TRIM33

gene
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Also known as TIF1GAMMAFLJ11429KIAA1113TIFGAMMARFG7TF1GTIF1GPTC7

Summary

TRIM33 (tripartite motif containing 33, HGNC:16290) is a protein-coding gene on chromosome 1p13.2, encoding E3 ubiquitin-protein ligase TRIM33 (Q9UPN9). Acts as an E3 ubiquitin-protein ligase.

The protein encoded by this gene is thought to be a transcriptional corepressor. However, molecules that interact with this protein have not yet been identified. The protein is a member of the tripartite motif family. This motif includes three zinc-binding domains, a RING, a B-box type 1 and a B-box type 2, and a coiled-coil region. Three alternatively spliced transcript variants for this gene have been described, however, the full-length nature of one variant has not been determined.

Source: NCBI Gene 51592 — RefSeq curated summary.

At a glance

  • Gene–disease (curated): developmental dysplasia of the hip (Limited, GenCC)
  • GWAS associations: 17
  • Clinical variants (ClinVar): 85 total — 1 pathogenic, 1 likely-pathogenic
  • Phenotypes (HPO): 23
  • Druggable target: yes — 1 molecules with ChEMBL bioactivity
  • Cancer driver (intOGen): loss-of-function (tumor-suppressor-like) across 1 cancer types
  • MANE Select transcript: NM_015906

Identifiers

Gene identifiers

FieldValue
HGNC IDHGNC:16290
Approved symbolTRIM33
Nametripartite motif containing 33
Location1p13.2
Locus typegene with protein product
StatusApproved
AliasesTIF1GAMMA, FLJ11429, KIAA1113, TIFGAMMA, RFG7, TF1G, TIF1G, PTC7
Ensembl geneENSG00000197323
Ensembl biotypeprotein_coding
OMIM605769
Entrez51592

Gene structure

Transcript identifiers

Ensembl transcripts: 15 — 12 protein_coding, 3 protein_coding_CDS_not_defined

ENST00000358465, ENST00000369543, ENST00000448034, ENST00000476908, ENST00000478032, ENST00000492227, ENST00000925752, ENST00000925753, ENST00000925754, ENST00000925755, ENST00000925756, ENST00000925757, ENST00000925758, ENST00000964324, ENST00000964325

RefSeq mRNA: 2 — MANE Select: NM_015906 NM_015906, NM_033020

CCDS: CCDS872, CCDS873

Canonical transcript exons

ENST00000358465 — 20 exons

ExonStartEnd
ENSE00000784400114427177114427294
ENSE00000784402114424591114424755
ENSE00000784403114421436114421636
ENSE00000784404114410184114410316
ENSE00000784405114408677114408740
ENSE00000784406114406941114407100
ENSE00000784407114405410114405759
ENSE00000784408114402760114402883
ENSE00000784409114401389114401463
ENSE00000784411114397940114397990
ENSE00001215827114425449114425723
ENSE00001450301114392790114397860
ENSE00001595585114463412114463556
ENSE00001749166114464270114464388
ENSE00003521752114399457114399609
ENSE00003711583114463104114463236
ENSE00003720468114433617114433733
ENSE00003727990114427748114427894
ENSE00003729043114430798114430912
ENSE00003846759114510551114511203

Expression profiles

Bgee: expression breadth ubiquitous, 294 present calls, max score 99.22.

FANTOM5 (CAGE): breadth ubiquitous, TPM avg 32.8618 / max 333.5770, expressed in 1818 samples.

FANTOM5 promoters (6 alternative TSS)

Promoter IDTPM avgSamples expressed
1394630.79581818
139441.0880600
139450.7056438
139400.110618
139410.107628
139420.054211

Top tissues by expression

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

TissueAnatomy IDExpression scoreQuality
endometrium epitheliumUBERON:000481199.22gold quality
secondary oocyteCL:000065599.14gold quality
oocyteCL:000002398.97gold quality
choroid plexus epitheliumUBERON:000391196.75gold quality
Brodmann (1909) area 23UBERON:001355496.39gold quality
corpus epididymisUBERON:000435995.60gold quality
nippleUBERON:000203095.53gold quality
cerebellar vermisUBERON:000472095.35gold quality
tibiaUBERON:000097994.68gold quality
tongue squamous epitheliumUBERON:000691994.61gold quality
CA1 field of hippocampusUBERON:000388194.31gold quality
epithelium of nasopharynxUBERON:000195194.07gold quality
seminal vesicleUBERON:000099894.05gold quality
dorsal motor nucleus of vagus nerveUBERON:000287093.83gold quality
gingival epitheliumUBERON:000194993.82gold quality
postcentral gyrusUBERON:000258193.49gold quality
hair follicleUBERON:000207393.48gold quality
middle temporal gyrusUBERON:000277193.47gold quality
parietal lobeUBERON:000187293.39gold quality
germinal epithelium of ovaryUBERON:000130493.37gold quality
visceral pleuraUBERON:000240193.36gold quality
epithelial cell of pancreasCL:000008393.29gold quality
entorhinal cortexUBERON:000272893.26gold quality
caput epididymisUBERON:000435893.26gold quality
cauda epididymisUBERON:000436093.19gold quality
upper leg skinUBERON:000426293.09gold quality
cardia of stomachUBERON:000116292.91gold quality
urethraUBERON:000005792.86gold quality
corpus callosumUBERON:000233692.82gold quality
squamous epitheliumUBERON:000691492.81gold quality

Single-cell (SCXA)

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

ExperimentMarker?Max mean expression
E-ANND-3yes8.61

Regulation

Is transcription factor: no

Upstream regulators (CollecTRI, top): SOX2

miRNA regulators (miRDB)

389 targeting TRIM33, 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-429100.0073.442698
HSA-MIR-200B-3P100.0073.312693
HSA-MIR-200C-3P100.0073.352685
HSA-MIR-3064-3P100.0070.091254
HSA-MIR-5692A100.0074.406850
HSA-MIR-3646100.0073.565283
HSA-MIR-4776-3P100.0068.731340
HSA-MIR-3163100.0077.238605
HSA-MIR-3924100.0072.092394
HSA-MIR-1277-5P100.0073.955056
HSA-MIR-6867-5P100.0082.213464
HSA-MIR-4692100.0067.322066
HSA-MIR-12118100.0065.881270
HSA-MIR-4668-3P100.0068.742635
HSA-MIR-656-3P100.0072.152788
HSA-MIR-5011-5P100.0083.465820
HSA-MIR-3613-3P100.0076.367965
HSA-MIR-366299.9973.825684
HSA-MIR-548C-3P99.9974.017587
HSA-MIR-548AW99.9972.573559
HSA-MIR-428299.9975.366408
HSA-MIR-451499.9967.101870
HSA-MIR-371B-5P99.9975.344759
HSA-MIR-4789-3P99.9970.752484
HSA-MIR-450099.9972.722367
HSA-MIR-477599.9875.006394
HSA-MIR-19A-3P99.9875.332762
HSA-MIR-19B-3P99.9875.442754
HSA-MIR-548N99.9871.944170
HSA-MIR-1213699.9872.815713

