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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_HUMAN              Reviewed;         676 AA.
Q05655; B0KZ81; B2R834; Q15144; Q86XJ6;
01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
02-SEP-2008, sequence version 2.
30-AUG-2017, entry version 196.
RecName: Full=Protein kinase C delta type;
EC=2.7.11.13 {ECO:0000269|PubMed:18285462};
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;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS SER-375 AND
MET-593.
TISSUE=Liver;
PubMed=8357834; DOI=10.1016/0167-4781(93)90111-P;
Aris J.P., Basta P.V., Holmes W.D., Ballas L.M., Moomaw C.,
Rankl N.B., Blobel G., Loomis C.R., Burns D.J.;
"Molecular and biochemical characterization of a recombinant human
PKC-delta family member.";
Biochim. Biophys. Acta 1174:171-181(1993).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Skin;
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 [MRNA] OF 1-365 (ISOFORM 1).
TISSUE=Hippocampus;
Hug H.;
"Partial cDNA Sequence of human protein kinase C delta.";
Submitted (MAR-1993) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 51-676 (ISOFORM 1).
PubMed=9427282; DOI=10.1046/j.1365-2443.1997.1470346.x;
Nomoto S., Watanabe Y., Ninomiya-Tsuji J., Yang L.-X., Kikuchi K.,
Hagiwara M., Hidaka H., Matsumoto K., Irie K.;
"Functional analyses of mammalian protein kinase C isozymes in budding
yeast and mammalian fibroblasts.";
Genes Cells 2:601-614(1997).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 224-371 (ISOFORM 2).
PubMed=18092819; DOI=10.1021/bi7019782;
Jiang K., Apostolatos A.H., Ghansah T., Watson J.E., Vickers T.,
Cooper D.R., Epling-Burnette P.K., Patel N.A.;
"Identification of a novel antiapoptotic human protein kinase C delta
isoform, PKCdeltaVIII in NT2 cells.";
Biochemistry 47:787-797(2008).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 432-533 (ISOFORM 1), AND VARIANT
VAL-494.
PubMed=7988719; DOI=10.1016/0014-5793(94)01202-4;
Palmer R.H., Ridden J., Parker P.J.;
"Identification of multiple, novel, protein kinase C-related gene
products.";
FEBS Lett. 356:5-8(1994).
[9]
FUNCTION.
PubMed=11748588; DOI=10.1002/jcp.10022;
Bankers-Fulbright J.L., Kita H., Gleich G.J., O'Grady S.M.;
"Regulation of human eosinophil NADPH oxidase activity: a central role
for PKCdelta.";
J. Cell. Physiol. 189:306-315(2001).
[10]
MUTAGENESIS OF THR-507.
PubMed=11772397;
Liu Y., Graham C., Li A., Fisher R.J., Shaw S.;
"Phosphorylation of the protein kinase C-theta activation loop and
hydrophobic motif regulates its kinase activity, but only activation
loop phosphorylation is critical to in vivo nuclear-factor-kappaB
induction.";
Biochem. J. 361:255-265(2002).
[11]
INTERACTION WITH PDPK1, AND PHOSPHORYLATION.
PubMed=11781095; DOI=10.1021/bi010719z;
Hodgkinson C.P., Sale G.J.;
"Regulation of both PDK1 and the phosphorylation of PKC-zeta and
-delta by a C-terminal PRK2 fragment.";
Biochemistry 41:561-569(2002).
[12]
INTERACTION WITH MUC1, AND FUNCTION.
PubMed=11877440; DOI=10.1074/jbc.M200436200;
Ren J., Li Y., Kufe D.;
"Protein kinase C delta regulates function of the DF3/MUC1 carcinoma
antigen in beta-catenin signaling.";
J. Biol. Chem. 277:17616-17622(2002).
[13]
INTERACTION WITH RAD9A.
PubMed=12628935; DOI=10.1093/emboj/cdg134;
Yoshida K., Wang H.-G., Miki Y., Kufe D.;
"Protein kinase Cdelta is responsible for constitutive and DNA damage-
induced phosphorylation of Rad9.";
EMBO J. 22:1431-1441(2003).
[14]
FUNCTION, SUBCELLULAR LOCATION, AND PHOSPHORYLATION AT TYR-155.
PubMed=15774464; DOI=10.1074/jbc.M501374200;
Okhrimenko H., Lu W., Xiang C., Ju D., Blumberg P.M., Gomel R.,
Kazimirsky G., Brodie C.;
"Roles of tyrosine phosphorylation and cleavage of protein kinase
Cdelta in its protective effect against tumor necrosis factor-related
apoptosis inducing ligand-induced apoptosis.";
J. Biol. Chem. 280:23643-23652(2005).
[15]
FUNCTION IN PLATELET AGGREGATION, AND INTERACTION WITH VASP.
