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Q02156

- KPCE_HUMAN

UniProt

Q02156 - KPCE_HUMAN

Protein

Protein kinase C epsilon type

Gene

PRKCE

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 153 (01 Oct 2014)
      Sequence version 1 (01 Jul 1993)
      Previous versions | rss
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    Functioni

    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 AKT1.7 Publications

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.

    Enzyme regulationi

    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.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei437 – 4371ATPPROSITE-ProRule annotation
    Active sitei532 – 5321Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri169 – 22052Phorbol-ester/DAG-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri242 – 29251Phorbol-ester/DAG-type 2PROSITE-ProRule annotationAdd
    BLAST
    Nucleotide bindingi414 – 4229ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. actin monomer binding Source: UniProtKB
    2. ATP binding Source: UniProtKB-KW
    3. calcium-independent protein kinase C activity Source: Ensembl
    4. enzyme activator activity Source: BHF-UCL
    5. enzyme binding Source: UniProtKB
    6. ethanol binding Source: Ensembl
    7. metal ion binding Source: UniProtKB-KW
    8. protein binding Source: IntAct
    9. protein kinase C activity Source: BHF-UCL
    10. receptor activator activity Source: Ensembl
    11. signal transducer activity Source: ProtInc

    GO - Biological processi

    1. activation of phospholipase C activity Source: Reactome
    2. apoptotic process Source: ProtInc
    3. blood coagulation Source: Reactome
    4. cell adhesion Source: UniProtKB-KW
    5. cell cycle Source: UniProtKB-KW
    6. cell division Source: UniProtKB-KW
    7. cellular response to ethanol Source: Ensembl
    8. cellular response to hypoxia Source: Ensembl
    9. epidermal growth factor receptor signaling pathway Source: Reactome
    10. Fc-gamma receptor signaling pathway involved in phagocytosis Source: Reactome
    11. fibroblast growth factor receptor signaling pathway Source: Reactome
    12. innate immune response Source: Reactome
    13. intracellular signal transduction Source: InterPro
    14. lipopolysaccharide-mediated signaling pathway Source: UniProtKB
    15. locomotory exploration behavior Source: Ensembl
    16. macrophage activation involved in immune response Source: Ensembl
    17. neurotrophin TRK receptor signaling pathway Source: Reactome
    18. platelet activation Source: Reactome
    19. positive regulation of actin filament polymerization Source: UniProtKB
    20. positive regulation of cell-substrate adhesion Source: Ensembl
    21. positive regulation of cellular glucuronidation Source: BHF-UCL
    22. positive regulation of cytokinesis Source: UniProtKB
    23. positive regulation of epithelial cell migration Source: UniProtKB
    24. positive regulation of fibroblast migration Source: UniProtKB
    25. positive regulation of I-kappaB kinase/NF-kappaB signaling Source: Ensembl
    26. positive regulation of insulin secretion Source: Ensembl
    27. positive regulation of lipid catabolic process Source: Ensembl
    28. positive regulation of MAPK cascade Source: Ensembl
    29. positive regulation of mucus secretion Source: Ensembl
    30. positive regulation of synaptic transmission, GABAergic Source: Ensembl
    31. positive regulation of wound healing Source: UniProtKB
    32. protein phosphorylation Source: BHF-UCL
    33. regulation of insulin secretion involved in cellular response to glucose stimulus Source: Ensembl
    34. regulation of peptidyl-tyrosine phosphorylation Source: Ensembl
    35. release of sequestered calcium ion into cytosol Source: Ensembl
    36. response to morphine Source: Ensembl
    37. signal transduction Source: Reactome
    38. TRAM-dependent toll-like receptor 4 signaling pathway Source: UniProtKB

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Biological processi

    Cell adhesion, Cell cycle, Cell division, Immunity

    Keywords - Ligandi

    ATP-binding, Metal-binding, Nucleotide-binding, Zinc

    Enzyme and pathway databases

    BRENDAi2.7.11.13. 2681.
    ReactomeiREACT_111064. DAG and IP3 signaling.
    REACT_160158. Role of phospholipids in phagocytosis.
    REACT_19333. G alpha (z) signalling events.
    REACT_2202. Effects of PIP2 hydrolysis.
    SignaLinkiQ02156.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein kinase C epsilon type (EC:2.7.11.13)
    Alternative name(s):
    nPKC-epsilon
    Gene namesi
    Name:PRKCE
    Synonyms:PKCE
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:9401. PRKCE.

