Prkcb
entrez
25023
canonical
uniprot
P68403
canonical
ensembl
ENSRNOG00000012061
resolver
ensembl
ENSRNOG00055008014
resolver
ensembl
ENSRNOG00060030161
resolver
ensembl
ENSRNOG00065013001
resolver
ensp
ENSRNOP00000016417
resolver
ensp
ENSRNOP00000073511
resolver
ensp
ENSRNOP00000111645
resolver
genesymbol
Prkcb
resolver
genesymbol_syn
Pkcb
resolver
genesymbol_syn
Prkcb1
resolver
uniprot
P04410
resolver
uniprot
P04411
resolver
uniprot_entry
KPCB_RAT
resolver
uniprot_sec
P04410
resolver
uniprot_sec
P04411
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-500 (activation loop of the kinase domain), Thr-642 (turn motif) and Ser-661 (hydrophobic region), need to be phosphorylated for its full activation. Specifically inhibited by enzastaurin (LY317615) (By similarity). {ECO:0000250}.
uniprot
proteins
amino_acid_sequence
MADPAAGPPPSEGEESTVRFARKGALRQKNVHEVKNHKFTARFFKQPTFCSHCTDFIWGFGKQGFQCQVCCFVVHKRCHEFVTFSCPGADKGPASDDPRSKHKFKIHTYSSPTFCDHCGSLLYGLIHQGMKCDTCMMNVHKRCVMNVPSLCGTDHTERRGRIYIQAHIDREVLIVVVRDAKNLVPMDPNGLSDPYVKLKLIPDPKSESKQKTKTIKCSLNPEWNETFRFQLKESDKDRRLSVEIWDWDLTSRNDFMGSLSFGISELQKAGVDGWFKLLSQEEGEYFNVPVPPEGSEGNEELRQKFERAKIGQGTKAPEEKTANTISKFDNNGNRDRMKLTDFNFLMVLGKGSFGKVMLSERKGTDELYAVKILKKDVVIQDDDVECTMVEKRVLALPGKPPFLTQLHSCFQTMDRLYFVMEYVNGGDLMYHIQQVGRFKEPHAVFYAAEIAIGLFFLQSKGIIYRDLKLDNVMLDSEGHIKIADFGMCKENIWDGVTTKTFCGTPDYIAPEIIAYQPYGKSVDWWAFGVLLYEMLAGQAPFEGEDEDELFQSIMEHNVAYPKSMSKEAVAICKGLMTKHPGKRLGCGPEGERDIKEHAFFRYIDWEKLERKEIQPPYKPKARDKRDTSNFDKEFTRQPVELTPTDKLFIMNLDQNEFAGFSYTNPEFVINV
uniprot
proteins
ec_number
2.7.11.13
uniprot
proteins
function
FUNCTION: Calcium-activated, phospholipid- and diacylglycerol (DAG)-dependent serine/threonine-protein kinase involved in various cellular processes such as regulation of the B-cell receptor (BCR) signalosome, oxidative stress-induced apoptosis, androgen receptor-dependent transcription regulation, insulin signaling and endothelial cells proliferation. Plays a key role in B-cell activation by regulating BCR-induced NF-kappa-B activation. Mediates the activation of the canonical NF-kappa-B pathway (NFKB1) by direct phosphorylation of CARD11/CARMA1 at 'Ser-559', 'Ser-644' and 'Ser-652'. Phosphorylation induces CARD11/CARMA1 association with lipid rafts and recruitment of the BCL10-MALT1 complex as well as MAP3K7/TAK1, which then activates IKK complex, resulting in nuclear translocation and activation of NFKB1. Plays a direct role in the negative feedback regulation of the BCR signaling, by down-modulating BTK function via direct phosphorylation of BTK at 'Ser-180', which results in the alteration of BTK plasma membrane localization and in turn inhibition of BTK activity. Involved in apoptosis following oxidative damage: in case of oxidative conditions, specifically phosphorylates 'Ser-36' of isoform p66Shc of SHC1, leading to mitochondrial accumulation of p66Shc, where p66Shc acts as a reactive oxygen species producer. Acts as a coactivator of androgen receptor (ANDR)-dependent transcription, by being recruited to ANDR target genes and specifically mediating phosphorylation of 'Thr-6' of histone H3 (H3T6ph), a specific tag for epigenetic transcriptional activation that prevents demethylation of histone H3 'Lys-4' (H3K4me) by LSD1/KDM1A. In insulin signaling, may function downstream of IRS1 in muscle cells and mediate insulin-dependent DNA synthesis through the RAF1-MAPK/ERK signaling cascade. Participates in the regulation of glucose transport in adipocytes by negatively modulating the insulin-stimulated translocation of the glucose transporter SLC2A4/GLUT4. Phosphorylates SLC2A1/GLUT1, promoting glucose uptake by SLC2A1/GLUT1. Under high glucose in pancreatic beta-cells, is probably involved in the inhibition of the insulin gene transcription, via regulation of MYC expression. In endothelial cells, activation of PRKCB induces increased phosphorylation of RB1, increased VEGFA-induced cell proliferation, and inhibits PI3K/AKT-dependent nitric oxide synthase (NOS3/eNOS) regulation by insulin, which causes endothelial dysfunction. Also involved in triglyceride homeostasis (By similarity). Phosphorylates ATF2 which promotes cooperation between ATF2 and JUN, activating transcription. Phosphorylates KLHL3 in response to angiotensin II signaling, decreasing the interaction between KLHL3 and WNK4 (By similarity). Phosphorylates and activates LRRK1, which phosphorylates RAB proteins involved in intracellular trafficking (By similarity). Acts as a regulator of dopamine signaling by mediating constitutive phosphorylation of dopamine receptors DRD1 and DRD2, inhibiting G protein-coupled receptor signaling (By similarity). {ECO:0000250|UniProtKB:P05771, ECO:0000250|UniProtKB:P68404, ECO:0000269|PubMed:10938109, ECO:0000269|PubMed:11714718, ECO:0000269|PubMed:19176525}.; FUNCTION: [Isoform Beta-II]: Acts as an activator of ferroptosis by mediating phosphorylation and activation of ACSL4. Also stimulates ferroptosis propagation by catalyzing phosphorylation of FOXK1. {ECO:0000250|UniProtKB:P05771}.
uniprot
proteins
mass_dalton
76751
uniprot
proteins
mutagenesis
MUTAGEN 16..17; /note="ST->AA: No effect."; /evidence="ECO:0000269|PubMed:8327493"; MUTAGEN 314; /note="T->A: No effect; when associated with A-323."; /evidence="ECO:0000269|PubMed:8327493"; MUTAGEN 324; /note="T->A: No effect; when associated with A-313."; /evidence="ECO:0000269|PubMed:8327493"; MUTAGEN 500; /note="T->E: 50% increase of enzymatic activity."; /evidence="ECO:0000269|PubMed:7961692"; MUTAGEN 500; /note="T->S: 50% decrease of enzymatic activity."; /evidence="ECO:0000269|PubMed:7961692"; MUTAGEN 500; /note="T->V,D: Loss of enzymatic activity."; /evidence="ECO:0000269|PubMed:7961692"; MUTAGEN 635; /note="T->A: Loss of enzymatic activity; when associated with T-643 change in subcellular location, loss of PMA-induced down-regulation and loss of enzymatic activity."; /evidence="ECO:0000269|PubMed:8034726, ECO:0000269|PubMed:8327493"; MUTAGEN 642; /note="T->A: Loss of enzymatic activity; when associated with T-636 change in subcellular location, loss of PMA-induced down-regulation and loss of enzymatic activity."; /evidence="ECO:0000269|PubMed:8034726, ECO:0000269|PubMed:8327493
uniprot
proteins
post_translational_modification
PTM: Phosphorylation on Thr-500 of isoform beta-I, within the activation loop, renders it competent to autophosphorylate. Subsequent autophosphorylation of Thr-642 maintains catalytic competence, and autophosphorylation on Ser-661 appears to release the kinase into the cytosol. Similarly, isoform beta-II is autophosphorylated on 'Thr-641' and 'Ser-660', subsequent to phosphorylation on Thr-500. Autophosphorylated on other sites i.e. in the N-terminal and hinge regions have no effect on enzyme activity. Phosphorylation at Tyr-662 by SYK induces binding with GRB2 and contributes to the activation of MAPK/ERK signaling cascade. {ECO:0000269|PubMed:21215369, ECO:0000269|PubMed:7961692, ECO:0000269|PubMed:8327493, ECO:0000269|PubMed:8749392}.
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
10938109
uniprot
proteins
pubmed
11714718
uniprot
proteins
pubmed
19176525
uniprot
proteins
pubmed
21215369
uniprot
proteins
pubmed
22673903
uniprot
proteins
pubmed
2428667
uniprot
proteins
pubmed
3345563
uniprot
proteins
pubmed
3469647
uniprot
proteins
pubmed
3755379
uniprot
proteins
pubmed
3755404
uniprot
proteins
pubmed
7961692
uniprot
proteins
pubmed
8034726
uniprot
proteins
pubmed
8327493
uniprot
proteins
pubmed
8749392
uniprot
proteins
pubmed
9817842
uniprot
proteins
sequence_length
671
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm. Nucleus {ECO:0000250}. Membrane; Peripheral membrane protein.
uniprot
proteins