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Protein kinase C alpha type (PKC-A) (PKC-alpha) (EC 2.7.11.13)

 KPCA_HUMAN              Reviewed;         672 AA.
P17252; B5BU22; Q15137; Q32M72; Q96RE4;
01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
11-JAN-2011, sequence version 4.
18-JUL-2018, entry version 215.
RecName: Full=Protein kinase C alpha type;
Short=PKC-A;
Short=PKC-alpha;
EC=2.7.11.13;
Name=PRKCA; Synonyms=PKCA, PRKACA;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ILE-568.
TISSUE=Blood;
PubMed=2336401; DOI=10.1093/nar/18.8.2183;
Finkenzeller G., Marme D., Hug H.;
"Sequence of human protein kinase C alpha.";
Nucleic Acids Res. 18:2183-2183(1990).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ILE-568.
PubMed=19054851; DOI=10.1038/nmeth.1273;
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 5:1011-1017(2008).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16625196; DOI=10.1038/nature04689;
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R.,
Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
"DNA sequence of human chromosome 17 and analysis of rearrangement in
the human lineage.";
Nature 440:1045-1049(2006).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ILE-568.
Mural R.J., Istrail S., Sutton 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.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ILE-568.
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).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 15-445.
PubMed=1714454;
McSwine-Kennick R.L., McKeegan E.M., Johnson M.D., Morin M.J.;
"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. 266:15135-15143(1991).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-57.
Haridasse V., Hackenbruck J., Glazer R.I.;
"Homo sapiens protein kinase C alpha 5-flanking sequence.";
Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
[8]
PROTEIN SEQUENCE OF 2-19.
TISSUE=Platelet;
PubMed=12665801; DOI=10.1038/nbt810;
Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
Thomas G.R., Vandekerckhove J.;
"Exploring proteomes and analyzing protein processing by mass
spectrometric identification of sorted N-terminal peptides.";
Nat. Biotechnol. 21:566-569(2003).
[9]
FUNCTION IN APOPTOSIS, AND SUBCELLULAR LOCATION.
PubMed=9738012; DOI=10.1074/jbc.273.39.25436;
Ruvolo P.P., Deng X., Carr B.K., May W.S.;
"A functional role for mitochondrial protein kinase Calpha in Bcl2
phosphorylation and suppression of apoptosis.";
J. Biol. Chem. 273:25436-25442(1998).
[10]
FUNCTION IN INFLAMMATORY RESPONSE.
PubMed=9830023; DOI=10.1074/jbc.273.49.32787;
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. 273:32787-32792(1998).
[11]
FUNCTION IN INFLAMMATORY RESPONSE.
PubMed=9873035; DOI=10.1074/jbc.274.2.939;
Han Y., Meng T., Murray N.R., Fields A.P., Brasier A.R.;
"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. 274:939-947(1999).
[12]
FUNCTION IN APOPTOSIS.
PubMed=9927633;
Shen L., Dean N.M., Glazer R.I.;
"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. 55:396-402(1999).
[13]
FUNCTION IN CELL CYCLE PROGRESSION.
PubMed=10848585; DOI=10.1128/MCB.20.13.4580-4590.2000;
Besson A., Yong V.W.;
"Involvement of p21(Waf1/Cip1) in protein kinase C alpha-induced cell
cycle progression.";
Mol. Cell. Biol. 20:4580-4590(2000).
[14]
FUNCTION IN ANGIOGENESIS.
PubMed=11909826; DOI=10.1161/01.RES.0000012503.30315.E8;
Wang A., Nomura M., Patan S., Ware J.A.;
"Inhibition of protein kinase Calpha prevents endothelial cell
migration and vascular tube formation in vitro and myocardial
neovascularization in vivo.";
Circ. Res. 90:609-616(2002).
[15]
INTERACTION WITH ADAP1.
PubMed=12893243; DOI=10.1016/S0006-291X(03)01187-2;
Zemlickova E., Dubois T., Kerai P., Clokie S., Cronshaw A.D.,
Wakefield R.I.D., Johannes F.-J., Aitken A.;
"Centaurin-alpha(1) associates with and is phosphorylated by isoforms
of protein kinase C.";
Biochem. Biophys. Res. Commun. 307:459-465(2003).
[16]
FUNCTION IN PLATELET AGGREGATION.
PubMed=12724315; DOI=10.1074/jbc.M212407200;
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. 278:26374-26379(2003).