    Subcellular locationi

    Cytoplasm 1 Publication. Cytoplasmcytoskeleton 1 Publication. Cell membrane 1 Publication. 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.By similarity

    GO - Cellular componenti

    1. cell periphery Source: UniProtKB
    2. cytoplasm Source: UniProtKB
    3. cytoskeleton Source: UniProtKB-SubCell
    4. cytosol Source: UniProtKB
    5. endoplasmic reticulum Source: BHF-UCL
    6. Golgi apparatus Source: Ensembl
    7. mitochondrion Source: Ensembl
    8. nucleus Source: UniProtKB-SubCell
    9. perinuclear region of cytoplasm Source: UniProtKB
    10. plasma membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Cytoskeleton, Membrane, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi437 – 4371K → W: Abolishes activity and S-729 phosphorylation. 1 Publication
    Mutagenesisi566 – 5661T → A: Abolishes phosphorylation by PDK1, and S-729 phosphorylation. 1 Publication
    Mutagenesisi566 – 5661T → E: No effect on S-729 phosphorylation. 1 Publication
    Mutagenesisi710 – 7101T → E: No effect on activity; no effect on S-729 phosphorylation. 1 Publication
    Mutagenesisi729 – 7291S → A: Enhances T-566 dephosphorylation. 1 Publication

    Organism-specific databases

    PharmGKBiPA33765.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 737737Protein kinase C epsilon typePRO_0000055697Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei228 – 2281Phosphothreonine1 Publication
    Modified residuei234 – 2341PhosphoserineBy similarity
    Modified residuei309 – 3091Phosphothreonine2 Publications
    Modified residuei316 – 3161Phosphoserine1 Publication
    Modified residuei329 – 3291Phosphoserine1 Publication
    Modified residuei346 – 3461Phosphoserine; by GSK3-beta1 Publication
    Modified residuei350 – 3501Phosphoserine; by MAPK11 and MAPK14Curated
    Modified residuei368 – 3681Phosphoserine; by autocatalysis1 Publication
    Modified residuei388 – 3881Phosphoserine1 Publication
    Modified residuei566 – 5661Phosphothreonine; by PDPK11 Publication
    Modified residuei703 – 7031Phosphothreonine; by autocatalysisSequence Analysis
    Modified residuei710 – 7101Phosphothreonine1 Publication
    Modified residuei729 – 7291Phosphoserine; by autocatalysis1 Publication

    Post-translational modificationi

    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.4 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ02156.
    PaxDbiQ02156.
    PRIDEiQ02156.

    PTM databases

    PhosphoSiteiQ02156.

    Miscellaneous databases

    PMAP-CutDBQ02156.

    Expressioni

    Gene expression databases

    ArrayExpressiQ02156.
    BgeeiQ02156.
    CleanExiHS_PRKCE.
    GenevestigatoriQ02156.

    Organism-specific databases

    HPAiCAB001948.

    Interactioni

    Subunit structurei

    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.By similarity2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    HSP90AB1P082382EBI-706254,EBI-352572
    IL32C6GKH12EBI-706254,EBI-9547476
    RPS6KA2Q153492EBI-706254,EBI-1384149
    YWHAZP631045EBI-706254,EBI-347088

    Protein-protein interaction databases

    BioGridi111567. 48 interactions.
    DIPiDIP-34186N.
    IntActiQ02156. 12 interactions.
    MINTiMINT-88515.
    STRINGi9606.ENSP00000306124.

    Structurei

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2WH0X-ray2.25Q/R342-372[»]
    ProteinModelPortaliQ02156.
    SMRiQ02156. Positions 1-136, 168-237, 243-736.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ02156.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 9999C2PROSITE-ProRule annotationAdd
    BLAST
    Domaini408 – 668261Protein kinasePROSITE-ProRule annotationAdd
    BLAST
    Domaini669 – 73769AGC-kinase C-terminalAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi223 – 2286Interaction with actinBy similarity

    Domaini

    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.

