NUMA1

gene
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Also known as NUMA

Summary

NUMA1 (nuclear mitotic apparatus protein 1, HGNC:8059) is a protein-coding gene on chromosome 11q13.4, encoding Nuclear mitotic apparatus protein 1 (Q14980). Microtubule (MT)-binding protein that plays a role in the formation and maintenance of the spindle poles and the alignement and the segregation of chromosomes during mitotic cell division. It is a selective cancer dependency (DepMap: 49.8% of cell lines).

This gene encodes a large protein that forms a structural component of the nuclear matrix. The encoded protein interacts with microtubules and plays a role in the formation and organization of the mitotic spindle during cell division. Chromosomal translocation of this gene with the RARA (retinoic acid receptor, alpha) gene on chromosome 17 have been detected in patients with acute promyelocytic leukemia. Alternative splicing results in multiple transcript variants.

Source: NCBI Gene 4926 — RefSeq curated summary.

At a glance

  • GWAS associations: 6
  • Clinical variants (ClinVar): 256 total — 1 pathogenic
  • Phenotypes (HPO): 36
  • Druggable target: yes — 1 molecules with ChEMBL bioactivity
  • Cancer driver (intOGen): loss-of-function (tumor-suppressor-like) across 2 cancer types
  • Cancer dependency (DepMap): dependent in 49.8% of screened cell lines
  • MANE Select transcript: NM_006185

Identifiers

Gene identifiers

FieldValue
HGNC IDHGNC:8059
Approved symbolNUMA1
Namenuclear mitotic apparatus protein 1
Location11q13.4
Locus typegene with protein product
StatusApproved
AliasesNUMA
Ensembl geneENSG00000137497
Ensembl biotypeprotein_coding
OMIM164009
Entrez4926

Gene structure

Transcript identifiers

Ensembl transcripts: 54 — 43 protein_coding, 5 retained_intron, 5 protein_coding_CDS_not_defined, 1 nonsense_mediated_decay

ENST00000351960, ENST00000358965, ENST00000366394, ENST00000368959, ENST00000393695, ENST00000534971, ENST00000534987, ENST00000535087, ENST00000535111, ENST00000535838, ENST00000535947, ENST00000536119, ENST00000537217, ENST00000537905, ENST00000537930, ENST00000540588, ENST00000540626, ENST00000540843, ENST00000541262, ENST00000541584, ENST00000541641, ENST00000541719, ENST00000542977, ENST00000543009, ENST00000543450, ENST00000543937, ENST00000544129, ENST00000544238, ENST00000545721, ENST00000546036, ENST00000546131, ENST00000613205, ENST00000620566, ENST00000863445, ENST00000863446, ENST00000863447, ENST00000863448, ENST00000863449, ENST00000863450, ENST00000863451, ENST00000863452, ENST00000921275, ENST00000921276, ENST00000921277, ENST00000921278, ENST00000967521, ENST00000967522, ENST00000967523, ENST00000967524, ENST00000967525, ENST00000967526, ENST00000967527, ENST00000967528, ENST00000967529

RefSeq mRNA: 2 — MANE Select: NM_006185 NM_001286561, NM_006185

CCDS: CCDS31633, CCDS66156

Canonical transcript exons

ENST00000393695 — 27 exons

ExonStartEnd
ENSE000009274977200868872008845
ENSE000009274987200896772009185
ENSE000009274997200926872009387
ENSE000009275007201078672010854
ENSE000009902527201240172012442
ENSE000014034607206984272069911
ENSE000024395337201640872016530
ENSE000024560337201768772017827
ENSE000025148087201289572016260
ENSE000034868297200718972007435
ENSE000034874817201882372018980
ENSE000034959857203590272035975
ENSE000035224337201839672018513
ENSE000035409067202233972022419
ENSE000035484647202920572029290
ENSE000036190707200523372005369
ENSE000036242897200464072004816
ENSE000036353977200603572006263
ENSE000036378427201949472019617
ENSE000036485587200422572004341
ENSE000036564927201818372018300
ENSE000036837327202120472021291
ENSE000036860177202427472024353
ENSE000036923337200388772004099
ENSE000036931827202306572023147
ENSE000039003237200286472003538
ENSE000039038647208045872080542

Expression profiles

Bgee: expression breadth ubiquitous, 294 present calls, max score 99.27.

FANTOM5 (CAGE): breadth ubiquitous, TPM avg 64.5793 / max 355.8293, expressed in 1825 samples.

FANTOM5 promoters (21 alternative TSS)

Promoter IDTPM avgSamples expressed
12114322.05931785
12113020.28121729
1211416.67021394
1211373.4666939
1211352.21221069
1211361.8502788
1211421.5771814
1211441.2795480
1211281.2670703
1211400.8529242

Top tissues by expression

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

TissueAnatomy IDExpression scoreQuality
right uterine tubeUBERON:000130299.27gold quality
body of uterusUBERON:000985399.09gold quality
endocervixUBERON:000045899.01gold quality
left ovaryUBERON:000211998.99gold quality
right ovaryUBERON:000211898.94gold quality
mucosa of stomachUBERON:000119998.90gold quality
muscle layer of sigmoid colonUBERON:003580598.90gold quality
right lobe of thyroid glandUBERON:000111998.84gold quality
ectocervixUBERON:001224998.84gold quality
ventricular zoneUBERON:000305398.81gold quality
esophagogastric junction muscularis propriaUBERON:003584198.77gold quality
right hemisphere of cerebellumUBERON:001489098.76gold quality
skin of abdomenUBERON:000141698.75gold quality
skin of legUBERON:000151198.74gold quality
lower esophagusUBERON:001347398.72gold quality
lower esophagus muscularis layerUBERON:003583398.72gold quality
cerebellar hemisphereUBERON:000224598.66gold quality
left lobe of thyroid glandUBERON:000112098.64gold quality
cerebellar cortexUBERON:000212998.61gold quality
tibial nerveUBERON:000132398.58gold quality
adenohypophysisUBERON:000219698.57gold quality
ganglionic eminenceUBERON:000402398.54gold quality
left uterine tubeUBERON:000130398.53gold quality
small intestine Peyer’s patchUBERON:000345498.52gold quality
lower esophagus mucosaUBERON:003583498.50gold quality
transverse colonUBERON:000115798.47gold quality
minor salivary glandUBERON:000183098.46gold quality
right coronary arteryUBERON:000162598.45gold quality
body of stomachUBERON:000116198.40gold quality
popliteal arteryUBERON:000225098.37gold quality

Single-cell (SCXA)

Detected in 3 experiment(s), a significant marker in 1.

