PRKCA
entrez
5578
canonical
uniprot
P17252
canonical
ensembl
ENSG00000154229
resolver
ensp
ENSP00000408695
resolver
ensp
ENSP00000462087
resolver
enst
ENST00000413366
resolver
enst
ENST00000578063
resolver
genesymbol
PRKCA
resolver
genesymbol_syn
PKCA
resolver
genesymbol_syn
PRKACA
resolver
hgnc
HGNC:9393
resolver
uniprot
B5BU22
resolver
uniprot
J3KRN5
resolver
uniprot
Q15137
resolver
uniprot
Q32M72
resolver
uniprot
Q7Z727
resolver
uniprot
Q96RE4
resolver
uniprot_entry
J3KRN5_HUMAN
resolver
uniprot_entry
KPCA_HUMAN
resolver
uniprot_entry
Q7Z727_HUMAN
resolver
uniprot_sec
B5BU22
resolver
uniprot_sec
Q15137
resolver
uniprot_sec
Q32M72
resolver
uniprot_sec
Q96RE4
resolver
activity_regulation
ACTIVITY REGULATION: Classical (or conventional) PKCs (PRKCA, PRKCB and PRKCG) are activated by calcium and diacylglycerol (DAG) in the presence of phosphatidylserine. Three specific sites; Thr-497 (activation loop of the kinase domain), Thr-638 (turn motif) and Ser-657 (hydrophobic region), need to be phosphorylated for its full activation. {ECO:0000269|PubMed:21806543}.
uniprot
proteins
amino_acid_sequence
MADVFPGNDSTASQDVANRFARKGALRQKNVHEVKDHKFIARFFKQPTFCSHCTDFIWGFGKQGFQCQVCCFVVHKRCHEFVTFSCPGADKGPDTDDPRSKHKFKIHTYGSPTFCDHCGSLLYGLIHQGMKCDTCDMNVHKQCVINVPSLCGMDHTEKRGRIYLKAEVADEKLHVTVRDAKNLIPMDPNGLSDPYVKLKLIPDPKNESKQKTKTIRSTLNPQWNESFTFKLKPSDKDRRLSVEIWDWDRTTRNDFMGSLSFGVSELMKMPASGWYKLLNQEEGEYYNVPIPEGDEEGNMELRQKFEKAKLGPAGNKVISPSEDRKQPSNNLDRVKLTDFNFLMVLGKGSFGKVMLADRKGTEELYAIKILKKDVVIQDDDVECTMVEKRVLALLDKPPFLTQLHSCFQTVDRLYFVMEYVNGGDLMYHIQQVGKFKEPQAVFYAAEISIGLFFLHKRGIIYRDLKLDNVMLDSEGHIKIADFGMCKEHMMDGVTTRTFCGTPDYIAPEIIAYQPYGKSVDWWAYGVLLYEMLAGQPPFDGEDEDELFQSIMEHNVSYPKSLSKEAVSVCKGLMTKHPAKRLGCGPEGERDVREHAFFRRIDWEKLENREIQPPFKPKVCGKGAENFDKFFTRGQPVLTPPDQLVIANIDQSDFEGFSYVNPQFVHPILQSAV
uniprot
proteins
ec_number
2.7.11.13
uniprot
proteins
function
FUNCTION: Calcium-activated, phospholipid- and diacylglycerol (DAG)-dependent serine/threonine-protein kinase that is involved in positive and negative regulation of cell proliferation, apoptosis, differentiation, migration and adhesion, tumorigenesis, cardiac hypertrophy, angiogenesis, platelet function and inflammation, by directly phosphorylating targets such as RAF1, BCL2, CSPG4, TNNT2/CTNT, or activating signaling cascade involving MAPK1/3 (ERK1/2) and RAP1GAP. Involved in cell proliferation and cell growth arrest by positive and negative regulation of the cell cycle. Can promote cell growth by phosphorylating and activating RAF1, which mediates the activation of the MAPK/ERK signaling cascade, and/or by up-regulating CDKN1A, which facilitates active cyclin-dependent kinase (CDK) complex formation in glioma cells. In intestinal cells stimulated by the phorbol ester PMA, can trigger a cell cycle arrest program which is associated with the accumulation of the hyper-phosphorylated growth-suppressive form of RB1 and induction of the CDK inhibitors CDKN1A and CDKN1B. Exhibits anti-apoptotic function in glioma cells and protects them from apoptosis by suppressing the p53/TP53-mediated activation of IGFBP3, and in leukemia cells mediates anti-apoptotic action by phosphorylating BCL2. During macrophage differentiation induced by macrophage colony-stimulating factor (CSF1), is translocated to the nucleus and is associated with macrophage development. After wounding, translocates from focal contacts to lamellipodia and participates in the modulation of desmosomal adhesion. Plays a role in cell motility by phosphorylating CSPG4, which induces association of CSPG4 with extensive lamellipodia at the cell periphery and polarization of the cell accompanied by increases in cell motility. During chemokine-induced CD4(+) T cell migration, phosphorylates CDC42-guanine exchange factor DOCK8 resulting in its dissociation from LRCH1 and the activation of GTPase CDC42 (PubMed:28028151). Is highly expressed in a number of cancer cells where it can act as a tumor promoter and is implicated in malignant phenotypes of several tumors such as gliomas and breast cancers. Negatively regulates myocardial contractility and positively regulates angiogenesis, platelet aggregation and thrombus formation in arteries. Mediates hypertrophic growth of neonatal cardiomyocytes, in part through a MAPK1/3 (ERK1/2)-dependent signaling pathway, and upon PMA treatment, is required to induce cardiomyocyte hypertrophy up to heart failure and death, by increasing protein synthesis, protein-DNA ratio and cell surface area. Regulates cardiomyocyte function by phosphorylating cardiac troponin T (TNNT2/CTNT), which induces significant reduction in actomyosin ATPase activity, myofilament calcium sensitivity and myocardial contractility. In angiogenesis, is required for full endothelial cell migration, adhesion to vitronectin (VTN), and