P05128
Gene name |
PRKCG |
Protein name |
Protein kinase C gamma type |
Names |
PKC-gamma , EC 2.7.11.13 |
Species |
Bos taurus (Bovine) |
KEGG Pathway |
bta:282002 |
EC number |
2.7.11.-: Protein-serine/threonine kinases |
Protein Class |
|

Descriptions
Autoinhibitory domains (AIDs)
Target domain |
338-585 (Protein kinase domain) |
Relief mechanism |
Ligand binding |
Assay |
|
Target domain |
338-585 (Protein kinase domain) |
Relief mechanism |
Ligand binding |
Assay |
|
Target domain |
338-585 (Protein kinase domain) |
Relief mechanism |
Ligand binding |
Assay |
|
Accessory elements
No accessory elements
References
- Yeon JH et al. (2016) "Systems-wide Identification of cis-Regulatory Elements in Proteins", Cell systems, 2, 89-100
- Slater SJ et al. (2002) "Regulation of PKC alpha activity by C1-C2 domain interactions", The Journal of biological chemistry, 277, 15277-85
- Jones AC et al. (2020) "Hypothesis: Unifying model of domain architecture for conventional and novel protein kinase C isozymes", IUBMB life, 72, 2584-2590
- Kirwan AF et al. (2003) "Inhibition of protein kinase C catalytic activity by additional regions within the human protein kinase Calpha-regulatory domain lying outside of the pseudosubstrate sequence", The Biochemical journal, 373, 571-81
- Steinberg SF (2008) "Structural basis of protein kinase C isoform function", Physiological reviews, 88, 1341-78
- Sommese RF et al. (2017) "The Role of Regulatory Domains in Maintaining Autoinhibition in the Multidomain Kinase PKCα", The Journal of biological chemistry, 292, 2873-2880
- Pears CJ et al. (1990) "Mutagenesis of the pseudosubstrate site of protein kinase C leads to activation", European journal of biochemistry, 194, 89-94
- Smith MK et al. (1990) "Specificities of autoinhibitory domain peptides for four protein kinases. Implications for intact cell studies of protein kinase function", The Journal of biological chemistry, 265, 1837-40
- Huang X et al. (2003) "Crystal structure of an inactive Akt2 kinase domain", Structure (London, England : 1993), 11, 21-30
- Truebestein L et al. (2021) "Structure of autoinhibited Akt1 reveals mechanism of PIP(3)-mediated activation", Proceedings of the National Academy of Sciences of the United States of America, 118,
- Lučić I et al. (2018) "Conformational sampling of membranes by Akt controls its activation and inactivation", Proceedings of the National Academy of Sciences of the United States of America, 115, E3940-E3949
- Wagner J et al. (2009) "Discovery of 3-(1H-indol-3-yl)-4-[2-(4-methylpiperazin-1-yl)quinazolin-4-yl]pyrrole-2,5-dione (AEB071), a potent and selective inhibitor of protein kinase C isotypes", Journal of medicinal chemistry, 52, 6193-6
Autoinhibited structure

Activated structure

1 structures for P05128
Entry ID | Method | Resolution | Chain | Position | Source |
---|---|---|---|---|---|
AF-P05128-F1 | Predicted | AlphaFoldDB |
No variants for P05128
Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
---|---|---|---|---|---|
No variants for P05128 |
No associated diseases with P05128
12 regional properties for P05128
Type | Name | Position | InterPro Accession |
---|---|---|---|
domain | C2 domain | 142 - 262 | IPR000008 |
domain | Protein kinase domain | 336 - 599 | IPR000719 |
domain | AGC-kinase, C-terminal | 600 - 670 | IPR000961 |
domain | Protein kinase C-like, phorbol ester/diacylglycerol-binding domain | 20 - 71 | IPR002219-1 |
domain | Protein kinase C-like, phorbol ester/diacylglycerol-binding domain | 85 - 137 | IPR002219-2 |
active_site | Serine/threonine-protein kinase, active site | 461 - 473 | IPR008271 |
binding_site | Protein kinase, ATP binding site | 342 - 365 | IPR017441 |