ExperimentMarker?Max mean expression
E-MTAB-6386no868.19
E-MTAB-7303no665.33
E-ANND-3no0.00

Regulation

Is transcription factor: no

miRNA regulators (miRDB)

46 targeting NUMA1, 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-453499.9966.581907
HSA-MIR-365899.9673.874379
HSA-MIR-4725-3P99.9669.532520
HSA-MIR-6780B-5P99.9669.602562
HSA-MIR-448799.9664.581252
HSA-MIR-808299.9567.271170
HSA-MIR-314399.9371.963104
HSA-MIR-124-3P99.8973.743043
HSA-MIR-506-3P99.8973.553057
HSA-MIR-605-3P99.8869.221833
HSA-MIR-427199.8868.322244
HSA-MIR-548D-3P99.8770.674362
HSA-MIR-548BB-3P99.8670.584354
HSA-MIR-548AC99.8470.774351
HSA-MIR-548H-3P99.8470.804349
HSA-MIR-548Z99.8470.804349
HSA-MIR-4699-3P99.7170.153142
HSA-MIR-120899.7068.281533
HSA-MIR-397599.6265.97697
HSA-MIR-361299.4566.021333
HSA-MIR-65099.4565.771309
HSA-MIR-6882-5P99.3571.131206
HSA-MIR-4695-5P99.0664.871151
HSA-MIR-6770-5P98.9766.761853
HSA-MIR-7155-5P98.6566.141290
HSA-MIR-4700-5P98.6367.431915
HSA-MIR-6873-5P98.4566.141417
HSA-MIR-5088-3P98.2966.631310
HSA-MIR-808997.7466.211698
HSA-MIR-4667-5P97.6166.671683

Functional genomics

DepMap (CRISPR cell-line fitness): dependent in 49.8% of screened cell lines.

Literature-anchored findings (GeneRIF, showing 40)

  • A domain within the C-terminal tail of NuMA interacts with tubulin and induces bundling and stabilisation of microtubules and leads to formation of abnormal mitotic spindles. (PMID:11956313)
  • NuMA is cleaved differently in Jurkat T and HeLa cells, suggesting that different sets of caspases are activated in these cell lines. The normal diffuse intranuclear distribution of NuMA changed during apoptosis. (PMID:12508117)
  • role in development of myelodi leukemia with promyelocytic features (PMID:14737102)
  • Proteins and open reading frames with a NuMA C terminus distal portion like region were found in a diverse set of vertebrate species including mammals, birds, amphibia, and early teleost fish. (PMID:15388855)
  • Multiple mechanisms regulate NUMA1 dynamics at spindle poles. (PMID:15561764)
  • concluded that variations in the NuMA gene are likely responsible for the observed increased breast cancer risk (PMID:15684076)
  • NuMA plays diverse important roles in vertebrate cells [review] (PMID:16146802)
  • NuMA has a role in mammary epithelial differentiation by influencing the organization of chromatin. (PMID:17108325)
  • point to the Rae1-NuMA interaction as a critical element for normal spindle formation in mitosis (PMID:17172455)
  • NuMA is a structural element in maintaining nuclear integrity. (PMID:17401638)
  • critical spindle pole-associated mechanism, called the END (Emi1/NuMA/dynein-dynactin) network, that spatially restricts APC/C activity in early mitosis (PMID:17609108)
  • The entire coding region and exon-intron boundaries of NuMa were screened in 92 familial breast cancer patients & the results do not support the role of NuMA variants as breast cancer susceptibility alleles. (PMID:18331640)
  • Kaposi’s sarcoma-associated herpesvirus-encoded LANA can interact with the nuclear mitotic apparatus protein to regulate genome maintenance and segregation. (PMID:18417561)
  • Inhibiting Crm1 in early metaphase causes the formation of excess acentriolar spindle poles containing NuMA and B23, but does not affect centrosome numbers. (PMID:19522705)
  • The levels of urinary NMP22 and CK18 in the patients with transitional cell carcinoma of the bladder were significantly higher than those in the non-transitional cell carcinoma of the bladder. (PMID:19615282)
  • Data suggest that pADPr provides a dynamic cross-linking function at spindle poles by extending from covalent modification sites on PARP-5a and NuMA and binding noncovalently to NuMA and that this function helps promote assembly of exactly two poles. (PMID:19759176)
  • These results suggest that NuMA may provide structural support in the interphase nucleus by contributing to the organization of chromatin. (PMID:20467816)
  • Ric-8A and Gi alpha recruit LGN, NuMA, and dynein to the cell cortex to help orient the mitotic spindle. (PMID:20479129)
  • Phenotype onset is correlated with NuMA-RARalpha copy number; mice with higher copy number developing disease later than those with lower copy number. (PMID:21255834)
  • Accurate distribution of NuMA is important for oocyte maturation, zygote and embryo development in humans. Proper assembly of NuMA is likely necessary for bipolar spindle organization and human oocyte developmental competence. (PMID:21297155)
  • NuMA is expressed in interphase nuclei of fibroblasts and oocytes. (PMID:21406448)
  • nuclear matrix protein 22 (nuclear mitotic apparatus protein, NuMA) has a role in upper tract urothelial tumors. (PMID:21865670)
  • During apoptotic rearrangement of interchromatin granule clusters, the nuclear matrix (NuMa rearrangement) and chromatin are closely associated. This process occurs in defined stages and depends on the activity of protein phosphatases, caspases and CAD. (PMID:22023725)
  • Without functional NuMA, microtubules lose connection to meiosis I spindle poles, resulting in highly disorganized early spindle assembly. (PMID:22552228)
  • Low NUMA1 is associtated with glioblastoma. (PMID:22619067)
  • NuMA expression was upregulated in tumours, with a significant association with disease stage in mucinous EOC subtypes, lymph node involvement and patient age (PMID:22719996)
  • Studies indicate that the Inscuteable (Insc)and NuMA are mutually exclusive interactors of LGN. (PMID:22977735)
  • Phosphorylation of NuMA by aurora-A is important for cell survival. (PMID:23097092)
  • Numa regulates spindle assemby in conjunction with Eg5. (PMID:23368718)
  • Data indicate that dynein- and astral microtubule-mediated transport of Galphai/LGN/nuclear mitotic apparatus (NuMA) complex from cell cortex to spindle poles. (PMID:23389635)
  • NuMA is required for the recruitment of cyclin-dependent kinase 8, a component of the Mediator complex and a promoter of p53-mediated p21 gene function. (PMID:23589328)
  • ectopic expression of BRAP2 inhibits nuclear localization of HMG20A and NuMA1, and prevents nuclear envelope accumulation of SYNE2. (PMID:23707952)
  • ectopic expression of NuMA can manipulate endogenous p53 and p21 transcriptional expression during interphase. (PMID:23828576)
  • NuMA phosphorylation by CDK1 couples mitotic progression with cortical dynein function. (PMID:23921553)
  • Hepatocyte Par1b defines lumen position in concert with the position of the astral microtubule anchoring complex LGN-NuMA to yield the distinct epithelial division phenotypes. (PMID:24165937)
  • The mitosis-dependent dynamic SUMO-1 modification of NuMA might contribute to NuMA-mediated formation and maintenance of mitotic spindle poles during mitosis. (PMID:24309115)
  • Retinoblastoma protein (pRB) have a novel function in regulating the mitotic function of NuMA and spindle organization, which are required for proper cell cycle progression. (PMID:24350565)
  • Study finds that frictional forces increase nonlinearly with microtubule-associated proteins (MAP) velocity across microtubules and depend on filament polarity, with NuMA’s friction being lower when moving toward minus ends, EB1’s lower toward plus ends, and PRC1’s exhibiting no directional preference. (PMID:24725408)
  • Letter: risk factors for false positive results when using urinary NMP22 as biomarker for early detection of bladder cancer. (PMID:24976592)
  • NuMA interacts with phosphoinositides and links the mitotic spindle with the plasma membrane.During anaphase correct NuMA localization is mediated by direct membrane phospholipid binding. (PMID:24996901)

