DB code: M00221

CATH domain 2.60.40.150 : Immunoglobulin-like
3.30.60.- : Wheat Germ Agglutinin (Isolectin 2); domain 1
3.30.60.- : Wheat Germ Agglutinin (Isolectin 2); domain 1
3.30.200.- : Phosphorylase Kinase; domain 1
1.10.510.- : Transferase(Phosphotransferase); domain 1
-.-.-.- :
E.C. 2.7.11.13
CSA
M-CSA
MACiE

CATH domain Related DB codes (homologues)
2.60.40.150 : Immunoglobulin-like M00183 M00043 M00118

Uniprot Enzyme Name
UniprotKB Protein name Synonyms RefSeq Pfam
P09215 Protein kinase C delta type
EC 2.7.11.13
nPKC-delta
NP_579841.1 (Protein)
NM_133307.1 (DNA/RNA sequence)
PF00130 (C1_1)
PF00069 (Pkinase)
PF00433 (Pkinase_C)
[Graphical View]

KEGG enzyme name
protein kinase C
calcium-dependent protein kinase C
calcium-independent protein kinase C
calcium/phospholipid dependent protein kinase
cPKCalpha
cPKCbeta
cPKCgamma
nPKCdelta
nPKCepsilon
nPKC
nPKC
PKC
PKCalpha
PKCbeta
PKCgamma
PKCdelta
PKCepsilon
PKCzeta
Pkc1p
protein kinase Cepsilon
STK24

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
P09215 KPCD_RAT ATP + a protein = ADP + a phosphoprotein. Interacts with PDK1, CDCP1, RAD9A and MUC1 (By similarity). Cytoplasm. Membrane, Peripheral membrane protein.

KEGG Pathways
Map code Pathways E.C.
MAP04070 Phosphatidylinositol signaling system

Compound table
Substrates Products Intermediates
KEGG-id C00002 C00017 C00008 C00562
E.C.
Compound ATP Protein ADP Phosphoprotein
Type amine group,nucleotide peptide/protein amine group,nucleotide peptide/protein,phosphate group/phosphate ion
ChEBI 15422
 15422
 		16761
 16761
PubChem 5957
 5957
 		6022
 6022
1bdyA Unbound Unbound Unbound Unbound
1bdyB Unbound Unbound Unbound Unbound

Reference for Active-site residues
resource references E.C.
literature [2]

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1bdyA TYR 52(phospholylated)
1bdyB TYR 52(phospholylated)

References for Catalytic Mechanism
References Sections No. of steps in catalysis

References
[1]
Resource
Comments
Medline ID
PubMed ID 9761878
Journal Acta Crystallogr D Biol Crystallogr
Year 1998
Volume 54
Pages 693-6
Authors Pappa H, Dekker LV, Parker PJ, McDonald NQ
Title Preliminary X-ray analysis of a C2-like domain from protein kinase C-delta.
Related PDB
Related UniProtKB
[2]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1-123
Medline ID 98362592
PubMed ID 9687370
Journal Structure
Year 1998
Volume 6
Pages 885-94
Authors Pappa H, Murray-Rust J, Dekker LV, Parker PJ, McDonald NQ
Title Crystal structure of the C2 domain from protein kinase C-delta.
Related PDB 1bdy
Related UniProtKB P09215
[3]
Resource
Comments
Medline ID
PubMed ID 11518534
Journal J Mol Biol
Year 2001
Volume 311
Pages 837-49
Authors Ochoa WF, Garcia-Garcia J, Fita I, Corbalan-Garcia S, Verdaguer N, Gomez-Fernandez JC
Title Structure of the C2 domain from novel protein kinase Cepsilon. A membrane binding model for Ca(2+)-independent C2 domains.
Related PDB
Related UniProtKB
[4]
Resource
Comments
Medline ID
PubMed ID 12460119
Journal Biochem J
Year 2003
Volume 370
Pages 901-12
Authors Raghunath A, Ling M, Larsson C
Title The catalytic domain limits the translocation of protein kinase C alpha in response to increases in Ca2+ and diacylglycerol.
Related PDB
Related UniProtKB

Comments
The E.C. number was transferred from 2.7.1.37 to 2.7.11.13
For this enzyme, only the tertiary structure of the N-terminal domain has been solved so far. The N-terminal domain is called C2 domain (PDB 1bdy, KPCD_RAT;P09215, residues 1-123), which serves to translocate protein kinase C to the plasma membrane, rather than acts as a catalytic domain (see paper [2]).

Created Updated
2003-07-31 2009-03-23