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Literature summary for 2.7.7.19 extracted from

  • Shin, J.; Paek, K.; Ivshina, M.; Stackpole, E.; Richter, J.
    Essential role for non-canonical poly(A) polymerase GLD4 in cytoplasmic polyadenylation and carbohydrate metabolism (2017), Nucleic Acids Res., 45, 6793-6804 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.7.7.19

Cloned(Commentary)

Cloned (Comment) Organism
expressed in HEK-293T cells Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
cytoplasm
-
 Homo sapiens 5737
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + RNAn Homo sapiens
-
 diphosphate + RNAn+1
-
 ?

Organism

Organism UniProt Comment Textmining
Homo sapiens Q8NDF8
-
-

Source Tissue

Source Tissue Comment Organism Textmining
glioblastoma cell
-
 Homo sapiens
-
U-87MG cell
-
 Homo sapiens
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + GLUT1 mRNA poly(A) tail
-
 Homo sapiens ?
-
 ?
ATP + RNAn
-
 Homo sapiens diphosphate + RNAn+1
-
 ?

Synonyms

Synonyms Comment Organism
GLD4
-
 Homo sapiens
PAP
-
 Homo sapiens
poly(A) polymerase
-
 Homo sapiens

General Information

General Information Comment Organism
malfunction enzyme depletion not only reduces GLUT1 poly(A) tail length, but also GLUT1 protein. Enzyme depletion impairs glucose deprivation-induced GLUT1 up-regulation Homo sapiens
physiological function enzyme-mediated translational control of GLUT1 mRNA is dependent of an RNA binding protein, CPEB1, and its binding elements in the 3_UTR. Through regulating GLUT1 level, the enzyme affects glucose uptake into cells and lactate levels. The enzyme affects glucose-dependent cellular phenotypes such as migration and invasion in glioblastoma cells Homo sapiens