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Literature summary extracted from

  • Cai, J.; Crotty, T.M.; Reichert, E.; Carraway, K.L.; Stafforini, D.M.; Topham, M.K.
    Diacylglycerol kinase (delta) and protein kinase Calpha modulate epidermal growth factor receptor abundance and degradation through ubiquitin-specific protease 8 (2010), J. Biol. Chem., 285, 6952-6959.
    View publication on PubMedView publication on EuropePMC

Activating Compound

EC Number Activating Compound Comment Organism Structure
2.7.11.13 diacylglycerol
-
 Homo sapiens

Organism

EC Number Organism UniProt Comment Textmining
2.7.11.13 Homo sapiens
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.7.11.13 HeLa cell
-
 Homo sapiens
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.11.13 ATP + Akt PKCalpha inhibits Akt activity that is necessary for proper ubiquitin-specific protease 8 expression Homo sapiens ADP + phosphorylated Akt
-
 ?
2.7.11.13 ATP + myristoylated alanine-rich C kinase substrate a major PKC substrate Homo sapiens ADP + phosphorylated myristoylated alanine-rich C kinase substrate
-
 ?
2.7.11.13 additional information PKCalpha modulates the levels of ubiquitinated epidermal growth factor receptor through Akt and ubiquitin-specific protease 8, PKCalpha is necessary for diacylglycerol kinase delta to modulate ubiquitin-specific protease 8 levels Homo sapiens ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.7.11.13 PKCalpha
-
 Homo sapiens
2.7.11.13 protein kinase Calpha
-
 Homo sapiens

Cofactor

EC Number Cofactor Comment Organism Structure
2.7.11.13 ATP
-
 Homo sapiens

Expression

EC Number Organism Comment Expression
2.7.11.13 Homo sapiens knockdown of diacylglycerol kinase delta enhances PKCalpha activity up

General Information

EC Number General Information Comment Organism
2.7.11.13 malfunction knockdown of PKCalpha almost completely reduces myristoylated alanine-rich C kinase substrate phosphorylation, indicating that PKCalpha is responsible for the majority of phosphorylated myristoylated alanine-rich C kinase substrate in the cells Homo sapiens