Cross-species orthologs

4 orthologs

OrganismSymbolGene ID
danio_rerionuma1ENSDARG00000102483
mus_musculusNuma1ENSMUSG00000066306
rattus_norvegicusNuma1ENSRNOG00000000417
drosophila_melanogasterGCC185FBGN0037979

Paralogs (3): GOLGA3 (ENSG00000090615), CEP164 (ENSG00000110274), GCC2 (ENSG00000135968)

Protein

Protein identifiers

Nuclear mitotic apparatus protein 1Q14980 (reviewed: Q14980)

Alternative names: Nuclear matrix protein-22, Nuclear mitotic apparatus protein, SP-H antigen

All UniProt accessions (18): Q14980, F5GWA2, F5GWK2, F5GZW1, F5H068, F5H073, F5H0Z7, F5H1L0, F5H2F3, F5H3L6, F5H4J1, F5H4Y4, F5H6Y5, F5H763, F5H7R5, F8W6T3, H0YFY6, K4DIE0

UniProt curated annotations — full annotation on UniProt →

Function. Microtubule (MT)-binding protein that plays a role in the formation and maintenance of the spindle poles and the alignement and the segregation of chromosomes during mitotic cell division. Functions to tether the minus ends of MTs at the spindle poles, which is critical for the establishment and maintenance of the spindle poles. Plays a role in the establishment of the mitotic spindle orientation during metaphase and elongation during anaphase in a dynein-dynactin-dependent manner. In metaphase, part of a ternary complex composed of GPSM2 and G(i) alpha proteins, that regulates the recruitment and anchorage of the dynein-dynactin complex in the mitotic cell cortex regions situated above the two spindle poles, and hence regulates the correct oritentation of the mitotic spindle. During anaphase, mediates the recruitment and accumulation of the dynein-dynactin complex at the cell membrane of the polar cortical region through direct association with phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2), and hence participates in the regulation of the spindle elongation and chromosome segregation. Also binds to other polyanionic phosphoinositides, such as phosphatidylinositol 3-phosphate (PIP), lysophosphatidic acid (LPA) and phosphatidylinositol triphosphate (PIP3), in vitro. Also required for proper orientation of the mitotic spindle during asymmetric cell divisions. Plays a role in mitotic MT aster assembly. Involved in anastral spindle assembly. Positively regulates TNKS protein localization to spindle poles in mitosis. Highly abundant component of the nuclear matrix where it may serve a non-mitotic structural role, occupies the majority of the nuclear volume. Required for epidermal differentiation and hair follicle morphogenesis.

Subunit / interactions. Homodimer. Also forms multiarm oligomers by association of C-terminal tail domains, oligomers may further assemble to form a hexagonal nuclear lattice-like network. Associates with the dynein-dynactin complex; this association promotes the transport and accumulation of NUMA1 at the mitotic spindle poles that is inhibited by the BRISC complex in a PLK1-dependent manner. Part of a spindle orientation complex at least composed of GNAI1, GPSM2 and NUMA1. Interacts (via C-terminus) with microtubules (MTs); this interaction is direct and promotes both MT bundle formation and stability in a dynein-dynactin complex- and CDK1-independent manner. Interacts with EPB41 and EPB41L2; these interactions are negatively regulated by CDK1 during metaphase and are important for anaphase-specific localization of NUMA1 in symmetrically dividing cells. Interacts (via C-terminus) with GPSM2 (via TPR repeats); this interaction is direct, prevented by competitive binding of INSC, is inhibited in a PLK1-dependent manner, blocks the association of NUMA1 with MTs and inhibits NUMA1-induced MT bundle formation, prevents the association of NUMA1 with SPAG5, induces mitotic spindle pole localization of GPSM2, both metaphase cell cortex localization of NUMA1 and mitotic spindle organization. Does not interact with GPSM2 during anaphase. Interacts (via C-terminus) with the nuclear importin alpha/importin beta receptor; this interaction is inhibited by RanGTP. Interacts (via C-terminus) with KPNB1; this interaction is inhibited by RanGTP and the BRISC complex. Interacts with ABRAXAS2 and the BRISC complex; these interactions regulate mitotic spindle assembly. Interacts (via N-terminal end of the coiled-coil domain) with RAE1; this interaction promotes mitotic spindle formation. Interacts (via C-terminus) with SPAG5 (via C-terminus); this interaction promotes the recruitment of SPAG5 to the MTs at spindle poles in a dynein-dynactin-dependent manner and regulates mitotic spindle organization and proper chromosome alignment during mitosis. Interacts with TNKS; this interaction occurs at the onset of mitosis. Interacts with TNKS2. Interacts with tubulin. Interacts with KHDC3L (via C-terminus).

Subcellular location. Nucleus. Nucleoplasm. Nucleus matrix. Chromosome. Cytoplasm. Cytoskeleton. Microtubule organizing center. Centrosome. Spindle pole. Cell cortex. Cell membrane. Lateral cell membrane Cytoplasm. Cytosol. Spindle pole Cytoplasm.

Post-translational modifications. Phosphorylation and dephosphorylation on Thr-2055 regulates the extent of cortical NUMA1 and the dynein-dynactin complex localization during mitotic metaphase and anaphase. In metaphase, phosphorylation on Thr-2055 occurs in a kinase CDK1-dependent manner; this phosphorylation maintains low levels of cortical dynein-dynactin complex at metaphase, and hence proper spindle positioning. In anaphase, dephosphorylated on Thr-2055 by phosphatase PPP2CA; this dephosphorylation stimulates its membrane association and with the dynein-dynactin complex its enrichment at the cell cortex, and hence robust spindle elongation. Probably also phosphorylated on Thr-2015 and Ser-2087 by CDK1; these phosphorylations may regulate its cell cortex recruitment during metaphase and anaphase. Phosphorylated on Thr-1047, Ser-1769, Ser-1772, Ser-1789 and Ser-1834 by PLK1; these phosphorylations induce cortical dynein-dynactin complex dissociation from the NUMA1-GPSM2 complex and negatively regulates cortical dynein-dynactin complex localization. ADP-ribosylated by TNKS at the onset of mitosis; ADP-ribosylation is not required for its localization to spindle poles. O-glycosylated during cytokinesis at sites identical or close to phosphorylation sites, this interferes with the phosphorylation status. Ubiquitinated with ‘Lys-63’-linked polyubiquitin chains. Deubiquitination by the BRISC complex is important for the incorporation of NUMA1 into mitotic spindle poles and normal spindle pole function, probably by modulating interactions between NUMA1, dynein-dynactin complex and importin-beta.

