Relation Results

Summary

Name TENT2
Full Name Poly
Synonyms hGLD-2, PAP-associated domain-containing protein 4, Terminal nucleotidyltransferase 2, Terminal uridylyltransferase 2, TUTase 2 | GLD2, PAPD4
Primary ID Q6PIY7
Links - -
Type protein
Relations 5
Function Cytoplasmic poly(A) RNA polymerase that adds successive AMP monomers to the 3'-end of specific RNAs, forming a poly(A) tail. In contrast to the canoni ...
View More

Viewer

Type: Score: Layout: SPV 
0.20.20.20.20.2PRKACGTENT2PRKACBAKT1PRKACAPKA

Search Tools

Refine search:

  • by mechanism


  • by effect
  • by organism:


  • by tissue:


  • by cell-line

▶Modifications Tables

Relations
Regulator
Mechanism
target
score ℹ
+ PRKACGdown-regulates activity img/direct_inhibition.png phosphorylation TENT2 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-259404 Ser116 LSGERRYsMPPLFHT Homo sapiens HEK-293 Cell
pmid sentence
We found that Gld2 activity is regulated by site-specific phosphorylation in its disordered N-terminal domain. We identified two phosphorylation sites (S62, S110) where phosphomimetic substitutions increased Gld2 activity and one site (S116) that markedly reduced activity. Using mass spectrometry, we confirmed that HEK 293 cells readily phosphorylate the N-terminus of Gld2. We identified protein kinase A (PKA) and protein kinase B (Akt1) as the kinases that site-specifically phosphorylate Gld2 at S116, abolishing Gld2-mediated nucleotide addition.
Publications: 1 Organism: Homo Sapiens
+ PRKACBdown-regulates activity img/direct_inhibition.png phosphorylation TENT2 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-259403 Ser116 LSGERRYsMPPLFHT Homo sapiens
pmid sentence
We found that Gld2 activity is regulated by site-specific phosphorylation in its disordered N-terminal domain. We identified two phosphorylation sites (S62, S110) where phosphomimetic substitutions increased Gld2 activity and one site (S116) that markedly reduced activity. Using mass spectrometry, we confirmed that HEK 293 cells readily phosphorylate the N-terminus of Gld2. We identified protein kinase A (PKA) and protein kinase B (Akt1) as the kinases that site-specifically phosphorylate Gld2 at S116, abolishing Gld2-mediated nucleotide addition.
Publications: 1 Organism: Homo Sapiens
+ AKT1down-regulates activity img/direct_inhibition.png phosphorylation TENT2 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-259405 Ser116 LSGERRYsMPPLFHT Homo sapiens HEK-293 Cell
pmid sentence
We found that Gld2 activity is regulated by site-specific phosphorylation in its disordered N-terminal domain. We identified two phosphorylation sites (S62, S110) where phosphomimetic substitutions increased Gld2 activity and one site (S116) that markedly reduced activity. Using mass spectrometry, we confirmed that HEK 293 cells readily phosphorylate the N-terminus of Gld2. We identified protein kinase A (PKA) and protein kinase B (Akt1) as the kinases that site-specifically phosphorylate Gld2 at S116, abolishing Gld2-mediated nucleotide addition.
Publications: 1 Organism: Homo Sapiens
+ PRKACAdown-regulates activity img/direct_inhibition.png phosphorylation TENT2 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-259402 Ser116 LSGERRYsMPPLFHT Homo sapiens
pmid sentence
We found that Gld2 activity is regulated by site-specific phosphorylation in its disordered N-terminal domain. We identified two phosphorylation sites (S62, S110) where phosphomimetic substitutions increased Gld2 activity and one site (S116) that markedly reduced activity. Using mass spectrometry, we confirmed that HEK 293 cells readily phosphorylate the N-terminus of Gld2. We identified protein kinase A (PKA) and protein kinase B (Akt1) as the kinases that site-specifically phosphorylate Gld2 at S116, abolishing Gld2-mediated nucleotide addition.
Publications: 1 Organism: Homo Sapiens
+ PKAdown-regulates activity img/direct_inhibition.png phosphorylation TENT2 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-270130 Homo sapiens HEK-293 Cell
pmid sentence
We found that Gld2 activity is regulated by site-specific phosphorylation in its disordered N-terminal domain. We identified two phosphorylation sites (S62, S110) where phosphomimetic substitutions increased Gld2 activity and one site (S116) that markedly reduced activity. Using mass spectrometry, we confirmed that HEK 293 cells readily phosphorylate the N-terminus of Gld2. We identified protein kinase A (PKA) and protein kinase B (Akt1) as the kinases that site-specifically phosphorylate Gld2 at S116, abolishing Gld2-mediated nucleotide addition.
Publications: 1 Organism: Homo Sapiens
a simple tooltip