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Protein kinase C delta type (EC 2.7.11.13) (Tyrosine-protein kinase PRKCD) (EC 2.7.10.2) (nPKC-delta) [Cleaved into: Protein kinase C delta type regulatory subunit; Protein kinase C delta type catalytic subunit (Sphingosine-dependent protein kinase-1) (SDK1)]

 KPCD_MOUSE              Reviewed;         674 AA.
P28867; Q91V85; Q9Z333;
01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
27-MAR-2002, sequence version 3.
25-OCT-2017, entry version 188.
RecName: Full=Protein kinase C delta type;
EC=2.7.11.13;
AltName: Full=Tyrosine-protein kinase PRKCD;
EC=2.7.10.2;
AltName: Full=nPKC-delta;
Contains:
RecName: Full=Protein kinase C delta type regulatory subunit;
Contains:
RecName: Full=Protein kinase C delta type catalytic subunit;
AltName: Full=Sphingosine-dependent protein kinase-1;
Short=SDK1;
Name=Prkcd; Synonyms=Pkcd;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=1868068; DOI=10.1021/bi00246a008;
Mischak H., Bodenteich A., Kolch W., Goodnight J., Hofer F.,
Mushinski J.F.;
"Mouse protein kinase C-delta, the major isoform expressed in mouse
hemopoietic cells: sequence of the cDNA, expression patterns, and
characterization of the protein.";
Biochemistry 30:7925-7931(1991).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
STRAIN=ICR; TISSUE=Brain;
PubMed=1765103; DOI=10.1111/j.1432-1033.1991.tb16453.x;
Mizuno K., Kubo K., Saido T.C., Akita Y., Osada S., Kuroki T.,
Ohno S., Suzuki K.;
"Structure and properties of a ubiquitously expressed protein kinase
C, nPKC delta.";
Eur. J. Biochem. 202:931-940(1991).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
STRAIN=129/SvJ;
Wheeler D.L., Gillis M.E., Verma A.K.;
"Intron/exon structure of the murine protein kinase C delta gene.";
Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
PubMed=11558579; DOI=10.1248/bpb.24.973;
Sakurai Y., Onishi Y., Tanimoto Y., Kizaki H.;
"Novel protein kinase C delta isoform insensitive to caspase-3.";
Biol. Pharm. Bull. 24:973-977(2001).
[5]
INTERACTION WITH CAVIN3.
PubMed=9054438; DOI=10.1074/jbc.272.11.7381;
Izumi Y., Hirai S., Tamai Y., Fujise-Matsuoka A., Nishimura Y.,
Ohno S.;
"A protein kinase Cdelta-binding protein SRBC whose expression is
induced by serum starvation.";
J. Biol. Chem. 272:7381-7389(1997).
[6]
FUNCTION.
PubMed=9705322; DOI=10.1074/jbc.273.34.21834;
Megidish T., Cooper J., Zhang L., Fu H., Hakomori S.;
"A novel sphingosine-dependent protein kinase (SDK1) specifically
phosphorylates certain isoforms of 14-3-3 protein.";
J. Biol. Chem. 273:21834-21845(1998).
[7]
FUNCTION.
PubMed=11976686; DOI=10.1038/416860a;
Mecklenbraeuker I., Saijo K., Zheng N.Y., Leitges M., Tarakhovsky A.;
"Protein kinase Cdelta controls self-antigen-induced B-cell
tolerance.";
Nature 416:860-865(2002).
[8]
PHOSPHORYLATION AT THR-505.
PubMed=9748166; DOI=10.1126/science.281.5385.2042;
Le Good J.A., Ziegler W.H., Parekh D.B., Alessi D.R., Cohen P.,
Parker P.J.;
"Protein kinase C isotypes controlled by phosphoinositide 3-kinase
through the protein kinase PDK1.";
Science 281:2042-2045(1998).
[9]
DISRUPTION PHENOTYPE, FUNCTION IN B CELL PROLIFERATION, AND FUNCTION
IN B-CELL IMMUNE RESPONSES.
