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Protein kinase C epsilon type (EC 2.7.11.13) (nPKC-epsilon)

 KPCE_HUMAN              Reviewed;         737 AA.
Q02156; B0LPH7; Q32MQ3; Q53SL4; Q53SM5; Q9UE81;
01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
01-JUL-1993, sequence version 1.
30-AUG-2017, entry version 181.
RecName: Full=Protein kinase C epsilon type;
EC=2.7.11.13;
AltName: Full=nPKC-epsilon;
Name=PRKCE; Synonyms=PKCE;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1382605; DOI=10.1016/0167-4781(92)90006-L;
Basta P., Strickland M.B., Holmes W., Loomis C.R., Ballas L.M.,
Burns D.J.;
"Sequence and expression of human protein kinase C-epsilon.";
Biochim. Biophys. Acta 1132:154-160(1992).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
SeattleSNPs variation discovery resource;
Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[4]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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]
FUNCTION IN PHOSPHORYLATION OF KRT8.
PubMed=1374067; DOI=10.1083/jcb.117.3.583;
Omary M.B., Baxter G.T., Chou C.F., Riopel C.L., Lin W.Y.,
Strulovici B.;
"PKC epsilon-related kinase associates with and phosphorylates
cytokeratin 8 and 18.";
J. Cell Biol. 117:583-593(1992).
[7]
PHOSPHORYLATION AT THR-566 AND SER-729, AND MUTAGENESIS OF LYS-437;
THR-566; THR-710 AND SER-729.
PubMed=11964154; DOI=10.1042/0264-6021:3630537;
Cenni V., Doeppler H., Sonnenburg E.D., Maraldi N., Newton A.C.,
Toker A.;
"Regulation of novel protein kinase C epsilon by phosphorylation.";
Biochem. J. 363:537-545(2002).
[8]
FUNCTION IN PHOSPHORYLATION OF TRPV1.
PubMed=11884385; DOI=10.1074/jbc.C200104200;
Numazaki M., Tominaga T., Toyooka H., Tominaga M.;
"Direct phosphorylation of capsaicin receptor VR1 by protein kinase
Cepsilon and identification of two target serine residues.";
J. Biol. Chem. 277:13375-13378(2002).
[9]
FUNCTION IN PHOSPHORYLATION OF IQGAP1.
PubMed=15355962; DOI=10.1074/jbc.M408113200;
Grohmanova K., Schlaepfer D., Hess D., Gutierrez P., Beck M.,
Kroschewski R.;
"Phosphorylation of IQGAP1 modulates its binding to Cdc42, revealing a
new type of rho-GTPase regulator.";
J. Biol. Chem. 279:48495-48504(2004).
[10]
INTERACTION WITH DGKQ.
PubMed=15632189; DOI=10.1074/jbc.M409301200;
van Baal J., de Widt J., Divecha N., van Blitterswijk W.J.;
"Translocation of diacylglycerol kinase theta from cytosol to plasma
membrane in response to activation of G protein-coupled receptors and
protein kinase C.";
J. Biol. Chem. 280:9870-9878(2005).
[11]
FUNCTION.
PubMed=16757566; DOI=10.1073/pnas.0600462103;
McGettrick A.F., Brint E.K., Palsson-McDermott E.M., Rowe D.C.,
Golenbock D.T., Gay N.J., Fitzgerald K.A., O'Neill L.A.J.;
"Trif-related adapter molecule is phosphorylated by PKCepsilon during
Toll-like receptor 4 signaling.";
Proc. Natl. Acad. Sci. U.S.A. 103:9196-9201(2006).
[12]
FUNCTION IN PHOSPHORYLATION OF STAT3, AND INTERACTION WITH STAT3.
PubMed=17875724; DOI=10.1158/0008-5472.CAN-07-1604;
Aziz M.H., Manoharan H.T., Church D.R., Dreckschmidt N.E., Zhong W.,
Oberley T.D., Wilding G., Verma A.K.;
"Protein kinase Cepsilon interacts with signal transducers and
activators of transcription 3 (Stat3), phosphorylates Stat3Ser727, and
regulates its constitutive activation in prostate cancer.";
Cancer Res. 67:8828-8838(2007).
