Basic Information
Gene ID
Potrx009412g00010
Position
Potrx009412:6944-9053 (-)
2109bp
Gene Type
gene
Gene Description (Protein Product)
serine threonine-protein phosphatase
Organism
Also AS Potri.015G068300AT1G10430Potri.015G068300.v4.1

Gene Structure

upstream:

Domain
Database EntryID E-Value Start end InterPro ID Description

Regulation&Interaction
Protein-protein interaction (PPI)
Potrx065361g00020 serine threonine-protein phosphatase
Potrx032947g00010 Serine threonine-protein phosphatase 2A 65 kDa regulatory subunit A
Potrx058237g00010 Serine threonine-protein phosphatase 2A 65 kDa regulatory subunit A
Regulatory gene
Potrx000515g00010 Myb-like DNA-binding domain
Potrx000925g00010 Dof zinc finger protein
Potrx001114g00010 MYB-CC type transfactor, LHEQLE motif

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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.