[17]
FUNCTION IN PHOSPHORYLATION OF TNNT2/CTNT.
PubMed=12832403; DOI=10.1074/jbc.M306325200;
Sumandea M.P., Pyle W.G., Kobayashi T., de Tombe P.P., Solaro R.J.;
"Identification of a functionally critical protein kinase C
phosphorylation residue of cardiac troponin T.";
J. Biol. Chem. 278:35135-35144(2003).
[18]
FUNCTION IN KIT SIGNALING.
PubMed=15526160; DOI=10.1007/s00018-004-4189-6;
Ronnstrand L.;
"Signal transduction via the stem cell factor receptor/c-Kit.";
Cell. Mol. Life Sci. 61:2535-2548(2004).
[19]
FUNCTION IN PHOSPHORYLATION OF TRPC1.
PubMed=15016832; DOI=10.1074/jbc.M313975200;
Ahmmed G.U., Mehta D., Vogel S., Holinstat M., Paria B.C.,
Tiruppathi C., Malik A.B.;
"Protein kinase Calpha phosphorylates the TRPC1 channel and regulates
store-operated Ca2+ entry in endothelial cells.";
J. Biol. Chem. 279:20941-20949(2004).
[20]
INTERACTION WITH PICK1.
PubMed=15247289; DOI=10.1074/jbc.M404499200;
Dev K.K., Nakanishi S., Henley J.M.;
"The PDZ domain of PICK1 differentially accepts protein kinase C-alpha
and GluR2 as interacting ligands.";
J. Biol. Chem. 279:41393-41397(2004).
[21]
FUNCTION IN PHOSPHORYLATION OF CSPG4, AND INTERACTION WITH CSPG4.
PubMed=15504744; DOI=10.1074/jbc.M411045200;
Makagiansar I.T., Williams S., Dahlin-Huppe K., Fukushi J.,
Mustelin T., Stallcup W.B.;
"Phosphorylation of NG2 proteoglycan by protein kinase C-alpha
regulates polarized membrane distribution and cell motility.";
J. Biol. Chem. 279:55262-55270(2004).
[22]
REVIEW ON ROLE IN KIT SIGNALING.
PubMed=16129412; DOI=10.1016/j.bbrc.2005.08.055;
Roskoski R. Jr.;
"Signaling by Kit protein-tyrosine kinase--the stem cell factor
receptor.";
Biochem. Biophys. Res. Commun. 337:1-13(2005).
[23]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[24]
INTERACTION WITH TRIM41.
PubMed=17893151; DOI=10.1074/jbc.M703320200;
Chen D., Gould C., Garza R., Gao T., Hampton R.Y., Newton A.C.;
"Amplitude control of protein kinase C by RINCK, a novel E3 ubiquitin
ligase.";
J. Biol. Chem. 282:33776-33787(2007).
[25]
FUNCTION IN ANGIOGENESIS.
PubMed=18056764; DOI=10.1093/cvr/cvm085;
Xu H., Czerwinski P., Hortmann M., Sohn H.Y., Foerstermann U., Li H.;
"Protein kinase C alpha promotes angiogenic activity of human
endothelial cells via induction of vascular endothelial growth
factor.";
Cardiovasc. Res. 78:349-355(2008).
[26]
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).
[27]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-638 AND SER-651, 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).
[28]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226, 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).
[29]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND 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).
[30]
FUNCTION.
PubMed=19176525; DOI=10.1074/jbc.M808719200;
Yamasaki T., Takahashi A., Pan J., Yamaguchi N., Yokoyama K.K.;
"Phosphorylation of activation transcription factor-2 at serine 121 by
protein kinase c controls c-Jun-mediated activation of
transcription.";
J. Biol. Chem. 284:8567-8581(2009).
[31]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226, 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).
[32]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-628, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[33]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226 AND THR-638, 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).
[34]
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).
[35]
FUNCTION IN PHOSPHORYLATION OF EIF4G1.
PubMed=21576361; DOI=10.1128/MCB.05589-11;
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. 31:2947-2959(2011).
[36]
REVIEW ON FUNCTION, AND REVIEW ON ENZYME REGULATION.
PubMed=12417014; DOI=10.1093/oxfordjournals.jbchem.a003272;
Nakashima S.;
"Protein kinase C alpha (PKC alpha): regulation and biological
function.";
J. Biochem. 132:669-675(2002).
[37]
REVIEW ON FUNCTION.
