Target name

P05771: Protein kinase C beta type


  Protein 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. May participate in the regulation of glucose transport in adipocytes by negatively modulating the insulin-stimulated translocation of the glucose transporter SLC2A4/GLUT4. 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.

  Database links

Uniprot primary ID P05771
PDB ID 2I0E
DrugBank ID DB00163 DB00675
BioGrid ID 111565
GuidetoPHARMACOLOGY ID 1483
PharmGKB ID PA33761
KEGG ID hsa:5579
DIP ID DIP-34187N
STRING ID 9606.ENSP00000305355
IntAct ID P05771
DMDM 20141488
BRENDA 2.7.11.13
Reactome R-HSA-4419969 R-HSA-418597 R-HSA-76005 R-HSA-416993 R-HSA-5099900 R-HSA-1169091 R-HSA-5218921 R-HSA-114516
SignaLink P05771
BioCyc
Entrez Gene (Gene ID) 5579
BindingDB P05771

  Model Performance Metrics

Fingerprint type Sensitivity SEN_std Specificity SPE_std Accuracy ACC_std F1-score F1-score_std AUC AUC_std MCC MCC_std Download model
FP2 fingerprints 0.696 0.008 0.974 0.000 0.835 0.005 0.810 0.005 0.920 0.000 0.697 0.007 Download
Estate fingerprints 0.757 0.008 0.715 0.013 0.736 0.008 0.740 0.007 0.828 0.006 0.471 0.013 Download
MACCS fingerprints 0.792 0.004 0.786 0.012 0.789 0.006 0.791 0.003 0.879 0.003 0.578 0.013 Download
Daylight fingerprints 0.743 0.005 0.897 0.003 0.820 0.000 0.804 0.005 0.869 0.003 0.648 0.006 Download
ECFP2 fingerprints 0.872 0.010 0.918 0.005 0.895 0.005 0.894 0.005 0.955 0.005 0.793 0.012 Download
ECFP4 fingerprints 0.888 0.006 0.976 0.003 0.932 0.004 0.929 0.006 0.979 0.003 0.870 0.007 Download
ECFP6 fingerprints 0.842 0.006 0.992 0.000 0.917 0.005 0.909 0.003 0.970 0.000 0.841 0.009 Download

  Download datasets

Positive dataset Negative dataset


Copyright @ 2012-2014 Computational Biology & Drug Design Group,
School of Pharmaceutical Sciences, Central South University. All rights reserved.

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