Basic Information
Gene Structure
Domain
Regulation&
Interaction
Annotation
Orthologus Group
Pathway
Basic Information
Gene ID
gene-IMY05_009G0042200
View in Genome Browser
Position
CM029807.1:4477663-4489949 (-)
12286bp
Gene Type
gene
Gene Description (Protein Product)
transport protein
Organism
Salix suchowensis
Also AS AT3G63460

Gene Structure

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

Regulation&Interaction
Protein-protein interaction (PPI)
gene-IMY05_010G0078200 Belongs to the WD repeat SEC13 family
gene-IMY05_010G0168100 Protein transport protein Sec24-like
gene-IMY05_013G0035600 Protein transport protein Sec24-like
Regulatory gene
gene-IMY05_001G0054900 AP2-like ethylene-responsive transcription factor
gene-IMY05_001G0065700 Dof domain, zinc finger
gene-IMY05_001G0068000 Dof domain, zinc finger

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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:0005829 cytosol CC
GO:0005911 cell-cell junction CC
GO:0009506 plasmodesma CC
GO:0016020 membrane CC
GO:0030054 cell junction CC
GO:0044424 obsolete intracellular part CC
GO:0044444 obsolete cytoplasmic part CC
GO:0044464 obsolete cell part CC
GO:0055044 symplast 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.