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Q02156

- KPCE_HUMAN

UniProt

Q02156 - KPCE_HUMAN

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Protein

Protein kinase C epsilon type

Gene
PRKCE, PKCE
Organism
Homo sapiens (Human)
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. 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 – 4371ATP By similarity
Active sitei532 – 5321Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri169 – 22052Phorbol-ester/DAG-type 1Add
BLAST
Zinc fingeri242 – 29251Phorbol-ester/DAG-type 2Add
BLAST
Nucleotide bindingi414 – 4229ATP By similarity

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
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. 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. 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.1 Publication

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
Complete GO annotation...

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 – 2341Phosphoserine By similarity
Modified residuei309 – 3091Phosphothreonine2 Publications
Modified residuei316 – 3161Phosphoserine1 Publication
Modified residuei329 – 3291Phosphoserine1 Publication
Modified residuei346 – 3461Phosphoserine; by GSK3-beta Inferred
Modified residuei350 – 3501Phosphoserine; by MAPK11 and MAPK14 Inferred
Modified residuei368 – 3681Phosphoserine; by autocatalysis Inferred
Modified residuei388 – 3881Phosphoserine1 Publication
Modified residuei566 – 5661Phosphothreonine; by PDPK11 Publication
Modified residuei703 – 7031Phosphothreonine; by autocatalysis Reviewed prediction
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.

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 STAT3.2 Publications

Binary interactionsi

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

Protein-protein interaction databases

BioGridi111567. 48 interactions.
DIPiDIP-34186N.
IntActiQ02156. 9 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.

Miscellaneous databases

EvolutionaryTraceiQ02156.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 9999C2Add
BLAST
Domaini408 – 668261Protein kinaseAdd
BLAST
Domaini669 – 73769AGC-kinase C-terminalAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi223 – 2286Interaction with actin By 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 C2 domain.

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri169 – 22052Phorbol-ester/DAG-type 1Add
BLAST
Zinc fingeri242 – 29251Phorbol-ester/DAG-type 2Add
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. 9 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

« Hide 'large scale' publications
  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: September 3, 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
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

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