PRKCE
entrez
5581
canonical
uniprot
Q02156
canonical
ensembl
ENSG00000171132
resolver
ensp
ENSP00000306124
resolver
ensp
ENSP00000721741
resolver
ensp
ENSP00000776968
resolver
ensp
ENSP00000797453
resolver
enst
ENST00000306156
resolver
genesymbol
PRKCE
resolver
genesymbol_syn
PKCE
resolver
hgnc
HGNC:9401
resolver
uniprot
B0LPH7
resolver
uniprot
Q32MQ3
resolver
uniprot
Q53SL4
resolver
uniprot
Q53SM5
resolver
uniprot
Q9UE81
resolver
uniprot_entry
KPCE_HUMAN
resolver
uniprot_sec
B0LPH7
resolver
uniprot_sec
Q32MQ3
resolver
uniprot_sec
Q53SL4
resolver
uniprot_sec
Q53SM5
resolver
uniprot_sec
Q9UE81
resolver
activity_regulation
ACTIVITY REGULATION: Novel PKCs (PRKCD, PRKCE, PRKCH and PRKCQ) are calcium-insensitive, but activated by diacylglycerol (DAG) and phosphatidylserine. Three specific sites; Thr-566 (activation loop of the kinase domain), Thr-710 (turn motif) and Ser-729 (hydrophobic region), need to be phosphorylated for its full activation (PubMed:21806543, PubMed:34593629). Inhibited by PRKCH upstream open reading frame 2 (PubMed:34593629). {ECO:0000269|PubMed:21806543, ECO:0000269|PubMed:34593629}.
uniprot
proteins
amino_acid_sequence
MVVFNGLLKIKICEAVSLKPTAWSLRHAVGPRPQTFLLDPYIALNVDDSRIGQTATKQKTNSPAWHDEFVTDVCNGRKIELAVFHDAPIGYDDFVANCTIQFEELLQNGSRHFEDWIDLEPEGRVYVIIDLSGSSGEAPKDNEERVFRERMRPRKRQGAVRRRVHQVNGHKFMATYLRQPTYCSHCRDFIWGVIGKQGYQCQVCTCVVHKRCHELIITKCAGLKKQETPDQVGSQRFSVNMPHKFGIHNYKVPTFCDHCGSLLWGLLRQGLQCKVCKMNVHRRCETNVAPNCGVDARGIAKVLADLGVTPDKITNSGQRRKKLIAGAESPQPASGSSPSEEDRSKSAPTSPCDQEIKELENNIRKALSFDNRGEEHRAASSPDGQLMSPGENGEVRQGQAKRLGLDEFNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDDDVDCTMTEKRILALARKHPYLTQLYCCFQTKDRLFFVMEYVNGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGILNGVTTTTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDVLYPVWLSKEAVSILKAFMTKNPHKRLGCVASQNGEDAIKQHPFFKEIDWVLLEQKKIKPPFKPRIKTKRDVNNFDQDFTREEPVLTLVDEAIVKQINQEEFKGFSYFGEDLMP
uniprot
proteins
ec_number
2.7.11.13
uniprot
proteins
function
FUNCTION: Calcium-independent, phospholipid- and diacylglycerol (DAG)-dependent serine/threonine-protein kinase that plays essential roles in the regulation of multiple cellular processes linked to cytoskeletal proteins, such as cell adhesion, motility, migration and cell cycle, functions in neuron growth and ion channel regulation, and is involved in immune response, cancer cell invasion and regulation of apoptosis. Mediates cell adhesion to the extracellular matrix via integrin-dependent signaling, by mediating angiotensin-2-induced activation of integrin beta-1 (ITGB1) in cardiac fibroblasts. Phosphorylates MARCKS, which phosphorylates and activates PTK2/FAK, leading to the spread of cardiomyocytes. Involved in the control of the directional transport of ITGB1 in mesenchymal cells by phosphorylating vimentin (VIM), an intermediate filament (IF) protein. In epithelial cells, associates with and phosphorylates keratin-8 (KRT8), which induces targeting of desmoplakin at desmosomes and regulates cell-cell contact. Phosphorylates IQGAP1, which binds to CDC42, mediating epithelial cell-cell detachment prior to migration. In HeLa cells, contributes to hepatocyte growth factor (HGF)-induced cell migration, and in human corneal epithelial cells, plays a critical role in wound healing after activation by HGF. During cytokinesis, forms a complex with YWHAB, which is crucial for daughter cell separation, and facilitates abscission by a mechanism which may implicate the regulation of RHOA. In cardiac myocytes, regulates myofilament function and excitation coupling at the Z-lines, where it is indirectly associated with F-actin via interaction with COPB1. During endothelin-induced cardiomyocyte hypertrophy, mediates activation of PTK2/FAK, which is critical for cardiomyocyte survival and regulation of sarcomere length. Plays a role in the pathogenesis of dilated cardiomyopathy via persistent phosphorylation of troponin I (TNNI3). Involved in nerve growth factor (NFG)-induced neurite outgrowth and neuron morphological change independently of its kinase activity, by inhibition of RHOA pathway, activation of CDC42 and cytoskeletal rearrangement. May be involved in presynaptic facilitation by mediating phorbol ester-induced synaptic potentiation. Phosphorylates gamma-aminobutyric acid receptor subunit gamma-2 (GABRG2), which reduces the response of GABA receptors to ethanol and benzodiazepines and may mediate acute tolerance to the intoxicating effects of ethanol. Upon PMA treatment, phosphorylates the capsaicin- and heat-activated cation