Basic Information
Gene ID
Position
chr3:16470567-16481052 (+)
10485bp
Gene Type
gene
Gene Description (Protein Product)
phosphatase 2A 55 kDa regulatory subunit B
Organism
Also AS Potri.003G034300AT1G17720Potri.003G034300.v4.1

Gene Structure

upstream:

Domain
Database EntryID E-Value Start end InterPro ID Description

Regulation&Interaction
Protein-protein interaction (PPI)
Potra2n6c14242 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
Potra2n8c18389 serine threonine-protein phosphatase
Potra2n6c13619 serine threonine-protein phosphatase
Regulatory gene
Potra2n10c20596 Dof zinc finger protein
Potra2n10c20949 Cyclic dof factor
Potra2n11c23230 Dof zinc finger protein

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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.