TUBA1B

gene
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Also known as K-ALPHA-1

Summary

TUBA1B (tubulin alpha 1b, HGNC:18809) is a protein-coding gene on chromosome 12q13.12, encoding Tubulin alpha-1B chain (P68363). Tubulin is the major constituent of microtubules, protein filaments consisting of alpha- and beta-tubulin heterodimers. It is a common-essential gene (DepMap: required in 93.0% of cancer cell lines).

Enables several functions, including GTP binding activity; GTPase activity; and ubiquitin protein ligase binding activity. A structural constituent of cytoskeleton. Involved in microtubule cytoskeleton organization. Located in cilium and microtubule. Is active in microtubule cytoskeleton.

Source: NCBI Gene 10376 — RefSeq curated summary.

At a glance

  • GWAS associations: 5
  • Clinical variants (ClinVar): 23 total
  • Druggable target: yes — 21 molecules with ChEMBL bioactivity
  • Cancer dependency (DepMap): dependent in 93.0% of screened cell lines (common-essential)
  • MANE Select transcript: NM_006082

Identifiers

Gene identifiers

FieldValue
HGNC IDHGNC:18809
Approved symbolTUBA1B
Nametubulin alpha 1b
Location12q13.12
Locus typegene with protein product
StatusApproved
AliasesK-ALPHA-1
Ensembl geneENSG00000123416
Ensembl biotypeprotein_coding
OMIM602530
Entrez10376

Gene structure

Transcript identifiers

Ensembl transcripts: 13 — 10 protein_coding, 2 retained_intron, 1 nonsense_mediated_decay

ENST00000332858, ENST00000336023, ENST00000547476, ENST00000547765, ENST00000549870, ENST00000550367, ENST00000551324, ENST00000552984, ENST00000920097, ENST00000920098, ENST00000920099, ENST00000920100, ENST00000920101

RefSeq mRNA: 1 — MANE Select: NM_006082 NM_006082

CCDS: CCDS31792

Canonical transcript exons

ENST00000336023 — 4 exons

ExonStartEnd
ENSE000023642434912778249128938
ENSE000034834664912924249129390
ENSE000035622794912950049129722
ENSE000036342934913129849131395

Expression profiles

Bgee: expression breadth ubiquitous, 153 present calls, max score 99.95.

FANTOM5 (CAGE): breadth ubiquitous, TPM avg 2023.6541 / max 9793.5382, expressed in 1828 samples.

FANTOM5 promoters (8 alternative TSS)

Promoter IDTPM avgSamples expressed
1308152012.62041828
1308096.06001560
1308102.14371042
1308121.7782875
1308130.6607286
1308110.218864
2066870.115626
1308140.056615

Top tissues by expression

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

TissueAnatomy IDExpression scoreQuality
ventricular zoneUBERON:000305399.95gold quality
superior frontal gyrusUBERON:000266199.90gold quality
frontal poleUBERON:000279599.90gold quality
prefrontal cortexUBERON:000045199.89gold quality
frontal cortexUBERON:000187099.88gold quality
dorsal plus ventral thalamusUBERON:000189799.88gold quality
right frontal lobeUBERON:000281099.86gold quality
dorsolateral prefrontal cortexUBERON:000983499.86gold quality
anterior cingulate cortexUBERON:000983599.86gold quality
Brodmann (1909) area 9UBERON:001354099.86gold quality
Brodmann (1909) area 10UBERON:001354199.86gold quality
cerebral cortexUBERON:000095699.84gold quality
ganglionic eminenceUBERON:000402399.84gold quality
primary visual cortexUBERON:000243699.80gold quality
dorsal root ganglionUBERON:000004499.79gold quality
hypothalamusUBERON:000189899.79gold quality
spinal cordUBERON:000224099.79gold quality
C1 segment of cervical spinal cordUBERON:000646999.79gold quality
endometrium epitheliumUBERON:000481199.77gold quality
smooth muscle tissueUBERON:000113599.74gold quality
cortical plateUBERON:000534399.70gold quality
temporal lobeUBERON:000187199.69gold quality
amygdalaUBERON:000187699.68gold quality
Ammon’s hornUBERON:000195499.68gold quality
substantia nigraUBERON:000203899.67gold quality
islet of LangerhansUBERON:000000699.66gold quality
cerebellumUBERON:000203799.66gold quality
cerebellar cortexUBERON:000212999.66gold quality
cerebellar hemisphereUBERON:000224599.66gold quality
right hemisphere of cerebellumUBERON:001489099.65gold quality

Single-cell (SCXA)

Detected in 86 experiment(s), a significant marker in 62.

ExperimentMarker?Max mean expression
E-CURD-79yes10163.25
E-GEOD-93593yes8469.28
E-HCAD-5yes8004.44
E-MTAB-9435yes7930.46
E-HCAD-25yes7630.57
E-MTAB-5061yes7458.31
E-HCAD-10yes7367.84
E-CURD-112yes6004.52
E-GEOD-135922yes5995.98
E-HCAD-6yes5977.90
E-HCAD-4yes5875.48
E-GEOD-114530yes5448.15
E-MTAB-10662yes5413.25
E-MTAB-7407yes5377.63
E-MTAB-10432yes5200.38

Regulation

Is transcription factor: no

Upstream regulators (CollecTRI, top): PPARA, RORA

miRNA regulators (miRDB)

27 targeting TUBA1B, top 30 by miRDB confidence (max_score; target_count = how many genes the miRNA targets in total — lower means more specific):

miRNAMax scoreAvg scoremiRNA target_count
HSA-MIR-3134100.0066.43777
HSA-MIR-223-3P99.9970.141140
HSA-MIR-453499.9966.581907
HSA-MIR-314899.9775.066478
HSA-MIR-3688-3P99.9772.022834
HSA-MIR-570-3P99.9672.414910
HSA-MIR-808299.9567.271170
HSA-MIR-612499.8769.783551
HSA-MIR-10395-5P99.8667.35676
HSA-MIR-3617-5P99.7569.411968
HSA-MIR-64199.7569.351975
HSA-MIR-4802-3P99.7270.131273
HSA-MIR-613299.6065.831554
HSA-MIR-6836-5P99.6065.621538
HSA-MIR-464399.4967.631791
HSA-MIR-56999.4266.321009
HSA-MIR-127299.3468.79878
HSA-MIR-6797-3P99.1766.94668
HSA-MIR-10399-5P99.1769.872610
HSA-MIR-6504-3P99.1769.312891
HSA-MIR-4717-3P99.0666.341072
HSA-MIR-607698.6165.69637
HSA-MIR-132297.9868.96625
HSA-MIR-431497.5067.301369
HSA-MIR-6895-5P97.0564.96522
HSA-MIR-3192-5P96.9865.761926
HSA-MIR-391896.1364.651300

Functional genomics

DepMap (CRISPR cell-line fitness): dependent in 93.0% of screened cell lines, common-essential.