PubMed=19969380; DOI=10.1016/j.tips.2009.10.006;
Konopatskaya O., Poole A.W.;
"Protein kinase Calpha: disease regulator and therapeutic target.";
Trends Pharmacol. Sci. 31:8-14(2010).
[38]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., 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. 109:12449-12454(2012).
[39]
FUNCTION IN CELL MIGRATION, AND SUBCELLULAR LOCATION.
PubMed=23990668; DOI=10.1093/jnci/djt224;
Evensen N.A., Kuscu C., Nguyen H.L., Zarrabi K., Dufour A., Kadam P.,
Hu Y.J., Pulkoski-Gross A., Bahou W.F., Zucker S., Cao J.;
"Unraveling the role of KIAA1199, a novel endoplasmic reticulum
protein, in cancer cell migration.";
J. Natl. Cancer Inst. 105:1402-1416(2013).
[40]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10 AND SER-226, 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).
[41]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226; THR-638 AND
SER-657, 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).
[42]
INTERACTION WITH PARD3.
PubMed=27925688; DOI=10.1002/humu.23153;
Chen X., An Y., Gao Y., Guo L., Rui L., Xie H., Sun M., Lam Hung S.,
Sheng X., Zou J., Bao Y., Guan H., Niu B., Li Z., Finnell R.H.,
Gusella J.F., Wu B.L., Zhang T.;
"Rare deleterious PARD3 variants in the aPKC-binding region are
implicated in the pathogenesis of human cranial neural tube defects
via disrupting apical tight junction formation.";
Hum. Mutat. 38:378-389(2017).
[43]
FUNCTION.
PubMed=28028151; DOI=10.1084/jem.20160068;
Xu X., Han L., Zhao G., Xue S., Gao Y., Xiao J., Zhang S., Chen P.,
Wu Z.Y., Ding J., Hu R., Wei B., Wang H.;
"LRCH1 interferes with DOCK8-Cdc42-induced T cell migration and
ameliorates experimental autoimmune encephalomyelitis.";
J. Exp. Med. 214:209-226(2017).
[44]
X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 320-672 IN COMPLEX WITH
INHIBITOR.
PubMed=19827831; DOI=10.1021/jm901108b;
Wagner J., von Matt P., Sedrani R., Albert R., Cooke N., Ehrhardt C.,
Geiser M., Rummel G., Stark W., Strauss A., Cowan-Jacob S.W.,
Beerli C., Weckbecker G., Evenou J.P., 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. 52:6193-6196(2009).
[45]
STRUCTURE BY NMR OF 88-169.
RIKEN structural genomics initiative (RSGI);
"Solution structure of the second phorbol esters/diacylglycerol
binding domain of human protein kinase C alpha type.";
Submitted (APR-2008) to the PDB data bank.
[46]
VARIANTS [LARGE SCALE ANALYSIS] SER-98; ASN-467 AND VAL-489.
PubMed=17344846; DOI=10.1038/nature05610;
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C.,
Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S.,
O'Meara S., Vastrik I., Schmidt E.E., 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 D.P., Louis D.N., Goldstraw P.,
Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E.,
DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E.,
Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T.,
Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.;
"Patterns of somatic mutation in human cancer genomes.";
Nature 446:153-158(2007).
-!- FUNCTION: Calcium-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. During chemokine-induced CD4(+) T cell migration,
phosphorylates CDC42-guanine exchange factor DOCK8 resulting in
its dissociation from LRCH1 and the activation of GTPase CDC42
(PubMed:28028151). 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.
{ECO:0000269|PubMed:10848585, ECO:0000269|PubMed:11909826,
ECO:0000269|PubMed:12724315, ECO:0000269|PubMed:12832403,
ECO:0000269|PubMed:15016832, ECO:0000269|PubMed:15504744,
ECO:0000269|PubMed:15526160, ECO:0000269|PubMed:18056764,
ECO:0000269|PubMed:19176525, ECO:0000269|PubMed:21576361,
ECO:0000269|PubMed:23990668, ECO:0000269|PubMed:28028151,
ECO:0000269|PubMed:9738012, ECO:0000269|PubMed:9830023,
ECO:0000269|PubMed:9873035, ECO:0000269|PubMed:9927633}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- COFACTOR:
Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
Evidence={ECO:0000250|UniProtKB:P05696};
Note=Binds 3 Ca(2+) ions per subunit. The ions are bound to the C2
domain. {ECO:0000250|UniProtKB:P05696};
-!- ENZYME REGULATION: Classical (or conventional) PKCs (PRKCA, PRKCB
and PRKCG) are activated by calcium and diacylglycerol (DAG) in
the presence of phosphatidylserine. Three specific sites; Thr-497
(activation loop of the kinase domain), Thr-638 (turn motif) and
Ser-657 (hydrophobic region), need to be phosphorylated for its
full activation.
