TUBA1A

Summary

TUBA1A (tubulin alpha 1a, HGNC:20766) is a protein-coding gene on chromosome 12q13.12, encoding Tubulin alpha-1A chain (Q71U36). Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers.

Microtubules of the eukaryotic cytoskeleton perform essential and diverse functions and are composed of a heterodimer of alpha and beta tubulins. The genes encoding these microtubule constituents belong to the tubulin superfamily, which is composed of six distinct families. Genes from the alpha, beta and gamma tubulin families are found in all eukaryotes. The alpha and beta tubulins represent the major components of microtubules, while gamma tubulin plays a critical role in the nucleation of microtubule assembly. There are multiple alpha and beta tubulin genes, which are highly conserved among species. This gene encodes alpha tubulin and is highly similar to the mouse and rat Tuba1 genes. Northern blot studies have shown that the gene expression is predominantly found in morphologically differentiated neurologic cells. This gene is one of three alpha-tubulin genes in a cluster on chromosome 12q. Mutations in this gene cause lissencephaly type 3 (LIS3) - a neurological condition characterized by microcephaly, intellectual disability, and early-onset epilepsy caused by defective neuronal migration. Alternative splicing results in multiple transcript variants encoding distinct isoforms.

Source: NCBI Gene 7846 — RefSeq curated summary.

At a glance

• Gene–disease (curated): tubulinopathy (Definitive, ClinGen) — +3 more curated relationships
• GWAS associations: 2
• Clinical variants (ClinVar): 435 total — 63 pathogenic, 89 likely-pathogenic
• Phenotypes (HPO): 110
• Druggable target: yes — 22 molecules with ChEMBL bioactivity
• Dosage sensitivity (ClinGen): haploinsufficiency no evidence, triplosensitivity no evidence
• MANE Select transcript: NM_006009

Identifiers

Gene identifiers

Field	Value
HGNC ID	HGNC:20766
Approved symbol	TUBA1A
Name	tubulin alpha 1a
Location	12q13.12
Locus type	gene with protein product
Status	Approved
Aliases	TUBA3, B-ALPHA-1, FLJ25113
Ensembl gene	ENSG00000167552
Ensembl biotype	protein_coding
OMIM	602529
Entrez	7846

Gene structure

Transcript identifiers

Ensembl transcripts: 13 — 10 protein_coding, 3 retained_intron

ENST00000295766, ENST00000301071, ENST00000546918, ENST00000547939, ENST00000548363, ENST00000550254, ENST00000550767, ENST00000550811, ENST00000552924, ENST00000679733, ENST00000715688, ENST00000871057, ENST00000928854

RefSeq mRNA: 3 — MANE Select: NM_006009 NM_001270399, NM_001270400, NM_006009

CCDS: CCDS58226, CCDS58227, CCDS8781

Canonical transcript exons

ENST00000301071 — 4 exons

Exon	Start	End
ENSE00002356541	49184795	49185990
ENSE00003365780	49186310	49186458
ENSE00003611441	49186611	49186833
ENSE00004027585	49188977	49189080

Expression profiles

Bgee: expression breadth ubiquitous, 288 present calls, max score 100.00.

FANTOM5 (CAGE): breadth ubiquitous, TPM avg 765.7774 / max 18141.6732, expressed in 1815 samples.

FANTOM5 promoters (16 alternative TSS)

Promoter ID	TPM avg	Samples expressed
130831	740.5900	1810
130829	15.7313	1756
130830	2.0903	1060
130827	1.5951	918
130832	1.2300	768
130822	1.0119	500
130821	0.8938	418
130818	0.7717	305
130826	0.6368	217
130820	0.5718	220

Top tissues by expression

288 total, by Bgee expression score (0-100, higher = more expressed):

Tissue	Anatomy ID	Expression score	Quality
endothelial cell	CL:0000115	100.00	gold quality
cortical plate	UBERON:0005343	100.00	gold quality
ganglionic eminence	UBERON:0004023	99.99	gold quality
inferior vagus X ganglion	UBERON:0005363	99.98	gold quality
dorsal root ganglion	UBERON:0000044	99.97	gold quality
medulla oblongata	UBERON:0001896	99.97	gold quality
inferior olivary complex	UBERON:0002127	99.97	gold quality
superior vestibular nucleus	UBERON:0007227	99.97	gold quality
bronchial epithelial cell	CL:0002328	99.96	gold quality
cranial nerve II	UBERON:0000941	99.96	gold quality
subthalamic nucleus	UBERON:0001906	99.96	gold quality
ventricular zone	UBERON:0003053	99.96	gold quality
globus pallidus	UBERON:0001875	99.95	gold quality
medial globus pallidus	UBERON:0002477	99.95	gold quality
Brodmann (1909) area 23	UBERON:0013554	99.95	gold quality
trigeminal ganglion	UBERON:0001675	99.94	gold quality
dorsal plus ventral thalamus	UBERON:0001897	99.94	gold quality
substantia nigra pars compacta	UBERON:0001965	99.94	gold quality
substantia nigra pars reticulata	UBERON:0001966	99.94	gold quality
epithelium of bronchus	UBERON:0002031	99.94	gold quality
ventral tegmental area	UBERON:0002691	99.94	gold quality
entorhinal cortex	UBERON:0002728	99.94	gold quality
middle temporal gyrus	UBERON:0002771	99.94	gold quality
CA1 field of hippocampus	UBERON:0003881	99.94	gold quality
choroid plexus epithelium	UBERON:0003911	99.94	gold quality
embryo	UBERON:0000922	99.93	gold quality
pons	UBERON:0000988	99.93	gold quality
dorsal motor nucleus of vagus nerve	UBERON:0002870	99.93	gold quality
bronchus	UBERON:0002185	99.92	gold quality
lateral globus pallidus	UBERON:0002476	99.92	gold quality

Single-cell (SCXA)

Detected in 43 experiment(s), a significant marker in 30.

Experiment	Marker?	Max mean expression
E-MTAB-6911	yes	25534.47
E-MTAB-11121	yes	20881.50
E-MTAB-10485	yes	14656.55
E-MTAB-9154	yes	12077.51
E-MTAB-6701	yes	9371.29
E-MTAB-8221	yes	8996.05
E-MTAB-7407	yes	8127.75
E-GEOD-84465	yes	7531.15
E-GEOD-124472	yes	7279.96
E-MTAB-10018	yes	5788.27
E-MTAB-9906	yes	4833.44
E-HCAD-10	yes	4760.27
E-GEOD-81547	yes	4663.95
E-HCAD-25	yes	4352.89
E-GEOD-125970	yes	800.46

Regulation

Is transcription factor: no

Upstream regulators (CollecTRI, top): CEBPG, FOXJ1, GDNF, KLF6

miRNA regulators (miRDB)

7 targeting TUBA1A, top 30 by miRDB confidence (max_score; target_count = how many genes the miRNA targets in total — lower means more specific):

miRNA	Max score	Avg score	miRNA target_count
HSA-MIR-3065-3P	99.87	70.25	1407
HSA-MIR-221-3P	99.86	71.56	1329
HSA-MIR-222-3P	99.86	71.35	1337
HSA-MIR-5003-3P	99.85	69.29	2517
HSA-MIR-1179	99.71	68.70	1040
HSA-MIR-1303	99.65	69.77	1662
HSA-MIR-330-3P	99.41	69.95	2521

Functional genomics

ClinGen dosage: haploinsufficiency 0 (no evidence), triplosensitivity 0 (no evidence). ClinGen Gene Dosage Map

Literature-anchored findings (GeneRIF, showing 40)

