TTLL6 report

I. Expression across cell types

Insufficient scRNA-seq data for expression of TTLL6 at single-cell level.

II. Expression across tissues

sc-RNAseq data

Insufficient scRNA-seq data for expression of TTLL6 at tissue level.

III. Associated gene sets

GO_0018095Biological processprotein polyglutamylation
GO_0051013Biological processmicrotubule severing
GO_0003353Biological processpositive regulation of cilium movement
GO_0060296Biological processregulation of cilium beat frequency involved in ciliary motility
GO_0001578Biological processmicrotubule bundle formation
GO_0000226Biological processmicrotubule cytoskeleton organization
GO_0005874Cellular componentmicrotubule
GO_0097731Cellular component9+0 non-motile cilium
GO_0005929Cellular componentcilium
GO_0036064Cellular componentciliary basal body
GO_0005829Cellular componentcytosol
GO_0070739Molecular functionprotein-glutamic acid ligase activity
GO_0070740Molecular functiontubulin-glutamic acid ligase activity
GO_0005515Molecular functionprotein binding
GO_0046872Molecular functionmetal ion binding
GO_0005524Molecular functionATP binding
GO_0015631Molecular functiontubulin binding

IV. Literature review

[source]
Gene nameTTLL6
Protein nameTubulin tyrosine ligase like 6
Tubulin polyglutamylase TTLL6 (EC 6.3.2.-) (Protein polyglutamylase TTLL6) (Tubulin--tyrosine ligase-like protein 6)
SynonymsTTL.6
DescriptionFUNCTION: Polyglutamylase which modifies both tubulin and non-tubulin proteins, generating alpha-linked polyglutamate side chains on the gamma-carboxyl group of specific glutamate residues of target proteins. Preferentially mediates ATP-dependent long polyglutamate chain elongation over the initiation step of the polyglutamylation reaction. Preferentially modifies the alpha-tubulin tail over a beta-tail. Promotes tubulin polyglutamylation which stimulates spastin/SPAST-mediated microtubule severing, thereby regulating microtubule functions. Mediates microtubule polyglutamylation in primary cilia axoneme, which is important for ciliary structural formation and motility. Mediates microtubule polyglutamylation in motile cilia, necessary for the regulation of ciliary coordinated beating. Polyglutamylates non-tubulin protein nucleotidyltransferase CGAS, leading to CGAS DNA-binding inhibition, thereby preventing antiviral defense response. .

AccessionsENST00000456415.1
Q8N841
ENST00000424018.1
F8WDP8
ENST00000393382.8 [Q8N841-1]
F6QD81
ENST00000376681.7
F8W896
ENST00000416950.5
F8W9N0