PPGR - Gene Detail

Basic Information

Gene Structure

Domain

Regulation&
Interaction

Annotation

Orthologus Group

Expresssion

Pathway

Basic Information

Gene ID	Potrx053963g00010 View in Genome Browser
Position	Potrx053963:990-4125 (+) 3135bp
Gene Type	gene
Gene Description (Protein Product)	heat shock protein heat shock
Organism	Populus tremula x Populus tremuloides
Also AS	Potri.001G466000AT5G56010AT5G56000Potri.001G466000.v4.1

upstream:

Domain

Database	EntryID	E-Value	Start	end	InterPro ID	Description

Regulation&Interaction

Protein-protein interaction (PPI)	Potrx066016g00030 Peptidyl-prolyl cis-trans isomerase Potrx059655g00010 Heat shock protein Potrx054955g00020 Heat shock protein
Regulatory gene	Potrx000030g00010 SANT SWI3, ADA2, N-CoR and TFIIIB'' DNA-binding domains Potrx000037g00010 Transcription factor MYB98-like Potrx000061g00010 Transcription factor

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Annotation

Orthologous Group

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

Expression Profile

DataSet	Number of Samples expressed(TPM>1)	Mean	Min	Max	Standard deviation(SD)	Coeffcient variation(CV)

Select Expression

Pathway

GO Term	Description	GO Category
GO:0002376	immune system process	BP
GO:0003674	molecular_function	MF
GO:0003824	catalytic activity	MF
GO:0005575	cellular_component	CC
GO:0005576	extracellular region	CC
GO:0005618	cell wall	CC
GO:0005622	intracellular anatomical structure	CC
GO:0005623	obsolete cell	CC
GO:0005634	nucleus	CC
GO:0005730	nucleolus	CC
GO:0005737	cytoplasm	CC
GO:0005773	vacuole	CC
GO:0005774	vacuolar membrane	CC
GO:0005794	Golgi apparatus	CC
GO:0005829	cytosol	CC
GO:0005886	plasma membrane	CC
GO:0006457	protein folding	BP
GO:0006950	response to stress	BP
GO:0006952	defense response	BP
GO:0006955	immune response	BP
GO:0008150	biological_process	BP
GO:0009266	response to temperature stimulus	BP
GO:0009408	response to heat	BP
GO:0009507	chloroplast	CC
GO:0009532	plastid stroma	CC
GO:0009536	plastid	CC
GO:0009570	chloroplast stroma	CC
GO:0009605	response to external stimulus	BP
GO:0009607	response to biotic stimulus	BP
GO:0009617	response to bacterium	BP
GO:0009628	response to abiotic stimulus	BP
GO:0009814	defense response to other organism	BP
GO:0009816	defense response to bacterium	BP
GO:0009987	cellular process	BP
GO:0010035	response to inorganic substance	BP
GO:0010038	response to metal ion	BP
GO:0012505	endomembrane system	CC
GO:0016020	membrane	CC
GO:0016043	cellular component organization	BP
GO:0016462	pyrophosphatase activity	MF
GO:0016787	hydrolase activity	MF
GO:0016817	hydrolase activity, acting on acid anhydrides	MF
GO:0016818	hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides	MF
GO:0016887	ATP hydrolysis activity	MF
GO:0017111	ribonucleoside triphosphate phosphatase activity	MF
GO:0022607	cellular component assembly	BP
GO:0030312	external encapsulating structure	CC
GO:0031090	organelle membrane	CC
GO:0031974	membrane-enclosed lumen	CC
GO:0031981	nuclear lumen	CC
GO:0034622	protein-containing complex assembly	BP
GO:0042221	response to chemical	BP
GO:0042742	defense response to bacterium	BP
GO:0043207	response to external biotic stimulus	BP
GO:0043226	organelle	CC
GO:0043227	membrane-bounded organelle	CC
GO:0043228	non-membrane-bounded organelle	CC
GO:0043229	intracellular organelle	CC
GO:0043231	intracellular membrane-bounded organelle	CC
GO:0043232	intracellular non-membrane-bounded organelle	CC
GO:0043233	organelle lumen	CC
GO:0043933	protein-containing complex organization	BP
GO:0044085	cellular component biogenesis	BP
GO:0044422	obsolete organelle part	CC
GO:0044424	obsolete intracellular part	CC
GO:0044428	obsolete nuclear part	CC
GO:0044434	obsolete chloroplast part	CC
GO:0044435	obsolete plastid part	CC
GO:0044437	obsolete vacuolar part	CC
GO:0044444	obsolete cytoplasmic part	CC
GO:0044446	obsolete intracellular organelle part	CC
GO:0044464	obsolete cell part	CC
GO:0045087	innate immune response	BP
GO:0048046	apoplast	CC
GO:0050896	response to stimulus	BP
GO:0051131	chaperone-mediated protein complex assembly	BP
GO:0051592	response to calcium ion	BP
GO:0051704	obsolete multi-organism process	BP
GO:0051707	response to other organism	BP
GO:0051716	cellular response to stimulus	BP
GO:0061077	chaperone-mediated protein folding	BP
GO:0065003	protein-containing complex assembly	BP
GO:0070013	intracellular organelle lumen	CC
GO:0070887	cellular response to chemical stimulus	BP
GO:0071241	cellular response to inorganic substance	BP
GO:0071248	cellular response to metal ion	BP
GO:0071277	cellular response to calcium ion	BP
GO:0071840	cellular component organization or biogenesis	BP
GO:0071944	cell periphery	CC
GO:0098542	defense response to other organism	BP
GO:0098588	bounding membrane of organelle	CC
GO:0098805	membrane	CC

KEGG Term	Name	Description
map04626	Plant-pathogen interaction	Plants lack animal-like adaptive immunity mechanisms, and therefore have evolved a specific system with multiple layers against invading pathogens. The primary response includes the perception of pathogens by cell-surface pattern-recognition receptors (PRRs) and is referred to as PAMP-triggered immunity (PTI). Activation of FLS2 and EFR triggers MAPK signaling pathway that activates defense genes for antimictobial compounds. The increase in the cytosolic Ca2+ concentration is also a regulator for production of reactive oxygen species and localized programmed cell death/hypersensitive response. The secondary response is called effector-triggered immunity (ETI). Pathogens can acquire the ability to suppress PTI by directly injecting effector proteins into the plant cell through secretion systems. In addition, pathogens can manipulate plant hormone signaling pathways to evade host immune responses using coronatine toxin. Some plants possess specific intracellular surveillance proteins (R proteins) to monitor the presence of pathogen virulence proteins. This ETI occurs with localized programmed cell death to arrest pathogen growth, resulting in cultivar-specific disease resistance.
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.