EzCatDB: M00221
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DB codeM00221
CATH domainDomain 12.60.40.150 : Immunoglobulin-like
Domain 23.30.60.- : Wheat Germ Agglutinin (Isolectin 2); domain 1
Domain 33.30.60.- : Wheat Germ Agglutinin (Isolectin 2); domain 1
Domain 43.30.200.- : Phosphorylase Kinase; domain 1
Domain 51.10.510.- : Transferase(Phosphotransferase); domain 1
Domain 6-.-.-.-
E.C.2.7.11.13

CATH domainRelated DB codes (homologues)
2.60.40.150 : Immunoglobulin-likeM00183,M00043,M00118

Enzyme Name
UniProtKBKEGG

P09215
Protein nameProtein kinase C delta typeprotein 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
SynonymsEC 2.7.11.13
nPKC-delta
RefSeqNP_579841.1 (Protein)
NM_133307.1 (DNA/RNA sequence)
PfamPF00130 (C1_1)
PF00069 (Pkinase)
PF00433 (Pkinase_C)
[Graphical view]

KEGG pathways
MAP codePathways
MAP04070Phosphatidylinositol signaling system

UniProtKB:Accession NumberP09215
Entry nameKPCD_RAT
ActivityATP + a protein = ADP + a phosphoprotein.
SubunitInteracts with PDK1, CDCP1, RAD9A and MUC1 (By similarity).
Subcellular locationCytoplasm. Membrane, Peripheral membrane protein.
Cofactor

Compound table: links to PDB-related databases & PoSSuM

SubstratesProducts
KEGG-idC00002C00017C00008C00562
CompoundATPProteinADPPhosphoprotein
Typeamine group,nucleotidepeptide/proteinamine group,nucleotidepeptide/protein,phosphate group/phosphate ion
ChEBI15422

16761

PubChem5957

6022

            
1bdyAUnboundUnboundUnboundUnbound
1bdyBUnboundUnboundUnboundUnbound

Active-site residues
resource
literature [2]
pdbModified residues
         
1bdyATYR 52(phospholylated)
1bdyBTYR 52(phospholylated)


references
[1]
PubMed ID9761878
JournalActa Crystallogr D Biol Crystallogr
Year1998
Volume54
Pages693-6
AuthorsPappa H, Dekker LV, Parker PJ, McDonald NQ
TitlePreliminary X-ray analysis of a C2-like domain from protein kinase C-delta.
[2]
CommentsX-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1-123
Medline ID98362592
PubMed ID9687370
JournalStructure
Year1998
Volume6
Pages885-94
AuthorsPappa H, Murray-Rust J, Dekker LV, Parker PJ, McDonald NQ
TitleCrystal structure of the C2 domain from protein kinase C-delta.
Related PDB1bdy
Related UniProtKBP09215
[3]
PubMed ID11518534
JournalJ Mol Biol
Year2001
Volume311
Pages837-49
AuthorsOchoa WF, Garcia-Garcia J, Fita I, Corbalan-Garcia S, Verdaguer N, Gomez-Fernandez JC
TitleStructure of the C2 domain from novel protein kinase Cepsilon. A membrane binding model for Ca(2+)-independent C2 domains.
[4]
PubMed ID12460119
JournalBiochem J
Year2003
Volume370
Pages901-12
AuthorsRaghunath A, Ling M, Larsson C
TitleThe catalytic domain limits the translocation of protein kinase C alpha in response to increases in Ca2+ and diacylglycerol.

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]).

createdupdated
2003-07-312009-03-23


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Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2006)
Funded by Grant-in-Aid for Scientific Research (B)/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (September 2005 - September 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (October 2007 - September 2010)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2011 - March 2012)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2012 - March 2013)
Supported by the commission for the Development of Artificial Gene Synthesis Technology for Creating Innovative Biomaterial from the Ministry of Economy, Trade and Industry (METI) (October 2012 - )
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