PubMed=16940418; DOI=10.1182/blood-2006-05-023739;
Pula G., Schuh K., Nakayama K., Nakayama K.I., Walter U., Poole A.W.;
"PKCdelta regulates collagen-induced platelet aggregation through
inhibition of VASP-mediated filopodia formation.";
Blood 108:4035-4044(2006).
[16]
PHOSPHORYLATION AT TYR-313 AND TYR-567.
PubMed=17570831; DOI=10.1042/BJ20070244;
Hall K.J., Jones M.L., Poole A.W.;
"Coincident regulation of PKCdelta in human platelets by
phosphorylation of Tyr311 and Tyr565 and phospholipase C signalling.";
Biochem. J. 406:501-509(2007).
[17]
SUBCELLULAR LOCATION, AUTOPHOSPHORYLATION, PHOSPHORYLATION AT SER-299;
SER-302 AND SER-304, AND MUTAGENESIS OF SER-299.
PubMed=17603046; DOI=10.1016/j.febslet.2007.06.035;
Durgan J., Michael N., Totty N., Parker P.J.;
"Novel phosphorylation site markers of protein kinase C delta
activation.";
FEBS Lett. 581:3377-3381(2007).
[18]
SUBCELLULAR LOCATION.
PubMed=17579121; DOI=10.1158/1541-7786.MCR-06-0255;
Gomel R., Xiang C., Finniss S., Lee H.K., Lu W., Okhrimenko H.,
Brodie C.;
"The localization of protein kinase Cdelta in different subcellular
sites affects its proapoptotic and antiapoptotic functions and the
activation of distinct downstream signaling pathways.";
Mol. Cancer Res. 5:627-639(2007).
[19]
PHOSPHORYLATION AT THR-50; THR-141; SER-304; THR-451; SER-506; THR-507
AND SER-664, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=17965192; DOI=10.1110/ps.072874607;
Welman A., Griffiths J.R., Whetton A.D., Dive C.;
"Protein kinase C delta is phosphorylated on five novel Ser/Thr sites
following inducible overexpression in human colorectal cancer cells.";
Protein Sci. 16:2711-2715(2007).
[20]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Platelet;
PubMed=18088087; DOI=10.1021/pr0704130;
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
Schuetz C., Walter U., Gambaryan S., Sickmann A.;
"Phosphoproteome of resting human platelets.";
J. Proteome Res. 7:526-534(2008).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-299; TYR-313; SER-503;
SER-654; SER-658 AND SER-664, AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[22]
FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
PubMed=18285462; DOI=10.1128/MCB.01530-07;
Doller A., Akool E.-S., Huwiler A., Mueller R., Radeke H.H.,
Pfeilschifter J., Eberhardt W.;
"Posttranslational modification of the AU-rich element binding protein
HuR by protein kinase Cdelta elicits angiotensin II-induced
stabilization and nuclear export of cyclooxygenase 2 mRNA.";
Mol. Cell. Biol. 28:2608-2625(2008).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-130; SER-302; SER-304;
SER-307 AND SER-664, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[24]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[25]
FUNCTION IN PLATELET RESPONSE.
PubMed=19587372; DOI=10.1182/blood-2008-11-188516;
Chari R., Kim S., Murugappan S., Sanjay A., Daniel J.L.,
Kunapuli S.P.;
"Lyn, PKC-delta, SHIP-1 interactions regulate GPVI-mediated platelet-
dense granule secretion.";
Blood 114:3056-3063(2009).
[26]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-218; TYR-313 AND
SER-664, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[27]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-313 AND SER-664, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[28]
FUNCTION IN PHOSPHORYLATION OF NCF1, AND PHOSPHORYLATION AT THR-507
AND SER-645.
PubMed=19801500; DOI=10.1189/jlb.0408230;
Kilpatrick L.E., Sun S., Li H., Vary T.C., Korchak H.M.;
"Regulation of TNF-induced oxygen radical production in human
neutrophils: role of delta-PKC.";
J. Leukoc. Biol. 87:153-164(2010).
[29]
REVIEW ON FUNCTION.
PubMed=12473183; DOI=10.1093/oxfordjournals.jbchem.a003294;
Kikkawa U., Matsuzaki H., Yamamoto T.;
"Protein kinase C delta (PKC delta): activation mechanisms and
functions.";
J. Biochem. 132:831-839(2002).
[30]
REVIEW ON FUNCTION.
