PPGR - Gene Detail

Basic Information

Gene ID	JsiChr09G11267.g View in Genome Browser
Position	chr9:11971966-11979331 (-) 7365bp
Gene Type	gene
Gene Description (Protein Product)	Endoplasmic
Organism	Juglans sigillata
Also AS	AT2G38960

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Domain

Database	EntryID	E-Value	Start	end	InterPro ID	Description

Regulation&Interaction

Protein-protein interaction (PPI)

JsiChr13G11887.g Protein disulfide isomerase-like

JsiChr16G10693.g disulfide-isomerase

JsiChr09G12381.g 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

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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: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:0005789	endoplasmic reticulum membrane	CC
GO:0006457	protein folding	BP
GO:0006464	protein modification process	BP
GO:0006807	nitrogen compound metabolic process	BP
GO:0008150	biological_process	BP
GO:0008152	metabolic process	BP
GO:0009987	cellular process	BP
GO:0012505	endomembrane system	CC
GO:0015035	protein-disulfide reductase activity	MF
GO:0015036	disulfide oxidoreductase activity	MF
GO:0016020	membrane	CC
GO:0016491	oxidoreductase activity	MF
GO:0016667	oxidoreductase activity, acting on a sulfur group of donors	MF
GO:0016853	isomerase activity	MF
GO:0016860	intramolecular oxidoreductase activity	MF
GO:0016864	intramolecular oxidoreductase activity, transposing S-S bonds	MF
GO:0019538	protein metabolic process	BP
GO:0031984	organelle subcompartment	CC
GO:0034975	protein folding in endoplasmic reticulum	BP
GO:0036211	protein modification process	BP
GO:0042175	nuclear outer membrane-endoplasmic reticulum membrane network	CC
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:0043412	macromolecule 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: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:0055114	obsolete oxidation-reduction process	BP
GO:0071704	organic substance metabolic process	BP
GO:0098827	endoplasmic reticulum subcompartment	CC
GO:0140096	catalytic activity, acting on a protein	MF
GO:1901564	organonitrogen compound metabolic 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.