Literature-anchored findings (GeneRIF, showing 29)

  • increased levels in paclitaxel-resistant breast cancer cells (PMID:12054644)
  • Candidate gene K-ALPHA-1 expression in malignant and non-malignant prostate tissue samples after microdissection. (PMID:17628775)
  • accumulation of alpha-synuclein might contribute to the pathogenesis of PD and other Lewy body diseases by promoting alterations in parkin and tubulin solubility (PMID:18195004)
  • N-terminal sequencing and blastx analysis as well as blocking with K-alpha1 tubulin-specific Ab identified the epithelial Ag as K-alpha1 tubulin[K-alpha1 tubulin] (PMID:18354170)
  • mitochondrial ribosomal protein S12 3’-UTR interacts specifically with TRAP1 (tumor necrosis factor receptor-associated protein1), hnRNPM4 (heterogeneous nuclear ribonucleoprotein M4), Hsp70 and Hsp60 (heat shock proteins 70 and 60), and alpha-tubulin (PMID:18790094)
  • These results imply that MeCP2 is involved in the regulation of neuronal alpha-tubulin and add molecular evidence that reversal of the effects of MeCP2 deficiency is achievable (PMID:19174478)
  • Increased expression of centrosomal TUBA1B in atypical ductal hyperplasia and carcinoma of the breast is reported. (PMID:19215229)
  • This protein has been found differentially expressed in the Wernicke’s Area from patients with schizophrenia. (PMID:19405953)
  • alpha-tubulin interacted with ARL7. (PMID:19409876)
  • Data show that 4-oxo-4-HPR inhibited tubulin polymerization and modulated gene expression of spindle aberration associated genes Kif 1C, Kif 2A, Eg5, Tara, tankyrase-1, centractin, and TOGp. (PMID:19996280)
  • Confocal microscopic analyses showed co-localization of the TaSP protein with alpha-tubulin and reciprocal immuno-co-precipitation experiments demonstrated an association of TaSP with alpha-tubulin in vivo. (PMID:20162433)
  • the ethyl acetate extract of Lactuca sativa induced HL-60 cell death, which correlated with the acetylation of alpha-tubulin. (PMID:20204303)
  • This protein has been found differentially expressed in the anterior cingulate cortex from patients with schizophrenia (PMID:20381070)
  • TQ induced a concentration- and time-dependent degradation of alpha/beta tubulin in both cancer cell types. (PMID:21881916)
  • ARHGAP21 is a Rho-GAP involved in cell-cell junction remodeling that affects migration and EMT through alpha-tubulin interaction and acetylation (PMID:23235160)
  • Increased TUBA1B expression is associated with poor overall survival in hepatocellular carcinoma. (PMID:23625295)
  • Data indicate that the derivatives exhibited much better potency to inhibit tubulin polymerization but a decreased activity to inhibit Hsp27 chaperone function. (PMID:23767669)
  • Results suggest that lithium chloride (LiCl) treatments activate alpha-tubulin N-acetyltransferase 1 (alphaTAT1) by the inhibition of glycogen synthase kinase 3 beta (GSK-3beta) and promote the alpha-tubulin acetylation, and then elongate the primary cilia. (PMID:24760594)
  • NAD-dependent regulation of alpha-tubulin acetylation is mediated by SIRT2. (PMID:24814981)
  • TUBA1B/ESR1 gene interaction might play pivotal roles in the occurrence and development of Postmenopausal Osteoporosis. (PMID:26676054)
  • Taken together our data provide valuable information regarding the interaction of CK1delta and a-tubulin and a novel approach for the development of pharmacological tools to inhibit proliferation of cancer cells. (PMID:26996302)
  • Data show that retinal endothelial cells (HREC) treated with low molecular weight fraction of commercial 5% human serum albumin (LMWF5A) exhibit a rapid increase in the amount and distribution of acetylated alpha-tubulin. (PMID:27613088)
  • The C-terminal tail from the tubulin beta I isotype, but not the beta III isotype, formed contacts in the putative binding site of a recently discovered antineoplastic peptide that disrupts microtubule formation in glioma cells. (PMID:28290671)
  • Structure of spastin bound to a glutamate-rich peptide implies a hand-over-hand mechanism of substrate translocation. (PMID:31767681)
  • The Expression and Potential Role of Tubulin Alpha 1b in Wilms’ Tumor. (PMID:32908931)
  • Lower levels of tubulin alpha 1b in the frontal pole in schizophrenia supports a role for changed cytoskeletal dynamics in the aetiology of the disorder. (PMID:34274903)
  • Dynamic Network Biomarker of Pre-Exhausted CD8(+) T Cells Contributed to T Cell Exhaustion in Colorectal Cancer. (PMID:34434188)
  • Integrated regulation of tubulin tyrosination and microtubule stability by human alpha-tubulin isotypes. (PMID:37379209)
  • Tubulin Alpha-1b as a Potential Biomarker for Lung Adenocarcinoma Diagnosis and Prognosis. (PMID:37489256)

Cross-species orthologs

4 orthologs

OrganismSymbolGene ID
mus_musculusTuba1bENSMUSG00000023004
rattus_norvegicusTuba1bENSRNOG00000072536
drosophila_melanogasteralphaTub84BFBGN0003884
drosophila_melanogasteralphaTub84DFBGN0003885

Paralogs (23): TUBG2 (ENSG00000037042), TUBE1 (ENSG00000074935), TUBA3D (ENSG00000075886), TUBB1 (ENSG00000101162), TUBB4A (ENSG00000104833), TUBD1 (ENSG00000108423), TUBA4A (ENSG00000127824), TUBG1 (ENSG00000131462), TUBB2A (ENSG00000137267), TUBB2B (ENSG00000137285), TUBA3E (ENSG00000152086), TUBA1A (ENSG00000167552), 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-1B chainP68363 (reviewed: P68363)

Alternative names: Alpha-tubulin ubiquitous, Tubulin K-alpha-1, Tubulin alpha-ubiquitous chain

All UniProt accessions (6): P68363, F8VRK0, F8VU66, F8VVB9, F8VWV9, F8VX09

UniProt curated annotations — full annotation on UniProt →

Function. Tubulin is the major constituent of microtubules, protein filaments consisting 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. Heterodimer of alpha- and beta-tubulin. 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. Interacts with gamma-tubulin; the interaction allows microtubules to nucleate from the gamma-tubulin ring complex (gTuRC). Nascent microtubule interacts (via alpha-tubulin MREC motif) with TTC5/STRAP; this interaction may result in tubulin mRNA-targeted degradation. Component of sperm flagellar doublet microtubules.

Subcellular location. Cytoplasm. Cytoskeleton.

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.

Domain organisation. The MREC motif mediates interaction with TTC5/STRAP and may be critical for tubulin autoregulation.

Induction. Autoregulated by feedback control of mRNA degradation. In excess of soluble tubulin, TTC5/STRAP cofactor triggers cotranslation degradation of tubulin mRNA.

Similarity. Belongs to the tubulin family.

