Ask about this productRelated genes to: CIRH1A antibody
- Gene:
- UTP4 NIH gene
- Name:
- UTP4 small subunit processome component
- Previous symbol:
- CIRH1A
- Synonyms:
- NAIC, FLJ14728, KIAA1988, TEX292, CIRHIN
- Chromosome:
- 16q22.1
- Locus Type:
- gene with protein product
- Date approved:
- 2000-03-15
- Date modifiied:
- 2019-01-22
Related products to: CIRH1A antibody
Related articles to: CIRH1A antibody
- UTP4 is a critical component of ribosome biogenesis, and its dysregulation may contribute to cancer development. However, the role of UTP4 in cancer remains unclear. The present study comprehensively investigated the expression and prognostic significance of UTP4 across multiple cancers, with a particular focus on gastric cancer (GC). Integrated bioinformatics analysis of public datasets, including The Cancer Genome Atlas, revealed that UTP4 is frequently overexpressed in various tumors and associated with poor prognosis. Further analysis uncovered its correlations with genetic mutations, immune infiltration and immune checkpoint expression. Based on these findings and CRISPR-Cas9 screening predictions, the functional role of UTP4 in GC cells was experimentally validated. The results demonstrated that UTP4 knockdown significantly inhibited cell proliferation, migration and invasion. These findings highlight UTP4 as a novel pan-cancer biomarker and potential therapeutic target, providing a foundation for further clinical investigations. - Source: PubMed
Publication date: 2026/02/13
Wei DiaoLei TianyuChe YuhangHu Qinyong - The nucleolus is a multifunctional nuclear body. To tease out the roles of nucleolar structure without resorting to the use of multi-action drugs, we knocked down the RNA polymerase I subunit RPA194 in HeLa cells by siRNA. Loss of RPA194 resulted in nucleolar-structural segregation and effects on both nucleolus-proximal and distal-nuclear components. The perinucleolar compartment was disrupted, centromere clustering around nucleoli was significantly reduced, and the intranuclear locations of specific genomic loci were altered. Moreover, Cajal bodies, distal from nucleoli, underwent morphological and some compositional changes. In comparison, when the preribosomal RNA-processing factor, UTP4, was knocked down, neither nucleolar segregation nor the intranuclear effects were observed, demonstrating that the changes of nucleolar proximal and distal nuclear domains in RPA194 knockdown cells unlikely arise from a cessation of ribosome synthesis, rather from the consequence of nucleolar-structure alteration. These findings point to a commutative system that links nucleolar structure to the maintenance and spatial organization of certain nuclear domains and genomic loci. - Source: PubMed
Publication date: 2023/08/23
Wang ChenMa HanhuiBaserga Susan JPederson ThoruHuang Sui - Infertility affects around 15% of all couples worldwide and is increasingly linked to variants in genes specifically expressed in the testis. Well-established causes of male infertility include pathogenic variants in the genes TEX11, TEX14, and TEX15, while few studies have recently reported variants in TEX13B, TEX13C, FAM9A (TEX39A), and FAM9B (TEX39B). - Source: PubMed
Publication date: 2023/08/18
Sieper Marie HGaikwad Avinash SFros MarionWeber PhilippDi Persio SaraOud Manon SKliesch SabineNeuhaus NinaStallmeyer BirgitTüttelmann FrankWyrwoll Margot J - The nucleolus is a multi-functional nuclear body. To tease out the roles of nucleolar structure without resorting to multi-action drugs, we knocked down RNA polymerase I subunit RPA194 in HeLa cells by siRNA. Loss of RPA194 resulted in nucleolar structural segregation and effects on both nucleolus-proximal and distal nuclear components. The perinucleolar compartment was disrupted, centromere-nucleolus interactions were significantly reduced, and the intranuclear locations of specific genomic loci were altered. Moreover, Cajal bodies, distal from nucleoli, underwent morphological and compositional changes. To distinguish whether these global reorganizations are the results of nucleolar structural disruption or inhibition of ribosome synthesis, the pre-ribosomal RNA processing factor, UTP4, was also knocked down, which did not lead to nucleolar segregation, nor the intranuclear effects seen with RPA195A knockdown, demonstrating that they do not arise from a cessation of ribosome synthesis. These findings point to a commutative system that links nucleolar structure to the maintenance and spatial organization of certain nuclear bodies and genomic loci. - Source: PubMed
Publication date: 2023/03/31
Wang ChenMa HanhuiBaserga Susan JPederson ThoruHuang Sui - Formation of the ribosome subunits is a complex and progressive cellular process that requires a plethora of non-ribosomal transient proteins and diverse small nucleolar RNAs, which are involved from the synthesis of the precursor ribosomal RNA in the nucleolus to the final ribosome processing steps in the cytoplasm. Employing PTP-tagged Nop56 as a fishing bait to capture pre-ribosomal particles by tandem affinity purifications, mass spectrometry assays and a robust in silico analysis, here we describe tens of ribosome assembly factors involved in the synthesis of both ribosomal subunits in the human pathogen Leishmania major, where the knowledge about ribosomal biogenesis is scarce. We identified a large number of proteins that participate in most stages of ribosome biogenesis in yeast and mammals. Among them, we found several putative orthologs of factors not previously identified in L. major, such as t-Utp4, t-Utp5, Rrp7, Nop9 and Nop15. Even more interesting is the fact that we identified several novel candidates that could participate in the assembly of the atypical 60S subunit in L. major, which contains eight different rRNA species. As these proteins do not seem to have a human counterpart, they have potential as targets for novel anti-leishmanial drugs. Also, numerous proteins whose function is not apparently linked to ribosome assembly were copurified, suggesting that the L. major nucleolus is a multifunctional nuclear body. - Source: PubMed
Publication date: 2022/01/15
Nepomuceno-Mejía TomásFlorencio-Martínez Luis EPineda-García IsabelMartínez-Calvillo Santiago