P00517
Gene name |
PRKACA |
Protein name |
cAMP-dependent protein kinase catalytic subunit alpha |
Names |
PKA C-alpha |
Species |
Bos taurus (Bovine) |
KEGG Pathway |
bta:282322 |
EC number |
2.7.11.11: Protein-serine/threonine kinases |
Protein Class |
|

Descriptions
The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.
Autoinhibitory domains (AIDs)
Target domain |
|
Relief mechanism |
|
Assay |
cis-regPred |
Accessory elements
184-204 (Activation loop from InterPro)
Target domain |
44-298 (Protein kinase domain) |
Relief mechanism |
|
Assay |
|
Autoinhibited structure

Activated structure

91 structures for P00517
Entry ID | Method | Resolution | Chain | Position | Source |
---|---|---|---|---|---|
1Q24 | X-ray | 260 A | A | 2-351 | PDB |
1Q61 | X-ray | 210 A | A | 2-351 | PDB |
1Q62 | X-ray | 230 A | A | 2-351 | PDB |
1Q8T | X-ray | 200 A | A | 2-351 | PDB |
1Q8U | X-ray | 190 A | A | 2-351 | PDB |
1Q8W | X-ray | 220 A | A | 2-351 | PDB |
1SMH | X-ray | 204 A | A | 2-351 | PDB |
1STC | X-ray | 230 A | E | 2-351 | PDB |
1SVE | X-ray | 249 A | A | 2-351 | PDB |
1SVG | X-ray | 202 A | A | 2-351 | PDB |
1SVH | X-ray | 230 A | A | 2-351 | PDB |
1SZM | X-ray | 250 A | A/B | 2-351 | PDB |
1VEB | X-ray | 289 A | A | 2-351 | PDB |
1XH4 | X-ray | 245 A | A | 2-351 | PDB |
1XH5 | X-ray | 205 A | A | 2-351 | PDB |
1XH6 | X-ray | 190 A | A | 2-351 | PDB |
1XH7 | X-ray | 247 A | A | 2-351 | PDB |
1XH8 | X-ray | 160 A | A | 2-351 | PDB |
1XH9 | X-ray | 164 A | A | 2-351 | PDB |
1XHA | X-ray | 246 A | A | 2-351 | PDB |
1YDR | X-ray | 220 A | E | 2-351 | PDB |
1YDS | X-ray | 220 A | E | 2-351 | PDB |
1YDT | X-ray | 230 A | E | 2-351 | PDB |
2C1A | X-ray | 195 A | A | 2-351 | PDB |
2C1B | X-ray | 200 A | A | 2-351 | PDB |
2F7E | X-ray | 200 A | E | 1-351 | PDB |
2F7X | X-ray | 190 A | E | 1-351 | PDB |
2F7Z | X-ray | 300 A | E | 1-351 | PDB |
2GFC | X-ray | 187 A | A | 2-351 | PDB |
2GNF | X-ray | 228 A | A | 2-351 | PDB |
2GNG | X-ray | 187 A | A | 2-351 | PDB |
2GNH | X-ray | 205 A | A | 2-351 | PDB |
2GNI | X-ray | 227 A | A | 2-351 | PDB |
2GNJ | X-ray | 228 A | A | 2-351 | PDB |
2GNL | X-ray | 260 A | A | 2-351 | PDB |
2JDS | X-ray | 200 A | A | 2-351 | PDB |
2JDT | X-ray | 215 A | A | 2-351 | PDB |
2JDV | X-ray | 208 A | A | 2-351 | PDB |
2OH0 | X-ray | 220 A | E | 1-351 | PDB |
2OJF | X-ray | 210 A | E | 1-351 | PDB |
2UVX | X-ray | 200 A | A | 2-351 | PDB |
2UVY | X-ray | 195 A | A | 2-351 | PDB |
2UVZ | X-ray | 194 A | A | 2-351 | PDB |
2UW0 | X-ray | 200 A | A | 2-351 | PDB |
2UW3 | X-ray | 219 A | A | 2-351 | PDB |
2UW4 | X-ray | 200 A | A | 2-351 | PDB |
2UW5 | X-ray | 214 A | A | 2-351 | PDB |
2UW6 | X-ray | 223 A | A | 2-351 | PDB |
2UW7 | X-ray | 210 A | A | 2-351 | PDB |
2UW8 | X-ray | 200 A | A | 2-351 | PDB |
2UZT | X-ray | 210 A | A | 16-351 | PDB |
2UZU | X-ray | 240 A | E | 16-351 | PDB |
2UZV | X-ray | 250 A | A | 16-351 | PDB |
2UZW | X-ray | 220 A | E | 16-351 | PDB |
2VNW | X-ray | 209 A | A | 1-351 | PDB |
2VNY | X-ray | 196 A | A | 1-351 | PDB |
2VO0 | X-ray | 194 A | A | 1-351 | PDB |
2VO3 | X-ray | 198 A | A | 1-351 | PDB |
2VO6 | X-ray | 197 A | A | 1-351 | PDB |
2VO7 | X-ray | 198 A | A | 1-351 | PDB |
3AG9 | X-ray | 200 A | A/B | 1-351 | PDB |
3BWJ | X-ray | 230 A | A | 2-351 | PDB |
3DND | X-ray | 226 A | A | 2-351 | PDB |
3DNE | X-ray | 200 A | A | 2-351 | PDB |
3E8C | X-ray | 220 A | A/B/C/D/E/F | 2-351 | PDB |
3E8E | X-ray | 200 A | A/B/E/I/L/P | 2-351 | PDB |
3KKV | X-ray | 180 A | A | 2-351 | PDB |
3ZO1 | X-ray | 200 A | A | 1-351 | PDB |
3ZO2 | X-ray | 198 A | A | 1-351 | PDB |
3ZO3 | X-ray | 210 A | A | 1-351 | PDB |
3ZO4 | X-ray | 165 A | A | 1-351 | PDB |
4AXA | X-ray | 190 A | A | 1-351 | PDB |
