Basic Information
Gene ID
Pop_G16G035754
Position
chrG16:117624-119081 (-)
1457bp
Gene Type
gene
Gene Description (Protein Product)
Serine threonine-protein phosphatase
Organism
Also AS Potri.016G142700AT2G39840Potri.016G142700.v4.1

Gene Structure

upstream:

Domain
Database EntryID E-Value Start end InterPro ID Description

Regulation&Interaction
Protein-protein interaction (PPI)
Pop_G17G066965 Cleavage and polyadenylation specificity factor subunit
Pop_G17G027387 WD repeat-containing protein
Pop_UnG069992 Cleavage and polyadenylation specificity factor
Regulatory gene
Pop_A01G004199 GAGA binding protein-like family
Pop_A02G005181 Protein BASIC PENTACYSTEINE6-like
Pop_A04G028302 Protein BASIC PENTACYSTEINE4-like

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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.