+ |
ATAT1 | up-regulates quantity by stabilization
acetylation
|
TUBA4A |
0.265 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-272249 |
Lys40 |
DGQMPSDkTIGGGDD |
in vitro |
|
pmid |
sentence |
29703898 |
Alpha-Tubulin acetyltransferase (alphaTAT1) is the major α-tubulin lysine-40 (K40) acetyltransferase in mammals, nematodes, and protozoa, and its activity plays a conserved role in several microtubule-based processes.|The tubulin subunits of microtubules are acetylated, and lysine-40 (K40) of the alpha-tubulin subunit has been identified as an important conserved site of microtubule acetylation (6–8). This modification is considered a hallmark of stable, long-lived microtubules |
|
Publications: |
1 |
Organism: |
In Vitro |
+ |
SYK | up-regulates activity
phosphorylation
|
TUBA4A |
0.335 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-246626 |
Tyr432 |
MAALEKDyEEVGIDS |
Homo sapiens |
B-lymphocyte |
pmid |
sentence |
9490415 |
Syk, Activated by Cross-linking the B-cell Antigen Receptor, Localizes to the Cytosol Where It Interacts with and Phosphorylates alpha-Tubulin on Tyrosine |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
paclitaxel | down-regulates activity
chemical inhibition
|
TUBA4A |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-259346 |
|
|
Homo sapiens |
|
pmid |
sentence |
28298489 |
Here we integrate a computational model for microtubule assembly with nanometer-scale fluorescence microscopy measurements to identify the kinetic and thermodynamic basis of kinetic stabilization by the MTAs paclitaxel, an assembly promoter, and vinblastine, a disassembly promoter. We identify two distinct modes of kinetic stabilization in live cells, one that truly suppresses on-off kinetics, characteristic of vinblastine, and the other a "pseudo" kinetic stabilization, characteristic of paclitaxel, that nearly eliminates the energy difference between the GTP- and GDP-tubulin thermodynamic states. By either mechanism, the main effect of both MTAs is to effectively stabilize the microtubule against disassembly in the absence of a robust GTP cap. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
eribulin mesylate | down-regulates activity
chemical inhibition
|
TUBA4A |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-259344 |
|
|
Homo sapiens |
|
pmid |
sentence |
16940412 |
The complex marine natural product halichondrin B was compared with NSC 707389 (E7389), a structurally simplified, synthetic macrocyclic ketone analog, which has been selected for clinical trials in human patients. NSC 707389 was invariably more potent than halichondrin B in its interactions with tubulin. Both compounds inhibited tubulin assembly, inhibited nucleotide exchange on beta-tubulin, and were noncompetitive inhibitors of the binding of radiolabeled vinblastine and dolastatin 10 to tubulin. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
TTL | down-regulates
tyrosination
|
TUBA4A |
0.29 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-176927 |
|
|
Homo sapiens |
|
pmid |
sentence |
22020298 |
Tubulin tyrosine ligase (ttl) adds a c-terminal tyr to __tubulin as part of a tyrosination/detyrosination cycle present in most eukaryotic cells. / ttl inhibits spontaneous tubulin polymerization |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
cabazitaxel | down-regulates activity
chemical inhibition
|
TUBA4A |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-259340 |
|
|
Homo sapiens |
|
pmid |
sentence |
21770474 |
Among these, larotaxel (XRP9881, formerly RPR109881A)[3,4] and cabazitaxel (XRP6258, TXD258, RPR116258A)[5] share a mechanism of action unique to taxanes, promoting tubulin assembly and stabilizing microtubules against cold-induced depolymerization |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
TUBA4A | up-regulates
|
Neuron_migration |
0.7 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-269730 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
19185337 |
We show here that Elongator regulates corticogenesis because an acute disruption of its activity in dorsal progenitors results in radial migration delays and defective terminal branching of projection neurons that come with a reduction in α-tubulin acetylation. Importantly, this complex interacts with the microtubule cytoskeleton, where Elp3 may directly acetylate α-tubulin, a posttranslational modification known to regulate the intracellular trafficking that is critical for cell shape remodeling during migration and terminal branching. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
Elongator complex | up-regulates activity
acetylation
|
TUBA4A |
0.254 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-269722 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
19185337 |
Elongator Subunits Interact with the Microtubules and Are Required for Proper Acetylation of α-Tubulin. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
docetaxel anhydrous | down-regulates activity
chemical inhibition
|
TUBA4A |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-259342 |
|
|
Homo sapiens |
|
pmid |
sentence |
23337758 |
Tubulin exists in the cell as dimers of α and β subunits, which complexes with a variety of regulatory proteins. There is a dynamic equilibrium between free and polymerized tubulin causing a state called "dynamic instability," which is a target of anticancer drugs, which inhibit tubulin through polymerization (taxanes, epothilones) or depolymerization (vinca alkaloids). Docetaxel-based therapy was the first such treatment to demonstrate a survival benefit in men with castration-resistant prostate cancer. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
NUMA1 | up-regulates
binding
|
TUBA4A |
0.494 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-116788 |
|
|
Homo sapiens |
|
pmid |
sentence |
11956313 |
Direct binding of numa to tubulin is mediated by a novel sequence motif in the tail domain that bundles and stabilizes microtubules. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |