Prkcb
entrez
18751
canonical
uniprot
P68404
canonical
ensembl
ENSMUSG00000052889
resolver
ensp
ENSMUSP00000064812
resolver
ensp
ENSMUSP00000070019
resolver
genesymbol
Prkcb
resolver
genesymbol_syn
Pkcb
resolver
genesymbol_syn
Prkcb1
resolver
uniprot
A0JNZ5
resolver
uniprot
F2Z441
resolver
uniprot
P04410
resolver
uniprot
P04411
resolver
uniprot_entry
KPCB_MOUSE
resolver
uniprot_sec
A0JNZ5
resolver
uniprot_sec
F2Z441
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. Phosphorylates ATF2 which promotes cooperation between ATF2 and JUN, activating transcription (By similarity). 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:0000269|PubMed:10499500, ECO:0000269|PubMed:11805327, ECO:0000269|PubMed:12070292, ECO:0000269|PubMed:12118249, ECO:0000269|PubMed:16301747, ECO:0000269|PubMed:16356855, ECO:0000269|PubMed:16505232, ECO:0000269|PubMed:17272725, ECO:0000269|PubMed:8670417}.; 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
post_translational_modification
PTM: Phosphorylation on Thr-500 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. Autophosphorylation on other sites i.e. in the N-terminal and hinge regions have no effect on enzyme activity (By similarity). Phosphorylation at Tyr-662 by SYK induces binding with GRB2 and contributes to the activation of MAPK/ERK signaling cascade. {ECO:0000250, ECO:0000269|PubMed:12881490}.; PTM: [Isoform Beta-II]: In response to growth factors, phosphorylated at Thr-634 by the mTORC2 complex, promoting autophosphorylation and activation. {ECO:0000269|PubMed:33850054}.
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
10499500
uniprot
proteins
pubmed
11805327
uniprot
proteins
pubmed
12070292
uniprot
proteins
pubmed
12118249
uniprot
proteins
pubmed
12881490
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16301747
uniprot
proteins
pubmed
16356855
uniprot
proteins
pubmed
16452087
uniprot
proteins
pubmed
16505232
uniprot
proteins
pubmed
17114649
uniprot
proteins
pubmed
17272725
uniprot
proteins
pubmed
17962198
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
2402470
uniprot
proteins
pubmed
33850054
uniprot
proteins
pubmed
8670417
uniprot
proteins
sequence_length
671
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
uniprot
proteins