BioPAX pathway converted from "PKC binds active G alpha (z)" in the Reactome database. PKC binds active G alpha (z) PKC binds active G alpha (z) G alpha z (Lounsbury et al. 1991) and G alpha 12 (Kozasa & Gilman, 1996) are excellent in vitro substrates for all three subtypes of protein kinase C (PKC). Activation of PKC in intact platelets by agents such as thrombin, thromboxane A2 (TXA2) analogues and phorbol esters leads to rapid and near-stoichiometric phosphorylation of G alpha z (Carlson et al. 1989). PKC can bind to G alpha z and facilitate its phosphorylation at Ser-27 (Lounsbury et al. 1993). This phosphorylation blocks the interaction of G alpha z with Gbeta:gamma suggesting that it is a regulatory mechanism for attenuating signalling by preventing subunit reassociation. Authored: Jupe, S, 2010-05-18 Reviewed: D'Eustachio, P, 2010-05-21 Edited: Jupe, Steve, 2017-05-11 Reactome DB_ID: 392003 1 plasma membrane GO 0005886 G-protein alpha (z):GTP [plasma membrane] G-protein alpha (z):GTP Reactome DB_ID: 29438 1 cytosol GO 0005829 GTP(4-) [ChEBI:37565] GTP(4-) GTP gtp guanosine 5'-triphosphate(4-) Reactome http://www.reactome.org ChEBI 37565 Reactome DB_ID: 167416 1 UniProt:P19086 GNAZ GNAZ GNAZ FUNCTION Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems.SUBUNIT G-proteins are composed of 3 units; alpha, beta and gamma. The alpha chain contains the guanine nucleotide binding site. Interacts with ADGRB2 (PubMed:28891236).SIMILARITY Belongs to the G-alpha family. G(i/o/t/z) subfamily. Homo sapiens NCBI Taxonomy 9606 UniProt P19086 Chain Coordinates 2 EQUAL 355 EQUAL Reactome Database ID Release 82 392003 Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=392003 Reactome R-HSA-392003 2 Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-HSA-392003.2 Converted from EntitySet in Reactome Reactome DB_ID: 804920 1 Protein kinase C conventional and novel isoforms [plasma membrane] Converted from EntitySet in Reactome. Each synonym is a name of a PhysicalEntity, and each XREF points to one PhysicalEntity Reactome DB_ID: 8982710 1 G-alpha(z):GTP:PKC [plasma membrane] G-alpha(z):GTP:PKC Reactome DB_ID: 392003 1 Converted from EntitySet in Reactome Reactome DB_ID: 804920 1 Reactome Database ID Release 82 8982710 Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=8982710 Reactome R-HSA-8982710 1 Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-HSA-8982710.1 Reactome Database ID Release 82 8982703 Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=8982703 Reactome R-HSA-8982703 2 Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-HSA-8982703.2 2502548 Pubmed 1989 Thrombin and phorbol esters cause the selective phosphorylation of a G protein other than Gi in human platelets Carlson, KE Brass, LF Manning, DR J Biol Chem 264:13298-305 7559455 Pubmed 1995 Phosphorylation of Gz alpha by protein kinase C blocks interaction with the beta gamma complex Fields, T A Casey, P J J. Biol. Chem. 270:23119-25 1939224 Pubmed 1991 Phosphorylation of Gz in human platelets. Selectivity and site of modification Lounsbury, KM Casey, PJ Brass, LF Manning, DR J Biol Chem 266:22051-6 8647866 Pubmed 1996 Protein kinase C phosphorylates G12 alpha and inhibits its interaction with G beta gamma Kozasa, T Gilman, AG J Biol Chem 271:12562-7 8429024 Pubmed 1993 Analysis of Gz alpha by site-directed mutagenesis. Sites and specificity of protein kinase C-dependent phosphorylation Lounsbury, KM Schlegel, B Poncz, M Brass, LF Manning, DR J Biol Chem 268:3494-8