PRKACA

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Protein kinase, cAMP-dependent, catalytic, alpha
Protein PRKACA PDB 1apm.png
PDB rendering based on 1apm.
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
Symbols PRKACA ; PKACA
External IDs OMIM601639 MGI97592 HomoloGene121574 ChEMBL: 4101 GeneCards: PRKACA Gene
EC number 2.7.11.11
Orthologs
Species Human Mouse
Entrez 5566 18747
Ensembl ENSG00000072062 ENSMUSG00000005469
UniProt P17612 P05132
RefSeq (mRNA) NM_002730 NM_001277898
RefSeq (protein) NP_002721 NP_001264827
Location (UCSC) Chr 19:
14.2 – 14.23 Mb
Chr 8:
83.97 – 84 Mb
PubMed search [1] [2]

cAMP-dependent protein kinase catalytic subunit alpha is an enzyme that in humans is encoded by the PRKACA gene.[1]

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 AMPK have been identified in humans. The protein encoded by this gene is a member of the Ser/Thr protein kinase family and is a catalytic subunit of AMPK. Alternatively spliced transcript variants encoding distinct isoforms have been observed.[2]

Interactive pathway map[edit]

Click on genes, proteins and metabolites below to link to respective articles. [§ 1]

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NicotineDopaminergic_WP1602 go to article go to article go to article Go to article go to article Go to article Go to article go to article go to article go to article go to article go to article go to article go to article go to article go to article go to article go to article Go to article go to article go to article go to article go to article Go to article Go to article go to article Go to article Go to article Go to article go to article Go to article Go to article Go to article go to article go to article go to article go to article go to article go to article Go to article go to article Go to article Go to article go to article go to article Go to article go to article Go to article Go to article go to article
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Nicotine Activity on Dopaminergic Neurons edit
  1. ^ The interactive pathway map can be edited at WikiPathways: "NicotineDopaminergic_WP1602". 

Interactions[edit]

PRKACA has been shown to interact with Phosphoinositide-dependent kinase-1,[3] IQGAP1,[4] KvLQT1[5] and Ryanodine receptor 2.[6]

References[edit]

  1. ^ Tasken K, Solberg R, Zhao Y, Hansson V, Jahnsen T, Siciliano MJ (February 1997). "The gene encoding the catalytic subunit C alpha of cAMP-dependent protein kinase (locus PRKACA) localizes to human chromosome region 19p13.1". Genomics 36 (3): 535–8. doi:10.1006/geno.1996.0501. PMID 8884279. 
  2. ^ "Entrez Gene: PRKACA protein kinase, cAMP-dependent, catalytic, alpha". 
  3. ^ Biondi, R M; Cheung P C, Casamayor A, Deak M, Currie R A, Alessi D R (March 2000). "Identification of a pocket in the PDK1 kinase domain that interacts with PIF and the C-terminal residues of PKA". EMBO J. (ENGLAND) 19 (5): 979–88. doi:10.1093/emboj/19.5.979. ISSN 0261-4189. PMC 305637. PMID 10698939. 
  4. ^ Nauert, J Brian; Rigas Johanna D, Lester Linda B (September 2003). "Identification of an IQGAP1/AKAP79 complex in beta-cells". J. Cell. Biochem. (United States) 90 (1): 97–108. doi:10.1002/jcb.10604. ISSN 0730-2312. PMID 12938160. 
  5. ^ Marx, Steven O; Kurokawa Junko, Reiken Steven, Motoike Howard, D'Armiento Jeanine, Marks Andrew R, Kass Robert S (January 2002). "Requirement of a macromolecular signaling complex for beta adrenergic receptor modulation of the KCNQ1-KCNE1 potassium channel". Science (United States) 295 (5554): 496–9. doi:10.1126/science.1066843. PMID 11799244. 
  6. ^ Marx, S O; 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. 

Further reading[edit]

  • Morishima-Kawashima M, Hasegawa M, Takio K, et al. (1995). "Hyperphosphorylation of tau in PHF.". Neurobiol. Aging 16 (3): 365–71; discussion 371–80. doi:10.1016/0197-4580(95)00027-C. PMID 7566346. 
  • Deng X, Kornblau SM, Ruvolo PP, May WS (2003). "Regulation of Bcl2 phosphorylation and potential significance for leukemic cell chemoresistance.". J. Natl. Cancer Inst. Monographs (28): 30–7. PMID 11158204. 
  • Ali A, Hoeflich KP, Woodgett JR (2002). "Glycogen synthase kinase-3: properties, functions, and regulation.". Chem. Rev. 101 (8): 2527–40. doi:10.1021/cr000110o. PMID 11749387. 
  • Holm C (2004). "Molecular mechanisms regulating hormone-sensitive lipase and lipolysis.". Biochem. Soc. Trans. 31 (Pt 6): 1120–4. doi:10.1042/BST0311120. PMID 14641008. 
  • Honeyman, Joshua N, Simon E, Robine N et al. (2014). "Detection of a Recurrent DNAJB1-PRKACA Chimeric Transcript in Fibrolamellar Hepatocellular Carcinoma.". Science 343: 1010–1014. doi:10.1126/science.1249484. PMID 24578576.