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Information on EC 2.7.11.13 - protein kinase C and Organism(s) Saccharomyces cerevisiae and UniProt Accession P24583

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IUBMB Comments
A family of serine- and threonine-specific protein kinases that depend on lipids for activity. They can be activated by calcium but have a requirement for the second messenger diacylglycerol. Members of this group of enzymes phosphorylate a wide variety of protein targets and are known to be involved in diverse cell-signalling pathways. Members of the protein kinase C family also serve as major receptors for phorbol esters, a class of tumour promoters.
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This record set is specific for:
Saccharomyces cerevisiae
UNIPROT: P24583
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Word Map
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The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
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ATP
+
a [protein]-(L-serine/L-threonine)
=
ADP
+
a [protein]-(L-serine/L-threonine) phosphate
+
a [protein]-(L-serine/L-threonine)
=
+
a [protein]-(L-serine/L-threonine) phosphate
Synonyms
protein kinase c, pkcalpha, pkc-alpha, pkc alpha, pkcepsilon, pkc-delta, pkczeta, pkc-epsilon, pkc delta, pkc-zeta, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
protein kinase C-like 1
-
Calcium-dependent protein kinase C
-
-
-
-
epsilonPKC
-
-
-
-
PKCdelta
-
isoform
protein kinase C
-
-
-
-
protein kinase-C
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
ATP:protein phosphotransferase (diacylglycerol-dependent)
A family of serine- and threonine-specific protein kinases that depend on lipids for activity. They can be activated by calcium but have a requirement for the second messenger diacylglycerol. Members of this group of enzymes phosphorylate a wide variety of protein targets and are known to be involved in diverse cell-signalling pathways. Members of the protein kinase C family also serve as major receptors for phorbol esters, a class of tumour promoters.
CAS REGISTRY NUMBER
COMMENTARY hide
141436-78-4
calcium-dependent protein kinase C
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + a protein
ADP + a phosphoprotein
show the reaction diagram
-
-
-
-
?
ATP + histone H2A
ADP + phosphorylated histone H2A
show the reaction diagram
-
-
-
-
?
ATP + Rad53 protein
ADP + phosphorylated Rad53 protein
show the reaction diagram
-
-
-
-
?
ATP + Xras2 protein
ADP + phosphorylated Xrs2 protein
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + a protein
ADP + a phosphoprotein
show the reaction diagram
-
-
-
-
?
ATP + histone H2A
ADP + phosphorylated histone H2A
show the reaction diagram
-
-
-
-
?
ATP + Rad53 protein
ADP + phosphorylated Rad53 protein
show the reaction diagram
-
-
-
-
?
ATP + Xras2 protein
ADP + phosphorylated Xrs2 protein
show the reaction diagram
-
-
-
-
?
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
QLMGGLHRHGAIINRKE
-
autoregulatory pseudosubstrate sequence, residues 391-407
Tween 80
-
inhibits the enzyme at high concentration
additional information
-
synthesis of peptides behaving as pseudosubstrates, determination of inhibitory potential
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
-
Ki values of the pseudosubstrates in nano- to micromolar range
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
-
the enzyme is required for activation of checkpoint kinases Mec1 and Tel1. Isoform PKCdelta is able to activate the DNA integrity checkpoint
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kemp, B.E.; Pearson, R.B.; House, M.
Pseudosubstrate-based peptide inhibitors
Methods Enzymol.
201
287-304
1991
Saccharomyces cerevisiae, Drosophila melanogaster, eukaryota, Homo sapiens
Manually annotated by BRENDA team
Baymiller, J.; McCullough, J.E.
Saccharomyces cerevisiae cell lysis mutations cly5 and cly7 define temperature-sensitive alleles of PKC1, the gene encoding yeast protein kinase C
Yeast
13
305-312
1997
Saccharomyces cerevisiae (P24583), Saccharomyces cerevisiae
Manually annotated by BRENDA team
Obermaier, B.; Gassenhuber, J.; Piravandi, E.; Domdey, H.
Sequence analysis of a 78.6 kb segment of the left end of Saccharomyces cerevisiae chromosome II
Yeast
11
1103-1112
1995
Saccharomyces cerevisiae (P24583)
Manually annotated by BRENDA team
Levin, D.E.; Fields, F.O.; Kunisawa, R.; Bishop, J.M.; Thorner, J.
A candidate protein kinase C gene, PKC1, is required for the S. cerevisiae cell cycle
Cell
62
213-224
1990
Saccharomyces cerevisiae (P24583), Saccharomyces cerevisiae
Manually annotated by BRENDA team
Igual, J.
Protein kinase C controls activation of the DNA integrity checkpoint
Nucleic Acids Res.
42
7084-7095
2014
Saccharomyces cerevisiae
Manually annotated by BRENDA team