    Sequence similaritiesi

    Contains 1 AGC-kinase C-terminal domain.Curated
    Contains 1 C2 domain.PROSITE-ProRule annotation
    Contains 2 phorbol-ester/DAG-type zinc fingers.PROSITE-ProRule annotation
    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri169 – 22052Phorbol-ester/DAG-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri242 – 29251Phorbol-ester/DAG-type 2PROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Repeat, Zinc-finger

    Phylogenomic databases

    eggNOGiCOG0515.
    HOGENOMiHOG000233022.
    HOVERGENiHBG108317.
    InParanoidiQ02156.
    KOiK18050.
    OMAiVANCNIS.
    OrthoDBiEOG77M8QM.
    PhylomeDBiQ02156.
    TreeFamiTF351133.

    Family and domain databases

    Gene3Di2.60.40.150. 1 hit.
    InterProiIPR000961. 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]
    PfamiPF00130. C1_1. 2 hits.
    PF00168. C2. 1 hit.
    PF00069. Pkinase. 1 hit.
    PF00433. Pkinase_C. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000551. PKC_delta. 1 hit.
    PIRSF501106. Protein_kin_C_epsilon. 1 hit.
    PRINTSiPR00008. DAGPEDOMAIN.
    SMARTiSM00109. C1. 2 hits.
    SM00239. C2. 1 hit.
    SM00133. S_TK_X. 1 hit.
    SM00220. S_TKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF49562. SSF49562. 1 hit.
    SSF56112. SSF56112. 1 hit.
    PROSITEiPS51285. 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]

    Sequencei

    Sequence statusi: Complete.

    Q02156-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVVFNGLLKI KICEAVSLKP TAWSLRHAVG PRPQTFLLDP YIALNVDDSR    50
    IGQTATKQKT NSPAWHDEFV TDVCNGRKIE LAVFHDAPIG YDDFVANCTI 100
    QFEELLQNGS RHFEDWIDLE PEGRVYVIID LSGSSGEAPK DNEERVFRER 150
    MRPRKRQGAV RRRVHQVNGH KFMATYLRQP TYCSHCRDFI WGVIGKQGYQ 200
    CQVCTCVVHK RCHELIITKC AGLKKQETPD QVGSQRFSVN MPHKFGIHNY 250
    KVPTFCDHCG SLLWGLLRQG LQCKVCKMNV HRRCETNVAP NCGVDARGIA 300
    KVLADLGVTP DKITNSGQRR KKLIAGAESP QPASGSSPSE EDRSKSAPTS 350
    PCDQEIKELE NNIRKALSFD NRGEEHRAAS SPDGQLMSPG ENGEVRQGQA 400
    KRLGLDEFNF IKVLGKGSFG KVMLAELKGK DEVYAVKVLK KDVILQDDDV 450
    DCTMTEKRIL ALARKHPYLT QLYCCFQTKD RLFFVMEYVN GGDLMFQIQR 500
    SRKFDEPRSR FYAAEVTSAL MFLHQHGVIY RDLKLDNILL DAEGHCKLAD 550
    FGMCKEGILN GVTTTTFCGT PDYIAPEILQ ELEYGPSVDW WALGVLMYEM 600
    MAGQPPFEAD NEDDLFESIL HDDVLYPVWL SKEAVSILKA FMTKNPHKRL 650
    GCVASQNGED AIKQHPFFKE IDWVLLEQKK IKPPFKPRIK TKRDVNNFDQ 700
    DFTREEPVLT LVDEAIVKQI NQEEFKGFSY FGEDLMP 737
    Length:737
    Mass (Da):83,674
    Last modified:July 1, 1993 - v1
    Checksum:i85032D0A091A1F7F
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti143 – 1431E → K in a colorectal cancer sample; somatic mutation. 1 Publication
    VAR_035466
    Natural varianti333 – 3331A → V.1 Publication
    Corresponds to variant rs55989965 [ dbSNP | Ensembl ].
    VAR_042307
    Natural varianti389 – 3891P → R.1 Publication
    Corresponds to variant rs55767130 [ dbSNP | Ensembl ].
    VAR_042308
    Natural varianti563 – 5631T → M.1 Publication
    Corresponds to variant rs34077350 [ dbSNP | Ensembl ].
    VAR_042309
    Natural varianti654 – 6541A → T.
    Corresponds to variant rs35777875 [ dbSNP | Ensembl ].
    VAR_050559

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS1824.1.
    PIRiS28942.
    RefSeqiNP_005391.1. NM_005400.2.
    XP_005264485.1. XM_005264428.1.
    UniGeneiHs.580351.

