NameProtein kinase C delta type
Synonyms
  • 2.7.11.13
  • nPKC-delta
  • Tyrosine-protein kinase PRKCD
Gene NamePRKCD
OrganismHuman
Amino acid sequence
>lcl|BSEQ0037204|Protein kinase C delta type
MAPFLRIAFNSYELGSLQAEDEANQPFCAVKMKEALSTERGKTLVQKKPTMYPEWKSTFD
AHIYEGRVIQIVLMRAAEEPVSEVTVGVSVLAERCKKNNGKAEFWLDLQPQAKVLMSVQY
FLEDVDCKQSMRSEDEAKFPTMNRRGAIKQAKIHYIKNHEFIATFFGQPTFCSVCKDFVW
GLNKQGYKCRQCNAAIHKKCIDKIIGRCTGTAANSRDTIFQKERFNIDMPHRFKVHNYMS
PTFCDHCGSLLWGLVKQGLKCEDCGMNVHHKCREKVANLCGINQKLLAEALNQVTQRASR
RSDSASSEPVGIYQGFEKKTGVAGEDMQDNSGTYGKIWEGSSKCNINNFIFHKVLGKGSF
GKVLLGELKGRGEYFAIKALKKDVVLIDDDVECTMVEKRVLTLAAENPFLTHLICTFQTK
DHLFFVMEFLNGGDLMYHIQDKGRFELYRATFYAAEIMCGLQFLHSKGIIYRDLKLDNVL
LDRDGHIKIADFGMCKENIFGESRASTFCGTPDYIAPEILQGLKYTFSVDWWSFGVLLYE
MLIGQSPFHGDDEDELFESIRVDTPHYPRWITKESKDILEKLFEREPTKRLGVTGNIKIH
PFFKTINWTLLEKRRLEPPFRPKVKSPRDYSNFDQEFLNEKARLSYSDKNLIDSMDQSAF
AGFSFVNPKFEHLLED
Number of residues676
Molecular Weight77504.445
Theoretical pI7.81
GO Classification
Functions
  • enzyme activator activity
  • metal ion binding
  • non-membrane spanning protein tyrosine kinase activity
  • calcium-independent protein kinase C activity
  • insulin receptor substrate binding
  • enzyme binding
  • protein kinase C activity
  • ATP binding
  • kinase binding
  • protein kinase activity
  • protein serine/threonine kinase activity
Processes
  • activation of phospholipase C activity
  • positive regulation of glucosylceramide catabolic process
  • Fc-gamma receptor signaling pathway involved in phagocytosis
  • protein stabilization
  • programmed cell death
  • regulation of receptor activity
  • positive regulation of phospholipid scramblase activity
  • innate immune response
  • negative regulation of glial cell apoptotic process
  • peptidyl-threonine phosphorylation
  • positive regulation of protein import into nucleus
  • regulation of actin cytoskeleton organization
  • histone phosphorylation
  • positive regulation of response to DNA damage stimulus
  • apoptotic process
  • interleukin-10 production
  • positive regulation of apoptotic signaling pathway
  • positive regulation of sphingomyelin catabolic process
  • fibroblast growth factor receptor signaling pathway
  • cellular senescence
  • positive regulation of protein dephosphorylation
  • termination of signal transduction
  • neurotrophin TRK receptor signaling pathway
  • positive regulation of ceramide biosynthetic process
  • cell cycle
  • regulation of mRNA stability
  • protein phosphorylation
  • platelet activation
  • interferon-gamma-mediated signaling pathway
  • stimulatory C-type lectin receptor signaling pathway
  • cellular response to hydroperoxide
  • negative regulation of MAP kinase activity
  • vascular endothelial growth factor receptor signaling pathway
  • defense response to bacterium
  • interleukin-12 production
  • positive regulation of superoxide anion generation
  • immunoglobulin mediated immune response
  • intrinsic apoptotic signaling pathway in response to oxidative stress
  • gene expression
  • negative regulation of insulin receptor signaling pathway
  • signal transduction
  • cell chemotaxis
  • negative regulation of actin filament polymerization
  • neutrophil activation
  • B cell proliferation
  • negative regulation of filopodium assembly
  • negative regulation of inflammatory response
  • negative regulation of peptidyl-tyrosine phosphorylation
  • cellular component disassembly involved in execution phase of apoptosis
  • blood coagulation
  • cytokine-mediated signaling pathway
  • negative regulation of platelet aggregation
  • negative regulation of protein binding
  • positive regulation of endodeoxyribonuclease activity
  • epidermal growth factor receptor signaling pathway
Components
  • endoplasmic reticulum
  • plasma membrane
  • cell-cell junction
  • cytoplasm
  • mitochondrion
  • cytosol
  • extracellular exosome
  • nucleoplasm
  • perinuclear region of cytoplasm
  • nucleus
  • nuclear matrix
General FunctionProtein serine/threonine kinase activity
Specific FunctionCalcium-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).
