PRKACG

PRKACG
Identifiers
Aliases	PRKACG, KAPG, PKACg, BDPLT19, protein kinase cAMP-activated catalytic subunit gamma
External IDs	OMIM: 176893; HomoloGene: 55677; GeneCards: PRKACG; OMA:PRKACG - orthologs
Gene location (Human)
Chr.	Chromosome 9 (human)
End	69,014,113 bp
RNA expression pattern
	Top expressed in
	sperm; ; left testis; ; right testis; ; buccal mucosa cell; ; amniotic fluid; ; tendon of biceps brachii; ; muscular system; ; muscle; ; muscle; ; skeletal muscle;
	n/a
	More reference expression data
	More reference expression data
Gene ontology
Molecular function	transferase activity; nucleotide binding; protein kinase activity; cAMP-dependent protein kinase activity; kinase activity; ATP binding; protein serine/threonine kinase activity;
Cellular component	nucleoplasm; cytosol; intercellular bridge; ciliary base;
Biological process	activation of protein kinase A activity; male gonad development; phosphorylation; cellular response to glucagon stimulus; blood coagulation; stimulatory C-type lectin receptor signaling pathway; protein phosphorylation; spermatogenesis; renal water homeostasis; high-density lipoprotein particle assembly;
	Sources:Amigo / QuickGO
Orthologs
	5568
	n/a
	ENSG00000165059
	n/a
	P22612
	n/a
	NM_002732
	n/a
	NP_002723
	n/a
	Wikidata
View/Edit Human

cAMP-dependent protein kinase catalytic subunit gamma is an enzyme that in humans is encoded by the PRKACG gene.^[3]^[4]^[5]

Cyclic AMP-dependent protein kinase (PKA) consists of two catalytic subunits and a regulatory subunit dimer. This gene encodes the gamma form of its catalytic subunit. The gene is intronless and is thought to be a retrotransposon derived from the gene for the alpha form of the PKA catalytic subunit.^[5]

Interactions

PRKACG has been shown to interact with Ryanodine receptor 2.^[6]

