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PRKACG

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From Wikipedia, the free encyclopedia

Protein-coding gene in the species Homo sapiens

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)^[1]

Band	9q21.11	Start	69,012,504bp^[1]
Band	9q21.11	End	69,014,113bp^[1]

RNA expression pattern

Bgee

Human

Mouse (ortholog)

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

BioGPS


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

Species

Human

Mouse

Entrez


5568


n/a

Ensembl


ENSG00000165059


n/a

UniProt


P22612


n/a

RefSeq (mRNA)


NM_002732


n/a

RefSeq (protein)


NP_002723


n/a

Location (UCSC)

Chr 9: 69.01 – 69.01 Mb

n/a

PubMed search

^[2]

n/a

Wikidata

View/Edit Human

cAMP-dependent protein kinase catalytic subunit gamma is anenzyme that in humans is encoded by thePRKACGgene.^[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 isintronless and is thought to be aretrotransposon derived from the gene for the alpha form of the PKAcatalytic subunit.^[5]

Interactions

[edit]

PRKACG has been shown tointeract withRyanodine receptor 2.^[6]

References

[edit]

^^a ^b ^cGRCh38: Ensembl release 89: ENSG00000165059 –Ensembl, May 2017
^"Human PubMed Reference:".National Center for Biotechnology Information, U.S. National Library of Medicine.
^Beebe SJ, Oyen O, Sandberg M, Froysa A, Hansson V, Jahnsen T (June 1990)."Molecular cloning of a tissue-specific protein kinase (C gamma) from human testis--representing a third isoform for the catalytic subunit of cAMP-dependent protein kinase".Mol Endocrinol.4 (3):465–75.doi:10.1210/mend-4-3-465.PMID 2342480.
^Reinton N, Haugen TB, Orstavik S, Skalhegg BS, Hansson V, Jahnsen T, Tasken K (August 1998). "The gene encoding the C gamma catalytic subunit of cAMP-dependent protein kinase is a transcribed retroposon".Genomics.49 (2):290–7.doi:10.1006/geno.1998.5240.PMID 9598317.
^^a ^b"Entrez Gene: PRKACG protein kinase, cAMP-dependent, catalytic, gamma".
^Marx SO, Reiken S, Hisamatsu Y, Jayaraman T, Burkhoff D, Rosemblit N, Marks A R (May 2000)."PKA phosphorylation dissociates FKBP12.6 from the calcium release channel (ryanodine receptor): defective regulation in failing hearts".Cell.101 (4). UNITED STATES:365–76.doi:10.1016/S0092-8674(00)80847-8.ISSN 0092-8674.PMID 10830164.S2CID 6496567.

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.

Kinases:Serine/threonine-specific protein kinases (EC 2.7.11-12)

Serine/threonine-specific protein kinases (EC 2.7.11.1-EC 2.7.11.20)