Literature-anchored findings (GeneRIF, showing 40)

  • TIF1alpha interacts with TIF1gamma and the coiled-coil region of TIF1gamma is necessary for this interaction. (PMID:12096914)
  • Thus, Smad2/3-TIF1gamma and Smad2/3-Smad4 function as complementary effector arms in the control of hematopoietic cell fate by the TGFbeta/Smad pathway. (PMID:16751102)
  • Study reports that TIF1gamma expression is markedly down-regulated in human pancreatic tumors by quantitative RT-PCR and immunohistochemistry. (PMID:19629168)
  • Hyperthermia incurred platelet glycoprotein Ibalpha ectodomain shedding. (PMID:20158380)
  • These studies are consistent with a model in which TIF1gamma acts to ubiquitinate LDB1 leading to degradation of LDB1 and changes in transcription of LDB1-dependent promoters. (PMID:20447379)
  • Chromatin immunoprecipitation assays in human CD34(+) cells supported a TIF1gamma-dependent recruitment of positive elongation factors to erythroid genes to promote transcription elongation by counteracting Pol II pausing. (PMID:20603019)
  • regulation of adult hematopoiesis through TIF1gamma-mediated transcriptional repression of TAL1 and PU.1 target genes. (PMID:21474105)
  • TIF1gamma was almost undetectable in leukemic cells of 35% of CMML patients. This downregulation was related to the hypermethylation of CpG sequences and specific histone modifications in the gene promoter. (PMID:21537084)
  • TIF1gamma binds to and represses the plasminogen activator inhibitor 1 promoter, demonstrating a direct role of TIF1gamma in TGF-beta-dependent gene expression (PMID:21597466)
  • TIF1gamma dictates the residence time of activated Smad complexes at promoters of TGF-beta superfamily target genes. (PMID:21726812)
  • Data suggest that over-expression of TIF1gamma occurs in early stages of colorectal carcinogenesis, is inversely related with Smad4 loss, and may be a prognostic indicator for poor outcome. (PMID:22046087)
  • These results suggest that E4-ORF3 targets proteins for relocalization through a loosely homologous sequence dependent on accessibility. (PMID:22123502)
  • Study reports an essential role for TRIM33 in the activation of Gsc and Mixl1 by nodal signals, and delineate how Smads gain access to poised promoters of master regulators under the command of nodal TGF-beta signals. (PMID:22196728)
  • Adenovirus E4orf3 targets TIF1 gamma for proteasome-dependent degradation during infection. (PMID:22205733)
  • Data suggest that the formation of transient TIF1gamma-Smad2-Smad4 ternary complexes is the only one that can account for TGF-beta signaling. (PMID:22461896)
  • Tif1gamma transgene is essential for the terminal differentiation of mammary alveolar epithelial cells at the end of pregnancy and to ensure lactation. (PMID:23154409)
  • TIF1gamma is an APC/C-interacting protein that regulates APC/C function. It is not a substrate for APC/C-dependent ubiquitylation but associates specifically with the APC/C holoenzyme & Cdc20 to affect APC/C activity & progression through mitosis. (PMID:23160376)
  • Case Report: suggest that TIF1gamma expression in neoplasms not only determines the tumour activity but also causes dermatomyositis. (PMID:23407650)
  • mutation and methylation in the promoter region of TIF1gamma in non-small cell lung cancer (PMID:23676978)
  • Results identify a new TGFbeta regulatory layer, whereby sumoylation strengthens the TIF1gamma repressive action on canonical TGFbeta signaling. (PMID:23788427)
  • TRIM33 plays a role in PARP-dependent DNA damage response and regulates ALC1 activity by promoting its timely removal from sites of DNA damage. (PMID:23926104)
  • These studies demonstrate that anti-NXP-2 and anti-TIF-1gamma antibodies are frequent DM specificities (found in 55% of patients) and are present in most patients with cancer-associated dermatomyositis. (PMID:24037894)
  • Study suggests TRIM33 and NRAS-CSDE1 as candidate genes for autism, and may provide a novel insight into the etiology of autism (PMID:24189344)
  • regulates tumor growth and metastasis through inhibition of TGF-beta/Smad signaling and may serve as a novel prognostic biomarker in hepatocellular carcinoma (PMID:24954480)
  • Data indicate that tripartite motif containing 33 protein TIF1gamma promotes sumoylation of SKI-like proto-oncogene protein SnoN1 and regulates epithelial-mesenchymal transition (EMT). (PMID:25059663)
  • The ubiquitination of DHX33 by TRIM33 is lysine 63 specific and is required for the formation of the DHX33-NLRP3 inflammasome complex. (PMID:25172487)
  • The dermatomyositis autoantigen TIF1gamma is markedly up-regulated during muscle regeneration in human and mouse muscle cells. (PMID:25186009)
  • Results show that TRIM33 is significantly downregulated in clear renal cell carcinoma tissues which seems to correlate with pathologic stages and grades. (PMID:25381221)
  • Tumour suppressor TRIM33 targets nuclear beta-catenin degradation (PMID:25639486)
  • our findings reveal a new mechanism by which SOX2-mediated transcription repression of TIF1gamma promotes TGF-beta-induced epithelial-mesenchymal transition in non-small-cell lung cancer (PMID:25961934)
  • our work indicates that TIF1gamma exerts its tumor-suppressive functions in part by promoting chromosomal stability. (PMID:26282171)
  • The adenovirus E4-ORF3 protein functions as a SUMO E3 ligase for TIF-1gamma sumoylation and poly-SUMO chain elongation. (PMID:27247387)
  • suggest that SnoN suppresses TGF-betainduced epithelial-mesenchymal transition and invasion of bladder cancer cells in a TIF1gammadependent manner (PMID:27430247)
  • Data show that tripartite motif-containing protein 33 (TRIM33) silencing attenuates down-regulation of MYC and TGF-beta signaling in response to bromodomain and extraterminal domain protein inhibitors (BETi). (PMID:27432991)
  • Anti-TIF1gamma antibodies are rarely present in patients with solid cancers or paraneoplastic rheumatic syndromes. This finding strengthens the approach to using anti-TIF1gamma IgG as a marker for cancer-associated dermatomyositis. (PMID:28704599)
  • Tumors from paraneoplastic anti-TIF1gamma-positive cancer-associated myositis patients showed an increased number of genetic alterations, such as mutations and loss of heterozygosity, in TIF1 genes. (PMID:29149307)
  • Not only did anti-TIF1gamma antibodies correlate strongly with malignancy in dermatomyositis patients, but cancers were also significantly more advanced in anti-TIF1gamma-positive DM patients than in anti-TIF1gamma-negative patients. (PMID:29745874)
  • These results suggest that nuclear c-Abl-mediated tyrosine phosphorylation of TIF1gamma has a desuppressive role in TGF-beta-Smad2/3 signaling. (PMID:30177833)
  • Our findings show that circPTK2 (hsa_circ_0008305) inhibits TGF-beta-induced EMT and metastasis by controlling TIF1gamma in NSCLC, revealing a novel mechanism by which circRNA regulates TGF-beta-induced EMT and tumor metastasis, and suggesting that circPTK2 overexpression could provide a therapeutic strategy for advanced NSCLC. (PMID:30261900)
  • The expression of TIF1gamma in the muscle of idiopathic inflammatory myopathies was related to the positivity for serum anti-TIF1gamma antibody and presence of tubuloreticular bodies in the muscle biopsies. (PMID:30398003)

