Basic Information
Gene Structure
Domain
Regulation&
Interaction
Annotation
Orthologus Group
Pathway
Basic Information
Gene ID
SESE_110949.g
View in Genome Browser
Position
Scaffold_159103:5304-5920 (-)
616bp
Gene Type
gene
Gene Description (Protein Product)
Belongs to the small heat shock protein (HSP20) family
Organism
Sequoia sempervirens
Also AS AT1G53540

Gene Structure

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Domain
Database EntryID E-Value Start end InterPro ID Description

Regulation&Interaction
Protein-protein interaction (PPI)
SESE_117324.g Belongs to the small heat shock protein (HSP20) family
SESE_116364.g kDa class I heat shock
SESE_114619.g Belongs to the small heat shock protein (HSP20) family
Regulatory gene
SESE_001495.g B3 domain-containing protein
SESE_002563.g reveille
SESE_003268.g Transcription factor

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Annotation

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


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: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:0009636 response to toxic substance BP
GO:0010033 response to organic substance BP
GO:0010035 response to inorganic substance BP
GO:0010038 response to metal ion BP
GO:0042221 response to chemical BP
GO:0042493 response to xenobiotic stimulus BP
GO:0042542 response to hydrogen peroxide BP
GO:0045471 response to ethanol BP
GO:0046677 response to antibiotic BP
GO:0046685 response to arsenic-containing substance BP
GO:0046686 response to cadmium ion BP
GO:0046688 response to copper ion BP
GO:0050896 response to stimulus BP
GO:0097305 response to alcohol 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.