An interaction is inferred from the biochemical effect of one protein upon another, for example, GTP-GDP exchange activity or phosphorylation of a substrate by a kinase. The bait protein executes the activity on the substrate hit protein. A Modification value is recorded for interactions of this type with the possible values Phosphorylation, Ubiquitination, Sumoylation, Dephosphorylation, Methylation, Prenylation, Acetylation, Deubiquitination, Proteolytic Processing, Glucosylation, Nedd(Rub1)ylation, Deacetylation, No Modification, Demethylation.

Publication

PRK1 phosphorylates MARCKS at the PKC sites: serine 152, serine 156 and serine 163.

Palmer RH, Schoenwasser DC, Rahman D, Pappin DJ, Herget T, Parker PJ

The 80kDa Myristolated Alanine-Rich C-Kinase Substrate (MARCKS) is a major in vivo substrate of protein kinase C (PKC). Here we report that MARCKS is a major substrate for the lipid-activated PKC-related kinase (PRK1) in cell extracts. Furthermore, PRK1 is shown to phosphorylate MARCKS on the same sites as PKC in vitro. Thus, control of MARCKS phosphorylation on these previously identified ... [more]

FEBS Lett. Jan. 15, 1996; 378(3);281-5 [Pubmed: 8557118]

Throughput

Low Throughput

Curated By

BioGRID

Interaction Summary

PRKCB

Gene Ontology Biological Process

Gene Ontology Molecular Function

androgen receptor binding [IDA]chromatin binding [IDA]histone binding [IDA]histone kinase activity (H3-T6 specific) [IDA]ligand-dependent nuclear receptor transcription coactivator activity [IMP]protein binding [IPI]protein kinase C binding [IPI]protein serine/threonine kinase activity [TAS]

Gene Ontology Cellular Component

MARCKS