Relation Results

Summary

Name PRKCB
Full Name Protein kinase C beta type
Synonyms PKC-B, PKC-beta | PKCB, PRKCB1
Primary ID P05771-2
Links - -
Type protein
Relations 4
Function Calcium-activated, phospholipid- and diacylglycerol (DAG)-dependent serine/threonine-protein kinase involved in various cellular processes such as reg ...
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Type: Score: Layout: SPV 
0.4390.461PPP2CAPRKCBPPP2CB

Modifications Tables

Relations

Regulator
Mechanism
target
score
+ down-regulates activity img/direct_inhibition.png dephosphorylation PRKCB (isoform 2) 0.439
Identifier Residue Sequence Organism Cell Line
SIGNOR-248621 Ser660 QSEFEGFsFVNSEFL Rattus norvegicus
pmid sentence
Inhibition of PP2A increased phosphorylation at Ser660 that determines calcium sensitivity and activity of PKCbetaII isoform
Identifier Residue Sequence Organism Cell Line
SIGNOR-248622 Thr641 TRHPPVLtPPDQEVI Rattus norvegicus
pmid sentence
Specifically, the threonine at position 500 (T500) on the activation loop, and T641 and S660 on the carboxyl terminus of protein kinase C beta II are phosphorylated in vivo. T500 and S660 are selectively dephosphorylated in vitro by protein phosphatase 2A to yield an enzyme that is still capable of lipid-dependent activation, whereas all three residues are dephosphorylated by protein phosphatase 1 to yield an inactive enzyme.
Publications: 2 Organism: Rattus Norvegicus
+ down-regulates activity img/direct_inhibition.png dephosphorylation PRKCB (isoform 2) 0.461
Identifier Residue Sequence Organism Cell Line
SIGNOR-248586 Ser660 QSEFEGFsFVNSEFL Rattus norvegicus
pmid sentence
Inhibition of PP2A increased phosphorylation at Ser660 that determines calcium sensitivity and activity of PKCbetaII isoform
Identifier Residue Sequence Organism Cell Line
SIGNOR-248587 Thr641 TRHPPVLtPPDQEVI Rattus norvegicus
pmid sentence
Specifically, the threonine at position 500 (T500) on the activation loop, and T641 and S660 on the carboxyl terminus of protein kinase C beta II are phosphorylated in vivo. T500 and S660 are selectively dephosphorylated in vitro by protein phosphatase 2A to yield an enzyme that is still capable of lipid-dependent activation, whereas all three residues are dephosphorylated by protein phosphatase 1 to yield an inactive enzyme.
Publications: 2 Organism: Rattus Norvegicus
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