PubMed=20002545; DOI=10.1111/j.1538-7836.2009.03722.x;
Harper M.T., Poole A.W.;
"Diverse functions of protein kinase C isoforms in platelet activation
and thrombus formation.";
J. Thromb. Haemost. 8:454-462(2010).
[31]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-304; TYR-374; SER-645
AND SER-664, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[32]
REVIEW ON FUNCTION.
PubMed=21103796; DOI=10.1100/tsw.2010.214;
Basu A., Pal D.;
"Two faces of protein kinase Cdelta: the contrasting roles of PKCdelta
in cell survival and cell death.";
ScientificWorldJournal 10:2272-2284(2010).
[33]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[34]
REVIEW ON FUNCTION.
PubMed=21810427; DOI=10.1016/j.yjmcc.2011.07.013;
Duquesnes N., Lezoualc'h F., Crozatier B.;
"PKC-delta and PKC-epsilon: Foes of the same family or strangers?";
J. Mol. Cell. Cardiol. 51:665-673(2011).
[35]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-304 AND SER-645, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[36]
REVIEW.
PubMed=22918451; DOI=10.1007/s00005-012-0188-8;
Zhao M., Xia L., Chen G.Q.;
"Protein kinase cdelta in apoptosis: a brief overview.";
Arch. Immunol. Ther. Exp. 60:361-372(2012).
[37]
INVOLVEMENT IN ALPS3.
PubMed=23319571; DOI=10.1182/blood-2012-10-460741;
Salzer E., Santos-Valente E., Klaver S., Ban S.A., Emminger W.,
Prengemann N.K., Garncarz W., Mullauer L., Kain R., Boztug H.,
Heitger A., Arbeiter K., Eitelberger F., Seidel M.G., Holter W.,
Pollak A., Pickl W.F., Forster-Waldl E., Boztug K.;
"B-cell deficiency and severe autoimmunity caused by deficiency of
protein kinase C delta.";
Blood 121:3112-3116(2013).
[38]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-141; SER-299; SER-302;
SER-304; SER-307; SER-503 AND SER-664, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[39]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-664, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[40]
INTERACTION WITH PRKD2.
PubMed=28428613; DOI=10.1038/s41598-017-00800-w;
Cobbaut M., Derua R., Doeppler H., Lou H.J., Vandoninck S., Storz P.,
Turk B.E., Seufferlein T., Waelkens E., Janssens V., Van Lint J.;
"Differential regulation of PKD isoforms in oxidative stress
conditions through phosphorylation of a conserved Tyr in the P+1
loop.";
Sci. Rep. 7:887-887(2017).
[41]
X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 1-123 IN COMPLEX WITH
PHOSPHOTYROSINE-CONTAINING PEPTIDE, AND INTERACTION WITH CDCP1.
PubMed=15851033; DOI=10.1016/j.cell.2005.02.019;
Benes C.H., Wu N., Elia A.E.H., Dharia T., Cantley L.C., Soltoff S.P.;
"The C2 domain of PKCdelta is a phosphotyrosine binding domain.";
Cell 121:271-280(2005).
[42]
STRUCTURE BY NMR OF 149-218.
RIKEN structural genomics initiative (RSGI);
"Solution structure of the first phorbol esters/diacylglycerol binding
domain of human protein kinase C, delta.";
Submitted (APR-2008) to the PDB data bank.
-!- 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 as well as
survival of several cancers, 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. Is highly
expressed in a number of cancer cells and promotes cell survival
and resistance against chemotherapeutic drugs by inducing cyclin
D1 (CCND1) and hyperphosphorylation of RB1, and via several pro-
survival pathways, including NF-kappa-B, AKT1 and MAPK1/3
(ERK1/2). 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 (By
similarity). Phosphorylates ELAVL1 in response to angiotensin-2
treatment (PubMed:18285462). {ECO:0000250,
ECO:0000269|PubMed:11748588, ECO:0000269|PubMed:11877440,
ECO:0000269|PubMed:15774464, ECO:0000269|PubMed:16940418,
ECO:0000269|PubMed:18285462, ECO:0000269|PubMed:19587372,
ECO:0000269|PubMed:19801500}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
{ECO:0000269|PubMed:18285462}.
-!- 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-507 (activation loop
of the kinase domain), Ser-645 (turn motif) and Ser-664
(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)
(PubMed:11781095). Interacts with RAD9A (PubMed:12628935).