• the dipole moments of each tubulin isotype may influence their functional characteristics within the cell, resulting in differences for MT assembly kinetics and stability (PMID:16941085)
• Mutations in alpha-tubulin in mice and humans that affect neuronal migration result in abnormal lamination of brain structures with associated behavioral deficits. (PMID:17218254)
• Given that Spastin engages the MT in two places, we propose that severing occurs by forces exerted on the C-terminal tail of tubulin, which results in a conformational change in tubulin, which releases it from the polymer. (PMID:17389232)
• Retrospective examination of MR images suggests that patients with TUBA1A mutations share not only cortical dysgenesis, but also cerebellar, hippocampal, corpus callosum, and brainstem abnormalities (PMID:17584854)
• Increased expression of tubulin alpha is associated with pulmonary sclerosing hemangioma (PMID:17914564)
• The diminished production of TUBA1A tubulin in R264C individuals is consistent with haploinsufficiency as a cause of the disease phenotype. (PMID:18199681)
• the TUBA1A phenotype is distinct from LIS1, DCX, RELN and ARX lissencephalies. Compared with the phenotypes of children mutated for TUBA1A, these prenatally diagnosed fetal cases occur at the severe end of the TUBA1A lissencephaly spectrum. (PMID:18669490)
• Missense mutations within the TUBA1A gene are associated with specific abnormalities in lissencephaly. (PMID:18728072)
• mutation analysis in the TUBA1A gene in 46 patients with classical lissencephaly. (PMID:18954413)
• This protein has been found differentially expressed in the Wernicke’s Area from patients with schizophrenia. (PMID:19405953)
• LIS-associated mutations of TUBA1A operate via diverse mechanisms that include disruption of binding sites for microtubule-associated proteins. (PMID:20466733)
• The expression of alpha-tubulin and MDR1 may play an important role in the development and progression of human non-small cell lung carcinoma. (PMID:20510079)
• Mutations in TUBA1A result in defects in the tubulin folding and heterodimer assembly. (PMID:20603323)
• Data show that IAV-infected cells contain elevated level of AcTub and alpha-tubulin. (PMID:21094644)
• Alpha2B-adrenergic receptor interaction with tubulin controls its transport from the endoplasmic reticulum to the cell surface (PMID:21357695)
• We report a mutation in TUBA1A as a cause of polymicrogyria. So far, all mutations in TUBA1A have occurred de novo, resulting in isolated cases. This article describes familial recurrence of TUBA1A mutations due to somatic mosaicism in a parent. (PMID:21403111)
• study describes a 14-month-old girl with TUBA1A mutation-associated lissencephaly, and summarize the clinical and neuroradiologic findings of 19 cases in the literature (PMID:22264709)
• Data show that Na(+),K(+)-ATPase activity was >50% lower and membrane-associated tubulin content was >200% higher in erythrocyte membranes from diabetic patients. (PMID:22565168)
• We described the clinical course and pathological findings in a child with TUBA1A mutation (PMID:22633752)
• Missense mutations in TUBA1A were found in 3 patients with polymicrogyria. (PMID:22948023)
• TUBA1A and TUBB2B coding regions have been sequenced that are associated with cortical malformations. (PMID:23361065)
• case provides new insight into the wide spectrum of disease phenotypes associated with TUBA1A mutation (PMID:23528852)
• Studies suggest that tubulin-interactive agents have the potential to play a significant role in the fight against cancer. (PMID:23818224)
• The present study confirms that mutations in tubulin genes are responsible for complex brain malformation. (PMID:24392928)
• These findings call attention to PKC-mediated phosphorylation of alpha-tubulin as a novel mechanism for controlling the dynamics of microtubules that result in cell movement. (PMID:24574051)
• These results demonstrated that SelP interacts with tubulin, alpha 1a (TUBA1A). (PMID:24914767)
• Lysine 40 acetylation of alpha-tubulin does not result in significant changes in kinesin-1’s landing rate or motility parameters. (PMID:24940781)
• This study show all foetuses with lissencephaly and cerebellar hypoplasia carried distinct TUBA1A mutations. (PMID:25059107)
• Data from studies using peptide fragment of alpha-tubulin (residues 31-49) suggest that Ser38 is crucial for substrate recognition by alpha-tubulin acetylase 1 (ATAT1); Asp39, Ile42, the glycine stretch (residues 43-45), and Asp46 are also involved. (PMID:25602620)
• Data suggest that tubulin functionally interact with the vimentin network in a cell-type specific manner. (PMID:26161965)
• Data show that tubulin phosphorylation and acetylation play important roles in the control of microtubule assembly and stability. (PMID:26165356)
• Studies indicate that alpha-tubulin acetylation and microtubule level is mainly governed by opposing actions of alpha-tubulin acetyltransferase 1 (ATAT1) and histone deacetylase 6 (HDAC6). (PMID:26227334)
• Data show that plasma membrane Ca(2+)-ATPase (PMCA) was associated with tubulin in normotensive and hypertensive erythrocytes. (PMID:26307527)
• data suggest that the TUBA1A mutations disrupting lateral interactions have pronounced dominant-negative effects on microtubule dynamics that are associated with the severe end of the lissencephaly spectrum (PMID:26493046)
• Long intergenic non-coding RNA APOC1P1-3 inhibits apoptosis by decreasing alpha-tubulin acetylation in breast cancer. (PMID:27228351)
• induced pluripotent stem cells (iPSCs) from the umbilical cord and peripheral blood of two lissencephaly patients with different clinical severities carrying alpha tubulin (TUBA1A) missense mutations, were generated. (PMID:27431206)
• Molecular docking studies revealed that 6f interacted and bound ef fi ciently with the colchicine-binding site of tubulin. In addition, 6f treatment induced G2/M cell cycle arrest dose-dependently and subsequently induced cell apoptosis (PMID:28440465)
• Results show that Tuba1a plays an essential, noncompensated role in neuronal saltatory migration in vivo and highlight the importance of microtubule flexibility in nucleus-centrosome coupling and neuronal-branching regulation during neuronal migration. (PMID:28687665)
• These data unequivocally show that free tubulin dimers represent the preferred HDAC6 substrate, with a K M value of 0.23 microM and a deacetylation rate over 1,500-fold higher than that of assembled microtubules. (PMID:28912522)
• A de novo heterozygous c.320A>G [p.(His 107 Arg)] mutation in TUBA1A was identified in a patient with microcephaly, epileptic seizures, and severe developmental delay. (PMID:29109381)

Cross-species orthologs

4 orthologs

Organism	Symbol	Gene ID
mus_musculus	Tuba1a	ENSMUSG00000072235
rattus_norvegicus		ENSRNOG00000070725
drosophila_melanogaster	alphaTub84B	FBGN0003884
drosophila_melanogaster	alphaTub84D	FBGN0003885

Paralogs (23): TUBG2 (ENSG00000037042), TUBE1 (ENSG00000074935), TUBA3D (ENSG00000075886), TUBB1 (ENSG00000101162), TUBB4A (ENSG00000104833), TUBD1 (ENSG00000108423), TUBA1B (ENSG00000123416), TUBA4A (ENSG00000127824), TUBG1 (ENSG00000131462), TUBB2A (ENSG00000137267), TUBB2B (ENSG00000137285), TUBA3E (ENSG00000152086), TUBA1C (ENSG00000167553), TUBB8B (ENSG00000173213), TUBB6 (ENSG00000176014), TUBAL3 (ENSG00000178462), TUBA8 (ENSG00000183785), TUBB4B (ENSG00000188229), TUBB (ENSG00000196230), TUBA3C (ENSG00000198033), TUBA4B (ENSG00000243910), TUBB3 (ENSG00000258947), TUBB8 (ENSG00000261456)

Protein

Protein identifiers

Tubulin alpha-1A chain — Q71U36 (reviewed: Q71U36)

Alternative names: Alpha-tubulin 3, Tubulin B-alpha-1, Tubulin alpha-3 chain

All UniProt accessions (5): A0A7P0Z4A1, Q71U36, F8VQQ4, F8VRZ4, F8W0F6

UniProt curated annotations — full annotation on UniProt →

Function. Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin.

Subunit / interactions. Dimer of alpha and beta chains. A typical microtubule is a hollow water-filled tube with an outer diameter of 25 nm and an inner diameter of 15 nM. Alpha-beta heterodimers associate head-to-tail to form protofilaments running lengthwise along the microtubule wall with the beta-tubulin subunit facing the microtubule plus end conferring a structural polarity. Microtubules usually have 13 protofilaments but different protofilament numbers can be found in some organisms and specialized cells. Component of sperm flagellar doublet microtubules.

Subcellular location. Cytoplasm. Cytoskeleton. Flagellum axoneme.

Tissue specificity. Expressed at a high level in fetal brain.

Post-translational modifications. Some glutamate residues at the C-terminus are polyglutamylated, resulting in polyglutamate chains on the gamma-carboxyl group. Polyglutamylation plays a key role in microtubule severing by spastin (SPAST). SPAST preferentially recognizes and acts on microtubules decorated with short polyglutamate tails: severing activity by SPAST increases as the number of glutamates per tubulin rises from one to eight, but decreases beyond this glutamylation threshold. Glutamylation is also involved in cilia motility. Some glutamate residues at the C-terminus are monoglycylated but not polyglycylated due to the absence of functional TTLL10 in human. Monoglycylation is mainly limited to tubulin incorporated into cilia and flagella axonemes, which is required for their stability and maintenance. Flagella glycylation controls sperm motility. Both polyglutamylation and monoglycylation can coexist on the same protein on adjacent residues, and lowering glycylation levels increases polyglutamylation, and reciprocally. Acetylation of alpha chains at Lys-40 is located inside the microtubule lumen. This modification has been correlated with increased microtubule stability, intracellular transport and ciliary assembly. Methylation of alpha chains at Lys-40 is found in mitotic microtubules and is required for normal mitosis and cytokinesis contributing to genomic stability. Nitration of Tyr-451 is irreversible and interferes with normal dynein intracellular distribution. Undergoes a tyrosination/detyrosination cycle, the cyclic removal and re-addition of a C-terminal tyrosine residue by the enzymes tubulin tyrosine carboxypeptidase (MATCAP1/KIAA0895L, VASH1 or VASH2) and tubulin tyrosine ligase (TTL), respectively. Tyrosination promotes microtubule interaction with CAP-Gly domain-containing proteins such as CLIP1, CLIP2 and DCTN1. Tyrosination regulates the initiation of dynein-dynactin motility via interaction with DCTN1, which brings the dynein-dynactin complex into contact with microtubules. In neurons, tyrosinated tubulins mediate the initiation of retrograde vesicle transport. Detyrosination is involved in metaphase plate congression by guiding chromosomes during mitosis: detyrosination promotes interaction with CENPE, promoting pole-proximal transport of chromosomes toward the equator. Detyrosination increases microtubules-dependent mechanotransduction in dystrophic cardiac and skeletal muscle. In cardiomyocytes, detyrosinated microtubules are required to resist to contractile compression during contraction: detyrosination promotes association with desmin (DES) at force-generating sarcomeres, leading to buckled microtubules and mechanical resistance to contraction.

Disease relevance. Lissencephaly 3 (LIS3) [MIM:611603] A classic type lissencephaly associated with psychomotor retardation and seizures. Features include agyria or pachygyria or laminar heterotopia, severe intellectual disability, motor delay, variable presence of seizures, and abnormalities of corpus callosum, hippocampus, cerebellar vermis and brainstem. The disease is caused by variants affecting the gene represented in this entry.

Similarity. Belongs to the tubulin family.

Isoforms (2)

UniProt ID	Names	Canonical?
Q71U36-1	1	yes
Q71U36-2	2

RefSeq proteins (3): NP_001257328, NP_001257329, NP_006000* (*=MANE)

Domains & families (InterPro)

ID	Name	Type
IPR000217	Tubulin	Family
IPR002452	Alpha_tubulin	Family
IPR003008	Tubulin_FtsZ_GTPase	Domain
IPR008280	Tub_FtsZ_C	Homologous_superfamily
IPR017975	Tubulin_CS	Conserved_site
IPR018316	Tubulin/FtsZ_2-layer-sand-dom	Domain
IPR023123	Tubulin_C	Homologous_superfamily
IPR036525	Tubulin/FtsZ_GTPase_sf	Homologous_superfamily
IPR037103	Tubulin/FtsZ-like_C	Homologous_superfamily

Pfam: PF00091, PF03953

Catalyzed reactions (Rhea), 1 shown:

• GTP + H2O = GDP + phosphate + H(+) (RHEA:19669)

UniProt features (74 total): helix 21, strand 15, binding site 9, sequence variant 9, modified residue 6, sequence conflict 4, turn 4, chain 2, site 1, region of interest 1, splice variant 1, active site 1

Structure

Experimental structures (PDB)

15 structures.