References

Foss KB, Simard J, Bérubé D, Beebe S, Sandberg M, Grzeschik KH, Gagné R, Hansson V, Jahnsen T (1992). "Localization of the catalytic subunit C gamma of the cAMP-dependent protein kinase gene (PRKACG) to human chromosome region 9q13". Cytogenet. Cell Genet. 60 (1): 22–5. doi:10.1159/000133286. PMID 1339328.
Hofmann B, Nishanian P, Baldwin RL, Insixiengmay P, Nel A, Fahey JL (1991). "HIV inhibits the early steps of lymphocyte activation, including initiation of inositol phospholipid metabolism". J. Immunol. 145 (11): 3699–705. doi:10.4049/jimmunol.145.11.3699. PMID 1978848.
Hofmann B, Nishanian P, Nguyen T, Insixiengmay P, Fahey JL (1993). "Human immunodeficiency virus proteins induce the inhibitory cAMP/protein kinase A pathway in normal lymphocytes". Proc. Natl. Acad. Sci. U.S.A. 90 (14): 6676–80. Bibcode:1993PNAS...90.6676H. doi:10.1073/pnas.90.14.6676. PMC 46995. PMID 7688126.
Hofmann B, Nishanian P, Fan J, Nguyen T, Fahey JL (1994). "HIV Gag p17 protein impairs proliferation of normal lymphocytes in vitro". AIDS. 8 (7): 1016–7. doi:10.1097/00002030-199407000-00025. PMID 7946090.
Swingler S, Gallay P, Camaur D, Song J, Abo A, Trono D (1997). "The Nef protein of human immunodeficiency virus type 1 enhances serine phosphorylation of the viral matrix". J. Virol. 71 (6): 4372–7. doi:10.1128/JVI.71.6.4372-4377.1997. PMC 191654. PMID 9151826.
Chen P, Mayne M, Power C, Nath A (1997). "The Tat protein of HIV-1 induces tumor necrosis factor-alpha production. Implications for HIV-1-associated neurological diseases". J. Biol. Chem. 272 (36): 22385–8. doi:10.1074/jbc.272.36.22385. PMID 9278385.
Liapi C, Takahashi N, Raynaud F, Evain-Brion D, Anderson WB (1998). "Effects of [D-Ala1] peptide T-NH2 and HIV envelope glycoprotein gp120 on cyclic AMP dependent protein kinases in normal and psoriatic human fibroblasts". J. Invest. Dermatol. 110 (4): 332–7. doi:10.1046/j.1523-1747.1998.00149.x. PMID 9540970.
Zidovetzki R, Wang JL, Chen P, Jeyaseelan R, Hofman F (1998). "Human immunodeficiency virus Tat protein induces interleukin 6 mRNA expression in human brain endothelial cells via protein kinase C- and cAMP-dependent protein kinase pathways". AIDS Res. Hum. Retroviruses. 14 (10): 825–33. doi:10.1089/aid.1998.14.825. PMID 9671211.
Mayne M, Bratanich AC, Chen P, Rana F, Nath A, Power C (1998). "HIV-1 tat molecular diversity and induction of TNF-alpha: implications for HIV-induced neurological disease". Neuroimmunomodulation. 5 (3–4): 184–92. doi:10.1159/000026336. PMID 9730685. S2CID 19529677.
Bodnar RJ, Xi X, Li Z, Berndt MC, Du X (2003). "Regulation of glycoprotein Ib-IX-von Willebrand factor interaction by cAMP-dependent protein kinase-mediated phosphorylation at Ser 166 of glycoprotein Ib(beta)". J. Biol. Chem. 277 (49): 47080–7. doi:10.1074/jbc.M208329200. PMID 12361948.
Strausberg RL, Feingold EA, Grouse LH, Derge JG, Klausner RD, Collins FS, Wagner L, Shenmen CM, Schuler GD (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
Cartier C, Hemonnot B, Gay B, Bardy M, Sanchiz C, Devaux C, Briant L (2003). "Active cAMP-dependent protein kinase incorporated within highly purified HIV-1 particles is required for viral infectivity and interacts with viral capsid protein". J. Biol. Chem. 278 (37): 35211–9. doi:10.1074/jbc.M301257200. PMID 12842892.
Masci AM, Galgani M, Cassano S, De Simone S, Gallo A, De Rosa V, Zappacosta S, Racioppi L (2004). "HIV-1 gp120 induces anergy in naive T lymphocytes through CD4-independent protein kinase-A-mediated signaling". J. Leukoc. Biol. 74 (6): 1117–24. doi:10.1189/jlb.0503239. PMID 12972513. S2CID 13393007.
Zhang W, Morris GZ, Beebe SJ (2004). "Characterization of the cAMP-dependent protein kinase catalytic subunit Cgamma expressed and purified from sf9 cells". Protein Expr. Purif. 35 (1): 156–69. doi:10.1016/j.pep.2004.01.006. PMID 15039079.
Stevanin G, Hahn V, Lohmann E, Bouslam N, Gouttard M, Soumphonphakdy C, Welter ML, Ollagnon-Roman E, Lemainque A (2004). "Mutation in the catalytic domain of protein kinase C gamma and extension of the phenotype associated with spinocerebellar ataxia type 14". Arch. Neurol. 61 (8): 1242–8. doi:10.1001/archneur.61.8.1242. PMID 15313841.
Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R (2004). "The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)

PRKACG

Interactions

References

Further reading

Suggest as cover photo

Thank you for helping!

Install Wikiwand

Don't forget to rate us

Tell your friends about Wikiwand!

Enjoying Wikiwand?

Tell your friends and spread the love:

Your preferred languages

All languages

Follow Us

Don't forget to rate us

Our magic isn't perfect

Thank you for helping!

Oh no, there's been an error