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Protein kinase C delta type (EC 2.7.11.13) (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_RAT                Reviewed;         673 AA.
P09215; Q6DG48; Q9JK29; Q9JL03;
01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
01-JUL-1989, sequence version 1.
20-JUN-2018, entry version 193.
RecName: Full=Protein kinase C delta type;
EC=2.7.11.13;
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;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=2834397;
Ono Y., Fujii T., Ogita K., Kikkawa U., Igarashi K., Nishizuka Y.;
"The structure, expression, and properties of additional members of
the protein kinase C family.";
J. Biol. Chem. 263:6927-6932(1988).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=Wistar Kyoto;
PubMed=10721703; DOI=10.1016/S0378-1119(99)00539-9;
Kurkinen K.M.A., Keinanen R.A., Karhu R., Koistinaho J.;
"Genomic structure and chromosomal localization of the rat PKCdelta-
gene.";
Gene 242:115-123(2000).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
PubMed=10708593; DOI=10.1006/bbrc.2000.2331;
Ueyama T., Ren Y., Ohmori S., Sakai K., Tamaki N., Saito N.;
"cDNA cloning of an alternative splicing variant of protein kinase C
delta (PKC deltaIII), a new truncated form of PKCdelta, in rats.";
Biochem. Biophys. Res. Commun. 269:557-563(2000).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Lung;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
NUCLEOTIDE SEQUENCE OF 123-286.
PubMed=3691811; DOI=10.1016/0014-5793(87)80564-1;
Ono Y., Fujii T., Ogita K., Kikkawa U., Igarashi K., Nishizuka Y.;
"Identification of three additional members of rat protein kinase C
family: delta-, epsilon- and zeta-subspecies.";
FEBS Lett. 226:125-128(1987).
[6]
PROTEIN SEQUENCE OF 142-153.
PubMed=1915352; DOI=10.1111/j.1432-1033.1991.tb16248.x;
Olivier A.R., Parker P.J.;
"Expression and characterization of protein kinase C-delta.";
Eur. J. Biochem. 200:805-810(1991).
[7]
MUTAGENESIS OF THR-505, AND PHOSPHORYLATION AT THR-505.
PubMed=9677322; DOI=10.1042/bj3330631;
Garcia-Paramio P., Cabrerizo Y., Bornancin F., Parker P.J.;
"The broad specificity of dominant inhibitory protein kinase C mutants
infers a common step in phosphorylation.";
Biochem. J. 333:631-636(1998).
[8]
IDENTIFICATION BY MASS SPECTROMETRY, CLEAVAGE BY CASPASE-3, AND ENZYME
REGULATION.
PubMed=12855683; DOI=10.1074/jbc.M305294200;
Hamaguchi A., Suzuki E., Murayama K., Fujimura T., Hikita T.,
Iwabuchi K., Handa K., Withers D.A., Masters S.C., Fu H., Hakomori S.;
"Sphingosine-dependent protein kinase-1, directed to 14-3-3, is
identified as the kinase domain of protein kinase C delta.";
J. Biol. Chem. 278:41557-41565(2003).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-662, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=16396499; DOI=10.1021/pr0503073;
Moser K., White F.M.;
"Phosphoproteomic analysis of rat liver by high capacity IMAC and LC-
MS/MS.";
J. Proteome Res. 5:98-104(2006).
[10]
SUBCELLULAR LOCATION, AND PHOSPHORYLATION AT TYR-64 AND TYR-155.
PubMed=17562707; DOI=10.1074/jbc.M703661200;
DeVries-Seimon T.A., Ohm A.M., Humphries M.J., Reyland M.E.;
"Induction of apoptosis is driven by nuclear retention of protein
kinase C delta.";
J. Biol. Chem. 282:22307-22314(2007).
[11]
PHOSPHORYLATION AT THR-505.
PubMed=17569658; DOI=10.1074/jbc.M701676200;
Rybin V.O., Guo J., Gertsberg Z., Elouardighi H., Steinberg S.F.;
"Protein kinase Cepsilon (PKCepsilon) and Src control PKCdelta
activation loop phosphorylation in cardiomyocytes.";
J. Biol. Chem. 282:23631-23638(2007).
[12]
PHOSPHORYLATION AT TYR-311; TYR-332 AND THR-505.
PubMed=18550549; DOI=10.1074/jbc.M802396200;
Sumandea M.P., Rybin V.O., Hinken A.C., Wang C., Kobayashi T.,
Harleton E., Sievert G., Balke C.W., Feinmark S.J., Solaro R.J.,
Steinberg S.F.;
"Tyrosine phosphorylation modifies protein kinase C delta-dependent
phosphorylation of cardiac troponin I.";
J. Biol. Chem. 283:22680-22689(2008).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-311; SER-643 AND
SER-662, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
[14]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1-123.
PubMed=9687370; DOI=10.1016/S0969-2126(98)00090-2;
Pappa H., Murray-Rust J., Dekker L.V., Parker P.J., McDonald N.Q.;
"Crystal structure of the C2 domain from protein kinase C-delta.";
Structure 6:885-894(1998).
-!- 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. 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 (By similarity). 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}.
-!- FUNCTION: Truncated isoform 2 is inactive.
-!- 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. {ECO:0000269|PubMed:12855683}.
-!- SUBUNIT: Interacts with PDPK1 (via N-terminal region). Interacts
with RAD9A (By similarity). Interacts with CDCP1. Interacts with
MUC1. Interacts with VASP. Interacts with CAVIN3. 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. {ECO:0000250|UniProtKB:P28867,
ECO:0000250|UniProtKB:Q05655}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17562707}.
Nucleus {ECO:0000269|PubMed:17562707}. Cytoplasm, perinuclear
region {ECO:0000269|PubMed:17562707}. Membrane
{ECO:0000269|PubMed:17562707}; Peripheral membrane protein
{ECO:0000269|PubMed:17562707}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=PKC-delta-I;
IsoId=P09215-1; Sequence=Displayed;
Name=2; Synonyms=PKC-delta-III;
IsoId=P09215-2; Sequence=VSP_004742;
-!- 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). Phosphorylated at Tyr-311 and Tyr-332 by SRC;
phosphorylation leads to enhanced autophosphorylation at Thr-505.
{ECO:0000250, ECO:0000269|PubMed:12855683,
ECO:0000269|PubMed:17562707, ECO:0000269|PubMed:17569658,
ECO:0000269|PubMed:18550549, ECO:0000269|PubMed:9677322}.
-!- PTM: Proteolytically cleaved into a catalytic subunit and a
regulatory subunit by caspase-3 during apoptosis which results in
kinase activation. {ECO:0000269|PubMed:12855683}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
protein kinase family. PKC subfamily. {ECO:0000305}.
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EMBL; M18330; AAA41871.1; -; mRNA.
EMBL; AJ230617; CAB75578.1; -; Genomic_DNA.
EMBL; AJ230618; CAB75578.1; JOINED; Genomic_DNA.
EMBL; AJ230619; CAB75578.1; JOINED; Genomic_DNA.
EMBL; AJ230620; CAB75578.1; JOINED; Genomic_DNA.
EMBL; AJ230621; CAB75578.1; JOINED; Genomic_DNA.
EMBL; AJ230622; CAB75578.1; JOINED; Genomic_DNA.
EMBL; AJ230623; CAB75578.1; JOINED; Genomic_DNA.
EMBL; AJ230624; CAB75578.1; JOINED; Genomic_DNA.
EMBL; AJ230625; CAB75578.1; JOINED; Genomic_DNA.
EMBL; AJ230626; CAB75578.1; JOINED; Genomic_DNA.
EMBL; AJ230627; CAB75578.1; JOINED; Genomic_DNA.
EMBL; AJ230628; CAB75578.1; JOINED; Genomic_DNA.
EMBL; AJ230629; CAB75578.1; JOINED; Genomic_DNA.
EMBL; AJ230630; CAB75578.1; JOINED; Genomic_DNA.
EMBL; AJ230631; CAB75578.1; JOINED; Genomic_DNA.
EMBL; AJ230632; CAB75578.1; JOINED; Genomic_DNA.
EMBL; AJ230633; CAB75578.1; JOINED; Genomic_DNA.
EMBL; AF219629; AAF32345.1; -; mRNA.
EMBL; BC076505; AAH76505.1; -; mRNA.
PIR; A28163; KIRTCD.
RefSeq; NP_579841.1; NM_133307.1. [P09215-1]
UniGene; Rn.98279; -.
PDB; 1BDY; X-ray; 2.20 A; A/B=1-123.
PDBsum; 1BDY; -.
ProteinModelPortal; P09215; -.
SMR; P09215; -.
BioGrid; 250924; 8.
IntAct; P09215; 3.
STRING; 10116.ENSRNOP00000025858; -.
ChEMBL; CHEMBL3633; -.
iPTMnet; P09215; -.
PhosphoSitePlus; P09215; -.
PaxDb; P09215; -.
PRIDE; P09215; -.
GeneID; 170538; -.
KEGG; rno:170538; -.
UCSC; RGD:67383; rat. [P09215-1]
CTD; 5580; -.
RGD; 67383; Prkcd.
eggNOG; KOG0694; Eukaryota.
eggNOG; ENOG410XNPH; LUCA.
HOGENOM; HOG000233022; -.
HOVERGEN; HBG108317; -.
InParanoid; P09215; -.
KO; K06068; -.
PhylomeDB; P09215; -.
BRENDA; 2.7.11.13; 5301.
EvolutionaryTrace; P09215; -.
PMAP-CutDB; P09215; -.
PRO; PR:P09215; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0005737; C:cytoplasm; IDA:RGD.
GO; GO:0005829; C:cytosol; IDA:RGD.
GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
GO; GO:0016020; C:membrane; IDA:RGD.
GO; GO:0005739; C:mitochondrion; IDA:RGD.
GO; GO:0005634; C:nucleus; IDA:RGD.
GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; IDA:RGD.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004699; F:calcium-independent protein kinase C activity; IDA:RGD.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0019901; F:protein kinase binding; IPI:RGD.
GO; GO:0004697; F:protein kinase C activity; ISS:UniProtKB.
GO; GO:0070976; F:TIR domain binding; IPI:BHF-UCL.
GO; GO:0007568; P:aging; IEP:RGD.
GO; GO:0006915; P:apoptotic process; IMP:CACAO.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:1904385; P:cellular response to angiotensin; ISS:UniProtKB.
GO; GO:0042149; P:cellular response to glucose starvation; IEP:RGD.
GO; GO:0032869; P:cellular response to insulin stimulus; IEP:RGD.
GO; GO:0034599; P:cellular response to oxidative stress; IDA:CACAO.
GO; GO:0032963; P:collagen metabolic process; IMP:RGD.
GO; GO:0070779; P:D-aspartate import across plasma membrane; IMP:RGD.
GO; GO:0042742; P:defense response to bacterium; ISS:UniProtKB.
GO; GO:0035556; P:intracellular signal transduction; IDA:RGD.
GO; GO:0030837; P:negative regulation of actin filament polymerization; ISS:UniProtKB.
GO; GO:0051490; P:negative regulation of filopodium assembly; ISS:UniProtKB.
GO; GO:0034351; P:negative regulation of glial cell apoptotic process; ISS:UniProtKB.
GO; GO:0090331; P:negative regulation of platelet aggregation; ISS:UniProtKB.
GO; GO:0018105; P:peptidyl-serine phosphorylation; ISS:UniProtKB.
GO; GO:0043065; P:positive regulation of apoptotic process; IMP:RGD.
GO; GO:0046326; P:positive regulation of glucose import; IMP:RGD.
GO; GO:0043406; P:positive regulation of MAP kinase activity; IMP:RGD.
GO; GO:0043410; P:positive regulation of MAPK cascade; IMP:RGD.
GO; GO:0032930; P:positive regulation of superoxide anion generation; ISS:UniProtKB.
GO; GO:0046777; P:protein autophosphorylation; IDA:RGD.
GO; GO:0006468; P:protein phosphorylation; IDA:RGD.
GO; GO:0042325; P:regulation of phosphorylation; IDA:CACAO.
GO; GO:0043200; P:response to amino acid; IEP:RGD.
GO; GO:0042493; P:response to drug; IEP:RGD.
GO; GO:0045471; P:response to ethanol; IEP:RGD.
GO; GO:0009749; P:response to glucose; IEP:RGD.
GO; GO:0009408; P:response to heat; IEP:RGD.
GO; GO:0042542; P:response to hydrogen peroxide; IEP:RGD.
GO; GO:0001666; P:response to hypoxia; IEP:RGD.
GO; GO:0009612; P:response to mechanical stimulus; IEP:RGD.
GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
GO; GO:0010243; P:response to organonitrogen compound; IEP:RGD.
GO; GO:0006979; P:response to oxidative stress; IMP:RGD.
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_sf.
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; 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; Complete proteome; Cytoplasm; Direct protein sequencing;
Kinase; Membrane; Metal-binding; Nucleotide-binding; Nucleus;
Phosphoprotein; Reference proteome; Repeat;
Serine/threonine-protein kinase; Transferase; Tumor suppressor; Zinc;
Zinc-finger.
CHAIN 1 673 Protein kinase C delta type.
/FTId=PRO_0000055696.
CHAIN 1 327 Protein kinase C delta type regulatory
subunit.
/FTId=PRO_0000421671.
CHAIN 328 673 Protein kinase C delta type catalytic
subunit.
/FTId=PRO_0000421672.
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:0000305}.
MOD_RES 43 43 Phosphothreonine.
{ECO:0000250|UniProtKB:P28867}.
MOD_RES 50 50 Phosphothreonine.
{ECO:0000250|UniProtKB:Q05655}.
MOD_RES 64 64 Phosphotyrosine.
{ECO:0000269|PubMed:17562707}.
MOD_RES 130 130 Phosphoserine.
{ECO:0000250|UniProtKB:Q05655}.
MOD_RES 141 141 Phosphothreonine.
{ECO:0000250|UniProtKB:Q05655}.
MOD_RES 155 155 Phosphotyrosine.
{ECO:0000269|PubMed:17562707}.
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:22673903,
ECO:0000269|PubMed:18550549}.
MOD_RES 332 332 Phosphotyrosine; by SRC.
{ECO:0000269|PubMed:18550549}.
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:0000269|PubMed:17569658,
ECO:0000269|PubMed:18550549,
ECO:0000269|PubMed:9677322}.
MOD_RES 565 565 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q05655}.
MOD_RES 643 643 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 652 652 Phosphoserine.
{ECO:0000250|UniProtKB:Q05655}.
MOD_RES 662 662 Phosphoserine.
{ECO:0000244|PubMed:16396499,
ECO:0000244|PubMed:22673903}.
VAR_SEQ 327 673 DNNGTYGKIWEGSNRCRLENFTFQKVLGKGSFGKVLLAELK
GKERYFAIKYLKKDVVLIDDDVECTMVEKRVLALAWENPFL
THLICTFQTKDHLFFVMEFLNGGDLMFHIQDKGRFELYRAT
FYAAEIICGLQFLHGKGIIYRDLKLDNVMLDKDGHIKIADF
GMCKENIFGENRASTFCGTPDYIAPEILQGLKYSFSVDWWS
FGVLLYEMLIGQSPFHGDDEDELFESIRVDTPHYPRWITKE
SKDIMEKLFERDPAKRLGVTGNIRLHPFFKTINWNLLEKRK
VEPPFKPKVKSPSDYSNFDPEFLNEKPQLSFSDKNLIDSMD
QTAFKGFSFVNPKYEQFLE -> GESGSHIPLKLPFPDRAR
EKNSSETWDKTTTGPMARSGRGATGAALRTSPSRKYLAKAA
LARYCLQN (in isoform 2).
{ECO:0000303|PubMed:10708593}.
/FTId=VSP_004742.
MUTAGEN 505 505 T->A: Decrease in the phosphorylation
level. {ECO:0000269|PubMed:9677322}.
CONFLICT 147 147 A -> S (in Ref. 6; AA sequence).
{ECO:0000305}.
CONFLICT 249 249 T -> S (in Ref. 2; CAB75578 and 4;
AAH76505). {ECO:0000305}.
STRAND 3 13 {ECO:0000244|PDB:1BDY}.
STRAND 27 35 {ECO:0000244|PDB:1BDY}.
HELIX 38 40 {ECO:0000244|PDB:1BDY}.
STRAND 43 46 {ECO:0000244|PDB:1BDY}.
STRAND 58 62 {ECO:0000244|PDB:1BDY}.
STRAND 68 76 {ECO:0000244|PDB:1BDY}.
STRAND 79 87 {ECO:0000244|PDB:1BDY}.
HELIX 88 96 {ECO:0000244|PDB:1BDY}.
TURN 97 100 {ECO:0000244|PDB:1BDY}.
STRAND 101 107 {ECO:0000244|PDB:1BDY}.
STRAND 109 111 {ECO:0000244|PDB:1BDY}.
STRAND 113 122 {ECO:0000244|PDB:1BDY}.
SEQUENCE 673 AA; 77520 MW; D2C767E55863A23C CRC64;
MAPFLRISFN SYELGSLQAE DDASQPFCAV KMKEALTTDR GKTLVQKKPT MYPEWKSTFD
AHIYEGRVIQ IVLMRAAEDP MSEVTVGVSV LAERCKKNNG KAEFWLDLQP QAKVLMCVQY
FLEDGDCKQS MRSEEEAMFP TMNRRGAIKQ AKIHYIKNHE FIATFFGQPT FCSVCKEFVW
GLNKQGYKCR QCNAAIHKKC IDKIIGRCTG TATNSRDTIF QKERFNIDMP HRFKVYNYMS
PTFCDHCGTL LWGLVKQGLK CEDCGMNVHH KCREKVANLC GINQKLLAEA LNQVTQKASR
KPETPETVGI YQGFEKKTAV SGNDIPDNNG TYGKIWEGSN RCRLENFTFQ KVLGKGSFGK
VLLAELKGKE RYFAIKYLKK DVVLIDDDVE CTMVEKRVLA LAWENPFLTH LICTFQTKDH
LFFVMEFLNG GDLMFHIQDK GRFELYRATF YAAEIICGLQ FLHGKGIIYR DLKLDNVMLD
KDGHIKIADF GMCKENIFGE NRASTFCGTP DYIAPEILQG LKYSFSVDWW SFGVLLYEML
IGQSPFHGDD EDELFESIRV DTPHYPRWIT KESKDIMEKL FERDPAKRLG VTGNIRLHPF
FKTINWNLLE KRKVEPPFKP KVKSPSDYSN FDPEFLNEKP QLSFSDKNLI DSMDQTAFKG
FSFVNPKYEQ FLE


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