PDB	Method	Resolution (Å)
9WD9	ELECTRON MICROSCOPY	2.26
6J8F	X-RAY DIFFRACTION	2.28
9WD7	ELECTRON MICROSCOPY	2.34
9WDA	ELECTRON MICROSCOPY	2.35
9WDB	ELECTRON MICROSCOPY	2.39
22AK	ELECTRON MICROSCOPY	2.41
22AJ	ELECTRON MICROSCOPY	2.48
9OX7	ELECTRON MICROSCOPY	2.69
8SH7	ELECTRON MICROSCOPY	2.8
6WSL	ELECTRON MICROSCOPY	3.1
7UNG	ELECTRON MICROSCOPY	3.6
5JCO	ELECTRON MICROSCOPY	4
8J07	ELECTRON MICROSCOPY	4.1
7UN1	ELECTRON MICROSCOPY	6
7C1M	SOLUTION NMR

Predicted structure (AlphaFold)

Model	pLDDT	Fraction very-high
AF-Q71U36-F1	91.32	0.80

Functional residue map

Curated UniProt residues grouped by drug-discovery relevance — catalytic, ligand-binding, modification, and mutation-validated positions. Source: UniProtKB sequence features.

Catalytic / active sites (2): 451 (involved in polymerization); 254

Ligand- & substrate-binding residues (9): 179; 206; 228; 11; 71; 71; 140; 144; 145

Post-translational modifications (6): 40, 282, 439, 443, 445, 451

Function

Pathways and Gene Ontology

Reactome pathways

93 pathways

ID	Pathway
R-HSA-1445148	Translocation of SLC2A4 (GLUT4) to the plasma membrane
R-HSA-190840	Microtubule-dependent trafficking of connexons from Golgi to the plasma membrane
R-HSA-190861	Gap junction assembly
R-HSA-2132295	MHC class II antigen presentation
R-HSA-2467813	Separation of Sister Chromatids
R-HSA-2500257	Resolution of Sister Chromatid Cohesion
R-HSA-2565942	Regulation of PLK1 Activity at G2/M Transition
R-HSA-3371497	HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand
R-HSA-380259	Loss of Nlp from mitotic centrosomes
R-HSA-380270	Recruitment of mitotic centrosome proteins and complexes
R-HSA-380284	Loss of proteins required for interphase microtubule organization from the centrosome
R-HSA-380320	Recruitment of NuMA to mitotic centrosomes
R-HSA-389957	Prefoldin mediated transfer of substrate to CCT/TriC
R-HSA-389960	Formation of tubulin folding intermediates by CCT/TriC
R-HSA-389977	Post-chaperonin tubulin folding pathway
R-HSA-437239	Recycling pathway of L1
R-HSA-5610787	Hedgehog ‘off’ state
R-HSA-5620912	Anchoring of the basal body to the plasma membrane
R-HSA-5620920	Cargo trafficking to the periciliary membrane
R-HSA-5620924	Intraflagellar transport
R-HSA-5626467	RHO GTPases activate IQGAPs
R-HSA-5663220	RHO GTPases Activate Formins
R-HSA-6807878	COPI-mediated anterograde transport
R-HSA-6811434	COPI-dependent Golgi-to-ER retrograde traffic
R-HSA-6811436	COPI-independent Golgi-to-ER retrograde traffic
R-HSA-68877	Mitotic Prometaphase
R-HSA-8852276	The role of GTSE1 in G2/M progression after G2 checkpoint
R-HSA-8854518	AURKA Activation by TPX2
R-HSA-8955332	Carboxyterminal post-translational modifications of tubulin
R-HSA-9609690	HCMV Early Events

MSigDB gene sets: 807 (showing top): GOBP_MEMORY, GOBP_DENTATE_GYRUS_DEVELOPMENT, WU_APOPTOSIS_BY_CDKN1A_VIA_TP53, GOBP_HINDBRAIN_DEVELOPMENT, GOBP_RESPONSE_TO_NITROGEN_COMPOUND, BORCZUK_MALIGNANT_MESOTHELIOMA_UP, GOBP_METENCEPHALON_DEVELOPMENT, GOBP_COGNITION, GOBP_BEHAVIOR, CCAWYNNGAAR_UNKNOWN, REACTOME_ADAPTIVE_IMMUNE_SYSTEM, GOBP_FOREBRAIN_MORPHOGENESIS, GOBP_INTRACELLULAR_PROTEIN_TRANSPORT, REACTOME_CYTOKINE_SIGNALING_IN_IMMUNE_SYSTEM, GOBP_RESPONSE_TO_ACID_CHEMICAL

GO Biological Process (40): microtubule cytoskeleton organization (GO:0000226), mitotic cell cycle (GO:0000278), neuron migration (GO:0001764), startle response (GO:0001964), intracellular protein transport (GO:0006886), microtubule-based process (GO:0007017), centrosome cycle (GO:0007098), smoothened signaling pathway (GO:0007224), memory (GO:0007613), adult locomotory behavior (GO:0008344), visual learning (GO:0008542), response to mechanical stimulus (GO:0009612), glial cell differentiation (GO:0010001), gene expression (GO:0010467), dentate gyrus development (GO:0021542), cerebellar cortex morphogenesis (GO:0021696), pyramidal neuron differentiation (GO:0021859), cerebral cortex development (GO:0021987), flagellated sperm motility (GO:0030317), cytoskeleton-dependent intracellular transport (GO:0030705), response to tumor necrosis factor (GO:0034612), locomotory exploration behavior (GO:0035641), microtubule polymerization (GO:0046785), forebrain morphogenesis (GO:0048853), homeostasis of number of cells within a tissue (GO:0048873), regulation of synapse organization (GO:0050807), synapse organization (GO:0050808), cell division (GO:0051301), neuron apoptotic process (GO:0051402), motor behavior (GO:0061744), cellular response to calcium ion (GO:0071277), organelle transport along microtubule (GO:0072384), neuron projection arborization (GO:0140058), response to L-glutamate (GO:1902065), cytoskeleton organization (GO:0007010), locomotory behavior (GO:0007626), hippocampus development (GO:0021766), neurogenesis (GO:0022008), neuron differentiation (GO:0030182), adult behavior (GO:0030534)

GO Molecular Function (10): structural molecule activity (GO:0005198), structural constituent of cytoskeleton (GO:0005200), GTP binding (GO:0005525), hydrolase activity (GO:0016787), identical protein binding (GO:0042802), protein-containing complex binding (GO:0044877), metal ion binding (GO:0046872), protein heterodimerization activity (GO:0046982), nucleotide binding (GO:0000166), protein binding (GO:0005515)

GO Cellular Component (19): condensed chromosome (GO:0000793), nucleus (GO:0005634), cytoplasm (GO:0005737), cytosol (GO:0005829), microtubule (GO:0005874), axonemal microtubule (GO:0005879), plasma membrane (GO:0005886), cilium (GO:0005929), microtubule cytoskeleton (GO:0015630), neuromuscular junction (GO:0031594), sperm flagellum (GO:0036126), cytoplasmic ribonucleoprotein granule (GO:0036464), recycling endosome (GO:0055037), extracellular exosome (GO:0070062), cytoskeleton (GO:0005856), cytoplasmic microtubule (GO:0005881), motile cilium (GO:0031514), cell projection (GO:0042995), synapse (GO:0045202)

Reactome top-level categories

Rollup of top-15 pathways:

Category	Pathways
Assembly of the 9+0 primary cilium	3
Mitotic Prometaphase	2
Centrosome maturation	2
Cooperation of Prefoldin and TriC/CCT in actin and tubulin folding	2
Membrane Trafficking	1
Transport of connexons to the plasma membrane	1
Gap junction trafficking	1
Adaptive Immune System	1
Mitotic Anaphase	1
G2/M Transition	1
Cellular responses to stress	1
Loss of proteins required for interphase microtubule organization from the centrosome	1
Protein folding	1
L1CAM interactions	1
Signaling by Hedgehog	1

GO top-level categories

Rollup of top GO terms by namespace:

Category	Terms
cellular anatomical structure	3
cytoplasm	3
cytoskeleton organization	2
response to external stimulus	2
intracellular transport	2
anatomical structure development	2
cytoskeleton	2
binding	2
microtubule-based process	1
cell cycle	1
mitotic nuclear division	1
cell migration	1
generation of neurons	1
neuromuscular process	1
intracellular protein localization	1
protein transport	1
cellular process	1
cell cycle process	1
microtubule organizing center organization	1
cell surface receptor signaling pathway	1
learning or memory	1
locomotory behavior	1
adult behavior	1
visual behavior	1
associative learning	1
response to abiotic stimulus	1
cell differentiation	1
gliogenesis	1
macromolecule biosynthetic process	1
hippocampus development	1
anatomical structure morphogenesis	1
cerebellum morphogenesis	1
cerebellar cortex development	1
central nervous system neuron differentiation	1
pallium development	1
cilium-dependent cell motility	1
cilium movement involved in cell motility	1
sperm motility	1
molecular_function	1
structural molecule activity	1

Protein interactions and networks

STRING

0 interactions, top by confidence (×1000):

IntAct

487 interactions, top by confidence:

A	B	Type	Score
DNAJB11	HSPA5	psi-mi:“MI:0914”(association)	0.830
EGFR	TUBA1A	psi-mi:“MI:0915”(physical association)	0.750
VSX1	USP12	psi-mi:“MI:0914”(association)	0.730
MAPT	ANXA2	psi-mi:“MI:0914”(association)	0.720
TUBA1A	TUBB3	psi-mi:“MI:0914”(association)	0.710
TUBA1A	MAPT	psi-mi:“MI:0915”(physical association)	0.690
KLK5	DENND11	psi-mi:“MI:0914”(association)	0.640
TUBA1B	TXNDC9	psi-mi:“MI:0914”(association)	0.640
CLIP1	TUBA1A	psi-mi:“MI:0407”(direct interaction)	0.620
TUBA1A	TUBA4A	psi-mi:“MI:0914”(association)	0.610
TUBA1A	TUBA1A	psi-mi:“MI:0915”(physical association)	0.590
APP	TUBA1A	psi-mi:“MI:0915”(physical association)	0.560
HTT	TUBA1A	psi-mi:“MI:0915”(physical association)	0.560
TUBB	TUBA1A	psi-mi:“MI:0915”(physical association)	0.550
TUBB3	POTEF	psi-mi:“MI:0914”(association)	0.530
ANTXR1	POTEF	psi-mi:“MI:0914”(association)	0.530
ADAMTS4	MANBA	psi-mi:“MI:0914”(association)	0.530
LRP1	NME4	psi-mi:“MI:0914”(association)	0.530

