Basic Information
Gene ID
AmTr_scaff00048.40.v1.0.g
Position
AmTr_scaff00048:933240-948890 (-)
15650bp
Gene Type
gene
Gene Description (Protein Product)
Serine threonine-protein phosphatase 2A 65 kDa regulatory subunit A
Organism
Also AS AT3G25800AMTR_s00048p00082810

Gene Structure

upstream:

Domain
Database EntryID E-Value Start end InterPro ID Description

Regulation&Interaction
Protein-protein interaction (PPI)
AmTr_scaff00171.40.v1.0.g serine threonine-protein phosphatase
AmTr_scaff00123.4.v1.0.g The B regulatory subunit might modulate substrate selectivity and catalytic activity, and also might direct the localization of the catalytic enzyme to a particular subcellular compartment
AmTr_scaff00049.40.v1.0.g The B regulatory subunit might modulate substrate selectivity and catalytic activity, and also might direct the localization of the catalytic enzyme to a particular subcellular compartment
Regulatory gene
AmTr_scaff00006.175.v1.0.g bpc6, bbr bpc6, atbpc6 atbpc6
AmTr_scaff00024.47.v1.0.g Protein BASIC PENTACYSTEINE2-like
AmTr_scaff00185.21.v1.0.g Protein BASIC PENTACYSTEINE6-like

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Annotation

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


Pathway
KEGG Term Name Description
map03015 mRNA surveillance pathway The mRNA surveillance pathway is a quality control mechanism that detects and degrades abnormal mRNAs. These pathways include nonsense-mediated mRNA decay (NMD), nonstop mRNA decay (NSD), and no-go decay (NGD). NMD is a mechanism that eliminates mRNAs containing premature translation-termination codons (PTCs). In vertebrates, PTCs trigger efficient NMD when located upstream of an exon junction complex (EJC). Upf3, together with Upf1 and Upf2, may signal the presence of the PTC to the 5'end of the transcript, resulting in decapping and rapid exonucleolytic digestion of the mRNA. In the NSD pathway, which targets mRNAs lacking termination codons, the ribosome is believed to translate through the 3' untranslated region and stall at the end of the poly(A) tail. NSD involves an eRF3-like protein, Ski7p, which is hypothesized to bind the empty A site of the ribosome and recruit the exosome to degrade the mRNA from the 3' end. NGD targets mRNAs with stalls in translation elongation for endonucleolytic cleavage in a process involving the Dom34 and Hbs1 proteins.