Isoforms (2)

UniProt IDNamesCanonical?
P68363-11yes
P68363-22

RefSeq proteins (1): NP_006073* (*=MANE)

Domains & families (InterPro)

IDNameType
IPR000217TubulinFamily
IPR002452Alpha_tubulinFamily
IPR003008Tubulin_FtsZ_GTPaseDomain
IPR008280Tub_FtsZ_CHomologous_superfamily
IPR017975Tubulin_CSConserved_site
IPR018316Tubulin/FtsZ_2-layer-sand-domDomain
IPR023123Tubulin_CHomologous_superfamily
IPR036525Tubulin/FtsZ_GTPase_sfHomologous_superfamily
IPR037103Tubulin/FtsZ-like_CHomologous_superfamily

Pfam: PF00091, PF03953

Catalyzed reactions (Rhea), 1 shown:

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

UniProt features (95 total): helix 24, strand 21, binding site 18, modified residue 10, turn 6, sequence conflict 4, mutagenesis site 3, chain 2, cross-link 2, region of interest 1, site 1, short sequence motif 1, splice variant 1, active site 1

Structure

Experimental structures (PDB)

39 structures, top 30 by resolution.

PDBMethodResolution (Å)
6S8LX-RAY DIFFRACTION1.8
6J8OX-RAY DIFFRACTION1.85
7PJFX-RAY DIFFRACTION1.86
6J4VX-RAY DIFFRACTION2.1
8VT7ELECTRON MICROSCOPY2.66
7Z6SELECTRON MICROSCOPY2.9
8V2JELECTRON MICROSCOPY2.9
9COCELECTRON MICROSCOPY2.9
9BP6ELECTRON MICROSCOPY3.1
9CMMELECTRON MICROSCOPY3.1
7LXBELECTRON MICROSCOPY3.26
9HQ4ELECTRON MICROSCOPY3.28
7M18ELECTRON MICROSCOPY3.38
6E7BELECTRON MICROSCOPY3.5
6I2IELECTRON MICROSCOPY3.6
7SJ8ELECTRON MICROSCOPY3.6
7ZCWELECTRON MICROSCOPY3.6
8T42ELECTRON MICROSCOPY3.6
8U3ZELECTRON MICROSCOPY3.6
9F3BELECTRON MICROSCOPY3.6
6E7CELECTRON MICROSCOPY3.65
5IJ9ELECTRON MICROSCOPY3.7
6QUSELECTRON MICROSCOPY3.7
6QVEELECTRON MICROSCOPY3.7
5IJ0ELECTRON MICROSCOPY3.8
6QUYELECTRON MICROSCOPY3.8
6QVJELECTRON MICROSCOPY3.8
7SJ7ELECTRON MICROSCOPY3.8
7SJ9ELECTRON MICROSCOPY3.8
7SJAELECTRON MICROSCOPY3.8

Predicted structure (AlphaFold)

ModelpLDDTFraction very-high
AF-P68363-F191.850.84

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 (18): 71; 99; 140; 143; 144; 145; 146; 179; 183; 206; 224; 228

Post-translational modifications (12): 40, 40, 48, 232, 282, 339, 439, 443, 445, 451, 326, 370

Mutagenesis-validated functional residues (3):

PositionPhenotype
254abolished gtpase activity; microtubules have an expanded lattice with a negative twist and display high binding to micro
254promotes microtubule nucleation efficiency and slows gtp hydrolysis.
254abolished gtpase activity; microtubules have an expanded lattice with a positive twist and display low binding to microt

Function

Pathways and Gene Ontology

Reactome pathways

87 pathways

IDPathway
R-HSA-1445148Translocation of SLC2A4 (GLUT4) to the plasma membrane
R-HSA-190840Microtubule-dependent trafficking of connexons from Golgi to the plasma membrane
R-HSA-190861Gap junction assembly
R-HSA-2132295MHC class II antigen presentation
R-HSA-2467813Separation of Sister Chromatids
R-HSA-2500257Resolution of Sister Chromatid Cohesion
R-HSA-3371497HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand
R-HSA-380320Recruitment of NuMA to mitotic centrosomes
R-HSA-389960Formation of tubulin folding intermediates by CCT/TriC
R-HSA-389977Post-chaperonin tubulin folding pathway
R-HSA-437239Recycling pathway of L1
R-HSA-5610787Hedgehog ‘off’ state
R-HSA-5620920Cargo trafficking to the periciliary membrane
R-HSA-5620924Intraflagellar transport
R-HSA-5626467RHO GTPases activate IQGAPs
R-HSA-5663220RHO GTPases Activate Formins
R-HSA-6807878COPI-mediated anterograde transport
R-HSA-6811434COPI-dependent Golgi-to-ER retrograde traffic
R-HSA-6811436COPI-independent Golgi-to-ER retrograde traffic
R-HSA-68877Mitotic Prometaphase
R-HSA-8852276The role of GTSE1 in G2/M progression after G2 checkpoint
R-HSA-8955332Carboxyterminal post-translational modifications of tubulin
R-HSA-9013407RHOH GTPase cycle
R-HSA-9609690HCMV Early Events
R-HSA-9609736Assembly and cell surface presentation of NMDA receptors
R-HSA-9619483Activation of AMPK downstream of NMDARs
R-HSA-9646399Aggrephagy
R-HSA-9648025EML4 and NUDC in mitotic spindle formation
R-HSA-9668328Sealing of the nuclear envelope (NE) by ESCRT-III
R-HSA-983189Kinesins

MSigDB gene sets: 377 (showing top): HONMA_DOCETAXEL_RESISTANCE, REACTOME_ADAPTIVE_IMMUNE_SYSTEM, REACTOME_CYTOKINE_SIGNALING_IN_IMMUNE_SYSTEM, GOBP_RESPONSE_TO_INTERLEUKIN_4, GOBP_RESPONSE_TO_PEPTIDE, MORF_UBE2I, MATTIOLI_MGUS_VS_PCL, PID_PRL_SIGNALING_EVENTS_PATHWAY, THEILGAARD_NEUTROPHIL_AT_SKIN_WOUND_DN, WEIGEL_OXIDATIVE_STRESS_BY_TBH_AND_H2O2, GOBP_NEUROGENESIS, REACTOME_MEMBRANE_TRAFFICKING, PUJANA_CHEK2_PCC_NETWORK, SHETH_LIVER_CANCER_VS_TXNIP_LOSS_PAM1, GROSS_ELK3_TARGETS_UP

GO Biological Process (7): microtubule cytoskeleton organization (GO:0000226), mitotic cell cycle (GO:0000278), microtubule-based process (GO:0007017), cytoskeleton-dependent intracellular transport (GO:0030705), cell division (GO:0051301), cellular response to interleukin-4 (GO:0071353), cytoskeleton organization (GO:0007010)

GO Molecular Function (9): double-stranded RNA binding (GO:0003725), GTPase activity (GO:0003924), structural molecule activity (GO:0005198), structural constituent of cytoskeleton (GO:0005200), GTP binding (GO:0005525), ubiquitin protein ligase binding (GO:0031625), nucleotide binding (GO:0000166), protein binding (GO:0005515), hydrolase activity (GO:0016787)