BioGRID (949): TUBA1A (Affinity Capture-MS), TUBA1A (Affinity Capture-MS), TUBA1A (Affinity Capture-Western), FAM110C (Affinity Capture-Western), TUBA1A (Affinity Capture-Western), TUBA1A (Affinity Capture-MS), TUBA1A (Affinity Capture-MS), TUBA1A (Two-hybrid), TUBA1A (Affinity Capture-MS), TUBA1A (Affinity Capture-MS), TUBA1A (Affinity Capture-MS), TUBA1A (Affinity Capture-MS), TUBA1A (Affinity Capture-MS), TUBA1A (Affinity Capture-MS), TUBA1A (Affinity Capture-MS)

ESM2 similar proteins: A5A6J1, P02550, P02552, P05213, P05214, P06603, P06604, P06605, P08537, P09644, P0DPH7, P0DPH8, P18258, P18288, P30436, P34690, P36220, P41383, P52273, P68360, P68361, P68362, P68363, P68365, P68366, P68367, P68368, P68369, P68370, P68373, P81947, P81948, Q06331, Q28IX8, Q2HJ86, Q2XVP4, Q32KN8, Q3ZCJ7, Q4R538, Q52PV9

Diamond homologs: A0AAL4, A5A6J1, B9DGT7, B9DHQ0, O22347, O22348, O22349, P02550, P02552, P04105, P04106, P05213, P05214, P06603, P06604, P08537, P09204, P09205, P09243, P0DPH7, P0DPH8, P10872, P10873, P11139, P11237, P11480, P11481, P12543, P14640, P14641, P14642, P18258, P18288, P22275, P28268, P28287, P28752, P29511, P30436, P32255

SIGNOR signaling

8 interactions.

A	Effect	B	Mechanism
NUMA1	up-regulates	TUBA1A	binding
TTL	down-regulates	TUBA1A	tyrosination
“vincaleukoblastine sulfate”	“down-regulates activity”	TUBA1A	“chemical inhibition”
FOXJ1	“up-regulates quantity by expression”	TUBA1A	“transcriptional regulation”
“Elongator complex”	“up-regulates activity”	TUBA1A	acetylation
TUBA1A	up-regulates	Neuron_migration
GDNF	“down-regulates quantity by repression”	TUBA1A	“transcriptional regulation”
ATAT1	“up-regulates quantity by stabilization”	TUBA1A	acetylation

Enriched among interaction partners

Reactome pathways and GO biological processes over-represented among this gene’s 235 IntAct physical interaction partners (hypergeometric vs the genome-wide background, BH-FDR, gene-set size 15–500, ranked by fold). A functional readout of the neighbourhood — distinct from this gene’s own memberships above, and biased toward well-studied / hub proteins, so read it as themes rather than proof.

Reactome pathways:

Pathway	Partners	Fold	FDR
Microtubule-dependent trafficking of connexons from Golgi to the plasma membrane	10	35.3×	6e-12
Transport of connexons to the plasma membrane	10	35.3×	6e-12
Gap junction trafficking and regulation	11	34.0×	1e-12
Gap junction trafficking	11	34.0×	1e-12
RIP-mediated NFkB activation via ZBP1	7	30.5×	2e-08
Post-chaperonin tubulin folding pathway	9	27.8×	4e-10
Activation of AMPK downstream of NMDARs	11	27.2×	9e-12
RHO GTPases activate IQGAPs	12	27.0×	1e-12

GO biological processes:

GO term	Partners	Fold	FDR
non-canonical NF-kappaB signal transduction	5	20.9×	1e-03
positive regulation of axon extension	5	12.6×	9e-03
cytoplasmic microtubule organization	7	11.9×	9e-04
canonical NF-kappaB signal transduction	6	10.9×	4e-03
microtubule cytoskeleton organization	17	10.2×	1e-09
mitotic cell cycle	14	9.3×	3e-07

Disease & clinical

Clinical variants and AI predictions

ClinVar

435 variants total. Per-class counts are floors (≥ shown; pagination cap):

Classification	Count (floor)
Pathogenic	63
Likely pathogenic	89
Uncertain significance	90
Likely benign	90
Benign	14

Top pathogenic / likely-pathogenic (30)

Variant ID	HGVS	Classification
1065497	NM_006009.4(TUBA1A):c.1288_1302del (p.Lys430_Glu434del)	Pathogenic
1164064	NM_006009.4(TUBA1A):c.431G>T (p.Gly144Val)	Pathogenic
1172808	NM_006009.4(TUBA1A):c.50G>A (p.Gly17Asp)	Pathogenic
1211068	NM_006009.4(TUBA1A):c.268G>C (p.Glu90Gln)	Pathogenic
1211836	NM_006009.4(TUBA1A):c.1181A>G (p.Lys394Arg)	Pathogenic
1330376	NM_006009.4(TUBA1A):c.656T>C (p.Ile219Thr)	Pathogenic
1330377	NM_006009.4(TUBA1A):c.1264C>A (p.Arg422Ser)	Pathogenic
160147	NM_006009.4(TUBA1A):c.1205G>T (p.Arg402Leu)	Pathogenic
160167	NM_006009.4(TUBA1A):c.986A>G (p.Asn329Ser)	Pathogenic
1686683	NM_006009.4(TUBA1A):c.1216C>T (p.His406Tyr)	Pathogenic
2446561	NM_006009.4(TUBA1A):c.667A>G (p.Thr223Ala)	Pathogenic
2637677	NM_006009.4(TUBA1A):c.637_640del (p.Cys213fs)	Pathogenic
2664153	NM_006009.4(TUBA1A):c.303T>A (p.Asn101Lys)	Pathogenic
3063674	NM_006009.4(TUBA1A):c.1225G>T (p.Val409Phe)	Pathogenic
3255105	NM_006009.4(TUBA1A):c.4C>T (p.Arg2Cys)	Pathogenic
3340611	NM_006009.4(TUBA1A):c.167C>G (p.Thr56Arg)	Pathogenic
3694178	NM_006009.4(TUBA1A):c.236G>C (p.Arg79Pro)	Pathogenic
381537	NM_006009.4(TUBA1A):c.79G>C (p.Glu27Gln)	Pathogenic
3906528	NM_006009.4(TUBA1A):c.661C>T (p.Arg221Cys)	Pathogenic
4072026	NM_006009.4(TUBA1A):c.955T>A (p.Tyr319Asn)	Pathogenic
4074869	NM_006009.4(TUBA1A):c.788C>T (p.Pro263Leu)	Pathogenic
438298	NM_006009.4(TUBA1A):c.1177C>T (p.His393Tyr)	Pathogenic
4526974	NM_006009.4(TUBA1A):c.466C>T (p.Arg156Cys)	Pathogenic
4685070	NM_006009.4(TUBA1A):c.465A>C (p.Glu155Asp)	Pathogenic
4745169	NM_006009.4(TUBA1A):c.1160C>A (p.Ala387Asp)	Pathogenic
4795427	NM_006009.4(TUBA1A):c.893C>T (p.Pro298Leu)	Pathogenic
488628	NM_006009.4(TUBA1A):c.1169G>A (p.Arg390His)	Pathogenic
520585	NM_006009.4(TUBA1A):c.283G>T (p.Gly95Cys)	Pathogenic
625472	NM_006009.4(TUBA1A):c.163G>A (p.Glu55Lys)	Pathogenic
625474	NM_006009.4(TUBA1A):c.629A>G (p.Tyr210Cys)	Pathogenic

SpliceAI

395 predictions. Top by Δscore:

Variant	Effect	Δscore
12:49185986:TCGGC:T	acceptor_gain	1.0000
12:49185987:CGGC:C	acceptor_gain	1.0000
12:49185987:CGGCC:C	acceptor_gain	1.0000
12:49185988:GGC:G	acceptor_gain	1.0000
12:49185989:GC:G	acceptor_gain	1.0000
12:49185990:CC:C	acceptor_gain	1.0000
12:49185991:C:CC	acceptor_gain	1.0000
12:49185993:A:AC	acceptor_gain	1.0000
12:49185993:A:C	acceptor_gain	1.0000
12:49185997:C:CT	acceptor_gain	1.0000
12:49185998:A:T	acceptor_gain	1.0000
12:49186305:CATA:C	donor_loss	1.0000
12:49186306:ATAC:A	donor_loss	1.0000
12:49186308:A:AC	donor_gain	1.0000
12:49186308:ACCAG:A	donor_gain	1.0000
12:49186309:C:CT	donor_gain	1.0000
12:49186309:CCA:C	donor_gain	1.0000
12:49186309:CCAG:C	donor_gain	1.0000
12:49186309:CCAGC:C	donor_gain	1.0000
12:49186458:TCTG:T	acceptor_loss	1.0000
12:49186459:C:CC	acceptor_gain	1.0000
12:49186467:CATGA:C	acceptor_gain	1.0000
12:49186468:A:AC	acceptor_gain	1.0000
12:49186468:A:C	acceptor_gain	1.0000
12:49186468:A:T	acceptor_gain	1.0000
12:49186471:A:AC	acceptor_gain	1.0000
12:49186471:A:C	acceptor_gain	1.0000
12:49186604:AACTC:A	donor_loss	1.0000
12:49186605:ACTCA:A	donor_loss	1.0000
12:49186606:CTCA:C	donor_loss	1.0000

AlphaMissense

2969 scored. Top likely-pathogenic:

Variant	Protein change	am_pathogenicity
12:49185072:A:G	Y432H	1.000
12:49185074:T:A	D431V	1.000
12:49185075:C:G	D431H	1.000
12:49185083:A:G	L428P	1.000
12:49185083:A:T	L428H	1.000
12:49185101:C:G	R422P	1.000
12:49185102:G:T	R422S	1.000
12:49185104:G:T	A421D	1.000
12:49185105:C:G	A421P	1.000
12:49185112:A:C	F418L	1.000
12:49185112:A:T	F418L	1.000
12:49185113:A:C	F418C	1.000
12:49185113:A:G	F418S	1.000
12:49185114:A:G	F418L	1.000
12:49185120:C:G	G416R	1.000
12:49185132:C:A	G412W	1.000
12:49185132:C:G	G412R	1.000
12:49185132:C:T	G412R	1.000
12:49185147:A:G	W407R	1.000
12:49185147:A:T	W407R	1.000
12:49185150:G:C	H406D	1.000
12:49185152:A:T	V405D	1.000
12:49185154:A:C	F404L	1.000
12:49185154:A:T	F404L	1.000
12:49185155:A:C	F404C	1.000
12:49185155:A:G	F404S	1.000
12:49185156:A:G	F404L	1.000
12:49185156:A:T	F404I	1.000
12:49185158:G:T	A403D	1.000
12:49185161:C:G	R402P	1.000

dbSNP variants (sampled 300 via entrez): RS1000599828 (12:49186800 C>T), RS1000998665 (12:49188715 C>G,T), RS1001031347 (12:49188420 G>A), RS1001712334 (12:49184869 C>T), RS1001817626 (12:49189848 G>C), RS1002036799 (12:49190238 A>G), RS1002468880 (12:49189369 G>A,C), RS1004440499 (12:49190199 G>A,T), RS1005367439 (12:49187612 A>G), RS1006369928 (12:49188997 T>G), RS1006574690 (12:49187713 T>A,C,G), RS1006602408 (12:49187411 T>A), RS1006973410 (12:49190573 G>T), RS1007573023 (12:49189113 A>C,G), RS1011204421 (12:49189885 A>G)

Disease associations

OMIM: gene MIM:602529 | disease phenotypes: MIM:611603, MIM:607432, MIM:608099, MIM:217990, MIM:219050, MIM:220200, MIM:135700, MIM:213000

GenCC curated gene-disease

Disease	Classification	Inheritance
lissencephaly due to TUBA1A mutation	Definitive	Autosomal dominant
congenital fibrosis of extraocular muscles	Strong	Autosomal dominant
tubulinopathy-associated dysgyria	Supportive	Autosomal dominant

ClinGen Gene-Disease Validity (1)

Expert-panel classifications — Definitive > Strong > Moderate > Limited > Disputed > Refuted.

Disease	Classification	Inheritance
tubulinopathy	Definitive	AD

Mondo (20): lissencephaly due to TUBA1A mutation (MONDO:0012703), cerebral palsy (MONDO:0006497), lissencephaly due to LIS1 mutation (MONDO:0011830), congenital nervous system disorder (MONDO:0002320), tubulinopathy-associated dysgyria (MONDO:0018763), lissencephaly spectrum disorders (MONDO:0018838), infantile spasms (MONDO:0018097), tubulinopathy (MONDO:0100153), autosomal recessive limb-girdle muscular dystrophy type 2D (MONDO:0011968), neurodevelopmental disorder (MONDO:0700092), corpus callosum, agenesis of (MONDO:0009022), cryptorchidism (MONDO:0009047), lissencephaly type 3 (MONDO:0015148), bilateral perisylvian polymicrogyria (MONDO:0020340), Dandy-Walker syndrome (MONDO:0009072)

Orphanet (17): Lissencephaly due to TUBA1A mutation (Orphanet:171680), Lissencephaly due to LIS1 mutation (Orphanet:95232), Tubulinopathy-associated dysgyria (Orphanet:467166), Lissencephaly (Orphanet:48471), West syndrome (Orphanet:3451), Infantile epileptic spasms syndrome (Orphanet:697160), Alpha-sarcoglycan-related limb-girdle muscular dystrophy R3 (Orphanet:62), Isolated corpus callosum agenesis (Orphanet:200), Lissencephaly type 3 (Orphanet:102011), Bilateral perisylvian polymicrogyria (Orphanet:98889), Isolated Dandy-Walker malformation (Orphanet:217), Rare genetic intellectual disability (Orphanet:183757), Polymicrogyria (Orphanet:35981), Congenital fibrosis of extraocular muscles (Orphanet:45358), Isolated cerebellar agenesis (Orphanet:1398)

HPO phenotypes

110 total (30 of 110 shown, HPO-id order):

HPO	Term
HP:0000006	Autosomal dominant inheritance
HP:0000028	Cryptorchidism
HP:0000044	Hypogonadotropic hypogonadism
HP:0000175	Cleft palate
HP:0000252	Microcephaly
HP:0000256	Macrocephaly
HP:0000308	Microretrognathia
HP:0000316	Hypertelorism
HP:0000347	Micrognathia
HP:0000358	Posteriorly rotated ears
HP:0000473	Torticollis
HP:0000476	Cystic hygroma
HP:0000486	Strabismus
HP:0000508	Ptosis
HP:0000512	Abnormal electroretinogram
HP:0000518	Cataract
HP:0000539	Abnormality of refraction
HP:0000542	Impaired ocular adduction
HP:0000565	Esotropia
HP:0000577	Exotropia
HP:0000609	Optic nerve hypoplasia
HP:0000616	Miosis
HP:0000639	Nystagmus
HP:0000646	Amblyopia
HP:0000657	Oculomotor apraxia
HP:0001059	Pterygium
HP:0001249	Intellectual disability
HP:0001250	Seizure
HP:0001251	Ataxia
HP:0001252	Hypotonia

GWAS associations

2 associations (top):

Study	Trait	p-value
GCST008574_4	Composite immunoglobulin trait (IgG/IgM)	3.000000e-06
GCST010703_9	Brain morphology (MOSTest)	8.000000e-10

EFO canonical traits (1, from GWAS)

EFO ID	Trait name
EFO:0004346	neuroimaging measurement

MeSH disease descriptors (12)

Descriptor	Name	Tree numbers
D061085	Agenesis of Corpus Callosum	C10.500.034; C16.131.666.034; C23.300.008
D002547	Cerebral Palsy	C10.228.140.140.254
D003456	Cryptorchidism	C12.100.500.829.258; C12.200.294.829.258; C12.200.706.258; C12.800.258; C16.131.939.258; C19.391.829.258
D003616	Dandy-Walker Syndrome	C10.228.140.252.300; C10.228.140.602.500; C10.500.205; C16.131.666.205
D008607	Intellectual Disability	C10.597.606.360; C23.888.592.604.646; F01.700.687; F03.625.539
D054082	Lissencephaly	C10.500.507.450.499; C16.131.666.507.450.499
D009069	Movement Disorders	C10.228.662
D065886	Neurodevelopmental Disorders	F03.625
D065706	Polymicrogyria	C10.500.507.500.500; C16.131.666.507.500.500
C562568	Cerebellar Hypoplasia (supp.)
C566908	Lissencephaly 3 (supp.)
C580012	congenital fibrosis of the extraocular muscles (supp.)

Drugs & pharmacology

Drug and pharmacology data

Is drug target: yes

ChEMBL targets (5): CHEMBL2095182 (PROTEIN COMPLEX GROUP), CHEMBL3661 (SINGLE PROTEIN), CHEMBL3832941 (PROTEIN FAMILY), CHEMBL3885647 (PROTEIN COMPLEX GROUP), CHEMBL6067579 (PROTEIN-PROTEIN INTERACTION)

Molecules with ChEMBL bioactivity

22 molecules (phase ≥1), by development phase (incl. off-target/promiscuous compounds). Patent mentions across the top 20 by phase: 1,641,397 (via chembl_molecule»patent_compound — counts attach to the compound, not the gene–compound relationship, so off-target/promiscuous molecules can dominate).

Molecule	Name	Phase	Patents
CHEMBL107	COLCHICINE	4	93,932
CHEMBL159	VINBLASTINE	4	412,636
CHEMBL33	LEVOFLOXACIN ANHYDROUS	4	43,403
CHEMBL3545252	DOCETAXEL	4	1,009
CHEMBL364713	NOSCAPINE	4	14,987
CHEMBL378544	VINBLASTINE SULFATE	4	32,829
CHEMBL428647	PACLITAXEL	4	332,542
CHEMBL5315124	LEVOFLOXACIN	4	189
CHEMBL553025	VINORELBINE	4	142,159
CHEMBL571546	TIRBANIBULIN	4	1,192
CHEMBL61	PODOFILOX	4	37,640
CHEMBL90555	VINCRISTINE	4	268,031
CHEMBL92	DOCETAXEL ANHYDROUS	4	196,686
CHEMBL94657	PATUPILONE	3	14,934
CHEMBL20684	ABT-751	2	2,238
CHEMBL292702	MAYTANSINE	2	9,300
CHEMBL39541	DOLASTATIN-10	2	1,380
CHEMBL49642	INDIBULIN	2	963
CHEMBL528271	PARBENDAZOLE	2	6,102
CHEMBL9514	NOCODAZOLE	2	29,245
CHEMBL1232461	MOLIBRESIB	2
CHEMBL246600	COMBRETASTATIN	1

PharmGKB: 1 entry (VIP=true, CPIC=false)

GtoPdb / IUPHAR curated pharmacology

(IUPHAR/BPS Guide to Pharmacology — expert-curated)

Target class: other protein — Tubulins

ChEMBL bioactivities

1161 potent at pChembl≥5 of 1312 total, top 50 by pChembl (potency: 10 = 0.1 nM, 6 = 1 µM).