-!- SUBUNIT: Recruited in a circadian manner into a nuclear complex
which also includes BMAL1 and RACK1 (By similarity). Interacts
with ADAP1/CENTA1 (PubMed:12893243). Interacts with CSPG4
(PubMed:15504744). Binds to CAVIN2 in the presence of
phosphatidylserine (By similarity). Interacts with PRKCABP/PICK1
(via PDZ domain) (PubMed:15247289). Interacts with TRIM41
(PubMed:17893151). Interacts with PARD3 (PubMed:27925688).
{ECO:0000250|UniProtKB:P05696, ECO:0000250|UniProtKB:P20444,
ECO:0000269|PubMed:12893243, ECO:0000269|PubMed:15247289,
ECO:0000269|PubMed:15504744, ECO:0000269|PubMed:17893151,
ECO:0000269|PubMed:27925688}.
-!- INTERACTION:
P00533:EGFR; NbExp=2; IntAct=EBI-1383528, EBI-297353;
Q9UBN7:HDAC6; NbExp=2; IntAct=EBI-1383528, EBI-301697;
Q24008:inaD (xeno); NbExp=2; IntAct=EBI-1383528, EBI-195326;
P31431:SDC4; NbExp=2; IntAct=EBI-1383528, EBI-3913237;
P0CG48:UBC; NbExp=2; IntAct=EBI-1383528, EBI-3390054;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23990668}.
Cell membrane {ECO:0000269|PubMed:23990668}; Peripheral membrane
protein {ECO:0000305|PubMed:23990668}. Mitochondrion membrane
{ECO:0000269|PubMed:9738012}; Peripheral membrane protein
{ECO:0000305|PubMed:9738012}. Nucleus
{ECO:0000250|UniProtKB:P20444}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
protein kinase family. PKC subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; X52479; CAA36718.1; -; mRNA.
EMBL; AB451258; BAG70072.1; -; mRNA.
EMBL; AB451383; BAG70197.1; -; mRNA.
EMBL; AC005918; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC005988; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC006263; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC006947; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC009452; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC060796; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471099; EAW89014.1; -; Genomic_DNA.
EMBL; BC109273; AAI09274.1; -; mRNA.
EMBL; BC109274; AAI09275.1; -; mRNA.
EMBL; M22199; AAA60098.1; -; mRNA.
EMBL; AF395829; AAK84184.1; -; Genomic_DNA.
CCDS; CCDS11664.1; -.
PIR; S09496; KIHUCA.
RefSeq; NP_002728.1; NM_002737.2.
UniGene; Hs.531704; -.
UniGene; Hs.708867; -.
PDB; 2ELI; NMR; -; A=93-169.
PDB; 3IW4; X-ray; 2.80 A; A/B/C=320-672.
PDB; 4DNL; X-ray; 1.90 A; A=155-293.
PDB; 4RA4; X-ray; 2.63 A; A=318-672.
PDBsum; 2ELI; -.
PDBsum; 3IW4; -.
PDBsum; 4DNL; -.
PDBsum; 4RA4; -.
ProteinModelPortal; P17252; -.
SMR; P17252; -.
BioGrid; 111564; 160.
CORUM; P17252; -.
DIP; DIP-531N; -.
IntAct; P17252; 35.
MINT; P17252; -.
STRING; 9606.ENSP00000408695; -.
BindingDB; P17252; -.
ChEMBL; CHEMBL299; -.
DrugBank; DB08846; Ellagic Acid.
DrugBank; DB05013; Ingenol Mebutate.
DrugBank; DB00144; Phosphatidyl serine.
DrugBank; DB00675; Tamoxifen.
DrugBank; DB00163; Vitamin E.
GuidetoPHARMACOLOGY; 1482; -.
iPTMnet; P17252; -.
PhosphoSitePlus; P17252; -.
SwissPalm; P17252; -.
BioMuta; PRKCA; -.
DMDM; 317373571; -.
EPD; P17252; -.
