue449Phosphoserine
Modified residue453Phosphoserine
Modified residue483Phosphoserine
Modified residue512Phosphoserine
Modified residue547Phosphoserine

Post-translational modification

Autophosphorylates following homodimerization, leading to activation of the protein.

Keywords

Proteomic databases

Interaction

Subunit

Homodimer; homodimerization is required for activation segment autophosphorylation.

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for domain, region, compositional bias, coiled coil.

Type
IDPosition(s)Description
Domain36-294Protein kinase
Region175-224Activation segment
Compositional bias318-331Acidic residues
Region318-411Disordered
Region424-512Disordered
Compositional bias452-467Polar residues
Compositional bias486-512Polar residues
Coiled coil571-945
Region666-688Disordered
Region825-863Disordered
Compositional bias833-863Basic and acidic residues
Region941-966Disordered

Sequence similarities

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    966
  • Mass (Da)
    111,615
  • Last updated
    2011-12-14 v3
  • MD5 Checksum
    104063F95BD5A2C999997A704E384C80
MAFANFRRILRLSTFEKRKSREYEHVRRDLDPNEVWEIVGELGDGAFGKVYKAKNKETGALAAAKVIETNSEEELEDYIVEIEILATCDHPYIVKLLGAYYYDGKLWIMIEFCPGGAVDAIMLELDRGLTEPQIQVVCRQMLEALTFLHGKKIIHRDLKAGNVLMTLEGDIRLADFGVSAKNLKTLQKRDSFIGTPYWMAPEVVMCETMKDTPYDYKADIWSLGITLIEMAQIEPPHHELNPMRVLLKIAKSDPPTLLSPSKWSAEFRDFLKTALDKNPETRPSAAQLLEHPFVSSVTSNKALRELVAEAKAEVMEEIEDGRDEGDEEDAVEAASPLENHTRDSSEVSQLSIDADKLLKESPFTPPPPSQPQDGANGPSEPPGHGALPATSPLDVAPGNENGQAVPVPLRKFRPVSMGARIQVSEEKQAADQGGDLSPAASRSQKASQSRPNSSALETLRSELTNGSLELPTPGAQSLSKRDSDCGSVSTSGSTDFGTSLSADMSVNKESGSLSIKDSRLHNKTLKRTRKFVVDGVEVSITTSKIISEDEKKDEEMRFLRRQELRELRLLQKEEHRNQTQLSSKHELQLEQMHKRFEQEINAKKKFFDIELENLERQQKQQVEKMEQDHAVRRREEAKRIRLEQERDYAKFQEQLKLMKKEVKNEVEKLPRQQRKESMKQKMEEHTQKKQLLDRDFLAKQKEDLELAMKRITADNRREICDKERECLTRKQELLRDREAALWEMEEHHLQERHQLVKQQLKDQYFLQRHELLRKHEKEREQMQRYNQRMIEQLKVRQQQEKARLPKIQRSEGKTRMAMYKKSLHINGGGSAAEQREKIKQFSQQEEKRQKAERLQQQQKHENQMRDMLAQCESNMSELQQLQNEKCHLLIEHETQKLKALDESHNQNLKEWRDKLRPRKKALEEDLNQKKREQEMFFKMNEESECANPTSPNKVTKFFPYSSADAA

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias318-331Acidic residues
Compositional bias452-467Polar residues
Compositional bias486-512Polar residues
Compositional bias833-863Basic and acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AAFC03041244
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
AAFC03048417
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
AAFC03048418
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
AAFC03048420
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
This website requires cookies, and the limited processing of your personal data in order to function. By using the site you are agreeing to this as outlined in our Privacy Notice.
Help