channel TRPV1, which is required for bradykinin-induced sensitization of the heat response in nociceptive neurons. Is able to form a complex with PDLIM5 and N-type calcium channel, and may enhance channel activities and potentiates fast synaptic transmission by phosphorylating the pore-forming alpha subunit CACNA1B (CaV2.2). In prostate cancer cells, interacts with and phosphorylates STAT3, which increases DNA-binding and transcriptional activity of STAT3 and seems to be essential for prostate cancer cell invasion. Downstream of TLR4, plays an important role in the lipopolysaccharide (LPS)-induced immune response by phosphorylating and activating TICAM2/TRAM, which in turn activates the transcription factor IRF3 and subsequent cytokines production. In differentiating erythroid progenitors, is regulated by EPO and controls the protection against the TNFSF10/TRAIL-mediated apoptosis, via BCL2. May be involved in the regulation of the insulin-induced phosphorylation and activation of AKT1. Phosphorylates NLRP5/MATER and may thereby modulate AKT pathway activation in cumulus cells (PubMed:19542546). 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:0000269|PubMed:11884385, ECO:0000269|PubMed:1374067, ECO:0000269|PubMed:15355962, ECO:0000269|PubMed:16757566, ECO:0000269|PubMed:17603037, ECO:0000269|PubMed:17875639, ECO:0000269|PubMed:17875724, ECO:0000269|PubMed:19542546, ECO:0000269|PubMed:20969574, ECO:0000269|PubMed:21806543, ECO:0000269|PubMed:36040231}.
uniprot
proteins
mass_dalton
83674
uniprot
proteins
mutagenesis
MUTAGEN 437; /note="K->W: Abolishes activity and S-729 phosphorylation."; /evidence="ECO:0000269|PubMed:11964154, ECO:0000269|PubMed:21806543"; MUTAGEN 566; /note="T->A: Abolishes phosphorylation by PDPK1/PDK1, and S-729 phosphorylation."; /evidence="ECO:0000269|PubMed:11964154"; MUTAGEN 566; /note="T->E: No effect on S-729 phosphorylation."; /evidence="ECO:0000269|PubMed:11964154"; MUTAGEN 710; /note="T->E: No effect on activity; no effect on S-729 phosphorylation."; /evidence="ECO:0000269|PubMed:11964154"; MUTAGEN 729; /note="S->A: Enhances T-566 dephosphorylation."; /evidence="ECO:0000269|PubMed:11964154
uniprot
proteins
post_translational_modification
PTM: Phosphorylation on Thr-566 by PDPK1 triggers autophosphorylation on Ser-729 (PubMed:11964154). Phosphorylation in the hinge domain at Ser-350 by MAPK11 or MAPK14, Ser-346 by GSK3B and Ser-368 by autophosphorylation is required for interaction with YWHAB (PubMed:19662078). In response to growth factors, phosphorylated at Thr-703 and Ser-729 by the mTORC2 complex, promoting autophosphorylation and activation of PRKCE (PubMed:21806543). {ECO:0000269|PubMed:11964154, ECO:0000269|PubMed:19662078, 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
11884385
uniprot
proteins
pubmed
11964154
uniprot
proteins
pubmed
12473185
uniprot
proteins
pubmed
1374067
uniprot
proteins
pubmed
1382605
uniprot
proteins
pubmed
15355962
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15632189
uniprot
proteins
pubmed
15815621
uniprot
proteins
pubmed
16584980
uniprot
proteins
pubmed
16757566
uniprot
proteins
pubmed
16959974
uniprot
proteins
pubmed
17344846
uniprot
proteins
pubmed
17603037
uniprot
proteins
pubmed
17875639
uniprot
proteins
pubmed
17875724
uniprot
proteins
pubmed
18408015
uniprot
proteins
pubmed
18637120
uniprot
proteins
pubmed
18637121
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
18691976
uniprot
proteins
pubmed
19542546
uniprot
proteins
pubmed
19662078
uniprot
proteins
pubmed
20350291
uniprot
proteins
pubmed
20353823
uniprot
proteins
pubmed
20969574
uniprot
proteins
pubmed
21681677
uniprot
proteins
pubmed
21806543
uniprot
proteins
pubmed
21810427
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
34593629
uniprot
proteins
pubmed
36040231
uniprot
proteins
sequence_length
737
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17603037, ECO:0000269|PubMed:19542546}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:17603037}. Cell membrane {ECO:0000269|PubMed:17603037}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P16054}. Nucleus {ECO:0000250|UniProtKB:P16054}. Note=Translocated to plasma membrane in epithelial cells stimulated by HGF (PubMed:17603037). Associated with the Golgi at the perinuclear site in pre-passage fibroblasts (By similarity). In passaging cells, translocated to the cell periphery (By similarity). Translocated to the nucleus in PMA-treated cells (By similarity). {ECO:0000250|UniProtKB:P16054, ECO:0000269|PubMed:17603037}.
uniprot
proteins