Protein kinase C alpha type

NameProtein kinase C alpha type
Synonyms2.7.11.13 PKC-A PKCA PRKACA
Gene NamePRKCA
OrganismHuman
Amino acid sequence
>lcl|BSEQ0020507|Protein kinase C alpha type
MADVFPGNDSTASQDVANRFARKGALRQKNVHEVKDHKFIARFFKQPTFCSHCTDFIWGF
GKQGFQCQVCCFVVHKRCHEFVTFSCPGADKGPDTDDPRSKHKFKIHTYGSPTFCDHCGS
LLYGLIHQGMKCDTCDMNVHKQCVINVPSLCGMDHTEKRGRIYLKAEVADEKLHVTVRDA
KNLIPMDPNGLSDPYVKLKLIPDPKNESKQKTKTIRSTLNPQWNESFTFKLKPSDKDRRL
SVEIWDWDRTTRNDFMGSLSFGVSELMKMPASGWYKLLNQEEGEYYNVPIPEGDEEGNME
LRQKFEKAKLGPAGNKVISPSEDRKQPSNNLDRVKLTDFNFLMVLGKGSFGKVMLADRKG
TEELYAIKILKKDVVIQDDDVECTMVEKRVLALLDKPPFLTQLHSCFQTVDRLYFVMEYV
NGGDLMYHIQQVGKFKEPQAVFYAAEISIGLFFLHKRGIIYRDLKLDNVMLDSEGHIKIA
DFGMCKEHMMDGVTTRTFCGTPDYIAPEIIAYQPYGKSVDWWAYGVLLYEMLAGQPPFDG
EDEDELFQSIMEHNVSYPKSLSKEAVSVCKGLMTKHPAKRLGCGPEGERDVREHAFFRRI
DWEKLENREIQPPFKPKVCGKGAENFDKFFTRGQPVLTPPDQLVIANIDQSDFEGFSYVN
PQFVHPILQSAV
Number of residues672
Molecular Weight76749.445
Theoretical pI7.05
GO Classification
Functions
    calcium-dependent protein kinase C activity
histone kinase activity (H3-T6 specific)
ATP binding
protein kinase C activity
protein kinase activity
protein serine/threonine kinase activity
zinc ion binding
enzyme binding
Processes
    regulation of platelet aggregation
regulation of peptidyl-tyrosine phosphorylation
positive regulation of cell migration
positive regulation of inflammatory response
regulation of rhodopsin mediated signaling pathway
activation of adenylate cyclase activity
desmosome assembly
cellular response to carbohydrate stimulus
phototransduction, visible light
rhodopsin mediated signaling pathway
gene expression
positive regulation of mitotic cell cycle
fibroblast growth factor receptor signaling pathway
histone H3-T6 phosphorylation
cell adhesion
angiogenesis
positive regulation of blood vessel endothelial cell migration
small molecule metabolic process
positive regulation of angiogenesis
negative regulation of cell proliferation
mitotic nuclear envelope disassembly
mitotic cell cycle
regulation of muscle contraction
neurotrophin TRK receptor signaling pathway
negative regulation of insulin receptor signaling pathway
blood coagulation
cellular calcium ion homeostasis
inactivation of MAPK activity
apoptotic signaling pathway
protein phosphorylation
regulation of the force of heart contraction
negative regulation of adenylate cyclase activity
positive regulation of endothelial cell proliferation
vascular endothelial growth factor receptor signaling pathway
induction of positive chemotaxis
activation of phospholipase C activity
intrinsic apoptotic signaling pathway
peptidyl-serine autophosphorylation
chondrocyte differentiation
synaptic transmission
positive regulation of cardiac muscle hypertrophy
response to interleukin-1
negative regulation of glucose import
epidermal growth factor receptor signaling pathway
energy reserve metabolic process
negative regulation of glial cell apoptotic process
platelet activation
positive regulation of endothelial cell migration
positive regulation of lipopolysaccharide-mediated signaling pathway
innate immune response
regulation of mRNA stability
regulation of insulin secretion
positive regulation of macrophage differentiation
positive regulation of ERK1 and ERK2 cascade
extracellular matrix organization
positive regulation of dense core granule biogenesis
positive regulation of cell adhesion
signal transduction
neutrophil chemotaxis
Components
    mitochondrial membrane
neuronal cell body
cytosol
apical part of cell
extracellular exosome
endoplasmic reticulum
photoreceptor outer segment
nucleoplasm
plasma membrane
perinuclear region of cytoplasm
dendrite
cytoplasm
mitochondrion
General FunctionZinc ion binding
