PRKACB

PRKACB
Identifiers
Aliases	PRKACB , PKA C-beta, PKACB, protein kinase cAMP-activated catalytic subunit beta, CAFD2
External IDs	OMIM: 176892 MGI: 97594 HomoloGene: 121718 GeneCards: PRKACB
Gene location (Human)
Chr.	Chromosome 1 (human)
End	84,238,498 bp
Gene location (Mouse)
Chr.	Chromosome 3 (mouse)
End	146,518,745 bp
RNA expression pattern
	Top expressed in
	endothelial cell; ; Brodmann area 23; ; postcentral gyrus; ; middle temporal gyrus; ; entorhinal cortex; ; orbitofrontal cortex; ; pons; ; Brodmann area 46; ; superior vestibular nucleus; ; corpus callosum;
	Top expressed in
	ventromedial nucleus; ; dorsomedial hypothalamic nucleus; ; mammillary body; ; arcuate nucleus; ; paraventricular nucleus of hypothalamus; ; lateral hypothalamus; ; ventral tegmental area; ; primary motor cortex; ; median eminence; ; piriform cortex;
	More reference expression data
	; ;
	More reference expression data
Gene ontology
Molecular function	transferase activity ; nucleotide binding ; protein kinase activity ; cAMP-dependent protein kinase activity ; protein binding ; ATP binding ; ubiquitin protein ligase binding ; magnesium ion binding ; kinase activity ; protein serine/threonine kinase activity ; protein kinase A regulatory subunit binding ;
Cellular component	cytoplasm ; centrosome ; membrane ; plasma membrane ; nucleoplasm ; ciliary base ; perinuclear region of cytoplasm ; cAMP-dependent protein kinase complex ; extracellular exosome ; nucleus ; cytosol ; intercellular bridge ;
Biological process	negative regulation of meiotic cell cycle ; activation of protein kinase A activity ; phosphorylation ; adenylate cyclase-modulating G protein-coupled receptor signaling pathway ; cellular response to glucagon stimulus ; negative regulation of smoothened signaling pathway involved in dorsal/ventral neural tube patterning ; blood coagulation ; stimulatory C-type lectin receptor signaling pathway ; regulation of protein processing ; protein phosphorylation ; neural tube closure ; response to clozapine ; renal water homeostasis ; signal transduction ; high-density lipoprotein particle assembly ; G protein-coupled receptor signaling pathway ;
	Sources:Amigo / QuickGO
Orthologs
	5567
	18749
	ENSG00000142875
	ENSMUSG00000005034
	P22694
	P68181
NM_001242857 ; NM_001242858 ; NM_001242859 ; NM_001242860 ; NM_001242861 ;
	NM_001242862 ; NM_001300915 ; NM_001300916 ; NM_001300917 ; NM_002731 ; NM_182948 ; NM_207578 ; NM_001375560 ; NM_001375561 ; NM_001375562 ; NM_001375563 ; NM_001375564 ; NM_001375565 ; NM_001375569 ; NM_001375571 ; NM_001375572 ; NM_001375573 ; NM_001375574 ; NM_001375575 ; NM_001375576 ; NM_001375577 ; NM_001375578 ; NM_001375579 ; NM_001375580 ; NM_001375581 Contents Interactions ; References ; Further reading ;
	NM_001164198 ; NM_001164199 ; NM_001164200 ; NM_011100
NP_001229786 ; NP_001229787 ; NP_001229788 ; NP_001229789 ; NP_001229790 ;
	NP_001229791 ; NP_001287844 ; NP_001287845 ; NP_001287846 ; NP_002722 ; NP_891993 ; NP_997461 ; NP_001362489 ; NP_001362490 ; NP_001362491 ; NP_001362492 ; NP_001362493 ; NP_001362494 ; NP_001362498 ; NP_001362500 ; NP_001362501 ; NP_001362502 ; NP_001362503 ; NP_001362504 ; NP_001362505 ; NP_001362506 ; NP_001362507 ; NP_001362508 ; NP_001362509 ; NP_001362510 ; NP_002722.1
	NP_001157670 ; NP_001157671 ; NP_001157672 ; NP_035230
	Wikidata
View/Edit Human	View/Edit Mouse

Last updated December 24, 2023

cAMP-dependent protein kinase catalytic subunit beta is an enzyme that in humans is encoded by the PRKACB gene.^[5]

cAMP is a signaling molecule important for a variety of cellular functions. cAMP exerts its effects by activating the protein kinase A (PKA), which transduces the signal through phosphorylation of different target proteins. The inactive holoenzyme of PKA is a tetramer composed of two regulatory and two catalytic subunits. cAMP causes the dissociation of the inactive holoenzyme into a dimer of regulatory subunits bound to four cAMP and two free monomeric catalytic subunits. Four different regulatory subunits and three catalytic subunits of PKA have been identified in humans. The protein encoded by this gene is a member of the serine/threonine protein kinase family and is a catalytic subunit of PKA. Three alternatively spliced transcript variants encoding distinct isoforms have been observed.^[5]