Cross-species orthologs

3 orthologs

OrganismSymbolGene ID
danio_reriotrim33ENSDARG00000016181
mus_musculusTrim33ENSMUSG00000033014
rattus_norvegicusTrim33ENSRNOG00000018946

Paralogs (80): MID2 (ENSG00000080561), TRIM9 (ENSG00000100505), MID1 (ENSG00000101871), MEFV (ENSG00000103313), TRIM35 (ENSG00000104228), TRIM14 (ENSG00000106785), TRIM37 (ENSG00000108395), TRIM2 (ENSG00000109654), TRIM3 (ENSG00000110171), TRIM38 (ENSG00000112343), TRIM62 (ENSG00000116525), TRIM67 (ENSG00000119283), TRIM32 (ENSG00000119401), BSPRY (ENSG00000119411), TRIM25 (ENSG00000121060), TRIM6 (ENSG00000121236), TRIM24 (ENSG00000122779), TRIM51 (ENSG00000124900), TRIM28 (ENSG00000130726), TRIM21 (ENSG00000132109), TRIM5 (ENSG00000132256), TRIM22 (ENSG00000132274), TRIM47 (ENSG00000132481), TRIM45 (ENSG00000134253), TRIM29 (ENSG00000137699), TRIM54 (ENSG00000138100), PML (ENSG00000140464), TRIM65 (ENSG00000141569), TRIM43B (ENSG00000144010), TRIM43 (ENSG00000144015), TRIM7 (ENSG00000146054), TRIM41 (ENSG00000146063), TRIM50 (ENSG00000146755), TRIM4 (ENSG00000146833), TRIM55 (ENSG00000147573), TRIM48 (ENSG00000150244), TRIM36 (ENSG00000152503), TRIM11 (ENSG00000154370), TRIM74 (ENSG00000155428), TRIM42 (ENSG00000155890)

Protein

Protein identifiers

E3 ubiquitin-protein ligase TRIM33Q9UPN9 (reviewed: Q9UPN9)

Alternative names: Ectodermin homolog, RET-fused gene 7 protein, RING-type E3 ubiquitin transferase TRIM33, Transcription intermediary factor 1-gamma, Tripartite motif-containing protein 33

All UniProt accessions (2): Q9UPN9, H0Y612

UniProt curated annotations — full annotation on UniProt →

Function. Acts as an E3 ubiquitin-protein ligase. Promotes SMAD4 ubiquitination, nuclear exclusion and degradation via the ubiquitin proteasome pathway. According to PubMed:16751102, does not promote a decrease in the level of endogenous SMAD4. May act as a transcriptional repressor. Inhibits the transcriptional response to TGF-beta/BMP signaling cascade. Plays a role in the control of cell proliferation. Its association with SMAD2 and SMAD3 stimulates erythroid differentiation of hematopoietic stem/progenitor. Monoubiquitinates SMAD4 and acts as an inhibitor of SMAD4-dependent TGF-beta/BMP signaling cascade (Monoubiquitination of SMAD4 hampers its ability to form a stable complex with activated SMAD2/3 resulting in inhibition of TGF-beta/BMP signaling cascade).

Subunit / interactions. Homooligomer and heterooligomer with TRIM24 and TRIM28 family members. Interacts with SMAD4 in unstimulated cells. Found in a complex with SMAD2 and SMAD3 upon addition of TGF-beta. Interacts with SMAD2 and SMAD3. Interacts with SMAD4 under basal and induced conditions and, upon TGF-beta signaling, with activated SMAD2. Forms a ternary complex with SMAD4 and SMAD2 upon TGF-beta signaling.

Subcellular location. Nucleus.

Tissue specificity. Expressed in stem cells at the bottom of the crypts of the colon (at protein level). Expressed in colon adenomas and adenocarcinomas (at protein level). Expressed in brain, lung, liver, spleen, thymus, prostate, kidney, testis, heart, placenta, pancreas, small intestine, ovary, colon, skeletal muscle and hematopoietic progenitors.

Post-translational modifications. Sumoylated with SUMO1.

Disease relevance. A chromosomal aberration involving TRIM33 is found in papillary thyroid carcinomas (PTCs). Translocation t(1;10)(p13;q11) with RET. The translocation generates the TRIM33/RET (PTC7) oncogene. Developmental dysplasia of the hip 4 (DDH4) [MIM:621311] An autosomal recessive form of congenital dysplasia of the hip, a common skeletal anomaly in which the normal seating of the femoral head in the acetabulum is disrupted. Its severity ranges from mild instability of the femoral head with slight capsular laxity, permitting minimal lateral displacement, through moderate lateral displacement of the femoral head, without loss of contact of the head with the acetabulum, up to complete dislocation of the femoral head from the acetabulum. The disease may be caused by variants affecting the gene represented in this entry.