[13]
FUNCTION IN CELL MOTILITY, AND SUBCELLULAR LOCATION.
PubMed=17603037; DOI=10.1016/j.exer.2007.05.004;
Sharma G.D., Kakazu A., Bazan H.E.;
"Protein kinase C alpha and epsilon differentially modulate hepatocyte
growth factor-induced epithelial proliferation and migration.";
Exp. Eye Res. 85:289-297(2007).
[14]
FUNCTION IN PHOSPHORYLATION OF GABRG2.
PubMed=17875639; DOI=10.1074/jbc.M707233200;
Qi Z.H., Song M., Wallace M.J., Wang D., Newton P.M., McMahon T.,
Chou W.H., Zhang C., Shokat K.M., Messing R.O.;
"Protein kinase C epsilon regulates gamma-aminobutyrate type A
receptor sensitivity to ethanol and benzodiazepines through
phosphorylation of gamma2 subunits.";
J. Biol. Chem. 282:33052-33063(2007).
[15]
REVIEW ON FUNCTION.
PubMed=12473185; DOI=10.1093/oxfordjournals.jbchem.a003296;
Akita Y.;
"Protein kinase C-epsilon (PKC-epsilon): its unique structure and
function.";
J. Biochem. 132:847-852(2002).
[16]
REVIEW ON FUNCTION IN APOPTOSIS.
PubMed=16584980;
Vitale M., Gobbi G., Mirandola P., Ponti C., Sponzilli I., Rinaldi L.,
Manzoli F.A.;
"TNF-related apoptosis-inducing ligand (TRAIL) and erythropoiesis: a
role for PKC epsilon.";
Eur. J. Histochem. 50:15-18(2006).
[17]
REVIEW ON FUNCTION IN NEURONS.
PubMed=18637121; DOI=10.1111/j.1742-4658.2008.06556.x;
Shirai Y., Adachi N., Saito N.;
"Protein kinase Cepsilon: function in neurons.";
FEBS J. 275:3988-3994(2008).
[18]
REVIEW ON FUNCTION IN CYTOSKELETON.
PubMed=18637120; DOI=10.1111/j.1742-4658.2008.06557.x;
Akita Y.;
"Protein kinase Cepsilon: multiple roles in the function of, and
signaling mediated by, the cytoskeleton.";
FEBS J. 275:3995-4004(2008).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-228; THR-309; SER-329;
SER-388 AND THR-710, 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).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-309 AND SER-316, 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).
[21]
REVIEW.
PubMed=20350291; DOI=10.1042/BJ20091302;
Newton P.M., Messing R.O.;
"The substrates and binding partners of protein kinase Cepsilon.";
Biochem. J. 427:189-196(2010).
[22]
INTERACTION WITH HSP90AB1.
PubMed=20353823; DOI=10.1016/j.cellsig.2010.03.012;
Cheng M.B., Zhang Y., Zhong X., Sutter B., Cao C.Y., Chen X.S.,
Cheng X.K., Zhang Y., Xiao L., Shen Y.F.;
"Stat1 mediates an auto-regulation of hsp90beta gene in heat shock
response.";
Cell. Signal. 22:1206-1213(2010).
[23]
REVIEW ON FUNCTION IN NEURONS.
PubMed=21681677; DOI=10.1007/s11684-011-0119-9;
Chen Y., Tian Q.;
"The role of protein kinase C epsilon in neural signal transduction
and neurogenic diseases.";
Front. Med. 5:70-76(2011).
[24]
REVIEW.
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).
[25]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-368, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
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).
[26]
X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 342-372, AND PHOSPHORYLATION
AT SER-346 AND SER-368.
PubMed=19662078; DOI=10.1038/embor.2009.150;
Kostelecky B., Saurin A.T., Purkiss A., Parker P.J., McDonald N.Q.;
"Recognition of an intra-chain tandem 14-3-3 binding site within
PKCepsilon.";
EMBO Rep. 10:983-989(2009).
[27]
VARIANT [LARGE SCALE ANALYSIS] LYS-143.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
[28]
VARIANTS [LARGE SCALE ANALYSIS] VAL-333; ARG-389 AND MET-563.
