Literature summary for 2.7.7.14 extracted from

Pavlovic, Z.; Zhu, L.; Pereira, L.; Singh, R.; Cornel, R.; Bakovic, M.
Isoform-specific and protein kinase C-mediated regulation of CTP:phosphoethanolamine cytidylyltransferase phosphorylation (2014), J. Biol. Chem., 289, 9053-9064.

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Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	Q99447	-	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
phosphoprotein	splice variant Pcyt2beta is specifically phosphorylated at the end of the first cytidylyltransferase domain. Splice variant Pcyt2alpha is phosphorylated within the alpha-specific motif that is spliced out in Pcyt2beta and on two protein kinase C consensus serine residues, Ser215 and Ser223. Single and double mutations of protein kinase C consensus sites reduce Pcyt2alpha phosphorylation, activity, and phosphatidylethanolamine synthesis by 50-90%. The phosphorylation and activity of endogenous Pcyt2 are dramatically increased with phorbol esters and reduced by specific protein kinase C inhibitors. In vitro translated Pcyt2 is phosphorylated by protein kinase Calpha, protein kinase CbetaI, and protein kinase CbetaII. The phosphorylated sites cluster within and flanking the central linker region that connects the two catalytic domains and is a regulatory segment not present in other cytidylyltransferases	Homo sapiens

Source Tissue

Source Tissue	Comment	Organism	Textmining
MCF-7 cell	-	Homo sapiens	-

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Release 2023.1 (January 2023)