Pfam Domain Function
Transmembrane RegionsNot Available
GenBank Protein IDNot Available
UniProtKB IDQ05655
UniProtKB Entry NameKPCD_HUMAN
Cellular LocationCytoplasm
Gene sequence
>lcl|BSEQ0011729|Protein kinase C delta type (PRKCD)
ATGGCGCCGTTCCTGCGCATCGCCTTCAACTCCTATGAGCTGGGCTCCCTGCAGGCCGAG
GACGAGGCGAACCAGCCCTTCTGTGCCGTGAAGATGAAGGAGGCGCTCAGCACAGAGCGT
GGGAAAACACTGGTGCAGAAGAAGCCGACCATGTATCCTGAGTGGAAGTCGACGTTCGAT
GCCCACATCTATGAGGGGCGCGTCATCCAGATTGTGCTAATGCGGGCAGCAGAGGAGCCA
GTGTCTGAGGTGACCGTGGGTGTGTCGGTGCTGGCCGAGCGCTGCAAGAAGAACAATGGC
AAGGCTGAGTTCTGGCTGGACCTGCAGCCTCAGGCCAAGGTGTTGATGTCTGTTCAGTAT
TTCCTGGAGGACGTGGATTGCAAACAGTCTATGCGCAGTGAGGACGAGGCCAAGTTCCCA
ACGATGAACCGCCGCGGAGCCATCAAACAGGCCAAAATCCACTACATCAAGAACCATGAG
TTTATCGCCACCTTCTTTGGGCAACCCACCTTCTGTTCTGTGTGCAAAGACTTTGTCTGG
GGCCTCAACAAGCAAGGCTACAAATGCAGGCAATGTAACGCTGCCATCCACAAGAAATGC
ATCGACAAGATCATCGGCAGATGCACTGGCACCGCGGCCAACAGCCGGGACACTATATTC
CAGAAAGAACGCTTCAACATCGACATGCCGCACCGCTTCAAGGTTCACAACTACATGAGC
CCCACCTTCTGTGACCACTGCGGCAGCCTGCTCTGGGGACTGGTGAAGCAGGGATTAAAG
TGTGAAGACTGCGGCATGAATGTGCACCATAAATGCCGGGAGAAGGTGGCCAACCTCTGC
GGCATCAACCAGAAGCTTTTGGCTGAGGCCTTGAACCAAGTCACCCAGAGAGCCTCCCGG
AGATCAGACTCAGCCTCCTCAGAGCCTGTTGGGATATATCAGGGTTTCGAGAAGAAGACC
GGAGTTGCTGGGGAGGACATGCAAGACAACAGTGGGACCTACGGCAAGATCTGGGAGGGC
AGCAGCAAGTGCAACATCAACAACTTCATCTTCCACAAGGTCCTGGGCAAAGGCAGCTTC
GGGAAGGTGCTGCTTGGAGAGCTGAAGGGCAGAGGAGAGTACTTTGCCATCAAGGCCCTC
AAGAAGGATGTGGTCCTGATCGACGACGACGTGGAGTGCACCATGGTTGAGAAGCGGGTG
CTGACACTTGCCGCAGAGAATCCCTTTCTCACCCACCTCATCTGCACCTTCCAGACCAAG
GACCACCTGTTCTTTGTGATGGAGTTCCTCAACGGGGGGGACCTGATGTACCACATCCAG
GACAAAGGCCGCTTTGAACTCTACCGTGCCACGTTTTATGCCGCTGAGATAATGTGTGGA
CTGCAGTTTCTACACAGCAAGGGCATCATTTACAGGGACCTCAAACTGGACAATGTGCTG
CTGGACCGGGATGGCCACATCAAGATTGCCGACTTTGGGATGTGCAAAGAGAACATATTC
GGGGAGAGCCGGGCCAGCACCTTCTGCGGCACCCCTGACTATATCGCCCCTGAGATCCTA
CAGGGCCTGAAGTACACATTCTCTGTGGACTGGTGGTCTTTCGGGGTCCTTCTGTACGAG
ATGCTCATTGGCCAGTCCCCCTTCCATGGTGATGATGAGGATGAACTCTTCGAGTCCATC
CGTGTGGACACGCCACATTATCCCCGCTGGATCACCAAGGAGTCCAAGGACATCCTGGAG
AAGCTCTTTGAAAGGGAACCAACCAAGAGGCTGGGAGTGACCGGAAACATCAAAATCCAC
CCCTTCTTCAAGACCATAAACTGGACTCTGCTGGAAAAGCGGAGGTTGGAGCCACCTTTC
AGGCCCAAAGTGAAGTCACCCAGAGACTACAGTAACTTTGACCAGGAGTTCCTGAACGAG
AAGGCGCGCCTCTCCTACAGCGACAAGAACCTCATCGACTCCATGGACCAGTCTGCATTC
GCTGGCTTCTCCTTTGTGAACCCCAAATTCGAGCACCTCCTGGAAGATTGA
GenBank Gene IDL07860
GeneCard IDNot Available
GenAtlas IDPRKCD
HGNC IDHGNC:9399
Chromosome Location3
Locus3p21.31
References
  1. Aris JP, Basta PV, Holmes WD, Ballas LM, Moomaw C, Rankl NB, Blobel G, Loomis CR, Burns DJ: Molecular and biochemical characterization of a recombinant human PKC-delta family member. Biochim Biophys Acta. 1993 Aug 19;1174(2):171-81. 8357834
  2. 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 TO, 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. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. 14702039
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. 15489334
  4. Nomoto S, Watanabe Y, Ninomiya-Tsuji J, Yang LX, Nagai Y, Kiuchi 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. 1997 Oct;2(10):601-14. 9427282
