Basic Information
Gene Structure
Domain
Regulation&
Interaction
Annotation
Orthologus Group
Expresssion
Pathway
Basic Information
Gene ID
Pop_G10G048233
View in Genome Browser
Position
chrG10:8197109-8203317 (-)
6208bp
Gene Type
gene
Gene Description (Protein Product)
Serine threonine-protein phosphatase 2A 65 kDa regulatory subunit A
Organism
Populus alba x Populus glandulosa
Also AS Potri.010G127500AT3G25800Potri.010G127500.v4.1

Gene Structure

upstream:
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Domain
Database EntryID E-Value Start end InterPro ID Description

Regulation&Interaction
Protein-protein interaction (PPI)
Pop_G16G068604 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
Pop_G15G048876 phosphatase 2A 55 kDa regulatory subunit B
Pop_UnG037338 serine threonine-protein phosphatase
Regulatory gene
Pop_A01G003954 Homeobox-leucine zipper protein
Pop_A01G004152 Homeobox-leucine zipper protein
Pop_A01G015498 Homeobox-leucine zipper 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
Go Pathway KEGG Pathway
GO Term Description GO Category
GO:0000159 protein phosphatase type 2A complex CC
GO:0001101 response to acid chemical BP
GO:0005575 cellular_component CC
GO:0005618 cell wall CC
GO:0005622 intracellular anatomical structure CC
GO:0005623 obsolete cell CC
GO:0005634 nucleus CC
GO:0005737 cytoplasm CC
GO:0005829 cytosol CC
GO:0005886 plasma membrane CC
GO:0006810 transport BP
GO:0007154 cell communication BP
GO:0007165 signal transduction BP
GO:0008150 biological_process BP
GO:0008287 protein serine/threonine phosphatase complex CC
GO:0009719 response to endogenous stimulus BP
GO:0009723 response to ethylene BP
GO:0009725 response to hormone BP
GO:0009737 response to abscisic acid BP
GO:0009738 abscisic acid-activated signaling pathway BP
GO:0009755 hormone-mediated signaling pathway BP
GO:0009787 regulation of abscisic acid-activated signaling pathway BP
GO:0009789 positive regulation of abscisic acid-activated signaling pathway BP
GO:0009914 hormone transport BP
GO:0009926 auxin polar transport BP
GO:0009966 regulation of signal transduction BP
GO:0009967 positive regulation of signal transduction BP
GO:0009987 cellular process BP
GO:0010033 response to organic substance BP
GO:0010035 response to inorganic substance BP
GO:0010038 response to metal ion BP
GO:0010119 regulation of stomatal movement BP
GO:0010646 regulation of cell communication BP
GO:0010647 positive regulation of cell communication BP
GO:0010817 regulation of hormone levels BP
GO:0016020 membrane CC
GO:0019220 regulation of phosphate metabolic process BP
GO:0019222 regulation of metabolic process BP
GO:0023051 regulation of signaling BP
GO:0023052 signaling BP
GO:0023056 positive regulation of signaling BP
GO:0030312 external encapsulating structure CC
GO:0031323 regulation of cellular metabolic process BP
GO:0031399 regulation of protein modification process BP
GO:0032268 regulation of protein metabolic process BP
GO:0032870 cellular response to hormone stimulus BP
GO:0032991 protein-containing complex CC
GO:0033993 response to lipid BP
GO:0035303 regulation of dephosphorylation BP
GO:0035304 regulation of protein dephosphorylation BP
GO:0042221 response to chemical BP
GO:0042325 regulation of phosphorylation BP
GO:0043226 organelle CC
GO:0043227 membrane-bounded organelle CC
GO:0043229 intracellular organelle CC
GO:0043231 intracellular membrane-bounded organelle CC
GO:0044424 obsolete intracellular part CC
GO:0044444 obsolete cytoplasmic part CC
GO:0044464 obsolete cell part CC
GO:0046686 response to cadmium ion BP
GO:0048518 positive regulation of biological process BP
GO:0048522 positive regulation of cellular process BP
GO:0048583 regulation of response to stimulus BP
GO:0048584 positive regulation of response to stimulus BP
GO:0050789 regulation of biological process BP
GO:0050794 regulation of cellular process BP
GO:0050896 response to stimulus BP
GO:0051171 regulation of nitrogen compound metabolic process BP
GO:0051174 regulation of phosphorus metabolic process BP
GO:0051179 localization BP
GO:0051234 establishment of localization BP
GO:0051246 regulation of protein metabolic process BP
GO:0051716 cellular response to stimulus BP
GO:0060255 regulation of macromolecule metabolic process BP
GO:0060918 auxin transport BP
GO:0065007 biological regulation BP
GO:0065008 regulation of biological quality BP
GO:0070887 cellular response to chemical stimulus BP
GO:0071215 cellular response to abscisic acid stimulus BP
GO:0071229 cellular response to acid chemical BP
GO:0071310 cellular response to organic substance BP
GO:0071396 cellular response to lipid BP
GO:0071495 cellular response to endogenous stimulus BP
GO:0071944 cell periphery CC
GO:0080090 regulation of primary metabolic process BP
GO:0097305 response to alcohol BP
GO:0097306 cellular response to alcohol BP
GO:1901419 regulation of response to alcohol BP
GO:1901421 positive regulation of response to alcohol BP
GO:1901700 response to oxygen-containing compound BP
GO:1901701 cellular response to oxygen-containing compound BP
GO:1902494 catalytic complex CC
GO:1903293 phosphatase complex CC
GO:1905957 regulation of cellular response to alcohol BP
GO:1905959 positive regulation of cellular response to alcohol BP
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.