Ask about this productRelated genes to: SR140 antibody
- Gene:
- U2SURP NIH gene
- Name:
- U2 snRNP associated SURP domain containing
- Previous symbol:
- -
- Synonyms:
- fSAPa, SR140
- Chromosome:
- 3q23
- Locus Type:
- gene with protein product
- Date approved:
- 2011-02-07
- Date modifiied:
- 2016-04-04
Related products to: SR140 antibody
Related articles to: SR140 antibody
- Hepatocellular carcinoma (HCC) is fatal, with increasing incidence and mortality rates and resistance to classical chemotherapies. This paper investigates the molecular mechanism of U2SURP with lenvatinib (LEV) resistance in HCC cells. - Source: PubMed
Publication date: 2026/04/14
Zhang TiantianCao RuiruiLi YaweiWu YueShi MengtingSun WeijieLiu YangWang Rui - Pre-mRNA splicing determines the expressed proteome and is frequently dysregulated in cancer. The tumour-suppressor RBM5 controls an exon network regulating apoptosis, yet its molecular mechanism is elusive. Using in vivo spliceosome capture and cryogenic electron microscopy, we determined structures of precatalytic spliceosomes arrested by RBM5 immediately after U2 snRNP branchpoint recognition. Despite intron diversity, the U2-pre-mRNA duplex, branchpoint adenine, and downstream polypyrimidine tract are well-resolved. RBM5 binds the outer SF3B1 HEAT surface and performs dual functions: First, its helix-loop-helix motif and upstream zinc-finger domain sterically block tri-snRNP and Prp8 docking and prevent progression to pre-B and B complexes; Second, its G-patch activates DHX15 and places this DExH-box helicase on the pre-mRNA as it exits SF3B1, poised for branch helix unwinding. DHX15 binding to SF3B1 is facilitated by U2SURP/SR140, which engages SF3B1 near RBM5's helix-loop-helix. Functional assays confirm that disruption of the RBM5 interfaces with either DHX15 or SF3B1 inhibit exon repression. Mutations at these regulatory interfaces are common in cancer genomes and predicted to disrupt its regulation of apoptotic isoforms. Thus, RBM5 acts as a dual-action spliceosome gatekeeper that couples helicase activation with physical stalling to enforce tumour-suppressive alternative splicing programmes. - Source: PubMed
Publication date: 2026/04/08
Liu ShihengSu TiantianHuang JeffreyLin Chia-HoBlack Douglas LDamianov AndreyZhou Z Hong - Pre-mRNA splicing determines the expressed proteome and is frequently dysregulated in cancer. The tumour-suppressor RBM5 controls an exon network regulating apoptosis, yet its molecular mechanism is elusive. Using in vivo spliceosome capture and cryogenic electron microscopy, we determined structures of precatalytic spliceosomes arrested by RBM5 immediately after U2 snRNP branchpoint recognition. Despite intron diversity, the U2-pre-mRNA duplex, branchpoint adenine, and downstream polypyrimidine tract are well-resolved. RBM5 binds the outer SF3B1 HEAT surface and performs dual functions: First, its helix-loop-helix motif and upstream zinc-finger domain sterically block tri-snRNP and Prp8 docking and prevent progression to pre-B and B complexes; Second, its G-patch activates DHX15 and places this DExH-box helicase on the pre-mRNA as it exits SF3B1, poised for branch helix unwinding. DHX15 binding to SF3B1 is facilitated by U2SURP/SR140, which engages SF3B1 near RBM5's helix-loop-helix. Functional assays confirm that disruption of the RBM5 interfaces with either DHX15 or SF3B1 inhibit exon repression. Mutations at these regulatory interfaces are common in cancer genomes and predicted to disrupt its regulation of apoptotic isoforms. Thus, RBM5 acts as a dual-action spliceosome gatekeeper that couples helicase activation with physical stalling to enforce tumour-suppressive alternative splicing programmes. - Source: PubMed
Publication date: 2026/03/27
Liu ShihengSu TiantianHuang JeffreyLin Chia-HoBlack Douglas LDamianov AndreyZhou Z Hong - The prognosis of CML is affected not only by BCR::ABL1-independent resistance but also by BCR::ABL1-dependent resistance, particularly kinase mutations, both of which cause severe harm and have attracted worldwide attention. Circular RNAs (circRNA) have been assessed as potent regulators of tumor progression and drug resistance by manipulating the expression of target genes in cells and intercellular transmission via exosomes. In our previously study, we screened and identified a novel circRNA, circ_0058493, which presented significant negative relevance with imatinib resistance in CML. However, the underlying mechanism remains obscure. In this study, we found that circ_0058493 could be transmitted from imatinib-resistant cells to sensitive cells and induce sensitive cells to develop imatinib resistance. More critically, we showed that circ_0058493 competitively binds with miR-548b-3p, upregulating its target gene U2SURP expression and affecting the imatinib sensitivity of CML cells. Moreover, U2SURP knockdown suppressed the expression of p-ERK, a crucial protein in Ras/MAPK cancerous signaling pathway. Compared with imatinib optimal responders, the level of miR-548b-3p significantly decreased in PBMCs from patients who failed in imatinib treatment. The analysis of clinical database revealed that elevated U2SURP in HSCs was correlated with the occurrence of CML. In conclusion, our data suggested that targeting circ_0058493/miR-548b-3p/U2SURP axis and exosomal circ_0058493 is a potential therapeutic strategy for improving imatinib efficacy in CML. - Source: PubMed
Publication date: 2025/11/18
Tang Bing-JieChen LeiHuang Shu-TingZhong An-NiYin YiXiao JieCheng Yi-NingTan Yu-HanJiang Zhi-PingXu Ping - Pancreatic cancer (PC) has a strong ability to invade and metastasize, which has brought insurmountable obstacles to the treatment of PC. Exploring the molecular mechanism of PC metastasis is still the focus of PC research. The purpose of this study was to explore the molecular mechanism of long noncoding RNA HNF1A-AS1 in promoting PC metastasis, hoping to provide help for the diagnosis and treatment of PC. - Source: PubMed
Publication date: 2025/06/15
Lei ShanZhang ZhixueZeng ZhiruiCao WenpengSun YatingLi DahuanPan JigangWu YingminZhang TuoChen Tengxiang