4C33 | X-ray | 170 A | A | 1-351 | PDB |
4C34 | X-ray | 178 A | A | 1-351 | PDB |
4C35 | X-ray | 219 A | A | 1-351 | PDB |
4C36 | X-ray | 198 A | A | 1-351 | PDB |
4C37 | X-ray | 170 A | A | 1-351 | PDB |
4C38 | X-ray | 158 A | A | 1-351 | PDB |
4IE9 | X-ray | 192 A | A | 1-351 | PDB |
4IJ9 | X-ray | 255 A | A | 2-351 | PDB |
4YXR | X-ray | 200 A | A | 2-351 | PDB |
4YXS | X-ray | 211 A | A | 2-351 | PDB |
4Z83 | X-ray | 180 A | E | 2-351 | PDB |
4Z84 | X-ray | 155 A | A | 1-351 | PDB |
5VHB | X-ray | 161 A | A | 1-351 | PDB |
5VI9 | X-ray | 195 A | A | 1-351 | PDB |
5VIB | X-ray | 237 A | A | 1-351 | PDB |
6E99 | X-ray | 188 A | A | 1-351 | PDB |
6E9L | X-ray | 280 A | A | 1-351 | PDB |
8SF8 | X-ray | 170 A | A | 1-351 | PDB |
AF-P00517-F1 | Predicted | AlphaFoldDB |
65 variants for P00517
Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
---|---|---|---|---|---|
rs437880744 | 16 | V>A | No | EVA | |
rs474365808 | 19 | F>C | No | EVA | |
rs456161929 | 19 | F>I | No | EVA | |
rs453651433 | 24 | K>N | No | EVA | |
rs472079162 | 30 | K>T | No | EVA | |
rs440619596 | 32 | E>D | No | EVA | |
rs459072430 | 34 | P>R | No | EVA | |
rs477787135 | 36 | Q>R | No | EVA | |
rs476556558 | 39 | A>P | No | EVA | |
rs443640113 | 40 | H>P | No | EVA | |
rs443640113 | 40 | H>R | No | EVA | |
rs480185575 | 43 | Q>H | No | EVA | |
rs461785768 | 43 | Q>K | No | EVA | |
rs447518825 | 45 | E>G | No | EVA | |
rs478132306 | 49 | T>P | No | EVA | |
rs444833757 | 50 | L>R | No | EVA | |
rs469797547 | 54 | S>P | No | EVA | |
rs481920938 | 55 | F>C | No | EVA | |
rs448961914 | 55 | F>L | No | EVA | |
rs468789039 | 57 | R>G | No | EVA | |
rs435752071 | 58 | V>G | No | EVA | |
rs454290690 | 60 | L>R | No | EVA | |
rs135880103 | 64 | M>R | No | EVA | |
rs433461975 | 65 | E>D | No | EVA | |
rs133097611 | 66 | T>P | No | EVA | |
rs443708200 | 70 | Y>* | No | EVA | |
rs455645476 | 74 | I>S | No | EVA | |
rs441026838 | 75 | L>F | No | EVA | |
rs459540400 | 75 | L>P | No | EVA | |
rs438640633 | 78 | Q>K | No | EVA | |
rs876116479 | 80 | V>G | No | EVA | |
rs876556665 | 89 | T>P | No | EVA | |
rs876248256 | 97 | Q>H | No | EVA | |
rs876652318 | 97 | Q>R | No | EVA | |
rs876017790 | 98 | A>E | No | EVA | |
rs876017790 | 98 | A>G | No | EVA | |
rs477996790 | 132 | H>R | No | EVA | |
rs463386636 | 142 | P>R | No | EVA | |
rs442366602 | 169 | K>T | No | EVA | |
rs463906637 | 183 | V>G | No | EVA | |
rs482537925 | 191 | R>C | No | EVA | |
rs449270596 | 196 | T>S | No | EVA | |
rs521811997 | 199 | L>S | No | EVA | |
rs479991410 | 202 | T>N | No | EVA | |
rs465189161 | 207 | A>D | No | EVA | |
rs446832560 | 223 | W>C | No | EVA | |
rs465477331 | 225 | L>Q | No | EVA | |
rs477454735 | 227 | V>G | No | EVA | |
rs450767996 | 232 | M>R | No | EVA | |
rs469144504 | 241 | A>S | No | EVA | |
rs436328147 | 242 | D>A | No | EVA | |
rs448263515 | 243 | Q>P | No | EVA | |
rs480269950 | 261 | H>R | No | EVA | |
rs447164635 | 263 | S>R | No | EVA | |
rs459451891 | 269 | L>M | No | EVA | |
rs477851364 | 276 | V>G | No | EVA | |
rs462178229 | 280 | K>N | No | EVA | |
rs464749729 | 302 | D>A | No | EVA | |
rs438316858 | 307 | Y>* | No | EVA | |
rs468819393 | 309 | R>G | No | EVA | |
rs435590673 | 310 | K>E | No | EVA | |
rs453937304 | 310 | K>N | No | EVA | |
rs453248079 | 311 | V>G | No | EVA | |
rs471656339 | 314 | P>A | No | EVA | |
rs438423959 | 323 | G>V | No | EVA |
No associated diseases with P00517
4 regional properties for P00517
Functions
Description | ||
---|---|---|
EC Number | 2.7.11.11 | Protein-serine/threonine kinases |
Subcellular Localization |
|
|
PANTHER Family | ||
PANTHER Subfamily | ||
PANTHER Protein Class | ||
PANTHER Pathway Category | No pathway information available |
14 GO annotations of cellular component
