PRKACB

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Protein kinase, cAMP-dependent, catalytic, beta
Protein PRKACB PDB 1apm.png
PDB rendering based on 1apm.
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
Symbols PRKACB ; PKACB
External IDs OMIM176892 MGI97594 HomoloGene121718 ChEMBL: 2918 GeneCards: PRKACB Gene
EC number 2.7.11.11
RNA expression pattern
PBB GE PRKACB 202742 s at tn.png
PBB GE PRKACB 202741 at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 5567 18749
Ensembl ENSG00000142875 ENSMUSG00000005034
UniProt P22694 P68181
RefSeq (mRNA) NM_001242857 NM_001164198
RefSeq (protein) NP_001229786 NP_001157670
Location (UCSC) Chr 1:
84.54 – 84.7 Mb
Chr 3:
146.73 – 146.81 Mb
PubMed search [1] [2]

cAMP-dependent protein kinase catalytic subunit beta is an enzyme that in humans is encoded by the PRKACB 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 PKA 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 PKA. Three alternatively spliced transcript variants encoding distinct isoforms have been observed.[1]

Interactions[edit]

PRKACB has been shown to interact with Ryanodine receptor 2[2] and Low affinity nerve growth factor receptor.[3]

References[edit]

  1. ^ a b "Entrez Gene: PRKACB protein kinase, cAMP-dependent, catalytic, beta". 
  2. ^ 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. 
  3. ^ Higuchi, Haruhisa; Yamashita Toshihide; Yoshikawa Hideki; Tohyama Masaya (April 2003). "PKA phosphorylates the p75 receptor and regulates its localization to lipid rafts". EMBO J. (England) 22 (8): 1790–800. doi:10.1093/emboj/cdg177. ISSN 0261-4189. PMC 154469. PMID 12682012. 

Further reading[edit]