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Literature summary for 2.7.11.1 extracted from

  • Masure, S.; Haefner, B.; Wesselink, J.J.; Hoefnagel, E.; Mortier, E.; Verhasselt, P.; Tuytelaars, A.; Gordon, R.; Richardson, A.
    Molecular cloning, expression and characterization of the human serine/threonine kinase Akt-3 (1999), Eur. J. Biochem., 265, 353-360.
    View publication on PubMed
Search for more literature for 2.7.11.1

Cloned(Commentary)

Cloned (Comment) Organism
-
 Homo sapiens

Protein Variants

Protein Variants Comment Organism
additional information phosphorylation of Ser472 and phosphorylation of Thr305 appears to contribute to the activation of Akt-3 because mutation of both these residues to aspartate increases the catalytic activity of Akt-3, whereas mutation to alanine inhibits activation Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
Ro 31-8220
-
 Homo sapiens
staurosporine
-
 Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens Q9Y243
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
phosphoprotein Akt-3 also possess a C-terminal 'tail' that contains a phosphorylation site Ser472 thought to be involved in the activation of Akt kinases. In addition to phosphorylation of Ser472, phosphorylation of Thr305 also appears to contribute to the activation of Akt-3 Homo sapiens

Source Tissue

Source Tissue Comment Organism Textmining
liver not highly expressed Homo sapiens
-
additional information expressed widely Homo sapiens
-
skeletal muscle not highly expressed Homo sapiens
-

Synonyms

Synonyms Comment Organism
Akt-3
-
 Homo sapiens
RAC-gamma serine/threonine protein kinase
-
 Homo sapiens