UniProt functional annotation for P00514



	UniProt functional annotation for P00514

UniProt code: P00514.

Organism: Bos taurus (Bovine).

Taxonomy: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae; Bovinae; Bos.

Function: Regulatory subunit of the cAMP-dependent protein kinases involved in cAMP signaling in cells.

Subunit: The inactive holoenzyme is composed of two regulatory chains and two catalytic chains. Activation by cAMP releases the two active catalytic monomers and the regulatory dimer. PRKAR1A also interacts with RFC2; the complex may be involved in cell survival. Interacts with AKAP4. Interacts with RARA; the interaction occurs in the presence of cAMP or FSH and regulates RARA transcriptional activity (By similarity). Interacts with the phosphorylated form of PJA2 (By similarity). Interacts with CBFA2T3 (By similarity). Interacts with PRKX; regulates this cAMP-dependent protein kinase (By similarity). Interacts with smAKAP; this interaction may target PRKAR1A to the plasma membrane (By similarity). Interacts with AICDA (By similarity). {ECO:0000250}.

Subcellular location: Cell membrane {ECO:0000250}.

Tissue specificity: Four types of regulatory chains are found: I-alpha, I-beta, II-alpha, and II-beta. Their expression varies among tissues and is in some cases constitutive and in others inducible.

Ptm: The pseudophosphorylation site binds to the substrate-binding region of the catalytic chain, resulting in the inhibition of its activity. The physiological significance of the in vitro phosphorylation of a proximal serine is unclear.

Similarity: Belongs to the cAMP-dependent kinase regulatory chain family. {ECO:0000305}.

Annotations taken from UniProtKB at the EBI.


Organism:		Bos taurus (Bovine).
Taxonomy:		Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae; Bovinae; Bos.



Function:		Regulatory subunit of the cAMP-dependent protein kinases involved in cAMP signaling in cells.


Subunit:		The inactive holoenzyme is composed of two regulatory chains and two catalytic chains. Activation by cAMP releases the two active catalytic monomers and the regulatory dimer. PRKAR1A also interacts with RFC2; the complex may be involved in cell survival. Interacts with AKAP4. Interacts with RARA; the interaction occurs in the presence of cAMP or FSH and regulates RARA transcriptional activity (By similarity). Interacts with the phosphorylated form of PJA2 (By similarity). Interacts with CBFA2T3 (By similarity). Interacts with PRKX; regulates this cAMP-dependent protein kinase (By similarity). Interacts with smAKAP; this interaction may target PRKAR1A to the plasma membrane (By similarity). Interacts with AICDA (By similarity). {ECO:0000250}.
Subcellular location:		Cell membrane {ECO:0000250}.
Tissue specificity:		Four types of regulatory chains are found: I-alpha, I-beta, II-alpha, and II-beta. Their expression varies among tissues and is in some cases constitutive and in others inducible.
Ptm:		The pseudophosphorylation site binds to the substrate-binding region of the catalytic chain, resulting in the inhibition of its activity. The physiological significance of the in vitro phosphorylation of a proximal serine is unclear.
Similarity:		Belongs to the cAMP-dependent kinase regulatory chain family. {ECO:0000305}.