| + |
KANSL1 | up-regulates 
|
Microtubule_polimerization |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267170 |
|
|
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 26243146 |
Here we uncover a novel function of the NSL complex members in mitosis. As the cell enters mitosis, KANSL1 and KANSL3 undergo a marked relocalisation from the chromatin to the mitotic spindle. By stabilizing microtubule minus ends in a RanGTP-dependent manner, they are essential for spindle assembly and chromosome segregation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CLIP1 | up-regulates 
binding
|
Microtubule_polimerization |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264830 |
|
|
|
|
| pmid |
sentence |
| 17889670 |
Microtubule plus end binding proteins (+TIPs) localize to the dynamic plus ends of microtubules, where they stimulate microtubule growth and recruit signaling molecules. Three main +TIP classes have been identified (XMAP215, EB1, and CLIP-170) |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264832 |
|
|
|
|
| pmid |
sentence |
| 17889670 |
Microtubule plus end binding proteins (+TIPs) localize to the dynamic plus ends of microtubules, where they stimulate microtubule growth and recruit signaling molecules. Three main +TIP classes have been identified (XMAP215, EB1, and CLIP-170) |
|
| Publications: |
2 |
| + |
HAUS6 | up-regulates
|
Microtubule_polimerization |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261420 |
|
|
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 19029337 |
FAM29A interacts with the NEDD1-gamma-tubulin complex and recruits this complex to the spindle, which, in turn, promotes MT polymerization. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
Tubulin | up-regulates
|
Microtubule_polimerization |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266827 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 28347630 |
Microtubules are essential for the generation, migration and differentiation of neurons. Within dendrites microtubules have also been implicated in the formation and plasticity of spines. For instance, the treatment of hippocampal neurons with low doses of the microtubule destabilizing drug Nocodazole impairs BDNF induced dendritic spine formation |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
TUBE1 | up-regulates
|
Microtubule_polimerization |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267178 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 28347630 |
Microtubules are essential for the generation, migration and differentiation of neurons. Within dendrites microtubules have also been implicated in the formation and plasticity of spines. For instance, the treatment of hippocampal neurons with low doses of the microtubule destabilizing drug Nocodazole impairs BDNF induced dendritic spine formation |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MAPRE1 | up-regulates
binding
|
Microtubule_polimerization |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264831 |
|
|
|
|
| pmid |
sentence |
| 17889670 |
Microtubule plus end binding proteins (+TIPs) localize to the dynamic plus ends of microtubules, where they stimulate microtubule growth and recruit signaling molecules. Three main +TIP classes have been identified (XMAP215, EB1, and CLIP-170) |
|
| Publications: |
1 |
| + |
GNAI1 | down-regulates 
|
Microtubule_polimerization |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-256523 |
|
|
in vitro |
|
| pmid |
sentence |
| 10224115 |
G protein alpha subunits Gi1alpha, Gsalpha, and Goalpha are shown to activate the GTPase activity of tubulin, inhibit microtubule assembly, and accelerate microtubule dynamics. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
GNAS | down-regulates
|
Microtubule_polimerization |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-256524 |
|
|
in vitro |
|
| pmid |
sentence |
| 10224115 |
G protein alpha subunits Gi1alpha, Gsalpha, and Goalpha are shown to activate the GTPase activity of tubulin, inhibit microtubule assembly, and accelerate microtubule dynamics. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
TUBG1 | up-regulates
|
Microtubule_polimerization |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261423 |
|
|
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 19029337 |
It has been reported that NEDD1 directly interacts with and recruits the γ-tubulin ring complex to centrosomes and to spindle MTs to promote MT nucleation and spindle assembly |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
KATNA1 | down-regulates
|
Microtubule_polimerization |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271794 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19287380 |
Katanin, one of the best-characterized microtubule (MT) severing proteins, is composed of two subunits: catalytic p60-katanin, and regulatory p80-katanin. p60-katanin triggers MT reorganization by severing them. MT reorganization is essential for both mitotic cells and post-mitotic neurons in numerous vital processes such as intracellular transport, mitosis, cellular differentiation and apoptosis. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
Microtubule_polimerization | up-regulates
|
Neurite_outgrowth |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266830 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 28347630 |
Microtubules are essential for the generation, migration and differentiation of neurons. Within dendrites microtubules have also been implicated in the formation and plasticity of spines. For instance, the treatment of hippocampal neurons with low doses of the microtubule destabilizing drug Nocodazole impairs BDNF induced dendritic spine formation |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