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-independent, phospholipid- and diacylglycerol
(DAG)-dependent serine/threonine-protein kinase that plays
essential roles in the regulation of multiple cellular processes
linked to cytoskeletal proteins, such as cell adhesion, motility,
migration and cell cycle, functions in neuron growth and ion
channel regulation, and is involved in immune response, cancer
cell invasion and regulation of apoptosis. Mediates cell adhesion
to the extracellular matrix via integrin-dependent signaling, by
mediating angiotensin-2-induced activation of integrin beta-1
(ITGB1) in cardiac fibroblasts. Phosphorylates MARCKS, which
phosphorylates and activates PTK2/FAK, leading to the spread of
cardiomyocytes. Involved in the control of the directional
transport of ITGB1 in mesenchymal cells by phosphorylating
vimentin (VIM), an intermediate filament (IF) protein. In
epithelial cells, associates with and phosphorylates keratin-8
(KRT8), which induces targeting of desmoplakin at desmosomes and
regulates cell-cell contact. Phosphorylates IQGAP1, which binds to
CDC42, mediating epithelial cell-cell detachment prior to
migration. In HeLa cells, contributes to hepatocyte growth factor
(HGF)-induced cell migration, and in human corneal epithelial
cells, plays a critical role in wound healing after activation by
HGF. During cytokinesis, forms a complex with YWHAB, which is
crucial for daughter cell separation, and facilitates abscission
by a mechanism which may implicate the regulation of RHOA. In
cardiac myocytes, regulates myofilament function and excitation
coupling at the Z-lines, where it is indirectly associated with F-
actin via interaction with COPB1. During endothelin-induced
cardiomyocyte hypertrophy, mediates activation of PTK2/FAK, which
is critical for cardiomyocyte survival and regulation of sarcomere
length. Plays a role in the pathogenesis of dilated cardiomyopathy
via persistent phosphorylation of troponin I (TNNI3). Involved in
nerve growth factor (NFG)-induced neurite outgrowth and neuron
morphological change independently of its kinase activity, by
inhibition of RHOA pathway, activation of CDC42 and cytoskeletal
rearrangement. May be involved in presynaptic facilitation by
mediating phorbol ester-induced synaptic potentiation.
Phosphorylates gamma-aminobutyric acid receptor subunit gamma-2
(GABRG2), which reduces the response of GABA receptors to ethanol
and benzodiazepines and may mediate acute tolerance to the
intoxicating effects of ethanol. Upon PMA treatment,
phosphorylates the capsaicin- and heat-activated cation channel
TRPV1, which is required for bradykinin-induced sensitization of
the heat response in nociceptive neurons. Is able to form a
complex with PDLIM5 and N-type calcium channel, and may enhance
channel activities and potentiates fast synaptic transmission by
phosphorylating the pore-forming alpha subunit CACNA1B (CaV2.2).
In prostate cancer cells, interacts with and phosphorylates STAT3,
which increases DNA-binding and transcriptional activity of STAT3
and seems to be essential for prostate cancer cell invasion.
Downstream of TLR4, plays an important role in the
lipopolysaccharide (LPS)-induced immune response by
phosphorylating and activating TICAM2/TRAM, which in turn
activates the transcription factor IRF3 and subsequent cytokines
production. In differentiating erythroid progenitors, is regulated
by EPO and controls the protection against the TNFSF10/TRAIL-
mediated apoptosis, via BCL2. May be involved in the regulation of
the insulin-induced phosphorylation and activation of AKT1.
{ECO:0000269|PubMed:11884385, ECO:0000269|PubMed:1374067,
ECO:0000269|PubMed:15355962, ECO:0000269|PubMed:16757566,
ECO:0000269|PubMed:17603037, ECO:0000269|PubMed:17875639,
ECO:0000269|PubMed:17875724}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- ENZYME REGULATION: Novel PKCs (PRKCD, PRKCE, PRKCH and PRKCQ) are
calcium-insensitive, but activated by diacylglycerol (DAG) and
phosphatidylserine. Three specific sites; Thr-566 (activation loop
of the kinase domain), Thr-710 (turn motif) and Ser-729
(hydrophobic region), need to be phosphorylated for its full
activation.