Domain organisation. The C-terminal tubulin-binding domain mediates direct binding to microtubules, independently of dynein-dynactin complex, and induces their bundling and stabilization. The 4.1-binding domain is necessary for its cortical stability and spindle orientation.

Miscellaneous. Also known as nuclear matrix protein-22/NMP-22/NMP22, an antigen used in diagnostic tests of bladder cancer.

Isoforms (5)

UniProt IDNamesCanonical?
Q14980-11, Numa-1, p230yes
Q14980-22
Q14980-33, Numa-m, p195
Q14980-44, Numa-s, p194
Q14980-55

RefSeq proteins (2): NP_001273490, NP_006176* (*=MANE)

Domains & families (InterPro)

IDNameType
IPR048724NuMA_N_HOOKDomain
IPR048726NuMA_LGNBDDomain
IPR051841MT-Golgi_org_proteinFamily

Pfam: PF21670

UniProt features (132 total): modified residue 49, region of interest 16, compositionally biased region 16, helix 11, mutagenesis site 9, sequence conflict 7, sequence variant 6, strand 4, cross-link 4, splice variant 4, short sequence motif 2, chain 1, turn 1, coiled-coil region 1, glycosylation site 1

Structure

Experimental structures (PDB)

5 structures.

PDBMethodResolution (Å)
6QJAX-RAY DIFFRACTION1.54
3RO2X-RAY DIFFRACTION2.3
5GXWX-RAY DIFFRACTION2.39
6HC2X-RAY DIFFRACTION4.31
9HHLELECTRON MICROSCOPY6.53

Predicted structure (AlphaFold)

ModelpLDDTFraction very-high
AF-Q14980-F165.190.00

Functional residue map

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

Post-translational modifications (53): 162, 163, 169, 203, 211, 271, 379, 388, 395, 820, 891, 1047, 1187, 1225, 1511, 1601, 1721, 1724, 1728, 1757 …

Glycosylation sites (1): 1844

Mutagenesis-validated functional residues (9):

PositionPhenotype
1910abolishes interaction with gpsm2.
1984no effect on nuclear localization.
1988abolishes nuclear localization.
2015abolishes association with the mitotic spindle. increases premature accumulation at the cell cortex during metaphase; wh
2055increases premature accumulation at the cell membrane of the polar cortical region in prophase and metaphase. reduces as
2055increases localization at the spindle poles. decreases localization at the cell cortex.
2055absence of cell membrane association even in anaphase. increased localization at spindle poles and chromosome congressio
2087abolishes association with the mitotic spindle. increases premature accumulation at the cell cortex during metaphase; wh
2106abolishes association with the mitotic spindle.

Function

Pathways and Gene Ontology

Reactome pathways

2 pathways

IDPathway
R-HSA-380320Recruitment of NuMA to mitotic centrosomes
R-HSA-68875Mitotic Prophase

MSigDB gene sets: 479 (showing top): GOBP_POSITIVE_REGULATION_OF_EPITHELIAL_CELL_DIFFERENTIATION, GGGACCA_MIR133A_MIR133B, GOBP_CHROMOSOME_ORGANIZATION, GOBP_ESTABLISHMENT_OF_SPINDLE_ORIENTATION, GOBP_REGULATION_OF_CELLULAR_RESPONSE_TO_GROWTH_FACTOR_STIMULUS, GOBP_EPITHELIUM_DEVELOPMENT, GOBP_PROTEIN_LOCALIZATION_TO_CYTOSKELETON, GOBP_REGULATION_OF_PROTEIN_POLYMERIZATION, GOBP_CYTOPLASMIC_MICROTUBULE_ORGANIZATION, GOBP_ESTABLISHMENT_OR_MAINTENANCE_OF_CELL_POLARITY, GOBP_REGULATION_OF_MICROTUBULE_BASED_PROCESS, GOBP_POSITIVE_REGULATION_OF_KERATINOCYTE_DIFFERENTIATION, GOBP_REGULATION_OF_EPIDERMIS_DEVELOPMENT, GOBP_SPINDLE_LOCALIZATION, GOBP_CHROMOSOME_LOCALIZATION

GO Biological Process (21): establishment of mitotic spindle orientation (GO:0000132), microtubule bundle formation (GO:0001578), nucleus organization (GO:0006997), positive regulation of BMP signaling pathway (GO:0030513), astral microtubule organization (GO:0030953), positive regulation of microtubule polymerization (GO:0031116), positive regulation of intracellular transport (GO:0032388), positive regulation of keratinocyte differentiation (GO:0045618), cell division (GO:0051301), meiotic cell cycle (GO:0051321), positive regulation of hair follicle development (GO:0051798), positive regulation of chromosome segregation (GO:0051984), anastral spindle assembly (GO:0055048), regulation of mitotic spindle organization (GO:0060236), regulation of metaphase plate congression (GO:0090235), positive regulation of protein localization to spindle pole body (GO:1902365), positive regulation of mitotic spindle elongation (GO:1902846), positive regulation of protein localization to cell cortex (GO:1904778), positive regulation of chromosome separation (GO:1905820), positive regulation of spindle assembly (GO:1905832), chromosome segregation (GO:0007059)

GO Molecular Function (12): structural molecule activity (GO:0005198), microtubule binding (GO:0008017), tubulin binding (GO:0015631), protein domain specific binding (GO:0019904), phosphatidylinositol binding (GO:0035091), protein-containing complex binding (GO:0044877), microtubule plus-end binding (GO:0051010), microtubule minus-end binding (GO:0051011), dynein complex binding (GO:0070840), disordered domain specific binding (GO:0097718), protein binding (GO:0005515), lipid binding (GO:0008289)

