Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 2.7.11.13 - protein kinase C and Organism(s) Drosophila melanogaster and UniProt Accession P05130

for references in articles please use BRENDA:EC2.7.11.13
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
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.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Drosophila melanogaster
UNIPROT: P05130
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
The taxonomic range for the selected organisms is: Drosophila melanogaster
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
+
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, brain isoenzyme
-
Calcium-dependent protein kinase C
-
-
-
-
epsilonPKC
-
-
-
-
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
-
-
-
-
?
additional information
?
-
-
substrate specificity
-
-
?
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
-
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NKMKSRLRKGALKKNV
-
autoregulatory pseudosubstrate sequence, residues 24-40
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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
KPC1_DROME
679
0
77695
Swiss-Prot
other Location (Reliability: 1)
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
structure and nucleotide sequence of a Drosophila melanogaster protein kinase C gene
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
Rosenthal, A.; Rhee, L.; Yadegari, R.; Paro, R.; Ullrich, A.; Goeddel, D.V.
Structure and nucleotide sequence of a Drosophila melanogaster protein kinase C gene
EMBO J.
6
433-441
1987
Drosophila melanogaster (P05130), Drosophila melanogaster
Manually annotated by BRENDA team
Schaeffer, E.; Smith, D.; Mardon, G.; Quinn, W.; Zuker, C.
Isolation and characterization of two new Drosophila protein kinase C genes, including one specifically expressed in photoreceptor cells
Cell
57
403-412
1989
Drosophila melanogaster (P13678)
Manually annotated by BRENDA team