Basic Information
Gene Structure
Domain
Regulation&
Interaction
Annotation
Orthologus Group
Expresssion
Pathway
Basic Information
Gene ID
FRAEX38873_v2_000256150
View in Genome Browser
Position
Contig4926:64767-69751 (-)
4984bp
Gene Type
gene
Gene Description (Protein Product)
Thioredoxin-like domain
Organism
Fraxinus excelsior
Also AS AT1G77510

Gene Structure

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Domain
Database EntryID E-Value Start end InterPro ID Description

Regulation&Interaction
Protein-protein interaction (PPI)
FRAEX38873_v2_000399160 Endoplasmic
FRAEX38873_v2_000272400 Belongs to the peptidase C1 family
FRAEX38873_v2_000328910 Belongs to the peptidase C1 family
Regulatory gene
FRAEX38873_v2_000008150 Dof zinc finger protein
FRAEX38873_v2_000018390 Protein tesmin TSO1-like CXC 5
FRAEX38873_v2_000026520 dof zinc finger protein

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Annotation

Orthologous Group
Orthologous ID Species Number All hits in PereRegDB Hits of this species Orthologous Detail

Expression Profile
DataSet Number of Samples expressed(TPM>1) Mean Min Max Standard deviation(SD) Coeffcient variation(CV)


Pathway
Go Pathway KEGG Pathway
GO Term Description GO Category
GO:0000003 reproduction BP
GO:0003006 developmental process involved in reproduction BP
GO:0003674 molecular_function MF
GO:0003756 protein disulfide isomerase activity MF
GO:0003824 catalytic activity MF
GO:0005575 cellular_component CC
GO:0005622 intracellular anatomical structure CC
GO:0005623 obsolete cell CC
GO:0005737 cytoplasm CC
GO:0005783 endoplasmic reticulum CC
GO:0005788 endoplasmic reticulum lumen CC
GO:0006457 protein folding BP
GO:0006950 response to stress BP
GO:0007275 multicellular organism development BP
GO:0008150 biological_process BP
GO:0009791 post-embryonic development BP
GO:0009888 tissue development BP
GO:0009960 endosperm development BP
GO:0009987 cellular process BP
GO:0010154 fruit development BP
GO:0012505 endomembrane system CC
GO:0016853 isomerase activity MF
GO:0016860 intramolecular oxidoreductase activity MF
GO:0016864 intramolecular oxidoreductase activity, transposing S-S bonds MF
GO:0022414 reproductive process BP
GO:0031974 membrane-enclosed lumen CC
GO:0032501 multicellular organismal process BP
GO:0032502 developmental process BP
GO:0033554 cellular response to stress BP
GO:0034975 protein folding in endoplasmic reticulum BP
GO:0034976 response to endoplasmic reticulum stress BP
GO:0043226 organelle CC
GO:0043227 membrane-bounded organelle CC
GO:0043229 intracellular organelle CC
GO:0043231 intracellular membrane-bounded organelle CC
GO:0043233 organelle lumen CC
GO:0044422 obsolete organelle part CC
GO:0044424 obsolete intracellular part CC
GO:0044432 obsolete endoplasmic reticulum part CC
GO:0044444 obsolete cytoplasmic part CC
GO:0044446 obsolete intracellular organelle part CC
GO:0044464 obsolete cell part CC
GO:0048316 seed development BP
GO:0048608 reproductive structure development BP
GO:0048731 system development BP
GO:0048856 anatomical structure development BP
GO:0050896 response to stimulus BP
GO:0051716 cellular response to stimulus BP
GO:0061458 reproductive system development BP
GO:0070013 intracellular organelle lumen CC
GO:0140096 catalytic activity, acting on a protein MF
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.