GO Cellular Component (6): cytoplasm (GO:0005737), microtubule (GO:0005874), cytoplasmic microtubule (GO:0005881), cilium (GO:0005929), microtubule cytoskeleton (GO:0015630), cytoskeleton (GO:0005856)

Reactome top-level categories

Rollup of top-16 pathways:

CategoryPathways
Mitotic Prometaphase2
Assembly of the 9+0 primary cilium2
RHO GTPase Effectors2
Golgi-to-ER retrograde transport2
Membrane Trafficking1
Transport of connexons to the plasma membrane1
Gap junction trafficking1
Adaptive Immune System1
Mitotic Anaphase1
Cellular responses to stress1
Cooperation of Prefoldin and TriC/CCT in actin and tubulin folding1
Protein folding1
L1CAM interactions1
Signaling by Hedgehog1
ER to Golgi Anterograde Transport1

GO top-level categories

Rollup of top GO terms by namespace:

CategoryTerms
cytoskeleton organization2
cellular process2
cytoskeleton2
microtubule-based process1
cell cycle1
mitotic nuclear division1
intracellular transport1
response to interleukin-41
cellular response to cytokine stimulus1
organelle organization1
RNA binding1
ribonucleoside triphosphate phosphatase activity1
molecular_function1
structural molecule activity1
guanyl ribonucleotide binding1
purine ribonucleoside triphosphate binding1
ubiquitin-like protein ligase binding1
nucleoside phosphate binding1
heterocyclic compound binding1
binding1
catalytic activity1
intracellular anatomical structure1
cellular anatomical structure1
microtubule cytoskeleton1
polymeric cytoskeletal fiber1
cytoplasm1
microtubule1
intraciliary transport particle1
membrane-bounded organelle1
plasma membrane bounded cell projection1
intracellular membraneless organelle1

Protein interactions and networks

STRING

0 interactions, top by confidence (×1000):

IntAct

215 interactions, top by confidence:

ABTypeScore
STAG2RAD21psi-mi:“MI:0914”(association)0.970
EHMT2WIZpsi-mi:“MI:0914”(association)0.730
MTMR2CCDC22psi-mi:“MI:0914”(association)0.730
CCT2TXNDC9psi-mi:“MI:0914”(association)0.730
CFTRESYT2psi-mi:“MI:2364”(proximity)0.710
TUBB3TUBA1Bpsi-mi:“MI:0914”(association)0.660
TUBA1BTXNDC9psi-mi:“MI:0914”(association)0.640
MAPK7PFDN6psi-mi:“MI:0914”(association)0.640
ATXN7L3USP27Xpsi-mi:“MI:0914”(association)0.640
KDM5ASIN3Bpsi-mi:“MI:0914”(association)0.640
LIN28AIGF2BP3psi-mi:“MI:0914”(association)0.640
NCBP1KPNA3psi-mi:“MI:0914”(association)0.640
CCT3TXNDC9psi-mi:“MI:0914”(association)0.640
CCT5TXNDC9psi-mi:“MI:0914”(association)0.640
THOC1DDX39Apsi-mi:“MI:0914”(association)0.640
TUBA1BAGTRAPpsi-mi:“MI:0915”(physical association)0.560
AGTRAPTUBA1Bpsi-mi:“MI:0915”(physical association)0.560
APPTUBA1Bpsi-mi:“MI:0915”(physical association)0.560
SNCATUBA1Bpsi-mi:“MI:0915”(physical association)0.560
MAP2K2BAG2psi-mi:“MI:0914”(association)0.530
KDM6AKMT2Dpsi-mi:“MI:0914”(association)0.530
PPP2R2BDDX3Xpsi-mi:“MI:0914”(association)0.460

BioGRID (644): TUBA1B (Affinity Capture-MS), AGTRAP (Two-hybrid), MTCL1 (Reconstituted Complex), TUBA1B (Affinity Capture-MS), TUBA1B (Affinity Capture-MS), TUBA1B (Affinity Capture-MS), TUBA1B (Affinity Capture-MS), TUBA1B (Affinity Capture-MS), TUBA1B (Affinity Capture-MS), TUBA1B (Reconstituted Complex), TUBA1B (Affinity Capture-MS), TUBA1B (Reconstituted Complex), TUBA1B (Biochemical Activity), TUBA1B (Affinity Capture-MS), TUBA1B (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

6 interactions.

AEffectBMechanism
NUMA1up-regulatesTUBA1Bbinding
TTLdown-regulatesTUBA1Btyrosination
SETD2“up-regulates activity”TUBA1Bmethylation
“Elongator complex”“up-regulates activity”TUBA1Bacetylation
TUBA1Bup-regulatesNeuron_migration
ATAT1“up-regulates quantity by stabilization”TUBA1Bacetylation

Enriched among interaction partners

Reactome pathways and GO biological processes over-represented among this gene’s 258 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:

PathwayPartnersFoldFDR
Prefoldin mediated transfer of substrate to CCT/TriC818.3×8e-06
Formation of tubulin folding intermediates by CCT/TriC614.8×1e-03
Cooperation of Prefoldin and TriC/CCT in actin and tubulin folding614.2×1e-03
Dengue Virus Genome Translation and Replication611.1×3e-03
Chaperonin-mediated protein folding610.5×3e-03
Aggrephagy710.1×1e-03
FCERI mediated MAPK activation510.1×7e-03
Protein folding69.1×4e-03

GO biological processes:

GO termPartnersFoldFDR
protein folding125.5×3e-03

Disease & clinical

Clinical variants and AI predictions

ClinVar

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

ClassificationCount (floor)
Pathogenic0
Likely pathogenic0
Uncertain significance4
Likely benign1
Benign4

Top pathogenic / likely-pathogenic (0)

SpliceAI

376 predictions. Top by Δscore:

VariantEffectΔscore
12:49128935:CAGC:Cacceptor_gain1.0000
12:49128937:GC:Gacceptor_gain1.0000
12:49128937:GCCTG:Gacceptor_loss1.0000
12:49128938:CC:Cacceptor_gain1.0000
12:49128938:CCTG:Cacceptor_loss1.0000
12:49128939:C:CCacceptor_gain1.0000
12:49129236:GCTTA:Gdonor_loss1.0000
12:49129237:CTTA:Cdonor_loss1.0000
12:49129238:TTAC:Tdonor_loss1.0000
12:49129239:TACC:Tdonor_loss1.0000
12:49129240:A:ACdonor_gain1.0000
12:49129240:AC:Adonor_gain1.0000
12:49129240:ACCA:Adonor_loss1.0000
12:49129240:ACCAG:Adonor_gain1.0000
12:49129241:C:CGdonor_gain1.0000
12:49129241:CC:Cdonor_gain1.0000
12:49129241:CCA:Cdonor_gain1.0000
12:49129241:CCAG:Cdonor_gain1.0000
12:49129241:CCAGC:Cdonor_gain1.0000
12:49129386:TTCAT:Tacceptor_gain1.0000
12:49129387:TCAT:Tacceptor_gain1.0000
12:49129387:TCATC:Tacceptor_gain1.0000
12:49129388:CAT:Cacceptor_gain1.0000
12:49129388:CATC:Cacceptor_gain1.0000
12:49129388:CATCT:Cacceptor_gain1.0000
12:49129389:AT:Aacceptor_gain1.0000
12:49129389:ATCTG:Aacceptor_gain1.0000
12:49129390:TCTGG:Tacceptor_gain1.0000
12:49129391:C:CCacceptor_gain1.0000
12:49129391:CT:Cacceptor_gain1.0000

