P27791
uniprot
P27791
canonical
activity_regulation
ACTIVITY REGULATION: Allosterically activated by various compounds, including ATP. Activated by cAMP; the nucleotide acts as a dynamic and allosteric activator by coupling the two lobes of apo PKA, enhancing the enzyme dynamics synchronously and priming it for catalysis.
uniprot
proteins
amino_acid_sequence
MGNAAAAKKGSEQESVKEFLAKAKEDFLKKWEDPSQNTAQLDHFDRIKTLGTGSFGRVMLVKHKESGNHYAMKILDKQKVVKLKQIEHTLNEKRILQAVNFPFLVKLEFSFKDNSNLYMVMEYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDQQGYIQVTDFGFAKRVKGRTWTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFSSDLKDLLRNLLQVDLTKRFGNLKNGVNDIKNHKWFATTDWIAIYQRKVEAPFIPKFKGPGDTSNFDDYEEEEIRVSINEKCGKEFTEF
uniprot
proteins
ec_number
2.7.11.11
uniprot
proteins
function
FUNCTION: Phosphorylates a large number of substrates in the cytoplasm and the nucleus. Phosphorylates CDC25B, ABL1, NFKB1, CLDN3, histone H1.4 (H1-4), PSMC5/RPT6, PJA2, RYR2, RORA, SLC6A6, SOX9, UHRF1 and VASP. Regulates the abundance of compartmentalized pools of its regulatory subunits through phosphorylation of PJA2 which binds and ubiquitinates these subunits, leading to their subsequent proteolysis. RORA is activated by phosphorylation. Required for glucose-mediated adipogenic differentiation increase and osteogenic differentiation inhibition from osteoblasts (By similarity). Involved in chondrogenesis by mediating phosphorylation of SOX9 (By similarity). Involved in the regulation of platelets in response to thrombin and collagen; maintains circulating platelets in a resting state by phosphorylating proteins in numerous platelet inhibitory pathways when in complex with NF-kappa-B (NFKB1 and NFKB2) and I-kappa-B-alpha (NFKBIA), but thrombin and collagen disrupt these complexes and free active PRKACA stimulates platelets and leads to platelet aggregation by phosphorylating VASP. Prevents the antiproliferative and anti-invasive effects of alpha-difluoromethylornithine in breast cancer cells when activated. RYR2 channel activity is potentiated by phosphorylation in presence of luminal Ca(2+), leading to reduced amplitude and increased frequency of store overload-induced Ca(2+) release (SOICR) characterized by an increased rate of Ca(2+) release and propagation velocity of spontaneous Ca(2+) waves, despite reduced wave amplitude and resting cytosolic Ca(2+). PSMC5/RPT6 activation by phosphorylation stimulates proteasome. Negatively regulates tight junctions (TJs) in ovarian cancer cells via CLDN3 phosphorylation. NFKB1 phosphorylation promotes NF-kappa-B p50-p50 DNA binding (By similarity). Acts as a key inhibitor of smoothened signaling pathway by mediating phosphorylation of GLI (GLI1, GLI2 and GLI3) transcription factors in absence of hedgehog (DHH, IHH or SHH) morphogens: GLI phosphorylation promotes their processing and prevents transcriptional activation of smoothened target genes (By similarity). GLI transcription factor phosphorylation is inhibited by interaction of PRKACA with SMO which sequesters PRKACA at the cell membrane (By similarity). Also inhibits the smoothened signaling pathway in embryonic development by catalyzing phosphorylation of OFD1 in ciliogenesis (By similarity). Prevents meiosis resumption in prophase-arrested oocytes via CDC25B inactivation by phosphorylation (By similarity). May also regulate rapid eye movement (REM) sleep in the pedunculopontine tegmental (PPT) (PubMed:20844122). Phosphorylates APOBEC3G and AICDA. Phosphorylates HSF1; this phosphorylation promotes HSF1 nuclear localization and transcriptional activity upon heat shock. Acts as a negative regulator of mTORC1 by mediating phosphorylation of RPTOR. Phosphorylates AKAP19 (By similarity). {ECO:0000250|UniProtKB:P05132, ECO:0000250|UniProtKB:P17612, ECO:0000269|PubMed:20844122}.
uniprot
proteins
mass_dalton
40620
uniprot
proteins
post_translational_modification
PTM: Asn-3 is deaminated to Asp in more than 25% of the proteins, giving rise to 2 major isoelectric variants, called CB and CA respectively (0.4 pH unit change). Deamidation proceeds via the so-called beta-aspartyl shift mechanism and yields either 'D-Asp-2' (major) or 'D-isoAsp-2' (minor), in addition to L-isomers. Deamidation occurs after the addition of myristate. The Asn-3 form reaches a significantly larger nuclear/cytoplasmic ratio than the 'Asp-2' form. {ECO:0000269|PubMed:9521123}.; PTM: Autophosphorylated. Phosphorylation is enhanced by vitamin K(2). Phosphorylated on threonine and serine residues. Phosphorylation on Thr-198 is required for full activity (By similarity). Phosphorylated at Tyr-331 by activated receptor tyrosine kinases EGFR and PDGFR; this increases catalytic efficiency (By similarity). {ECO:0000250|UniProtKB:P05132, ECO:0000250|UniProtKB:P17612}.; PTM: When myristoylated, Ser-11 is autophosphorylated probably in conjunction with deamidation of Asn-3. {ECO:0000250|UniProtKB:P05132}.
uniprot
proteins
protein_family
AGC Ser/Thr protein kinase family
uniprot
proteins
protein_family
Protein kinase superfamily
uniprot
proteins
protein_family
cAMP subfamily
uniprot
proteins
pubmed
14514679
uniprot
proteins
pubmed
1711374
uniprot
proteins
pubmed
20844122
uniprot
proteins
pubmed
22673903
uniprot
proteins
pubmed
23419316
uniprot
proteins
pubmed
9521123
uniprot
proteins
sequence_length
351
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P17612}. Cell membrane {ECO:0000250|UniProtKB:P17612}. Membrane {ECO:0000250|UniProtKB:P17612}; Lipid-anchor {ECO:0000250|UniProtKB:P17612}. Nucleus {ECO:0000250|UniProtKB:P17612}. Mitochondrion {ECO:0000250|UniProtKB:P05132}. Note=Translocates into the nucleus (monomeric catalytic subunit). The inactive holoenzyme is found in the cytoplasm. Distributed throughout the cytoplasm in meiotically incompetent oocytes. Associated to mitochondrion as meiotic competence is acquired. Aggregates around the germinal vesicles (GV) at the immature GV stage oocytes (By similarity). Colocalizes with HSF1 in nuclear stress bodies (nSBs) upon heat shock (By similarity). Recruited to the cell membrane through interaction with SMO (By similarity). {ECO:0000250|UniProtKB:P05132, ECO:0000250|UniProtKB:P17612}.; SUBCELLULAR LOCATION: [Isoform 2]: Cell projection, cilium, flagellum {ECO:0000250|UniProtKB:P05132}. Cytoplasmic vesicle, secretory vesicle, acrosome {ECO:0000250|UniProtKB:P05132}. Note=Expressed in the midpiece region of the sperm flagellum. Expressed in the midpiece region of the sperm flagellum. Colocalizes with MROH2B and TCP11 on the acrosome and tail regions in round spermatids and spermatozoa regardless of the capacitation status of the sperm. {ECO:0000250, ECO:0000250|UniProtKB:P05132}.
uniprot
proteins