Interactions

PRKACB has been shown to interact with Ryanodine receptor 2 ^[6] and Low affinity nerve growth factor receptor.^[7]

Related Research Articles

<span class="mw-page-title-main">Protein kinase A</span> Family of enzymes

In cell biology, protein kinase A (PKA) is a family of serine-threonine kinase whose activity is dependent on cellular levels of cyclic AMP (cAMP). PKA is also known as cAMP-dependent protein kinase. PKA has several functions in the cell, including regulation of glycogen, sugar, and lipid metabolism. It should not be confused with 5'-AMP-activated protein kinase.

Biological crosstalk refers to instances in which one or more components of one signal transduction pathway affects another. This can be achieved through a number of ways with the most common form being crosstalk between proteins of signaling cascades. In these signal transduction pathways, there are often shared components that can interact with either pathway. A more complex instance of crosstalk can be observed with transmembrane crosstalk between the extracellular matrix (ECM) and the cytoskeleton.

Phosphorylase kinase (PhK) is a serine/threonine-specific protein kinase which activates glycogen phosphorylase to release glucose-1-phosphate from glycogen. PhK phosphorylates glycogen phosphorylase at two serine residues, triggering a conformational shift which favors the more active glycogen phosphorylase “a” form over the less active glycogen phosphorylase b.

The catalytic subunit α of protein kinase A is a key regulatory enzyme that in humans is encoded by the PRKACA gene. This enzyme is responsible for phosphorylating other proteins and substrates, changing their activity. Protein kinase A catalytic subunit is a member of the AGC kinase family, and contributes to the control of cellular processes that include glucose metabolism, cell division, and contextual memory. PKA Cα is part of a larger protein complex that is responsible for controlling when and where proteins are phosphorylated. Defective regulation of PKA holoenzyme activity has been linked to the progression of cardiovascular disease, certain endocrine disorders and cancers.

cAMP-dependent protein kinase type I-alpha regulatory subunit is an enzyme that in humans is encoded by the PRKAR1A gene.

cAMP-dependent protein kinase type II-alpha regulatory subunit is an enzyme that in humans is encoded by the PRKAR2A gene.

5'-AMP-activated protein kinase catalytic subunit alpha-1 is an enzyme that in humans is encoded by the PRKAA1 gene.

5'-AMP-activated protein kinase subunit beta-1 is an enzyme that in humans is encoded by the PRKAB1 gene.

cAMP-dependent protein kinase type II-beta regulatory subunit is an enzyme that in humans is encoded by the PRKAR2B gene.

5'-AMP-activated protein kinase subunit gamma-2 is an enzyme that in humans is encoded by the PRKAG2 gene.

Phosphatidylinositol-4,5-bisphosphate 3-kinase catalytic subunit beta isoform is an enzyme that in humans is encoded by the PIK3CB gene.

A-kinase anchor protein 5 is a protein that in humans is encoded by the AKAP5 gene.

Serine/threonine-protein kinase D3 (PKD3) or PKC-nu is an enzyme that in humans is encoded by the PRKD3 gene.

5'-AMP-activated protein kinase subunit gamma-1 is an enzyme that in humans is encoded by the PRKAG1 gene.

cAMP-dependent protein kinase type I-beta regulatory subunit is an enzyme that in humans is encoded by the PRKAR1B gene.

A kinase anchor protein 1, mitochondrial is an enzyme that in humans is encoded by the AKAP1 gene.

5'-AMP-activated protein kinase subunit beta-2 is an enzyme that in humans is encoded by the PRKAB2 gene.

cAMP-dependent protein kinase catalytic subunit gamma is an enzyme that in humans is encoded by the PRKACG gene.

cAMP-dependent protein kinase inhibitor alpha is a protein that in humans is encoded by the PKIA gene.

In the field of molecular biology, the cAMP-dependent pathway, also known as the adenylyl cyclase pathway, is a G protein-coupled receptor-triggered signaling cascade used in cell communication.

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000142875 - Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000005034 - Ensembl, May 2017
↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
1 2 "Entrez Gene: PRKACB protein kinase, cAMP-dependent, catalytic, beta".
↑ 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. UNITED STATES. 101 (4): 365–76. doi: 10.1016/S0092-8674(00)80847-8 . ISSN 0092-8674. PMID 10830164. S2CID 6496567.
↑ Higuchi H, Yamashita Toshihide, Yoshikawa Hideki, Tohyama Masaya (April 2003). "PKA phosphorylates the p75 receptor and regulates its localization to lipid rafts". EMBO J. England. 22 (8): 1790–800. doi:10.1093/emboj/cdg177. ISSN 0261-4189. PMC 154469 . PMID 12682012.

