Basic Information
Gene Structure
Domain
Regulation&
Interaction
Annotation
Orthologus Group
Expresssion
Pathway
Basic Information
Gene ID
CSS0036209.g
View in Genome Browser
Position
Chr7:182972560-182974569 (+)
2009bp
Gene Type
gene
Gene Description (Protein Product)
Belongs to the small heat shock protein (HSP20) family
Organism
Camellia sinensis
Also AS AT4G27670

Gene Structure

upstream:
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Domain
Database EntryID E-Value Start end InterPro ID Description

Regulation&Interaction
Protein-protein interaction (PPI)
CSS0050326.g lactate/malate dehydrogenase, alpha/beta C-terminal domain
CSS0040190.g lactate/malate dehydrogenase, alpha/beta C-terminal domain
CSS0040062.g lactate/malate dehydrogenase, alpha/beta C-terminal domain
Regulatory gene
CSS0004712.g GAGA binding protein-like family
CSS0007067.g Protein BASIC PENTACYSTEINE6-like
CSS0008658.g Protein BASIC PENTACYSTEINE2-like

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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 Pathway KEGG Pathway
GO Term Description GO Category
GO:0000302 response to reactive oxygen species BP
GO:0003674 molecular_function MF
GO:0005488 binding MF
GO:0005515 protein binding MF
GO:0005575 cellular_component CC
GO:0005622 intracellular anatomical structure CC
GO:0005623 obsolete cell CC
GO:0005737 cytoplasm CC
GO:0006355 regulation of DNA-templated transcription BP
GO:0006950 response to stress BP
GO:0006979 response to oxidative stress BP
GO:0006996 organelle organization BP
GO:0008150 biological_process BP
GO:0009266 response to temperature stimulus BP
GO:0009295 nucleoid CC
GO:0009314 response to radiation BP
GO:0009408 response to heat BP
GO:0009416 response to light stimulus BP
GO:0009507 chloroplast CC
GO:0009532 plastid stroma CC
GO:0009536 plastid CC
GO:0009570 chloroplast stroma CC
GO:0009628 response to abiotic stimulus BP
GO:0009636 response to toxic substance BP
GO:0009642 response to light intensity BP
GO:0009644 response to high light intensity BP
GO:0009657 plastid organization BP
GO:0009658 chloroplast organization BP
GO:0009889 regulation of biosynthetic process BP
GO:0009987 cellular process BP
GO:0010035 response to inorganic substance BP
GO:0010468 regulation of gene expression BP
GO:0010556 regulation of macromolecule biosynthetic process BP
GO:0016043 cellular component organization BP
GO:0019219 regulation of nucleobase-containing compound metabolic process BP
GO:0019222 regulation of metabolic process BP
GO:0031323 regulation of cellular metabolic process BP
GO:0031326 regulation of cellular biosynthetic process BP
GO:0032991 protein-containing complex CC
GO:0042221 response to chemical BP
GO:0042493 response to xenobiotic stimulus BP
GO:0042542 response to hydrogen peroxide BP
GO:0042644 chloroplast nucleoid CC
GO:0042646 plastid nucleoid CC
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:0043621 protein self-association MF
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:0046677 response to antibiotic BP
GO:0050789 regulation of biological process BP
GO:0050794 regulation of cellular process BP
GO:0050896 response to stimulus BP
GO:0051171 regulation of nitrogen compound metabolic process BP
GO:0051252 regulation of RNA metabolic process BP
GO:0060255 regulation of macromolecule metabolic process BP
GO:0065007 biological regulation BP
GO:0071840 cellular component organization or biogenesis BP
GO:0080090 regulation of primary metabolic process BP
GO:0101031 chaperone complex CC
GO:1901700 response to oxygen-containing compound BP
GO:1903506 regulation of nucleic acid-templated transcription BP
GO:2000112 regulation of cellular macromolecule biosynthetic process BP
GO:2001141 regulation of RNA biosynthetic process 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.