Basic Information
Gene ID
gene-DKX38_029792
Position
CM018590.1:16828319-16830208 (+)
1889bp
Gene Type
gene
Gene Description (Protein Product)
E3 ubiquitin-protein ligase
Organism
Also AS AT4G03510

Gene Structure

upstream:

Domain
Database EntryID E-Value Start end InterPro ID Description

Regulation&Interaction
Protein-protein interaction (PPI)
gene-DKX38_029951 Belongs to the ubiquitin-conjugating enzyme family

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Annotation

Orthologous Group
Orthologous ID Species Number All hits in PereRegDB Hits of this species Orthologous Detail


Pathway
GO Term Description GO Category
GO:0001101 response to acid chemical BP
GO:0003674 molecular_function MF
GO:0003824 catalytic activity MF
GO:0004842 ubiquitin-protein transferase 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:0005737 cytoplasm CC
GO:0005783 endoplasmic reticulum CC
GO:0005789 endoplasmic reticulum membrane CC
GO:0006464 protein modification process BP
GO:0006508 proteolysis BP
GO:0006511 ubiquitin-dependent protein catabolic process BP
GO:0006515 protein quality control for misfolded or incompletely synthesized proteins BP
GO:0006807 nitrogen compound metabolic process BP
GO:0006810 transport BP
GO:0006886 intracellular protein transport BP
GO:0006950 response to stress BP
GO:0006970 response to osmotic stress BP
GO:0008104 protein localization BP
GO:0008150 biological_process BP
GO:0008152 metabolic process BP
GO:0009056 catabolic process BP
GO:0009057 macromolecule catabolic process BP
GO:0009266 response to temperature stimulus BP
GO:0009409 response to cold BP
GO:0009414 response to water deprivation BP
GO:0009415 response to water BP
GO:0009611 response to wounding BP
GO:0009628 response to abiotic stimulus BP
GO:0009719 response to endogenous stimulus BP
GO:0009723 response to ethylene BP
GO:0009725 response to hormone BP
GO:0009987 cellular process BP
GO:0010033 response to organic substance BP
GO:0010035 response to inorganic substance BP
GO:0010243 response to organonitrogen compound BP
GO:0010498 proteasomal protein catabolic process BP
GO:0012505 endomembrane system CC
GO:0015031 protein transport BP
GO:0015833 peptide transport BP
GO:0016020 membrane CC
GO:0016567 protein ubiquitination BP
GO:0016740 transferase activity MF
GO:0019538 protein metabolic process BP
GO:0019787 ubiquitin-like protein transferase activity MF
GO:0019899 enzyme binding MF
GO:0019941 modification-dependent protein catabolic process BP
GO:0030163 protein catabolic process BP
GO:0031984 organelle subcompartment CC
GO:0032446 protein modification by small protein conjugation BP
GO:0032527 protein exit from endoplasmic reticulum BP
GO:0032991 protein-containing complex CC
GO:0033036 macromolecule localization BP
GO:0033554 cellular response to stress BP
GO:0034613 protein localization 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:0036503 ERAD pathway BP
GO:0036513 Derlin-1 retrotranslocation complex CC
GO:0042175 nuclear outer membrane-endoplasmic reticulum membrane network CC
GO:0042221 response to chemical BP
GO:0042886 amide transport 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:0043229 intracellular organelle CC
GO:0043231 intracellular membrane-bounded organelle CC
GO:0043412 macromolecule modification BP
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:0044390 ubiquitin-like protein conjugating enzyme binding MF
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:0045184 establishment of protein localization BP
GO:0046907 intracellular transport BP
GO:0050896 response to stimulus BP
GO:0051179 localization BP
GO:0051234 establishment of localization BP
GO:0051603 proteolysis involved in protein catabolic process BP
GO:0051641 cellular localization BP
GO:0051649 establishment of localization in cell BP
GO:0051716 cellular response to stimulus BP
GO:0051788 response to misfolded protein BP
GO:0070647 protein modification by small protein conjugation or removal BP
GO:0070727 cellular macromolecule localization BP
GO:0070887 cellular response to chemical stimulus BP
GO:0071218 cellular response to misfolded protein BP
GO:0071310 cellular response to organic substance BP
GO:0071702 organic substance transport BP
GO:0071704 organic substance metabolic process BP
GO:0071705 nitrogen compound transport BP
GO:0071712 ER-associated misfolded protein catabolic process BP
GO:0098796 membrane protein complex CC
GO:0098827 endoplasmic reticulum subcompartment CC
GO:0140096 catalytic activity, acting on a protein MF
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
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.