PubMed=11976687; DOI=10.1038/416865a;
Miyamoto A., Nakayama K., Imaki H., Hirose S., Jiang Y., Abe M.,
Tsukiyama T., Nagahama H., Ohno S., Hatakeyama S., Nakayama K.I.;
"Increased proliferation of B cells and auto-immunity in mice lacking
protein kinase Cdelta.";
Nature 416:865-869(2002).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-311, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Mast cell;
PubMed=17947660; DOI=10.4049/jimmunol.179.9.5864;
Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
Kawakami T., Salomon A.R.;
"Quantitative time-resolved phosphoproteomic analysis of mast cell
signaling.";
J. Immunol. 179:5864-5876(2007).
[11]
FUNCTION, AND PHOSPHORYLATION AT THR-505.
PubMed=18025218; DOI=10.4049/jimmunol.179.11.7720;
Cheng N., He R., Tian J., Dinauer M.C., Ye R.D.;
"A critical role of protein kinase C delta activation loop
phosphorylation in formyl-methionyl-leucyl-phenylalanine-induced
phosphorylation of p47(phox) and rapid activation of nicotinamide
adenine dinucleotide phosphate oxidase.";
J. Immunol. 179:7720-7728(2007).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-311, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=18034455; DOI=10.1021/pr0701254;
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
"Large-scale identification and evolution indexing of tyrosine
phosphorylation sites from murine brain.";
J. Proteome Res. 7:311-318(2008).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-43; TYR-311 AND SER-662,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
Thibault P.;
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Immunity 30:143-154(2009).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-311, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic fibroblast;
PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
"Large scale localization of protein phosphorylation by use of
electron capture dissociation mass spectrometry.";
Mol. Cell. Proteomics 8:904-912(2009).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-311; THR-505; SER-643
AND SER-662, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Brain, Kidney, Lung, Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[16]
FUNCTION IN PHOSPHORYLATION OF CDK1.
PubMed=19917613; DOI=10.1074/jbc.M109.055392;
LaGory E.L., Sitailo L.A., Denning M.F.;
"The protein kinase Cdelta catalytic fragment is critical for
maintenance of the G2/M DNA damage checkpoint.";
J. Biol. Chem. 285:1879-1887(2010).
[17]
X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 231-280 IN COMPLEX WITH
PHORBOL ESTER AND ZINC IONS.
PubMed=7781068; DOI=10.1016/0092-8674(95)90011-X;
Zhang G., Kazanietz M.G., Blumberg P.M., Hurley J.H.;
"Crystal structure of the cys2 activator-binding domain of protein
kinase C delta in complex with phorbol ester.";
Cell 81:917-924(1995).
-!- FUNCTION: Calcium-independent, phospholipid- and diacylglycerol
(DAG)-dependent serine/threonine-protein kinase that plays
contrasting roles in cell death and cell survival by functioning
as a pro-apoptotic protein during DNA damage-induced apoptosis,
but acting as an anti-apoptotic protein during cytokine receptor-
initiated cell death, is involved in tumor suppression, is
required for oxygen radical production by NADPH oxidase and acts
as positive or negative regulator in platelet functional
responses. Negatively regulates B cell proliferation and also has
an important function in self-antigen induced B cell tolerance
induction. Upon DNA damage, activates the promoter of the death-
promoting transcription factor BCLAF1/Btf to trigger BCLAF1-
mediated p53/TP53 gene transcription and apoptosis. In response to
oxidative stress, interact with and activate CHUK/IKKA in the
nucleus, causing the phosphorylation of p53/TP53. In the case of
ER stress or DNA damage-induced apoptosis, can form a complex with
the tyrosine-protein kinase ABL1 which trigger apoptosis
independently of p53/TP53. In cytosol can trigger apoptosis by
activating MAPK11 or MAPK14, inhibiting AKT1 and decreasing the
level of X-linked inhibitor of apoptosis protein (XIAP), whereas
in nucleus induces apoptosis via the activation of MAPK8 or MAPK9.