AlphaMissense

2975 scored. Top likely-pathogenic:

VariantProtein changeam_pathogenicity
12:49128023:C:GD431H1.000
12:49128031:A:GL428P1.000
12:49128031:A:TL428H1.000
12:49128035:C:GA427P1.000
12:49128049:C:GR422P1.000
12:49128050:G:TR422S1.000
12:49128052:G:TA421D1.000
12:49128053:C:GA421P1.000
12:49128060:A:CF418L1.000
12:49128060:A:TF418L1.000
12:49128061:A:CF418C1.000
12:49128061:A:GF418S1.000
12:49128062:A:GF418L1.000
12:49128068:C:GG416R1.000
12:49128076:A:GM413T1.000
12:49128080:C:AG412W1.000
12:49128080:C:GG412R1.000
12:49128080:C:TG412R1.000
12:49128095:A:GW407R1.000
12:49128095:A:TW407R1.000
12:49128098:G:CH406D1.000
12:49128100:A:TV405D1.000
12:49128102:A:CF404L1.000
12:49128102:A:TF404L1.000
12:49128103:A:CF404C1.000
12:49128103:A:GF404S1.000
12:49128104:A:GF404L1.000
12:49128104:A:TF404I1.000
12:49128106:G:TA403D1.000
12:49128109:C:GR402P1.000

dbSNP variants (sampled 300 via entrez): RS1000230147 (12:49129908 G>A,T), RS1001196149 (12:49132527 A>C), RS1001642284 (12:49128994 T>C), RS1003255509 (12:49127524 G>A,C,T), RS1003470056 (12:49132695 G>T), RS1004301572 (12:49127297 T>C), RS1005694818 (12:49130140 G>A), RS1005719741 (12:49130224 C>G), RS1006311457 (12:49131372 A>C,G), RS1007110807 (12:49131199 A>C), RS1007272084 (12:49133080 A>C,G), RS1007660054 (12:49132710 C>A,T), RS1008039303 (12:49127795 GACTTT>G), RS1009254572 (12:49132624 A>G), RS1009303739 (12:49132263 G>A)

Disease associations

OMIM: gene MIM:602530 | disease phenotypes: MIM:135700

GenCC curated gene-disease

Mondo (2): congenital fibrosis of extraocular muscles (MONDO:0007614), neuromuscular disease (MONDO:0019056)

Orphanet (2): Congenital fibrosis of extraocular muscles (Orphanet:45358), Neuromuscular disease (Orphanet:68381)

HPO phenotypes

0 total (0 of 0 shown, HPO-id order):

GWAS associations

5 associations (top):

StudyTraitp-value
GCST008103_109Bipolar disorder4.000000e-06
GCST010703_9Brain morphology (MOSTest)8.000000e-10
GCST90010427_15Left–right brain asymmetry1.000000e-11
GCST90013420_4Ambidextrousness1.000000e-09
GCST90013421_10Left-handedness2.000000e-10

EFO canonical traits (2, from GWAS)

EFO IDTrait name
EFO:0004346neuroimaging measurement
EFO:0009902handedness

MeSH disease descriptors (2)

DescriptorNameTree numbers
D009468Neuromuscular DiseasesC10.668
C580012congenital fibrosis of the extraocular muscles (supp.)

Drugs & pharmacology

Drug and pharmacology data

Is drug target: yes

ChEMBL targets (4): CHEMBL2095182 (PROTEIN COMPLEX GROUP), CHEMBL3797010 (SINGLE PROTEIN), CHEMBL3832941 (PROTEIN FAMILY), CHEMBL6067579 (PROTEIN-PROTEIN INTERACTION)

Molecules with ChEMBL bioactivity

21 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).

MoleculeNamePhasePatents
CHEMBL107COLCHICINE493,932
CHEMBL159VINBLASTINE4412,636
CHEMBL33LEVOFLOXACIN ANHYDROUS443,403
CHEMBL3545252DOCETAXEL41,009
CHEMBL364713NOSCAPINE414,987
CHEMBL378544VINBLASTINE SULFATE432,829
CHEMBL428647PACLITAXEL4332,542
CHEMBL5315124LEVOFLOXACIN4189
CHEMBL553025VINORELBINE4142,159
CHEMBL571546TIRBANIBULIN41,192
CHEMBL61PODOFILOX437,640
CHEMBL90555VINCRISTINE4268,031
CHEMBL92DOCETAXEL ANHYDROUS4196,686
CHEMBL94657PATUPILONE314,934
CHEMBL20684ABT-75122,238
CHEMBL292702MAYTANSINE29,300
CHEMBL39541DOLASTATIN-1021,380
CHEMBL49642INDIBULIN2963
CHEMBL528271PARBENDAZOLE26,102
CHEMBL9514NOCODAZOLE229,245
CHEMBL246600COMBRETASTATIN1

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

ChEMBL bioactivities

1163 potent at pChembl≥5 of 1314 total, top 50 by pChembl (potency: 10 = 0.1 nM, 6 = 1 µM).

pChemblTypeValueUnitMolecule
10.26IC500.0551nMCHEMBL5194719
9.75IC500.176nMCHEMBL5203711
9.51IC500.308nMVINORELBINE
9.30IC500.5nMDOLASTATIN-10
8.92IC501.2nMCHEMBL5169466
8.85IC501.4nMCHEMBL4575066
8.74IC501.8nMPATUPILONE
8.59IC502.6nMCHEMBL2024544
8.52Ki3nMCOMBRETASTATIN A4
8.52IC503nMCOMBRETASTATIN A4
8.52IC503nMDOLASTATIN-10
8.52Kd3nMCHEMBL5410715
8.52IC503nMCOLCHICINE
8.46IC503.5nMPATUPILONE
8.38IC504.2nMCHEMBL5197739
8.27IC505.4nMCHEMBL5280519
8.22IC506nMCHEMBL498271
8.05EC509nMCOMBRETASTATIN A4
8.01EC509.8nMCOMBRETASTATIN A4
8.01IC509.77nMCHEMBL4778826
8.00Ki10nMCHEMBL381852
8.00IC5010nMCHEMBL204241
7.96Kd11nMCHEMBL5611905
7.89IC5012.9nMCOMBRETASTATIN A4
7.85Kd14nMMAYTANSINE
7.70IC5020nMCHEMBL2369093
7.70Ki20nMCHEMBL369927
7.70IC5020nMCHEMBL5183440
7.70Kd20nMCHEMBL5613121
7.64IC5023nMCOMBRETASTATIN A4
7.62EC5024nMCHEMBL4250191
7.58IC5026nMPIRONETIN
7.52IC5030nMCHEMBL381122
7.52IC5030nMCOMBRETASTATIN A4
7.52IC5030nMCHEMBL203062
7.52IC5030nMCHEMBL204710
7.51EC5031nMPACLITAXEL
7.40EC5040nMCHEMBL1688184
7.35EC5045nMCHEMBL4239716
7.34IC5046nMCHEMBL374257
7.33Kd47nMCHEMBL5542101
7.30Ki50nMCHEMBL196966
7.30EC5050nMCHEMBL1688183
7.30EC5050nMCHEMBL1688189
7.29Kd51nMCHEMBL5614306
7.28EC5053nMCHEMBL4241638
7.24Kd58nMCOLCHICINE
7.22Ki60nMCHEMBL198522
7.16IC5070nMCHEMBL2369084
7.16IC5070nMVINBLASTINE

