Prkcb | ENSRNOG00000012061 | NCBI 25023

Details for: Prkcb

Gene ID: 25023

Symbol: Prkcb

Ensembl ID: ENSRNOG00000012061

Description: protein kinase C, beta

Associated with

Activation of nf-kappab in b cells
(R-RNO-1169091)
Adaptive immune system
(R-RNO-1280218)
Beta-catenin independent wnt signaling
(R-RNO-3858494)
Cell cycle
(R-RNO-1640170)
Cell cycle, mitotic
(R-RNO-69278)
Depolymerization of the nuclear lamina
(R-RNO-4419969)
Disinhibition of snare formation
(R-RNO-114516)
Downstream signaling events of b cell receptor (bcr)
(R-RNO-1168372)
Glutamate binding, activation of ampa receptors and synaptic plasticity
(R-RNO-399721)
Hemostasis
(R-RNO-109582)
Immune system
(R-RNO-168256)
Mitotic prophase
(R-RNO-68875)
M phase
(R-RNO-68886)
Neuronal system
(R-RNO-112316)
Neurotransmitter receptors and postsynaptic signal transmission
(R-RNO-112314)
Nuclear envelope breakdown
(R-RNO-2980766)
Pcp/ce pathway
(R-RNO-4086400)
Platelet activation, signaling and aggregation
(R-RNO-76002)
Response to elevated platelet cytosolic ca2+
(R-RNO-76005)
Rho gtpase effectors
(R-RNO-195258)
Rho gtpases activate nadph oxidases
(R-RNO-5668599)
Signaling by receptor tyrosine kinases
(R-RNO-9006934)
Signaling by rho gtpases
(R-RNO-194315)
Signaling by rho gtpases, miro gtpases and rhobtb3
(R-RNO-9716542)
Signaling by the b cell receptor (bcr)
(R-RNO-983705)
Signaling by vegf
(R-RNO-194138)
Signaling by wnt
(R-RNO-195721)
Signal transduction
(R-RNO-162582)
Trafficking of ampa receptors
(R-RNO-399719)
Trafficking of glur2-containing ampa receptors
(R-RNO-416993)
Transmission across chemical synapses
(R-RNO-112315)
Vegfa-vegfr2 pathway
(R-RNO-4420097)
Vegfr2 mediated cell proliferation
(R-RNO-5218921)
Wnt5a-dependent internalization of fzd4
(R-RNO-5099900)
Adaptive immune response
(GO:0002250)
Apoptotic process
(GO:0006915)
Atp binding
(GO:0005524)
B cell activation
(GO:0042113)
B cell receptor signaling pathway
(GO:0050853)
Brush border membrane
(GO:0031526)
Calcium channel regulator activity
(GO:0005246)
Calcium ion transport
(GO:0006816)
Calyx of held
(GO:0044305)
Cellular response to carbohydrate stimulus
(GO:0071322)
Centrosome
(GO:0005813)
Chromatin binding
(GO:0003682)
Chromatin remodeling
(GO:0006338)
Cytoplasm
(GO:0005737)
Cytosol
(GO:0005829)
Diacylglycerol-dependent serine/threonine kinase activity
(GO:0004697)
Dibenzo-p-dioxin metabolic process
(GO:0018894)
Histone binding
(GO:0042393)
Histone h3t6 kinase activity
(GO:0035403)
Intracellular calcium ion homeostasis
(GO:0006874)
Intracellular signal transduction
(GO:0035556)
Membrane
(GO:0016020)
Negative regulation of glucose transmembrane transport
(GO:0010829)
Negative regulation of insulin receptor signaling pathway
(GO:0046627)
Nuclear androgen receptor binding
(GO:0050681)
Nuclear receptor coactivator activity
(GO:0030374)
Nucleoplasm
(GO:0005654)
Nucleus
(GO:0005634)
Peptidyl-serine phosphorylation
(GO:0018105)
Phospholipase c-activating g protein-coupled acetylcholine receptor signaling pathway
(GO:0007207)
Phosphorylation
(GO:0016310)
Plasma membrane
(GO:0005886)
Positive regulation of angiogenesis
(GO:0045766)
Positive regulation of b cell receptor signaling pathway
(GO:0050861)
Positive regulation of canonical nf-kappab signal transduction
(GO:0043123)
Positive regulation of dna-templated transcription
(GO:0045893)
Positive regulation of insulin secretion
(GO:0032024)
Positive regulation of odontogenesis of dentin-containing tooth
(GO:0042488)
Positive regulation of vascular endothelial growth factor receptor signaling pathway
(GO:0030949)
Post-translational protein modification
(GO:0043687)
Presynapse
(GO:0098793)
Presynaptic cytosol
(GO:0099523)
Presynaptic modulation of chemical synaptic transmission
(GO:0099171)
Protein binding
(GO:0005515)
Protein kinase c binding
(GO:0005080)
Protein serine/threonine kinase activity
(GO:0004674)
Protein serine kinase activity
(GO:0106310)
Regulation of dopamine secretion
(GO:0014059)
Regulation of glucose transmembrane transport
(GO:0010827)
Regulation of growth
(GO:0040008)
Regulation of synaptic vesicle exocytosis
(GO:2000300)
Regulation of transcription by rna polymerase ii
(GO:0006357)
Response to ethanol
(GO:0045471)
Response to glucose
(GO:0009749)
Response to hypoxia
(GO:0001666)
Response to vitamin d
(GO:0033280)
Response to xenobiotic stimulus
(GO:0009410)
Spectrin
(GO:0008091)
Zinc ion binding
(GO:0008270)