Interacts with CDCP1 (PubMed:15851033). Interacts with MUC1
(PubMed:11877440). Interacts with VASP (PubMed:16940418).
Interacts with CAVIN3 (By similarity). 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 (PubMed:28428613). {ECO:0000250|UniProtKB:P28867,
ECO:0000269|PubMed:11781095, ECO:0000269|PubMed:11877440,
ECO:0000269|PubMed:12628935, ECO:0000269|PubMed:15851033,
ECO:0000269|PubMed:16940418, ECO:0000269|PubMed:28428613}.
-!- INTERACTION:
Q9BXL7:CARD11; NbExp=7; IntAct=EBI-704279, EBI-7006141;
Q9NR28:DIABLO; NbExp=4; IntAct=EBI-704279, EBI-517508;
P06241:FYN; NbExp=5; IntAct=EBI-704279, EBI-515315;
P17677:GAP43; NbExp=4; IntAct=EBI-704279, EBI-1267511;
C6GKH1:IL32; NbExp=3; IntAct=EBI-704279, EBI-9547476;
P24001-2:IL32; NbExp=7; IntAct=EBI-704279, EBI-8800907;
P19878:NCF2; NbExp=3; IntAct=EBI-704279, EBI-489611;
P11388:TOP2A; NbExp=10; IntAct=EBI-704279, EBI-539628;
P04637:TP53; NbExp=4; IntAct=EBI-704279, EBI-366083;
Q9H3D4:TP63; NbExp=2; IntAct=EBI-704279, EBI-2337775;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15774464,
ECO:0000269|PubMed:17603046, ECO:0000269|PubMed:18285462}.
Cytoplasm, perinuclear region {ECO:0000269|PubMed:15774464,
ECO:0000269|PubMed:17603046}. Nucleus
{ECO:0000269|PubMed:15774464, ECO:0000269|PubMed:17603046,
ECO:0000269|PubMed:18285462}. Cell membrane
{ECO:0000269|PubMed:17603046}; Peripheral membrane protein
{ECO:0000305|PubMed:17603046}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q05655-1; Sequence=Displayed;
Name=2; Synonyms=PKCdeltaVIII;
IsoId=Q05655-2; Sequence=VSP_043899;
Note=Antiapoptotic isoform, resistant to caspase-3 cleavage.;
-!- 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.
-!- PTM: Autophosphorylated and/or phosphorylated at Thr-507, within
the activation loop; phosphorylation at Thr-507 is not a
prerequisite for enzymatic activity. Autophosphorylated at Ser-
299, Ser-302 and Ser-304. 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-313, Tyr-334 and Tyr-567;
phosphorylation of Tyr-313 and Tyr-567 following thrombin
stimulation potentiates its kinase activity. Phosphorylated by
protein kinase PDPK1; phosphorylation is inhibited by the
apoptotic C-terminal cleavage product of PKN2.
{ECO:0000269|PubMed:11781095, ECO:0000269|PubMed:15774464,
ECO:0000269|PubMed:17570831, ECO:0000269|PubMed:17603046,
ECO:0000269|PubMed:19801500}.
-!- PTM: Proteolytically cleaved into a catalytic subunit and a
regulatory subunit by caspase-3 during apoptosis which results in
kinase activation. {ECO:0000250}.
-!- DISEASE: Autoimmune lymphoproliferative syndrome 3 (ALPS3)
[MIM:615559]: A primary immunodeficiency characterized by antibody
deficiency, hypogammaglobulinemia, recurrent bacterial infections
and an inability to mount an antibody response to antigen. The
defect results from a failure of B-cell differentiation and
impaired secretion of immunoglobulins; the numbers of circulating
B-cells is usually in the normal range, but can be low. CVID9
patients have B-cell deficiency and severe autoimmunity.
{ECO:0000269|PubMed:23319571}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
protein kinase family. PKC subfamily. {ECO:0000305}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/PRKCDID42901ch3p21.html";
-----------------------------------------------------------------------
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EMBL; L07860; AAA03176.1; -; mRNA.
EMBL; L07861; AAA03175.1; -; mRNA.
EMBL; AK313216; BAG36031.1; -; mRNA.
EMBL; CH471055; EAW65279.1; -; Genomic_DNA.
EMBL; BC043350; AAH43350.1; -; mRNA.
EMBL; Z22521; CAA80249.1; -; mRNA.
EMBL; D10495; BAA01381.1; -; mRNA.
EMBL; DQ516383; ABF68960.1; -; mRNA.
CCDS; CCDS2870.1; -. [Q05655-1]
PIR; S35704; S35704.