Non-specific serine/threonine protein kinases (EC 2.7.11.1)	LATS1 LATS2 MAST1 MAST2 STK38 STK38L CIT ROCK1 SGK SGK2 SGK3 Protein kinase B AKT1 AKT2 AKT3 Ataxia telangiectasia mutated mTOR EIF-2 kinases PKR HRI EIF2AK3 EIF2AK4 Wee1 WEE1
Pyruvate dehydrogenase kinase (EC 2.7.11.2)	PDK1 PDK2 PDK3 PDK4
Dephospho-(reductase kinase) kinase (EC 2.7.11.3)	AMP-activated protein kinase α PRKAA1 PRKAA2 β PRKAB1 PRKAB2 γ PRKAG1 PRKAG2 PRKAG3
3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring) kinase (EC 2.7.11.4)	BCKDK BCKDHA BCKDHB
(isocitrate dehydrogenase (NADP+)) kinase (EC 2.7.11.5)	IDH2 IDH3A IDH3B IDH3G
(tyrosine 3-monooxygenase) kinase (EC 2.7.11.6)	STK4
Myosin-heavy-chain kinase (EC 2.7.11.7)	Aurora kinase Aurora A kinase Aurora B kinase Aurora C kinase
Fas-activated serine/threonine kinase (EC 2.7.11.8)	FASTK STK10
Goodpasture-antigen-binding protein kinase (EC 2.7.11.9)	-
IκB kinase (EC 2.7.11.10)	CHUK IKK2 TBK1 IKBKE IKBKG IKBKAP
cAMP-dependent protein kinase (EC 2.7.11.11)	Protein kinase A PRKACG PRKACB PRKACA PRKY
cGMP-dependent protein kinase (EC 2.7.11.12)	Protein kinase G PRKG1
Protein kinase C (EC 2.7.11.13)	Protein kinase C Protein kinase Cζ PKC alpha PRKCB1 PRKCD PRKCE PRKCH PRKCG PRKCI PRKCQ Protein kinase N1 PKN2 PKN3
Rhodopsin kinase (EC 2.7.11.14)	Rhodopsin kinase
Beta adrenergic receptor kinase (EC 2.7.11.15)	Beta adrenergic receptor kinase Beta adrenergic receptor kinase-2
G-protein coupled receptor kinases (EC 2.7.11.16)	GRK4 GRK5 GRK6
Ca2+/calmodulin-dependent (EC 2.7.11.17)	BRSK2 CAMK1 CAMK1A CAMK1B CAMK1D CAMK1G CAMK2 CAMK2A CAMK2B CAMK2D CAMK2G CAMK4 MLCK CASK CHEK1 CHEK2 DAPK1 DAPK2 DAPK3 STK11 MAPKAPK2 MAPKAPK3 MAPKAPK5 MARK1 MARK2 MARK3 MARK4 MELK MKNK1 MKNK2 NUAK1 NUAK2 OBSCN PASK PHKG1 PHKG2 PIM1 PIM2 PKD1 PRKD2 PRKD3 PSKH1 SNF1LK2 KIAA0999 STK40 SNF1LK SNRK SPEG TSSK2 Kalirin TRIB1 TRIB2 TRIB3 TRIO Titin DCLK1
Myosin light-chain kinase (EC 2.7.11.18)	MYLK MYLK2 MYLK3 MYLK4
Phosphorylase kinase (EC 2.7.11.19)	PHKA1 PHKA2 PHKB PHKG1 PHKG2
Elongation factor 2 kinase (EC 2.7.11.20)	EEF2K STK19
Polo kinase (EC 2.7.11.21)	PLK1 PLK2 PLK3 PLK4

Serine/threonine-specific protein kinases (EC 2.7.11.21-EC 2.7.11.30)

Polo kinase (EC 2.7.11.21)	PLK1 PLK2 PLK3 PLK4
Cyclin-dependent kinase (EC 2.7.11.22)	CDK1 CDK2 CDKL2 CDK3 CDK4 CDK5 CDKL5 CDK6 CDK7 CDK8 CDK9 CDK10 CDK12 CDC2L5 PCTK1 PCTK2 PCTK3 PFTK1 CDC2L1
(RNA-polymerase)-subunit kinase (EC 2.7.11.23)	RPS6KA5 RPS6KA4 P70S6 kinase P70-S6 Kinase 1 RPS6KB2 RPS6KA2 RPS6KA3 RPS6KA1 RPS6KC1
Mitogen-activated protein kinase (EC 2.7.11.24)	Extracellular signal-regulated MAPK1 MAPK3 MAPK4 MAPK6 MAPK7 MAPK12 MAPK15 C-Jun N-terminal MAPK8 MAPK9 MAPK10 P38 mitogen-activated protein MAPK11 MAPK13 MAPK14
MAP3K (EC 2.7.11.25)	MAP kinase kinase kinases MAP3K1 MAP3K2 MAP3K3 MAP3K4 MAP3K5 MAP3K6 MAP3K7 MAP3K8 RAFs ARAF BRAF KSR1 KSR2 MLKs MAP3K12 MAP3K13 MAP3K9 MAP3K10 MAP3K11 MAP3K7 ZAK CDC7 MAP3K14
Tau-protein kinase (EC 2.7.11.26)	TPK1 TTK GSK-3
(acetyl-CoA carboxylase) kinase (EC 2.7.11.27)	-
Tropomyosin kinase (EC 2.7.11.28)	-
Low-density-lipoprotein receptor kinase (EC 2.7.11.29)	-
Receptor protein serine/threonine kinase (EC 2.7.11.30)	Bone morphogenetic protein receptors BMPR1 BMPR1A BMPR1B BMPR2 ACVR1 ACVR1B ACVR1C ACVR2A ACVR2B ACVRL1 Anti-Müllerian hormone receptor

Dual-specificity kinases (EC 2.7.12)

MAP2K	MAP2K1 MAP2K2 MAP2K3 MAP2K4 MAP2K5 MAP2K6 MAP2K7

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	EC1Oxidoreductases (list) EC2Transferases (list) EC3Hydrolases (list) EC4Lyases (list) EC5Isomerases (list) EC6Ligases (list) EC7Translocases (list)

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