Pathway. Protein modification; protein ubiquitination.

Similarity. Belongs to the TRIM/RBCC family.

Isoforms (2)

UniProt IDNamesCanonical?
Q9UPN9-1Alphayes
Q9UPN9-2Beta

RefSeq proteins (2): NP_056990, NP_148980 (=MANE)

Domains & families (InterPro)

IDNameType
IPR000315Znf_B-boxDomain
IPR001487BromodomainDomain
IPR001841Znf_RINGDomain
IPR001965Znf_PHDDomain
IPR003649Bbox_CDomain
IPR011011Znf_FYVE_PHDHomologous_superfamily
IPR013083Znf_RING/FYVE/PHDHomologous_superfamily
IPR017907Znf_RING_CSConserved_site
IPR019786Zinc_finger_PHD-type_CSConserved_site
IPR019787Znf_PHD-fingerDomain
IPR036427Bromodomain-like_sfHomologous_superfamily

Pfam: PF00439, PF00628, PF00643

UniProt features (109 total): modified residue 20, cross-link 19, compositionally biased region 10, sequence variant 9, region of interest 8, binding site 8, helix 7, strand 7, turn 6, zinc finger region 4, sequence conflict 4, mutagenesis site 2, chain 1, domain 1, coiled-coil region 1, site 1, splice variant 1

Structure

Experimental structures (PDB)

9 structures.

PDBMethodResolution (Å)
7ZDDX-RAY DIFFRACTION1.62
5MR8X-RAY DIFFRACTION1.74
3U5NX-RAY DIFFRACTION1.95
3U5OX-RAY DIFFRACTION2.7
3U5PX-RAY DIFFRACTION2.8
8BDYX-RAY DIFFRACTION3.05
3U5MX-RAY DIFFRACTION3.08
8BD8X-RAY DIFFRACTION3.1
8BD9X-RAY DIFFRACTION3.2

Predicted structure (AlphaFold)

ModelpLDDTFraction very-high
AF-Q9UPN9-F162.490.25

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 (1): 964–965 (breakpoint for translocation to form trim33-ret oncogene)

Ligand- & substrate-binding residues (8): 217; 220; 241; 245; 276; 279; 299; 304

Post-translational modifications (39): 515, 515, 535, 577, 591, 591, 598, 604, 763, 769, 793, 803, 815, 862, 951, 953, 1051, 1102, 1105, 1119 …

Mutagenesis-validated functional residues (2):

PositionPhenotype
125abolishes e3 activity but does not affect interaction with smad4; when associated with a-128.
128abolishes e3 activity but does not affect interaction with smad4; when associated with a-125.

Function

Pathways and Gene Ontology

Reactome pathways

2 pathways

IDPathway
R-HSA-2173795Downregulation of SMAD2/3:SMAD4 transcriptional activity
R-HSA-9754189Germ layer formation at gastrulation

MSigDB gene sets: 357 (showing top): GOBP_REGULATION_OF_CELLULAR_RESPONSE_TO_GROWTH_FACTOR_STIMULUS, AAGCAAT_MIR137, REACTOME_SIGNALING_BY_TGF_BETA_RECEPTOR_COMPLEX, GCM_GSPT1, MAZ_Q6, BROWNE_HCMV_INFECTION_16HR_UP, MEF2_02, AP2_Q3, BILD_SRC_ONCOGENIC_SIGNATURE, GCM_BCL2L1, TCF4_Q5, GOBP_NEGATIVE_REGULATION_OF_CELLULAR_RESPONSE_TO_GROWTH_FACTOR_STIMULUS, CAGCAGG_MIR370, ONKEN_UVEAL_MELANOMA_UP, WATANABE_RECTAL_CANCER_RADIOTHERAPY_RESPONSIVE_UP

GO Biological Process (5): negative regulation of transcription by RNA polymerase II (GO:0000122), protein ubiquitination (GO:0016567), regulation of transforming growth factor beta receptor signaling pathway (GO:0017015), negative regulation of BMP signaling pathway (GO:0030514), negative regulation of DNA-templated transcription (GO:0045892)

GO Molecular Function (9): DNA binding (GO:0003677), ubiquitin-protein transferase activity (GO:0004842), zinc ion binding (GO:0008270), ubiquitin protein ligase activity (GO:0061630), co-SMAD binding (GO:0070410), R-SMAD binding (GO:0070412), protein binding (GO:0005515), transferase activity (GO:0016740), metal ion binding (GO:0046872)

GO Cellular Component (4): chromatin (GO:0000785), nucleus (GO:0005634), nucleoplasm (GO:0005654), nuclear lumen (GO:0031981)

Reactome top-level categories

Rollup of top-2 pathways:

CategoryPathways
Transcriptional activity of SMAD2/SMAD3:SMAD4 heterotrimer1
Gastrulation1

GO top-level categories

Rollup of top GO terms by namespace:

CategoryTerms
SMAD binding2
cellular anatomical structure2
regulation of transcription by RNA polymerase II1
transcription by RNA polymerase II1
negative regulation of DNA-templated transcription1
protein modification by small protein conjugation1
transforming growth factor beta receptor signaling pathway1
regulation of transmembrane receptor protein serine/threonine kinase signaling pathway1
regulation of cellular response to transforming growth factor beta stimulus1
BMP signaling pathway1
regulation of BMP signaling pathway1
negative regulation of transmembrane receptor protein serine/threonine kinase signaling pathway1
negative regulation of cellular response to growth factor stimulus1
DNA-templated transcription1
regulation of DNA-templated transcription1
negative regulation of RNA biosynthetic process1
nucleic acid binding1
ubiquitin-like protein transferase activity1
transition metal ion binding1
ubiquitin-protein transferase activity1
ubiquitin-like protein ligase activity1
binding1
catalytic activity1
cation binding1
chromosome1
intracellular membrane-bounded organelle1
nuclear lumen1
nucleus1
intracellular organelle lumen1

Protein interactions and networks

STRING

2400 interactions, top by confidence (×1000):

Protein AProtein BPartner UniProtScore
TRIM33SMAD2Q15796993
TRIM33SMAD3P84022953
TRIM33MORC3Q14149924
TRIM33H3C1P02295840
TRIM33SMAD4Q13485824
TRIM33RETP07949819
TRIM33IFIH1Q9BYX4818
TRIM33SAE1Q9UBE0806
TRIM33RETP07949786
TRIM33TRIM28Q13263771
TRIM33NCOA4Q13772758
TRIM33TRIM21P19474752
TRIM33TRAT1Q6PIZ9746
TRIM33TRIM17Q9Y577731
TRIM33H3-3AP06351721

