Basic Information
Gene ID
geneMaker00024856
Position
GWHBGXC00000005:62120741-62158669 (+)
37928bp
Gene Type
gene
Gene Description (Protein Product)
serine threonine-protein kinase endoribonuclease
Organism
Also AS AT2G17520

Gene Structure

upstream:

Domain
Database EntryID E-Value Start end InterPro ID Description

Regulation&Interaction
Protein-protein interaction (PPI)
geneMaker00029041 E3 ubiquitin-protein ligase COP1
Regulatory gene
geneMaker00000164 MADS-box transcription factor
geneMaker00000173 MYB family transcription factor
geneMaker00000453 NAC domain-containing protein 21

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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:0001101 response to acid chemical BP
GO:0002376 immune system process BP
GO:0003674 molecular_function MF
GO:0003824 catalytic activity MF
GO:0004518 nuclease activity MF
GO:0004519 endonuclease activity MF
GO:0004521 RNA endonuclease activity MF
GO:0004540 ribonuclease activity MF
GO:0004672 protein kinase activity MF
GO:0004674 protein serine/threonine kinase activity 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:0005634 nucleus CC
GO:0005737 cytoplasm CC
GO:0005783 endoplasmic reticulum CC
GO:0005789 endoplasmic reticulum membrane CC
GO:0005975 carbohydrate metabolic process BP
GO:0006020 inositol metabolic process BP
GO:0006066 alcohol metabolic process BP
GO:0006139 nucleobase-containing compound metabolic process BP
GO:0006396 RNA processing BP
GO:0006464 protein modification process BP
GO:0006468 protein phosphorylation BP
GO:0006725 cellular aromatic compound metabolic process BP
GO:0006793 phosphorus metabolic process BP
GO:0006796 phosphate-containing compound metabolic process BP
GO:0006807 nitrogen compound metabolic process BP
GO:0006950 response to stress BP
GO:0006952 defense response BP
GO:0006955 immune response BP
GO:0006986 response to unfolded protein BP
GO:0007154 cell communication BP
GO:0007165 signal transduction BP
GO:0008104 protein localization BP
GO:0008150 biological_process BP
GO:0008152 metabolic process BP
GO:0008380 RNA splicing BP
GO:0009605 response to external stimulus BP
GO:0009607 response to biotic stimulus BP
GO:0009617 response to bacterium BP
GO:0009719 response to endogenous stimulus BP
GO:0009725 response to hormone BP
GO:0009751 response to salicylic acid BP
GO:0009814 defense response to other organism BP
GO:0009816 defense response to bacterium BP
GO:0009987 cellular process BP
GO:0010033 response to organic substance BP
GO:0010467 gene expression BP
GO:0012505 endomembrane system CC
GO:0014070 response to organic cyclic compound BP
GO:0016020 membrane CC
GO:0016021 membrane CC
GO:0016043 cellular component organization BP
GO:0016070 RNA metabolic process BP
GO:0016301 kinase activity MF
GO:0016310 phosphorylation BP
GO:0016740 transferase activity MF
GO:0016772 transferase activity, transferring phosphorus-containing groups MF
GO:0016773 phosphotransferase activity, alcohol group as acceptor MF
GO:0016787 hydrolase activity MF
GO:0016788 hydrolase activity, acting on ester bonds MF
GO:0019538 protein metabolic process BP
GO:0019751 polyol metabolic process BP
GO:0019898 extrinsic component of membrane CC
GO:0022607 cellular component assembly BP
GO:0023052 signaling BP
GO:0030176 obsolete integral component of endoplasmic reticulum membrane CC
GO:0030968 endoplasmic reticulum unfolded protein response BP
GO:0031090 organelle membrane CC
GO:0031224 obsolete intrinsic component of membrane CC
GO:0031227 obsolete intrinsic component of endoplasmic reticulum membrane CC
GO:0031312 extrinsic component of organelle membrane CC
GO:0031505 fungal-type cell wall organization BP
GO:0031984 organelle subcompartment CC
GO:0033036 macromolecule localization BP
GO:0033365 protein localization to organelle BP
GO:0033554 cellular response to stress BP
GO:0034067 protein localization to Golgi apparatus BP
GO:0034613 protein localization BP
GO:0034620 cellular response to unfolded protein BP
GO:0034641 cellular nitrogen compound metabolic process BP
GO:0034976 response to endoplasmic reticulum stress BP
GO:0035966 response to topologically incorrect protein BP
GO:0035967 cellular response to topologically incorrect protein BP
GO:0036211 protein modification process BP
GO:0036290 protein trans-autophosphorylation BP
GO:0042175 nuclear outer membrane-endoplasmic reticulum membrane network CC
GO:0042221 response to chemical BP
GO:0042406 extrinsic component of endoplasmic reticulum membrane CC
GO:0042493 response to xenobiotic stimulus BP
GO:0042742 defense response to bacterium BP
GO:0042802 identical protein binding MF
GO:0042803 protein homodimerization activity MF
GO:0043170 macromolecule metabolic process BP
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:0043412 macromolecule modification BP
GO:0043933 protein-containing complex organization BP
GO:0044085 cellular component biogenesis BP
GO:0044237 cellular metabolic process BP
GO:0044238 primary metabolic process BP
GO:0044260 cellular macromolecule metabolic process BP
GO:0044262 cellular carbohydrate metabolic process BP
GO:0044267 protein metabolic process BP
GO:0044281 small molecule metabolic process BP
GO:0044422 obsolete organelle part CC
GO:0044424 obsolete intracellular part CC
GO:0044425 obsolete membrane part CC
GO:0044432 obsolete endoplasmic reticulum part CC
GO:0044444 obsolete cytoplasmic part CC
GO:0044446 obsolete intracellular organelle part CC
GO:0044464 obsolete cell part CC
GO:0045087 innate immune response BP
GO:0045229 external encapsulating structure organization BP
GO:0046483 heterocycle metabolic process BP
GO:0046677 response to antibiotic BP
GO:0046777 protein autophosphorylation BP
GO:0046983 protein dimerization activity 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:0051179 localization BP
GO:0051259 protein complex oligomerization BP
GO:0051260 protein homooligomerization BP
GO:0051641 cellular localization BP
GO:0051704 obsolete multi-organism process BP
GO:0051707 response to other organism BP
GO:0051716 cellular response to stimulus BP
GO:0065003 protein-containing complex assembly BP
GO:0065007 biological regulation BP
GO:0070727 cellular macromolecule localization BP
GO:0070887 cellular response to chemical stimulus BP
GO:0071310 cellular response to organic substance BP
GO:0071554 cell wall organization or biogenesis BP
GO:0071555 cell wall organization BP
GO:0071704 organic substance metabolic process BP
GO:0071840 cellular component organization or biogenesis BP
GO:0071852 fungal-type cell wall organization or biogenesis BP
GO:0090304 nucleic acid metabolic process BP
GO:0090305 nucleic acid phosphodiester bond hydrolysis BP
GO:0090501 RNA phosphodiester bond hydrolysis BP
GO:0090502 RNA phosphodiester bond hydrolysis, endonucleolytic BP
GO:0098542 defense response to other organism BP
GO:0098827 endoplasmic reticulum subcompartment CC
GO:0140096 catalytic activity, acting on a protein MF
GO:0140098 catalytic activity, acting on RNA MF
GO:1901360 organic cyclic compound metabolic process BP
GO:1901564 organonitrogen compound metabolic process BP
GO:1901615 organic hydroxy compound metabolic process BP
GO:1901700 response to oxygen-containing 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.