vascular endothelial growth factor A (VEGFA)-dependent regulation of kinase activation and vascular tube formation. Involved in the stabilization of VEGFA mRNA at post-transcriptional level and mediates VEGFA-induced cell proliferation. In the regulation of calcium-induced platelet aggregation, mediates signals from the CD36/GP4 receptor for granule release, and activates the integrin heterodimer ITGA2B-ITGB3 through the RAP1GAP pathway for adhesion. During response to lipopolysaccharides (LPS), may regulate selective LPS-induced macrophage functions involved in host defense and inflammation. But in some inflammatory responses, may negatively regulate NF-kappa-B-induced genes, through IL1A-dependent induction of NF-kappa-B inhibitor alpha (NFKBIA/IKBA). Upon stimulation with 12-O-tetradecanoylphorbol-13-acetate (TPA), phosphorylates EIF4G1, which modulates EIF4G1 binding to MKNK1 and may be involved in the regulation of EIF4E phosphorylation. Phosphorylates KIT, leading to inhibition of KIT activity. Phosphorylates ATF2 which promotes cooperation between ATF2 and JUN, activating transcription. Phosphorylates SOCS2 at 'Ser-52' facilitating its ubiquitination and proteasomal degradation (By similarity). Phosphorylates KLHL3 in response to angiotensin II signaling, decreasing the interaction between KLHL3 and WNK4 (PubMed:25313067). Phosphorylates and activates LRRK1, which phosphorylates RAB proteins involved in intracellular trafficking (PubMed:36040231). Acts as a regulator of dopamine signaling by mediating constitutive phosphorylation of dopamine receptor DRD1, inhibiting G protein-coupled receptor signaling (PubMed:20969574). {ECO:0000250|UniProtKB:P20444, ECO:0000269|PubMed:10848585, ECO:0000269|PubMed:11909826, ECO:0000269|PubMed:12724315, ECO:0000269|PubMed:12832403, ECO:0000269|PubMed:15016832, ECO:0000269|PubMed:15504744, ECO:0000269|PubMed:15526160, ECO:0000269|PubMed:18056764, ECO:0000269|PubMed:19176525, ECO:0000269|PubMed:20969574, ECO:0000269|PubMed:21576361, ECO:0000269|PubMed:21806543, ECO:0000269|PubMed:23990668, ECO:0000269|PubMed:25313067, ECO:0000269|PubMed:28028151, ECO:0000269|PubMed:36040231, ECO:0000269|PubMed:9738012, ECO:0000269|PubMed:9830023, ECO:0000269|PubMed:9873035, ECO:0000269|PubMed:9927633}.
uniprot
proteins
mass_dalton
76750
uniprot
proteins
mutagenesis
MUTAGEN 368; /note="K->M: Abolished protein kinase activity."; /evidence="ECO:0000269|PubMed:21806543
uniprot
proteins
post_translational_modification
PTM: In response to growth factors, phosphorylated at Thr-631 and Ser-657 by the mTORC2 complex, promoting autophosphorylation and activation of PRKCA. {ECO:0000269|PubMed:21806543}.
uniprot
proteins
protein_family
AGC Ser/Thr protein kinase family
uniprot
proteins
protein_family
PKC subfamily
uniprot
proteins
protein_family
Protein kinase superfamily
uniprot
proteins
pubmed
10848585
uniprot
proteins
pubmed
11909826
uniprot
proteins
pubmed
12417014
uniprot
proteins
pubmed
12665801
uniprot
proteins
pubmed
12724315
uniprot
proteins
pubmed
12832403
uniprot
proteins
pubmed
12893243
uniprot
proteins
pubmed
15016832
uniprot
proteins
pubmed
15247289
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15504744
uniprot
proteins
pubmed
15526160
uniprot
proteins
pubmed
16129412
uniprot
proteins
pubmed
16625196
uniprot
proteins
pubmed
17081983
uniprot
proteins
pubmed
1714454
uniprot
proteins
pubmed
17344846
uniprot
proteins
pubmed
17893151
uniprot
proteins
pubmed
18056764
uniprot
proteins
pubmed
18088087
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
18691976
uniprot
proteins
pubmed
19054851
uniprot
proteins
pubmed
19176525
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19608861
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
19827831
uniprot
proteins
pubmed
19969380
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20969574
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21576361
uniprot
proteins
pubmed
21806543
uniprot
proteins
pubmed
22814378
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
2336401
uniprot
proteins
pubmed
23990668
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25313067
uniprot
proteins
pubmed
27925688
uniprot
proteins
pubmed
28028151
uniprot
proteins
pubmed
36040231
uniprot
proteins
pubmed
9738012
uniprot
proteins
pubmed
9830023
uniprot
proteins
pubmed
9873035
uniprot
proteins
pubmed
9927633
uniprot
proteins
sequence_length
672
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23990668}. Cell membrane {ECO:0000269|PubMed:23990668, ECO:0000269|PubMed:36040231}; Peripheral membrane protein {ECO:0000305|PubMed:23990668, ECO:0000305|PubMed:36040231}. Mitochondrion membrane {ECO:0000269|PubMed:9738012}; Peripheral membrane protein {ECO:0000305|PubMed:9738012}. Nucleus {ECO:0000250|UniProtKB:P20444}.
uniprot
proteins