PPGR - Gene Detail

Basic Information

Gene ID	gene-IMY05_015G0074600 View in Genome Browser
Position	CM029813.1:8942048-8946719 (+) 4671bp
Gene Type	gene
Gene Description (Protein Product)	Cell division cycle protein 48 homolog
Organism	Salix suchowensis
Also AS	AT5G03340

upstream:

Domain

Database	EntryID	E-Value	Start	end	InterPro ID	Description

Regulation&Interaction

Protein-protein interaction (PPI)

gene-IMY05_C4625000200 Belongs to the AAA ATPase family

gene-IMY05_019G0094500 Belongs to the protein kinase superfamily. Ser Thr protein kinase family

gene-IMY05_017G0026400 Ubiquitin exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked

Regulatory gene

gene-IMY05_001G0168300 MADS-box transcription factor

gene-IMY05_002G0023100 Floral homeotic protein

gene-IMY05_002G0028800 Zinc-finger homeodomain protein

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Annotation

Orthologous Group

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

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.