-!- SUBUNIT: Forms a ternary complex with TRIM63 and GN2BL1. Can form
a complex with PDLIM5 and N-type calcium channel. Interacts with
COPB1 and YWHAB (By similarity). Interacts with DGKQ and STAT3.
Interacts with HSP90AB1; promotes functional activation in a heat
shock-dependent manner (PubMed:20353823). {ECO:0000250,
ECO:0000269|PubMed:15632189, ECO:0000269|PubMed:17875724,
ECO:0000269|PubMed:20353823}.
-!- INTERACTION:
P08238:HSP90AB1; NbExp=2; IntAct=EBI-706254, EBI-352572;
C6GKH1:IL32; NbExp=2; IntAct=EBI-706254, EBI-9547476;
Q15349:RPS6KA2; NbExp=2; IntAct=EBI-706254, EBI-1384149;
P63104:YWHAZ; NbExp=5; IntAct=EBI-706254, EBI-347088;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17603037}.
Cytoplasm, cytoskeleton {ECO:0000269|PubMed:17603037}. Cell
membrane {ECO:0000269|PubMed:17603037}. Cytoplasm, perinuclear
region {ECO:0000250}. Nucleus {ECO:0000250}. Note=Translocated to
plasma membrane in epithelial cells stimulated by HGF. Associated
with the Golgi at the perinuclear site in pre-passage fibroblasts
(By similarity). In passaging cells, translocated to the cell
periphery (By similarity). Translocated to the nucleus in PMA-
treated cells (By similarity). {ECO:0000250}.
-!- DOMAIN: The C1 domain, containing the phorbol ester/DAG-type
region 1 (C1A) and 2 (C1B), is the diacylglycerol sensor and the
C2 domain is a non-calcium binding domain.
-!- PTM: Phosphorylation on Thr-566 by PDPK1 triggers
autophosphorylation on Ser-729. Phosphorylation in the hinge
domain at Ser-350 by MAPK11 or MAPK14, Ser-346 by GSK3B and Ser-
368 by autophosphorylation is required for interaction with YWHAB.
{ECO:0000269|PubMed:11964154, ECO:0000269|PubMed:19662078}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
protein kinase family. PKC subfamily. {ECO:0000305}.
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EMBL; X65293; CAA46388.1; -; mRNA.
EMBL; EU332867; ABY87556.1; -; Genomic_DNA.
EMBL; U51244; AAD08855.1; -; Genomic_DNA.
EMBL; AC017078; AAY14773.1; -; Genomic_DNA.
EMBL; AC017006; AAX93253.1; -; Genomic_DNA.
EMBL; CH471053; EAX00258.1; -; Genomic_DNA.
EMBL; BC109033; AAI09034.1; -; mRNA.
EMBL; BC109034; AAI09035.1; -; mRNA.
CCDS; CCDS1824.1; -.
PIR; S28942; S28942.
RefSeq; NP_005391.1; NM_005400.2.
RefSeq; XP_005264485.1; XM_005264428.1.
UniGene; Hs.580351; -.
UniGene; Hs.677120; -.
PDB; 2WH0; X-ray; 2.25 A; Q/R=342-372.
PDB; 5LIH; X-ray; 3.25 A; F/G=149-164.
PDBsum; 2WH0; -.
PDBsum; 5LIH; -.
ProteinModelPortal; Q02156; -.
SMR; Q02156; -.
BioGrid; 111567; 62.
DIP; DIP-34186N; -.
ELM; Q02156; -.
IntAct; Q02156; 13.
MINT; MINT-88515; -.
STRING; 9606.ENSP00000306124; -.
BindingDB; Q02156; -.
ChEMBL; CHEMBL3582; -.
DrugBank; DB06064; KAI-1455.
DrugBank; DB00675; Tamoxifen.
GuidetoPHARMACOLOGY; 1486; -.
iPTMnet; Q02156; -.
PhosphoSitePlus; Q02156; -.
BioMuta; PRKCE; -.
DMDM; 400135; -.
EPD; Q02156; -.
MaxQB; Q02156; -.
PaxDb; Q02156; -.
