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P16054

- KPCE_MOUSE

UniProt

P16054 - KPCE_MOUSE

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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

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 serine/threonine kinase activity Source: MGI
  9. 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
Complete GO annotation...

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.
REACT_258013. G alpha (z) signalling events.

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-KW
  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-KW
Complete GO annotation...

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

BgeeiP16054.
CleanExiMM_PRKCE.
ExpressionAtlasiP16054. baseline and differential.
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.
GeneTreeiENSGT00770000120449.
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.
IPR002219. PE/DAG-bd.
IPR027274. PKC_epsilon.
IPR017892. Pkinase_C.
IPR014376. Prot_kin_PKC_delta.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
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

        10         20         30         40         50
MVVFNGLLKI KICEAVSLKP TAWSLRHAVG PRPQTFLLDP YIALNVDDSR
60 70 80 90 100
IGQTATKQKT NSPAWHDEFV TDVCNGRKIE LAVFHDAPIG YDDFVANCTI
110 120 130 140 150
QFEELLQNGS RHFEDWIDLE PEGKVYVIID LSGSSGEAPK DNEERVFRER
160 170 180 190 200
MRPRKRQGAV RRRVHQVNGH KFMATYLRQP TYCSHCRDFI WGVIGKQGYQ
210 220 230 240 250
CQVCTCVVHK RCHELIITKC AGLKKQETPD EVGSQRFSVN MPHKFGIHNY
260 270 280 290 300
KVPTFCDHCG SLLWGLLRQG LQCKVCKMNV HRRCETNVAP NCGVDARGIA
310 320 330 340 350
KVLADLGVTP DKITNSGQRR KKLAAGAESP QPASGNSPSE DDRSKSAPTS
360 370 380 390 400
PCDQELKELE NNIRKALSFD NRGEEHRASS ATDGQLASPG ENGEVRPGQA
410 420 430 440 450
KRLGLDEFNF IKVLGKGSFG KVMLAELKGK DEVYAVKVLK KDVILQDDDV
460 470 480 490 500
DCTMTEKRIL ALARKHPYLT QLYCCFQTKD RLFFVMEYVN GGDLMFQIQR
510 520 530 540 550
SRKFDEPRSR FYAAEVTSAL MFLHQHGVIY RDLKLDNILL DAEGHCKLAD
560 570 580 590 600
FGMCKEGIMN GVTTTTFCGT PDYIAPEILQ ELEYGPSVDW WALGVLMYEM
610 620 630 640 650
MAGQPPFEAD NEDDLFESIL HDDVLYPVWL SKEAVSILKA FMTKNPHKRL
660 670 680 690 700
GCVAAQNGED AIKQHPFFKE IDWVLLEQKK IKPPFKPRIK TKRDVNNFDQ
710 720 730
DFTREEPILT LVDEAIIKQI NQEEFKGFSY FGEDLMP
Length:737
Mass (Da):83,561
Last modified:April 1, 1990 - v1
Checksum:i7AEBB8CC10C99F57
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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 ENSGT00770000120449.
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.
REACT_258013. G alpha (z) signalling events.

Miscellaneous databases

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

Gene expression databases

Bgeei P16054.
CleanExi MM_PRKCE.
ExpressionAtlasi P16054. baseline and differential.
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.
IPR002219. PE/DAG-bd.
IPR027274. PKC_epsilon.
IPR017892. Pkinase_C.
IPR014376. Prot_kin_PKC_delta.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 154 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

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