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; OMA:PRKACB - orthologs
Gene location (Human) Chr. Chromosome 1 (human) [1] Band 1p31.1 Start 84,078,062 bp [1] End 84,238,498 bp [1]
Gene location (Mouse) Chr. Chromosome 3 (mouse) [2] Band 3|3 H2 Start 146,435,329 bp [2] End 146,518,745 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) 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 anterior amygdaloid area lateral septal nucleus dorsomedial hypothalamic nucleus mammillary body arcuate nucleus paraventricular nucleus of hypothalamus lateral hypothalamus ventral tegmental area primary motor cortex 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 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 Species Human Mouse Entrez 5567 18749 Ensembl ENSG00000142875 ENSMUSG00000005034 UniProt P22694 P68181 RefSeq (mRNA) 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 NM_001164198 NM_001164199 NM_001164200 NM_011100 RefSeq (protein) 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 Location (UCSC) Chr 1: 84.08 – 84.24 Mb Chr 3: 146.44 – 146.52 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

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]

References

1. GRCh38: Ensembl release 89: ENSG00000142875 – Ensembl, May 2017
2. 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.
5. "Entrez Gene: PRKACB protein kinase, cAMP-dependent, catalytic, beta".
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. 101 (4). UNITED STATES: 365–76. doi: 10.1016/S0092-8674(00)80847-8 . ISSN   0092-8674. PMID   10830164. S2CID   6496567.
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. 22 (8). England: 1790–800. doi:10.1093/emboj/cdg177. ISSN   0261-4189. PMC   154469 . PMID   12682012.

Further reading

• 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.