PeptideAtlas; Q02156; -.
PRIDE; Q02156; -.
DNASU; 5581; -.
Ensembl; ENST00000306156; ENSP00000306124; ENSG00000171132.
GeneID; 5581; -.
KEGG; hsa:5581; -.
UCSC; uc002rut.4; human.
CTD; 5581; -.
DisGeNET; 5581; -.
GeneCards; PRKCE; -.
HGNC; HGNC:9401; PRKCE.
HPA; CAB001948; -.
HPA; HPA044496; -.
HPA; HPA054252; -.
MIM; 176975; gene.
neXtProt; NX_Q02156; -.
OpenTargets; ENSG00000171132; -.
PharmGKB; PA33765; -.
eggNOG; KOG0694; Eukaryota.
eggNOG; ENOG410XNPH; LUCA.
GeneTree; ENSGT00820000126964; -.
HOGENOM; HOG000233022; -.
HOVERGEN; HBG108317; -.
InParanoid; Q02156; -.
KO; K18050; -.
OMA; PCDQELK; -.
OrthoDB; EOG091G0QRS; -.
PhylomeDB; Q02156; -.
TreeFam; TF351133; -.
BRENDA; 2.7.11.13; 2681.
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.
SABIO-RK; Q02156; -.
SignaLink; Q02156; -.
SIGNOR; Q02156; -.
ChiTaRS; PRKCE; human.
EvolutionaryTrace; Q02156; -.
GeneWiki; PRKCE; -.
GenomeRNAi; 5581; -.
PMAP-CutDB; Q02156; -.
PRO; PR:Q02156; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000171132; -.
CleanEx; HS_PRKCE; -.
ExpressionAtlas; Q02156; baseline and differential.
Genevisible; Q02156; HS.
GO; GO:0071944; C:cell periphery; ISS:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0005783; C:endoplasmic reticulum; IDA:BHF-UCL.
GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0071889; F:14-3-3 protein binding; IEA:Ensembl.
GO; GO:0003785; F:actin monomer binding; ISS:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004699; F:calcium-independent protein kinase C activity; IEA:Ensembl.
GO; GO:0008047; F:enzyme activator activity; IMP:BHF-UCL.
GO; GO:0019899; F:enzyme binding; IDA:BHF-UCL.
GO; GO:0035276; F:ethanol binding; IEA:Ensembl.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004697; F:protein kinase C activity; IDA:BHF-UCL.
GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
GO; GO:0030546; F:receptor activator activity; IEA:Ensembl.
GO; GO:0004871; F:signal transducer activity; TAS:ProtInc.
GO; GO:0007202; P:activation of phospholipase C activity; TAS:Reactome.
GO; GO:0006915; P:apoptotic process; TAS:ProtInc.
GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0071361; P:cellular response to ethanol; IEA:Ensembl.
GO; GO:0071456; P:cellular response to hypoxia; IEA:Ensembl.
GO; GO:0071380; P:cellular response to prostaglandin E stimulus; IEA:Ensembl.
GO; GO:0038096; P:Fc-gamma receptor signaling pathway involved in phagocytosis; TAS:Reactome.
GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
GO; GO:0031663; P:lipopolysaccharide-mediated signaling pathway; ISS:UniProtKB.
GO; GO:0035641; P:locomotory exploration behavior; IEA:Ensembl.
GO; GO:0002281; P:macrophage activation involved in immune response; IEA:Ensembl.
GO; GO:0031397; P:negative regulation of protein ubiquitination; IEA:Ensembl.
GO; GO:2000650; P:negative regulation of sodium ion transmembrane transporter activity; TAS:BHF-UCL.
GO; GO:0018105; P:peptidyl-serine phosphorylation; IDA:UniProtKB.
GO; GO:0030168; P:platelet activation; TAS:Reactome.
GO; GO:0030838; P:positive regulation of actin filament polymerization; ISS:UniProtKB.
GO; GO:0010811; P:positive regulation of cell-substrate adhesion; IEA:Ensembl.
GO; GO:2001031; P:positive regulation of cellular glucuronidation; IMP:BHF-UCL.
GO; GO:0032467; P:positive regulation of cytokinesis; IMP:UniProtKB.
GO; GO:0010634; P:positive regulation of epithelial cell migration; IMP:UniProtKB.
GO; GO:0010763; P:positive regulation of fibroblast migration; ISS:UniProtKB.
GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IEA:Ensembl.
GO; GO:0032024; P:positive regulation of insulin secretion; IEA:Ensembl.
GO; GO:0050996; P:positive regulation of lipid catabolic process; IEA:Ensembl.
GO; GO:0043410; P:positive regulation of MAPK cascade; IEA:Ensembl.
GO; GO:0070257; P:positive regulation of mucus secretion; IEA:Ensembl.
GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; TAS:ParkinsonsUK-UCL.
GO; GO:0032230; P:positive regulation of synaptic transmission, GABAergic; IEA:Ensembl.
GO; GO:0090303; P:positive regulation of wound healing; IMP:UniProtKB.
GO; GO:0006468; P:protein phosphorylation; IDA:BHF-UCL.
GO; GO:0061178; P:regulation of insulin secretion involved in cellular response to glucose stimulus; IEA:Ensembl.
GO; GO:0050730; P:regulation of peptidyl-tyrosine phosphorylation; IEA:Ensembl.
GO; GO:0051279; P:regulation of release of sequestered calcium ion into cytosol; IEA:Ensembl.
GO; GO:0051209; P:release of sequestered calcium ion into cytosol; IEA:Ensembl.
GO; GO:0043278; P:response to morphine; IEA:Ensembl.
GO; GO:0007165; P:signal transduction; TAS:Reactome.
GO; GO:0035669; P:TRAM-dependent toll-like receptor 4 signaling pathway; ISS:UniProtKB.
CDD; cd00029; C1; 2.
CDD; cd05591; STKc_nPKC_epsilon; 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; IPR034669; nPKC_epsilon.
InterPro; IPR002219; PE/DAG-bd.
InterPro; IPR027274; PKC_epsilon.
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; PF00168; C2; 1.
Pfam; PF00069; Pkinase; 1.
Pfam; PF00433; Pkinase_C; 1.
PIRSF; PIRSF000551; PKC_delta; 1.
PIRSF; PIRSF501106; Protein_kin_C_epsilon; 1.
PRINTS; PR00008; DAGPEDOMAIN.
SMART; SM00109; C1; 2.
SMART; SM00239; C2; 1.
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; 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; ATP-binding; Cell adhesion; Cell cycle; Cell division;
Cell membrane; Complete proteome; Cytoplasm; Cytoskeleton; Immunity;
Kinase; Membrane; Metal-binding; Nucleotide-binding; Nucleus;
Phosphoprotein; Polymorphism; Reference proteome; Repeat;
Serine/threonine-protein kinase; Transferase; Zinc; Zinc-finger.
CHAIN 1 737 Protein kinase C epsilon type.
/FTId=PRO_0000055697.
DOMAIN 1 99 C2. {ECO:0000255|PROSITE-
ProRule:PRU00041}.
DOMAIN 408 668 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
DOMAIN 669 737 AGC-kinase C-terminal.
ZN_FING 169 220 Phorbol-ester/DAG-type 1.
{ECO:0000255|PROSITE-ProRule:PRU00226}.
ZN_FING 242 292 Phorbol-ester/DAG-type 2.
{ECO:0000255|PROSITE-ProRule:PRU00226}.
NP_BIND 414 422 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOTIF 223 228 Interaction with actin. {ECO:0000250}.
ACT_SITE 532 532 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 437 437 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 62 62 Phosphoserine.
{ECO:0000250|UniProtKB:P16054}.
MOD_RES 228 228 Phosphothreonine.
{ECO:0000244|PubMed:18691976}.
MOD_RES 234 234 Phosphoserine.
{ECO:0000250|UniProtKB:P16054}.
MOD_RES 309 309 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976}.
MOD_RES 316 316 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 329 329 Phosphoserine.
{ECO:0000244|PubMed:18691976}.
MOD_RES 337 337 Phosphoserine.
{ECO:0000250|UniProtKB:P16054}.
MOD_RES 346 346 Phosphoserine; by GSK3-beta.