PubChem BioAssay actives

1090 with measured affinity, of 5781 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.

CompoundAssayTypeValueUnit
(Z)-1-[4-bromo-2-(4-fluorophenyl)-1-benzofuran-7-yl]-3-(4-methoxyphenyl)prop-2-en-1-one1882651: Inhibition of tubulin polymerization (unknown origin) measured every 3 secs for 1 hr by spectroflourimetric analysisic500.0001uM
(Z)-1-[4-bromo-2-(4-fluorophenyl)-1-benzofuran-7-yl]-3-[4-(trifluoromethoxy)phenyl]prop-2-en-1-one1882651: Inhibition of tubulin polymerization (unknown origin) measured every 3 secs for 1 hr by spectroflourimetric analysisic500.0002uM
Vinorelbine1993632: Inhibition of tubulin polymerization (unknown origin)ic500.0003uM
(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-dimethylbutanamide270819: Inhibition of tubulin polymerizationic500.0005uM
(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-dimethylbutanamide1896115: Binding affinity to tubulin (unknown origin)ic500.0012uM
(3Z,6Z)-3-[(5-tert-butyl-1H-imidazol-4-yl)methylidene]-6-phenacylidenepiperazine-2,5-dione1587857: Inhibition of tubulin polymerization (unknown origin)ic500.0014uM
(3Z,6Z)-3-[(5-tert-butyl-1H-imidazol-4-yl)methylidene]-6-[(2,5-difluorophenyl)methylidene]piperazine-2,5-dione1587857: Inhibition of tubulin polymerization (unknown origin)ic500.0026uM
3-hydroxy-2-[N-[2-(methoxymethyl)-1-benzofuran-7-yl]-C-methylcarbonimidoyl]-5-phenylcyclohex-2-en-1-one2034736: 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 constantkd0.0030uM
2-methoxy-5-[(Z)-2-(3,4,5-trimethoxyphenyl)ethenyl]phenol1862628: Inhibition of tubulin polymerization in human HeLa cells assessed as microtubule network polymerization after 30 mins by immunofluorescence analysisic500.0030uM
Colchicine2074087: Inhibition of microtubule polymerization in human K562 cells measured for 60 mins by fluorescence based analysisic500.0030uM
(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-dione1408257: Inhibition of tubulin polymerization in human MCF7 cells assessed as induction of mitotic arrestic500.0035uM
tert-butyl (3R,4S,5S)-4-[[(2S)-2-[[(2S)-2-(dimethylamino)-3-methylbutanoyl]amino]-3-methylbutanoyl]-methylamino]-3-methoxy-5-methylheptanoate1896110: Inhibition of tubulin (unknown origin) polymerization assessed as reduction in microtubule formation measured for 20 mins by spectrophotometric analysisic500.0042uM
3-methoxy-6-[4-(3,4,5-trimethoxyphenyl)-1H-pyrazol-5-yl]benzene-1,2-diol1929685: Inhibition of tubulin polymerization in human SH-SY5Y cells incubated for 24 hrs by SDS-PAGE based analysisic500.0054uM
2-methoxy-5-[1-(3,4,5-trimethoxyphenyl)ethenyl]phenol1862628: Inhibition of tubulin polymerization in human HeLa cells assessed as microtubule network polymerization after 30 mins by immunofluorescence analysisic500.0060uM
(E)-1-[1-(4-chlorophenyl)-5-methyltriazol-4-yl]-3-(3,4-dimethoxyphenyl)prop-2-en-1-one1689700: Inhibition of Tubulin in human RPMI-8226 cells incubated for 2 hrs by ELISAic500.0098uM
N-(1,3-benzodioxol-5-yl)-5-[2-(3,5-dimethoxyphenoxy)-3-pyridinyl]-1H-1,2,4-triazol-3-amine256882: Displacement of [3H]colchicine from tubulinki0.0100uM
N-(2,3-dihydro-1,4-benzodioxin-6-yl)-5-[2-(pyridin-2-ylmethylamino)phenyl]-1,3-oxazol-2-amine261214: Displacement of [3H]colchicine from tubulin at 65 nMic500.0100uM
[(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] acetate2126113: Displacement of fluorescent Maytansine probe from tubulin (unknown origin) assessed as dissociation constant by competitive binding based fluorescence anisotropykd0.0110uM
[(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]propanoate2126113: Displacement of fluorescent Maytansine probe from tubulin (unknown origin) assessed as dissociation constant by competitive binding based fluorescence anisotropykd0.0140uM
N-(2,3-dihydro-1,4-benzodioxin-6-yl)-5-[2-(3,5-dimethoxyphenoxy)-3-pyridinyl]-1H-1,2,4-triazol-3-amine256882: Displacement of [3H]colchicine from tubulinki0.0200uM
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-carboxylate214333: The compound tested for the inhibition of tubulin polymerization.ic500.0200uM
(E)-3-[5-[(2-cyanoquinolin-4-yl)-methylamino]-2-methoxyphenyl]-N-hydroxyprop-2-enamide1862628: Inhibition of tubulin polymerization in human HeLa cells assessed as microtubule network polymerization after 30 mins by immunofluorescence analysisic500.0200uM
[(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-ynoate2126113: Displacement of fluorescent Maytansine probe from tubulin (unknown origin) assessed as dissociation constant by competitive binding based fluorescence anisotropykd0.0200uM
N-(4-methoxyphenyl)-N,5-dimethylfuro[2,3-d]pyrimidin-4-amine1635267: Induction of microtubule depolymerization in human A10 cells incubated for 18 hrs by indirect immunofluorescence analysisec500.0240uM
(2R,3R)-3-ethyl-2-[(E,2R,3S,4R,5S)-2-hydroxy-4-methoxy-3,5-dimethylnon-7-enyl]-2,3-dihydropyran-6-one1572465: Inhibition of tubulin alpha in human A2780 cells assessed as reduction in cell growthic500.0260uM
N-(2,3-dihydro-1,4-benzodioxin-6-yl)-5-[2-(pyridin-3-ylmethylamino)-3-pyridinyl]-1,3,4-oxadiazol-2-amine261214: Displacement of [3H]colchicine from tubulin at 65 nMic500.0300uM
N-(1,3-benzodioxol-5-yl)-5-[2-(pyridin-4-ylmethylamino)-3-pyridinyl]-1,3,4-oxadiazol-2-amine261214: Displacement of [3H]colchicine from tubulin at 65 nMic500.0300uM
N-(1,3-benzodioxol-5-yl)-5-[2-(pyridin-2-ylmethylamino)-3-pyridinyl]-1,3,4-oxadiazol-2-amine261214: Displacement of [3H]colchicine from tubulin at 65 nMic500.0300uM
Paclitaxel260235: Effect on induction of mitotic arrest by phosphohistone H3 (pH3) assayec500.0310uM
6-(3-chloro-6,11,11-trioxobenzo[b][1,4]benzothiazepin-5-yl)-N-hydroxyhexanamide580932: Inhibition of HDAC activity in human NB4 cells assessed as acetylated tubulin after 24 hrs by Western blot analysisec500.0400uM
N,5-dimethyl-N-(4-methylsulfanylphenyl)furo[2,3-d]pyrimidin-4-amine1635267: Induction of microtubule depolymerization in human A10 cells incubated for 18 hrs by indirect immunofluorescence analysisec500.0450uM
[7-(3-hydroxyprop-1-ynyl)-6-methoxy-2H-indazol-3-yl]-(3,4,5-trimethoxyphenyl)methanone280080: Displacement of [3H]colchicine from tubulin in MCF7 cellsic500.0460uM
(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-tetrone2061859: Binding affinity to tubulin (unknown origin) assessed as dissociation constant by SPR analysiskd0.0470uM
N-hydroxy-6-(3-methoxy-6,11,11-trioxobenzo[b][1,4]benzothiazepin-5-yl)hexanamide580932: Inhibition of HDAC activity in human NB4 cells assessed as acetylated tubulin after 24 hrs by Western blot analysisec500.0500uM
N-hydroxy-6-(6,11,11-trioxobenzo[b][1,4]benzothiazepin-5-yl)hexanamide580932: Inhibition of HDAC activity in human NB4 cells assessed as acetylated tubulin after 24 hrs by Western blot analysisec500.0500uM
5-[2-(3,5-dimethoxyphenoxy)-3-pyridinyl]-N-(3-methoxyphenyl)-1H-1,2,4-triazol-3-amine256882: Displacement of [3H]colchicine from tubulinki0.0500uM
[(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] benzoate2126113: Displacement of fluorescent Maytansine probe from tubulin (unknown origin) assessed as dissociation constant by competitive binding based fluorescence anisotropykd0.0510uM
N-ethyl-N-(4-methoxyphenyl)-5-methylfuro[2,3-d]pyrimidin-4-amine1635267: Induction of microtubule depolymerization in human A10 cells incubated for 18 hrs by indirect immunofluorescence analysisec500.0530uM
3-[3-(1,3-benzodioxol-5-ylamino)-1H-1,2,4-triazol-5-yl]-N-(3,5-dimethoxyphenyl)pyridin-2-amine256882: Displacement of [3H]colchicine from tubulinki0.0600uM
Vinblastine214333: The compound tested for the inhibition of tubulin polymerization.ic500.0700uM
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-carboxylate214333: The compound tested for the inhibition of tubulin polymerization.ic500.0700uM
N-(2,3-dihydro-1,4-benzodioxin-6-yl)-5-[3-(pyridin-2-ylmethylamino)thiophen-2-yl]-1,3,4-oxadiazol-2-amine261214: Displacement of [3H]colchicine from tubulin at 65 nMic500.0750uM
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-carboxylate214333: The compound tested for the inhibition of tubulin polymerization.ic500.0800uM
4-methoxy-2-[(Z)-2-(3,4,5-trimethoxyphenyl)ethenyl]thiophene1267532: Inhibition of Tubulin polymerization in human HeLa cells assessed as decrease in dynamic tyrosinated microtubules after 2 hrs by microplate reader analysisec500.0810uM
N-[2-[[(E)-(2,4-dihydroxyphenyl)methylideneamino]carbamoyl]phenyl]furan-2-carboxamide1882654: Inhibition of tubulin polymerization (unknown origin)ic500.0876uM
N-hydroxy-6-(3-methoxy-6-oxobenzo[b][1,4]benzoxazepin-5-yl)hexanamide580932: Inhibition of HDAC activity in human NB4 cells assessed as acetylated tubulin after 24 hrs by Western blot analysisec500.0900uM
N-(3,5-dimethoxyphenyl)-3-[3-(3-methoxyanilino)-1H-1,2,4-triazol-5-yl]pyridin-2-amine256882: Displacement of [3H]colchicine from tubulinki0.1000uM
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-carboxylate214333: The compound tested for the inhibition of tubulin polymerization.ic500.1000uM
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-carboxylate214333: The compound tested for the inhibition of tubulin polymerization.ic500.1000uM
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-carboxylate214333: The compound tested for the inhibition of tubulin polymerization.ic500.1000uM

