Basic Information
Gene Structure
Domain
Regulation&
Interaction
Annotation
Orthologus Group
Expresssion
Pathway
Basic Information
Gene ID
CSS0049484.g
View in Genome Browser
Position
Chr3:30594324-30599532 (-)
5208bp
Gene Type
gene
Gene Description (Protein Product)
Belongs to the heat shock protein 70 family
Organism
Camellia sinensis
Also AS AT5G09590

Gene Structure

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

Regulation&Interaction
Protein-protein interaction (PPI)
CSS0049799.g Belongs to the universal ribosomal protein uL14 family
CSS0050274.g Belongs to the glyceraldehyde-3-phosphate dehydrogenase family
CSS0049596.g Ubiquitin-40S ribosomal protein
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:0000166 nucleotide binding MF
GO:0000988 obsolete transcription factor activity, protein binding MF
GO:0000989 obsolete transcription factor activity, transcription factor binding MF
GO:0003674 molecular_function MF
GO:0003824 catalytic activity MF
GO:0005488 binding MF
GO:0005515 protein binding MF
GO:0005524 ATP binding MF
GO:0005575 cellular_component CC
GO:0005622 intracellular anatomical structure CC
GO:0005623 obsolete cell CC
GO:0005737 cytoplasm CC
GO:0005739 mitochondrion CC
GO:0005829 cytosol CC
GO:0006457 protein folding BP
GO:0006458 'de novo' protein folding BP
GO:0006950 response to stress BP
GO:0006986 response to unfolded protein BP
GO:0008144 obsolete drug binding MF
GO:0008150 biological_process BP
GO:0008270 zinc ion binding MF
GO:0009266 response to temperature stimulus BP
GO:0009408 response to heat BP
GO:0009628 response to abiotic stimulus BP
GO:0009889 regulation of biosynthetic process BP
GO:0009987 cellular process BP
GO:0010033 response to organic substance BP
GO:0010556 regulation of macromolecule biosynthetic process BP
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:0016989 sigma factor antagonist activity MF
GO:0017076 purine nucleotide binding MF
GO:0017111 ribonucleoside triphosphate phosphatase activity MF
GO:0019219 regulation of nucleobase-containing compound metabolic process BP
GO:0019222 regulation of metabolic process BP
GO:0022607 cellular component assembly BP
GO:0030554 adenyl nucleotide binding MF
GO:0031323 regulation of cellular metabolic process BP
GO:0031326 regulation of cellular biosynthetic process BP
GO:0032553 ribonucleotide binding MF
GO:0032555 purine ribonucleotide binding MF
GO:0032559 adenyl ribonucleotide binding MF
GO:0032991 protein-containing complex CC
GO:0033554 cellular response to stress BP
GO:0034620 cellular response to unfolded protein BP
GO:0035639 purine ribonucleoside triphosphate binding MF
GO:0035966 response to topologically incorrect protein BP
GO:0035967 cellular response to topologically incorrect protein BP
GO:0036094 small molecule binding MF
GO:0042221 response to chemical BP
GO:0043167 ion binding MF
GO:0043168 anion binding MF
GO:0043169 cation binding MF
GO:0043226 organelle CC
GO:0043227 membrane-bounded organelle CC
GO:0043229 intracellular organelle CC
GO:0043231 intracellular membrane-bounded organelle CC
GO:0043531 ADP binding MF
GO:0043933 protein-containing complex organization BP
GO:0044085 cellular component biogenesis BP
GO:0044183 protein folding chaperone MF
GO:0044424 obsolete intracellular part CC
GO:0044444 obsolete cytoplasmic part CC
GO:0044464 obsolete cell part CC
GO:0046872 metal ion binding MF
GO:0046914 transition metal ion binding MF
GO:0050789 regulation of biological process BP
GO:0050794 regulation of cellular process BP
GO:0050896 response to stimulus BP
GO:0051082 unfolded protein binding MF
GO:0051084 'de novo' post-translational protein folding BP
GO:0051085 chaperone cofactor-dependent protein refolding BP
GO:0051087 chaperone binding MF
GO:0051171 regulation of nitrogen compound metabolic process BP
GO:0051252 regulation of RNA metabolic process BP
GO:0051716 cellular response to stimulus BP
GO:0060255 regulation of macromolecule metabolic process BP
GO:0061077 chaperone-mediated protein folding BP
GO:0065003 protein-containing complex assembly BP
GO:0065007 biological regulation BP
GO:0070887 cellular response to chemical stimulus BP
GO:0071310 cellular response to organic substance BP
GO:0071840 cellular component organization or biogenesis BP
GO:0080090 regulation of primary metabolic process BP
GO:0097159 organic cyclic compound binding MF
GO:0097367 carbohydrate derivative binding MF
GO:0140110 transcription regulator activity MF
GO:1901265 nucleoside phosphate binding MF
GO:1901363 heterocyclic compound binding MF
GO:1903506 regulation of nucleic acid-templated transcription BP
GO:2001141 regulation of RNA biosynthetic process BP
KEGG Term Name Description
map03018 RNA degradation The correct processing, quality control and turnover of cellular RNA molecules are critical to many aspects in the expression of genetic information. In eukaryotes, two major pathways of mRNA decay exist and both pathways are initiated by poly(A) shortening of the mRNA. In the 5' to 3' pathway, this is followed by decapping which then permits the 5' to 3' exonucleolytic degradation of transcripts. In the 3' to 5' pathway, the exosome, a large multisubunit complex, plays a key role. The exosome exists in archaeal cells, too. In bacteria, endoribonuclease E, a key enzyme involved in RNA decay and processing, organizes a protein complex called degradosome. RNase E or R interacts with the phosphate-dependent exoribonuclease polynucleotide phosphorylase, DEAD-box helicases, and additional factors in the RNA-degrading complex.