Upon ionizing radiation treatment, is required for the activation
of the apoptosis regulators BAX and BAK, which trigger the
mitochondrial cell death pathway. Can phosphorylate MCL1 and
target it for degradation which is sufficient to trigger for BAX
activation and apoptosis. Is required for the control of cell
cycle progression both at G1/S and G2/M phases. Mediates phorbol
12-myristate 13-acetate (PMA)-induced inhibition of cell cycle
progression at G1/S phase by up-regulating the CDK inhibitor
CDKN1A/p21 and inhibiting the cyclin CCNA2 promoter activity. In
response to UV irradiation can phosphorylate CDK1, which is
important for the G2/M DNA damage checkpoint activation. Can
protect glioma cells from the apoptosis induced by TNFSF10/TRAIL,
probably by inducing increased phosphorylation and subsequent
activation of AKT1. Can also act as tumor suppressor upon
mitogenic stimulation with PMA or TPA. In N-formyl-methionyl-
leucyl-phenylalanine (fMLP)-treated cells, is required for NCF1
(p47-phox) phosphorylation and activation of NADPH oxidase
activity, and regulates TNF-elicited superoxide anion production
in neutrophils, by direct phosphorylation and activation of NCF1
or indirectly through MAPK1/3 (ERK1/2) signaling pathways. May
also play a role in the regulation of NADPH oxidase activity in
eosinophil after stimulation with IL5, leukotriene B4 or PMA. In
collagen-induced platelet aggregation, acts a negative regulator
of filopodia formation and actin polymerization by interacting
with and negatively regulating VASP phosphorylation. Downstream of
PAR1, PAR4 and CD36/GP4 receptors, regulates differentially
platelet dense granule secretion; acts as a positive regulator in
PAR-mediated granule secretion, whereas it negatively regulates
CD36/GP4-mediated granule release. Phosphorylates MUC1 in the C-
terminal and regulates the interaction between MUC1 and beta-
catenin. The catalytic subunit phosphorylates 14-3-3 proteins
(YWHAB, YWHAZ and YWHAH) in a sphingosine-dependent fashion.
Phosphorylates ELAVL1 in response to angiotensin-2 treatment (By
similarity). {ECO:0000250|UniProtKB:Q05655,
ECO:0000269|PubMed:11976686, ECO:0000269|PubMed:11976687,
ECO:0000269|PubMed:18025218, ECO:0000269|PubMed:19917613,
ECO:0000269|PubMed:9705322}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
[protein]-L-tyrosine phosphate. {ECO:0000255|PROSITE-
ProRule:PRU10027}.
-!- ENZYME REGULATION: Novel PKCs (PRKCD, PRKCE, PRKCH and PRKCQ) are
calcium-insensitive, but activated by diacylglycerol (DAG) and
phosphatidylserine. Three specific sites; Thr-505 (activation loop
of the kinase domain), Ser-643 (turn motif) and Ser-662
(hydrophobic region), need to be phosphorylated for its full
activation. Activated by caspase-3 (CASP3) cleavage during
apoptosis. After cleavage, the pseudosubstrate motif in the
regulatory subunit is released from the substrate recognition site
of the catalytic subunit, which enables PRKCD to become
constitutively activated. The catalytic subunit which displays
properties of a sphingosine-dependent protein kinase is activated
by D-erythro-sphingosine (Sph) or N,N-dimethyl-D-
erythrosphingosine (DMS) or N,N,N-trimethyl-D-erythrosphingosine
(TMS), but not by ceramide or Sph-1-P and is strongly inhibited by
phosphatidylserine (By similarity). {ECO:0000250}.
-!- SUBUNIT: Interacts with PDPK1 (via N-terminal region) (By
similarity). Interacts with RAD9A (By similarity). Interacts with
CDCP1 (By similarity). Interacts with MUC1 (By similarity).
Interacts with VASP (By similarity). Interacts with CAVIN3
(PubMed:9054438). Interacts with PRKD2 (via N-terminus and zing-
finger domain 1 and 2) in response to oxidative stress; the
interaction is independent of PRKD2 tyrosine phosphorylation (By
similarity). {ECO:0000250|UniProtKB:Q05655,
ECO:0000269|PubMed:9054438}.
-!- INTERACTION:
P23242:Gja1; NbExp=4; IntAct=EBI-1551324, EBI-298630;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q05655}.
Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q05655}.
Nucleus {ECO:0000250|UniProtKB:Q05655}. Cell membrane
{ECO:0000250|UniProtKB:Q05655}; Peripheral membrane protein
{ECO:0000250|UniProtKB:Q05655}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=PKC-delta-I;
IsoId=P28867-1; Sequence=Displayed;
Name=2; Synonyms=PKC-delta-II;
IsoId=P28867-2; Sequence=VSP_004741;
-!- TISSUE SPECIFICITY: Isoform 1 is highly expressed in developing
pro- and pre-B-cells and moderately in mature T-cells. Isoform 2
is highly expressed in testis and ovary and at a lower level in
thymocytes, brain and kidney.
-!- DOMAIN: The C1 domain, containing the phorbol ester/DAG-type
region 1 (C1A) and 2 (C1B), is the diacylglycerol sensor.
-!- DOMAIN: The C2 domain is a non-calcium binding domain. It binds
proteins containing phosphotyrosine in a sequence-specific manner
(By similarity). {ECO:0000250}.
-!- PTM: Autophosphorylated and/or phosphorylated at Thr-505, within
the activation loop; phosphorylation at Thr-505 is not a
prerequisite for enzymatic activity. Autophosphorylated at Ser-
299. Upon TNFSF10/TRAIL treatment, phosphorylated at Tyr-155;
phosphorylation is required for its translocation to the
endoplasmic reticulum and cleavage by caspase-3. Phosphorylated at
Tyr-311, Tyr-332 and Tyr-565; phosphorylation of Tyr-311 and Tyr-
565 following thrombin stimulation potentiates its kinase
activity. Phosphorylated by protein kinase PDPK1; phosphorylation
is inhibited by the apoptotic C-terminal cleavage product of PKN2
(By similarity). {ECO:0000250}.
-!- PTM: Proteolytically cleaved into a catalytic subunit and a
regulatory subunit by caspase-3 during apoptosis which results in
kinase activation. {ECO:0000250}.
-!- DISRUPTION PHENOTYPE: Mice are viable up to 1 year despite
detection of auto-immune disease in these animals. They exhibit
glomerulonephritis, splenomegaly and lymphadenopathy associated
with B-cell expansion and defective B-cell tolerance to self-
antigen. {ECO:0000269|PubMed:11976687}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
protein kinase family. PKC subfamily. {ECO:0000305}.
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EMBL; M69042; AAA73056.1; -; mRNA.
EMBL; X60304; CAA42845.1; -; mRNA.
EMBL; AF274044; AAF79208.1; -; Genomic_DNA.
EMBL; AF251036; AAF64316.1; -; mRNA.
EMBL; AB011812; BAA36408.1; -; mRNA.
CCDS; CCDS26895.1; -. [P28867-1]
CCDS; CCDS79285.1; -. [P28867-2]
PIR; A40281; KIMSCD.
RefSeq; NP_035233.1; NM_011103.3. [P28867-1]
RefSeq; XP_006518758.1; XM_006518695.2. [P28867-2]
RefSeq; XP_017171407.1; XM_017315918.1. [P28867-2]
UniGene; Mm.2314; -.
PDB; 1PTQ; X-ray; 1.95 A; A=231-280.
PDB; 1PTR; X-ray; 2.20 A; A=231-280.
PDB; 3UEJ; X-ray; 1.30 A; A/B=231-280.
PDB; 3UEY; X-ray; 1.30 A; A/B=231-280.
PDB; 3UFF; X-ray; 1.30 A; A/B=231-280.
PDB; 3UGD; X-ray; 1.45 A; A/B=231-280.
PDB; 3UGI; X-ray; 1.36 A; A/B=231-280.
PDB; 3UGL; X-ray; 1.36 A; A/B=231-280.
PDBsum; 1PTQ; -.
PDBsum; 1PTR; -.
PDBsum; 3UEJ; -.
PDBsum; 3UEY; -.
PDBsum; 3UFF; -.
PDBsum; 3UGD; -.
PDBsum; 3UGI; -.
PDBsum; 3UGL; -.
ProteinModelPortal; P28867; -.
SMR; P28867; -.
BioGrid; 202197; 7.
DIP; DIP-1169N; -.
IntAct; P28867; 6.
MINT; MINT-97906; -.
STRING; 10090.ENSMUSP00000107827; -.
BindingDB; P28867; -.
ChEMBL; CHEMBL2560; -.
iPTMnet; P28867; -.
PhosphoSitePlus; P28867; -.
EPD; P28867; -.
PaxDb; P28867; -.
PeptideAtlas; P28867; -.
PRIDE; P28867; -.
Ensembl; ENSMUST00000022521; ENSMUSP00000022521; ENSMUSG00000021948. [P28867-2]
Ensembl; ENSMUST00000112210; ENSMUSP00000107829; ENSMUSG00000021948. [P28867-1]
Ensembl; ENSMUST00000112211; ENSMUSP00000107830; ENSMUSG00000021948. [P28867-2]
GeneID; 18753; -.
KEGG; mmu:18753; -.
UCSC; uc007sve.2; mouse. [P28867-1]
UCSC; uc007svg.2; mouse. [P28867-2]
CTD; 5580; -.
MGI; MGI:97598; Prkcd.
eggNOG; KOG0694; Eukaryota.
eggNOG; ENOG410XNPH; LUCA.
GeneTree; ENSGT00820000126964; -.
HOGENOM; HOG000233022; -.
HOVERGEN; HBG108317; -.
InParanoid; P28867; -.
KO; K06068; -.
OMA; FIFHKVL; -.
OrthoDB; EOG091G0QRS; -.
PhylomeDB; P28867; -.
TreeFam; TF102004; -.
BRENDA; 2.7.11.13; 3474.
Reactome; R-MMU-111465; Apoptotic cleavage of cellular proteins.
Reactome; R-MMU-111933; Calmodulin induced events.
Reactome; R-MMU-114508; Effects of PIP2 hydrolysis.
Reactome; R-MMU-1489509; DAG and IP3 signaling.
Reactome; R-MMU-2029485; Role of phospholipids in phagocytosis.
Reactome; R-MMU-450520; HuR (ELAVL1) binds and stabilizes mRNA.
Reactome; R-MMU-5218921; VEGFR2 mediated cell proliferation.
Reactome; R-MMU-5607764; CLEC7A (Dectin-1) signaling.
Reactome; R-MMU-6798695; Neutrophil degranulation.
Reactome; R-MMU-877300; Interferon gamma signaling.
ChiTaRS; Prkcd; mouse.
EvolutionaryTrace; P28867; -.
PRO; PR:P28867; -.
Proteomes; UP000000589; Chromosome 14.
Bgee; ENSMUSG00000021948; -.
CleanEx; MM_PRKCD; -.
ExpressionAtlas; P28867; baseline and differential.
Genevisible; P28867; MM.
GO; GO:0005911; C:cell-cell junction; IDA:MGI.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0016020; C:membrane; IDA:MGI.
GO; GO:0016363; C:nuclear matrix; IDA:MGI.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; ISO:MGI.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004699; F:calcium-independent protein kinase C activity; ISO:MGI.
GO; GO:0008047; F:enzyme activator activity; ISO:MGI.
GO; GO:0019899; F:enzyme binding; ISO:MGI.
GO; GO:0043560; F:insulin receptor substrate binding; IPI:BHF-UCL.
GO; GO:0019900; F:kinase binding; ISO:MGI.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IEA:UniProtKB-EC.
GO; GO:0004672; F:protein kinase activity; ISO:MGI.
GO; GO:0019901; F:protein kinase binding; ISO:MGI.
GO; GO:0004697; F:protein kinase C activity; IDA:UniProtKB.
GO; GO:0004674; F:protein serine/threonine kinase activity; ISO:MGI.
GO; GO:0032147; P:activation of protein kinase activity; ISO:MGI.
GO; GO:0006915; P:apoptotic process; ISO:MGI.
GO; GO:0042100; P:B cell proliferation; IMP:MGI.
GO; GO:0060326; P:cell chemotaxis; ISO:MGI.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:1904385; P:cellular response to angiotensin; ISS:UniProtKB.
GO; GO:0070301; P:cellular response to hydrogen peroxide; ISO:MGI.
GO; GO:0071447; P:cellular response to hydroperoxide; ISO:MGI.
GO; GO:0090398; P:cellular senescence; ISO:MGI.
GO; GO:0042742; P:defense response to bacterium; IMP:UniProtKB.
GO; GO:0016572; P:histone phosphorylation; ISO:MGI.
GO; GO:0016064; P:immunoglobulin mediated immune response; IMP:MGI.
GO; GO:0032613; P:interleukin-10 production; IMP:MGI.
GO; GO:0032615; P:interleukin-12 production; IMP:MGI.
GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
GO; GO:0030837; P:negative regulation of actin filament polymerization; IMP:UniProtKB.
GO; GO:0051490; P:negative regulation of filopodium assembly; IMP:UniProtKB.
GO; GO:0034351; P:negative regulation of glial cell apoptotic process; ISS:UniProtKB.
GO; GO:0046627; P:negative regulation of insulin receptor signaling pathway; IMP:BHF-UCL.
GO; GO:0043407; P:negative regulation of MAP kinase activity; ISO:MGI.
GO; GO:0050732; P:negative regulation of peptidyl-tyrosine phosphorylation; IMP:BHF-UCL.
GO; GO:0090331; P:negative regulation of platelet aggregation; IMP:UniProtKB.
GO; GO:0042119; P:neutrophil activation; ISO:MGI.
GO; GO:0018105; P:peptidyl-serine phosphorylation; ISS:UniProtKB.
GO; GO:0018107; P:peptidyl-threonine phosphorylation; ISO:MGI.
GO; GO:2001235; P:positive regulation of apoptotic signaling pathway; IDA:MGI.
GO; GO:2000304; P:positive regulation of ceramide biosynthetic process; ISO:MGI.
GO; GO:0032079; P:positive regulation of endodeoxyribonuclease activity; ISO:MGI.
GO; GO:2000753; P:positive regulation of glucosylceramide catabolic process; ISO:MGI.
GO; GO:1900163; P:positive regulation of phospholipid scramblase activity; ISO:MGI.
GO; GO:0035307; P:positive regulation of protein dephosphorylation; ISO:MGI.
GO; GO:0042307; P:positive regulation of protein import into nucleus; ISO:MGI.
GO; GO:2001022; P:positive regulation of response to DNA damage stimulus; ISO:MGI.
GO; GO:2000755; P:positive regulation of sphingomyelin catabolic process; ISO:MGI.
GO; GO:0032930; P:positive regulation of superoxide anion generation; ISS:UniProtKB.
GO; GO:0006468; P:protein phosphorylation; ISO:MGI.
GO; GO:0032956; P:regulation of actin cytoskeleton organization; ISO:MGI.
GO; GO:0023021; P:termination of signal transduction; ISO:MGI.
CDD; cd00029; C1; 2.
Gene3D; 2.60.40.150; -; 1.
InterPro; IPR000961; AGC-kinase_C.
InterPro; IPR035892; C2_domain_sf.
InterPro; IPR020454; DAG/PE-bd.
InterPro; IPR011009; Kinase-like_dom.
InterPro; IPR002219; PE/DAG-bd.
InterPro; IPR027436; PKC_delta.
InterPro; IPR017892; Pkinase_C.
InterPro; IPR014376; Prot_kin_PKC_delta.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR008271; Ser/Thr_kinase_AS.
Pfam; PF00130; C1_1; 2.
Pfam; PF00069; Pkinase; 1.
Pfam; PF00433; Pkinase_C; 1.
PIRSF; PIRSF000551; PKC_delta; 1.
PIRSF; PIRSF501104; Protein_kin_C_delta; 1.
PRINTS; PR00008; DAGPEDOMAIN.
SMART; SM00109; C1; 2.
SMART; SM00133; S_TK_X; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF49562; SSF49562; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS51285; AGC_KINASE_CTER; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PROSITE; PS00479; ZF_DAG_PE_1; 2.
PROSITE; PS50081; ZF_DAG_PE_2; 2.
1: Evidence at protein level;
3D-structure; Alternative splicing; Apoptosis; ATP-binding;
Cell cycle; Cell membrane; Complete proteome; Cytoplasm; Kinase;
Membrane; Metal-binding; Nucleotide-binding; Nucleus; Phosphoprotein;
Reference proteome; Repeat; Serine/threonine-protein kinase;
Transferase; Tumor suppressor; Zinc; Zinc-finger.
CHAIN 1 674 Protein kinase C delta type.
/FTId=PRO_0000055695.
CHAIN 1 327 Protein kinase C delta type regulatory
subunit. {ECO:0000250}.
/FTId=PRO_0000421669.
CHAIN 328 674 Protein kinase C delta type catalytic
subunit. {ECO:0000250}.
/FTId=PRO_0000421670.
DOMAIN 1 90 C2.
DOMAIN 347 601 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
DOMAIN 602 673 AGC-kinase C-terminal.
ZN_FING 158 208 Phorbol-ester/DAG-type 1.
{ECO:0000255|PROSITE-ProRule:PRU00226}.
ZN_FING 230 280 Phorbol-ester/DAG-type 2.
{ECO:0000255|PROSITE-ProRule:PRU00226}.
NP_BIND 353 361 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
ACT_SITE 471 471 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 376 376 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
SITE 48 48 Interaction with phosphotyrosine-
containing peptide. {ECO:0000250}.
SITE 62 62 Interaction with phosphotyrosine-
containing peptide. {ECO:0000250}.
SITE 67 67 Interaction with phosphotyrosine-
containing peptide. {ECO:0000250}.
SITE 123 123 Interaction with phosphotyrosine-
containing peptide. {ECO:0000250}.
SITE 327 328 Cleavage; by caspase-3. {ECO:0000250}.
MOD_RES 43 43 Phosphothreonine.
{ECO:0000244|PubMed:19144319}.
MOD_RES 50 50 Phosphothreonine.
{ECO:0000250|UniProtKB:Q05655}.
MOD_RES 64 64 Phosphotyrosine.
{ECO:0000250|UniProtKB:P09215}.
MOD_RES 130 130 Phosphoserine.
{ECO:0000250|UniProtKB:Q05655}.
MOD_RES 141 141 Phosphothreonine.
{ECO:0000250|UniProtKB:Q05655}.
MOD_RES 155 155 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q05655}.
MOD_RES 218 218 Phosphothreonine.
{ECO:0000250|UniProtKB:Q05655}.
MOD_RES 299 299 Phosphoserine; by autocatalysis.
{ECO:0000250|UniProtKB:Q05655}.
MOD_RES 311 311 Phosphotyrosine; by SRC.
{ECO:0000244|PubMed:17947660,
ECO:0000244|PubMed:18034455,
ECO:0000244|PubMed:19131326,
ECO:0000244|PubMed:19144319,
ECO:0000244|PubMed:21183079}.
MOD_RES 332 332 Phosphotyrosine; by SRC.
{ECO:0000250|UniProtKB:P09215}.
MOD_RES 372 372 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q05655}.
MOD_RES 449 449 Phosphothreonine.
{ECO:0000250|UniProtKB:Q05655}.
MOD_RES 504 504 Phosphoserine.
{ECO:0000250|UniProtKB:Q05655}.
MOD_RES 505 505 Phosphothreonine; by autocatalysis.