domain | Protein kinase, C-terminal | 627 - 660 | IPR017892 |
domain | Diacylglycerol/phorbol-ester binding | 18 - 32 | IPR020454-1 |
domain | Diacylglycerol/phorbol-ester binding | 34 - 43 | IPR020454-2 |
domain | Diacylglycerol/phorbol-ester binding | 47 - 58 | IPR020454-3 |
domain | Diacylglycerol/phorbol-ester binding | 124 - 136 | IPR020454-4 |
Functions
Description | ||
---|---|---|
EC Number | 2.7.11.- | Protein-serine/threonine kinases |
Subcellular Localization |
|
|
PANTHER Family | ||
PANTHER Subfamily | ||
PANTHER Protein Class | ||
PANTHER Pathway Category | No pathway information available |
5 GO annotations of cellular component
Name | Definition |
---|---|
cytosol | The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. |
dendrite | A neuron projection that has a short, tapering, morphology. Dendrites receive and integrate signals from other neurons or from sensory stimuli, and conduct nerve impulses towards the axon or the cell body. In most neurons, the impulse is conveyed from dendrites to axon via the cell body, but in some types of unipolar neuron, the impulse does not travel via the cell body. |
perinuclear region of cytoplasm | Cytoplasm situated near, or occurring around, the nucleus. |
plasma membrane | The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins. |
synapse | The junction between an axon of one neuron and a dendrite of another neuron, a muscle fiber or a glial cell. As the axon approaches the synapse it enlarges into a specialized structure, the presynaptic terminal bouton, which contains mitochondria and synaptic vesicles. At the tip of the terminal bouton is the presynaptic membrane; facing it, and separated from it by a minute cleft (the synaptic cleft) is a specialized area of membrane on the receiving cell, known as the postsynaptic membrane. In response to the arrival of nerve impulses, the presynaptic terminal bouton secretes molecules of neurotransmitters into the synaptic cleft. These diffuse across the cleft and transmit the signal to the postsynaptic membrane. |
5 GO annotations of molecular function
Name | Definition |
---|---|
ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
diacylglycerol-dependent serine/threonine kinase activity | Catalysis of the reaction |
protein serine kinase activity | Catalysis of the reactions |
protein serine/threonine kinase activity | Catalysis of the reactions |
zinc ion binding | Binding to a zinc ion (Zn). |
10 GO annotations of biological process
Name | Definition |
---|---|
intracellular signal transduction | The process in which a signal is passed on to downstream components within the cell, which become activated themselves to further propagate the signal and finally trigger a change in the function or state of the cell. |
negative regulation of neuron apoptotic process | Any process that stops, prevents, or reduces the frequency, rate or extent of cell death by apoptotic process in neurons. |
negative regulation of proteasomal protein catabolic process | Any process that stops, prevents or reduces the frequency, rate or extent of proteasomal protein catabolic process. |
negative regulation of protein ubiquitination | Any process that stops, prevents, or reduces the frequency, rate or extent of the addition of ubiquitin groups to a protein. |
phosphorylation | The process of introducing a phosphate group into a molecule, usually with the formation of a phosphoric ester, a phosphoric anhydride or a phosphoric amide. |
regulation of circadian rhythm | Any process that modulates the frequency, rate or extent of a circadian rhythm. A circadian rhythm is a biological process in an organism that recurs with a regularity of approximately 24 hours. |