Specific FunctionCalcium-activated, phospholipid- and diacylglycerol (DAG)-dependent serine/threonine-protein kinase that is involved in positive and negative regulation of cell proliferation, apoptosis, differentiation, migration and adhesion, tumorigenesis, cardiac hypertrophy, angiogenesis, platelet function and inflammation, by directly phosphorylating targets such as RAF1, BCL2, CSPG4, TNNT2/CTNT, or activating signaling cascade involving MAPK1/3 (ERK1/2) and RAP1GAP. Involved in cell proliferation and cell growth arrest by positive and negative regulation of the cell cycle. Can promote cell growth by phosphorylating and activating RAF1, which mediates the activation of the MAPK/ERK signaling cascade, and/or by up-regulating CDKN1A, which facilitates active cyclin-dependent kinase (CDK) complex formation in glioma cells. In intestinal cells stimulated by the phorbol ester PMA, can trigger a cell cycle arrest program which is associated with the accumulation of the hyper-phosphorylated growth-suppressive form of RB1 and induction of the CDK inhibitors CDKN1A and CDKN1B. Exhibits anti-apoptotic function in glioma cells and protects them from apoptosis by suppressing the p53/TP53-mediated activation of IGFBP3, and in leukemia cells mediates anti-apoptotic action by phosphorylating BCL2. During macrophage differentiation induced by macrophage colony-stimulating factor (CSF1), is translocated to the nucleus and is associated with macrophage development. After wounding, translocates from focal contacts to lamellipodia and participates in the modulation of desmosomal adhesion. Plays a role in cell motility by phosphorylating CSPG4, which induces association of CSPG4 with extensive lamellipodia at the cell periphery and polarization of the cell accompanied by increases in cell motility. Is highly expressed in a number of cancer cells where it can act as a tumor promoter and is implicated in malignant phenotypes of several tumors such as gliomas and breast cancers. Negatively regulates myocardial contractility and positively regulates angiogenesis, platelet aggregation and thrombus formation in arteries. Mediates hypertrophic growth of neonatal cardiomyocytes, in part through a MAPK1/3 (ERK1/2)-dependent signaling pathway, and upon PMA treatment, is required to induce cardiomyocyte hypertrophy up to heart failure and death, by increasing protein synthesis, protein-DNA ratio and cell surface area. Regulates cardiomyocyte function by phosphorylating cardiac troponin T (TNNT2/CTNT), which induces significant reduction in actomyosin ATPase activity, myofilament calcium sensitivity and myocardial contractility. In angiogenesis, is required for full endothelial cell migration, adhesion to vitronectin (VTN), and vascular endothelial growth factor A (VEGFA)-dependent regulation of kinase activation and vascular tube formation. Involved in the stabilization of VEGFA mRNA at post-transcriptional level and mediates VEGFA-induced cell proliferation. In the regulation of calcium-induced platelet aggregation, mediates signals from the CD36/GP4 receptor for granule release, and activates the integrin heterodimer ITGA2B-ITGB3 through the RAP1GAP pathway for adhesion. During response to lipopolysaccharides (LPS), may regulate selective LPS-induced macrophage functions involved in host defense and inflammation. But in some inflammatory responses, may negatively regulate NF-kappa-B-induced genes, through IL1A-dependent induction of NF-kappa-B inhibitor alpha (NFKBIA/IKBA). Upon stimulation with 12-O-tetradecanoylphorbol-13-acetate (TPA), phosphorylates EIF4G1, which modulates EIF4G1 binding to MKNK1 and may be involved in the regulation of EIF4E phosphorylation. Phosphorylates KIT, leading to inhibition of KIT activity. Phosphorylates ATF2 which promotes cooperation between ATF2 and JUN, activating transcription.