IntAct

163 interactions, top by confidence:

ABTypeScore
SMAD3SMAD4psi-mi:“MI:0914”(association)0.980
RB1CC1ATG13psi-mi:“MI:0914”(association)0.820
TRIM33TRIM24psi-mi:“MI:0914”(association)0.790
TRIM24TRIM33psi-mi:“MI:0915”(physical association)0.790
TRIM33SMAD4psi-mi:“MI:0914”(association)0.750
TRIM33SMAD4psi-mi:“MI:0915”(physical association)0.750
RABGGTBYKT6psi-mi:“MI:0914”(association)0.740
CNOT3CNOT1psi-mi:“MI:0914”(association)0.740
HSPB2BAG3psi-mi:“MI:0914”(association)0.670
SMAD2TRIM33psi-mi:“MI:0915”(physical association)0.660
TRIM33SMAD2psi-mi:“MI:0915”(physical association)0.660
QPRTPIK3C2Apsi-mi:“MI:0914”(association)0.640
KPNA1TCERG1psi-mi:“MI:0914”(association)0.640
JUNNFATC1psi-mi:“MI:0914”(association)0.610
TRIM28TRIM24psi-mi:“MI:0914”(association)0.600
TRIM28ZNF316psi-mi:“MI:0914”(association)0.530
RABGGTBPIPSLpsi-mi:“MI:0914”(association)0.530
ZNF324BZNF316psi-mi:“MI:0914”(association)0.530
NUP62RGPD8psi-mi:“MI:0914”(association)0.530
ZNF764SH3PXD2Bpsi-mi:“MI:0914”(association)0.530
TRIM28ZNF320psi-mi:“MI:0914”(association)0.530
ZNRD2MYO9Apsi-mi:“MI:0914”(association)0.530

BioGRID (605): DHX33 (Affinity Capture-Western), DHX33 (Biochemical Activity), UBE2N (Reconstituted Complex), UBE2E1 (Reconstituted Complex), UBE2D3 (Reconstituted Complex), TRIM33 (Affinity Capture-Western), TRIM33 (Reconstituted Complex), TRIM33 (Affinity Capture-Western), TRIM33 (Affinity Capture-MS), TRIM33 (Affinity Capture-MS), TRIM33 (Affinity Capture-MS), TRIM33 (Affinity Capture-MS), TRIM33 (Affinity Capture-MS), TRIM33 (Affinity Capture-MS), TRIM33 (Co-fractionation)

ESM2 similar proteins: A0A1L8GR68, A2A791, B2GUN4, E1BP74, E1BZ85, F1QLG5, F7AQ22, O00472, O15164, O15550, O70546, O88974, O95789, P49140, P55265, P70365, Q14202, Q14596, Q15047, Q15788, Q4PJW2, Q5R413, Q5RC94, Q5RDJ2, Q5VZL5, Q64127, Q69Z66, Q6H8Q1, Q6KC51, Q6NXK2, Q6P3Y5, Q6PFK1, Q7Z3K3, Q8BJ34, Q8BL65, Q8BZH4, Q8CHY6, Q8IZD4, Q8TEW8, Q8VIG2

Diamond homologs: A0A0R4IXF6, A0A7U2QYM2, A2AUY4, A2BIL7, A8DZJ1, B2KF05, B2RRD7, B2RWS6, B7ZS37, D4A7T3, E9Q2Z1, F1QW93, F1R5H6, F7DRV9, G5E8P1, G5EGM3, O15164, O60885, O74350, O88379, O95696, P13709, P21675, P25440, P35177, P45481, P51123, P55201, Q03330, Q07442, Q08D75, Q09472, Q12830, Q15059, Q1LUC3, Q23590, Q32S26, Q338B9, Q4R8Y1, Q54BA2

SIGNOR signaling

6 interactions.

AEffectBMechanism
TRIM33up-regulatesSMAD3binding
TRIM33“up-regulates activity”SMAD3binding
TRIM33“up-regulates activity”SMAD2binding
TRIM33“down-regulates quantity by destabilization”CTNNB1binding
Ub:E2“up-regulates activity”TRIM33ubiquitination
TRIM33“down-regulates quantity by destabilization”CTNNB1ubiquitination

Enriched among interaction partners

Reactome pathways and GO biological processes over-represented among this gene’s 185 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
Formation of definitive endoderm527.2×1e-04
Transcriptional activity of SMAD2/SMAD3:SMAD4 heterotrimer514.1×2e-03
Gastrulation611.9×9e-04
SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription511.8×3e-03
TP53 Regulates Transcription of DNA Repair Genes811.1×1e-04
Deactivation of the beta-catenin transactivating complex58.9×7e-03
HIV Life Cycle67.4×5e-03
TCF dependent signaling in response to WNT76.3×5e-03

GO biological processes:

GO termPartnersFoldFDR
SMAD protein signal transduction521.2×6e-04
positive regulation of miRNA transcription711.8×5e-04
transcription by RNA polymerase II135.3×3e-04

Disease & clinical

Cancer significance

From intOGen — cancer-driver classification: loss-of-function (tumor-suppressor-like) across 1 cancer types — MBL.

Clinical variants and AI predictions

ClinVar

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

ClassificationCount (floor)
Pathogenic1
Likely pathogenic1
Uncertain significance50
Likely benign1
Benign8

Top pathogenic / likely-pathogenic (2)

Variant IDHGVSClassification
4075745NM_015906.4(TRIM33):c.1636ACA[6] (p.Thr550_Gln551insThr)Pathogenic
3063595NM_015906.4(TRIM33):c.1650_1651insTGT (p.Thr550_Gln551insCys)Likely pathogenic

SpliceAI

3206 predictions. Top by Δscore:

VariantEffectΔscore
1:114397650:A:ACdonor_gain1.0000
1:114397651:C:CCdonor_gain1.0000
1:114397673:T:Cdonor_gain1.0000
1:114398004:C:CTacceptor_gain1.0000
1:114399455:A:ACdonor_gain1.0000
1:114399456:C:CTdonor_gain1.0000
1:114399456:CT:Cdonor_gain1.0000
1:114399456:CTT:Cdonor_gain1.0000
1:114399458:T:TAdonor_gain1.0000
1:114399466:CCTT:Cdonor_gain1.0000
1:114399610:C:CCacceptor_gain1.0000
1:114401470:C:CTacceptor_gain1.0000
1:114401470:C:Tacceptor_gain1.0000
1:114401471:A:Tacceptor_gain1.0000
1:114406357:CATA:Cacceptor_gain1.0000
1:114406934:AGCTT:Adonor_loss1.0000
1:114406935:GCTT:Gdonor_loss1.0000
1:114406936:CTTA:Cdonor_loss1.0000
1:114406937:TTACC:Tdonor_loss1.0000
1:114406938:TACC:Tdonor_loss1.0000
1:114406939:A:ACdonor_gain1.0000
1:114406939:A:Cdonor_loss1.0000
1:114406940:C:CCdonor_gain1.0000
1:114407096:CACAG:Cacceptor_gain1.0000
1:114407098:CAG:Cacceptor_gain1.0000
1:114407101:C:CCacceptor_gain1.0000
1:114407851:T:Cdonor_gain1.0000
1:114408673:TCA:Tdonor_loss1.0000
1:114408674:CA:Cdonor_loss1.0000
1:114408675:A:ACdonor_gain1.0000

AlphaMissense

7431 scored. Top likely-pathogenic:

VariantProtein changeam_pathogenicity
1:114397802:A:GL1077P1.000
1:114397814:A:GF1073S1.000
1:114397835:C:TG1066E1.000
1:114397836:C:AG1066W1.000
1:114397836:C:GG1066R1.000
1:114397836:C:TG1066R1.000
1:114399463:A:CF1038L1.000
1:114399463:A:TF1038L1.000
1:114399464:A:GF1038S1.000
1:114399465:A:GF1038L1.000
1:114399472:A:CC1035W1.000
1:114399473:C:TC1035Y1.000
1:114399474:A:GC1035R1.000
1:114399475:G:CN1034K1.000
1:114399475:G:TN1034K1.000
1:114399482:A:GF1032S1.000
1:114399491:C:GR1029P1.000
1:114399494:A:TV1028D1.000
1:114399506:A:GF1024S1.000
1:114399525:A:CY1018D1.000
1:114399548:A:GL1010P1.000
1:114399548:A:TL1010H1.000
1:114399556:T:AK1007N1.000
1:114399556:T:GK1007N1.000
1:114399560:A:TV1006E1.000
1:114399569:A:GL1003S1.000
1:114399587:A:TI997K1.000
1:114399599:T:CY993C1.000
1:114399600:A:CY993D1.000
1:114399600:A:GY993H1.000

dbSNP variants (sampled 300 via entrez): RS1000046024 (1:114415133 T>C), RS1000050646 (1:114430439 C>T), RS1000051280 (1:114494148 G>C), RS1000081587 (1:114470053 G>T), RS1000103253 (1:114508137 A>G), RS1000103788 (1:114407839 G>C,T), RS1000112604 (1:114443737 A>G), RS1000124950 (1:114501284 A>G), RS1000238605 (1:114400676 C>G,T), RS1000280324 (1:114393439 G>T), RS1000317939 (1:114474968 G>C), RS1000351648 (1:114456538 C>T), RS1000376420 (1:114438391 A>C,T), RS1000398886 (1:114501054 G>A), RS1000417346 (1:114393957 G>C,T)

Disease associations

OMIM: gene MIM:605769 | disease phenotypes: MIM:167000, MIM:142700, MIM:621311

GenCC curated gene-disease

DiseaseClassificationInheritance
developmental dysplasia of the hipLimitedAutosomal recessive

Mondo (3): ovarian cancer (MONDO:0008170), developmental dysplasia of the hip (MONDO:0000158), developmental dysplasia of the hip 4 (MONDO:0979872)

Orphanet (1): Rare ovarian cancer (Orphanet:213500)

HPO phenotypes

23 total (23 of 23 shown, HPO-id order):

HPOTerm
HP:0000007Autosomal recessive inheritance
HP:0000023Inguinal hernia
HP:0000079Abnormality of the urinary system
HP:0000160Narrow mouth
HP:0000174Abnormal palate morphology
HP:0000272Malar flattening
HP:0000286Epicanthus
HP:0000316Hypertelorism
HP:0000364Hearing abnormality
HP:0000431Wide nasal bridge
HP:0000457Depressed nasal ridge
HP:0000463Anteverted nares
HP:0001374Congenital hip dislocation
HP:0001382Joint hypermobility
HP:0001385Hip dysplasia
HP:0001643Patent ductus arteriosus
HP:0001671Abnormal cardiac septum morphology
HP:0001702Abnormal tricuspid valve morphology
HP:0002815Abnormality of the knee
HP:0003577Congenital onset
HP:0004097Deviation of finger
HP:0010759Prominence of the premaxilla
HP:0011328Abnormal fontanelle morphology

GWAS associations

17 associations (top):

StudyTraitp-value
GCST002268_3Autism2.000000e-07
GCST002268_4Autism6.000000e-08
GCST002268_5Autism6.000000e-08
GCST002268_6Autism4.000000e-08
GCST002268_7Autism8.000000e-08
GCST002268_8Autism7.000000e-08
GCST002268_9Autism3.000000e-08
GCST004630_9Mean corpuscular hemoglobin3.000000e-14
GCST007576_116Chronotype8.000000e-09
GCST010151_3Carotid intima media thickness x smoking interaction9.000000e-06
GCST90002390_9Mean corpuscular hemoglobin1.000000e-20
GCST90002392_276Mean corpuscular volume7.000000e-23
GCST90002396_140Mean reticulocyte volume4.000000e-20
GCST90002397_770Mean spheric corpuscular volume6.000000e-20
GCST90002401_353Platelet distribution width1.000000e-10
GCST90002403_14Red blood cell count1.000000e-09
GCST90002404_472Red cell distribution width2.000000e-11

EFO canonical traits (7, from GWAS)

EFO IDTrait name
EFO:0004527mean corpuscular hemoglobin
EFO:0008328chronotype measurement
EFO:0006527smoking status measurement
EFO:0010701mean reticulocyte volume
EFO:0007984platelet component distribution width
EFO:0004305erythrocyte count
EFO:0009188Red cell distribution width

MeSH disease descriptors (2)

DescriptorNameTree numbers
D000082602Developmental Dysplasia of the HipC05.550.518.384.500; C05.660.297; C16.131.621.297
D010051Ovarian NeoplasmsC04.588.322.455; C12.050.351.500.056.630.705; C12.050.351.937.418.685; C12.100.250.056.630.705; C12.900.418.685; C19.344.410; C19.391.630.705