GO Cellular Component (32): spindle pole (GO:0000922), nucleus (GO:0005634), nucleoplasm (GO:0005654), chromosome (GO:0005694), centrosome (GO:0005813), spindle (GO:0005819), cytosol (GO:0005829), spindle microtubule (GO:0005876), plasma membrane (GO:0005886), cell cortex (GO:0005938), lateral plasma membrane (GO:0016328), nuclear matrix (GO:0016363), dendrite (GO:0030425), spindle pole centrosome (GO:0031616), protein-containing complex (GO:0032991), microtubule plus-end (GO:0035371), microtubule minus-end (GO:0036449), neuronal cell body (GO:0043025), cortical microtubule (GO:0055028), mitotic spindle astral microtubule (GO:0061673), extracellular exosome (GO:0070062), mitotic spindle (GO:0072686), microtubule bundle (GO:0097427), mitotic spindle pole (GO:0097431), lateral cell cortex (GO:0097575), cell cortex region (GO:0099738), cytoplasmic microtubule bundle (GO:1905720), mitotic spindle midzone (GO:1990023), cytoplasm (GO:0005737), cytoskeleton (GO:0005856), microtubule (GO:0005874), membrane (GO:0016020)

Reactome top-level categories

Rollup of top-2 pathways:

CategoryPathways
Mitotic Prometaphase1
M Phase1

GO top-level categories

Rollup of top GO terms by namespace:

CategoryTerms
cellular anatomical structure5
positive regulation of cell cycle process3
binding3
positive regulation of multicellular organismal process2
spindle assembly2
microtubule binding2
spindle2
nuclear lumen2
intracellular membraneless organelle2
cytoplasm2
cell periphery2
microtubule end2
mitotic cell cycle1
establishment of mitotic spindle localization1
establishment of spindle orientation1
microtubule cytoskeleton organization1
organelle organization1
BMP signaling pathway1
regulation of BMP signaling pathway1
positive regulation of transmembrane receptor protein serine/threonine kinase signaling pathway1
spindle organization1
cytoplasmic microtubule organization1
positive regulation of microtubule polymerization or depolymerization1
regulation of microtubule polymerization1
positive regulation of protein polymerization1
microtubule polymerization1
positive regulation of supramolecular fiber organization1
regulation of intracellular transport1
intracellular transport1
positive regulation of cellular process1
positive regulation of transport1
keratinocyte differentiation1
positive regulation of epidermal cell differentiation1
regulation of keratinocyte differentiation1
cellular process1
cell cycle1
sexual reproduction1
reproductive process1
meiotic nuclear division1
hair follicle development1

Protein interactions and networks

STRING

3474 interactions, top by confidence (×1000):

Protein AProtein BPartner UniProtScore
NUMA1GPSM2P81274949
NUMA1HAUS6Q7Z4H7919
NUMA1TNKSO95271884
NUMA1EPB41L2O43491834
NUMA1RARAP10276829
NUMA1NPM1P06748817
NUMA1ZBTB16Q05516816
NUMA1TUBG1P23258800
NUMA1KIF11P52732734
NUMA1KIFC1Q9BW19720
NUMA1HAUS1Q96CS2714
NUMA1HAUS3Q68CZ6709
NUMA1PRKAR1AP10644708
NUMA1HAUS8Q9BT25703
NUMA1DCTN1Q14203694

IntAct

189 interactions, top by confidence:

ABTypeScore
RAE1NUP98psi-mi:“MI:0914”(association)0.930
HDAC2KDM1Apsi-mi:“MI:0914”(association)0.890
MED9MED19psi-mi:“MI:0914”(association)0.790
YEATS4ZNHIT1psi-mi:“MI:0914”(association)0.790
XPCCETN3psi-mi:“MI:0914”(association)0.730
MED19MED19psi-mi:“MI:0914”(association)0.730
RAE1NUMA1psi-mi:“MI:0915”(physical association)0.710
CFTRESYT2psi-mi:“MI:2364”(proximity)0.710
TNKS2NUMA1psi-mi:“MI:0915”(physical association)0.660
NUMA1TNKS2psi-mi:“MI:0407”(direct interaction)0.660
GPSM2NUMA1psi-mi:“MI:0915”(physical association)0.600
GNAI1NUMA1psi-mi:“MI:0915”(physical association)0.600
NUMA1GNAI1psi-mi:“MI:0914”(association)0.600
NUMA1GPSM2psi-mi:“MI:0915”(physical association)0.600
CCDC57NUMA1psi-mi:“MI:0915”(physical association)0.560
FLJ13057NUMA1psi-mi:“MI:0915”(physical association)0.560
NUMA1FLJ13057psi-mi:“MI:0915”(physical association)0.560
NUMA1KRT4psi-mi:“MI:0915”(physical association)0.560

BioGRID (619): GMCL1 (Two-hybrid), CCDC57 (Two-hybrid), NUMA1 (Affinity Capture-RNA), NUMA1 (Affinity Capture-RNA), NUMA1 (Affinity Capture-RNA), NUMA1 (Two-hybrid), NUMA1 (Affinity Capture-MS), NUMA1 (Affinity Capture-MS), NUMA1 (Affinity Capture-MS), NUMA1 (Affinity Capture-MS), NUMA1 (Affinity Capture-MS), NUMA1 (Affinity Capture-MS), NUMA1 (Affinity Capture-MS), NUMA1 (Affinity Capture-MS), NUMA1 (Affinity Capture-MS)

ESM2 similar proteins: A0JMK8, A0JNT9, A2AUM9, A2BGD5, A6PWD2, A9QT41, B8JK76, E9Q1U1, O75335, O88522, P0CB05, P0CF95, Q08378, Q0KK56, Q14980, Q1LWB0, Q29RS0, Q2KJ21, Q2TAC2, Q3TMW1, Q502I3, Q5RD60, Q5U3A8, Q60952, Q66HR5, Q6DD09, Q6P132, Q6P402, Q6PGZ0, Q6PHN1, Q6TMG5, Q6ZP65, Q804T6, Q8BMK0, Q8CGU1, Q8CHW5, Q8K2I2, Q8K3K8, Q8R5M4, Q8VDC1

Diamond homologs: E9Q7G0, Q14980

SIGNOR signaling

20 interactions.