RefSeq; NP_001303256.1; NM_001316327.1. [Q05655-1]
RefSeq; NP_006245.2; NM_006254.3. [Q05655-1]
RefSeq; NP_997704.1; NM_212539.1. [Q05655-1]
RefSeq; XP_006713322.1; XM_006713259.2. [Q05655-1]
RefSeq; XP_016862344.1; XM_017006855.1. [Q05655-1]
RefSeq; XP_016862345.1; XM_017006856.1. [Q05655-1]
UniGene; Hs.155342; -.
PDB; 1YRK; X-ray; 1.70 A; A=1-123.
PDB; 2YUU; NMR; -; A=149-218.
PDBsum; 1YRK; -.
PDBsum; 2YUU; -.
ProteinModelPortal; Q05655; -.
SMR; Q05655; -.
BioGrid; 111566; 98.
DIP; DIP-29954N; -.
ELM; Q05655; -.
IntAct; Q05655; 48.
MINT; MINT-1346366; -.
STRING; 9606.ENSP00000331602; -.
BindingDB; Q05655; -.
ChEMBL; CHEMBL2996; -.
DrugBank; DB04376; 13-Acetylphorbol.
DrugBank; DB05013; Ingenol Mebutate.
DrugBank; DB00675; Tamoxifen.
GuidetoPHARMACOLOGY; 1485; -.
iPTMnet; Q05655; -.
PhosphoSitePlus; Q05655; -.
BioMuta; PRKCD; -.
DMDM; 205371776; -.
EPD; Q05655; -.
MaxQB; Q05655; -.
PaxDb; Q05655; -.
PeptideAtlas; Q05655; -.
PRIDE; Q05655; -.
DNASU; 5580; -.
Ensembl; ENST00000330452; ENSP00000331602; ENSG00000163932. [Q05655-1]
Ensembl; ENST00000394729; ENSP00000378217; ENSG00000163932. [Q05655-1]
GeneID; 5580; -.
KEGG; hsa:5580; -.
UCSC; uc003dgl.4; human. [Q05655-1]
CTD; 5580; -.
DisGeNET; 5580; -.
GeneCards; PRKCD; -.
HGNC; HGNC:9399; PRKCD.
HPA; CAB010469; -.
HPA; CAB013225; -.
HPA; HPA001863; -.
HPA; HPA001890; -.
MalaCards; PRKCD; -.
MIM; 176977; gene.
MIM; 615559; phenotype.
neXtProt; NX_Q05655; -.
OpenTargets; ENSG00000163932; -.
Orphanet; 3261; Autoimmune lymphoproliferative syndrome.
Orphanet; 300345; Autosomal recessive systemic lupus erythematosus.
Orphanet; 1572; Common variable immunodeficiency.
PharmGKB; PA33763; -.
eggNOG; KOG0694; Eukaryota.
eggNOG; ENOG410XNPH; LUCA.
GeneTree; ENSGT00820000126964; -.
HOGENOM; HOG000233022; -.
HOVERGEN; HBG108317; -.
InParanoid; Q05655; -.
KO; K06068; -.
OMA; FIFHKVL; -.
OrthoDB; EOG091G0QRS; -.
PhylomeDB; Q05655; -.
TreeFam; TF102004; -.
BRENDA; 2.7.11.13; 2681.
Reactome; R-HSA-111465; Apoptotic cleavage of cellular proteins.
Reactome; R-HSA-111933; Calmodulin induced events.
Reactome; R-HSA-114508; Effects of PIP2 hydrolysis.
Reactome; R-HSA-1250196; SHC1 events in ERBB2 signaling.
Reactome; R-HSA-1489509; DAG and IP3 signaling.
Reactome; R-HSA-2029485; Role of phospholipids in phagocytosis.
Reactome; R-HSA-418597; G alpha (z) signalling events.
Reactome; R-HSA-450520; HuR (ELAVL1) binds and stabilizes mRNA.
Reactome; R-HSA-5218921; VEGFR2 mediated cell proliferation.
Reactome; R-HSA-5607764; CLEC7A (Dectin-1) signaling.
Reactome; R-HSA-6798695; Neutrophil degranulation.
Reactome; R-HSA-877300; Interferon gamma signaling.
SABIO-RK; Q05655; -.
SignaLink; Q05655; -.
SIGNOR; Q05655; -.
ChiTaRS; PRKCD; human.
EvolutionaryTrace; Q05655; -.
GeneWiki; PRKCD; -.
GenomeRNAi; 5580; -.
PMAP-CutDB; Q05655; -.
PRO; PR:Q05655; -.
