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Literature summary for 2.7.11.1 extracted from

  • Brauksiepe, B.; Mujica, A.O.; Herrmann, H.; Schmidt, E.R.
    The Serine/threonine kinase Stk33 exhibits autophosphorylation and phosphorylates the intermediate filament protein Vimentin (2008), BMC Biochem., 9, 25.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.7.11.1

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli Mus musculus

Protein Variants

Protein Variants Comment Organism
additional information co-immunoprecipitation experiments employing cultured cell extracts indicate that Stk33 and vimentin are associated in vivo Mus musculus

Organism

Organism UniProt Comment Textmining
Mus musculus Q924X7
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-

Posttranslational Modification

Posttranslational Modification Comment Organism
phosphoprotein Stk33 is able to perform autophosphorylation Mus musculus

Source Tissue

Source Tissue Comment Organism Textmining
Sertoli cell sertoli cell culture SerW3 is used Mus musculus
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + vimentin kinase assays demonstrate that Stk33 is able to specifically phosphorylate the non-alpha-helical amino-terminal domain of vimentin in vitro Mus musculus ADP + phosphorylated vimentin
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 ?

Synonyms

Synonyms Comment Organism
serine/threonine kinase
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 Mus musculus
Stk33
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 Mus musculus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
 assay at Mus musculus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
 assay at Mus musculus