AEffectBMechanism
NUMA1up-regulatesTUBA1Bbinding
NUMA1up-regulatesTUBA1Abinding
NUMA1up-regulatesTUBA1Cbinding
NUMA1up-regulates“TUBAC Family”binding
NUMA1up-regulatesTUBA3Ebinding
NUMA1up-regulatesTUBA4Abinding
NUMA1up-regulatesTUBA8binding
NUMA1up-regulatesTUBBbinding
NUMA1up-regulatesTUBB2Abinding
NUMA1up-regulatesTUBB3binding
NUMA1up-regulatesTUBB4Abinding
NUMA1up-regulatesTUBB4Bbinding
NUMA1up-regulatesTUBB6binding
NUMA1up-regulatesTUBD1binding
NUMA1up-regulatesTUBG1binding
CDK1down-regulatesNUMA1phosphorylation
NUMA1up-regulatesTubulinbinding
EPB41“up-regulates activity”NUMA1relocalization
TBK1“up-regulates activity”NUMA1phosphorylation
PLK1“down-regulates activity”NUMA1phosphorylation

Enriched among interaction partners

Reactome pathways and GO biological processes over-represented among this gene’s 210 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
NEP/NS2 Interacts with the Cellular Export Machinery615.1×9e-04
Nuclear import of Rev protein614.6×9e-04
Rev-mediated nuclear export of HIV RNA613.8×9e-04
Transport of Ribonucleoproteins into the Host Nucleus512.9×3e-03
NS1 Mediated Effects on Host Pathways612.4×9e-04
Vpr-mediated nuclear import of PICs512.2×3e-03
Transport of the SLBP independent Mature mRNA511.8×3e-03
Transport of the SLBP Dependant Mature mRNA511.5×3e-03

GO biological processes:

GO termPartnersFoldFDR
RNA export from nucleus525.2×3e-04
establishment of mitotic spindle orientation512.9×6e-03
neuron projection morphogenesis68.9×8e-03
telomere maintenance68.6×8e-03
protein import into nucleus118.5×4e-05
heterochromatin formation68.2×8e-03
chromatin remodeling155.9×4e-05
mitotic cell cycle85.8×8e-03

Disease & clinical

Cancer significance

From intOGen — cancer-driver classification: loss-of-function (tumor-suppressor-like) across 2 cancer types — BRCA, ESCA.

Clinical variants and AI predictions

ClinVar

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

ClassificationCount (floor)
Pathogenic1
Likely pathogenic0
Uncertain significance189
Likely benign29
Benign11

Top pathogenic / likely-pathogenic (1)

Variant IDHGVSClassification
1801783NM_006185.4(NUMA1):c.3716G>C (p.Arg1239Pro)Pathogenic

SpliceAI

4466 predictions. Top by Δscore:

VariantEffectΔscore
11:72003890:G:Adonor_gain1.0000
11:72004098:GCC:Gacceptor_loss1.0000
11:72004099:CCT:Cacceptor_loss1.0000
11:72004100:C:CCacceptor_gain1.0000
11:72004219:CCTCA:Cdonor_loss1.0000
11:72004220:CTCAC:Cdonor_loss1.0000
11:72004221:TCAC:Tdonor_loss1.0000
11:72004222:CAC:Cdonor_loss1.0000
11:72004223:A:ACdonor_gain1.0000
11:72004223:A:AGdonor_loss1.0000
11:72004224:C:CCdonor_gain1.0000
11:72004224:C:Gdonor_loss1.0000
11:72004337:TTAGA:Tacceptor_gain1.0000
11:72004338:TAGA:Tacceptor_gain1.0000
11:72004339:AGA:Aacceptor_gain1.0000
11:72004340:GA:Gacceptor_gain1.0000
11:72004342:C:CCacceptor_gain1.0000
11:72004342:C:CGacceptor_loss1.0000
11:72004343:T:Gacceptor_loss1.0000
11:72004344:A:Cacceptor_gain1.0000
11:72004635:CCTA:Cdonor_loss1.0000
11:72004636:CTA:Cdonor_loss1.0000
11:72004637:TAC:Tdonor_loss1.0000
11:72004638:ACCT:Adonor_loss1.0000
11:72004639:C:Gdonor_loss1.0000
11:72004812:GAAGG:Gacceptor_gain1.0000
11:72004813:AAGG:Aacceptor_gain1.0000
11:72004814:AGG:Aacceptor_gain1.0000
11:72004814:AGGC:Aacceptor_loss1.0000
11:72004815:GG:Gacceptor_gain1.0000

AlphaMissense

13753 scored. Top likely-pathogenic:

VariantProtein changeam_pathogenicity
11:72005285:C:GR1926P0.998
11:72005313:A:GW1917R0.998
11:72005313:A:TW1917R0.998
11:72005261:A:GL1934P0.997
11:72005286:G:TR1926S0.997
11:72005294:A:GL1923P0.997
11:72005311:C:AW1917C0.997
11:72005311:C:GW1917C0.997
11:72009176:C:GA1617P0.997
11:72007224:G:TR1810S0.996
11:72005281:A:CN1927K0.995
11:72005281:A:TN1927K0.995
11:72005257:C:AK1935N0.994
11:72005257:C:GK1935N0.994
11:72013697:A:GL1269P0.994
11:72018214:A:GL316P0.994
11:72018256:A:GL302P0.994
11:72005306:C:GR1919P0.993
11:72007327:G:CF1775L0.993
11:72007327:G:TF1775L0.993
11:72007329:A:GF1775L0.993
11:72018909:A:GL219P0.993
11:72005301:C:GA1921P0.991
11:72005303:A:CI1920S0.991
11:72009153:C:AK1624N0.991
11:72009153:C:GK1624N0.991
11:72012905:A:GL1533P0.991
11:72018286:A:GL292P0.991
11:72005303:A:TI1920N0.990
11:72008836:C:GA1690P0.990

dbSNP variants (sampled 300 via entrez): RS1000061300 (11:72014287 C>T), RS1000067371 (11:72060084 A>G), RS1000076172 (11:72066970 T>C), RS1000094189 (11:72020743 T>C,G), RS1000135636 (11:72061348 G>A), RS1000200302 (11:72027309 C>T), RS1000224007 (11:72050380 A>G), RS1000273913 (11:72027639 T>A,C), RS1000300466 (11:72040764 T>C), RS1000308658 (11:72074341 A>G), RS1000423045 (11:72046974 A>G), RS1000458108 (11:72062016 T>C), RS1000526484 (11:72020922 C>T), RS1000534995 (11:72073020 C>A), RS1000542596 (11:72025693 G>A)

Disease associations

OMIM: gene MIM:164009 | disease phenotypes: MIM:612376, MIM:611451

GenCC curated gene-disease

Mondo (3): myoepithelial tumor (MONDO:0002380), acute promyelocytic leukemia (MONDO:0012883), autosomal recessive nonsyndromic hearing loss 63 (MONDO:0012670)

Orphanet (2): Acute promyelocytic leukemia (Orphanet:520), Rare autosomal recessive non-syndromic sensorineural deafness type DFNB (Orphanet:90636)

HPO phenotypes

36 total (30 of 36 shown, HPO-id order):

HPOTerm
HP:0000212Gingival overgrowth
HP:0000225Gingival bleeding
HP:0000421Epistaxis
HP:0000790Hematuria
HP:0000967Petechiae
HP:0000978Bruising susceptibility
HP:0000979Purpura
HP:0001324Muscle weakness
HP:0001824Weight loss
HP:0001873Thrombocytopenia
HP:0001875Decreased total neutrophil count
HP:0001876Pancytopenia
HP:0001882Decreased total leukocyte count
HP:0001892Abnormal bleeding
HP:0001903Anemia
HP:0001945Fever
HP:0001974Increased total leukocyte count
HP:0002027Abdominal pain
HP:0002039Anorexia
HP:0002321Vertigo
HP:0002653Bone pain
HP:0002716Lymphadenopathy
HP:0002875Exertional dyspnea
HP:0005521Disseminated intravascular coagulation
HP:0010280Stomatitis
HP:0011900Hypofibrinogenemia
HP:0012378Fatigue
HP:0025420Diffuse alveolar hemorrhage
HP:0030140Oral cavity bleeding
HP:0030955Addictive alcohol use