Proteomes; UP000005640; Chromosome 3.
Bgee; ENSG00000163932; -.
CleanEx; HS_PRKCD; -.
ExpressionAtlas; Q05655; baseline and differential.
Genevisible; Q05655; HS.
GO; GO:0035578; C:azurophil granule lumen; TAS:Reactome.
GO; GO:0005911; C:cell-cell junction; IEA:Ensembl.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0016363; C:nuclear matrix; IEA:Ensembl.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004699; F:calcium-independent protein kinase C activity; EXP:Reactome.
GO; GO:0008047; F:enzyme activator activity; IDA:UniProtKB.
GO; GO:0019899; F:enzyme binding; IDA:BHF-UCL.
GO; GO:0043560; F:insulin receptor substrate binding; ISS:BHF-UCL.
GO; GO:0019900; F:kinase binding; IPI:UniProtKB.
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; IDA:UniProtKB.
GO; GO:0019901; F:protein kinase binding; IPI:ParkinsonsUK-UCL.
GO; GO:0004697; F:protein kinase C activity; ISS:UniProtKB.
GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
GO; GO:0007202; P:activation of phospholipase C activity; TAS:Reactome.
GO; GO:0032147; P:activation of protein kinase activity; IDA:ParkinsonsUK-UCL.
GO; GO:0006915; P:apoptotic process; IDA:UniProtKB.
GO; GO:0042100; P:B cell proliferation; IEA:Ensembl.
GO; GO:0060326; P:cell chemotaxis; IMP:UniProtKB.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:1904385; P:cellular response to angiotensin; IDA:UniProtKB.
GO; GO:0070301; P:cellular response to hydrogen peroxide; IDA:ParkinsonsUK-UCL.
GO; GO:0071447; P:cellular response to hydroperoxide; IDA:UniProtKB.
GO; GO:0090398; P:cellular senescence; IMP:BHF-UCL.
GO; GO:0042742; P:defense response to bacterium; ISS:UniProtKB.
GO; GO:0097194; P:execution phase of apoptosis; TAS:Reactome.
GO; GO:0038096; P:Fc-gamma receptor signaling pathway involved in phagocytosis; TAS:Reactome.
GO; GO:0016572; P:histone phosphorylation; IDA:UniProtKB.
GO; GO:0016064; P:immunoglobulin mediated immune response; IEA:Ensembl.
GO; GO:0060333; P:interferon-gamma-mediated signaling pathway; TAS:Reactome.
GO; GO:0032613; P:interleukin-10 production; IEA:Ensembl.
GO; GO:0032615; P:interleukin-12 production; IEA:Ensembl.
GO; GO:0008631; P:intrinsic apoptotic signaling pathway in response to oxidative stress; TAS:ParkinsonsUK-UCL.
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; IMP:UniProtKB.
GO; GO:0050728; P:negative regulation of inflammatory response; IC:BHF-UCL.
GO; GO:0046627; P:negative regulation of insulin receptor signaling pathway; ISS:BHF-UCL.
GO; GO:0043407; P:negative regulation of MAP kinase activity; IMP:BHF-UCL.
GO; GO:0050732; P:negative regulation of peptidyl-tyrosine phosphorylation; ISS:BHF-UCL.
GO; GO:0090331; P:negative regulation of platelet aggregation; ISS:UniProtKB.
GO; GO:0032091; P:negative regulation of protein binding; TAS:BHF-UCL.
GO; GO:0042119; P:neutrophil activation; IDA:UniProtKB.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
GO; GO:0018105; P:peptidyl-serine phosphorylation; IDA:UniProtKB.
GO; GO:0018107; P:peptidyl-threonine phosphorylation; IDA:UniProtKB.
GO; GO:0030168; P:platelet activation; TAS:Reactome.
GO; GO:2001235; P:positive regulation of apoptotic signaling pathway; IEA:Ensembl.
GO; GO:2000304; P:positive regulation of ceramide biosynthetic process; IMP:BHF-UCL.
GO; GO:0032079; P:positive regulation of endodeoxyribonuclease activity; IMP:UniProtKB.
GO; GO:2000753; P:positive regulation of glucosylceramide catabolic process; IMP:BHF-UCL.
GO; GO:1900163; P:positive regulation of phospholipid scramblase activity; IMP:UniProtKB.
GO; GO:0035307; P:positive regulation of protein dephosphorylation; IMP:BHF-UCL.
GO; GO:0042307; P:positive regulation of protein import into nucleus; IMP:UniProtKB.
GO; GO:2001022; P:positive regulation of response to DNA damage stimulus; IMP:UniProtKB.
