Basic Information
Gene Structure
Domain
Regulation&
Interaction
Annotation
Orthologus Group
Pathway
Basic Information
Gene ID
ACNE_04679.g
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Position
acne_103:22468763-22469197 (-)
434bp
Gene Type
gene
Gene Description (Protein Product)
heat- shock
Organism
Acer negundo
Also AS AT1G07400

Gene Structure

upstream:
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Domain
Database EntryID E-Value Start end InterPro ID Description

Regulation&Interaction
Protein-protein interaction (PPI)
ACNE_09629.g Ankyrin repeat domain-containing protein
ACNE_10327.g 14 kDa zinc-binding
ACNE_24272.g SAGA-associated factor 11
Regulatory gene
ACNE_06606.g Heat Stress Transcription Factor
ACNE_06928.g Heat stress transcription factor
ACNE_07446.g Heat stress 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:0003674 molecular_function MF
GO:0005488 binding MF
GO:0005515 protein binding MF
GO:0005575 cellular_component CC
GO:0005622 intracellular anatomical structure CC
GO:0005623 obsolete cell CC
GO:0005737 cytoplasm CC
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:0043621 protein self-association MF
GO:0044424 obsolete intracellular 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.