PPGR - Gene Detail

Basic Information

Gene ID	PtXG17620 View in Genome Browser
Position	chr10:524251816-524252286 (-) 470bp
Gene Type	gene
Gene Description (Protein Product)	heat shock protein
Organism	Pinus tabuliformis
Also AS	AT1G16030

upstream:

Domain

Database	EntryID	E-Value	Start	end	InterPro ID	Description

Regulation&Interaction

Protein-protein interaction (PPI)

PtXG22250 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

PtXG22250 Ubiquitin family

PtXG53520 60S ribosomal protein

Regulatory gene

Pt0G01630 dof zinc finger protein

Pt0G07980 dof zinc finger protein

Pt1G66310 Dof domain, zinc finger

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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:0005575	cellular_component	CC
GO:0005618	cell wall	CC
GO:0005622	intracellular anatomical structure	CC
GO:0005623	obsolete cell	CC
GO:0005737	cytoplasm	CC
GO:0005886	plasma membrane	CC
GO:0006950	response to stress	BP
GO:0008150	biological_process	BP
GO:0009266	response to temperature stimulus	BP
GO:0009408	response to heat	BP
GO:0009507	chloroplast	CC
GO:0009536	plastid	CC
GO:0009605	response to external stimulus	BP
GO:0009607	response to biotic stimulus	BP
GO:0009615	response to virus	BP
GO:0009628	response to abiotic stimulus	BP
GO:0016020	membrane	CC
GO:0030312	external encapsulating structure	CC
GO:0043207	response to external biotic stimulus	BP
GO:0043226	organelle	CC
GO:0043227	membrane-bounded organelle	CC
GO:0043229	intracellular organelle	CC
GO:0043231	intracellular membrane-bounded organelle	CC
GO:0044424	obsolete intracellular part	CC
GO:0044444	obsolete cytoplasmic part	CC
GO:0044464	obsolete cell part	CC
GO:0050896	response to stimulus	BP
GO:0051704	obsolete multi-organism process	BP
GO:0051707	response to other organism	BP
GO:0071944	cell periphery	CC

KEGG Term	Name	Description
map04144	Endocytosis	Endocytosis is a mechanism for cells to remove ligands, nutrients, and plasma membrane (PM) proteins, and lipids from the cell surface, bringing them into the cell interior. Transmembrane proteins entering through clathrin-dependent endocytosis (CDE) have sequences in their cytoplasmic domains that bind to the APs (adaptor-related protein complexes) and enable their rapid removal from the PM. In addition to APs and clathrin, there are numerous accessory proteins including dynamin. Depending on the various proteins that enter the endosome membrane, these cargoes are sorted to distinct destinations. Some cargoes, such as nutrient receptors, are recycled back to the PM. Ubiquitylated membrane proteins, such as activated growth-factor receptors, are sorted into intraluminal vesicles and eventually end up in the lysosome lumen via multivesicular endosomes (MVEs). There are distinct mechanisms of clathrin-independent endocytosis (CIE) depending upon the cargo and the cell type.
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.
map03040	Spliceosome	After transcription, eukaryotic mRNA precursors contain protein-coding exons and noncoding introns. In the following splicing, introns are excised and exons are joined by a macromolecular complex, the spliceosome. The standard spliceosome is made up of five small nuclear ribonucleoproteins (snRNPs), U1, U2, U4, U5, and U6 snRNPs, and several spliceosome-associated proteins (SAPs). Spliceosomes are not a simple stable complex, but a dynamic family of particles that assemble on the mRNA precursor and help fold it into a conformation that allows transesterification to proceed. Various spliceosome forms (e.g. A-, B- and C-complexes) have been identified.