MaxQB; P17252; -.
PaxDb; P17252; -.
PeptideAtlas; P17252; -.
PRIDE; P17252; -.
ProteomicsDB; 53464; -.
DNASU; 5578; -.
Ensembl; ENST00000413366; ENSP00000408695; ENSG00000154229.
GeneID; 5578; -.
KEGG; hsa:5578; -.
UCSC; uc002jfp.2; human.
CTD; 5578; -.
DisGeNET; 5578; -.
EuPathDB; HostDB:ENSG00000154229.11; -.
GeneCards; PRKCA; -.
HGNC; HGNC:9393; PRKCA.
HPA; CAB003844; -.
HPA; CAB016290; -.
HPA; HPA006563; -.
HPA; HPA006564; -.
MIM; 176960; gene.
neXtProt; NX_P17252; -.
OpenTargets; ENSG00000154229; -.
PharmGKB; PA33759; -.
eggNOG; KOG0694; Eukaryota.
eggNOG; ENOG410XNPH; LUCA.
GeneTree; ENSGT00920000148938; -.
HOGENOM; HOG000233022; -.
HOVERGEN; HBG108317; -.
InParanoid; P17252; -.
KO; K02677; -.
OMA; SSLNPCW; -.
OrthoDB; EOG091G0QRS; -.
PhylomeDB; P17252; -.
TreeFam; TF351133; -.
BRENDA; 2.7.11.13; 2681.
Reactome; R-HSA-111933; Calmodulin induced events.
Reactome; R-HSA-114516; Disinhibition of SNARE formation.
Reactome; R-HSA-1250196; SHC1 events in ERBB2 signaling.
Reactome; R-HSA-1433557; Signaling by SCF-KIT.
Reactome; R-HSA-1433559; Regulation of KIT signaling.
Reactome; R-HSA-2179392; EGFR Transactivation by Gastrin.
Reactome; R-HSA-2514859; Inactivation, recovery and regulation of the phototransduction cascade.
Reactome; R-HSA-3000170; Syndecan interactions.
Reactome; R-HSA-399997; Acetylcholine regulates insulin secretion.
Reactome; R-HSA-4086398; Ca2+ pathway.
Reactome; R-HSA-416993; Trafficking of GluR2-containing AMPA receptors.
Reactome; R-HSA-418597; G alpha (z) signalling events.
Reactome; R-HSA-4419969; Depolymerisation of the Nuclear Lamina.
Reactome; R-HSA-450520; HuR (ELAVL1) binds and stabilizes mRNA.
Reactome; R-HSA-5099900; WNT5A-dependent internalization of FZD4.
Reactome; R-HSA-5218921; VEGFR2 mediated cell proliferation.
Reactome; R-HSA-76005; Response to elevated platelet cytosolic Ca2+.
Reactome; R-HSA-8853659; RET signaling.
Reactome; R-HSA-9010642; ROBO receptors bind AKAP5.
SABIO-RK; P17252; -.
SignaLink; P17252; -.
SIGNOR; P17252; -.
ChiTaRS; PRKCA; human.
EvolutionaryTrace; P17252; -.
GeneWiki; PKC_alpha; -.
GenomeRNAi; 5578; -.
PMAP-CutDB; P17252; -.
PRO; PR:P17252; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000154229; -.
CleanEx; HS_PRKACA; -.
CleanEx; HS_PRKCA; -.
ExpressionAtlas; P17252; baseline and differential.
Genevisible; P17252; HS.
GO; GO:0035866; C:alphav-beta3 integrin-PKCalpha complex; ISS:BHF-UCL.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0005783; C:endoplasmic reticulum; IDA:BHF-UCL.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
GO; GO:0005739; C:mitochondrion; HDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004698; F:calcium-dependent protein kinase C activity; TAS:Reactome.
GO; GO:0019899; F:enzyme binding; IDA:BHF-UCL.
GO; GO:0035403; F:histone kinase activity (H3-T6 specific); IDA:UniProtKB.
GO; GO:0005178; F:integrin binding; ISS:BHF-UCL.
GO; GO:0004672; F:protein kinase activity; IDA:UniProtKB.
GO; GO:0004697; F:protein kinase C activity; ISS:BHF-UCL.
GO; GO:0004674; F:protein serine/threonine kinase activity; EXP:Reactome.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
GO; GO:0097190; P:apoptotic signaling pathway; TAS:ProtInc.