CTD chemical–gene interactions

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

ChemicalActions (top 5)PubMed papers
sodium arsenitedecreases expression, increases expression3
bisphenol Aaffects expression, affects cotreatment, decreases expression2
perfluorooctanoic acidaffects cotreatment, affects expression, decreases expression2
Air Pollutantsaffects cotreatment, decreases expression, increases abundance, increases expression2
Benzo(a)pyreneaffects methylation, increases expression2
Copperaffects binding, decreases expression2
Hydrogen Peroxideaffects cotreatment, decreases expression2
Silicon Dioxidedecreases acetylation, decreases reaction, affects secretion2
Tobacco Smoke Pollutiondecreases expression, increases metabolic processing2
tert-Butylhydroperoxidedecreases expression2
GSK-J4decreases expression1
FR900359affects phosphorylation1
bisphenol Faffects cotreatment, decreases expression1
ammonium 2,3,3,3-tetrafluoro-2-(heptafluoropropoxy)-propanoateaffects expression, affects cotreatment1
beauvericinincreases expression, affects cotreatment1
alpha-pineneaffects cotreatment, decreases expression, increases abundance1
decabromobiphenyl etherdecreases expression1
tris(2-butoxyethyl) phosphateaffects expression1
arseniteaffects binding, increases reaction1
2,6-dichloro-4-nitrophenolincreases expression1
tris(1,3-dichloro-2-propyl)phosphatedecreases expression1
zinc chlorideincreases expression1
zinc chromateincreases abundance, decreases expression1
4-hydroxy-2-nonenalaffects binding1
coumarinincreases phosphorylation1
methacrylaldehydeincreases abundance, affects cotreatment, decreases expression1
diallyl trisulfidedecreases expression1
pinosylvindecreases expression1
cordycepinaffects binding, decreases reaction, decreases expression, affects metabolic processing1
di-n-butylphosphoric acidaffects expression1