pChembl	Type	Value	Unit	Molecule
10.26	IC50	0.0551	nM	CHEMBL5194719
9.75	IC50	0.176	nM	CHEMBL5203711
9.51	IC50	0.308	nM	VINORELBINE
9.30	IC50	0.5	nM	DOLASTATIN-10
8.92	IC50	1.2	nM	CHEMBL5169466
8.85	IC50	1.4	nM	CHEMBL4575066
8.74	IC50	1.8	nM	PATUPILONE
8.59	IC50	2.6	nM	CHEMBL2024544
8.52	Ki	3	nM	COMBRETASTATIN A4
8.52	IC50	3	nM	COMBRETASTATIN A4
8.52	IC50	3	nM	DOLASTATIN-10
8.52	Kd	3	nM	CHEMBL5410715
8.52	IC50	3	nM	COLCHICINE
8.46	IC50	3.5	nM	PATUPILONE
8.38	IC50	4.2	nM	CHEMBL5197739
8.27	IC50	5.4	nM	CHEMBL5280519
8.22	IC50	6	nM	CHEMBL498271
8.05	EC50	9	nM	COMBRETASTATIN A4
8.01	EC50	9.8	nM	COMBRETASTATIN A4
8.01	IC50	9.77	nM	CHEMBL4778826
8.00	Ki	10	nM	CHEMBL381852
8.00	IC50	10	nM	CHEMBL204241
7.96	Kd	11	nM	CHEMBL5611905
7.89	IC50	12.9	nM	COMBRETASTATIN A4
7.85	Kd	14	nM	MAYTANSINE
7.70	IC50	20	nM	CHEMBL2369093
7.70	Ki	20	nM	CHEMBL369927
7.70	IC50	20	nM	CHEMBL5183440
7.70	Kd	20	nM	CHEMBL5613121
7.64	IC50	23	nM	COMBRETASTATIN A4
7.62	EC50	24	nM	CHEMBL4250191
7.58	IC50	26	nM	PIRONETIN
7.52	IC50	30	nM	CHEMBL381122
7.52	IC50	30	nM	COMBRETASTATIN A4
7.52	IC50	30	nM	CHEMBL203062
7.52	IC50	30	nM	CHEMBL204710
7.51	EC50	31	nM	PACLITAXEL
7.40	EC50	40	nM	CHEMBL1688184
7.35	EC50	45	nM	CHEMBL4239716
7.34	IC50	46	nM	CHEMBL374257
7.33	Kd	47	nM	CHEMBL5542101
7.30	Ki	50	nM	CHEMBL196966
7.30	EC50	50	nM	CHEMBL1688183
7.30	EC50	50	nM	CHEMBL1688189
7.29	Kd	51	nM	CHEMBL5614306
7.28	EC50	53	nM	CHEMBL4241638
7.24	Kd	58	nM	COLCHICINE
7.22	Ki	60	nM	CHEMBL198522
7.16	IC50	70	nM	CHEMBL2369084
7.16	IC50	70	nM	VINBLASTINE

PubChem BioAssay actives

1090 with measured affinity, of 5790 total; 50 most potent distinct compounds. Largely complementary to BindingDB; screening values are coarse (µM, 4 dp), so sub-nM hits tie at the floor.

