Basic Information
Gene Structure
Domain
Regulation&
Interaction
Annotation
Orthologus Group
Pathway
Basic Information
Gene ID
evm.TU.Chr13.2412
View in Genome Browser
Position
Chr13:44292559-44302338 (-)
9779bp
Gene Type
gene
Gene Description (Protein Product)
Sec12-like protein 1
Organism
Diospyros oleifera Cheng
Also AS AT3G52190

Gene Structure

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Domain
Database EntryID E-Value Start end InterPro ID Description

Regulation&Interaction
Protein-protein interaction (PPI)
evm.TU.Chr6.745 -
evm.TU.Chr6.745 Sec12-like protein 2
evm.TU.Chr9.2310 May be involved in the degradation of misfolded endoplasmic reticulum (ER) luminal proteins
Regulatory gene
evm.TU.Chr12.68 Protein BASIC PENTACYSTEINE2-like
evm.TU.Chr14.1632 Protein BASIC PENTACYSTEINE4-like
evm.TU.Chr4.807 Glutamate-gated receptor that probably acts as non- selective cation channel

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Annotation

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


Pathway
Go Pathway KEGG Pathway
GO Term Description GO Category
GO:0002790 peptide secretion BP
GO:0003400 regulation of COPII vesicle coating BP
GO:0003674 molecular_function MF
GO:0005085 guanyl-nucleotide exchange factor activity MF
GO:0005090 guanyl-nucleotide exchange factor activity MF
GO:0005096 GTPase activator 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:0005886 plasma membrane CC
GO:0006810 transport BP
GO:0006811 monoatomic ion transport BP
GO:0006817 phosphate ion transport BP
GO:0006820 monoatomic anion transport BP
GO:0006888 endoplasmic reticulum to Golgi vesicle-mediated transport BP
GO:0006950 response to stress BP
GO:0007154 cell communication BP
GO:0008047 enzyme activator activity MF
GO:0008104 protein localization BP
GO:0008150 biological_process BP
GO:0009267 cellular response to starvation BP
GO:0009306 protein secretion BP
GO:0009605 response to external stimulus BP
GO:0009987 cellular process BP
GO:0009991 response to extracellular stimulus BP
GO:0012505 endomembrane system CC
GO:0015031 protein transport BP
GO:0015698 inorganic anion transport BP
GO:0015833 peptide transport BP
GO:0016020 membrane CC
GO:0016021 membrane CC
GO:0016036 cellular response to phosphate starvation BP
GO:0016192 vesicle-mediated transport BP
GO:0019899 enzyme binding MF
GO:0030176 obsolete integral component of endoplasmic reticulum membrane CC
GO:0030234 enzyme regulator activity MF
GO:0030695 GTPase regulator activity MF
GO:0031224 obsolete intrinsic component of membrane CC
GO:0031227 obsolete intrinsic component of endoplasmic reticulum membrane CC
GO:0031667 response to nutrient levels BP
GO:0031668 cellular response to extracellular stimulus BP
GO:0031669 cellular response to nutrient levels BP
GO:0031984 organelle subcompartment CC
GO:0032386 regulation of intracellular transport BP
GO:0032879 regulation of localization BP
GO:0032940 secretion by cell BP
GO:0033036 macromolecule localization BP
GO:0033043 regulation of organelle organization BP
GO:0033554 cellular response to stress BP
GO:0042175 nuclear outer membrane-endoplasmic reticulum membrane network CC
GO:0042594 response to starvation BP
GO:0042886 amide transport BP
GO:0043085 positive regulation of catalytic activity BP
GO:0043087 regulation of GTPase activity BP
GO:0043226 organelle CC
GO:0043227 membrane-bounded organelle CC
GO:0043229 intracellular organelle CC
GO:0043231 intracellular membrane-bounded organelle CC
GO:0043254 regulation of protein-containing complex assembly BP
GO:0043547 positive regulation of GTPase activity BP
GO:0044087 regulation of cellular component biogenesis BP
GO:0044093 positive regulation of molecular function 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:0045184 establishment of protein localization BP
GO:0046903 secretion BP
GO:0046907 intracellular transport BP
GO:0048193 Golgi vesicle transport BP
GO:0048209 regulation of vesicle targeting, to, from or within Golgi BP
GO:0050789 regulation of biological process BP
GO:0050790 regulation of catalytic activity BP
GO:0050794 regulation of cellular process BP
GO:0050896 response to stimulus BP
GO:0051020 GTPase binding MF
GO:0051049 regulation of transport BP
GO:0051128 regulation of cellular component organization BP
GO:0051179 localization BP
GO:0051234 establishment of localization BP
GO:0051336 regulation of hydrolase activity BP
GO:0051345 positive regulation of hydrolase activity BP
GO:0051641 cellular localization BP
GO:0051649 establishment of localization in cell BP
GO:0051716 cellular response to stimulus BP
GO:0060341 regulation of cellular localization BP
GO:0060589 nucleoside-triphosphatase regulator activity MF
GO:0060627 regulation of vesicle-mediated transport BP
GO:0060628 regulation of ER to Golgi vesicle-mediated transport BP
GO:0065007 biological regulation BP
GO:0065009 regulation of molecular function BP
GO:0071496 cellular response to external stimulus BP
GO:0071702 organic substance transport BP
GO:0071705 nitrogen compound transport BP
GO:0071944 cell periphery CC
GO:0090113 obsolete regulation of ER to Golgi vesicle-mediated transport by GTP hydrolysis BP
GO:0098772 molecular function regulator activity MF
GO:0098827 endoplasmic reticulum subcompartment CC
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.