Basic Information
Gene Structure
Domain
Regulation&
Interaction
Annotation
Orthologus Group
Pathway
Basic Information
Gene ID
Atru.chr9.684.g
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Position
chr9:19775921-19776221 (+)
300bp
Gene Type
gene
Gene Description (Protein Product)
BAG family molecular chaperone regulator
Organism
Acer truncatum
Also AS

Gene Structure

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Domain
Database EntryID E-Value Start end InterPro ID Description

Regulation&Interaction
Protein-protein interaction (PPI)
Atru.chr9.807.g Belongs to the peptidase A1 family
Atru.chr9.933.g T-complex protein 1 subunit

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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:0000003 reproduction BP
GO:0003006 developmental process involved in reproduction BP
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:0006950 response to stress BP
GO:0006970 response to osmotic stress BP
GO:0007275 multicellular organism development BP
GO:0008150 biological_process BP
GO:0009266 response to temperature stimulus BP
GO:0009409 response to cold BP
GO:0009628 response to abiotic stimulus BP
GO:0009651 response to salt stress BP
GO:0009791 post-embryonic development BP
GO:0010228 vegetative to reproductive phase transition of meristem BP
GO:0022414 reproductive process BP
GO:0032501 multicellular organismal process BP
GO:0032502 developmental process BP
GO:0044424 obsolete intracellular part CC
GO:0044444 obsolete cytoplasmic part CC
GO:0044464 obsolete cell part CC
GO:0048608 reproductive structure development BP
GO:0048731 system development BP
GO:0048856 anatomical structure development BP
GO:0050896 response to stimulus BP
GO:0061458 reproductive system development 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.