Basic Information
Gene ID
Pop_G13G024588
Position
chrG13:6428638-6429397 (-)
759bp
Gene Type
gene
Gene Description (Protein Product)
Belongs to the small heat shock protein (HSP20) family
Organism
Also AS Potri.013G089200AT4G10250Potri.013G089200.v4.1

Gene Structure

upstream:

Domain
Database EntryID E-Value Start end InterPro ID Description

Regulation&Interaction
Protein-protein interaction (PPI)
Pop_G19G009775 Belongs to the small heat shock protein (HSP20) family
Pop_G15G015223 small heat shock protein
Pop_UnG069985 small heat shock protein
Regulatory gene
Pop_A01G004206 Myb family transcription factor
Pop_A01G004498 Tesmin/TSO1-like CXC domain
Pop_A01G005990 MADS-box transcription factor

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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:0005575 cellular_component CC
GO:0005622 intracellular anatomical structure CC
GO:0005623 obsolete cell CC
GO:0005737 cytoplasm CC
GO:0005783 endoplasmic reticulum CC
GO:0006950 response to stress BP
GO:0008150 biological_process BP
GO:0009266 response to temperature stimulus BP
GO:0009408 response to heat BP
GO:0009628 response to abiotic stimulus BP
GO:0012505 endomembrane system CC
GO:0043226 organelle CC
GO:0043227 membrane-bounded organelle CC
GO:0043229 intracellular organelle CC
GO:0043231 intracellular membrane-bounded organelle CC
GO:0044424 obsolete intracellular part CC
GO:0044444 obsolete cytoplasmic part CC
GO:0044464 obsolete cell part CC
GO:0050896 response to stimulus 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.