Transmembrane Regions
GenBank Protein ID35483
UniProtKB IDP17252
UniProtKB Entry NameKPCA_HUMAN
Cellular LocationCytoplasm
Gene sequence
>lcl|BSEQ0020508|Protein kinase C alpha type (PRKCA)
ATGGCTGACGTTTTCCCGGGCAACGACTCCACGGCGTCTCAGGACGTGGCCAACCGCTTC
GCCCGCAAAGGGGCGCTGAGGCAGAAGAACGTGCACGAGGTGAAGGACCACAAATTCATC
GCGCGCTTCTTCAAGCAGCCCACCTTCTGCAGCCACTGCACCGACTTCATCTGGGGGTTT
GGGAAACAAGGCTTCCAGTGCCAAGTTTGCTGTTTTGTGGTCCACAAGAGGTGCCATGAA
TTTGTTACTTTTTCTTGTCCGGGTGCGGATAAGGGACCCGACACTGATGACCCCAGGAGC
AAGCACAAGTTCAAAATCCACACTTACGGAAGCCCCACCTTCTGCGATCACTGTGGGTCA
CTGCTCTATGGACTTATCCATCAAGGGATGAAATGTGACACCTGCGATATGAACGTTCAC
AAGCAATGCGTCATCAATGTCCCCAGCCTCTGCGGAATGGATCACACTGAGAAGAGGGGG
CGGATTTACCTAAAGGCTGAGGTTGCTGATGAAAAGCTCCATGTCACAGTACGAGATGCA
AAAAATCTAATCCCTATGGATCCAAACGGGCTTTCAGATCCTTATGTGAAGCTGAAACTT
ATTCCTGATCCCAAGAATGAAAGCAAGCAAAAAACCAAAACCATCCGCTCCACACTAAAT
CCGCAGTGGAATGAGTCCTTTACATTCAAATTGAAACCTTCAGACAAAGACCGACGACTG
TCTGTAGAAATCTGGGACTGGGATCGAACAACAAGGAATGACTTCATGGGATCCCTTTCC
TTTGGAGTTTCGGAGCTGATGAAGATGCCGGCCAGTGGATGGTACAAGTTGCTTAACCAA
GAAGAAGGTGAGTACTACAACGTACCCATTCCGGAAGGGGACGAGGAAGGAAACATGGAA
CTCAGGCAGAAATTCGAGAAAGCCAAACTTGGCCCTGCTGGCAACAAAGTCATCAGTCCC
TCTGAAGACAGGAAACAACCTTCCAACAACCTTGACCGAGTGAAACTCACGGACTTCAAT
TTCCTCATGGTGTTGGGAAAGGGGAGTTTTGGAAAGGTGATGCTTGCCGACAGGAAGGGC
ACAGAAGAACTGTATGCAATCAAAATCCTGAAGAAGGATGTGGTGATTCAGGATGATGAC
GTGGAGTGCACCATGGTAGAAAAGCGAGTCTTGGCCCTGCTTGACAAACCCCCGTTCTTG
ACGCAGCTGCACTCCTGCTTCCAGACAGTGGATCGGCTGTACTTCGTCATGGAATATGTC
AACGGTGGGGACCTCATGTACCACATTCAGCAAGTAGGAAAATTTAAGGAACCACAAGCA
GTATTCTATGCGGCAGAGATTTCCATCGGATTGTTCTTTCTTCATAAAAGAGGAATCATT
TATAGGGATCTGAAGTTAGATAACGTCATGTTGGATTCAGAAGGACATATCAAAATTGCT
GACTTTGGGATGTGCAAGGAACACATGATGGATGGAGTCACGACCAGGACCTTCTGTGGG
ACTCCAGATTATATCGCCCCAGAGATAATCGCTTATCAGCCGTATGGAAAATCTGTGGAC
TGGTGGGCCTATGGCGTCCTGTTGTATGAAATGCTTGCCGGGCAGCCTCCATTTGATGGT
GAAGATGAAGACGAGCTATTTCAGTCTATCATGGAGCACAACGTTTCCTATCCAAAATCC
TTGTCCAAGGAGGCTGTTTCTATCTGCAAAGGACTGATGACCAAACACCCAGCCAAGCGG
CTGGGCTGTGGGCCTGAGGGGGAGAGGGACGTGAGAGAGCATGCCTTCTTCCGGAGGATC
GACTGGGAAAAACTGGAGAACAGGGAGATCCAGCCACCATTCAAGCCCAAAGTGTGTGGC
AAAGGAGCAGAGAACTTTGACAAGTTCTTCACACGAGGACAGCCCGTCTTAACACCACCT
GATCAGCTGGTTATTGCTAACATAGACCAGTCTGATTTTGAAGGGTTCTCGTATGTCAAC
CCCCAGTTTGTGCACCCCATCTTACAGAGTGCAGTATGA
GenBank Gene IDX52479
GeneCard IDNone
GenAtlas IDPRKCA
HGNC IDHGNC:9393
Chromosome Location17
Locus17q22-q23.2
References
  1. Goshima N, Kawamura Y, Fukumoto A, Miura A, Honma R, Satoh R, Wakamatsu A, Yamamoto J, Kimura K, Nishikawa T, Andoh T, Iida Y, Ishikawa K, Ito E, Kagawa N, Kaminaga C, Kanehori K, Kawakami B, Kenmochi K, Kimura R, Kobayashi M, Kuroita T, Kuwayama H, Maruyama Y, Matsuo K, Minami K, Mitsubori M, Mori M, Morishita R, Murase A, Nishikawa A, Nishikawa S, Okamoto T, Sakagami N, Sakamoto Y, Sasaki Y, Seki T, Sono S, Sugiyama A, Sumiya T, Takayama T, Takayama Y, Takeda H, Togashi T, Yahata K, Yamada H, Yanagisawa Y, Endo Y, Imamoto F, Kisu Y, Tanaka S, Isogai T, Imai J, Watanabe S, Nomura N: Human protein factory for converting the transcriptome into an in vitro-expressed proteome,. Nat Methods. 2008 Dec;5(12):1011-7.[19054851 ]
  2. 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 ]
  3. Shen L, Dean NM, Glazer RI: Induction of p53-dependent, insulin-like growth factor-binding protein-3-mediated apoptosis in glioblastoma multiforme cells by a protein kinase Calpha antisense oligonucleotide. Mol Pharmacol. 1999 Feb;55(2):396-402.[9927633 ]
  4. 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 ]
  5. 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 ]
  6. Wagner J, von Matt P, Sedrani R, Albert R, Cooke N, Ehrhardt C, Geiser M, Rummel G, Stark W, Strauss A, Cowan-Jacob SW, Beerli C, Weckbecker G, Evenou JP, Zenke G, Cottens S: Discovery of 3-(1H-indol-3-yl)-4-[2-(4-methylpiperazin-1-yl)quinazolin-4-yl]pyrrole-2,5-dione (AEB071), a potent and selective inhibitor of protein kinase C isotypes. J Med Chem. 2009 Oct 22;52(20):6193-6. doi: 10.1021/jm901108b.[19827831 ]
  7. Greenman C, Stephens P, Smith R, Dalgliesh GL, Hunter C, Bignell G, Davies H, Teague J, Butler A, Stevens C, Edkins S, O'Meara S, Vastrik I, Schmidt EE, Avis T, Barthorpe S, Bhamra G, Buck G, Choudhury B, Clements J, Cole J, Dicks E, Forbes S, Gray K, Halliday K, Harrison R, Hills K, Hinton J, Jenkinson A, Jones D, Menzies A, Mironenko T, Perry J, Raine K, Richardson D, Shepherd R, Small A, Tofts C, Varian J, Webb T, West S, Widaa S, Yates A, Cahill DP, Louis DN, Goldstraw P, Nicholson AG, Brasseur F, Looijenga L, Weber BL, Chiew YE, DeFazio A, Greaves MF, Green AR, Campbell P, Birney E, Easton DF, Chenevix-Trench G, Tan MH, Khoo SK, Teh BT, Yuen ST, Leung SY, Wooster R, Futreal PA, Stratton MR: Patterns of somatic mutation in human cancer genomes. Nature. 2007 Mar 8;446(7132):153-8.[17344846 ]
  8. Finkenzeller G, Marme D, Hug H: Sequence of human protein kinase C alpha. Nucleic Acids Res. 1990 Apr 25;18(8):2183.[2336401 ]
  9. Zody MC, Garber M, Adams DJ, Sharpe T, Harrow J, Lupski JR, Nicholson C, Searle SM, Wilming L, Young SK, Abouelleil A, Allen NR, Bi W, Bloom T, Borowsky ML, Bugalter BE, Butler J, Chang JL, Chen CK, Cook A, Corum B, Cuomo CA, de Jong PJ, DeCaprio D, Dewar K, FitzGerald M, Gilbert J, Gibson R, Gnerre S, Goldstein S, Grafham DV, Grocock R, Hafez N, Hagopian DS, Hart E, Norman CH, Humphray S, Jaffe DB, Jones M, Kamal M, Khodiyar VK, LaButti K, Laird G, Lehoczky J, Liu X, Lokyitsang T, Loveland J, Lui A, Macdonald P, Major JE, Matthews L, Mauceli E, McCarroll SA, Mihalev AH, Mudge J, Nguyen C, Nicol R, O'Leary SB, Osoegawa K, Schwartz DC, Shaw-Smith C, Stankiewicz P, Steward C, Swarbreck D, Venkataraman V, Whittaker CA, Yang X, Zimmer AR, Bradley A, Hubbard T, Birren BW, Rogers J, Lander ES, Nusbaum C: DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage. Nature. 2006 Apr 20;440(7087):1045-9.[16625196 ]
  10. McSwine-Kennick RL, McKeegan EM, Johnson MD, Morin MJ: Phorbol diester-induced alterations in the expression of protein kinase C isozymes and their mRNAs. Analysis in wild-type and phorbol diester-resistant HL-60 cell clones. J Biol Chem. 1991 Aug 15;266(23):15135-43.[1714454 ]