GO; GO:2000755; P:positive regulation of sphingomyelin catabolic process; IMP:BHF-UCL.
GO; GO:0032930; P:positive regulation of superoxide anion generation; IMP:UniProtKB.
GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
GO; GO:0050821; P:protein stabilization; NAS:UniProtKB.
GO; GO:0032956; P:regulation of actin cytoskeleton organization; IMP:CACAO.
GO; GO:0043488; P:regulation of mRNA stability; TAS:Reactome.
GO; GO:0010469; P:regulation of receptor activity; TAS:BHF-UCL.
GO; GO:0007165; P:signal transduction; TAS:Reactome.
GO; GO:0002223; P:stimulatory C-type lectin receptor signaling pathway; TAS:Reactome.
GO; GO:0023021; P:termination of signal transduction; IMP:BHF-UCL.
CDD; cd00029; C1; 2.
CDD; cd05620; STKc_nPKC_delta; 1.
Gene3D; 2.60.40.150; -; 1.
InterPro; IPR000961; AGC-kinase_C.
InterPro; IPR000008; C2_dom.
InterPro; IPR020454; DAG/PE-bd.
InterPro; IPR011009; Kinase-like_dom.
InterPro; IPR034667; nPKC_delta.
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;
Polymorphism; Reference proteome; Repeat;
Serine/threonine-protein kinase; Transferase; Tumor suppressor; Zinc;
Zinc-finger.
CHAIN 1 676 Protein kinase C delta type.
/FTId=PRO_0000055694.
CHAIN 1 329 Protein kinase C delta type regulatory
subunit. {ECO:0000250}.
/FTId=PRO_0000421667.
CHAIN 330 676 Protein kinase C delta type catalytic
subunit. {ECO:0000250}.
/FTId=PRO_0000421668.
DOMAIN 1 90 C2.
DOMAIN 349 603 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
DOMAIN 604 675 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 355 363 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
ACT_SITE 473 473 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 378 378 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
SITE 48 48 Interaction with phosphotyrosine-
containing peptide.
SITE 62 62 Interaction with phosphotyrosine-
containing peptide.
SITE 67 67 Interaction with phosphotyrosine-
containing peptide.
SITE 123 123 Interaction with phosphotyrosine-
containing peptide.
SITE 329 330 Cleavage; by caspase-3. {ECO:0000250}.
MOD_RES 43 43 Phosphothreonine.
{ECO:0000250|UniProtKB:P28867}.
MOD_RES 50 50 Phosphothreonine.
{ECO:0000269|PubMed:17965192}.
MOD_RES 64 64 Phosphotyrosine.
{ECO:0000250|UniProtKB:P09215}.
MOD_RES 130 130 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 141 141 Phosphothreonine.
{ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:17965192}.
MOD_RES 155 155 Phosphotyrosine.
{ECO:0000269|PubMed:15774464}.
MOD_RES 218 218 Phosphothreonine.
{ECO:0000244|PubMed:19369195}.
MOD_RES 299 299 Phosphoserine; by autocatalysis.
{ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:17603046}.
MOD_RES 302 302 Phosphoserine; by autocatalysis.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:17603046}.
MOD_RES 304 304 Phosphoserine; by autocatalysis.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:17603046,
ECO:0000269|PubMed:17965192}.
MOD_RES 307 307 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 313 313 Phosphotyrosine.
{ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19369195,
ECO:0000244|PubMed:19690332,
ECO:0000269|PubMed:17570831}.
MOD_RES 334 334 Phosphotyrosine; by SRC.
{ECO:0000305|PubMed:11781095}.
MOD_RES 374 374 Phosphotyrosine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 451 451 Phosphothreonine.
{ECO:0000269|PubMed:17965192}.
MOD_RES 503 503 Phosphoserine.
{ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:23186163}.
MOD_RES 506 506 Phosphoserine.
{ECO:0000269|PubMed:17965192}.
MOD_RES 507 507 Phosphothreonine; by autocatalysis.
{ECO:0000269|PubMed:17965192,
ECO:0000305|PubMed:19801500}.
MOD_RES 567 567 Phosphotyrosine.
{ECO:0000269|PubMed:17570831}.
MOD_RES 645 645 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000269|PubMed:19801500}.
MOD_RES 654 654 Phosphoserine.
{ECO:0000244|PubMed:18691976}.
MOD_RES 658 658 Phosphoserine.
{ECO:0000244|PubMed:18691976}.
MOD_RES 664 664 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19369195,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569,
ECO:0000269|PubMed:17965192}.
