Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Protein kinase C beta type  

UniProtKB / Swiss-Prot ID :  KPCB_MOUSE

Gene Name (Synonyms) : 
Prkcb, Pkcb, Prkcb1  

Species :  Mus musculus (Mouse). 

Subcellular Localization :  Cytoplasm (By similarity). Nucleus (By similarity). Membrane; Peripheral membrane protein (By similarity). 

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). 

Protein Sequence MADPAAGPPPSEGEESTVRFARKGALRQKNVHEVKNHKFTARFFKQPTFCSHCTDFIWGFGKQGFQCQVC...
Predicted Secondary Structure CCCCCCCCCCCCCCCCCCCCCCCCCCHHHCCEECCCCEEEEECCCCCCCHHHHHHHHHHHHCCCCEECCC...
Protein Variant -
- top -

Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
- top -

Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
11PhosphoserineGPPPSEGEE
CCCCCCCCC
65.10SysPTM
Link-
195PhosphotyrosineLSDPYVKLK
CCCCHHHHC
18.40SysPTM
Link-
195Phosphotyrosine.LSDPYVKLK
CCCCHHHHC
18.40UniProtKB
Link-
217S-nitrosocysteineKTIKCSLNP
EEECCCCCC
5.03dbSNO
Link-
500PhosphothreonineVTTKTFCGT
CEEEEECCC
23.28SysPTM
Link-
642PhosphothreoninePVELTPTDK
CCCCCCCHH
15.61PhosphoELM
Link-
662Phosphotyrosine; by SYK.AGFSYTNPE
CCCCCCHHH
14.31UniProtKB
Link-
- top -

Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
There are no Protein-Protein Interactions.
- top -

Disease Reference
Drug Reference
- top -
Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A Ras activation pathway dependent on Syk phosphorylation of proteinkinase C.";
Kawakami Y., Kitaura J., Yao L., McHenry R.W., Kawakami Y.,Newton A.C., Kang S., Kato R.M., Leitges M., Rawlings D.J.,Kawakami T.;
Proc. Natl. Acad. Sci. U.S.A. 100:9470-9475(2003).
Cited for: PHOSPHORYLATION AT TYR-662.
"Large-scale identification and evolution indexing of tyrosinephosphorylation sites from murine brain.";
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
J. Proteome Res. 7:311-318(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-195, AND MASSSPECTROMETRY.
- top -
Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures