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P16054

- KPCE_MOUSE

UniProt

P16054 - KPCE_MOUSE

Protein

Protein kinase C epsilon type

Gene

Prkce

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 152 (01 Oct 2014)
      Sequence version 1 (01 Apr 1990)
      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. 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). 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. 14-3-3 protein binding Source: UniProtKB
    2. actin monomer binding Source: UniProtKB
    3. ATP binding Source: UniProtKB-KW
    4. calcium-independent protein kinase C activity Source: MGI
    5. enzyme activator activity Source: Ensembl
    6. ethanol binding Source: MGI
    7. metal ion binding Source: UniProtKB-KW
    8. protein binding Source: UniProtKB
    9. protein serine/threonine kinase activity Source: MGI
    10. receptor activator activity Source: MGI

    GO - Biological processi

    1. cell adhesion Source: UniProtKB-KW
    2. cell cycle Source: UniProtKB-KW
    3. cell division Source: UniProtKB-KW
    4. cellular response to ethanol Source: MGI
    5. cellular response to hypoxia Source: MGI
    6. chemosensory behavior Source: MGI
    7. intracellular signal transduction Source: InterPro
    8. lipopolysaccharide-mediated signaling pathway Source: UniProtKB
    9. locomotory exploration behavior Source: MGI
    10. macrophage activation involved in immune response Source: MGI
    11. positive regulation of actin filament polymerization Source: UniProtKB
    12. positive regulation of cell-substrate adhesion Source: MGI
    13. positive regulation of cellular glucuronidation Source: Ensembl
    14. positive regulation of cytokinesis Source: UniProtKB
    15. positive regulation of epithelial cell migration Source: UniProtKB
    16. positive regulation of fibroblast migration Source: UniProtKB
    17. positive regulation of I-kappaB kinase/NF-kappaB signaling Source: MGI
    18. positive regulation of insulin secretion Source: MGI
    19. positive regulation of lipid catabolic process Source: MGI
    20. positive regulation of MAPK cascade Source: MGI
    21. positive regulation of mucus secretion Source: MGI
    22. positive regulation of receptor activity Source: GOC
    23. positive regulation of synaptic transmission, GABAergic Source: MGI
    24. positive regulation of wound healing Source: UniProtKB
    25. protein phosphorylation Source: MGI
    26. regulation of insulin secretion involved in cellular response to glucose stimulus Source: MGI
    27. regulation of lipid metabolic process Source: MGI
    28. regulation of peptidyl-tyrosine phosphorylation Source: MGI
    29. release of sequestered calcium ion into cytosol Source: MGI
    30. response to morphine Source: MGI
    31. 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. 3474.
    ReactomeiREACT_188269. DAG and IP3 signaling.
    REACT_210240. Role of phospholipids in phagocytosis.
    REACT_219232. Effects of PIP2 hydrolysis.

    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, Pkcea
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 17

    Organism-specific databases

    MGIiMGI:97599. Prkce.

    Subcellular locationi

    Cytoplasm By similarity. Cytoplasmcytoskeleton By similarity. Cell membrane By similarity. Cytoplasmperinuclear region 1 Publication. Nucleus 1 Publication
    Note: Translocated to plasma membrane in epithelial cells stimulated by HGF By similarity. Associated with the Golgi at the perinuclear site in pre-passage fibroblasts. In passaging cells, translocated to the cell periphery. Translocated to the nucleus in PMA-treated cells.By similarity

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Cytoskeleton, Membrane, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi346 – 3461S → A: Loss of interaction with YWHAB and defects in the completion of cytokinesis. 1 Publication
    Mutagenesisi368 – 3681S → A: Loss of interaction with YWHAB and defects in the completion of cytokinesis. 1 Publication
    Mutagenesisi729 – 7291S → A, E or T: Loss of localization to the perinuclear region. Loss of translocation to the nucleus upon PMA stimulation. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 737737Protein kinase C epsilon typePRO_0000055698Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei228 – 2281PhosphothreonineBy similarity
    Modified residuei234 – 2341Phosphoserine1 Publication
    Modified residuei309 – 3091PhosphothreonineBy similarity
    Modified residuei316 – 3161Phosphoserine1 Publication
    Modified residuei329 – 3291PhosphoserineBy similarity
    Modified residuei346 – 3461Phosphoserine; by GSK3-beta1 Publication
    Modified residuei350 – 3501Phosphoserine; by MAPK11 and MAPK141 Publication
    Modified residuei368 – 3681Phosphoserine; by autocatalysis2 Publications
    Modified residuei388 – 3881PhosphoserineBy similarity
    Modified residuei566 – 5661Phosphothreonine; by PDPK1By similarity
    Modified residuei703 – 7031Phosphothreonine; by autocatalysisSequence Analysis
    Modified residuei710 – 7101Phosphothreonine; alternate1 Publication
    Modified residuei710 – 7101Phosphothreonine; by autocatalysis; alternateSequence Analysis
    Modified residuei729 – 7291Phosphoserine; by autocatalysis1 Publication

    Post-translational modificationi

    Phosphorylation on Thr-566 by PDPK1 triggers autophosphorylation on Ser-729 By similarity. 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.By similarity4 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP16054.
    PaxDbiP16054.
    PRIDEiP16054.

    PTM databases

    PhosphoSiteiP16054.

    Expressioni

    Gene expression databases

    ArrayExpressiP16054.
    BgeeiP16054.
    CleanExiMM_PRKCE.
    GenevestigatoriP16054.

    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, DGKQ and STAT3 By similarity. Interacts with YWHAB.By similarity2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    YwhabQ9CQV86EBI-298451,EBI-771608

    Protein-protein interaction databases

    BioGridi202198. 7 interactions.
    DIPiDIP-31066N.
    IntActiP16054. 92 interactions.
    MINTiMINT-98243.

    Structurei

    3D structure databases

    ProteinModelPortaliP16054.
    SMRiP16054. Positions 1-136, 168-736.
    ModBaseiSearch...
    MobiDBiSearch...

    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 actin

    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.
    GeneTreeiENSGT00750000117682.
    HOGENOMiHOG000233022.
    HOVERGENiHBG108317.
    InParanoidiP16054.
    KOiK18050.
    OMAiVANCNIS.
    OrthoDBiEOG77M8QM.
    PhylomeDBiP16054.
    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.

    P16054-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVVFNGLLKI KICEAVSLKP TAWSLRHAVG PRPQTFLLDP YIALNVDDSR    50
    IGQTATKQKT NSPAWHDEFV TDVCNGRKIE LAVFHDAPIG YDDFVANCTI 100
    QFEELLQNGS RHFEDWIDLE PEGKVYVIID LSGSSGEAPK DNEERVFRER 150
    MRPRKRQGAV RRRVHQVNGH KFMATYLRQP TYCSHCRDFI WGVIGKQGYQ 200
    CQVCTCVVHK RCHELIITKC AGLKKQETPD EVGSQRFSVN MPHKFGIHNY 250
    KVPTFCDHCG SLLWGLLRQG LQCKVCKMNV HRRCETNVAP NCGVDARGIA 300
    KVLADLGVTP DKITNSGQRR KKLAAGAESP QPASGNSPSE DDRSKSAPTS 350
    PCDQELKELE NNIRKALSFD NRGEEHRASS ATDGQLASPG ENGEVRPGQA 400
    KRLGLDEFNF IKVLGKGSFG KVMLAELKGK DEVYAVKVLK KDVILQDDDV 450
    DCTMTEKRIL ALARKHPYLT QLYCCFQTKD RLFFVMEYVN GGDLMFQIQR 500
    SRKFDEPRSR FYAAEVTSAL MFLHQHGVIY RDLKLDNILL DAEGHCKLAD 550
    FGMCKEGIMN GVTTTTFCGT PDYIAPEILQ ELEYGPSVDW WALGVLMYEM 600
    MAGQPPFEAD NEDDLFESIL HDDVLYPVWL SKEAVSILKA FMTKNPHKRL 650
    GCVAAQNGED AIKQHPFFKE IDWVLLEQKK IKPPFKPRIK TKRDVNNFDQ 700
    DFTREEPILT LVDEAIIKQI NQEEFKGFSY FGEDLMP 737
    Length:737
    Mass (Da):83,561
    Last modified:April 1, 1990 - v1
    Checksum:i7AEBB8CC10C99F57
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF028009 mRNA. Translation: AAB84189.1.
    AF325507 mRNA. Translation: AAG53692.1.
    CCDSiCCDS29008.1.
    PIRiS02270. KIMSCE.
    RefSeqiNP_035234.1. NM_011104.3.
    UniGeneiMm.24614.

    Genome annotation databases

    EnsembliENSMUST00000097274; ENSMUSP00000094873; ENSMUSG00000045038.
    ENSMUST00000097275; ENSMUSP00000094874; ENSMUSG00000045038.
    GeneIDi18754.
    KEGGimmu:18754.
    UCSCiuc008dug.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF028009 mRNA. Translation: AAB84189.1 .
    AF325507 mRNA. Translation: AAG53692.1 .
    CCDSi CCDS29008.1.
    PIRi S02270. KIMSCE.
    RefSeqi NP_035234.1. NM_011104.3.
    UniGenei Mm.24614.

    3D structure databases

    ProteinModelPortali P16054.
    SMRi P16054. Positions 1-136, 168-736.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 202198. 7 interactions.
    DIPi DIP-31066N.
    IntActi P16054. 92 interactions.
    MINTi MINT-98243.

    Chemistry

    BindingDBi P16054.
    ChEMBLi CHEMBL4366.

    PTM databases

    PhosphoSitei P16054.

    Proteomic databases

    MaxQBi P16054.
    PaxDbi P16054.
    PRIDEi P16054.

