P10102
Gene name |
PRKCA |
Protein name |
Protein kinase C alpha type |
Names |
PKC-A, PKC-alpha |
Species |
Oryctolagus cuniculus (Rabbit) |
KEGG Pathway |
ocu:100037720 |
EC number |
2.7.11.13: 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
480-503 (Activation loop from InterPro)
Target domain |
328-668 (Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha) |
Relief mechanism |
|
Assay |
|
Autoinhibited structure
Activated structure
1 structures for P10102
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-P10102-F1 | Predicted | AlphaFoldDB |
No variants for P10102
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for P10102 | |||||
No associated diseases with P10102
12 regional properties for P10102
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | C2 domain | 158 - 277 | IPR000008 |
| domain | Protein kinase domain | 339 - 597 | IPR000719 |
| domain | AGC-kinase, C-terminal | 598 - 668 | IPR000961 |
| domain | Protein kinase C-like, phorbol ester/diacylglycerol-binding domain | 36 - 87 | IPR002219-1 |
| domain | Protein kinase C-like, phorbol ester/diacylglycerol-binding domain | 101 - 153 | IPR002219-2 |
| active_site | Serine/threonine-protein kinase, active site | 459 - 471 | IPR008271 |
| binding_site | Protein kinase, ATP binding site | 345 - 368 | IPR017441 |
| domain | Diacylglycerol/phorbol-ester binding | 34 - 48 | IPR020454-1 |
| domain | Diacylglycerol/phorbol-ester binding | 50 - 59 | IPR020454-2 |
| domain | Diacylglycerol/phorbol-ester binding | 63 - 74 | IPR020454-3 |
| domain | Diacylglycerol/phorbol-ester binding | 140 - 152 | IPR020454-4 |
| domain | Classical Protein Kinase C alpha, catalytic domain | 328 - 668 | IPR034663 |
Functions
| Description | ||
|---|---|---|
| EC Number | 2.7.11.13 | Protein-serine/threonine kinases |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
6 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
| cytosol | The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. |
| mitochondrial membrane | Either of the lipid bilayers that surround the mitochondrion and form the mitochondrial envelope. |
| 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 | The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins. |
4 GO annotations of molecular function
| Name | Definition |
|---|---|
| ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
| calcium-dependent protein kinase C activity | Calcium-dependent catalysis of the reaction: ATP + a protein = ADP + a phosphoprotein. |
| protein serine kinase activity | Catalysis of the reactions: ATP + protein serine = ADP + protein serine phosphate. |
| zinc ion binding | Binding to a zinc ion (Zn). |
17 GO annotations of biological process
| Name | Definition |
|---|---|
| angiogenesis | Blood vessel formation when new vessels emerge from the proliferation of pre-existing blood vessels. |
| apoptotic process | A programmed cell death process which begins when a cell receives an internal (e.g. DNA damage) or external signal (e.g. an extracellular death ligand), and proceeds through a series of biochemical events (signaling pathway phase) which trigger an execution phase. The execution phase is the last step of an apoptotic process, and is typically characterized by rounding-up of the cell, retraction of pseudopodes, reduction of cellular volume (pyknosis), chromatin condensation, nuclear fragmentation (karyorrhexis), plasma membrane blebbing and fragmentation of the cell into apoptotic bodies. When the execution phase is completed, the cell has died. |
| cell adhesion | The attachment of a cell, either to another cell or to an underlying substrate such as the extracellular matrix, via cell adhesion molecules. |