Simard J, Bérubé D, Sandberg M, et al. (1992). "Assignment of the gene encoding the catalytic subunit C beta of cAMP-dependent protein kinase to the p36 band on chromosome 1". Hum. Genet. 88 (6): 653–7. doi:10.1007/BF02265292. PMID 1551670. S2CID 20799373.
Hofmann B, Nishanian P, Baldwin RL, et al. (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.
Beebe SJ, Oyen O, Sandberg M, et al. (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.
Scarpetta MA, Uhler MD (1993). "Evidence for two additional isoforms of the endogenous protein kinase inhibitor of cAMP-dependent protein kinase in mouse". J. Biol. Chem. 268 (15): 10927–31. doi: 10.1016/S0021-9258(18)82074-9 . PMID 7684369.
Hofmann B, Nishanian P, Nguyen T, et al. (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, et al. (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.
Gamm DM, Baude EJ, Uhler MD (1996). "The major catalytic subunit isoforms of cAMP-dependent protein kinase have distinct biochemical properties in vitro and in vivo". J. Biol. Chem. 271 (26): 15736–42. doi: 10.1074/jbc.271.26.15736 . PMID 8662989.
Swingler S, Gallay P, Camaur D, et al. (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, et al. (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.
Rabbi MF, al-Harthi L, Saifuddin M, Roebuck KA (1998). "The cAMP-dependent protein kinase A and protein kinase C-beta pathways synergistically interact to activate HIV-1 transcription in latently infected cells of monocyte/macrophage lineage". Virology. 245 (2): 257–69. doi: 10.1006/viro.1998.9158 . PMID 9636365.
Zidovetzki R, Wang JL, Chen P, et al. (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, et al. (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.
Hartley JL, Temple GF, Brasch MA (2001). "DNA cloning using in vitro site-specific recombination". Genome Res. 10 (11): 1788–95. doi:10.1101/gr.143000. PMC 310948 . PMID 11076863.
Jiang CH, Tsien JZ, Schultz PG, Hu Y (2001). "The effects of aging on gene expression in the hypothalamus and cortex of mice". Proc. Natl. Acad. Sci. U.S.A. 98 (4): 1930–4. Bibcode:2001PNAS...98.1930J. doi: 10.1073/pnas.98.4.1930 . PMC 29359 . PMID 11172053.
Ørstavik S, Reinton N, Frengen E, et al. (2001). "Identification of novel splice variants of the human catalytic subunit Cbeta of cAMP-dependent protein kinase". Eur. J. Biochem. 268 (19): 5066–73. doi: 10.1046/j.0014-2956.2001.02429.x . PMID 11589697.
Wu KJ, Mattioli M, Morse HC, Dalla-Favera R (2002). "c-MYC activates protein kinase A (PKA) by direct transcriptional activation of the PKA catalytic subunit beta (PKA-Cbeta) gene". Oncogene. 21 (51): 7872–82. doi: 10.1038/sj.onc.1205986 . PMID 12420224.
Strausberg RL, Feingold EA, Grouse LH, et al. (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.
Higuchi H, Yamashita T, Yoshikawa H, Tohyama M (2003). "PKA phosphorylates the p75 receptor and regulates its localization to lipid rafts". EMBO J. 22 (8): 1790–800. doi:10.1093/emboj/cdg177. PMC 154469 . PMID 12682012.
Gassel M, Breitenlechner CB, Rüger P, et al. (2003). "Mutants of protein kinase A that mimic the ATP-binding site of protein kinase B (AKT)". J. Mol. Biol. 329 (5): 1021–34. doi:10.1016/S0022-2836(03)00518-7. PMID 12798691.

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[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000142875 - Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000005034 - Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[entrez-5] 1 2 "Entrez Gene: PRKACB protein kinase, cAMP-dependent, catalytic, beta".

[pmid10830164-6] 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. UNITED STATES. 101 (4): 365–76. doi: 10.1016/S0092-8674(00)80847-8 . ISSN 0092-8674. PMID 10830164. S2CID 6496567.

[pmid12682012-7] Higuchi H, Yamashita Toshihide, Yoshikawa Hideki, Tohyama Masaya (April 2003). "PKA phosphorylates the p75 receptor and regulates its localization to lipid rafts". EMBO J. England. 22 (8): 1790–800. doi:10.1093/emboj/cdg177. ISSN 0261-4189. PMC 154469 . PMID 12682012.

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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)

PRKACB

Contents

Interactions

Related Research Articles

References

Further reading