ChEMBL screening assays

1689 unique, capped per target: 1648 binding, 35 functional, 6 admet

Representative assays (with source publication via chembl_document):

Assay IDTypeDescriptionSource paper
CHEMBL1009021BindingInhibition of tubulin polymerization in human MCF7 cells at 1 uM after 2 hrs by SDS-PAGEA new cytotoxic epothilone from modified polyketide synthases heterologously expressed in Myxococcus xanthus. — J Nat Prod
CHEMBL4146506ADMETInhibition of tubulin polymerization in human HaCaT cells assessed as chromatin condensation at 1 uM after 24 hrs by Hoechst 33258 staining-based fluorescence microscopic analysisDesign, synthesis, and biological evaluation of novel combretastatin A-4 thio derivatives as microtubule targeting agents. — Eur J Med Chem
CHEMBL5056161FunctionalInhibition of tubulin polymerization (unknown origin) assessed as fluorescence intensity measured for 90 mins by DAPI based microplate readerDesign, 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

Clinical trials (associated diseases)

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

TrialPhaseStatusTitle
NCT00331656PHASE4UNKNOWNComparative Study of Non-Invasive Mask Ventilation vs Cuirass Ventilation in Patients With Acute Respiratory Failure.
NCT00994552PHASE4UNKNOWNComparison of Pressure Support and Pressure Control Ventilation in Chronic Respiratory Failure
NCT00839033PHASE3TERMINATEDEvaluation of a Mechanical Device During Acute Respiratory Failure in Patients With Neuromuscular Disorders
NCT00942227PHASE3COMPLETEDThe Value of Traction in Treatment of Lumbar Radiculopathy
NCT00979108PHASE3COMPLETEDThe Value of Traction in the Treatment of Cervical Radiculopathy
NCT01826487PHASE3COMPLETEDPhase 3 Study of Ataluren in Participants With Nonsense Mutation Duchenne Muscular Dystrophy (nmDMD)
NCT02090959PHASE3TERMINATEDAn Extension Study of Ataluren (PTC124) in Participants With Nonsense Mutation Dystrophinopathy
NCT02436096PHASE3COMPLETEDA Study to Evaluate eFFIcacy and Safety of Sublingual TNX-102 SL Tablet Taken at Bedtime in Patients With fibRoMyalgia
NCT02829814PHASE3TERMINATEDRepeat of: A Study to Evaluate Efficacy and Safety of Sublingual TNX-102 SL Tablet Taken at Bedtime in Patients With Fibromyalgia
NCT03179631PHASE3COMPLETEDLong-Term Outcomes of Ataluren in Duchenne Muscular Dystrophy
NCT05126758PHASE3ACTIVE_NOT_RECRUITINGA Study of Deramiocel (CAP-1002) in Ambulatory and Non-Ambulatory Patients With Duchenne Muscular Dystrophy
NCT05156320PHASE3COMPLETEDEfficacy and Safety of Apitegromab in Patients With Later-Onset Spinal Muscular Atrophy Treated With Nusinersen or Risdiplam
NCT05337553PHASE3ACTIVE_NOT_RECRUITINGA Study to Evaluate the Efficacy and Safety of Taldefgrobep Alfa in Participants With Spinal Muscular Atrophy
NCT05626855PHASE3ACTIVE_NOT_RECRUITINGLong-Term Safety & Efficacy of Apitegromab in Patients With SMA Who Completed Previous Trials of Apitegromab
NCT06672237PHASE3RECRUITINGA Phase 3 Study of NTLA-2001 in ATTRv-PN
NCT01074359PHASE2TERMINATEDSafety and Efficacy Study of A0001 in Patients With the A3243G Mitochondrial DNA Point Mutation
NCT01371149PHASE2COMPLETEDPatient -Ventilator Interaction in Chronic Respiratory Failure
NCT02022072PHASE2TERMINATEDEvaluation of Vital Capacity
NCT03127514PHASE2COMPLETEDAMX0035 in Patients With Amyotrophic Lateral Sclerosis (ALS)
NCT03406780PHASE2COMPLETEDA Study of CAP-1002 in Ambulatory and Non-Ambulatory Patients With Duchenne Muscular Dystrophy
NCT03921528PHASE2COMPLETEDAn Active Treatment Study of SRK-015 in Patients With Type 2 or Type 3 Spinal Muscular Atrophy
NCT05479981PHASE2COMPLETEDExtension of AOC 1001-CS1 (MARINA) Study in Adult Myotonic Dystrophy Type 1 (DM1) Patients
NCT06339580PHASE2RECRUITINGAssessment of Volume-targeted Ventilation in Patients With Neuromuscular Disease
NCT07071935PHASE2NOT_YET_RECRUITINGA Clinical Trial of Early Ventilation in Amyotrophic Lateral Sclerosis (EVENT ALS)
NCT07287189PHASE2RECRUITINGPhase 2 Study of SAT-3247 in Pediatric Ambulatory Patients
NCT00252252PHASE1COMPLETEDAutoVPAP Versus VPAP; Assessment of Sleep and Ventilation
NCT01560741PHASE1UNKNOWNTelemedicine and Ventilator Titration in Chronic Respiratory Patients Initiating Non-invasive Ventilation
NCT01621984PHASE1COMPLETEDTherapeutic Riding and Neuromuscular Disease
NCT01758510PHASE1COMPLETEDSafety Study of HLA-haplo Matched Allogenic Bone Marrow Derived Stem Cell Treatment in Amyotrophic Lateral Sclerosis
NCT03440034PHASE1COMPLETEDStudy of Pioglitazone in Sporadic Inclusion Body Myositis
NCT05730842PHASE1COMPLETEDAbsorption, Metabolism, Excretion and Absolute Bioavailability of EDG-5506 in Healthy Volunteers
NCT03059420Not specifiedRECRUITINGGenetic Studies of Strabismus, Congenital Cranial Dysinnervation Disorders (CCDDs), and Their Associated Anomalies
NCT03272802PHASE2/PHASE3UNKNOWNTreatment Effect of Edaravone in Patients With Amyotrophic Lateral Sclerosis (ALS)
NCT00860951PHASE1/PHASE2COMPLETEDP300 Brain Computer Interface Keyboard to Operate Assistive Technology
NCT02362425PHASE1/PHASE2COMPLETEDAntioxidant Therapy in RYR1-Related Congenital Myopathy
NCT00001201Not specifiedCOMPLETEDEvaluation of Neuromuscular Disease
NCT00002044Not specifiedCOMPLETEDA Pilot Study To Evaluate the Effect of Retrovir (Zidovudine: AZT) in the Treatment of Human Immunodeficiency Virus (HIV) Associated Dementia and Neuromuscular Diseases
NCT00004553Not specifiedCOMPLETEDElectromyography to Diagnose Neuromuscular Disorders
NCT00015470Not specifiedCOMPLETEDDiagnostic Evaluation of Patients With Neuromuscular Disease
NCT00017745Not specifiedCOMPLETEDPhenotype/Genotype Correlations in Neuromuscular Disorders