Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q02156 (KPCE_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 148. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein kinase C epsilon type

EC=2.7.11.13
Alternative name(s):
nPKC-epsilon
Gene names
Name:PRKCE
Synonyms:PKCE
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length737 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.6 Ref.8 Ref.9 Ref.11 Ref.12 Ref.13 Ref.14

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 structure

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. Ref.10 Ref.12

Subcellular location

Cytoplasm. Cytoplasmcytoskeleton. Cell membrane. Cytoplasmperinuclear region By similarity. Nucleus By similarity. 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. Ref.13

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.

Post-translational modification

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.

Sequence similarities

Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. PKC subfamily.

Contains 1 AGC-kinase C-terminal domain.

Contains 1 C2 domain.

Contains 2 phorbol-ester/DAG-type zinc fingers.

Contains 1 protein kinase domain.

Ontologies

Keywords
   Biological processCell adhesion
Cell cycle
Cell division
Immunity
   Cellular componentCell membrane
Cytoplasm
Cytoskeleton
Membrane
Nucleus
   Coding sequence diversityPolymorphism
   DomainRepeat
Zinc-finger
   LigandATP-binding
Metal-binding
Nucleotide-binding
Zinc
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processFc-gamma receptor signaling pathway involved in phagocytosis

Traceable author statement. Source: Reactome

TRAM-dependent toll-like receptor 4 signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

activation of phospholipase C activity

Traceable author statement. Source: Reactome

apoptotic process

Traceable author statement PubMed 10438519. Source: ProtInc

blood coagulation

Traceable author statement. Source: Reactome

cell adhesion

Inferred from electronic annotation. Source: UniProtKB-KW

cell cycle

Inferred from electronic annotation. Source: UniProtKB-KW

cell division

Inferred from electronic annotation. Source: UniProtKB-KW

cellular response to ethanol

Inferred from electronic annotation. Source: Ensembl

cellular response to hypoxia

Inferred from electronic annotation. Source: Ensembl

epidermal growth factor receptor signaling pathway

Traceable author statement. Source: Reactome

fibroblast growth factor receptor signaling pathway

Traceable author statement. Source: Reactome

innate immune response

Traceable author statement. Source: Reactome

intracellular signal transduction

Inferred from electronic annotation. Source: InterPro

lipopolysaccharide-mediated signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

locomotory exploration behavior

Inferred from electronic annotation. Source: Ensembl

macrophage activation involved in immune response

Inferred from electronic annotation. Source: Ensembl

neurotrophin TRK receptor signaling pathway

Traceable author statement. Source: Reactome

platelet activation

Traceable author statement. Source: Reactome

positive regulation of I-kappaB kinase/NF-kappaB signaling

Inferred from electronic annotation. Source: Ensembl

positive regulation of MAPK cascade

Inferred from electronic annotation. Source: Ensembl

positive regulation of actin filament polymerization

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of cell-substrate adhesion

Inferred from electronic annotation. Source: Ensembl

positive regulation of cellular glucuronidation

Inferred from mutant phenotype PubMed 18556656. Source: BHF-UCL

positive regulation of cytokinesis

Inferred from mutant phenotype PubMed 18604201. Source: UniProtKB

positive regulation of epithelial cell migration

Inferred from mutant phenotype Ref.13. Source: UniProtKB

positive regulation of fibroblast migration

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of insulin secretion

Inferred from electronic annotation. Source: Ensembl

positive regulation of lipid catabolic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of mucus secretion

Inferred from electronic annotation. Source: Ensembl

positive regulation of synaptic transmission, GABAergic

Inferred from electronic annotation. Source: Ensembl

positive regulation of wound healing

Inferred from mutant phenotype Ref.13. Source: UniProtKB

protein phosphorylation

Inferred from direct assay PubMed 18556656. Source: BHF-UCL

regulation of insulin secretion involved in cellular response to glucose stimulus

Inferred from electronic annotation. Source: Ensembl

regulation of peptidyl-tyrosine phosphorylation

Inferred from electronic annotation. Source: Ensembl

release of sequestered calcium ion into cytosol

Inferred from electronic annotation. Source: Ensembl

response to morphine

Inferred from electronic annotation. Source: Ensembl

signal transduction

Traceable author statement. Source: Reactome

   Cellular_componentGolgi apparatus

Inferred from electronic annotation. Source: Ensembl

cell periphery

Inferred from sequence or structural similarity. Source: UniProtKB

cytoplasm

Inferred from direct assay Ref.10. Source: UniProtKB

cytoskeleton

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytosol

Inferred from direct assay Ref.13. Source: UniProtKB

endoplasmic reticulum

Inferred from direct assay PubMed 18556656. Source: BHF-UCL

mitochondrion

Inferred from electronic annotation. Source: Ensembl

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

perinuclear region of cytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

plasma membrane

Inferred from direct assay Ref.10Ref.13. Source: UniProtKB

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

actin monomer binding

Inferred from sequence or structural similarity. Source: UniProtKB

calcium-independent protein kinase C activity

Inferred from electronic annotation. Source: Ensembl

enzyme activator activity

Inferred from mutant phenotype PubMed 18556656. Source: BHF-UCL

enzyme binding

Inferred from physical interaction Ref.10. Source: UniProtKB

ethanol binding

Inferred from electronic annotation. Source: Ensembl

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein kinase C activity

Inferred from direct assay PubMed 18556656. Source: BHF-UCL

receptor activator activity

Inferred from electronic annotation. Source: Ensembl

signal transducer activity

Traceable author statement PubMed 10438519Ref.1. Source: ProtInc

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 737737Protein kinase C epsilon type
PRO_0000055697

Regions

Domain1 – 9999C2
Domain408 – 668261Protein kinase
Domain669 – 73769AGC-kinase C-terminal
Zinc finger169 – 22052Phorbol-ester/DAG-type 1
Zinc finger242 – 29251Phorbol-ester/DAG-type 2
Nucleotide binding414 – 4229ATP By similarity
Motif223 – 2286Interaction with actin By similarity

Sites

Active site5321Proton acceptor By similarity
Binding site4371ATP By similarity

Amino acid modifications

Modified residue2281Phosphothreonine Ref.19
Modified residue2341Phosphoserine By similarity
Modified residue3091Phosphothreonine Ref.19 Ref.20
Modified residue3161Phosphoserine Ref.20
Modified residue3291Phosphoserine Ref.19
Modified residue3461Phosphoserine; by GSK3-beta Probable
Modified residue3501Phosphoserine; by MAPK11 and MAPK14 Probable
Modified residue3681Phosphoserine; by autocatalysis Probable
Modified residue3881Phosphoserine Ref.19
Modified residue5661Phosphothreonine; by PDPK1 Ref.7
Modified residue7031Phosphothreonine; by autocatalysis Potential
Modified residue7101Phosphothreonine Ref.19
Modified residue7291Phosphoserine; by autocatalysis Ref.7

Natural variations

Natural variant1431E → K in a colorectal cancer sample; somatic mutation. Ref.25
VAR_035466
Natural variant3331A → V. Ref.26
Corresponds to variant rs55989965 [ dbSNP | Ensembl ].
VAR_042307
Natural variant3891P → R. Ref.26
Corresponds to variant rs55767130 [ dbSNP | Ensembl ].
VAR_042308
Natural variant5631T → M. Ref.26
Corresponds to variant rs34077350 [ dbSNP | Ensembl ].
VAR_042309
Natural variant6541A → T.
Corresponds to variant rs35777875 [ dbSNP | Ensembl ].
VAR_050559

Experimental info

Mutagenesis4371K → W: Abolishes activity and S-729 phosphorylation. Ref.7
Mutagenesis5661T → A: Abolishes phosphorylation by PDK1, and S-729 phosphorylation. Ref.7
Mutagenesis5661T → E: No effect on S-729 phosphorylation. Ref.7
Mutagenesis7101T → E: No effect on activity; no effect on S-729 phosphorylation. Ref.7
Mutagenesis7291S → A: Enhances T-566 dephosphorylation. Ref.7

Sequences

Sequence LengthMass (Da)Tools
Q02156 [UniParc].

