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TTLL3 TTLL3 TTLL12 TTLL12 TTL TTL TTLL2 TTLL2 TTLL7 TTLL7 TTLL1 TTLL1 TTLL5 TTLL5 TTLL11 TTLL11 TTLL10 TTLL10 TTLL4 TTLL4 TTLL6 TTLL6 ARPC4-TTLL3 ARPC4-TTLL3 TTLL8 TTLL8 TTLL9 TTLL9 TTLL13P TTLL13P
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splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
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query proteins and first shell of interactors
white nodes:
second shell of interactors
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proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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Edges represent protein-protein associations
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experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
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TTLL3Tubulin monoglycylase TTLL3; Monoglycylase which modifies alpha- and beta-tubulin, generating side chains of glycine on the gamma-carboxyl groups of specific glutamate residues within the C-terminal tail of alpha- and beta-tubulin. Involved in the side-chain initiation step of the glycylation reaction by adding a single glycine chain to generate monoglycine side chains. Not involved in elongation step of the polyglycylation reaction. (915 aa)
TTLL12Tubulin--tyrosine ligase-like protein 12; Negatively regulates post-translational modifications of tubulin, including detyrosination of the C-terminus and polyglutamylation of glutamate residues. Also, indirectly promotes histone H4 trimethylation at 'Lys-20' (H4K20me3). Probably by controlling tubulin and/or histone H4 post-translational modifications, plays a role in mitosis and in maintaining chromosome number stability. During RNA virus-mediated infection, acts as a negative regulator of the DDX58/RIG-I pathway by preventing MAVS binding to TBK1 and IKBKE. (644 aa)
TTLTubulin--tyrosine ligase; Catalyzes the post-translational addition of a tyrosine to the C-terminal end of detyrosinated alpha-tubulin. (377 aa)
TTLL2Probable tubulin polyglutamylase TTLL2; Probable tubulin polyglutamylase that forms polyglutamate side chains on tubulin. Probably acts when complexed with other proteins (By similarity); Belongs to the tubulin--tyrosine ligase family. (592 aa)
TTLL7Tubulin polyglutamylase TTLL7; Polyglutamylase which preferentially modifies beta-tubulin. Mediates both ATP-dependent initiation and elongation of polyglutamylation of microtubules. Required for neurite growth; responsible for the strong increase in tubulin polyglutamylation during postnatal neuronal maturation (By similarity); Belongs to the tubulin--tyrosine ligase family. (887 aa)
TTLL1Probable tubulin polyglutamylase TTLL1; Catalytic subunit of the neuronal tubulin polyglutamylase complex. Modifies alpha- and beta-tubulin, generating side chains of glutamate on the gamma-carboxyl groups of specific glutamate residues within the C-terminal tail of alpha- and beta-tubulin (By similarity). (423 aa)
TTLL5Tubulin polyglutamylase TTLL5; Polyglutamylase which preferentially modifies alpha-tubulin (By similarity). Involved in the side-chain initiation step of the polyglutamylation reaction rather than in the elongation step (By similarity). Required for CCSAP localization to both spindle and cilia microtubules. Increases the effects of NCOA2 in glucocorticoid receptor-mediated repression and induction and in androgen receptor-mediated induction. Belongs to the tubulin--tyrosine ligase family. (1281 aa)
TTLL11Tubulin polyglutamylase TTLL11; Polyglutamase which preferentially modifies alpha-tubulin. Involved in the side-chain elongation step of the polyglutamylation reaction rather than in the initiation step (By similarity). Required for CCSAP localization to both spindle and cilia microtubules. Generates long side-chains (By similarity). (800 aa)
TTLL10Inactive polyglycylase TTLL10; Inactive polyglycylase. (673 aa)
TTLL4Tubulin polyglutamylase TTLL4; Glutamylase which preferentially modifies beta-tubulin and non-tubulin proteins, such as NAP1L1, NAP1L4 and CGAS. Involved in the side-chain initiation step of the polyglutamylation reaction rather than in the elongation step. Involved in formation of short side- chains. Mediates initiation of polyglutamylation of nucleosome assembly proteins NAP1L1 and NAP1L4. Also acts as a monoglutamylase: generates monoglutamylation of CGAS, leading to impair the nucleotidyltransferase activity of CGAS; Belongs to the tubulin--tyrosine ligase family. (1199 aa)
TTLL6Tubulin polyglutamylase TTLL6; Polyglutamylase which preferentially modifies alpha-tubulin. Mediates tubulin polyglutamylation in cilia. Involved in the side-chain elongation step of the polyglutamylation reaction rather than in the initiation step. Generates long side-chains. Generates polyglutamylation of CGAS, leading to impair the DNA-binding activity of CGAS. (891 aa)
ARPC4-TTLL3ARPC4-TTLL3 readthrough. (625 aa)
TTLL8Protein monoglycylase TTLL8; Monoglycylase which modifies both tubulin and non-tubulin proteins, generating side chains of glycine on the gamma-carboxyl groups of specific glutamate residues of target proteins. Monoglycylates tubulin, with a preference for alpha-tubulin toward beta-tubulin. Has the ability to modify non-tubulin proteins such as ANP32A, ANP32B, SET and NCL. Involved in the side-chain initiation step of the glycylation reaction by adding a single glycine chain to generate monoglycine side chains. Not involved in elongation step of the polyglycylation reaction (By similarity). (849 aa)
TTLL9Probable tubulin polyglutamylase TTLL9; Probable tubulin polyglutamylase that forms polyglutamate side chains on tubulin. Acts when complexed with other proteins. By mediating tubulin polyglutamylation, plays a role in the establishment of microtubule heterogeneity in sperm flagella. (439 aa)
TTLL13PTubulin polyglutamylase TTLL13P; Polyglutamylase which preferentially modifies alpha-tubulin. Involved in the side-chain elongation step of the polyglutamylation reaction rather than in the initiation step (By similarity). Belongs to the tubulin--tyrosine ligase family. (815 aa)
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, human, man
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