  11. Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J: Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. Nat Biotechnol. 2003 May;21(5):566-9. Epub 2003 Mar 31.[12665801 ]
  12. Ruvolo PP, Deng X, Carr BK, May WS: A functional role for mitochondrial protein kinase Calpha in Bcl2 phosphorylation and suppression of apoptosis. J Biol Chem. 1998 Sep 25;273(39):25436-42.[9738012 ]
  13. St-Denis A, Chano F, Tremblay P, St-Pierre Y, Descoteaux A: Protein kinase C-alpha modulates lipopolysaccharide-induced functions in a murine macrophage cell line. J Biol Chem. 1998 Dec 4;273(49):32787-92.[9830023 ]
  14. Han Y, Meng T, Murray NR, Fields AP, Brasier AR: Interleukin-1-induced nuclear factor-kappaB-IkappaBalpha autoregulatory feedback loop in hepatocytes. A role for protein kinase calpha in post-transcriptional regulation of ikappabalpha resynthesis. J Biol Chem. 1999 Jan 8;274(2):939-47.[9873035 ]
  15. Besson A, Yong VW: Involvement of p21(Waf1/Cip1) in protein kinase C alpha-induced cell cycle progression. Mol Cell Biol. 2000 Jul;20(13):4580-90.[10848585 ]
  16. Wang A, Nomura M, Patan S, Ware JA: Inhibition of protein kinase Calpha prevents endothelial cell migration and vascular tube formation in vitro and myocardial neovascularization in vivo. Circ Res. 2002 Mar 22;90(5):609-16.[11909826 ]
  17. Zemlickova E, Dubois T, Kerai P, Clokie S, Cronshaw AD, Wakefield RI, Johannes FJ, Aitken A: Centaurin-alpha(1) associates with and is phosphorylated by isoforms of protein kinase C. Biochem Biophys Res Commun. 2003 Aug 1;307(3):459-65.[12893243 ]
  18. Tabuchi A, Yoshioka A, Higashi T, Shirakawa R, Nishioka H, Kita T, Horiuchi H: Direct demonstration of involvement of protein kinase Calpha in the Ca2+-induced platelet aggregation. J Biol Chem. 2003 Jul 18;278(29):26374-9. Epub 2003 Apr 30.[12724315 ]
  19. Sumandea MP, Pyle WG, Kobayashi T, de Tombe PP, Solaro RJ: Identification of a functionally critical protein kinase C phosphorylation residue of cardiac troponin T. J Biol Chem. 2003 Sep 12;278(37):35135-44. Epub 2003 Jun 28.[12832403 ]
  20. Ronnstrand L: Signal transduction via the stem cell factor receptor/c-Kit. Cell Mol Life Sci. 2004 Oct;61(19-20):2535-48.[15526160 ]
  21. Ahmmed GU, Mehta D, Vogel S, Holinstat M, Paria BC, Tiruppathi C, Malik AB: Protein kinase Calpha phosphorylates the TRPC1 channel and regulates store-operated Ca2+ entry in endothelial cells. J Biol Chem. 2004 May 14;279(20):20941-9. Epub 2004 Mar 10.[15016832 ]
  22. Dev KK, Nakanishi S, Henley JM: The PDZ domain of PICK1 differentially accepts protein kinase C-alpha and GluR2 as interacting ligands. J Biol Chem. 2004 Oct 1;279(40):41393-7. Epub 2004 Jul 9.[15247289 ]
  23. Makagiansar IT, Williams S, Dahlin-Huppe K, Fukushi J, Mustelin T, Stallcup WB: Phosphorylation of NG2 proteoglycan by protein kinase C-alpha regulates polarized membrane distribution and cell motility. J Biol Chem. 2004 Dec 31;279(53):55262-70. Epub 2004 Oct 25.[15504744 ]