GO; GO:0007411; P:axon guidance; TAS:Reactome.
GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
GO; GO:0002159; P:desmosome assembly; IMP:BHF-UCL.
GO; GO:0038128; P:ERBB2 signaling pathway; TAS:Reactome.
GO; GO:0035408; P:histone H3-T6 phosphorylation; IDA:UniProtKB.
GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
GO; GO:0007077; P:mitotic nuclear envelope disassembly; TAS:Reactome.
GO; GO:0034351; P:negative regulation of glial cell apoptotic process; IMP:UniProtKB.
GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
GO; GO:0018107; P:peptidyl-threonine phosphorylation; ISS:ARUK-UCL.
GO; GO:0030168; P:platelet activation; TAS:Reactome.
GO; GO:0106071; P:positive regulation of adenylate cyclase-activating G-protein coupled receptor signaling pathway; ISS:BHF-UCL.
GO; GO:0045766; P:positive regulation of angiogenesis; IMP:UniProtKB.
GO; GO:0043536; P:positive regulation of blood vessel endothelial cell migration; IDA:DFLAT.
GO; GO:0045780; P:positive regulation of bone resorption; ISS:BHF-UCL.
GO; GO:0010613; P:positive regulation of cardiac muscle hypertrophy; ISS:UniProtKB.
GO; GO:0045785; P:positive regulation of cell adhesion; IMP:UniProtKB.
GO; GO:0030335; P:positive regulation of cell migration; IMP:UniProtKB.
GO; GO:2000707; P:positive regulation of dense core granule biogenesis; ISS:UniProtKB.
GO; GO:0010595; P:positive regulation of endothelial cell migration; IMP:UniProtKB.
GO; GO:0001938; P:positive regulation of endothelial cell proliferation; IMP:UniProtKB.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISS:UniProtKB.
GO; GO:0031666; P:positive regulation of lipopolysaccharide-mediated signaling pathway; IMP:UniProtKB.
GO; GO:0045651; P:positive regulation of macrophage differentiation; ISS:UniProtKB.
GO; GO:0045931; P:positive regulation of mitotic cell cycle; IMP:UniProtKB.
GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
GO; GO:0050796; P:regulation of insulin secretion; TAS:Reactome.
GO; GO:0043488; P:regulation of mRNA stability; TAS:Reactome.
GO; GO:0090330; P:regulation of platelet aggregation; IDA:UniProtKB.
GO; GO:0070555; P:response to interleukin-1; IMP:BHF-UCL.
CDD; cd00029; C1; 2.
CDD; cd05615; STKc_cPKC_alpha; 1.
Gene3D; 2.60.40.150; -; 1.
InterPro; IPR000961; AGC-kinase_C.
InterPro; IPR000008; C2_dom.
InterPro; IPR035892; C2_domain_sf.
InterPro; IPR034663; cPKC_alpha.
InterPro; IPR020454; DAG/PE-bd.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR002219; PE/DAG-bd.
InterPro; IPR017892; Pkinase_C.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR014375; Protein_kinase_C_a/b/g.
InterPro; IPR008271; Ser/Thr_kinase_AS.
Pfam; PF00130; C1_1; 2.
Pfam; PF00168; C2; 1.
Pfam; PF00069; Pkinase; 1.
Pfam; PF00433; Pkinase_C; 1.
PIRSF; PIRSF000550; PKC_alpha; 1.
PRINTS; PR00360; C2DOMAIN.
PRINTS; PR00008; DAGPEDOMAIN.
SMART; SM00109; C1; 2.
SMART; SM00239; C2; 1.
SMART; SM00133; S_TK_X; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS51285; AGC_KINASE_CTER; 1.
PROSITE; PS50004; C2; 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; Acetylation; Angiogenesis; Apoptosis; ATP-binding;
Calcium; Cell adhesion; Cell membrane; Complete proteome; Cytoplasm;
Direct protein sequencing; Kinase; Membrane; Metal-binding;
Mitochondrion; Nucleotide-binding; Nucleus; Phosphoprotein;
Polymorphism; Proto-oncogene; Reference proteome; Repeat;
Serine/threonine-protein kinase; Transferase; Zinc; Zinc-finger.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22814378,
ECO:0000269|PubMed:12665801}.
CHAIN 2 672 Protein kinase C alpha type.
/FTId=PRO_0000055679.