| negative regulation of glial cell apoptotic process | Any process that stops, prevents, or reduces the frequency, rate, or extent of glial cell apoptotic process. |
| positive regulation of angiogenesis | Any process that activates or increases angiogenesis. |
| positive regulation of cardiac muscle hypertrophy | Any process that increases the rate, frequency or extent of the enlargement or overgrowth of all or part of the heart due to an increase in size (not length) of individual cardiac muscle fibers, without cell division. |
| positive regulation of cell adhesion | Any process that activates or increases the frequency, rate or extent of cell adhesion. |
| positive regulation of cell migration | Any process that activates or increases the frequency, rate or extent of cell migration. |
| positive regulation of dense core granule biogenesis | Any process that activates or increases the frequency, rate or extent of dense core granule biogenesis. |
| positive regulation of endothelial cell migration | Any process that increases the rate, frequency, or extent of the orderly movement of an endothelial cell into the extracellular matrix to form an endothelium. |
| positive regulation of endothelial cell proliferation | Any process that activates or increases the rate or extent of endothelial cell proliferation. |
| positive regulation of ERK1 and ERK2 cascade | Any process that activates or increases the frequency, rate or extent of signal transduction mediated by the ERK1 and ERK2 cascade. |
| positive regulation of lipopolysaccharide-mediated signaling pathway | Any process that activates or increases the frequency, rate or extent of signaling in response to detection of lipopolysaccharide. |
| positive regulation of macrophage differentiation | Any process that activates or increases the frequency, rate or extent of macrophage differentiation. |
| positive regulation of mitotic cell cycle | Any process that activates or increases the rate or extent of progression through the mitotic cell cycle. |
| protein phosphorylation | The process of introducing a phosphate group on to a protein. |
| regulation of platelet aggregation | Any process that modulates the rate, frequency or extent of platelet aggregation. Platelet aggregation is the adhesion of one platelet to one or more other platelets via adhesion molecules. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MADVFPANDS | TASQDVANRF | ARKGALRQKN | VHEVKDHKFI | ARFFKQPTFC | SHCTDFIWGF |
| 70 | 80 | 90 | 100 | 110 | 120 |
| GKQGFQCQVC | CFVVHKRCHE | FVTFSCPGAD | KGPDTDDPRS | KHKFKIHTYG | SPTFCDHCGS |
| 130 | 140 | 150 | 160 | 170 | 180 |
| LLYGLIHQGM | KCDTCDMNVH | KQCVINVPSL | CGMDHTEKRG | RIYLKAEVTD | EKLHVTVRDA |
| 190 | 200 | 210 | 220 | 230 | 240 |
| KNLIPMDPNG | LSDPYVKLKL | IPDPKNESKQ | KTKTIRSTLN | PQWNESFTFK | LKPSDKDRRL |
| 250 | 260 | 270 | 280 | 290 | 300 |
| SVEIWDWDRT | TRNDFMGSLS | FGVSELMKMP | ASGWYKLLNQ | EEGEYYNVPI | PEGDEDGNVE |
| 310 | 320 | 330 | 340 | 350 | 360 |
| LRQKFEKAKL | GPAGNKVISP | SEDRKQPSNN | LDRVKLTDFN | FLMVLGKGSF | GKVMLADRKG |
| 370 | 380 | 390 | 400 | 410 | 420 |
| TEELYAIKIL | KKDVVIQDDD | VECTMVEKRV | LALMDKPPFL | TQLHSCFQTV | DRLYFVMEYV |
| 430 | 440 | 450 | 460 | 470 | 480 |
| NGGDLMYHIQ | QVGKFKEPQA | VFYAAEISIG | LFFLHKRGII | YRDLKLDNVM | LDSEGHIKIA |
| 490 | 500 | 510 | 520 | 530 | 540 |
| DFGMCKEHMM | DGVTTRTFCG | TPDYIAPEII | AYQPYGKSVD | WWAYGVLLYE | MLAGQPPFDG |
| 550 | 560 | 570 | 580 | 590 | 600 |
| EDEDELFQSI | MEHNVSYPKS | LSKEAVSICK | GLMTKHPAKR | LGCGPEGERD | VREHAFFRRI |
| 610 | 620 | 630 | 640 | 650 | 660 |
| DWEKLENREI | QPPFKPKVCG | KGAENFDKFF | TRGQPVVTPP | DQLVIANIDQ | SDFEGFSYVN |
| 670 | |||||
| PQFVHPILQS | SV |