Last modified July 1, 1993. Version 1.
Checksum: 85032D0A091A1F7F

FASTA73783,674
        10         20         30         40         50         60 
MVVFNGLLKI KICEAVSLKP TAWSLRHAVG PRPQTFLLDP YIALNVDDSR IGQTATKQKT 

        70         80         90        100        110        120 
NSPAWHDEFV TDVCNGRKIE LAVFHDAPIG YDDFVANCTI QFEELLQNGS RHFEDWIDLE 

       130        140        150        160        170        180 
PEGRVYVIID LSGSSGEAPK DNEERVFRER MRPRKRQGAV RRRVHQVNGH KFMATYLRQP 

       190        200        210        220        230        240 
TYCSHCRDFI WGVIGKQGYQ CQVCTCVVHK RCHELIITKC AGLKKQETPD QVGSQRFSVN 

       250        260        270        280        290        300 
MPHKFGIHNY KVPTFCDHCG SLLWGLLRQG LQCKVCKMNV HRRCETNVAP NCGVDARGIA 

       310        320        330        340        350        360 
KVLADLGVTP DKITNSGQRR KKLIAGAESP QPASGSSPSE EDRSKSAPTS PCDQEIKELE 

       370        380        390        400        410        420 
NNIRKALSFD NRGEEHRAAS SPDGQLMSPG ENGEVRQGQA KRLGLDEFNF IKVLGKGSFG 

       430        440        450        460        470        480 
KVMLAELKGK DEVYAVKVLK KDVILQDDDV DCTMTEKRIL ALARKHPYLT QLYCCFQTKD 

       490        500        510        520        530        540 
RLFFVMEYVN GGDLMFQIQR SRKFDEPRSR FYAAEVTSAL MFLHQHGVIY RDLKLDNILL 

       550        560        570        580        590        600 
DAEGHCKLAD FGMCKEGILN GVTTTTFCGT PDYIAPEILQ ELEYGPSVDW WALGVLMYEM 

       610        620        630        640        650        660 
MAGQPPFEAD NEDDLFESIL HDDVLYPVWL SKEAVSILKA FMTKNPHKRL GCVASQNGED 

       670        680        690        700        710        720 
AIKQHPFFKE IDWVLLEQKK IKPPFKPRIK TKRDVNNFDQ DFTREEPVLT LVDEAIVKQI 

