Basic Information
Gene ID
Position
Chr14:69714419-69714985 (-)
566bp
Gene Type
gene
Gene Description (Protein Product)
Belongs to the heat shock protein 70 family
Organism
Also AS AT5G28540

Gene Structure

upstream:

Domain
Database EntryID E-Value Start end InterPro ID Description

Regulation&Interaction
Protein-protein interaction (PPI)
CSS0046348.g Belongs to the TRAFAC class myosin-kinesin ATPase superfamily. Myosin family
CSS0050244.g mediator of RNA polymerase II transcription subunit
CSS0049671.g mediator of RNA polymerase II transcription subunit
Regulatory gene
CSS0000220.g Transcription factor
CSS0000442.g transcription factor
CSS0000465.g SANT SWI3, ADA2, N-CoR and TFIIIB'' DNA-binding domains

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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)


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:0005634 nucleus CC
GO:0005654 nucleoplasm CC
GO:0005730 nucleolus CC
GO:0005737 cytoplasm CC
GO:0005773 vacuole CC
GO:0005774 vacuolar membrane CC
GO:0005783 endoplasmic reticulum CC
GO:0005794 Golgi apparatus CC
GO:0005829 cytosol CC
GO:0005886 plasma membrane CC
GO:0005911 cell-cell junction CC
GO:0006508 proteolysis BP
GO:0006511 ubiquitin-dependent protein catabolic process BP
GO:0006807 nitrogen compound metabolic process BP
GO:0006950 response to stress BP
GO:0008150 biological_process BP
GO:0008152 metabolic process BP
GO:0009056 catabolic process BP
GO:0009057 macromolecule catabolic process BP
GO:0009506 plasmodesma CC
GO:0009507 chloroplast CC
GO:0009536 plastid CC
GO:0009719 response to endogenous stimulus BP
GO:0009725 response to hormone BP
GO:0009735 response to cytokinin BP
GO:0009987 cellular process BP
GO:0010033 response to organic substance BP
GO:0010035 response to inorganic substance BP
GO:0010038 response to metal ion BP
GO:0010243 response to organonitrogen compound BP
GO:0010498 proteasomal protein catabolic process BP
GO:0012505 endomembrane system CC
GO:0016020 membrane CC
GO:0016592 mediator complex CC
GO:0019538 protein metabolic process BP
GO:0019941 modification-dependent protein catabolic process BP
GO:0030054 cell junction CC
GO:0030163 protein catabolic process BP
GO:0030312 external encapsulating structure CC
GO:0030433 ubiquitin-dependent ERAD pathway BP
GO:0031090 organelle membrane CC
GO:0031974 membrane-enclosed lumen CC
GO:0031981 nuclear lumen CC
GO:0032991 protein-containing complex CC
GO:0033554 cellular response to stress BP
GO:0034976 response to endoplasmic reticulum stress BP
GO:0036503 ERAD pathway BP
GO:0042221 response to chemical BP
GO:0043161 proteasome-mediated ubiquitin-dependent protein catabolic process BP
GO:0043170 macromolecule metabolic process 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:0043632 modification-dependent macromolecule catabolic process BP
GO:0044237 cellular metabolic process BP
GO:0044238 primary metabolic process BP
GO:0044248 cellular catabolic process BP
GO:0044257 protein catabolic process BP
GO:0044260 cellular macromolecule metabolic process BP
GO:0044265 cellular macromolecule catabolic process BP
GO:0044267 protein metabolic process BP
GO:0044422 obsolete organelle part CC
GO:0044424 obsolete intracellular part CC
GO:0044428 obsolete nuclear part CC
GO:0044437 obsolete vacuolar part CC
GO:0044444 obsolete cytoplasmic part CC
GO:0044446 obsolete intracellular organelle part CC
GO:0044451 obsolete nucleoplasm part CC
GO:0044464 obsolete cell part CC
GO:0046686 response to cadmium ion BP
GO:0050896 response to stimulus BP
GO:0051603 proteolysis involved in protein catabolic process BP
GO:0051716 cellular response to stimulus BP
GO:0055044 symplast CC
GO:0070013 intracellular organelle lumen CC
GO:0071704 organic substance metabolic process BP
GO:0071944 cell periphery CC
GO:0098588 bounding membrane of organelle CC
GO:0098805 membrane CC
GO:1901564 organonitrogen compound metabolic process BP
GO:1901565 organonitrogen compound catabolic process BP
GO:1901575 organic substance catabolic process BP
GO:1901698 response to nitrogen compound 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.
map03060 Protein export The protein export is the active transport of proteins from the cytoplasm to the exterior of the cell, or to the periplasmic compartment in Gram-negative bacteria. The sec dependent pathway is the general protein export system that transports newly synthesized proteins into or across the cell membrane. The translocation channel is formed from a conserved trimeric membrane protein complex, called the Sec61/SecY complex. The twin-arginine translocation (Tat) pathway is another protein transport system that transports folded proteins in bacteria, archaea, and chloroplasts. Many Tat systems comprise three functionally different membrane proteins, TatA, TatB, and TatC, but TatA and TatE seem to have overlapping functions, with TatA having by far the more important role.