Basic Information
Gene ID
Juni_Chr7.3574.g
Position
Chr7:49354215-49358663 (-)
4448bp
Gene Type
gene
Gene Description (Protein Product)
Eukaryotic translation initiation factor 2
Organism
Also AS AT2G40290

Gene Structure

upstream:

Domain
Database EntryID E-Value Start end InterPro ID Description

Regulation&Interaction
Protein-protein interaction (PPI)
Juni_Chr8.48.g Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome
Juni_Chr9.817.g Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis of a specialized repertoire of mRNAs and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation
Juni_Chr8.706.g Endoplasmin homolog

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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:0000075 cell cycle checkpoint signaling BP
GO:0000077 DNA damage checkpoint signaling BP
GO:0000278 mitotic cell cycle BP
GO:0002181 cytoplasmic translation BP
GO:0002183 cytoplasmic translational initiation BP
GO:0003674 molecular_function MF
GO:0003676 nucleic acid binding MF
GO:0003723 RNA binding MF
GO:0003729 mRNA binding MF
GO:0003743 translation initiation factor activity MF
GO:0005488 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:0005829 cytosol CC
GO:0005840 ribosome CC
GO:0005850 eukaryotic translation initiation factor 2 complex CC
GO:0005851 eukaryotic translation initiation factor 2B complex CC
GO:0006412 translation BP
GO:0006413 translational initiation BP
GO:0006518 peptide metabolic process BP
GO:0006807 nitrogen compound metabolic process BP
GO:0006950 response to stress BP
GO:0006974 cellular response to DNA damage stimulus BP
GO:0007049 cell cycle BP
GO:0007093 mitotic cell cycle checkpoint signaling BP
GO:0007346 regulation of mitotic cell cycle BP
GO:0008135 translation factor activity, RNA binding MF
GO:0008150 biological_process BP
GO:0008152 metabolic process BP
GO:0009058 biosynthetic process BP
GO:0009059 macromolecule biosynthetic process BP
GO:0009987 cellular process BP
GO:0010467 gene expression BP
GO:0010564 regulation of cell cycle process BP
GO:0010948 negative regulation of cell cycle process BP
GO:0019538 protein metabolic process BP
GO:0022402 cell cycle process BP
GO:0031570 DNA integrity checkpoint signaling BP
GO:0031571 mitotic G1 DNA damage checkpoint signaling BP
GO:0032991 protein-containing complex CC
GO:0033290 eukaryotic 48S preinitiation complex CC
GO:0033554 cellular response to stress BP
GO:0034641 cellular nitrogen compound metabolic process BP
GO:0034645 cellular macromolecule biosynthetic process BP
GO:0043021 ribonucleoprotein complex binding MF
GO:0043022 ribosome binding MF
GO:0043043 peptide biosynthetic process BP
GO:0043170 macromolecule metabolic process BP
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:0043603 amide metabolic process BP
GO:0043604 amide biosynthetic process BP
GO:0043614 multi-eIF complex CC
GO:0044237 cellular metabolic process BP
GO:0044238 primary metabolic process BP
GO:0044249 cellular biosynthetic process BP
GO:0044260 cellular macromolecule metabolic process BP
GO:0044267 protein metabolic process BP
GO:0044271 cellular nitrogen compound biosynthetic process BP
GO:0044424 obsolete intracellular part CC
GO:0044444 obsolete cytoplasmic part CC
GO:0044464 obsolete cell part CC
GO:0044773 mitotic DNA damage checkpoint signaling BP
GO:0044774 mitotic DNA integrity checkpoint signaling BP
GO:0044783 mitotic G1 DNA damage checkpoint signaling BP
GO:0044819 mitotic G1/S transition checkpoint signaling BP
GO:0044877 protein-containing complex binding MF
GO:0045786 negative regulation of cell cycle BP
GO:0045930 negative regulation of mitotic cell cycle BP
GO:0048519 negative regulation of biological process BP
GO:0048523 negative regulation of cellular process BP
GO:0050789 regulation of biological process BP
GO:0050794 regulation of cellular process BP
GO:0050896 response to stimulus BP
GO:0051716 cellular response to stimulus BP
GO:0051726 regulation of cell cycle BP
GO:0065007 biological regulation BP
GO:0070993 translation preinitiation complex CC
GO:0071704 organic substance metabolic process BP
GO:0097159 organic cyclic compound binding MF
GO:1901363 heterocyclic compound binding MF
GO:1901564 organonitrogen compound metabolic process BP
GO:1901566 organonitrogen compound biosynthetic process BP
GO:1901576 organic substance biosynthetic process BP
GO:1901987 regulation of cell cycle phase transition BP
GO:1901988 negative regulation of cell cycle phase transition BP
GO:1901990 regulation of mitotic cell cycle phase transition BP
GO:1901991 negative regulation of mitotic cell cycle phase transition BP
GO:1902806 regulation of cell cycle G1/S phase transition BP
GO:1902807 negative regulation of cell cycle G1/S phase transition BP
GO:1903047 mitotic cell cycle process BP
GO:1990904 ribonucleoprotein complex CC
GO:2000045 regulation of G1/S transition of mitotic cell cycle BP
GO:2000134 negative regulation of G1/S transition of mitotic cell cycle 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.