regulation of response to food | Any process that modulates the frequency, rate or extent of a response to a food stimulus. |
response to morphine | Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a morphine stimulus. Morphine is an opioid alkaloid, isolated from opium, with a complex ring structure. |
response to pain | Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a pain stimulus. Pain stimuli cause activation of nociceptors, peripheral receptors for pain, include receptors which are sensitive to painful mechanical stimuli, extreme heat or cold, and chemical stimuli. |
rhythmic process | Any process pertinent to the generation and maintenance of rhythms in the physiology of an organism. |
19 homologous proteins in AiPD
UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
---|---|---|---|---|
P24583 | PKC1 | Protein kinase C-like 1 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) | SS |
P05126 | PRKCB | Protein kinase C beta type | Bos taurus (Bovine) | SS |
A1A4I4 | PKN1 | Serine/threonine-protein kinase N1 | Bos taurus (Bovine) | SS |
P04409 | PRKCA | Protein kinase C alpha type | Bos taurus (Bovine) | EV SS |
A2VDV2 | STK38 | Serine/threonine-protein kinase 38 | Bos taurus (Bovine) | SS |
P13677 | inaC | Protein kinase C, eye isozyme | Drosophila melanogaster (Fruit fly) | SS |
P05130 | Pkc53E | Protein kinase C, brain isozyme | Drosophila melanogaster (Fruit fly) | SS |
P05771 | PRKCB | Protein kinase C beta type | Homo sapiens (Human) | SS |
P17252 | PRKCA | Protein kinase C alpha type | Homo sapiens (Human) | EV |
P05129 | PRKCG | Protein kinase C gamma type | Homo sapiens (Human) | SS |
P20444 | Prkca | Protein kinase C alpha type | Mus musculus (Mouse) | SS |
P68404 | Prkcb | Protein kinase C beta type | Mus musculus (Mouse) | SS |
P63318 | Prkcg | Protein kinase C gamma type | Mus musculus (Mouse) | SS |
P05696 | Prkca | Protein kinase C alpha type | Rattus norvegicus (Rat) | SS |
P68403 | Prkcb | Protein kinase C beta type | Rattus norvegicus (Rat) | SS |
P63319 | Prkcg | Protein kinase C gamma type | Rattus norvegicus (Rat) | SS |
P90980 | pkc-2 | Protein kinase C-like 2 | Caenorhabditis elegans | SS |
A8KBH6 | prkcb | Protein kinase C beta type | Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) | SS |
Q7SY24 | prkcbb | Protein kinase C beta type | Danio rerio (Zebrafish) (Brachydanio rerio) | SS |
10 | 20 | 30 | 40 | 50 | 60 |
RPLFCRKGAL | RQKVVHEVKS | HKFTARFFKQ | PTFCSHCTDF | IWGIGKQGLQ | CQVCSFVVHR |
70 | 80 | 90 | 100 | 110 | 120 |
RCHEFVTFEC | PGAGKGPQTD | DPRNKHKFRL | HSYSSPTFCD | HCGSLLYGLV | HQGMKCSCCE |
130 | 140 | 150 | 160 | 170 | 180 |
MNVHRRCVRS | VPSLCGVDHT | ERRGRLQLEI | RAPTSDEIHV | TVGEARNLIP | MDPNGLSDPY |
190 | 200 | 210 | 220 | 230 | 240 |
VKLKLIPDPR | NLTKQKTRTV | KATLNPVWNE | TFVFNLKPGD | VERRLSVEVW | DWDRTSRNDF |
250 | 260 | 270 | 280 | 290 | 300 |
MGAMSFGVSE | LLKAPVDGWY | KLLNQEEGEY | YNVPVADADN | CNLLQKFEAC | NYPLELYERV |
310 | 320 | 330 | 340 | 350 | 360 |
RTGPSSSPIP | SPSPSPTDSK | RCFFGASPGR | LHISDFSFLM | VLGKGSFGKV | MLAERRGSDE |
370 | 380 | 390 | 400 | 410 | 420 |
LYAIKILKKD | VIVQDDDVDC | TLVEKRVLAL | GGRGPGGRPH | FLTQLHSTFQ | TPDRLYFVME |
430 | 440 | 450 | 460 | 470 | 480 |
YVTGGDLMYH | IQQLGKFKEP | HAAFYAAEIA | IGLFFLHNQG | IIYRDLKLDN | VMLDAEGHIK |
490 | 500 | 510 | 520 | 530 | 540 |
ITDFGMCKEN | VFPGSTTRTF | CGTPDYIAPE | IIAYQPYGKS | VDWWSFGVLL | YEMLAGQPPF |
550 | 560 | 570 | 580 | 590 | 600 |
DGEDEEELFQ | AIMEQTVTYP | KSLSREAVAI | CKGFLTKHPA | KRLGSGPDGE | PTIRAHGFFR |
610 | 620 | 630 | 640 | 650 | 660 |
WIDWDRLERL | EIAPPFRPRP | CGRSGENFDK | FFTRAAPALT | PPDRLVLASI | DQAEFQGFTY |
670 | 680 | ||||
VNPDFVHPDA | RSPISPTPVP | VM |