PPGR - Gene Detail

Basic Information

Gene ID	JsiChr13G11467.g View in Genome Browser
Position	chr13:7957606-7958530 (+) 924bp
Gene Type	gene
Gene Description (Protein Product)	Belongs to the small heat shock protein (HSP20) family
Organism	Juglans sigillata
Also AS	AT1G53540

upstream:

Domain

Database	EntryID	E-Value	Start	end	InterPro ID	Description

Regulation&Interaction

Protein-protein interaction (PPI)

JsiChr15G11858.g heat shock

JsiChr14G11059.g Catalyzes the dehydration of the S-form of NAD(P)HX at the expense of ATP, which is converted to ADP. Together with NAD(P)HX epimerase, which catalyzes the epimerization of the S- and R-forms, the enzyme allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration

JsiChr14G10212.g Nucleoside diphosphate kinase

Regulatory gene

JsiChr01G10052.g Myb-related protein

JsiChr01G10055.g Myb-related protein

JsiChr01G10114.g MADS-box 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 Term	Description	GO Category
GO:0005575	cellular_component	CC
GO:0005622	intracellular anatomical structure	CC
GO:0005623	obsolete cell	CC
GO:0005737	cytoplasm	CC
GO:0044424	obsolete intracellular part	CC
GO:0044464	obsolete cell part	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.