  5. Jiang K, Apostolatos AH, Ghansah T, Watson JE, Vickers T, Cooper DR, Epling-Burnette PK, Patel NA: Identification of a novel antiapoptotic human protein kinase C delta isoform, PKCdeltaVIII in NT2 cells. Biochemistry. 2008 Jan 15;47(2):787-97. Epub 2007 Dec 20. 18092819
  6. Palmer RH, Ridden J, Parker PJ: Identification of multiple, novel, protein kinase C-related gene products. FEBS Lett. 1994 Dec 12;356(1):5-8. 7988719
  7. Bankers-Fulbright JL, Kita H, Gleich GJ, O'Grady SM: Regulation of human eosinophil NADPH oxidase activity: a central role for PKCdelta. J Cell Physiol. 2001 Dec;189(3):306-15. 11748588
  8. Liu Y, Graham C, Li A, Fisher RJ, 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. 2002 Jan 15;361(Pt 2):255-65. 11772397
  9. Hodgkinson CP, Sale GJ: Regulation of both PDK1 and the phosphorylation of PKC-zeta and -delta by a C-terminal PRK2 fragment. Biochemistry. 2002 Jan 15;41(2):561-9. 11781095
  10. 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. 2002 May 17;277(20):17616-22. Epub 2002 Mar 4. 11877440
  11. Yoshida K, Wang HG, Miki Y, Kufe D: Protein kinase Cdelta is responsible for constitutive and DNA damage-induced phosphorylation of Rad9. EMBO J. 2003 Mar 17;22(6):1431-41. 12628935
  12. Okhrimenko H, Lu W, Xiang C, Ju D, Blumberg PM, 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. 2005 Jun 24;280(25):23643-52. Epub 2005 Mar 17. 15774464
  13. Pula G, Schuh K, Nakayama K, Nakayama KI, Walter U, Poole AW: PKCdelta regulates collagen-induced platelet aggregation through inhibition of VASP-mediated filopodia formation. Blood. 2006 Dec 15;108(13):4035-44. Epub 2006 Aug 29. 16940418
  14. Hall KJ, Jones ML, Poole AW: Coincident regulation of PKCdelta in human platelets by phosphorylation of Tyr311 and Tyr565 and phospholipase C signalling. Biochem J. 2007 Sep 15;406(3):501-9. 17570831
  15. Durgan J, Michael N, Totty N, Parker PJ: Novel phosphorylation site markers of protein kinase C delta activation. FEBS Lett. 2007 Jul 24;581(18):3377-81. Epub 2007 Jun 26. 17603046
  16. Gomel R, Xiang C, Finniss S, Lee HK, 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. 2007 Jun;5(6):627-39. 17579121
  17. Welman A, Griffiths JR, Whetton AD, Dive C: Protein kinase C delta is phosphorylated on five novel Ser/Thr sites following inducible overexpression in human colorectal cancer cells. Protein Sci. 2007 Dec;16(12):2711-5. Epub 2007 Oct 26. 17965192
  18. Zahedi RP, Lewandrowski U, Wiesner J, Wortelkamp S, Moebius J, Schutz C, Walter U, Gambaryan S, Sickmann A: Phosphoproteome of resting human platelets. J Proteome Res. 2008 Feb;7(2):526-34. Epub 2007 Dec 19. 18088087
  19. Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, 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. 2008 Aug 8;31(3):438-48. doi: 10.1016/j.molcel.2008.07.007. 18691976
  20. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. doi: 10.1073/pnas.0805139105. Epub 2008 Jul 31. 18669648
  21. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. doi: 10.1021/ac9004309. 19413330
  22. Chari R, Kim S, Murugappan S, Sanjay A, Daniel JL, Kunapuli SP: Lyn, PKC-delta, SHIP-1 interactions regulate GPVI-mediated platelet-dense granule secretion. Blood. 2009 Oct 1;114(14):3056-63. doi: 10.1182/blood-2008-11-188516. Epub 2009 Jul 8. 19587372