Microtubule_polimerization | up-regulates
|
Neuron_migration |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266829 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 28347630 |
Microtubules are essential for the generation, migration and differentiation of neurons. Within dendrites microtubules have also been implicated in the formation and plasticity of spines. For instance, the treatment of hippocampal neurons with low doses of the microtubule destabilizing drug Nocodazole impairs BDNF induced dendritic spine formation |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SPAST | up-regulates
cleavage
|
Microtubule_polimerization |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269046 |
|
|
in vitro |
|
| pmid |
sentence |
| 15716377 |
Using real-time imaging, we show that Spastin severs microtubules when added to permeabilized, cytosol-depleted cells stably expressing GFP-tubulin. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
STMN3 | down-regulates quantity by destabilization 
binding
|
Microtubule_polimerization |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264896 |
|
|
|
|
| pmid |
sentence |
| 22577147 |
Stathmins can thus sequester free tubulin that may result in inhibiting microtubule growth and/or promoting microtubule collapse |
|
| Publications: |
1 |
| + |
GNAO1 | down-regulates
|
Microtubule_polimerization |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-256525 |
|
|
in vitro |
|
| pmid |
sentence |
| 10224115 |
G protein alpha subunits Gi1alpha, Gsalpha, and Goalpha are shown to activate the GTPase activity of tubulin, inhibit microtubule assembly, and accelerate microtubule dynamics. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
MAP1B | up-regulates quantity by stabilization
binding
|
Microtubule_polimerization |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264844 |
|
|
Homo sapiens |
Neuron |
| pmid |
sentence |
| 10649507 |
MAP1B is a microtubule-associated phosphoprotein that is particularly highly expressed in developing neurons. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MAP2 | up-regulates quantity by stabilization
binding
|
Microtubule_polimerization |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264837 |
|
|
Homo sapiens |
Neuron |
| pmid |
sentence |
| 10704996 |
MAP2 interacts with MTs through its tubulin-binding domain which mainly associates with the acidic region of the C-terminal region of tubulin|no neurite growth is observed when MAP2 expression is suppressed in neuronal cell cultures after treatment with specific antisense oligonucleotides |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
KATNB1 | down-regulates
|
Microtubule_polimerization |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267181 |
|
|
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 10751153 |
Katanin, a heterodimeric microtubule-severing ATPase, is found localized at mitotic spindle poles. In this paper we demonstrate that human p60 katanin and the C-terminal domain of human p80 katanin both bind microtubules in vitro. Association of these two proteins results in an increased microtubule affinity and increased microtubule-severing activity in vitro. Association of these subunits in transfected HeLa cells increases microtubule disassembly activity and targeting to spindle poles. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
TUBD1 | up-regulates
|
Microtubule_polimerization |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267177 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 28347630 |
Microtubules are essential for the generation, migration and differentiation of neurons. Within dendrites microtubules have also been implicated in the formation and plasticity of spines. For instance, the treatment of hippocampal neurons with low doses of the microtubule destabilizing drug Nocodazole impairs BDNF induced dendritic spine formation |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
KANSL3 | up-regulates
|
Microtubule_polimerization |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267169 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 26243146 |
Here we uncover a novel function of the NSL complex members in mitosis. As the cell enters mitosis, KANSL1 and KANSL3 undergo a marked relocalisation from the chromatin to the mitotic spindle. By stabilizing microtubule minus ends in a RanGTP-dependent manner, they are essential for spindle assembly and chromosome segregation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
DPYSL2 | up-regulates
|
Microtubule_polimerization |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264841 |
|
|
Homo sapiens |
Neuron |
| pmid |
sentence |
| 25040932 |
In the non-phosphorylated state, CRMP2 binding to tubulin induces the promotion of tubulin polymerisation leading to dendrite outgrowth while |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CLIP2 | up-regulates
|
Microtubule_polimerization |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265095 |
|
|
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 15631994 |
CLIP-associating protein (CLASP) 1 and CLASP2 are mammalian microtubule (MT) plus-end binding proteins, which associate with CLIP-170 and CLIP-115.|We demonstrate that the middle part of CLASPs binds directly to EB1 and to MTs. | Both EB1- and cortex-binding domains of CLASP are required to promote MT stability. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
Microtubule_polimerization