       730 
NQEEFKGFSY FGEDLMP 

« Hide

References

« Hide 'large scale' references
[1]"Sequence and expression of human protein kinase C-epsilon."
Basta P., Strickland M.B., Holmes W., Loomis C.R., Ballas L.M., Burns D.J.
Biochim. Biophys. Acta 1132:154-160(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]SeattleSNPs variation discovery resource
Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
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. expand/collapse author list , 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.
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]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. expand/collapse author list , 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
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[6]"PKC epsilon-related kinase associates with and phosphorylates cytokeratin 8 and 18."
Omary M.B., Baxter G.T., Chou C.F., Riopel C.L., Lin W.Y., Strulovici B.
J. Cell Biol. 117:583-593(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PHOSPHORYLATION OF KRT8.
[7]"Regulation of novel protein kinase C epsilon by phosphorylation."
Cenni V., Doeppler H., Sonnenburg E.D., Maraldi N., Newton A.C., Toker A.
Biochem. J. 363:537-545(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT THR-566 AND SER-729, MUTAGENESIS OF LYS-437; THR-566; THR-710 AND SER-729.
[8]"Direct phosphorylation of capsaicin receptor VR1 by protein kinase Cepsilon and identification of two target serine residues."
Numazaki M., Tominaga T., Toyooka H., Tominaga M.
J. Biol. Chem. 277:13375-13378(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PHOSPHORYLATION OF TRPV1.
[9]"Phosphorylation of IQGAP1 modulates its binding to Cdc42, revealing a new type of rho-GTPase regulator."
Grohmanova K., Schlaepfer D., Hess D., Gutierrez P., Beck M., Kroschewski R.
J. Biol. Chem. 279:48495-48504(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PHOSPHORYLATION OF IQGAP1.
[10]"Translocation of diacylglycerol kinase theta from cytosol to plasma membrane in response to activation of G protein-coupled receptors and protein kinase C."
van Baal J., de Widt J., Divecha N., van Blitterswijk W.J.
J. Biol. Chem. 280:9870-9878(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DGKQ.
[11]"Trif-related adapter molecule is phosphorylated by PKCepsilon during Toll-like receptor 4 signaling."
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.
Proc. Natl. Acad. Sci. U.S.A. 103:9196-9201(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[12]"Protein kinase Cepsilon interacts with signal transducers and activators of transcription 3 (Stat3), phosphorylates Stat3Ser727, and regulates its constitutive activation in prostate cancer."
Aziz M.H., Manoharan H.T., Church D.R., Dreckschmidt N.E., Zhong W., Oberley T.D., Wilding G., Verma A.K.
Cancer Res. 67:8828-8838(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PHOSPHORYLATION OF STAT3, INTERACTION WITH STAT3.
[13]"Protein kinase C alpha and epsilon differentially modulate hepatocyte growth factor-induced epithelial proliferation and migration."
Sharma G.D., Kakazu A., Bazan H.E.
Exp. Eye Res. 85:289-297(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN CELL MOTILITY, SUBCELLULAR LOCATION.
[14]"Protein kinase C epsilon regulates gamma-aminobutyrate type A receptor sensitivity to ethanol and benzodiazepines through phosphorylation of gamma2 subunits."
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.
J. Biol. Chem. 282:33052-33063(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PHOSPHORYLATION OF GABRG2.
[15]"Protein kinase C-epsilon (PKC-epsilon): its unique structure and function."
Akita Y.
J. Biochem. 132:847-852(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON FUNCTION.
[16]"TNF-related apoptosis-inducing ligand (TRAIL) and erythropoiesis: a role for PKC epsilon."
Vitale M., Gobbi G., Mirandola P., Ponti C., Sponzilli I., Rinaldi L., Manzoli F.A.
Eur. J. Histochem. 50:15-18(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON FUNCTION IN APOPTOSIS.
[17]"Protein kinase Cepsilon: function in neurons."
Shirai Y., Adachi N., Saito N.
FEBS J. 275:3988-3994(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON FUNCTION IN NEURONS.
[18]"Protein kinase Cepsilon: multiple roles in the function of, and signaling mediated by, the cytoskeleton."
Akita Y.
FEBS J. 275:3995-4004(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON FUNCTION IN CYTOSKELETON.
[19]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-228; THR-309; SER-329; SER-388 AND THR-710, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[20]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-309 AND SER-316, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[21]"The substrates and binding partners of protein kinase Cepsilon."
Newton P.M., Messing R.O.
Biochem. J. 427:189-196(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[22]"The role of protein kinase C epsilon in neural signal transduction and neurogenic diseases."
Chen Y., Tian Q.
Front. Med. 5:70-76(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON FUNCTION IN NEURONS.
[23]"PKC-delta and PKC-epsilon: Foes of the same family or strangers?"
Duquesnes N., Lezoualc'h F., Crozatier B.
J. Mol. Cell. Cardiol. 51:665-673(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[24]"Recognition of an intra-chain tandem 14-3-3 binding site within PKCepsilon."
Kostelecky B., Saurin A.T., Purkiss A., Parker P.J., McDonald N.Q.
EMBO Rep. 10:983-989(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 342-372, PHOSPHORYLATION AT SER-346 AND SER-368.
[25]"The consensus coding sequences of human breast and colorectal cancers."
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. expand/collapse author list , 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.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] LYS-143.
[26]"Patterns of somatic mutation in human cancer genomes."
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. expand/collapse author list , 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.
Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] VAL-333; ARG-389 AND MET-563.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X65293 mRNA. Translation: CAA46388.1.
EU332867 Genomic DNA. Translation: ABY87556.1.
U51244 Genomic DNA. Translation: AAD08855.1.
AC017078 Genomic DNA. Translation: AAY14773.1.
AC017006 Genomic DNA. Translation: AAX93253.1.
CH471053 Genomic DNA. Translation: EAX00258.1.
BC109033 mRNA. Translation: AAI09034.1.
BC109034 mRNA. Translation: AAI09035.1.
PIRS28942.
RefSeqNP_005391.1. NM_005400.2.
XP_005264485.1. XM_005264428.1.
UniGeneHs.580351.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2WH0X-ray2.25Q/R342-372[»]
ProteinModelPortalQ02156.
SMRQ02156. Positions 1-136, 168-237, 243-736.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111567. 48 interactions.
DIPDIP-34186N.
IntActQ02156. 9 interactions.
MINTMINT-88515.
STRING9606.ENSP00000306124.

Chemistry

BindingDBQ02156.
ChEMBLCHEMBL2093867.
GuidetoPHARMACOLOGY1486.

PTM databases

PhosphoSiteQ02156.

Polymorphism databases

DMDM400135.

Proteomic databases

PaxDbQ02156.
PRIDEQ02156.

Protocols and materials databases

DNASU5581.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000306156; ENSP00000306124; ENSG00000171132.
GeneID5581.
KEGGhsa:5581.
UCSCuc002rut.3. human.

Organism-specific databases

CTD5581.
GeneCardsGC02P045790.
HGNCHGNC:9401. PRKCE.
HPACAB001948.
MIM176975. gene.
neXtProtNX_Q02156.
PharmGKBPA33765.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000233022.
HOVERGENHBG108317.
InParanoidQ02156.
KOK18050.
OMAVANCNIS.
OrthoDBEOG77M8QM.
PhylomeDBQ02156.
TreeFamTF351133.

Enzyme and pathway databases

BRENDA2.7.11.13. 2681.
ReactomeREACT_111102. Signal Transduction.
REACT_116125. Disease.
REACT_604. Hemostasis.
REACT_6900. Immune System.
SignaLinkQ02156.

Gene expression databases

ArrayExpressQ02156.
BgeeQ02156.
CleanExHS_PRKCE.
GenevestigatorQ02156.

Family and domain databases

Gene3D2.60.40.150. 1 hit.
InterProIPR000961. AGC-kinase_C.
IPR000008. C2_dom.
IPR020454. DAG/PE-bd.
IPR011009. Kinase-like_dom.
IPR027274. PKC_epsilon.
IPR017892. Pkinase_C.
IPR014376. Prot_kin_PKC_delta.
IPR002219. Prot_Kinase_C-like_PE/DAG-bd.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamPF00130. C1_1. 2 hits.
PF00168. C2. 1 hit.
PF00069. Pkinase. 1 hit.
PF00433. Pkinase_C. 1 hit.
[Graphical view]
PIRSFPIRSF000551. PKC_delta. 1 hit.
PIRSF501106. Protein_kin_C_epsilon. 1 hit.
PRINTSPR00008. DAGPEDOMAIN.
SMARTSM00109. C1. 2 hits.
SM00239. C2. 1 hit.
SM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF49562. SSF49562. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEPS51285. AGC_KINASE_CTER. 1 hit.
PS50004. C2. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
PS00479. ZF_DAG_PE_1. 2 hits.
PS50081. ZF_DAG_PE_2. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPRKCE. human.
EvolutionaryTraceQ02156.
GeneWikiPRKCE.
GenomeRNAi5581.
NextBio21644.
PMAP-CutDBQ02156.
PROQ02156.
SOURCESearch...

Entry information

Entry nameKPCE_HUMAN
AccessionPrimary (citable) accession number: Q02156
Secondary accession number(s): B0LPH7 expand/collapse secondary AC list , Q32MQ3, Q53SL4, Q53SM5, Q9UE81
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: April 16, 2014
This is version 148 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM