Preferred Name

AKT kinase
Synonyms

PKB

AKT

serine-threonine kinase Akt

Definitions

A protein that has a core domain composition consisting of a PH domain (Pfam:PF00169), Protein kinase domain (Pfam:PF00069) and a Protein kinase C terminal domain (Pfam:PF00433). Mammals have three genes encoding AKT1, AKT2 and AKT3. The second messenger phosphatidylinositol-3,4,5-trisphosphate [PIP(3)], product of phosphatidylinositol 3-kinase, acts largely through its role as a kinase activator. Binding of the pleckstrin domain to PIP(3) results in its targeting to the plasma membrane. Full activity is gained only after phosphorylation at two sites.

ID

http://purl.obolibrary.org/obo/PR_000029189

definition

A protein that has a core domain composition consisting of a PH domain (Pfam:PF00169), Protein kinase domain (Pfam:PF00069) and a Protein kinase C terminal domain (Pfam:PF00433). Mammals have three genes encoding AKT1, AKT2 and AKT3. The second messenger phosphatidylinositol-3,4,5-trisphosphate [PIP(3)], product of phosphatidylinositol 3-kinase, acts largely through its role as a kinase activator. Binding of the pleckstrin domain to PIP(3) results in its targeting to the plasma membrane. Full activity is gained only after phosphorylation at two sites.

A protein that has a core domain composition consisting of a PH domain (Pfam:PF00169), Protein kinase domain (Pfam:PF00069) and a Protein kinase C terminal domain (Pfam:PF00433). Mammals have three genes encoding AKT1, AKT2 and AKT3. The second messenger phosphatidylinositol-3,4,5-trisphosphate [PIP(3)], product of phosphatidylinositol 3-kinase, acts largely through its role as a kinase activator. Binding of the pleckstrin domain to PIP(3) results in its targeting to the plasma membrane. Full activity is gained only after phosphorylation at two sites.

has role

http://purl.bioontology.org/ontology/HOIP/HOIP_0001966

has_broad_synonym

PKB

has_exact_synonym

AKT

serine-threonine kinase Akt

label

AKT kinase

prefixIRI

PR:000029189

prefLabel

AKT kinase

subClassOf

http://purl.obolibrary.org/obo/CHEBI_25367

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