6.3.2.B3: tubulin-glutamate ligase
This is an abbreviated version!
For detailed information about tubulin-glutamate ligase, go to the full flat file.
Word Map on EC 6.3.2.B3
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6.3.2.B3
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tubulins
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polyglutamylation
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microtubule
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ligase-like
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cilia
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polyglutamylase
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axonemal
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deglutamylation
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cone-rod
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ccp1
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deglutamylase
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polyglycylation
- 6.3.2.B3
- tubulins
-
polyglutamylation
- microtubule
-
ligase-like
- cilia
-
polyglutamylase
-
axonemal
-
deglutamylation
-
cone-rod
- ccp1
- deglutamylase
-
polyglycylation
deleted, replaced by EC 6.3.2.61, tubulin-glutamate ligase
Synonyms
Synonyms
alpha-tubulin polyglutamylase, TTHERM_00773080, TTL domain protein, TTLL1, TTLL9, tubulin glutamylase, tubulin tyrosine ligase domain protein
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General Information
General Information on EC 6.3.2.B3 - tubulin-glutamate ligase
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physiological function
Ttll1p glutamylase preferentially modifies alpha-tubulin. It shows a chain-initiating activity. The spatial restriction of modifying enzymes TTLL1 and TTLL9 appears to be a major mechanism that drives differential glutamylation at the subcellular level. Disruption of the isoforms TTLL1 and TTLL9 genes decreases the rates of cell multiplication and phagocytosis. Cells lacking both genes have fewer cortical microtubules and show defects in the maturation of basal bodies. In the TTLL1 and TTLL9 double knockout, a decrease in the levels of glutamylation on alpha-tubulin occurs
physiological function
Ttll9 glutamylase preferentially modifies alpha-tubulin. It has primarily a chain-elongating activity. The spatial restriction of modifying enzymes TTLL1 and TTLL9 appears to be a major mechanism that drives differential glutamylation at the subcellular level. Disruption of the isoforms TTLL1 and TTLL9 genes decreases the rates of cell multiplication and phagocytosis. Cells lacking both genes have fewer cortical microtubules and show defects in the maturation of basal bodies. In the TTLL1 and TTLL9 double knockout, a decrease in the levels of glutamylation on alpha-tubulin occurs
physiological function
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Ttll9 glutamylase preferentially modifies alpha-tubulin. It has primarily a chain-elongating activity. The spatial restriction of modifying enzymes TTLL1 and TTLL9 appears to be a major mechanism that drives differential glutamylation at the subcellular level. Disruption of the isoforms TTLL1 and TTLL9 genes decreases the rates of cell multiplication and phagocytosis. Cells lacking both genes have fewer cortical microtubules and show defects in the maturation of basal bodies. In the TTLL1 and TTLL9 double knockout, a decrease in the levels of glutamylation on alpha-tubulin occurs
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physiological function
-
Ttll1p glutamylase preferentially modifies alpha-tubulin. It shows a chain-initiating activity. The spatial restriction of modifying enzymes TTLL1 and TTLL9 appears to be a major mechanism that drives differential glutamylation at the subcellular level. Disruption of the isoforms TTLL1 and TTLL9 genes decreases the rates of cell multiplication and phagocytosis. Cells lacking both genes have fewer cortical microtubules and show defects in the maturation of basal bodies. In the TTLL1 and TTLL9 double knockout, a decrease in the levels of glutamylation on alpha-tubulin occurs
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