    Genome annotation databases

    EnsembliENST00000306156; ENSP00000306124; ENSG00000171132.
    GeneIDi5581.
    KEGGihsa:5581.
    UCSCiuc002rut.3. human.

    Polymorphism databases

    DMDMi400135.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS1824.1.
    PIRi S28942.
    RefSeqi NP_005391.1. NM_005400.2.
    XP_005264485.1. XM_005264428.1.
    UniGenei Hs.580351.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2WH0 X-ray 2.25 Q/R 342-372 [» ]
    ProteinModelPortali Q02156.
    SMRi Q02156. Positions 1-136, 168-237, 243-736.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111567. 48 interactions.
    DIPi DIP-34186N.
    IntActi Q02156. 12 interactions.
    MINTi MINT-88515.
    STRINGi 9606.ENSP00000306124.

    Chemistry

    BindingDBi Q02156.
    ChEMBLi CHEMBL2093867.
    GuidetoPHARMACOLOGYi 1486.

    PTM databases

    PhosphoSitei Q02156.

    Polymorphism databases

    DMDMi 400135.

    Proteomic databases

    MaxQBi Q02156.
    PaxDbi Q02156.
    PRIDEi Q02156.

    Protocols and materials databases

    DNASUi 5581.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000306156 ; ENSP00000306124 ; ENSG00000171132 .
    GeneIDi 5581.
    KEGGi hsa:5581.
    UCSCi uc002rut.3. human.

    Organism-specific databases

    CTDi 5581.
    GeneCardsi GC02P045790.
    HGNCi HGNC:9401. PRKCE.
    HPAi CAB001948.
    MIMi 176975. gene.
    neXtProti NX_Q02156.
    PharmGKBi PA33765.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000233022.
    HOVERGENi HBG108317.
    InParanoidi Q02156.
    KOi K18050.
    OMAi VANCNIS.
    OrthoDBi EOG77M8QM.
    PhylomeDBi Q02156.
    TreeFami TF351133.

    Enzyme and pathway databases

    BRENDAi 2.7.11.13. 2681.
    Reactomei REACT_111064. DAG and IP3 signaling.
    REACT_160158. Role of phospholipids in phagocytosis.
    REACT_19333. G alpha (z) signalling events.
    REACT_2202. Effects of PIP2 hydrolysis.
    SignaLinki Q02156.

    Miscellaneous databases

    ChiTaRSi PRKCE. human.
    EvolutionaryTracei Q02156.
    GeneWikii PRKCE.
    GenomeRNAii 5581.
    NextBioi 21644.
    PMAP-CutDB Q02156.
    PROi Q02156.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q02156.
    Bgeei Q02156.
    CleanExi HS_PRKCE.
    Genevestigatori Q02156.

    Family and domain databases

    Gene3Di 2.60.40.150. 1 hit.
    InterProi IPR000961. 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 ]
    Pfami PF00130. C1_1. 2 hits.
    PF00168. C2. 1 hit.
    PF00069. Pkinase. 1 hit.
    PF00433. Pkinase_C. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000551. PKC_delta. 1 hit.
    PIRSF501106. Protein_kin_C_epsilon. 1 hit.
    PRINTSi PR00008. DAGPEDOMAIN.
    SMARTi SM00109. C1. 2 hits.
    SM00239. C2. 1 hit.
    SM00133. S_TK_X. 1 hit.
    SM00220. S_TKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49562. SSF49562. 1 hit.
    SSF56112. SSF56112. 1 hit.
    PROSITEi PS51285. 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 ]
    ProtoNeti Search...

    Publicationsi

    1. 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.
      , 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. 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. 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. 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.
      , 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.

    Entry informationi

    Entry nameiKPCE_HUMAN
    AccessioniPrimary (citable) accession number: Q02156
    Secondary accession number(s): B0LPH7
    , Q32MQ3, Q53SL4, Q53SM5, Q9UE81
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1993
    Last sequence update: July 1, 1993
    Last modified: October 1, 2014
    This is version 153 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 2
      Human chromosome 2: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3