Drugs & pharmacology

Drug and pharmacology data

Is drug target: yes

ChEMBL targets (1): CHEMBL2176772 (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)

GtoPdb / IUPHAR curated pharmacology

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

Target class: enzyme — TIF1 family

ChEMBL bioactivities

40 potent at pChembl≥5 of 96 total, top 40 by pChembl (potency: 10 = 0.1 nM, 6 = 1 µM).

pChemblTypeValueUnitMolecule
8.50IC503.19nMCHEMBL4440737
7.86IC5013.72nMCHEMBL4470967
6.85IC50140nMMOLIBRESIB
6.76Kd173nMMOLIBRESIB
6.63IC50233.5nMCYCLOPENTANONE
6.62IC50240.3nMCHEMBL4467793
6.60IC50249.8nMCYCLOOCTANONE
6.57IC50268.9nMCHEMBL4572394
6.55IC50283.4nMCHEMBL543846
6.52IC50299.4nMSALICYLADEHYDE
6.52IC50300.6nMCHEMBL350966
6.51IC50305.4nMCHEMBL2229659
6.50IC50319.8nMCHEMBL4451080
6.49IC50325.6nMVANILLIN
6.47IC50335.7nMCHEMBL4592980
6.27IC50537.9nMCHEMBL4448530
6.26IC50553.2nMCHEMBL4452179
6.19IC50641nMCHEMBL4446283
5.99IC501026nMCHEMBL4452792
5.97IC501069nMCHEMBL4449227
5.93IC501165nMCHEMBL4446283
5.89IC501294nMCHEMBL4580867
5.87IC501356nMCHEMBL4457083
5.87IC501365nMCHEMBL4438332
5.71IC501934nMCHEMBL4470369
5.46IC503457nMCHEMBL4453026
5.45IC503576nMCHEMBL4461534
5.44IC503597nMCHEMBL4461549
5.42IC503777nMCHEMBL4461534
5.33IC504690nMCHEMBL4303781
5.26IC505484nMCHEMBL4473237
5.23IC505901nMCHEMBL4465785
5.20IC506323nMCHEMBL3774575
5.14IC507172nMCHEMBL4586564
5.13IC507451nMCHEMBL4548728
5.10IC507884nMCHEMBL4470427
5.07IC508574nMCHEMBL4546478
5.06IC508718nMCHEMBL4445295
5.02IC509597nMCHEMBL4457958
5.00IC501.007e+04nMCHEMBL4560434

PubChem BioAssay actives

2 with measured affinity, of 46 total; 1 most potent distinct compounds. Largely complementary to BindingDB; screening values are coarse (µM, 4 dp), so sub-nM hits tie at the floor.

CompoundAssayTypeValueUnit
2-[(4S)-6-(4-chlorophenyl)-8-methoxy-1-methyl-4H-[1,2,4]triazolo[4,3-a][1,4]benzodiazepin-4-yl]-N-ethylacetamide2178558: Inhibition of TRIM33 (unknown origin) incubated for 1 hr by colloidal coomassie staining based LC-MS/MS analysisic500.1400uM

CTD chemical–gene interactions

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

ChemicalActions (top 5)PubMed papers
Valproic Acidaffects cotreatment, decreases expression, affects expression, decreases methylation6
bisphenol Adecreases expression, increases expression2
7,8-Dihydro-7,8-dihydroxybenzo(a)pyrene 9,10-oxidedecreases expression2
aristolochic acid Idecreases expression1
FR900359affects phosphorylation1
TAK-243increases sumoylation1
2,4,6-tribromophenoldecreases expression1
decabromobiphenyl etherdecreases expression1
trichostatin Aincreases expression1
cobaltous chlorideincreases expression1
nickel sulfatedecreases expression1
isobutyl alcoholaffects cotreatment, decreases expression, increases abundance1
tamibarotenedecreases expression1
di-n-butylphosphoric acidaffects expression1
4-(5-benzo(1,3)dioxol-5-yl-4-pyridin-2-yl-1H-imidazol-2-yl)benzamideaffects cotreatment, decreases expression1
2,2’,4,4’-tetrabromodiphenyl etherdecreases expression1
dorsomorphinaffects cotreatment, decreases expression1
hexabrominated diphenyl ether 153decreases expression1
jinfukangdecreases expression1
(+)-JQ1 compounddecreases expression, decreases reaction, increases expression, affects binding, increases reaction (+2 more)1
Resveratrolaffects cotreatment, increases expression1
Leflunomideincreases expression1
Acetaminophenincreases expression1
Arsenicaffects methylation1
Caffeineaffects phosphorylation1
Enzyme Inhibitorsdecreases activity, increases O-linked glycosylation1
Gasolineaffects cotreatment, decreases expression, increases abundance1
Ivermectindecreases expression1
Methyl Methanesulfonateincreases expression1
Plant Extractsaffects cotreatment, increases expression1

ChEMBL screening assays

47 unique, capped per target: 47 binding

Representative assays (with source publication via chembl_document):

Assay IDTypeDescriptionSource paper
CHEMBL2186997BindingInhibition of His6FLAG-tagged TRIM33 isoform B expressed in Escherichia coli assessed as change in melting temperature at 100 uM by thermal shift assayFragment-based discovery of bromodomain inhibitors part 2: optimization of phenylisoxazole sulfonamides. — J Med Chem

Cellosaurus cell lines

5 cell lines: 5 cancer cell line

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

CellosaurusNameCategorySex
CVCL_B8REAbcam HCT 116 TRIM33 KOCancer cell lineMale
CVCL_B9TTAbcam A-549 TRIM33 KOCancer cell lineMale
CVCL_TU09HAP1 TRIM33 (-) 1Cancer cell lineMale
CVCL_TU10HAP1 TRIM33 (-) 2Cancer cell lineMale
CVCL_TU11HAP1 TRIM33 (-) 3Cancer cell lineMale

Clinical trials (associated diseases)