Compound	Assay	Type	Value	Unit
(Z)-1-[4-bromo-2-(4-fluorophenyl)-1-benzofuran-7-yl]-3-(4-methoxyphenyl)prop-2-en-1-one	1882651: Inhibition of tubulin polymerization (unknown origin) measured every 3 secs for 1 hr by spectroflourimetric analysis	ic50	0.0001	uM
(Z)-1-[4-bromo-2-(4-fluorophenyl)-1-benzofuran-7-yl]-3-[4-(trifluoromethoxy)phenyl]prop-2-en-1-one	1882651: Inhibition of tubulin polymerization (unknown origin) measured every 3 secs for 1 hr by spectroflourimetric analysis	ic50	0.0002	uM
Vinorelbine	1993632: Inhibition of tubulin polymerization (unknown origin)	ic50	0.0003	uM
(2S)-2-[[(2S)-2-(dimethylamino)-3-methylbutanoyl]amino]-N-[(3R,4S,5S)-3-methoxy-1-[(2S)-2-[(1R,2R)-1-methoxy-2-methyl-3-oxo-3-[[(1S)-2-phenyl-1-(1,3-thiazol-2-yl)ethyl]amino]propyl]pyrrolidin-1-yl]-5-methyl-1-oxoheptan-4-yl]-N,3-dimethylbutanamide	270819: Inhibition of tubulin polymerization	ic50	0.0005	uM
(2S)-2-[[(2S)-2-(dimethylamino)-3-methylbutanoyl]amino]-N-[(3R,4S,5S)-3-methoxy-1-[(2S)-2-[(1R,2R)-1-methoxy-2-methyl-3-oxo-3-(2-pyridin-2-ylethylamino)propyl]pyrrolidin-1-yl]-5-methyl-1-oxoheptan-4-yl]-N,3-dimethylbutanamide	1896115: Binding affinity to tubulin (unknown origin)	ic50	0.0012	uM
(3Z,6Z)-3-[(5-tert-butyl-1H-imidazol-4-yl)methylidene]-6-phenacylidenepiperazine-2,5-dione	1587857: Inhibition of tubulin polymerization (unknown origin)	ic50	0.0014	uM
(3Z,6Z)-3-[(5-tert-butyl-1H-imidazol-4-yl)methylidene]-6-[(2,5-difluorophenyl)methylidene]piperazine-2,5-dione	1587857: Inhibition of tubulin polymerization (unknown origin)	ic50	0.0026	uM
3-hydroxy-2-[N-[2-(methoxymethyl)-1-benzofuran-7-yl]-C-methylcarbonimidoyl]-5-phenylcyclohex-2-en-1-one	2034736: Displacement of fluorescent probe (R)-(+)-ethyl 5-amino2-methyl-1,2-dihydro-3-phenylpyrido[3,4-b]pyrazin-7-ylcarbamate from tubulin colchicine binding site (unknown origin) assessed as dissociation constant	kd	0.0030	uM
2-methoxy-5-[(Z)-2-(3,4,5-trimethoxyphenyl)ethenyl]phenol	1862628: Inhibition of tubulin polymerization in human HeLa cells assessed as microtubule network polymerization after 30 mins by immunofluorescence analysis	ic50	0.0030	uM
Colchicine	2074087: Inhibition of microtubule polymerization in human K562 cells measured for 60 mins by fluorescence based analysis	ic50	0.0030	uM
(1S,3S,7S,10R,11S,12S,16R)-7,11-dihydroxy-8,8,10,12,16-pentamethyl-3-[(E)-1-(2-methyl-1,3-thiazol-4-yl)prop-1-en-2-yl]-4,17-dioxabicyclo[14.1.0]heptadecane-5,9-dione	1408257: Inhibition of tubulin polymerization in human MCF7 cells assessed as induction of mitotic arrest	ic50	0.0035	uM
tert-butyl (3R,4S,5S)-4-[[(2S)-2-[[(2S)-2-(dimethylamino)-3-methylbutanoyl]amino]-3-methylbutanoyl]-methylamino]-3-methoxy-5-methylheptanoate	1896110: Inhibition of tubulin (unknown origin) polymerization assessed as reduction in microtubule formation measured for 20 mins by spectrophotometric analysis	ic50	0.0042	uM
3-methoxy-6-[4-(3,4,5-trimethoxyphenyl)-1H-pyrazol-5-yl]benzene-1,2-diol	1929685: Inhibition of tubulin polymerization in human SH-SY5Y cells incubated for 24 hrs by SDS-PAGE based analysis	ic50	0.0054	uM
2-methoxy-5-[1-(3,4,5-trimethoxyphenyl)ethenyl]phenol	1862628: Inhibition of tubulin polymerization in human HeLa cells assessed as microtubule network polymerization after 30 mins by immunofluorescence analysis	ic50	0.0060	uM
(E)-1-[1-(4-chlorophenyl)-5-methyltriazol-4-yl]-3-(3,4-dimethoxyphenyl)prop-2-en-1-one	1689700: Inhibition of Tubulin in human RPMI-8226 cells incubated for 2 hrs by ELISA	ic50	0.0098	uM
N-(1,3-benzodioxol-5-yl)-5-[2-(3,5-dimethoxyphenoxy)-3-pyridinyl]-1H-1,2,4-triazol-3-amine	256882: Displacement of [3H]colchicine from tubulin	ki	0.0100	uM
N-(2,3-dihydro-1,4-benzodioxin-6-yl)-5-[2-(pyridin-2-ylmethylamino)phenyl]-1,3-oxazol-2-amine	261214: Displacement of [3H]colchicine from tubulin at 65 nM	ic50	0.0100	uM
[(1S,2R,3S,5R,6S,16E,18E,20R,21S)-11-chloro-21-hydroxy-12,20-dimethoxy-2,5,9,16-tetramethyl-8,23-dioxo-4,24-dioxa-9,22-diazatetracyclo[19.3.1.110,14.03,5]hexacosa-10,12,14(26),16,18-pentaen-6-yl] acetate	2126113: Displacement of fluorescent Maytansine probe from tubulin (unknown origin) assessed as dissociation constant by competitive binding based fluorescence anisotropy	kd	0.0110	uM
[(1S,2R,3S,5S,6S,16E,18E,20R,21S)-11-chloro-21-hydroxy-12,20-dimethoxy-2,5,9,16-tetramethyl-8,23-dioxo-4,24-dioxa-9,22-diazatetracyclo[19.3.1.110,14.03,5]hexacosa-10,12,14(26),16,18-pentaen-6-yl] (2S)-2-[acetyl(methyl)amino]propanoate	2126113: Displacement of fluorescent Maytansine probe from tubulin (unknown origin) assessed as dissociation constant by competitive binding based fluorescence anisotropy	kd	0.0140	uM
N-(2,3-dihydro-1,4-benzodioxin-6-yl)-5-[2-(3,5-dimethoxyphenoxy)-3-pyridinyl]-1H-1,2,4-triazol-3-amine	256882: Displacement of [3H]colchicine from tubulin	ki	0.0200	uM
methyl (13S,15S,17S)-13-[(1R,9R,10S,11R,12R,19R)-10-(1-diethoxyphosphorylhexylcarbamoyl)-12-ethyl-10,11-dihydroxy-5-methoxy-8-methyl-8,16-diazapentacyclo[10.6.1.01,9.02,7.016,19]nonadeca-2,4,6,13-tetraen-4-yl]-17-ethyl-17-hydroxy-1,11-diazatetracyclo[13.3.1.04,12.05,10]nonadeca-4(12),5,7,9-tetraene-13-carboxylate	214333: The compound tested for the inhibition of tubulin polymerization.	ic50	0.0200	uM
(E)-3-[5-[(2-cyanoquinolin-4-yl)-methylamino]-2-methoxyphenyl]-N-hydroxyprop-2-enamide	1862628: Inhibition of tubulin polymerization in human HeLa cells assessed as microtubule network polymerization after 30 mins by immunofluorescence analysis	ic50	0.0200	uM
[(1S,2R,3S,5R,6S,16E,18E,20R,21S)-11-chloro-21-hydroxy-12,20-dimethoxy-2,5,9,16-tetramethyl-8,23-dioxo-4,24-dioxa-9,22-diazatetracyclo[19.3.1.110,14.03,5]hexacosa-10,12,14(26),16,18-pentaen-6-yl] hept-6-ynoate	2126113: Displacement of fluorescent Maytansine probe from tubulin (unknown origin) assessed as dissociation constant by competitive binding based fluorescence anisotropy	kd	0.0200	uM
N-(4-methoxyphenyl)-N,5-dimethylfuro[2,3-d]pyrimidin-4-amine	1635267: Induction of microtubule depolymerization in human A10 cells incubated for 18 hrs by indirect immunofluorescence analysis	ec50	0.0240	uM
(2R,3R)-3-ethyl-2-[(E,2R,3S,4R,5S)-2-hydroxy-4-methoxy-3,5-dimethylnon-7-enyl]-2,3-dihydropyran-6-one	1572465: Inhibition of tubulin alpha in human A2780 cells assessed as reduction in cell growth	ic50	0.0260	uM
N-(2,3-dihydro-1,4-benzodioxin-6-yl)-5-[2-(pyridin-3-ylmethylamino)-3-pyridinyl]-1,3,4-oxadiazol-2-amine	261214: Displacement of [3H]colchicine from tubulin at 65 nM	ic50	0.0300	uM
N-(1,3-benzodioxol-5-yl)-5-[2-(pyridin-4-ylmethylamino)-3-pyridinyl]-1,3,4-oxadiazol-2-amine	261214: Displacement of [3H]colchicine from tubulin at 65 nM	ic50	0.0300	uM
N-(1,3-benzodioxol-5-yl)-5-[2-(pyridin-2-ylmethylamino)-3-pyridinyl]-1,3,4-oxadiazol-2-amine	261214: Displacement of [3H]colchicine from tubulin at 65 nM	ic50	0.0300	uM
Paclitaxel	260235: Effect on induction of mitotic arrest by phosphohistone H3 (pH3) assay	ec50	0.0310	uM
6-(3-chloro-6,11,11-trioxobenzo[b][1,4]benzothiazepin-5-yl)-N-hydroxyhexanamide	580932: Inhibition of HDAC activity in human NB4 cells assessed as acetylated tubulin after 24 hrs by Western blot analysis	ec50	0.0400	uM
N,5-dimethyl-N-(4-methylsulfanylphenyl)furo[2,3-d]pyrimidin-4-amine	1635267: Induction of microtubule depolymerization in human A10 cells incubated for 18 hrs by indirect immunofluorescence analysis	ec50	0.0450	uM
[7-(3-hydroxyprop-1-ynyl)-6-methoxy-2H-indazol-3-yl]-(3,4,5-trimethoxyphenyl)methanone	280080: Displacement of [3H]colchicine from tubulin in MCF7 cells	ic50	0.0460	uM
(3S,10R,13E,16S)-10-[(3-chloro-4-methoxyphenyl)methyl]-6,6-dimethyl-3-(2-methylpropyl)-16-[(1S)-1-[(2R,3S)-3-phenyloxiran-2-yl]ethyl]-1,4-dioxa-8,11-diazacyclohexadec-13-ene-2,5,9,12-tetrone	2061859: Binding affinity to tubulin (unknown origin) assessed as dissociation constant by SPR analysis	kd	0.0470	uM
N-hydroxy-6-(3-methoxy-6,11,11-trioxobenzo[b][1,4]benzothiazepin-5-yl)hexanamide	580932: Inhibition of HDAC activity in human NB4 cells assessed as acetylated tubulin after 24 hrs by Western blot analysis	ec50	0.0500	uM
N-hydroxy-6-(6,11,11-trioxobenzo[b][1,4]benzothiazepin-5-yl)hexanamide	580932: Inhibition of HDAC activity in human NB4 cells assessed as acetylated tubulin after 24 hrs by Western blot analysis	ec50	0.0500	uM
5-[2-(3,5-dimethoxyphenoxy)-3-pyridinyl]-N-(3-methoxyphenyl)-1H-1,2,4-triazol-3-amine	256882: Displacement of [3H]colchicine from tubulin	ki	0.0500	uM
[(1S,2R,3S,5R,6S,16E,18E,20R,21S)-11-chloro-21-hydroxy-12,20-dimethoxy-2,5,9,16-tetramethyl-8,23-dioxo-4,24-dioxa-9,22-diazatetracyclo[19.3.1.110,14.03,5]hexacosa-10,12,14(26),16,18-pentaen-6-yl] benzoate	2126113: Displacement of fluorescent Maytansine probe from tubulin (unknown origin) assessed as dissociation constant by competitive binding based fluorescence anisotropy	kd	0.0510	uM
N-ethyl-N-(4-methoxyphenyl)-5-methylfuro[2,3-d]pyrimidin-4-amine	1635267: Induction of microtubule depolymerization in human A10 cells incubated for 18 hrs by indirect immunofluorescence analysis	ec50	0.0530	uM
3-[3-(1,3-benzodioxol-5-ylamino)-1H-1,2,4-triazol-5-yl]-N-(3,5-dimethoxyphenyl)pyridin-2-amine	256882: Displacement of [3H]colchicine from tubulin	ki	0.0600	uM
Vinblastine	214333: The compound tested for the inhibition of tubulin polymerization.	ic50	0.0700	uM
methyl (13S,15S,17S)-13-[(1R,9R,10S,11R,12R,19R)-10-[(1-diethoxyphosphoryl-2-phenylethyl)carbamoyl]-12-ethyl-10,11-dihydroxy-5-methoxy-8-methyl-8,16-diazapentacyclo[10.6.1.01,9.02,7.016,19]nonadeca-2,4,6,13-tetraen-4-yl]-17-ethyl-17-hydroxy-1,11-diazatetracyclo[13.3.1.04,12.05,10]nonadeca-4(12),5,7,9-tetraene-13-carboxylate	214333: The compound tested for the inhibition of tubulin polymerization.	ic50	0.0700	uM
N-(2,3-dihydro-1,4-benzodioxin-6-yl)-5-[3-(pyridin-2-ylmethylamino)thiophen-2-yl]-1,3,4-oxadiazol-2-amine	261214: Displacement of [3H]colchicine from tubulin at 65 nM	ic50	0.0750	uM
methyl (13S,15S,17S)-13-[(1R,9R,10S,11R,12R,19R)-10-[[(1S)-1-diethoxyphosphorylethyl]carbamoyl]-12-ethyl-10,11-dihydroxy-5-methoxy-8-methyl-8,16-diazapentacyclo[10.6.1.01,9.02,7.016,19]nonadeca-2,4,6,13-tetraen-4-yl]-17-ethyl-17-hydroxy-1,11-diazatetracyclo[13.3.1.04,12.05,10]nonadeca-4(12),5,7,9-tetraene-13-carboxylate	214333: The compound tested for the inhibition of tubulin polymerization.	ic50	0.0800	uM
4-methoxy-2-[(Z)-2-(3,4,5-trimethoxyphenyl)ethenyl]thiophene	1267532: Inhibition of Tubulin polymerization in human HeLa cells assessed as decrease in dynamic tyrosinated microtubules after 2 hrs by microplate reader analysis	ec50	0.0810	uM
N-[2-[[(E)-(2,4-dihydroxyphenyl)methylideneamino]carbamoyl]phenyl]furan-2-carboxamide	1882654: Inhibition of tubulin polymerization (unknown origin)	ic50	0.0876	uM
N-hydroxy-6-(3-methoxy-6-oxobenzo[b][1,4]benzoxazepin-5-yl)hexanamide	580932: Inhibition of HDAC activity in human NB4 cells assessed as acetylated tubulin after 24 hrs by Western blot analysis	ec50	0.0900	uM
N-(3,5-dimethoxyphenyl)-3-[3-(3-methoxyanilino)-1H-1,2,4-triazol-5-yl]pyridin-2-amine	256882: Displacement of [3H]colchicine from tubulin	ki	0.1000	uM
methyl (13S,15S,17S)-13-[(1R,9R,10S,11R,12R,19R)-10-[[(1R)-1-diethoxyphosphoryl-2-(1H-indol-3-yl)ethyl]carbamoyl]-12-ethyl-10,11-dihydroxy-5-methoxy-8-methyl-8,16-diazapentacyclo[10.6.1.01,9.02,7.016,19]nonadeca-2,4,6,13-tetraen-4-yl]-17-ethyl-17-hydroxy-1,11-diazatetracyclo[13.3.1.04,12.05,10]nonadeca-4(12),5,7,9-tetraene-13-carboxylate	214333: The compound tested for the inhibition of tubulin polymerization.	ic50	0.1000	uM
methyl (13S,15S,17S)-13-[(1R,9R,10S,11R,12R,19R)-10-(1-diethoxyphosphorylethylcarbamoyl)-12-ethyl-10,11-dihydroxy-5-methoxy-8-methyl-8,16-diazapentacyclo[10.6.1.01,9.02,7.016,19]nonadeca-2,4,6,13-tetraen-4-yl]-17-ethyl-17-hydroxy-1,11-diazatetracyclo[13.3.1.04,12.05,10]nonadeca-4(12),5,7,9-tetraene-13-carboxylate	214333: The compound tested for the inhibition of tubulin polymerization.	ic50	0.1000	uM
methyl (13S,15S,17S)-13-[(1R,9R,10S,11R,12R,19R)-10-[[(1S)-1-diethoxyphosphoryl-2-(1H-indol-3-yl)ethyl]carbamoyl]-12-ethyl-10,11-dihydroxy-5-methoxy-8-methyl-8,16-diazapentacyclo[10.6.1.01,9.02,7.016,19]nonadeca-2,4,6,13-tetraen-4-yl]-17-ethyl-17-hydroxy-1,11-diazatetracyclo[13.3.1.04,12.05,10]nonadeca-4(12),5,7,9-tetraene-13-carboxylate	214333: The compound tested for the inhibition of tubulin polymerization.	ic50	0.1000	uM

CTD chemical–gene interactions

114 total (human), top 30 by PubMed support.

