Prkce | ENSMUSG00000045038 | NCBI 18754

Details for: Prkce

Gene ID: 18754

Symbol: Prkce

Ensembl ID: ENSMUSG00000045038

Description: protein kinase C, epsilon

Associated with

Dag and ip3 signaling
(R-MMU-1489509)
Effects of pip2 hydrolysis
(R-MMU-114508)
Fcgamma receptor (fcgr) dependent phagocytosis
(R-MMU-2029480)
G alpha (q) signalling events
(R-MMU-416476)
Gpcr downstream signalling
(R-MMU-388396)
Hemostasis
(R-MMU-109582)
Immune system
(R-MMU-168256)
Innate immune system
(R-MMU-168249)
Intracellular signaling by second messengers
(R-MMU-9006925)
Platelet activation, signaling and aggregation
(R-MMU-76002)
Role of phospholipids in phagocytosis
(R-MMU-2029485)
Shc1 events in erbb2 signaling
(R-MMU-1250196)
Signaling by erbb2
(R-MMU-1227986)
Signaling by gpcr
(R-MMU-372790)
Signaling by receptor tyrosine kinases
(R-MMU-9006934)
Signal transduction
(R-MMU-162582)
14-3-3 protein binding
(GO:0071889)
Actin monomer binding
(GO:0003785)
Atp binding
(GO:0005524)
Cell-substrate adhesion
(GO:0031589)
Cell adhesion
(GO:0007155)
Cell cycle
(GO:0007049)
Cell division
(GO:0051301)
Cellular response to ethanol
(GO:0071361)
Cellular response to hypoxia
(GO:0071456)
Cellular response to platelet-derived growth factor stimulus
(GO:0036120)
Cellular response to prostaglandin e stimulus
(GO:0071380)
Chemosensory behavior
(GO:0007635)
Cytoplasm
(GO:0005737)
Cytoskeleton
(GO:0005856)
Cytosol
(GO:0005829)
Diacylglycerol-dependent, calcium-independent serine/threonine kinase activity
(GO:0004699)
Diacylglycerol-dependent serine/threonine kinase activity
(GO:0004697)
Endoplasmic reticulum
(GO:0005783)
Enzyme activator activity
(GO:0008047)
Enzyme binding
(GO:0019899)
Establishment of localization in cell
(GO:0051649)
Ethanol binding
(GO:0035276)
Golgi apparatus
(GO:0005794)
Golgi membrane
(GO:0000139)
Immune system process
(GO:0002376)
Insulin secretion
(GO:0030073)
Intracellular signal transduction
(GO:0035556)
Kinase activity
(GO:0016301)
Lipopolysaccharide-mediated signaling pathway
(GO:0031663)
Locomotory exploration behavior
(GO:0035641)
Macrophage activation involved in immune response
(GO:0002281)
Mapk cascade
(GO:0000165)
Membrane
(GO:0016020)
Metal ion binding
(GO:0046872)
Mitochondrion
(GO:0005739)
Mucus secretion
(GO:0070254)
Negative regulation of apoptotic process
(GO:0043066)
Negative regulation of mitochondrial calcium ion concentration
(GO:0051562)
Negative regulation of mitochondrial membrane potential
(GO:0010917)
Negative regulation of protein ubiquitination
(GO:0031397)
Negative regulation of release of sequestered calcium ion into cytosol
(GO:0051280)
Nucleotide binding
(GO:0000166)
Nucleus
(GO:0005634)
Peptidyl-serine phosphorylation
(GO:0018105)
Phosphorylation
(GO:0016310)
Plasma membrane
(GO:0005886)
Positive regulation of actin filament polymerization
(GO:0030838)
Positive regulation of canonical nf-kappab signal transduction
(GO:0043123)
Positive regulation of cell-substrate adhesion
(GO:0010811)
Positive regulation of cellular glucuronidation
(GO:2001031)
Positive regulation of cytokinesis
(GO:0032467)
Positive regulation of epithelial cell migration
(GO:0010634)
Positive regulation of fibroblast migration
(GO:0010763)
Positive regulation of insulin secretion
(GO:0032024)
Positive regulation of lipid catabolic process
(GO:0050996)
Positive regulation of mapk cascade
(GO:0043410)
Positive regulation of mucus secretion
(GO:0070257)
Positive regulation of synaptic transmission, gabaergic
(GO:0032230)
Positive regulation of wound healing
(GO:0090303)
Presynaptic modulation of chemical synaptic transmission
(GO:0099171)
Protein binding
(GO:0005515)
Protein kinase activity
(GO:0004672)
Protein kinase binding
(GO:0019901)
Protein phosphorylation
(GO:0006468)
Protein serine/threonine kinase activity
(GO:0004674)
Protein serine/threonine kinase binding
(GO:0120283)
Regulation of insulin secretion involved in cellular response to glucose stimulus
(GO:0061178)
Regulation of lipid metabolic process
(GO:0019216)
Regulation of peptidyl-tyrosine phosphorylation
(GO:0050730)
Regulation of release of sequestered calcium ion into cytosol
(GO:0051279)
Response to morphine
(GO:0043278)
Sh3 domain binding
(GO:0017124)
Signaling receptor activator activity
(GO:0030546)
Signaling receptor binding
(GO:0005102)
Synaptic transmission, gabaergic
(GO:0051932)
Tram-dependent toll-like receptor 4 signaling pathway
(GO:0035669)
Transferase activity
(GO:0016740)

