Prkci
entrez
84006
canonical
uniprot
F1M7Y5
canonical
ensembl
ENSRNOG00000009652
resolver
ensembl
ENSRNOG00055009646
resolver
ensembl
ENSRNOG00060002248
resolver
ensembl
ENSRNOG00065024212
resolver
ensp
ENSRNOP00000012924
resolver
ensp
ENSRNOP00055013108
resolver
ensp
ENSRNOP00060002411
resolver
ensp
ENSRNOP00065033924
resolver
enst
ENSRNOT00000012924
resolver
enst
ENSRNOT00055016309
resolver
enst
ENSRNOT00060003519
resolver
enst
ENSRNOT00065041525
resolver
genesymbol
Prkci
resolver
genesymbol_syn
Pkcl
resolver
uniprot
B1PZT8
resolver
uniprot_entry
KPCI_RAT
resolver
uniprot_sec
B1PZT8
resolver
activity_regulation
ACTIVITY REGULATION: Atypical PKCs (PRKCI and PRKCZ) exhibit an elevated basal enzymatic activity (that may be due to the interaction with SMG1 or SQSTM1) and are not regulated by diacylglycerol, phosphatidylserine, phorbol esters or calcium ions. Two specific sites, Thr-412 (activation loop of the kinase domain) and Thr-564 (turn motif), need to be phosphorylated for its full activation. Might also be a target for novel lipid activators that are elevated during nutrient-stimulated insulin secretion (By similarity). {ECO:0000250}.
uniprot
proteins
amino_acid_sequence
MPTQRDSSTMSHTVACGGGGDHSHQVRVKAYYRGDIMITHFEPSISFEGLCSEVRDMCSFDNEQPFTMKWIDEEGDPCTVSSQLELEEAFRLYELNKDSELLIHVFPCVPERPGMPCPGEDKSIYRRGARRWRKLYCANGHTFQAKRFNRRAHCAICTDRIWGLGRQGYKCINCKLLVHKKCHKLVTIECGRHSLPPEPMMPMDQSSMHPDHTQTVIPYNPSSHESLDQVGEEKEAMNTRESGKASSSLGLQDFDLLRVIGRGSYAKVLLVRLKKTDRIYAMKVVKKELVNDDEDIDWVQTEKHVFEQASNHPFLVGLHSCFQTESRLFFVIEYVNGGDLMFHMQRQRKLPEEHARFYSAEISLALNYLHERGIIYRDLKLDNVLLDSEGHIKLTDYGMCKEGLRPGDTTSTFCGTPNYIAPEILRGEDYGFSVDWWALGVLMFEMMAGRSPFDIVGSSDNPDQNTEDYLFQVILEKQIRIPRSLSVKAASVLKSFLNKDPKERLGCHPQTGFADIQGHPFFRNVDWDMMEQKQVVPPFKPNISGEFGLDNFDSQFTNEPVQLTPDDDDIVRKIDQSEFEGFEYINPLLMSAEECV
uniprot
proteins
ec_number
2.7.11.13
uniprot
proteins
function
FUNCTION: Calcium- and diacylglycerol-independent serine/ threonine-protein kinase that plays a general protective role against apoptotic stimuli, is involved in NF-kappa-B activation, cell survival, differentiation and polarity, and contributes to the regulation of microtubule dynamics in the early secretory pathway. Is necessary for BCR-ABL oncogene-mediated resistance to apoptotic drug in leukemia cells, protecting leukemia cells against drug-induced apoptosis. In cultured neurons, prevents amyloid beta protein-induced apoptosis by interrupting cell death process at a very early step. In glioblastoma cells, may function downstream of phosphatidylinositol 3-kinase (PI3K) and PDPK1 in the promotion of cell survival by phosphorylating and inhibiting the pro-apoptotic factor BAD. Can form a protein complex in non-small cell lung cancer (NSCLC) cells with PARD6A and ECT2 and regulate ECT2 oncogenic activity by phosphorylation, which in turn promotes transformed growth and invasion. In response to nerve growth factor (NGF), acts downstream of SRC to phosphorylate and activate IRAK1, allowing the subsequent activation of NF-kappa-B and neuronal cell survival. Functions in the organization of the apical domain in epithelial cells by phosphorylating EZR. This step is crucial for activation and normal distribution of EZR at the early stages of intestinal epithelial cell differentiation. Forms a protein complex with LLGL1 and PARD6B independently of PARD3 to regulate epithelial cell polarity. Plays a role in microtubule dynamics in the early secretory pathway through interaction with RAB2A and GAPDH and recruitment to vesicular tubular clusters (VTCs). In human coronary artery endothelial cells (HCAEC), is activated by saturated fatty acids and mediates lipid-induced apoptosis. Downstream of PI3K is required for insulin-stimulated glucose transport. Activates RAB4A and promotes its association with KIF3A which is required for the insulin-induced SLC2A4/GLUT4 translocation in adipocytes. Is essential in early embryogenesis and development of differentiating photoreceptors by playing a role in the establishment of epithelial and neuronal polarity (By similarity). Involved in early synaptic long term potentiation phase in CA1 hippocampal cells and short term memory formation (PubMed:27498875). {ECO:0000250, ECO:0000269|PubMed:27498875}.
uniprot
proteins
mass_dalton
68276
uniprot
proteins
mutagenesis
MUTAGEN 265; /note="Y->F: Loss of phosphorylation and nuclear import."; /evidence="ECO:0000269|PubMed:11891849
uniprot
proteins
post_translational_modification
PTM: Phosphorylation at Thr-412 in the activation loop is not mandatory for activation (By similarity). Upon neuronal growth factor (NGF) stimulation, phosphorylated by SRC at Tyr-265, Tyr-280 and Tyr-334 (By similarity). Phosphorylation at Tyr-265 facilitates binding to KPNB1/importin-beta regulating entry of PRKCI into the nucleus (PubMed:11891849). Phosphorylation on Tyr-334 is important for NF-kappa-B stimulation (By similarity). Phosphorylated at Thr-564 during the initial phase of long term potentiation (PubMed:27498875). {ECO:0000250|UniProtKB:P41743, ECO:0000250|UniProtKB:Q62074, ECO:0000269|PubMed:11891849, ECO:0000269|PubMed:27498875}.
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
11891849
uniprot
proteins
pubmed
15057822
uniprot
proteins
pubmed
19090727
uniprot
proteins
pubmed
22673903
uniprot
proteins
pubmed
27498875
uniprot
proteins
sequence_length
596
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11891849}. Membrane {ECO:0000250|UniProtKB:P41743}. Endosome {ECO:0000250|UniProtKB:P41743}. Nucleus {ECO:0000269|PubMed:11891849}. Note=Transported into the endosome through interaction with SQSTM1/p62. After phosphorylation by SRC, transported into the nucleus through interaction with KPNB1. Colocalizes with CDK7 in the cytoplasm and nucleus. Transported to vesicular tubular clusters (VTCs) through interaction with RAB2A. {ECO:0000250|UniProtKB:P41743}.
uniprot
proteins