Name | Definition |
---|---|
acrosomal vesicle | A structure in the head of a spermatozoon that contains acid hydrolases, and is concerned with the breakdown of the outer membrane of the ovum during fertilization. It lies just beneath the plasma membrane and is derived from the lysosome. |
axoneme | The bundle of microtubules and associated proteins that forms the core of cilia (also called flagella) in eukaryotic cells and is responsible for their movements. |
cAMP-dependent protein kinase complex | An enzyme complex, composed of regulatory and catalytic subunits, that catalyzes protein phosphorylation. Inactive forms of the enzyme have two regulatory chains and two catalytic chains; activation by cAMP produces two active catalytic monomers and a regulatory dimer. |
centrosome | A structure comprised of a core structure (in most organisms, a pair of centrioles) and peripheral material from which a microtubule-based structure, such as a spindle apparatus, is organized. Centrosomes occur close to the nucleus during interphase in many eukaryotic cells, though in animal cells it changes continually during the cell-division cycle. |
ciliary base | Area of the cilium (also called flagellum) where the basal body and the axoneme are anchored to the plasma membrane. The ciliary base encompasses the distal part of the basal body, transition fibers and transition zone and is structurally and functionally very distinct from the rest of the cilium. In this area proteins are sorted and filtered before entering the cilium, and many ciliary proteins localize specifically to this area. |
cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
dendritic spine | A small, membranous protrusion from a dendrite that forms a postsynaptic compartment, typically receiving input from a single presynapse. They function as partially isolated biochemical and an electrical compartments. Spine morphology is variable:they can be thin, stubby, mushroom, or branched, with a continuum of intermediate morphologies. They typically terminate in a bulb shape, linked to the dendritic shaft by a restriction. Spine remodeling is though to be involved in synaptic plasticity. |
mitochondrion | A semiautonomous, self replicating organelle that occurs in varying numbers, shapes, and sizes in the cytoplasm of virtually all eukaryotic cells. It is notably the site of tissue respiration. |
neuromuscular junction | The junction between the axon of a motor neuron and a muscle fiber. In response to the arrival of action potentials, the presynaptic button releases molecules of neurotransmitters into the synaptic cleft. These diffuse across the cleft and transmit the signal to the postsynaptic membrane of the muscle fiber, leading to a change in post-synaptic potential. |
nuclear speck | A discrete extra-nucleolar subnuclear domain, 20-50 in number, in which splicing factors are seen to be localized by immunofluorescence microscopy. |
nucleus | A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent. |
perinuclear region of cytoplasm | Cytoplasm situated near, or occurring around, the nucleus. |
plasma membrane raft | A membrane raft that is part of the plasma membrane. |
sperm flagellum | A microtubule-based flagellum (or cilium) that is part of a sperm, a mature male germ cell that develops from a spermatid. |
13 GO annotations of molecular function
Name | Definition |
---|---|
AMP-activated protein kinase activity | Catalysis of the reaction: ATP + a protein = ADP + a phosphoprotein. This reaction requires the presence of AMP. |
ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
cAMP-dependent protein kinase activity | cAMP-dependent catalysis of the reaction: ATP + a protein = ADP + a phosphoprotein. |