  23. Oppermann FS, Gnad F, Olsen JV, Hornberger R, Greff Z, Keri G, Mann M, Daub H: Large-scale proteomics analysis of the human kinome. Mol Cell Proteomics. 2009 Jul;8(7):1751-64. doi: 10.1074/mcp.M800588-MCP200. Epub 2009 Apr 15. 19369195
  24. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. doi: 10.1126/scisignal.2000007. 19690332
  25. Kilpatrick LE, Sun S, Li H, Vary TC, Korchak HM: Regulation of TNF-induced oxygen radical production in human neutrophils: role of delta-PKC. J Leukoc Biol. 2010 Jan;87(1):153-64. doi: 10.1189/jlb.0408230. Epub 2009 Oct 2. 19801500
  26. Kikkawa U, Matsuzaki H, Yamamoto T: Protein kinase C delta (PKC delta): activation mechanisms and functions. J Biochem. 2002 Dec;132(6):831-9. 12473183
  27. Harper MT, Poole AW: Diverse functions of protein kinase C isoforms in platelet activation and thrombus formation. J Thromb Haemost. 2010 Mar;8(3):454-62. doi: 10.1111/j.1538-7836.2009.03722.x. Epub 2009 Dec 11. 20002545
  28. Olsen JV, Vermeulen M, Santamaria A, Kumar C, Miller ML, Jensen LJ, Gnad F, Cox J, Jensen TS, Nigg EA, Brunak S, Mann M: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis. Sci Signal. 2010 Jan 12;3(104):ra3. doi: 10.1126/scisignal.2000475. 20068231
  29. Basu A, Pal D: Two faces of protein kinase Cdelta: the contrasting roles of PKCdelta in cell survival and cell death. ScientificWorldJournal. 2010 Nov 16;10:2272-84. doi: 10.1100/tsw.2010.214. 21103796
  30. Burkard TR, Planyavsky M, Kaupe I, Breitwieser FP, Burckstummer T, Bennett KL, Superti-Furga G, Colinge J: Initial characterization of the human central proteome. BMC Syst Biol. 2011 Jan 26;5:17. doi: 10.1186/1752-0509-5-17. 21269460
  31. Duquesnes N, Lezoualc'h F, Crozatier B: PKC-delta and PKC-epsilon: foes of the same family or strangers? J Mol Cell Cardiol. 2011 Nov;51(5):665-73. doi: 10.1016/j.yjmcc.2011.07.013. Epub 2011 Jul 23. 21810427
  32. Rigbolt KT, Prokhorova TA, Akimov V, Henningsen J, Johansen PT, Kratchmarova I, Kassem M, Mann M, Olsen JV, Blagoev B: System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation. Sci Signal. 2011 Mar 15;4(164):rs3. doi: 10.1126/scisignal.2001570. 21406692
  33. Zhao M, Xia L, Chen GQ: Protein kinase cdelta in apoptosis: a brief overview. Arch Immunol Ther Exp (Warsz). 2012 Oct;60(5):361-72. doi: 10.1007/s00005-012-0188-8. Epub 2012 Aug 24. 22918451
  34. Salzer E, Santos-Valente E, Klaver S, Ban SA, Emminger W, Prengemann NK, Garncarz W, Mullauer L, Kain R, Boztug H, Heitger A, Arbeiter K, Eitelberger F, Seidel MG, Holter W, Pollak A, Pickl WF, Forster-Waldl E, Boztug K: B-cell deficiency and severe autoimmunity caused by deficiency of protein kinase C delta. Blood. 2013 Apr 18;121(16):3112-6. doi: 10.1182/blood-2012-10-460741. Epub 2013 Jan 14. 23319571
  35. 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. 2014 Jan 16;96:253-62. doi: 10.1016/j.jprot.2013.11.014. Epub 2013 Nov 22. 24275569
  36. Benes CH, Wu N, Elia AE, Dharia T, Cantley LC, Soltoff SP: The C2 domain of PKCdelta is a phosphotyrosine binding domain. Cell. 2005 Apr 22;121(2):271-80. 15851033