Other Information

Proteins

Protein kinase C epsilon type

Genular Protein ID: 2605614967

Symbol: KPCE_MOUSE

Name: Protein kinase C epsilon type

UniProtKB Accession Codes:

P16054

Database IDs:

Citations:

PubMed ID: 2917656

Title: Unique substrate specificity and regulatory properties of PKC-epsilon: a rationale for diversity.

PubMed ID: 2917656

DOI: 10.1016/0014-5793(89)80160-7

PubMed ID: 9467942

Title: 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.

PubMed ID: 9467942

DOI: 10.1038/sj.onc.1201507

PubMed ID: 11746497

Title: Biochemical and morphogenic effects of the interaction between protein kinase C-epsilon and actin in vitro and in cultured NIH3T3 cells.

PubMed ID: 11746497

DOI: 10.1002/jcb.1246

PubMed ID: 12407104

Title: Protein kinase C phosphorylates protein kinase D activation loop Ser744 and Ser748 and releases autoinhibition by the pleckstrin homology domain.

PubMed ID: 12407104

DOI: 10.1074/jbc.m208075200

PubMed ID: 15345747

Title: Phosphoproteomic analysis of the developing mouse brain.

PubMed ID: 15345747

DOI: 10.1074/mcp.m400085-mcp200

PubMed ID: 15949469

Title: Protein kinase C epsilon mediates angiotensin II-induced activation of beta1-integrins in cardiac fibroblasts.

PubMed ID: 15949469

DOI: 10.1016/j.cardiores.2005.03.002

PubMed ID: 16270034

Title: PKCepsilon-mediated phosphorylation of vimentin controls integrin recycling and motility.

PubMed ID: 16270034

DOI: 10.1038/sj.emboj.7600847

PubMed ID: 16445938

Title: Partial replacement of cardiac troponin I with a non-phosphorylatable mutant at serines 43/45 attenuates the contractile dysfunction associated with PKCepsilon phosphorylation.

PubMed ID: 16445938

DOI: 10.1016/j.yjmcc.2005.12.009

PubMed ID: 16757566

Title: Trif-related adapter molecule is phosphorylated by PKCepsilon during Toll-like receptor 4 signaling.

PubMed ID: 16757566

DOI: 10.1073/pnas.0600462103

PubMed ID: 17611075

Title: Phosphorylation at Ser729 specifies a Golgi localisation for protein kinase C epsilon (PKCepsilon) in 3T3 fibroblasts.

PubMed ID: 17611075

DOI: 10.1016/j.cellsig.2007.05.009

PubMed ID: 18237277

Title: The identification and characterization of novel PKCepsilon phosphorylation sites provide evidence for functional cross-talk within the PKC superfamily.

PubMed ID: 18237277

DOI: 10.1042/bj20071348

PubMed ID: 18604201

Title: The regulated assembly of a PKCepsilon complex controls the completion of cytokinesis.

PubMed ID: 18604201

DOI: 10.1038/ncb1749

PubMed ID: 21183079

Title: A tissue-specific atlas of mouse protein phosphorylation and expression.

PubMed ID: 21183079

DOI: 10.1016/j.cell.2010.12.001

Sequence Information:

Length: 737
Mass: 83561
Checksum: 7AEBB8CC10C99F57
Sequence:

MVVFNGLLKI KICEAVSLKP TAWSLRHAVG PRPQTFLLDP YIALNVDDSR IGQTATKQKT 
NSPAWHDEFV TDVCNGRKIE LAVFHDAPIG YDDFVANCTI QFEELLQNGS RHFEDWIDLE 
PEGKVYVIID LSGSSGEAPK DNEERVFRER MRPRKRQGAV RRRVHQVNGH KFMATYLRQP 
TYCSHCRDFI WGVIGKQGYQ CQVCTCVVHK RCHELIITKC AGLKKQETPD EVGSQRFSVN 
MPHKFGIHNY KVPTFCDHCG SLLWGLLRQG LQCKVCKMNV HRRCETNVAP NCGVDARGIA 
KVLADLGVTP DKITNSGQRR KKLAAGAESP QPASGNSPSE DDRSKSAPTS PCDQELKELE 
NNIRKALSFD NRGEEHRASS ATDGQLASPG ENGEVRPGQA KRLGLDEFNF IKVLGKGSFG 
KVMLAELKGK DEVYAVKVLK KDVILQDDDV DCTMTEKRIL ALARKHPYLT QLYCCFQTKD 
RLFFVMEYVN GGDLMFQIQR SRKFDEPRSR FYAAEVTSAL MFLHQHGVIY RDLKLDNILL 
DAEGHCKLAD FGMCKEGIMN GVTTTTFCGT PDYIAPEILQ ELEYGPSVDW WALGVLMYEM 
MAGQPPFEAD NEDDLFESIL HDDVLYPVWL SKEAVSILKA FMTKNPHKRL GCVAAQNGED 
AIKQHPFFKE IDWVLLEQKK IKPPFKPRIK TKRDVNNFDQ DFTREEPILT LVDEAIIKQI 
NQEEFKGFSY FGEDLMP

The gene details are incomplete or unavailable at the moment.

Database document:

This is a preview of the gene's schema. Only a few entries are kept for 'singleCellExpressions,' 'mRNAExpressions,' and other large data arrays for visualization purposes. You can zoom in with the mouse wheel for a closer view, and the text will adjust automatically if necessary. For the full schema, download it here.

Details for: Prkce

Associated with

Other Information

Unique substrate specificity and regulatory properties of PKC-epsilon: a rationale for diversity. PubMed ID: 2917656

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. PubMed ID: 9467942

Biochemical and morphogenic effects of the interaction between protein kinase C-epsilon and actin in vitro and in cultured NIH3T3 cells. PubMed ID: 11746497

Protein kinase C phosphorylates protein kinase D activation loop Ser744 and Ser748 and releases autoinhibition by the pleckstrin homology domain. PubMed ID: 12407104

Phosphoproteomic analysis of the developing mouse brain. PubMed ID: 15345747

Protein kinase C epsilon mediates angiotensin II-induced activation of beta1-integrins in cardiac fibroblasts. PubMed ID: 15949469

PKCepsilon-mediated phosphorylation of vimentin controls integrin recycling and motility. PubMed ID: 16270034

Partial replacement of cardiac troponin I with a non-phosphorylatable mutant at serines 43/45 attenuates the contractile dysfunction associated with PKCepsilon phosphorylation. PubMed ID: 16445938

Trif-related adapter molecule is phosphorylated by PKCepsilon during Toll-like receptor 4 signaling. PubMed ID: 16757566

Phosphorylation at Ser729 specifies a Golgi localisation for protein kinase C epsilon (PKCepsilon) in 3T3 fibroblasts. PubMed ID: 17611075

The identification and characterization of novel PKCepsilon phosphorylation sites provide evidence for functional cross-talk within the PKC superfamily. PubMed ID: 18237277

The regulated assembly of a PKCepsilon complex controls the completion of cytokinesis. PubMed ID: 18604201

A tissue-specific atlas of mouse protein phosphorylation and expression. PubMed ID: 21183079