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

PRKACB
Identifiers
AliasesPRKACB, PKA C-beta, PKACB, protein kinase cAMP-activated catalytic subunit beta, CAFD2
External IDsOMIM: 176892; MGI: 97594; HomoloGene: 121718; GeneCards: PRKACB; OMA:PRKACB - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_001164198
NM_001164199
NM_001164200
NM_011100

RefSeq (protein)

NP_001157670
NP_001157671
NP_001157672
NP_035230

Location (UCSC)Chr 1: 84.08 – 84.24 MbChr 3: 146.44 – 146.52 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

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

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

References

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  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000142875Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000005034Ensembl, 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. ^ a b "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

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