  24. Roskoski R Jr: Signaling by Kit protein-tyrosine kinase--the stem cell factor receptor. Biochem Biophys Res Commun. 2005 Nov 11;337(1):1-13.[16129412 ]
  25. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48.[17081983 ]
  26. Chen D, Gould C, Garza R, Gao T, Hampton RY, Newton AC: Amplitude control of protein kinase C by RINCK, a novel E3 ubiquitin ligase. J Biol Chem. 2007 Nov 16;282(46):33776-87. Epub 2007 Sep 24.[17893151 ]
  27. Xu H, Czerwinski P, Hortmann M, Sohn HY, Forstermann U, Li H: Protein kinase C alpha promotes angiogenic activity of human endothelial cells via induction of vascular endothelial growth factor. Cardiovasc Res. 2008 May 1;78(2):349-55. Epub 2007 Dec 4.[18056764 ]
  28. 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 ]
  29. 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 ]
  30. 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 ]
  31. Yamasaki T, Takahashi A, Pan J, Yamaguchi N, Yokoyama KK: Phosphorylation of Activation Transcription Factor-2 at Serine 121 by Protein Kinase C Controls c-Jun-mediated Activation of Transcription. J Biol Chem. 2009 Mar 27;284(13):8567-81. doi: 10.1074/jbc.M808719200. Epub 2009 Jan 28.[19176525 ]
  32. 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 ]
  33. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. doi: 10.1126/science.1175371. Epub 2009 Jul 16.[19608861 ]
  34. 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 ]
  35. 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 ]
  36. Dobrikov M, Dobrikova E, Shveygert M, Gromeier M: Phosphorylation of eukaryotic translation initiation factor 4G1 (eIF4G1) by protein kinase C{alpha} regulates eIF4G1 binding to Mnk1. Mol Cell Biol. 2011 Jul;31(14):2947-59. doi: 10.1128/MCB.05589-11. Epub 2011 May 16.[21576361 ]
  37. Nakashima S: Protein kinase C alpha (PKC alpha): regulation and biological function. J Biochem. 2002 Nov;132(5):669-75.[12417014 ]
  38. Konopatskaya O, Poole AW: Protein kinase Calpha: disease regulator and therapeutic target. Trends Pharmacol Sci. 2010 Jan;31(1):8-14. doi: 10.1016/j.tips.2009.10.006. Epub 2009 Dec 5.[19969380 ]
  39. Van Damme P, Lasa M, Polevoda B, Gazquez C, Elosegui-Artola A, Kim DS, De Juan-Pardo E, Demeyer K, Hole K, Larrea E, Timmerman E, Prieto J, Arnesen T, Sherman F, Gevaert K, Aldabe R: N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB. Proc Natl Acad Sci U S A. 2012 Jul 31;109(31):12449-54. doi: 10.1073/pnas.1210303109. Epub 2012 Jul 18.[22814378 ]
  40. Evensen NA, Kuscu C, Nguyen HL, Zarrabi K, Dufour A, Kadam P, Hu YJ, Pulkoski-Gross A, Bahou WF, Zucker S, Cao J: Unraveling the role of KIAA1199, a novel endoplasmic reticulum protein, in cancer cell migration. J Natl Cancer Inst. 2013 Sep 18;105(18):1402-16. doi: 10.1093/jnci/djt224. Epub 2013 Aug 29.[23990668 ]

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