Basic Information
Gene Structure
Domain
Regulation&
Interaction
Annotation
Orthologus Group
Pathway
Basic Information
Gene ID
EVM0022445
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Position
GWHASIS00000025:600433-604878 (-)
4445bp
Gene Type
gene
Gene Description (Protein Product)
Cell division cycle protein 48 homolog
Organism
Acer catalpifolium
Also AS AT5G03340

Gene Structure

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Domain
Database EntryID E-Value Start end InterPro ID Description

Regulation&Interaction
Protein-protein interaction (PPI)
EVM0032750 UBA and UBX domain-containing protein
EVM0027613 Belongs to the protein kinase superfamily. Ser Thr protein kinase family
EVM0025937 Ubiquitin fusion degradation protein 1 homolog
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
EVM0003629 MADS-box protein
EVM0005245 MADS-box protein

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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:0005623 obsolete cell CC
GO:0005886 plasma membrane CC
GO:0016020 membrane CC
GO:0044464 obsolete cell part CC
GO:0071944 cell periphery 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.