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Information on EC 2.7.11.13 - protein kinase C and Organism(s) Aplysia californica and UniProt Accession Q16975

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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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Aplysia californica
UNIPROT: Q16975
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Word Map
The taxonomic range for the selected organisms is: Aplysia californica
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
calcium-independent protein kinase C
-
Calcium-dependent protein kinase C
epsilonPKC
-
-
-
-
PKC
-
-
-
-
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
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
phosphatidylserine
phosphatidylserine
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?
KPC2_APLCA
743
0
84414
Swiss-Prot
other Location (Reliability: 5)
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Pepio, A.M.; Fan, X.; Sossin, W.S.
The role of C2 domains in Ca2+-activated and Ca2+-independent protein kinase Cs in aplysia
J. Biol. Chem.
273
19040-19048
1998
Aplysia californica (Q16974), Aplysia californica (Q16975)
Manually annotated by BRENDA team
Sossin, W.S.; Diaz-Arrastia, R.; Schwartz, J.H.
Characterization of two isoforms of protein kinase C in the nervous system of Aplysia californica
J. Biol. Chem.
268
5763-5768
1993
Aplysia californica (Q16974), Aplysia californica (Q16975), Aplysia californica
Manually annotated by BRENDA team
Kruger, K.E.; Sossin, W.S.; Sacktor, T.C.; Bergold, P.J.; Beushausen, S.; Schwartz, J.H.
Cloning and characterization of Ca2+-dependent and Ca2+-independent PKCs expressed in Aplysia sensory cells
J. Neurosci.
11
2303-2313
1991
Aplysia californica (Q16974), Aplysia californica (Q16975)
Manually annotated by BRENDA team
Pepio, A.M.; Sossin, W.S.
The C2 domain of the Ca2+-independent protein kinase C Apl II inhibits phorbol ester binding to the C1 domain in a phosphatidic acid-sensitive manner
Biochemistry
37
1256-1263
1998
Aplysia californica (Q16975)
Manually annotated by BRENDA team
Sossin, W.S.; Schwartz, J.H.
Ca2+-independent protein kinase Cs contain an amino-terminal domain similar to the C2 consensus sequence
Trends Biochem. Sci.
18
207-208
1993
Aplysia californica (Q16975)
Manually annotated by BRENDA team