Basic Information
Gene ID
gene-LOC103941172
Position
NW_025999690.1:4198501-4203434 (-)
4933bp
Gene Type
gene
Gene Description (Protein Product)
PWI domain
Organism
Also AS MD17G1145400AT2G24350

Gene Structure

upstream:

Domain
Database EntryID E-Value Start end InterPro ID Description

Regulation&Interaction
Protein-protein interaction (PPI)
gene-LOC125469796 DEAD-box ATP-dependent RNA helicase
gene-LOC103965576 DEAD-box ATP-dependent RNA helicase
gene-LOC103946692 DEAD-box ATP-dependent RNA helicase
Regulatory gene
gene-LOC103926531 zinc finger CCCH domain-containing protein
gene-LOC103926579 transcription factor
gene-LOC103926580 Developmental protein SEPALLATA

Load All Networks

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.