PRKACB

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Protein kinase, cAMP-dependent, catalytic, beta
File:PBB Protein PRKACB image.jpg
PDB rendering based on 1apm.
Available structures
PDB Ortholog search: Template:Homologene2PDBe PDBe, Template:Homologene2uniprot RCSB
Identifiers
Symbols PRKACB ; DKFZp781I2452; MGC41879; MGC9320; PKACB
External IDs Template:OMIM5 Template:MGI HomoloGene55518
RNA expression pattern
File:PBB GE PRKACB 202742 s at tn.png
File:PBB GE PRKACB 202741 at tn.png
More reference expression data
Orthologs
Template:GNF Ortholog box
Species Human Mouse
Entrez n/a n/a
Ensembl n/a n/a
UniProt n/a n/a
RefSeq (mRNA) n/a n/a
RefSeq (protein) n/a n/a
Location (UCSC) n/a n/a
PubMed search n/a n/a

Protein kinase, cAMP-dependent, catalytic, beta, also known as PRKACB, is a human gene.[1]

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. Three alternatively spliced transcript variants encoding distinct isoforms have been observed.[1]

References

  1. 1.0 1.1 "Entrez Gene: PRKACB protein kinase, cAMP-dependent, catalytic, beta".

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. PMID 1551670.
  • 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. 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. 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. 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. 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. 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. 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. 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. 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. 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. PMID 9730685.
  • Hartley JL, Temple GF, Brasch MA (2001). "DNA cloning using in vitro site-specific recombination". Genome Res. 10 (11): 1788–95. 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. doi:10.1073/pnas.98.4.1930. 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. 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. doi:10.1073/pnas.242603899. 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. 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. PMID 12798691.

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