Basic Information
Gene ID
FRAEX38873_v2_000251870
Position
Contig4811:5612-10678 (+)
5066bp
Gene Type
gene
Gene Description (Protein Product)
Serine threonine-protein phosphatase 2A 65 kDa regulatory subunit A beta isoform
Organism
Also AS AT1G13320

Gene Structure

upstream:

Domain
Database EntryID E-Value Start end InterPro ID Description

Regulation&Interaction
Protein-protein interaction (PPI)
FRAEX38873_v2_000322630 belongs to the protein kinase superfamily
FRAEX38873_v2_000281620 E3 ubiquitin-protein ligase CHIP-like
FRAEX38873_v2_000340790 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
FRAEX38873_v2_000001740 (NAC) domain-containing protein
FRAEX38873_v2_000001820 HD-ZIP protein N terminus
FRAEX38873_v2_000004990 Mini zinc finger protein

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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
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.