    Protocols and materials databases

    DNASUi 18754.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000097274 ; ENSMUSP00000094873 ; ENSMUSG00000045038 .
    ENSMUST00000097275 ; ENSMUSP00000094874 ; ENSMUSG00000045038 .
    GeneIDi 18754.
    KEGGi mmu:18754.
    UCSCi uc008dug.2. mouse.

    Organism-specific databases

    CTDi 5581.
    MGIi MGI:97599. Prkce.

    Phylogenomic databases

    eggNOGi COG0515.
    GeneTreei ENSGT00750000117682.
    HOGENOMi HOG000233022.
    HOVERGENi HBG108317.
    InParanoidi P16054.
    KOi K18050.
    OMAi VANCNIS.
    OrthoDBi EOG77M8QM.
    PhylomeDBi P16054.
    TreeFami TF351133.

    Enzyme and pathway databases

    BRENDAi 2.7.11.13. 3474.
    Reactomei REACT_188269. DAG and IP3 signaling.
    REACT_210240. Role of phospholipids in phagocytosis.
    REACT_219232. Effects of PIP2 hydrolysis.

    Miscellaneous databases

    ChiTaRSi PRKCE. mouse.
    NextBioi 294933.
    PROi P16054.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P16054.
    Bgeei P16054.
    CleanExi MM_PRKCE.
    Genevestigatori P16054.

    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. "Unique substrate specificity and regulatory properties of PKC-epsilon: a rationale for diversity."
      Schaap D., Parker P.J., Bristol A., Kriz R., Knopf J.
      FEBS Lett. 243:351-357(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "The catalytic domain of PKC-epsilon, in reciprocal PKC-delta and - epsilon chimeras, is responsible for conferring tumorgenicity to NIH3T3 cells, whereas both regulatory and catalytic domains of PKC-epsilon contribute to in vitro transformation."
      Wang Q.J., Acs P., Goodnight J., Blumberg P.M., Mischak H., Mushinski J.F.
      Oncogene 16:53-60(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Brain.
    3. Wheeler D.L.
      Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Brain.
    4. "Biochemical and morphogenic effects of the interaction between protein kinase C-epsilon and actin in vitro and in cultured NIH3T3 cells."
      Hernandez R.M., Wescott G.G., Mayhew M.W., McJilton M.A., Terrian D.M.
      J. Cell. Biochem. 83:532-546(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH ACTIN, ACTIN-BINDING MOTIF.
    5. "Protein kinase C phosphorylates protein kinase D activation loop Ser744 and Ser748 and releases autoinhibition by the pleckstrin homology domain."
      Waldron R.T., Rozengurt E.
      J. Biol. Chem. 278:154-163(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF PRKD1.
    6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-710, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic brain.
    7. "Protein kinase C epsilon mediates angiotensin II-induced activation of beta1-integrins in cardiac fibroblasts."
      Stawowy P., Margeta C., Blaschke F., Lindschau C., Spencer-Haensch C., Leitges M., Biagini G., Fleck E., Graf K.
      Cardiovasc. Res. 67:50-59(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    8. "PKCepsilon-mediated phosphorylation of vimentin controls integrin recycling and motility."
      Ivaska J., Vuoriluoto K., Huovinen T., Izawa I., Inagaki M., Parker P.J.
      EMBO J. 24:3834-3845(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF VIM.
    9. "Partial replacement of cardiac troponin I with a non-phosphorylatable mutant at serines 43/45 attenuates the contractile dysfunction associated with PKCepsilon phosphorylation."
      Scruggs S.B., Walker L.A., Lyu T., Geenen D.L., Solaro R.J., Buttrick P.M., Goldspink P.H.
      J. Mol. Cell. Cardiol. 40:465-473(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF TNNI3.
    10. "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 IN PHOSPHORYLATION OF TICAM2/TRAM.
    11. "Phosphorylation at Ser729 specifies a Golgi localisation for protein kinase C epsilon (PKCepsilon) in 3T3 fibroblasts."
      Xu T.R., He G., Dobson K., England K., Rumsby M.
      Cell. Signal. 19:1986-1995(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-729, MUTAGENESIS OF SER-729.
    12. "The identification and characterization of novel PKCepsilon phosphorylation sites provide evidence for functional cross-talk within the PKC superfamily."
      Durgan J., Cameron A.J., Saurin A.T., Hanrahan S., Totty N., Messing R.O., Parker P.J.
      Biochem. J. 411:319-331(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-234; SER-316 AND SER-368.
    13. "The regulated assembly of a PKCepsilon complex controls the completion of cytokinesis."
      Saurin A.T., Durgan J., Cameron A.J., Faisal A., Marber M.S., Parker P.J.
      Nat. Cell Biol. 10:891-901(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH YWHAB, PHOSPHORYLATION AT SER-346; SER-350 AND SER-368, MUTAGENESIS OF SER-346 AND SER-368.

    Entry informationi

    Entry nameiKPCE_MOUSE
    AccessioniPrimary (citable) accession number: P16054
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1990
    Last sequence update: April 1, 1990
    Last modified: October 1, 2014
    This is version 152 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3