Basic Information
Gene Structure
Domain
Regulation&
Interaction
Annotation
Orthologus Group
Pathway
Basic Information
Gene ID
Potra2n1c2261
View in Genome Browser
Position
chr1:26988296-26991853 (-)
3557bp
Gene Type
gene
Gene Description (Protein Product)
transport protein
Organism
Populus tremula
Also AS Potri.001G260900AT3G63460Potri.001G260900.v4.1

Gene Structure

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Domain
Database EntryID E-Value Start end InterPro ID Description

Regulation&Interaction
Protein-protein interaction (PPI)
Potra2n8c17927 Belongs to the WD repeat SEC13 family
Potra2n5c12426 Protein transport protein Sec24-like
Potra2n8c17057 Protein transport protein Sec24-like
Regulatory gene
Potra2n10c20596 Dof zinc finger protein
Potra2n10c20932 Zinc-finger homeodomain protein
Potra2n10c20949 Cyclic dof 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: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.