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Proteins/UNIPROT:Q6ZT98
Polyglutamylase which modifies tubulin, generating polyglutamate side chains of variable lengths on the gamma-carboxyl group of specific glutamate residues within the C-terminal tail of tubulin. Mediates both ATP-dependent initiation and elongation steps of the polyglutamylation reaction. Preferentially modifies the beta-tubulin tail over an alpha-tail. Competes with monoglycylase TTLL3 for modification site on beta-tubulin substrate, thereby creating an anticorrelation between glycylation and glutamylation reactions (By similarity). Required for neurite growth; responsible for the strong increase in tubulin polyglutamylation during postnatal neuronal maturation (By similarity)..
Function from UniProtKB (Q6ZT98), read 2026-09-23. CC BY 4.0.
Curated compounds routed: 0
7 statements
7 statements · 3 reference databases · Subject: TTLL7 · Sources: Hetionet, Reactome, UniProt
2 reactions
L-glutamyl-[protein]+L-glutamate(1-)+ATP(4-)gamma-L-glutamyl-L-glutamyl-[protein]+ADP(3-)+hydrogenphosphate+hydron
Catalysed by TTLL4 or TTLL5 or TTLL7 or TTLL6 or TTLL11
Reaction pageLeft to rightBalance undeterminable
Rhea RHEA:60144CC BY 4.0Reference data
(L-glutamyl)(n)-gamma-L-glutamyl-L-glutamyl-[protein]+
2 names
Resolves to: TTLL7
Reaction pageLeft to rightBalance undeterminable
Rhea RHEA:60148CC BY 4.0Reference data