Basic Information
Gene Structure
Domain
Regulation&
Interaction
Annotation
Orthologus Group
Pathway
Basic Information
Gene ID
Potra2n9c18983
View in Genome Browser
Position
chr9:2473029-2477756 (-)
4727bp
Gene Type
gene
Gene Description (Protein Product)
Translocon-associated protein subunit
Organism
Populus tremula
Also AS Potri.009G129800AT2G21160Potri.009G129800.v4.1

Gene Structure

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Domain
Database EntryID E-Value Start end InterPro ID Description

Regulation&Interaction
Protein-protein interaction (PPI)
Potra2n9c20010 Sec61beta family
Potra2n9c19137 Phospholipase A-2-activating
Potra2n9c19130 Essential subunit of the N-oligosaccharyl transferase (OST) complex which catalyzes the transfer of a high mannose oligosaccharide from a lipid-linked oligosaccharide donor to an asparagine residue within an Asn-X-Ser Thr consensus motif in nascent polypeptide chains

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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:0005575 cellular_component CC
GO:0005622 intracellular anatomical structure CC
GO:0005623 obsolete cell CC
GO:0005737 cytoplasm CC
GO:0005773 vacuole CC
GO:0005774 vacuolar membrane CC
GO:0005783 endoplasmic reticulum CC
GO:0005789 endoplasmic reticulum membrane CC
GO:0005794 Golgi apparatus CC
GO:0005886 plasma membrane CC
GO:0006605 protein targeting BP
GO:0006612 protein targeting to membrane BP
GO:0006613 cotranslational protein targeting to membrane BP
GO:0006810 transport BP
GO:0006886 intracellular protein transport BP
GO:0008104 protein localization BP
GO:0008150 biological_process BP
GO:0009507 chloroplast CC
GO:0009534 chloroplast thylakoid CC
GO:0009535 chloroplast thylakoid membrane CC
GO:0009536 plastid CC
GO:0009579 thylakoid CC
GO:0012505 endomembrane system CC
GO:0015031 protein transport BP
GO:0015833 peptide transport BP
GO:0016020 membrane CC
GO:0031090 organelle membrane CC
GO:0031976 plastid thylakoid CC
GO:0031984 organelle subcompartment CC
GO:0033036 macromolecule localization BP
GO:0034357 photosynthetic membrane CC
GO:0034613 protein localization BP
GO:0042175 nuclear outer membrane-endoplasmic reticulum membrane network CC
GO:0042651 thylakoid membrane CC
GO:0042886 amide transport BP
GO:0043226 organelle CC
GO:0043227 membrane-bounded organelle CC
GO:0043229 intracellular organelle CC
GO:0043231 intracellular membrane-bounded organelle CC
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:0044434 obsolete chloroplast part CC
GO:0044435 obsolete plastid part CC
GO:0044436 obsolete thylakoid part CC
GO:0044437 obsolete vacuolar 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:0051179 localization BP
GO:0051234 establishment of localization BP
GO:0051641 cellular localization BP
GO:0051649 establishment of localization in cell BP
GO:0055035 plastid thylakoid membrane CC
GO:0070727 cellular macromolecule localization BP
GO:0071702 organic substance transport BP
GO:0071705 nitrogen compound transport BP
GO:0071944 cell periphery CC
GO:0072657 protein localization to membrane BP
GO:0090150 establishment of protein localization to membrane BP
GO:0098588 bounding membrane of organelle CC
GO:0098805 membrane CC
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.