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

TrialPhaseStatusTitle
NCT00208364PHASE4TERMINATEDA Two Centre Study to Assess the Long-term Performance of the Pinnacle™ Cup With a Metal-on-Metal Bearing in Primary Total Hip Replacement
NCT00208377PHASE4TERMINATEDA Multi-centre Study to Assess the Long-term Performance of the DePuy ASR™ System in Primary Hip Resurfacing Surgery
NCT00208390PHASE4TERMINATEDA Multi-centre Study to Assess the Long-term Performance of the Summit™ Hip in Primary Total Hip Replacement
NCT00208429PHASE4WITHDRAWNA Multi-centre Study to Assess the Long-term Performance of the Pinnacle™ Cup With a Polyethylene-on-metal Bearing in Primary Total Hip Replacement
NCT00208442PHASE4COMPLETEDA Randomised Single Centre Study to Compare the Long-term Wear Characteristics of Marathon™ and Enduron™ Polyethylene Cup Liners in Primary Total Hip Replacement
NCT00208455PHASE4TERMINATEDA Multi-centre Study to Assess the Long-term Performance of the DePuy PROXIMA™ Hip in Primary Total Hip Replacement
NCT00546598PHASE4TERMINATEDPost-approval Study of the DURALOC® Option Ceramic-on-Ceramic Hip Prosthesis System
NCT00715026PHASE4TERMINATEDTrilogy AB Acetabular Hip System Post Approval Study
NCT00872066PHASE4COMPLETEDA Study to Assess the Long-term Performance of SmartSet® HV and SmartSet® GHV Bone Cements in Primary Total Hip Replacement
NCT00872222PHASE4TERMINATEDA Single Centre Study to Assess the Long-term Performance of the Pinnacle™ Cup With a Ceramic-on-ceramic Bearing in Primary Total Hip Replacement
NCT00872547PHASE4TERMINATEDMulti-Centre Study to Assess the Long-term Performance of the DePuy ASR™ System in Resurfacing and Primary Total Hip Replacement
NCT00872573PHASE4TERMINATEDA Two Centre Study to Assess the Stability and Long-term Performance of the C-Stem™ AMT in a Total Primary Hip Replacement
NCT00872794PHASE4TERMINATEDA Single Centre Study to Assess the Long-term Performance of the DePuy ASR™ System in Primary Hip Resurfacing Surgery
NCT00873444PHASE4TERMINATEDA Randomised Study to Compare Metal Ion Release and Long-term Performance of the Pinnacle™ Cup With a Ceramic-on-Metal or a Metal-on-Metal Bearing
NCT01134445PHASE4TERMINATEDAn Electronic Data Capture Study to Assess the Long-term Performance of the DePuy PROXIMA™ Hip in Primary Total Hip Replacement
NCT01422564PHASE4TERMINATEDMetal on Metal Versus Metal on Highly Crossed Linked Polyethylene Sytem
NCT01635166PHASE4TERMINATEDMulti-centre Study to Assess the Long-term Performance of the Deltamotion Cup System in Primary Hip Replacement Surgery
NCT00190697PHASE4COMPLETEDA Study of LY353381 (Arzoxifene) for Patients Who Benefitted From This Drug in Other Oncology Trials and Wished to Continue Treatment
NCT00277160PHASE4COMPLETEDA Study of Primary Prophylaxis With Neulasta (Pegfilgrastim) Versus Secondary Prophylaxis After Chemotherapy in Elderly Subjects (>/= 65 Years Old) With Cancer
NCT00727961PHASE4COMPLETEDA Study to Evaluate Efficacy and Tolerance of Caelyx in Patients With Epithelial Ovarian Cancer. (Study P04072)(COMPLETED)
NCT00740116PHASE4COMPLETEDTranexamic Acid in Surgery of Advanced Ovarian Cancer
NCT00817479PHASE4COMPLETEDTumor Gene Expression in Women With Ovarian Cancer
NCT01432015PHASE4COMPLETEDFosaprepitant Versus Aprepitant in the Prevention of Chemotherapy Induced Nausea and Vomiting
NCT01706120PHASE4UNKNOWNStudy of Clinical and Biological Prognostic Factors in Patients With Ovarian Cancer Receiving Carboplatin +Paclitaxel With Bevacizumab
NCT01932125PHASE4COMPLETEDAn Interventional Study of Avastin (Bevacizumab) in Patients With Advanced/Metastatic Epithelial Ovarian Cancer, Fallopian Tube Cancer or Primary Peritoneal Cancer
NCT01953107PHASE4COMPLETEDOral Iron vs. Placebo in Newly Diagnosed Gynecologic Oncology Patients Who Are Surgical Candidates.
NCT02035345PHASE4TERMINATEDSlowed Carboplatin Infusion for Ovarian Cancer Patients Receiving Carboplatin Re-Treatment
NCT02243059PHASE4WITHDRAWNMagnetic Resonance Imaging for Lymph Node Staging in Ovarian Cancer
NCT03164980PHASE4TERMINATEDQoL-Comparison Between Trabectedin/PLD and Pt-based Therapy in Patients With Pt-sensitive Recurrent Ovarian Cancer
NCT03384511PHASE4COMPLETEDThe Use of 18F-ALF-NOTA-PRGD2 PET/CT Scan to Predict the Efficacy and Adverse Events of Apatinib in Malignancies.
NCT03543462PHASE4COMPLETEDDiaphragmatic Resection And Gynecological Ovarian Neoplasm
NCT03752216PHASE4COMPLETEDNIraparib and Quality of LifE is a Longitudinal Study Evaluating in Real Life the Tolerability of Niraparib.
NCT03858166PHASE4TERMINATEDEfficacy and Safety of PEG-rhG-CSF Secondary Prophylaxis vs. Therapeutic Administration in Patients With Ovarian Cancer
NCT04024254PHASE4COMPLETEDA Study of Serum Folate Levels in Patients Treated With Olaparib
NCT04330040PHASE4COMPLETEDProspective Multicentre Phase-IV Clinical Trial of Olaparib in Indian Patients With Ovarian and Metastatic Breast Cancer
NCT04352439PHASE4COMPLETEDAspirin for Prevention of Venous Thromboembolism Among Ovarian Cancer Patients Receiving Neoadjuvant Chemotherapy
NCT05187208PHASE4UNKNOWNPARP Inhibitor Oral Maintenance in Low-Risk Ovarian Cancer
NCT05606692PHASE4RECRUITINGInfluences of Propofol and Sevoflurane Anesthesia in Ovarian Cancer (Anesthetics)
NCT05926336PHASE4RECRUITINGThe Effects of Using Different Anesthetics on the Prognosis of Primary Tumors and Its Mechanism of Action
NCT06412120PHASE4RECRUITINGStudy Evaluating Safety, Tolerability, and Metabolism of Niraparib