PRKACA

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Protein kinase, cAMP-dependent, catalytic, alpha
PDB rendering based on 1apm.
Available structures: 1apm, 1atp, 1bkx, 1bx6, 1cdk, 1cmk, 1ctp, 1fmo, 1j3h, 1jbp, 1jlu, 1l3r, 1q24, 1q61, 1q62, 1q8t, 1q8u, 1q8w, 1rdq, 1re8, 1rej, 1rek, 1smh, 1stc, 1sve, 1svg, 1svh, 1syk, 1szm, 1u7e, 1veb, 1xh4, 1xh5, 1xh6, 1xh7, 1xh8, 1xh9, 1xha, 1ydr, 1yds, 1ydt, 2c1a, 2c1b, 2cpk, 2erz, 2f7e, 2f7x, 2f7z, 2gfc, 2gnf, 2gng, 2gnh, 2gni, 2gnj, 2gnl, 2gu8, 2jds, 2jdt, 2jdv, 2oh0, 2ojf, 2uvx, 2uvy, 2uvz, 2uw0, 2uw3, 2uw4, 2uw5, 2uw6, 2uw7, 2uw8, 2uzt, 2uzu, 2uzv, 2uzw
Identifiers
Symbol(s) PRKACA; MGC102831; MGC48865; PKACA
External IDs OMIM: 601639 MGI: 97592 HomoloGene: 68129
Orthologs
Human Mouse
Entrez 5566 18747


Refseq NM_002730 (mRNA)
NP_002721 (protein)		 NM_008854 (mRNA)
NP_032880 (protein)
Pubmed search [1] [2]

Protein kinase, cAMP-dependent, catalytic, alpha, also known as PRKACA, is a human gene.

cAMP is a signaling molecule important for a variety of cellular functions. cAMP exerts its effects by activating the cAMP-dependent protein kinase (AMPK), which transduces the signal through phosphorylation of different target proteins. The inactive holoenzyme of AMPK 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.[1]

[edit] References

  1. ^ Entrez Gene: PRKACA protein kinase, cAMP-dependent, catalytic, alpha.

[edit] Further reading

  • Morishima-Kawashima M, Hasegawa M, Takio K, et al. (1995). "Hyperphosphorylation of tau in PHF.". Neurobiol. Aging 16 (3): 365-71; discussion 371-80. 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. PMID 11749387. 
  • Holm C (2004). "Molecular mechanisms regulating hormone-sensitive lipase and lipolysis.". Biochem. Soc. Trans. 31 (Pt 6): 1120-4. doi:10.1042/. PMID 14641008. 
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