Basic Information
Gene Structure
Domain
Regulation&
Interaction
Annotation
Orthologus Group
Pathway
Basic Information
Gene ID
gene-DKX38_023464
View in Genome Browser
Position
CM018587.1:1862391-1874374 (+)
11983bp
Gene Type
gene
Gene Description (Protein Product)
Heat shock 70 kDa protein
Organism
Salix brachista
Also AS AT4G16660

Gene Structure

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Domain
Database EntryID E-Value Start end InterPro ID Description

Regulation&Interaction
Protein-protein interaction (PPI)
gene-DKX38_029313 Belongs to the heat shock protein 70 family
gene-DKX38_027514 Translocation protein SEC63 homolog
gene-DKX38_029623 disulfide-isomerase

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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:0005575 cellular_component CC
GO:0005622 intracellular anatomical structure CC
GO:0005623 obsolete cell CC
GO:0005737 cytoplasm CC
GO:0005773 vacuole CC
GO:0005774 vacuolar membrane CC
GO:0005783 endoplasmic reticulum CC
GO:0005794 Golgi apparatus CC
GO:0009507 chloroplast CC
GO:0009536 plastid CC
GO:0012505 endomembrane system CC
GO:0016020 membrane CC
GO:0031090 organelle membrane CC
GO:0043226 organelle CC
GO:0043227 membrane-bounded organelle CC
GO:0043229 intracellular organelle CC
GO:0043231 intracellular membrane-bounded organelle CC
GO:0044422 obsolete organelle part CC
GO:0044424 obsolete intracellular part CC
GO:0044437 obsolete vacuolar part CC
GO:0044444 obsolete cytoplasmic part CC
GO:0044446 obsolete intracellular organelle part CC
GO:0044464 obsolete cell part CC
GO:0098588 bounding membrane of organelle CC
GO:0098805 membrane CC
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.