magnesium ion binding | Binding to a magnesium (Mg) ion. |
manganese ion binding | Binding to a manganese ion (Mn). |
protein domain specific binding | Binding to a specific domain of a protein. |
protein kinase A regulatory subunit binding | Binding to one or both of the regulatory subunits of protein kinase A. |
protein kinase activity | Catalysis of the phosphorylation of an amino acid residue in a protein, usually according to the reaction: a protein + ATP = a phosphoprotein + ADP. |
protein kinase binding | Binding to a protein kinase, any enzyme that catalyzes the transfer of a phosphate group, usually from ATP, to a protein substrate. |
protein serine kinase activity | Catalysis of the reactions: ATP + protein serine = ADP + protein serine phosphate. |
protein serine/threonine kinase activity | Catalysis of the reactions: ATP + protein serine = ADP + protein serine phosphate, and ATP + protein threonine = ADP + protein threonine phosphate. |
protein serine/threonine/tyrosine kinase activity | Catalysis of the reactions: ATP + a protein serine = ADP + protein serine phosphate; ATP + a protein threonine = ADP + protein threonine phosphate; and ATP + a protein tyrosine = ADP + protein tyrosine phosphate. |
ubiquitin protein ligase binding | Binding to a ubiquitin protein ligase enzyme, any of the E3 proteins. |
23 GO annotations of biological process
Name | Definition |
---|---|
cellular response to cold | Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a cold stimulus, a temperature stimulus below the optimal temperature for that organism. |
cellular response to glucose stimulus | Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a glucose stimulus. |
cellular response to heat | Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a heat stimulus, a temperature stimulus above the optimal temperature for that organism. |
cellular response to parathyroid hormone stimulus | Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a parathyroid hormone stimulus. |
mesoderm formation | The process that gives rise to the mesoderm. This process pertains to the initial formation of the structure from unspecified parts. |
modulation of chemical synaptic transmission | Any process that modulates the frequency or amplitude of synaptic transmission, the process of communication from a neuron to a target (neuron, muscle, or secretory cell) across a synapse. Amplitude, in this case, refers to the change in postsynaptic membrane potential due to a single instance of synaptic transmission. |
mRNA processing | Any process involved in the conversion of a primary mRNA transcript into one or more mature mRNA(s) prior to translation into polypeptide. |
negative regulation of smoothened signaling pathway involved in dorsal/ventral neural tube patterning | Any process that stops, prevents or reduces the frequency, rate or extent of smoothened signaling pathway involved in dorsal/ventral neural tube patterning. |
neural tube closure | The last step in the formation of the neural tube, where the paired neural folds are brought together and fuse at the dorsal midline. |
peptidyl-serine phosphorylation | The phosphorylation of peptidyl-serine to form peptidyl-O-phospho-L-serine. |
peptidyl-threonine phosphorylation | The phosphorylation of peptidyl-threonine to form peptidyl-O-phospho-L-threonine. |
positive regulation of protein export from nucleus | Any process that activates or increases the frequency, rate or extent of directed movement of proteins from the nucleus into the cytoplasm. |
protein autophosphorylation | The phosphorylation by a protein of one or more of its own amino acid residues (cis-autophosphorylation), or residues on an identical protein (trans-autophosphorylation). |