{ECO:0000305|PubMed:19662078}.
MOD_RES 349 349 Phosphothreonine.
{ECO:0000250|UniProtKB:P16054}.
MOD_RES 350 350 Phosphoserine; by MAPK11 and MAPK14.
{ECO:0000250|UniProtKB:P16054,
ECO:0000305}.
MOD_RES 368 368 Phosphoserine; by autocatalysis.
{ECO:0000244|PubMed:23186163,
ECO:0000305|PubMed:19662078}.
MOD_RES 388 388 Phosphoserine.
{ECO:0000244|PubMed:18691976}.
MOD_RES 566 566 Phosphothreonine; by PDPK1.
{ECO:0000269|PubMed:11964154}.
MOD_RES 703 703 Phosphothreonine; by autocatalysis.
{ECO:0000255}.
MOD_RES 710 710 Phosphothreonine.
{ECO:0000244|PubMed:18691976}.
MOD_RES 729 729 Phosphoserine; by autocatalysis.
{ECO:0000269|PubMed:11964154}.
VARIANT 143 143 E -> K (in a colorectal cancer sample;
somatic mutation; dbSNP:rs772834505).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_035466.
VARIANT 333 333 A -> V (in dbSNP:rs55989965).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042307.
VARIANT 389 389 P -> R (in dbSNP:rs55767130).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042308.
VARIANT 563 563 T -> M (in dbSNP:rs34077350).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042309.
VARIANT 654 654 A -> T (in dbSNP:rs35777875).
/FTId=VAR_050559.
MUTAGEN 437 437 K->W: Abolishes activity and S-729
phosphorylation.
{ECO:0000269|PubMed:11964154}.
MUTAGEN 566 566 T->A: Abolishes phosphorylation by PDK1,
and S-729 phosphorylation.
{ECO:0000269|PubMed:11964154}.
MUTAGEN 566 566 T->E: No effect on S-729 phosphorylation.
{ECO:0000269|PubMed:11964154}.
MUTAGEN 710 710 T->E: No effect on activity; no effect on
S-729 phosphorylation.
{ECO:0000269|PubMed:11964154}.
MUTAGEN 729 729 S->A: Enhances T-566 dephosphorylation.
{ECO:0000269|PubMed:11964154}.
SEQUENCE 737 AA; 83674 MW; 85032D0A091A1F7F CRC64;
MVVFNGLLKI KICEAVSLKP TAWSLRHAVG PRPQTFLLDP YIALNVDDSR IGQTATKQKT
NSPAWHDEFV TDVCNGRKIE LAVFHDAPIG YDDFVANCTI QFEELLQNGS RHFEDWIDLE
PEGRVYVIID LSGSSGEAPK DNEERVFRER MRPRKRQGAV RRRVHQVNGH KFMATYLRQP
TYCSHCRDFI WGVIGKQGYQ CQVCTCVVHK RCHELIITKC AGLKKQETPD QVGSQRFSVN
MPHKFGIHNY KVPTFCDHCG SLLWGLLRQG LQCKVCKMNV HRRCETNVAP NCGVDARGIA
KVLADLGVTP DKITNSGQRR KKLIAGAESP QPASGSSPSE EDRSKSAPTS PCDQEIKELE
NNIRKALSFD NRGEEHRAAS SPDGQLMSPG ENGEVRQGQA KRLGLDEFNF IKVLGKGSFG
KVMLAELKGK DEVYAVKVLK KDVILQDDDV DCTMTEKRIL ALARKHPYLT QLYCCFQTKD
RLFFVMEYVN GGDLMFQIQR SRKFDEPRSR FYAAEVTSAL MFLHQHGVIY RDLKLDNILL
DAEGHCKLAD FGMCKEGILN GVTTTTFCGT PDYIAPEILQ ELEYGPSVDW WALGVLMYEM
MAGQPPFEAD NEDDLFESIL HDDVLYPVWL SKEAVSILKA FMTKNPHKRL GCVASQNGED
AIKQHPFFKE IDWVLLEQKK IKPPFKPRIK TKRDVNNFDQ DFTREEPVLT LVDEAIVKQI
NQEEFKGFSY FGEDLMP


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