Basic Information
Gene ID
geneMaker00012854
Position
GWHBGXC00000003:15914685-15916853 (-)
2168bp
Gene Type
gene
Gene Description (Protein Product)
Belongs to the small heat shock protein (HSP20) family
Organism
Also AS AT1G52560

Gene Structure

upstream:

Domain
Database EntryID E-Value Start end InterPro ID Description

Regulation&Interaction
Protein-protein interaction (PPI)
geneMaker00015072 Signal recognition particle 43 kDa protein
geneMaker00018054 Shikimate kinase
Regulatory gene
geneMaker00000164 MADS-box transcription factor
geneMaker00000573 WRKY Transcription Factor
geneMaker00001778 Agamous-like MADS-box protein AGL9 homolog

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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 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:0008150 biological_process BP
GO:0009266 response to temperature stimulus BP
GO:0009314 response to radiation BP
GO:0009408 response to heat BP
GO:0009416 response to light stimulus BP
GO:0009628 response to abiotic stimulus BP
GO:0009636 response to toxic substance BP
GO:0009642 response to light intensity BP
GO:0009644 response to high light intensity BP
GO:0010035 response to inorganic substance BP
GO:0042221 response to chemical BP
GO:0042493 response to xenobiotic stimulus BP
GO:0042542 response to hydrogen peroxide BP
GO:0046677 response to antibiotic BP
GO:0050896 response to stimulus BP
GO:1901700 response to oxygen-containing compound 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.