protein export from nucleus | The directed movement of a protein from the nucleus into the cytoplasm. |
protein kinase A signaling | A series of reactions, mediated by the intracellular serine/threonine kinase protein kinase A, which occurs as a result of a single trigger reaction or compound. |
protein localization to lipid droplet | A process in which a protein is transported to, or maintained in, a location on or within a lipid droplet. |
protein phosphorylation | The process of introducing a phosphate group on to a protein. |
regulation of bicellular tight junction assembly | Any process that modulates the frequency, rate or extent of tight junction assembly. |
regulation of cell cycle | Any process that modulates the rate or extent of progression through the cell cycle. |
regulation of osteoblast differentiation | Any process that modulates the frequency, rate or extent of osteoblast differentiation. |
regulation of proteasomal protein catabolic process | Any process that modulates the rate, frequency, or extent of the chemical reactions and pathways resulting in the breakdown of a protein or peptide by hydrolysis of its peptide bonds that is mediated by the proteasome. |
regulation of protein processing | Any process that modulates the frequency, rate or extent of protein processing, a protein maturation process achieved by the cleavage of a peptide bond or bonds within a protein. |
sperm capacitation | A process required for sperm to reach fertilization competence. Sperm undergo an incompletely understood series of morphological and molecular maturational processes, termed capacitation, involving, among other processes, protein tyrosine phosphorylation and increased intracellular calcium. |
11 homologous proteins in AiPD
UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
---|---|---|---|---|
P00516 | PRKG1 | cGMP-dependent protein kinase 1 | Bos taurus (Bovine) | SS |
Q8MJ44 | PRKACA | cAMP-dependent protein kinase catalytic subunit alpha | Canis lupus familiaris (Dog) (Canis familiaris) | PR |
Q03043 | for | cGMP-dependent protein kinase, isozyme 2 forms cD4/T1/T3A/T3B | Drosophila melanogaster (Fruit fly) | SS |
P16911 | Pka-C2 | cAMP-dependent protein kinase catalytic subunit 2 | Drosophila melanogaster (Fruit fly) | PR |
P17612 | PRKACA | cAMP-dependent protein kinase catalytic subunit alpha | Homo sapiens (Human) | PR |
Q922R0 | Prkx | cAMP-dependent protein kinase catalytic subunit PRKX | Mus musculus (Mouse) | PR |
P05132 | Prkaca | cAMP-dependent protein kinase catalytic subunit alpha | Mus musculus (Mouse) | PR |
P36887 | PRKACA | cAMP-dependent protein kinase catalytic subunit alpha | Sus scrofa (Pig) | PR |
O62846 | PRKACG | cAMP-dependent protein kinase catalytic subunit gamma | Macaca mulatta (Rhesus macaque) | PR |
Q7JP68 | F47F2.1 | cAMP-dependent protein kinase, catalytic subunit-like | Caenorhabditis elegans | PR |
P21137 | kin-1 | cAMP-dependent protein kinase catalytic subunit | Caenorhabditis elegans | PR |
10 | 20 | 30 | 40 | 50 | 60 |
MGNAAAAKKG | SEQESVKEFL | AKAKEDFLKK | WENPAQNTAH | LDQFERIKTL | GTGSFGRVML |
70 | 80 | 90 | 100 | 110 | 120 |
VKHMETGNHY | AMKILDKQKV | VKLKQIEHTL | NEKRILQAVN | FPFLVKLEFS | FKDNSNLYMV |
130 | 140 | 150 | 160 | 170 | 180 |
MEYVPGGEMF | SHLRRIGRFS | EPHARFYAAQ | IVLTFEYLHS | LDLIYRDLKP | ENLLIDQQGY |
190 | 200 | 210 | 220 | 230 | 240 |
IQVTDFGFAK | RVKGRTWTLC | GTPEYLAPEI | ILSKGYNKAV | DWWALGVLIY | EMAAGYPPFF |
250 | 260 | 270 | 280 | 290 | 300 |
ADQPIQIYEK | IVSGKVRFPS | HFSSDLKDLL | RNLLQVDLTK | RFGNLKNGVN | DIKNHKWFAT |
310 | 320 | 330 | 340 | 350 | |
TDWIAIYQRK | VEAPFIPKFK | GPGDTSNFDD | YEEEEIRVSI | NEKCGKEFSE | F |