VAR_SEQ 328 328 Q -> QGEAGSIAPLRFLFPLRPKKGDCPPFHCQVRQ (in
isoform 2).
{ECO:0000303|PubMed:18092819}.
/FTId=VSP_043899.
VARIANT 348 348 N -> S (in dbSNP:rs33911937).
/FTId=VAR_035347.
VARIANT 375 375 F -> S (in dbSNP:rs1056998).
{ECO:0000269|PubMed:8357834}.
/FTId=VAR_006175.
VARIANT 410 410 L -> F (in dbSNP:rs34502209).
/FTId=VAR_035348.
VARIANT 483 483 R -> W (in dbSNP:rs35891605).
/FTId=VAR_046009.
VARIANT 494 494 M -> V. {ECO:0000269|PubMed:7988719}.
/FTId=VAR_020610.
VARIANT 593 593 V -> M. {ECO:0000269|PubMed:8357834}.
/FTId=VAR_006176.
MUTAGEN 299 299 S->A: Loss of phosphorylation.
{ECO:0000269|PubMed:17603046}.
MUTAGEN 507 507 T->A: No effect on kinase activity.
{ECO:0000269|PubMed:11772397}.
CONFLICT 524 524 K -> R (in Ref. 2; BAG36031).
{ECO:0000305}.
CONFLICT 533 533 S -> A (in Ref. 8; no nucleotide entry).
{ECO:0000305}.
STRAND 1 13 {ECO:0000244|PDB:1YRK}.
STRAND 20 23 {ECO:0000244|PDB:1YRK}.
STRAND 27 38 {ECO:0000244|PDB:1YRK}.
STRAND 41 45 {ECO:0000244|PDB:1YRK}.
STRAND 58 62 {ECO:0000244|PDB:1YRK}.
STRAND 68 76 {ECO:0000244|PDB:1YRK}.
STRAND 79 87 {ECO:0000244|PDB:1YRK}.
HELIX 88 96 {ECO:0000244|PDB:1YRK}.
TURN 97 100 {ECO:0000244|PDB:1YRK}.
STRAND 101 107 {ECO:0000244|PDB:1YRK}.
STRAND 109 111 {ECO:0000244|PDB:1YRK}.
STRAND 113 123 {ECO:0000244|PDB:1YRK}.
HELIX 156 158 {ECO:0000244|PDB:2YUU}.
STRAND 161 164 {ECO:0000244|PDB:2YUU}.
STRAND 173 175 {ECO:0000244|PDB:2YUU}.
STRAND 181 183 {ECO:0000244|PDB:2YUU}.
STRAND 186 189 {ECO:0000244|PDB:2YUU}.
TURN 190 192 {ECO:0000244|PDB:2YUU}.
HELIX 200 202 {ECO:0000244|PDB:2YUU}.
SEQUENCE 676 AA; 77505 MW; 013F4314A2EE331A CRC64;
MAPFLRIAFN SYELGSLQAE DEANQPFCAV KMKEALSTER GKTLVQKKPT MYPEWKSTFD
AHIYEGRVIQ IVLMRAAEEP VSEVTVGVSV LAERCKKNNG KAEFWLDLQP QAKVLMSVQY
FLEDVDCKQS MRSEDEAKFP TMNRRGAIKQ AKIHYIKNHE FIATFFGQPT FCSVCKDFVW
GLNKQGYKCR QCNAAIHKKC IDKIIGRCTG TAANSRDTIF QKERFNIDMP HRFKVHNYMS
PTFCDHCGSL LWGLVKQGLK CEDCGMNVHH KCREKVANLC GINQKLLAEA LNQVTQRASR
RSDSASSEPV GIYQGFEKKT GVAGEDMQDN SGTYGKIWEG SSKCNINNFI FHKVLGKGSF
GKVLLGELKG RGEYFAIKAL KKDVVLIDDD VECTMVEKRV LTLAAENPFL THLICTFQTK
DHLFFVMEFL NGGDLMYHIQ DKGRFELYRA TFYAAEIMCG LQFLHSKGII YRDLKLDNVL
LDRDGHIKIA DFGMCKENIF GESRASTFCG TPDYIAPEIL QGLKYTFSVD WWSFGVLLYE
MLIGQSPFHG DDEDELFESI RVDTPHYPRW ITKESKDILE KLFEREPTKR LGVTGNIKIH
PFFKTINWTL LEKRRLEPPF RPKVKSPRDY SNFDQEFLNE KARLSYSDKN LIDSMDQSAF
AGFSFVNPKF EHLLED


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