DOMAIN 172 260 C2. {ECO:0000255|PROSITE-
ProRule:PRU00041}.
DOMAIN 339 597 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
DOMAIN 598 668 AGC-kinase C-terminal.
ZN_FING 36 86 Phorbol-ester/DAG-type 1.
{ECO:0000255|PROSITE-ProRule:PRU00226}.
ZN_FING 101 151 Phorbol-ester/DAG-type 2.
{ECO:0000255|PROSITE-ProRule:PRU00226}.
NP_BIND 345 353 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
ACT_SITE 463 463 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
METAL 186 186 Calcium 1; via carbonyl oxygen.
{ECO:0000250|UniProtKB:P05696}.
METAL 187 187 Calcium 1.
{ECO:0000250|UniProtKB:P05696}.
METAL 187 187 Calcium 2.
{ECO:0000250|UniProtKB:P05696}.
METAL 193 193 Calcium 2.
{ECO:0000250|UniProtKB:P05696}.
METAL 246 246 Calcium 1.
{ECO:0000250|UniProtKB:P05696}.
METAL 246 246 Calcium 2.
{ECO:0000250|UniProtKB:P05696}.
METAL 247 247 Calcium 2; via carbonyl oxygen.
{ECO:0000250|UniProtKB:P05696}.
METAL 248 248 Calcium 1.
{ECO:0000250|UniProtKB:P05696}.
METAL 248 248 Calcium 2.
{ECO:0000250|UniProtKB:P05696}.
METAL 248 248 Calcium 3.
{ECO:0000250|UniProtKB:P05696}.
METAL 252 252 Calcium 3; via carbonyl oxygen.
{ECO:0000250|UniProtKB:P05696}.
METAL 254 254 Calcium 1.
{ECO:0000250|UniProtKB:P05696}.
METAL 254 254 Calcium 3.
{ECO:0000250|UniProtKB:P05696}.
BINDING 195 195 Inositol phosphate group.
{ECO:0000250|UniProtKB:P05696}.
BINDING 245 245 Inositol phosphate group.
{ECO:0000250|UniProtKB:P05696}.
BINDING 368 368 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22814378}.
MOD_RES 10 10 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 226 226 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 319 319 Phosphoserine.
{ECO:0000250|UniProtKB:P05696}.
MOD_RES 494 494 Phosphothreonine.
{ECO:0000250|UniProtKB:P04409}.
MOD_RES 495 495 Phosphothreonine.
{ECO:0000250|UniProtKB:P04409}.
MOD_RES 497 497 Phosphothreonine; by PDPK1.
{ECO:0000250|UniProtKB:P04409,
ECO:0000305}.
MOD_RES 501 501 Phosphothreonine.
{ECO:0000250|UniProtKB:P05771}.
MOD_RES 628 628 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 631 631 Phosphothreonine; by autocatalysis.
{ECO:0000250|UniProtKB:P68403,
ECO:0000255}.
MOD_RES 638 638 Phosphothreonine; by autocatalysis.
{ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:24275569}.
MOD_RES 651 651 Phosphoserine.
{ECO:0000244|PubMed:18691976}.
MOD_RES 657 657 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 658 658 Phosphotyrosine; by SYK.
{ECO:0000250|UniProtKB:P20444}.
VARIANT 98 98 P -> S (in a colorectal adenocarcinoma
sample; somatic mutation).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042301.
VARIANT 467 467 D -> N (in a glioblastoma multiforme
sample; somatic mutation).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042302.
VARIANT 489 489 M -> V (in dbSNP:rs34406842).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042303.
VARIANT 568 568 V -> I (in dbSNP:rs6504459).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:19054851,
ECO:0000269|PubMed:2336401,
ECO:0000269|Ref.4}.
/FTId=VAR_050558.
CONFLICT 50 50 C -> S (in Ref. 6; AAA60098).
{ECO:0000305}.
TURN 98 100 {ECO:0000244|PDB:2ELI}.
STRAND 105 107 {ECO:0000244|PDB:2ELI}.
STRAND 116 118 {ECO:0000244|PDB:2ELI}.
STRAND 125 127 {ECO:0000244|PDB:2ELI}.
STRAND 129 131 {ECO:0000244|PDB:2ELI}.
STRAND 133 135 {ECO:0000244|PDB:2ELI}.
STRAND 138 140 {ECO:0000244|PDB:2ELI}.
TURN 141 146 {ECO:0000244|PDB:2ELI}.