Other Information

Proteins

Protein kinase C beta type

Genular Protein ID: 2191395147

Symbol: KPCB_RAT

Name: Protein kinase C beta type

UniProtKB Accession Codes:

P68403 P04410 P04411

Database IDs:

Citations:

PubMed ID: 3755379

Title: Cloning and expression of multiple protein kinase C cDNAs.

PubMed ID: 3755379

DOI: 10.1016/0092-8674(86)90874-3

PubMed ID: 2428667

Title: Two types of complementary DNAs of rat brain protein kinase C. Heterogeneity determined by alternative splicing.

PubMed ID: 2428667

DOI: 10.1016/0014-5793(86)81010-9

PubMed ID: 3345563

Title: Overproduction of protein kinase C causes disordered growth control in rat fibroblasts.

PubMed ID: 3345563

DOI: 10.1016/s0092-8674(88)80027-8

PubMed ID: 3755404

Title: Cloning of rat brain protein kinase C complementary DNA.

PubMed ID: 3755404

DOI: 10.1016/0014-5793(86)80724-4

PubMed ID: 3469647

Title: Isolation of cDNA clones encoding protein kinase C: evidence for a protein kinase C-related gene family.

PubMed ID: 3469647

DOI: 10.1073/pnas.84.4.1065

PubMed ID: 8749392

Title: Protein kinase C is regulated in vivo by three functionally distinct phosphorylations.

PubMed ID: 8749392

DOI: 10.1016/s0960-9822(95)00277-6

PubMed ID: 8327493

Title: Characterization of site-specific mutants altered at protein kinase C beta 1 isozyme autophosphorylation sites.

PubMed ID: 8327493

DOI: 10.1073/pnas.90.13.6130

PubMed ID: 8034726

Title: Phosphorylation of Thr642 is an early event in the processing of newly synthesized protein kinase C beta 1 and is essential for its activation.

PubMed ID: 8034726

DOI: 10.1016/s0021-9258(17)32208-1

PubMed ID: 7961692

Title: Requirement for negative charge on 'activation loop' of protein kinase C.

PubMed ID: 7961692

DOI: 10.1016/s0021-9258(18)47044-5

PubMed ID: 10938109

Title: Insulin-activated protein kinase Cbeta bypasses Ras and stimulates mitogen-activated protein kinase activity and cell proliferation in muscle cells.

PubMed ID: 10938109

DOI: 10.1128/mcb.20.17.6323-6333.2000

PubMed ID: 11714718

Title: Involvement of protein kinase C beta 2 in c-myc induction by high glucose in pancreatic beta-cells.

PubMed ID: 11714718

DOI: 10.1074/jbc.m109647200

PubMed ID: 19176525

Title: Phosphorylation of activation transcription factor-2 at serine 121 by protein kinase c controls c-Jun-mediated activation of transcription.

PubMed ID: 19176525

DOI: 10.1074/jbc.m808719200

PubMed ID: 22673903

Title: Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues.