GWAS associations

6 associations (top):

StudyTraitp-value
GCST002804_1Antibody level in response to infection8.000000e-07
GCST003123_25Severe influenza A (H1N1) infection8.000000e-17
GCST008790_42Urinary albumin-to-creatinine ratio9.000000e-10
GCST008791_13Microalbuminuria7.000000e-06
GCST008794_34Urinary albumin-to-creatinine ratio2.000000e-09
GCST009640_17Urinary albumin-to-creatinine ratio1.000000e-09

EFO canonical traits (4, from GWAS)

EFO IDTrait name
EFO:0007034seropositivity measurement
EFO:0007035Chlamydia pneumoniae seropositivity
EFO:1001488influenza A (H1N1)
EFO:0007778urinary albumin to creatinine ratio

MeSH disease descriptors (3)

DescriptorNameTree numbers
D015473Leukemia, Promyelocytic, AcuteC04.557.337.539.275.700; C15.378.508.539.275.700
D009208MyoepitheliomaC04.557.435.585
C566951Deafness, Autosomal Recessive 63 (supp.)

Drugs & pharmacology

Drug and pharmacology data

Is drug target: yes

ChEMBL targets (1): CHEMBL5725184 (SINGLE PROTEIN)

Molecules with ChEMBL bioactivity

1 molecules (phase ≥1), by development phase (incl. off-target/promiscuous compounds). Patent mentions across the top 20 by phase: 1,538 (via chembl_molecule»patent_compound — counts attach to the compound, not the gene–compound relationship, so off-target/promiscuous molecules can dominate).

MoleculeNamePhasePatents
CHEMBL1232461MOLIBRESIB21,538

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

PharmGKB clinical annotations

1 annotations.

VariantTypeLevelDrugsPhenotypes
rs10898815Efficacy3Calcium channel blockersHypertension

PharmGKB variants

1 variants.

VariantGenesLevelScore#Clin annotsDrugs
rs10898815NUMA132.251Calcium channel blockers

ChEMBL bioactivities

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

pChemblTypeValueUnitMolecule
9.51Kd0.308nMCHEMBL3752910
9.51ED500.308nMCHEMBL3752910
7.50Kd31.84nMCHEMBL5653589
7.50ED5031.84nMCHEMBL5653589
7.22Kd60nMMOLIBRESIB
7.05IC5090nMMOLIBRESIB

PubChem BioAssay actives

4 with measured affinity, of 11 total; 3 most potent distinct compounds. Largely complementary to BindingDB; screening values are coarse (µM, 4 dp), so sub-nM hits tie at the floor.

CompoundAssayTypeValueUnit
4-methyl-3-[(1-methyl-6-pyridin-3-ylpyrazolo[3,4-d]pyrimidin-4-yl)amino]-N-[3-(trifluoromethyl)phenyl]benzamide2148900: Binding affinity to human NUMA1 incubated for 45 mins by Kinobead based pull down assaykd0.0003uM
4-methyl-3-[(2-methyl-6-pyridin-3-ylpyrazolo[3,4-d]pyrimidin-4-yl)amino]-N-[3-(trifluoromethyl)phenyl]benzamide2148900: Binding affinity to human NUMA1 incubated for 45 mins by Kinobead based pull down assaykd0.0318uM
2-[(4S)-6-(4-chlorophenyl)-8-methoxy-1-methyl-4H-[1,2,4]triazolo[4,3-a][1,4]benzodiazepin-4-yl]-N-ethylacetamide2179160: Binding affinity against NUMA1 (unknown origin) assessed as apparent dissociation constant incubated for 1 hr by colloidal coomassie staining based LC-MS/MS analysiskd0.0600uM

CTD chemical–gene interactions

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

ChemicalActions (top 5)PubMed papers
Valproic Acidaffects expression, increases methylation, affects cotreatment, decreases expression7
bisphenol Adecreases expression, decreases methylation, increases expression3
Particulate Matterincreases expression, affects cotreatment, decreases expression, increases abundance3
4-(5-benzo(1,3)dioxol-5-yl-4-pyridin-2-yl-1H-imidazol-2-yl)benzamideaffects cotreatment, increases expression, decreases expression2
Acetaminophendecreases expression, increases expression2
Air Pollutantsdecreases expression, increases abundance, increases expression2
Nickelincreases expression2
N’-(3-bromo-4-hydroxybenzylidene)-2-(9-oxo-10(9H)-acridinyl)acetohydrazideaffects localization1
FR900359affects phosphorylation1
bisphenol Fincreases expression1
TAK-243increases sumoylation1
dicrotophosincreases expression1
bufotalindecreases expression1
triphenyl phosphateaffects expression1
decabromobiphenyl etherincreases expression1
trichostatin Adecreases expression1
beta-lapachonedecreases expression1
sodium arseniteincreases abundance, affects cotreatment, decreases expression1
butyraldehydedecreases expression1
perfluorooctanoic aciddecreases expression1
manganese chlorideaffects cotreatment, decreases expression, increases abundance1
coumarindecreases phosphorylation1
beta-methylcholineaffects expression1
CGP 52608affects binding, increases reaction1
N-(oxo-5,6-dihydrophenanthridin-2-yl)-N,N-dimethylacetamide hydrochlorideincreases metabolic processing, affects binding, decreases reaction1
nutlin 3affects cotreatment, increases secretion1
ON 01910affects localization1
Grape Seed Proanthocyanidinsaffects cotreatment, decreases expression1
dorsomorphinaffects cotreatment, decreases expression1
2-(1H-indazol-4-yl)-6-(4-methanesulfonylpiperazin-1-ylmethyl)-4-morpholin-4-ylthieno(3,2-d)pyrimidineincreases expression, increases response to substance1

ChEMBL screening assays

8 unique, capped per target: 8 binding

Representative assays (with source publication via chembl_document):

Assay IDTypeDescriptionSource paper
CHEMBL5651942BindingBinding affinity to human NUMA1 incubated for 45 mins by Kinobead based pull down assayNVP-BHG712: Effects of Regioisomers on the Affinity and Selectivity toward the EPHrin Family. — ChemMedChem

