Basic Information
Gene Structure
Domain
Regulation&
Interaction
Annotation
Orthologus Group
Expresssion
Pathway
Basic Information
Gene ID
CSS0039550.g
View in Genome Browser
Position
Chr5:132155557-132265494 (+)
109937bp
Gene Type
gene
Gene Description (Protein Product)
Serine threonine-protein kinase
Organism
Camellia sinensis
Also AS AT3G59410

Gene Structure

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Domain
Database EntryID E-Value Start end InterPro ID Description

Regulation&Interaction
Protein-protein interaction (PPI)
CSS0045626.g Nucleoside diphosphate kinase
CSS0048991.g Eukaryotic translation initiation factor 2 subunit
CSS0049914.g
Regulatory gene
CSS0000128.g tesmin tso1-like cxc
CSS0004360.g Dof zinc finger protein
CSS0004951.g dof zinc finger protein

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Annotation

Orthologous Group
Orthologous ID Species Number All hits in PereRegDB Hits of this species Orthologous Detail

Expression Profile
DataSet Number of Samples expressed(TPM>1) Mean Min Max Standard deviation(SD) Coeffcient variation(CV)


Pathway
Go Pathway KEGG Pathway
GO Term Description GO Category
GO:0000302 response to reactive oxygen species BP
GO:0006950 response to stress BP
GO:0006979 response to oxidative stress BP
GO:0007154 cell communication BP
GO:0008150 biological_process BP
GO:0009267 cellular response to starvation BP
GO:0009268 response to pH BP
GO:0009605 response to external stimulus BP
GO:0009628 response to abiotic stimulus BP
GO:0009636 response to toxic substance BP
GO:0009719 response to endogenous stimulus BP
GO:0009987 cellular process BP
GO:0009991 response to extracellular stimulus BP
GO:0010033 response to organic substance BP
GO:0010035 response to inorganic substance BP
GO:0010243 response to organonitrogen compound BP
GO:0010447 response to acidic pH BP
GO:0014070 response to organic cyclic compound BP
GO:0031667 response to nutrient levels BP
GO:0031668 cellular response to extracellular stimulus BP
GO:0031669 cellular response to nutrient levels BP
GO:0033554 cellular response to stress BP
GO:0034198 cellular response to amino acid starvation BP
GO:0034599 cellular response to oxidative stress BP
GO:0034614 cellular response to reactive oxygen species BP
GO:0035690 cellular response to xenobiotic stimulus BP
GO:0042221 response to chemical BP
GO:0042493 response to xenobiotic stimulus BP
GO:0042542 response to hydrogen peroxide BP
GO:0042594 response to starvation BP
GO:0046677 response to antibiotic BP
GO:0050896 response to stimulus BP
GO:0051716 cellular response to stimulus BP
GO:0060992 response to fungicide BP
GO:0070301 cellular response to hydrogen peroxide BP
GO:0070887 cellular response to chemical stimulus BP
GO:0071214 cellular response to abiotic stimulus BP
GO:0071236 cellular response to antibiotic BP
GO:0071310 cellular response to organic substance BP
GO:0071407 cellular response to organic cyclic compound BP
GO:0071417 cellular response to organonitrogen compound BP
GO:0071467 cellular response to pH BP
GO:0071468 cellular response to acidic pH BP
GO:0071495 cellular response to endogenous stimulus BP
GO:0071496 cellular response to external stimulus BP
GO:0072755 cellular response to benomyl BP
GO:0097237 cellular response to toxic substance BP
GO:0104004 cellular response to environmental stimulus BP
GO:1901561 response to benomyl BP
GO:1901698 response to nitrogen compound BP
GO:1901699 cellular response to nitrogen compound BP
GO:1901700 response to oxygen-containing compound BP
GO:1901701 cellular response to oxygen-containing compound BP
GO:1990451 cellular stress response to acidic pH BP
GO:1990928 response to amino acid starvation BP
KEGG Term Name Description
map04141 Protein processing in endoplasmic reticulum The endoplasmic reticulum (ER) is a subcellular organelle where proteins are folded with the help of lumenal chaperones. Newly synthesized peptides enter the ER via the sec61 pore and are glycosylated. Correctly folded proteins are packaged into transport vesicles that shuttle them to the Golgi complex. Misfolded proteins are retained within the ER lumen in complex with molecular chaperones. Proteins that are terminally misfolded bind to BiP and are directed toward degradation through the proteasome in a process called ER-associated degradation (ERAD). Accumulation of misfolded proteins in the ER causes ER stress and activates a signaling pathway called the unfolded protein response (UPR). In certain severe situations, however, the protective mechanisms activated by the UPR are not sufficient to restore normal ER function and cells die by apoptosis.