PubMed ID: 22673903

DOI: 10.1038/ncomms1871

PubMed ID: 9817842

Title: Structure of the protein kinase Cbeta phospholipid-binding C2 domain complexed with Ca2+.

PubMed ID: 9817842

DOI: 10.1016/s0969-2126(98)00139-7

PubMed ID: 21215369

Title: Crystal structure and allosteric activation of protein kinase C betaII.

PubMed ID: 21215369

DOI: 10.1016/j.cell.2010.12.013

Sequence Information:

Length: 671
Mass: 76751
Checksum: A1935030F758513C
Sequence:

MADPAAGPPP SEGEESTVRF ARKGALRQKN VHEVKNHKFT ARFFKQPTFC SHCTDFIWGF 
GKQGFQCQVC CFVVHKRCHE FVTFSCPGAD KGPASDDPRS KHKFKIHTYS SPTFCDHCGS 
LLYGLIHQGM KCDTCMMNVH KRCVMNVPSL CGTDHTERRG RIYIQAHIDR EVLIVVVRDA 
KNLVPMDPNG LSDPYVKLKL IPDPKSESKQ KTKTIKCSLN PEWNETFRFQ LKESDKDRRL 
SVEIWDWDLT SRNDFMGSLS FGISELQKAG VDGWFKLLSQ EEGEYFNVPV PPEGSEGNEE 
LRQKFERAKI GQGTKAPEEK TANTISKFDN NGNRDRMKLT DFNFLMVLGK GSFGKVMLSE 
RKGTDELYAV KILKKDVVIQ DDDVECTMVE KRVLALPGKP PFLTQLHSCF QTMDRLYFVM 
EYVNGGDLMY HIQQVGRFKE PHAVFYAAEI AIGLFFLQSK GIIYRDLKLD NVMLDSEGHI 
KIADFGMCKE NIWDGVTTKT FCGTPDYIAP EIIAYQPYGK SVDWWAFGVL LYEMLAGQAP 
FEGEDEDELF QSIMEHNVAY PKSMSKEAVA ICKGLMTKHP GKRLGCGPEG ERDIKEHAFF 
RYIDWEKLER KEIQPPYKPK ARDKRDTSNF DKEFTRQPVE LTPTDKLFIM NLDQNEFAGF 
SYTNPEFVIN V

The gene details are incomplete or unavailable at the moment.

Database document:

This is a preview of the gene's schema. Only a few entries are kept for 'singleCellExpressions,' 'mRNAExpressions,' and other large data arrays for visualization purposes. You can zoom in with the mouse wheel for a closer view, and the text will adjust automatically if necessary. For the full schema, download it here.

Details for: Prkcb

Associated with

Other Information

Cloning and expression of multiple protein kinase C cDNAs. PubMed ID: 3755379

Two types of complementary DNAs of rat brain protein kinase C. Heterogeneity determined by alternative splicing. PubMed ID: 2428667

Overproduction of protein kinase C causes disordered growth control in rat fibroblasts. PubMed ID: 3345563

Cloning of rat brain protein kinase C complementary DNA. PubMed ID: 3755404

Isolation of cDNA clones encoding protein kinase C: evidence for a protein kinase C-related gene family. PubMed ID: 3469647

Protein kinase C is regulated in vivo by three functionally distinct phosphorylations. PubMed ID: 8749392

Characterization of site-specific mutants altered at protein kinase C beta 1 isozyme autophosphorylation sites. PubMed ID: 8327493

Phosphorylation of Thr642 is an early event in the processing of newly synthesized protein kinase C beta 1 and is essential for its activation. PubMed ID: 8034726

Requirement for negative charge on 'activation loop' of protein kinase C. PubMed ID: 7961692

Insulin-activated protein kinase Cbeta bypasses Ras and stimulates mitogen-activated protein kinase activity and cell proliferation in muscle cells. PubMed ID: 10938109

Involvement of protein kinase C beta 2 in c-myc induction by high glucose in pancreatic beta-cells. PubMed ID: 11714718

Phosphorylation of activation transcription factor-2 at serine 121 by protein kinase c controls c-Jun-mediated activation of transcription. PubMed ID: 19176525

Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues. PubMed ID: 22673903

Structure of the protein kinase Cbeta phospholipid-binding C2 domain complexed with Ca2+. PubMed ID: 9817842

Crystal structure and allosteric activation of protein kinase C betaII. PubMed ID: 21215369