Chemical	Actions (top 5)	PubMed papers
Benzo(a)pyrene	affects methylation, decreases expression, increases expression, increases methylation	5
Cyclosporine	decreases expression, increases expression	5
bisphenol A	increases expression, affects cotreatment, decreases expression	4
Cisplatin	increases expression, affects expression, affects reaction, affects cotreatment, decreases expression	4
Tobacco Smoke Pollution	affects expression, decreases expression, increases metabolic processing	4
Air Pollutants	decreases expression, increases abundance, increases expression	3
Estradiol	affects cotreatment, increases expression	3
Smoke	decreases expression, increases abundance, increases expression	3
bisphenol F	increases expression, affects cotreatment, decreases expression	2
perfluorooctane sulfonic acid	affects expression, affects cotreatment, decreases expression	2
(+)-JQ1 compound	increases expression	2
Carbamazepine	affects expression	2
Tetrachlorodibenzodioxin	increases expression	2
Tunicamycin	decreases expression	2
Aflatoxin B1	affects expression, increases expression	2
Particulate Matter	decreases expression, increases abundance	2
ammonium 2,3,3,3-tetrafluoro-2-(heptafluoropropoxy)-propanoate	affects expression, affects cotreatment	1
sotorasib	increases expression, affects cotreatment	1
ginger extract	increases abundance, increases expression	1
dicrotophos	decreases expression	1
methyleugenol	increases expression	1
triphenyl phosphate	affects expression	1
uranyl acetate	affects expression	1
6-hydroxy-5-((p- sulfophenyl)azo)-2-naphthalenesulfonic acid disodium salt	affects cotreatment, increases expression	1
lead acetate	increases expression	1
withaferin A	decreases expression	1
trichostatin A	affects expression	1
pyrazolo(3,4-d)pyrimidine	affects expression	1
methylparaben	increases expression	1
sulforaphane	affects binding	1

ChEMBL screening assays

1696 unique, capped per target: 1655 binding, 35 functional, 6 admet

Representative assays (with source publication via chembl_document):

Assay ID	Type	Description	Source paper
CHEMBL1009021	Binding	Inhibition of tubulin polymerization in human MCF7 cells at 1 uM after 2 hrs by SDS-PAGE	A new cytotoxic epothilone from modified polyketide synthases heterologously expressed in Myxococcus xanthus. — J Nat Prod
CHEMBL4146506	ADMET	Inhibition of tubulin polymerization in human HaCaT cells assessed as chromatin condensation at 1 uM after 24 hrs by Hoechst 33258 staining-based fluorescence microscopic analysis	Design, synthesis, and biological evaluation of novel combretastatin A-4 thio derivatives as microtubule targeting agents. — Eur J Med Chem
CHEMBL5056161	Functional	Inhibition of tubulin polymerization (unknown origin) assessed as fluorescence intensity measured for 90 mins by DAPI based microplate reader	Design, synthesis and biological evaluation of indole-based [1,2,4]triazolo[4,3-a] pyridine derivatives as novel microtubule polymerization inhibitors. — Eur J Med Chem

Cellosaurus cell lines

7 cell lines: 5 induced pluripotent stem cell, 2 cancer cell line

First 10 cell lines (id-ordered, not curated):

Cellosaurus	Name	Category	Sex
CVCL_C0JQ	DHMCi008-A	Induced pluripotent stem cell	Female
CVCL_TV08	HAP1 TUBA1A (-) 1	Cancer cell line	Male
CVCL_TV09	HAP1 TUBA1A (-) 2	Cancer cell line	Male
CVCL_VG50	TUBA1A-iPS-A#1	Induced pluripotent stem cell	Male
CVCL_VG51	TUBA1A-iPS-A#3	Induced pluripotent stem cell	Male
CVCL_VG52	TUBA1A-iPS-B#1	Induced pluripotent stem cell	Male
CVCL_VG53	TUBA1A-iPS-B#2	Induced pluripotent stem cell	Male

Clinical trials (associated diseases)

301 trials via MONDO — disease-level, not drug-specific.

Trial	Phase	Status	Title
NCT00154830	PHASE4	COMPLETED	Alterations of Functional Activities and Leg Stiffness After Hamstring Lengthening in Cerebral Palsy Children
NCT00432055	PHASE4	COMPLETED	Effects of Botulinum Toxin Type A in Adults With Cerebral Palsy
NCT00549471	PHASE4	TERMINATED	Improvement After Botulinum Toxin Injections to the Arms in Children With Cerebral Palsy
NCT00752934	PHASE4	TERMINATED	Does Oral Baclofen Improve Care and Comfort in Spastic Children in Nursing Homes?
NCT00964639	PHASE4	COMPLETED	Postoperative Pain in Children With Cerebral Palsy After Pelvic and Femoral Osteotomies
NCT01386255	PHASE4	WITHDRAWN	Placebo Controlled Study of Baclofen for GERD in Children With Cerebral Palsy
NCT02546999	PHASE4	COMPLETED	Does Botulinum Toxin A Make Walking Easier in Children With Cerebral Palsy?
NCT02633241	PHASE4	COMPLETED	A Pilot Study of Dexmedetomidine-Propofol in Children Undergoing Magnetic Resonance Imaging
NCT03117322	PHASE4	COMPLETED	Synbiotic, Prebiotics and Probiotics in Children With Cerebral Palsy and Constipation
NCT03648658	PHASE4	UNKNOWN	Paracetamol Study in Patients With Low Muscle Mass
NCT04074265	PHASE4	COMPLETED	Peri-operative Use of a Pain Injection in Pediatric Patients With Cerebral Palsy
NCT04273737	PHASE4	TERMINATED	Amantadine in Treating Cognitive & Motor Impairments in Adolescents and Adults With Cerebral Palsy
NCT04523935	PHASE4	COMPLETED	Excessive Crying in Children With Cerebral Palsy and Communication Deficits
NCT05887765	PHASE4	COMPLETED	Effect of Systematic Dexamethasone on the Duration of Popliteal Nerve Block for Anesthesia After Pediatric Ankle Surgery
NCT06176430	PHASE4	UNKNOWN	Comparison of Twice Weekly Versus Daily Iron Therapy in Treating Anemia in Children With Cerebral Palsy
NCT06189781	PHASE4	RECRUITING	Pain Injection Versus Epidural Anesthesia for Hip Surgery in Pediatric Patients With Cerebral Palsy
NCT00014989	PHASE3	COMPLETED	Beneficial Effects of Antenatal Magnesium Sulfate (BEAM Trial)
NCT00065949	PHASE3	UNKNOWN	Magnesium Sulfate to Prevent Brain Injury in Premature Infants
NCT00367068	PHASE3	COMPLETED	Dutch National ITB Study in Children With Cerebral Palsy
NCT00491894	PHASE3	COMPLETED	Safety and Efficacy Study of Oral Glycopyrrolate Liquid for the Treatment of Pathologic (Chronic Moderate to Severe) Drooling in Pediatric Patients 3 to 18 Years of Age With Cerebral Palsy or Other Neurologic Conditions
NCT00632528	PHASE3	COMPLETED	MEOPA to Improve Physical Therapy Results After Multilevel Surgery
NCT00822029	PHASE3	TERMINATED	Use of Oral Bisphosphonates in the Treatment of Osteoporosis of Non-walking Children With Cerebral Palsy
NCT00922077	PHASE3	COMPLETED	Individualized Neurodevelopmental Treatment
NCT01249417	PHASE3	COMPLETED	Dysport® Pediatric Lower Limb Spasticity Study
NCT01251380	PHASE3	COMPLETED	Dysport® Pediatric Lower Limb Spasticity Follow-on Study
NCT01437644	PHASE3	COMPLETED	The Post-Operative Pain in Cerebral Palsy (POPPIES) Trial
NCT01492608	PHASE3	COMPLETED	Magnesium Sulphate for Preterm Birth (MASP Study)
NCT01603602	PHASE3	COMPLETED	BOTOX® Treatment in Pediatric Upper Limb Spasticity
NCT01603615	PHASE3	COMPLETED	BOTOX® Open-Label Treatment in Pediatric Upper Limb Spasticity
NCT01603628	PHASE3	COMPLETED	BOTOX® Treatment in Pediatric Lower Limb Spasticity
NCT01603641	PHASE3	COMPLETED	BOTOX® Open-Label Treatment in Pediatric Lower Limb Spasticity
NCT01633736	PHASE3	UNKNOWN	Targeted Hip Strength Training in Children With Cerebral Palsy (CP)
NCT01898520	PHASE3	COMPLETED	A Safety, Efficacy and Tolerability Study of Sativex for the Treatment of Spasticity in Children Aged 8 to 18 Years
NCT01929434	PHASE3	COMPLETED	Efficacy of Stem Cell Transplantation Compared to Rehabilitation Treatment of Patients With Cerebral Paralysis
NCT02002884	PHASE3	COMPLETED	Dose-response Study of Efficacy and Safety of Botulinum Toxin Type A to Treat Spasticity of the Arm(s) or of Arm(s) and Leg(s) in Cerebral Palsy
NCT02270736	PHASE3	COMPLETED	Clinical Study to Investigate the Efficacy and Safety of NT 201 Compared to Placebo in the Treatment of Chronic Troublesome Drooling Associated With Neurological Disorders and/or Intellectual Disability
NCT02839785	PHASE3	TERMINATED	Analgesia and Physiotherapy in Children With Cerebral Palsy (ANTALKINECP)
NCT03110341	PHASE3	UNKNOWN	Effect of Erythropoietin in Premature Infants on White Matter Lesions and Neurodevelopmental Outcome
NCT03302871	PHASE3	COMPLETED	Integrated Management Enhances Functional Gains in Children With Cerebral Palsy Treated by BoNT-A
NCT03306212	PHASE3	COMPLETED	Efficacy of Intermittent Serial Casting on Spastic Wrist Flexion Deformity