STRAND 161 169 {ECO:0000244|PDB:4DNL}.
STRAND 172 182 {ECO:0000244|PDB:4DNL}.
STRAND 194 202 {ECO:0000244|PDB:4DNL}.
STRAND 222 230 {ECO:0000244|PDB:4DNL}.
HELIX 233 237 {ECO:0000244|PDB:4DNL}.
STRAND 239 246 {ECO:0000244|PDB:4DNL}.
STRAND 249 251 {ECO:0000244|PDB:4DNL}.
STRAND 254 262 {ECO:0000244|PDB:4DNL}.
HELIX 263 268 {ECO:0000244|PDB:4DNL}.
STRAND 271 276 {ECO:0000244|PDB:4DNL}.
HELIX 282 284 {ECO:0000244|PDB:4DNL}.
HELIX 336 338 {ECO:0000244|PDB:4RA4}.
STRAND 339 350 {ECO:0000244|PDB:4RA4}.
STRAND 352 361 {ECO:0000244|PDB:4RA4}.
STRAND 364 371 {ECO:0000244|PDB:4RA4}.
HELIX 372 377 {ECO:0000244|PDB:4RA4}.
HELIX 381 392 {ECO:0000244|PDB:4RA4}.
STRAND 403 408 {ECO:0000244|PDB:4RA4}.
STRAND 410 417 {ECO:0000244|PDB:4RA4}.
STRAND 422 424 {ECO:0000244|PDB:3IW4}.
HELIX 425 432 {ECO:0000244|PDB:4RA4}.
HELIX 437 456 {ECO:0000244|PDB:4RA4}.
HELIX 466 468 {ECO:0000244|PDB:4RA4}.
STRAND 469 471 {ECO:0000244|PDB:4RA4}.
STRAND 477 479 {ECO:0000244|PDB:4RA4}.
HELIX 502 504 {ECO:0000244|PDB:4RA4}.
HELIX 507 510 {ECO:0000244|PDB:4RA4}.
HELIX 518 533 {ECO:0000244|PDB:4RA4}.
HELIX 543 552 {ECO:0000244|PDB:4RA4}.
HELIX 563 572 {ECO:0000244|PDB:4RA4}.
HELIX 577 579 {ECO:0000244|PDB:4RA4}.
HELIX 587 593 {ECO:0000244|PDB:4RA4}.
HELIX 595 597 {ECO:0000244|PDB:4RA4}.
HELIX 602 606 {ECO:0000244|PDB:4RA4}.
HELIX 642 646 {ECO:0000244|PDB:4RA4}.
HELIX 650 653 {ECO:0000244|PDB:4RA4}.
SEQUENCE 672 AA; 76750 MW; 9EB157789A062349 CRC64;
MADVFPGNDS TASQDVANRF ARKGALRQKN VHEVKDHKFI ARFFKQPTFC SHCTDFIWGF
GKQGFQCQVC CFVVHKRCHE FVTFSCPGAD KGPDTDDPRS KHKFKIHTYG SPTFCDHCGS
LLYGLIHQGM KCDTCDMNVH KQCVINVPSL CGMDHTEKRG RIYLKAEVAD EKLHVTVRDA
KNLIPMDPNG LSDPYVKLKL IPDPKNESKQ KTKTIRSTLN PQWNESFTFK LKPSDKDRRL
SVEIWDWDRT TRNDFMGSLS FGVSELMKMP ASGWYKLLNQ EEGEYYNVPI PEGDEEGNME
LRQKFEKAKL GPAGNKVISP SEDRKQPSNN LDRVKLTDFN FLMVLGKGSF GKVMLADRKG
TEELYAIKIL KKDVVIQDDD VECTMVEKRV LALLDKPPFL TQLHSCFQTV DRLYFVMEYV
NGGDLMYHIQ QVGKFKEPQA VFYAAEISIG LFFLHKRGII YRDLKLDNVM LDSEGHIKIA
DFGMCKEHMM DGVTTRTFCG TPDYIAPEII AYQPYGKSVD WWAYGVLLYE MLAGQPPFDG
EDEDELFQSI MEHNVSYPKS LSKEAVSVCK GLMTKHPAKR LGCGPEGERD VREHAFFRRI
DWEKLENREI QPPFKPKVCG KGAENFDKFF TRGQPVLTPP DQLVIANIDQ SDFEGFSYVN
PQFVHPILQS AV


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