{ECO:0000244|PubMed:21183079,
ECO:0000269|PubMed:18025218,
ECO:0000269|PubMed:9748166}.
MOD_RES 565 565 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q05655}.
MOD_RES 643 643 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 652 652 Phosphoserine.
{ECO:0000250|UniProtKB:Q05655}.
MOD_RES 662 662 Phosphoserine.
{ECO:0000244|PubMed:19144319,
ECO:0000244|PubMed:21183079}.
VAR_SEQ 326 326 L -> LGEAGSHISLKLSFPSRAKEKDSSETC (in
isoform 2).
{ECO:0000303|PubMed:11558579}.
/FTId=VSP_004741.
CONFLICT 214 214 N -> I (in Ref. 4; BAA36408).
{ECO:0000305}.
CONFLICT 226 226 N -> S (in Ref. 4; BAA36408).
{ECO:0000305}.
CONFLICT 319 319 E -> D (in Ref. 1; AAA73056).
{ECO:0000305}.
CONFLICT 330 330 G -> W (in Ref. 1; AAA73056).
{ECO:0000305}.
CONFLICT 337 337 E -> V (in Ref. 1; AAA73056).
{ECO:0000305}.
CONFLICT 501 501 G -> D (in Ref. 1; AAA73056).
{ECO:0000305}.
CONFLICT 503 503 A -> P (in Ref. 1; AAA73056).
{ECO:0000305}.
CONFLICT 513 513 I -> S (in Ref. 1; AAA73056).
{ECO:0000305}.
CONFLICT 518 520 LQG -> PARA (in Ref. 4; BAA36408).
{ECO:0000305}.
CONFLICT 538 538 E -> R (in Ref. 4; BAA36408).
{ECO:0000305}.
STRAND 233 236 {ECO:0000244|PDB:3UFF}.
TURN 245 247 {ECO:0000244|PDB:3UFF}.
STRAND 253 256 {ECO:0000244|PDB:3UFF}.
STRAND 258 261 {ECO:0000244|PDB:3UFF}.
TURN 262 264 {ECO:0000244|PDB:3UFF}.
HELIX 270 273 {ECO:0000244|PDB:3UFF}.
STRAND 278 280 {ECO:0000244|PDB:3UFF}.
SEQUENCE 674 AA; 77547 MW; 6E9F753348F03D59 CRC64;
MAPFLRISFN SYELGSLQVE DEASQPFCAV KMKEALSTER GKTLVQKKPT MYPEWKTTFD
AHIYEGRVIQ IVLMRAAEDP VSEVTVGVSV LAERCKKNNG KAEFWLDLQP QAKVLMCVQY
FLEDGDCKQS MRSEEEAKFP TMNRRGAIKQ AKIHYIKNHE FIATFFGQPT FCSVCKEFVW
GLNKQGYKCR QCNAAIHKKC IDKIIGRCTG TATNSRDTIF QKERFNIDMP HRFKVYNYMS
PTFCDHCGSL LWGLVKQGLK CEDCGMNVHH KCREKVANLC GINQKLLAEA LNQVTQRSSR
KLDTTESVGI YQGFEKKPEV SGSDILDNNG TYGKIWEGST RCTLENFTFQ KVLGKGSFGK
VLLAELKGKD KYFAIKCLKK DVVLIDDDVE CTMVEKRVLA LAWESPFLTH LICTFQTKDH
LFFVMEFLNG GDLMFHIQDK GRFELYRATF YAAEIICGLQ FLHSKGIIYR DLKLDNVMLD
RDGHIKIADF GMCKENIFGE GRASTFCGTP DYIAPEILQG LKYSFSVDWW SFGVLLYEML
IGQSPFHGDD EDELFESIRV DTPHYPRWIT KESKDIMEKL FERDPDKRLG VTGNIRIHPF
FKTINWSLLE KRKVEPPFKP KVKSPSDYSN FDPEFLNEKP QLSFSDKNLI DSMDQEAFHG
FSFVNPKFEQ FLDI


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