Basic Information
Gene Structure
Domain
Regulation&
Interaction
Annotation
Orthologus Group
Pathway
Basic Information
Gene ID
EVM0029903
View in Genome Browser
Position
GWHASIS00000022:10465728-10472271 (+)
6543bp
Gene Type
gene
Gene Description (Protein Product)
Membrane-bound transcription factor site-1
Organism
Acer catalpifolium
Also AS AT5G19660

Gene Structure

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Domain
Database EntryID E-Value Start end InterPro ID Description

Regulation&Interaction
Protein-protein interaction (PPI)
EVM0035058 21 kDa protein-like
EVM0035005 21 kDa protein-like
EVM0034588 21 kDa protein-like
Regulatory gene
EVM0001315 transcription factor that promotes early floral meristem identity in synergy with APETALA1; FRUITFULL and LEAFY. Is required subsequently for the transition of an inflorescence meristem into a floral meristem. Seems to be partially redundant to the function of APETALA1
EVM0001373 Transcriptional regulator
EVM0001785 transcription 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:0000139 Golgi membrane CC
GO:0003674 molecular_function MF
GO:0003824 catalytic activity MF
GO:0004175 endopeptidase activity MF
GO:0004222 metalloendopeptidase activity MF
GO:0004252 serine-type endopeptidase 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:0005789 endoplasmic reticulum membrane CC
GO:0005794 Golgi apparatus CC
GO:0006464 protein modification process BP
GO:0006508 proteolysis BP
GO:0006807 nitrogen compound metabolic process BP
GO:0006950 response to stress BP
GO:0006970 response to osmotic stress BP
GO:0006972 hyperosmotic response BP
GO:0006984 ER-nucleus signaling pathway BP
GO:0006986 response to unfolded protein BP
GO:0006996 organelle organization BP
GO:0007033 vacuole organization BP
GO:0007040 lysosome organization BP
GO:0007154 cell communication BP
GO:0007165 signal transduction BP
GO:0008150 biological_process BP
GO:0008152 metabolic process BP
GO:0008233 peptidase activity MF
GO:0008236 serine-type peptidase activity MF
GO:0008237 metallopeptidase activity MF
GO:0009628 response to abiotic stimulus BP
GO:0009651 response to salt stress BP
GO:0009889 regulation of biosynthetic process BP
GO:0009987 cellular process BP
GO:0010033 response to organic substance BP
GO:0012505 endomembrane system CC
GO:0016020 membrane CC
GO:0016043 cellular component organization BP
GO:0016787 hydrolase activity MF
GO:0017171 serine hydrolase activity MF
GO:0019216 regulation of lipid metabolic process BP
GO:0019218 regulation of steroid metabolic process BP
GO:0019222 regulation of metabolic process BP
GO:0019538 protein metabolic process BP
GO:0023052 signaling BP
GO:0030968 endoplasmic reticulum unfolded protein response BP
GO:0031090 organelle membrane CC
GO:0031293 membrane protein intracellular domain proteolysis BP
GO:0031974 membrane-enclosed lumen CC
GO:0031984 organelle subcompartment CC
GO:0033554 cellular response to stress BP
GO:0033619 membrane protein proteolysis BP
GO:0034620 cellular response to unfolded protein BP
GO:0034976 response to endoplasmic reticulum stress BP
GO:0035966 response to topologically incorrect protein BP
GO:0035967 cellular response to topologically incorrect protein BP
GO:0036211 protein modification process BP
GO:0036500 ATF6-mediated unfolded protein response BP
GO:0042175 nuclear outer membrane-endoplasmic reticulum membrane network CC
GO:0042221 response to chemical BP
GO:0042538 hyperosmotic salinity response BP
GO:0043170 macromolecule metabolic process 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:0043412 macromolecule modification BP
GO:0043687 post-translational protein modification BP
GO:0044237 cellular metabolic process BP
GO:0044238 primary metabolic process BP
GO:0044260 cellular macromolecule metabolic process BP
GO:0044267 protein metabolic process BP
GO:0044422 obsolete organelle part CC
GO:0044424 obsolete intracellular part CC
GO:0044425 obsolete membrane part CC
GO:0044431 obsolete Golgi apparatus 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:0045540 regulation of cholesterol biosynthetic process BP
GO:0046890 regulation of lipid biosynthetic process BP
GO:0050789 regulation of biological process BP
GO:0050794 regulation of cellular process BP
GO:0050810 regulation of steroid biosynthetic process BP
GO:0050896 response to stimulus BP
GO:0051716 cellular response to stimulus BP
GO:0062012 regulation of small molecule metabolic process BP
GO:0065007 biological regulation BP
GO:0070011 peptidase activity MF
GO:0070013 intracellular organelle lumen CC
GO:0070887 cellular response to chemical stimulus BP
GO:0071310 cellular response to organic substance BP
GO:0071704 organic substance metabolic process BP
GO:0071840 cellular component organization or biogenesis BP
GO:0080090 regulation of primary metabolic process BP
GO:0080171 lytic vacuole organization BP
GO:0090181 regulation of cholesterol metabolic process BP
GO:0098588 bounding membrane of organelle CC
GO:0098791 Golgi apparatus subcompartment CC
GO:0098827 endoplasmic reticulum subcompartment CC
GO:0106118 regulation of sterol biosynthetic process BP
GO:0140096 catalytic activity, acting on a protein MF
GO:1901564 organonitrogen compound metabolic process BP
GO:1902930 regulation of alcohol biosynthetic process 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.