Tubulin-tyrosine ligase/Tubulin polyglutamylase (IPR004344)

Short name: TTL/TTLL_fam

Overlapping homologous superfamilies


Family relationships


Tubulins and microtubules are subjected to several post-translational modifications of the carboxy-terminal end of most major forms of tubulins has been extensively analysed. This modification cycle involves a specific carboxypeptidase and the activity of the tubulin-tyrosine ligase (TTL) and the tubulin polyglutamylase (TTLL) [PMID: 10685598, PMID: 19524510]. Tubulin-tyrosine ligase (TTL) catalyses the ATP-dependent post-translational addition of a tyrosine to the carboxy terminal end of detyrosinated alpha-tubulin. Tubulin polyglutamylase (such as TTLL10) can modify both tubulin and non-tubulin proteins, generating side chains of glycine on the gamma-carboxyl groups of specific glutamate residues of target proteins [PMID: 19524510]. Tubulin polyglutamylation may be involved in the organisation of the neuronal microtubule network, in centriole stability, axoneme motility and mitosis [PMID: 15890843].

GO terms

Biological Process

GO:0006464 cellular protein modification process

Molecular Function

No terms assigned in this category.

Cellular Component

No terms assigned in this category.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.
PROSITE profiles