Cellosaurus cell lines

3 cell lines: 2 cancer cell line, 1 transformed cell line

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

CellosaurusNameCategorySex
CVCL_A7NI2XSBCancer cell lineFemale
CVCL_D7W7Ubigene A-549 NUMA1 KOCancer cell lineMale
CVCL_D9LRUbigene HEK293 NUMA1 KOTransformed cell lineFemale

Clinical trials (associated diseases)

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

TrialPhaseStatusTitle
NCT00196768PHASE4UNKNOWNTreatment Protocol for Relapsed Acute Promyelocytic Leukemia (APL) With Arsenic
NCT00408278PHASE4COMPLETEDTreatment of Newly Diagnosed Patients With Acute Promyelocytic Leukemia (PETHEMA LPA 2005)
NCT00465933PHASE4COMPLETEDTreatment of Acute Promyelocytic Leukemia With All-Trans Retinoic Acid (ATRA) and Idarubicin (AIDA)
NCT00504764PHASE4COMPLETEDTreatment of Relapsed Promyelocytic Leukemia With Arsenic Trioxide (ATO)
NCT01987297PHASE4UNKNOWNCombined Retinoic Acid,Arsenic Trioxide and Chemo for Newly-diagnosed APL
NCT02020161PHASE4UNKNOWNClinical Guidelines for APL Treatment
NCT01226303PHASE3UNKNOWNTreatment Study for Children and Adolescents With Acute Promyelocitic Leukemia
NCT02688140PHASE3COMPLETEDStudy for Patients With Newly Diagnosed, High-risk Acute Promyelocytic Leukemia
NCT02899169PHASE3UNKNOWNTreatment of Non-high-risk Acute Promyelocytic Leukemia (APL) With Realgar-Indigo Naturalis Formula (RIF)
NCT04175587PHASE3UNKNOWNRandomized,International Multi-center Clinical Trial of RIF Plus RA for Non-high-risk APL
NCT07296445PHASE3NOT_YET_RECRUITINGA Trial to Investigate Whether Oral Arsenic Trioxide Is Similar to Intravenous Arsenic Trioxide in Pharmacokinetics, Safety, and Efficacy (LATITUDE/SDKARS-301)
NCT07503730PHASE3RECRUITINGEarly Use of Realgar-Indigo Naturalis Formula (RIF) Combined With All-trans Retinoic Acid (ATRA) for Treating Acute Promyelocytic Leukemia (APL).
NCT07504458PHASE3RECRUITINGPivotal Open-label Phase 3 Clinical Study of QTX-2101 in Adult Patients With Acute Promyelocytic Leukemia
NCT00413166PHASE2COMPLETEDAll-trans Retinoic Acid, and Arsenic +/- Idarubicin
NCT00520208PHASE2COMPLETEDSafety, Efficacy, & Pharmacokinetic Study of Tamibarotene to Treat Patients With Relapsed or Refractory APL
NCT00670150PHASE2WITHDRAWNNew Retinoid Agent Combined With Arsenic Trioxide for Untreated Acute Promyelocytic Leukemia
NCT00675870PHASE2UNKNOWNStudy of NRX 195183 Therapy for Patients With Relapsed or Refractory Acute Promyelocytic Leukemia
NCT00907582PHASE2TERMINATEDASCT for Relapsed APL After Molecular Remission
NCT01064570PHASE2UNKNOWNAIDA 2000 Guidelines
NCT01253070PHASE2COMPLETEDSorafenib Tosylate and Chemotherapy in Treating Older Patients With Acute Myeloid Leukemia
NCT01404949PHASE2COMPLETEDCombined Tretinoin and Arsenic Trioxide for Patients With Newly Diagnosed Acute Promyelocytic Leukemia Followed by Risk-Adapted Postremission Therapy
NCT01409161PHASE2RECRUITINGTretinoin and Arsenic Trioxide With or Without Gemtuzumab Ozogamicin in Treating Patients With Previously Untreated Acute Promyelocytic Leukemia
NCT03624270PHASE2UNKNOWNOral Arsenic Trioxide for Newly Diagnosed Acute Promyelocytic Leukaemia
NCT04687176PHASE2RECRUITINGFrontline Oral Arsenic Trioxide for APL
NCT04793919PHASE2RECRUITINGTreatment Study for Children and Adolescents With Acute Promyelocytic Leukemia
NCT05881265PHASE2RECRUITINGTreatment of Chidamide and Venetoclax for Retinoic Acid and Arsenic Resistant Acute Promyelocytic Leukemia
NCT06982274PHASE2RECRUITINGOral Arsenic With ATRA for Newly Diagnosed Patients With Acute Promyelocytic Leukemia
NCT03600649PHASE1UNKNOWNClinical Trial of SP-2577 (Seclidemstat) in Patients With Relapsed or Refractory Ewing or Ewing-related Sarcomas
NCT00852709PHASE1TERMINATEDPhase I Dose-Escalation Trial of Clofarabine Followed by Escalating Doses of Fractionated Cyclophosphamide in Children With Relapsed or Refractory Acute Leukemias
NCT00985530PHASE1TERMINATEDTamibarotene and Arsenic Trioxide for Relapsed Acute Promyelocytic Leukemia
NCT01902329PHASE1COMPLETEDA Safety Study of SGN-CD33A in AML Patients
NCT02086773PHASE1COMPLETEDRed Cell Transfusion Goals in Patients With Acute Leukemias
NCT02390635PHASE1RECRUITINGPET/MRI, 18F-FDG PET/CT and Whole Body MRI in Finding Extramedullary Myeloid Leukemia in Patients With Newly Diagnosed Acute Myeloid Leukemia
NCT04996030PHASE1SUSPENDEDA Study for Oral SY-2101 for Participants With Acute Promyelocytic Leukemia
NCT06882031PHASE1COMPLETEDEvaluate the Pharmacokinetics of Oral Arsenic Trioxide Solution Under Fasting and Fed Conditions, to Compare Intravenous Arsenic Trioxide, in Acute Promyelocytic Leukemia
NCT05266196PHASE1/PHASE2UNKNOWNA Rollover Protocol to Allow for Continued Access to the LSD1 Inhibitor Seclidemstat (SP-2577)
NCT06239272PHASE1/PHASE2RECRUITINGNRSTS2021, A Risk Adapted Study Evaluating Maintenance Pazopanib, Limited Margin, Dose-Escalated Radiation Therapy and Selinexor in Non-Rhabdomyosarcoma Soft Tissue Sarcoma (NRSTS)
NCT06625190PHASE1/PHASE2RECRUITINGAlpha/Beta T and B Cell Depletion With Zoledronic Acid for Solid Tumors
NCT06244420Not specifiedCOMPLETEDMalignant Myoepithelioma of Bone and Soft Tissues: Diagnostic Imaging and Histology in Relation to Prognosis
NCT00517712PHASE2/PHASE3UNKNOWNSingle Agent Arsenic Trioxide in the Treatment of Newly Diagnosed Acute Promyelocytic Leukemia