PPGR - Gene Detail

Basic Information

Gene ID	ACSA_15866.g View in Genome Browser
Position	acsa_387:29767028-29771022 (+) 3994bp
Gene Type	gene
Gene Description (Protein Product)	Belongs to the heat shock protein 70 family
Organism	Acer saccharum
Also AS	AT5G49910

upstream:

Domain

Database	EntryID	E-Value	Start	end	InterPro ID	Description

Regulation&Interaction

Protein-protein interaction (PPI)

ACSA_21521.g Belongs to the 14-3-3 family

ACSA_31737.g Belongs to the ubiquitin-conjugating enzyme family

ACSA_33580.g Ubiquitin-conjugating enzyme E2, catalytic domain homologues

Load All Networks

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:0005576	extracellular region	CC
GO:0005622	intracellular anatomical structure	CC
GO:0005623	obsolete cell	CC
GO:0005737	cytoplasm	CC
GO:0006605	protein targeting	BP
GO:0006810	transport	BP
GO:0006886	intracellular protein transport	BP
GO:0006950	response to stress	BP
GO:0008104	protein localization	BP
GO:0008150	biological_process	BP
GO:0009266	response to temperature stimulus	BP
GO:0009408	response to heat	BP
GO:0009507	chloroplast	CC
GO:0009526	plastid envelope	CC
GO:0009532	plastid stroma	CC
GO:0009536	plastid	CC
GO:0009570	chloroplast stroma	CC
GO:0009579	thylakoid	CC
GO:0009628	response to abiotic stimulus	BP
GO:0009941	chloroplast envelope	CC
GO:0010035	response to inorganic substance	BP
GO:0010038	response to metal ion	BP
GO:0015031	protein transport	BP
GO:0015833	peptide transport	BP
GO:0031967	organelle envelope	CC
GO:0031975	envelope	CC
GO:0033036	macromolecule localization	BP
GO:0033365	protein localization to organelle	BP
GO:0034613	protein localization	BP
GO:0042221	response to chemical	BP
GO:0042886	amide transport	BP
GO:0043226	organelle	CC
GO:0043227	membrane-bounded organelle	CC
GO:0043229	intracellular organelle	CC
GO:0043231	intracellular membrane-bounded organelle	CC
GO:0044422	obsolete organelle part	CC
GO:0044424	obsolete intracellular part	CC
GO:0044434	obsolete chloroplast part	CC
GO:0044435	obsolete plastid part	CC
GO:0044444	obsolete cytoplasmic part	CC
GO:0044446	obsolete intracellular organelle part	CC
GO:0044464	obsolete cell part	CC
GO:0045036	protein targeting to chloroplast	BP
GO:0045184	establishment of protein localization	BP
GO:0046686	response to cadmium ion	BP
GO:0046907	intracellular transport	BP
GO:0048046	apoplast	CC
GO:0050896	response to stimulus	BP
GO:0051179	localization	BP
GO:0051234	establishment of localization	BP
GO:0051641	cellular localization	BP
GO:0051649	establishment of localization in cell	BP
GO:0070727	cellular macromolecule localization	BP
GO:0071702	organic substance transport	BP
GO:0071705	nitrogen compound transport	BP
GO:0072594	establishment of protein localization to organelle	BP
GO:0072596	establishment of protein localization to chloroplast	BP
GO:0072598	protein localization to chloroplast	BP

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.