Ask about this productRelated genes to: SFRS7 antibody
- Gene:
- SRSF7 NIH gene
- Name:
- serine and arginine rich splicing factor 7
- Previous symbol:
- SFRS7
- Synonyms:
- 9G8, ZCRB2, HSSG1, AAG3, RBM37, ZCCHC20
- Chromosome:
- 2p22.1
- Locus Type:
- gene with protein product
- Date approved:
- 1994-08-31
- Date modifiied:
- 2016-06-06
Related products to: SFRS7 antibody
Related articles to: SFRS7 antibody
- Non-small cell lung cancer (NSCLC) is one of the leading causes of cancer-related deaths worldwide, and its occurrence and development are closely related to complex molecular mechanisms. Alternative splicing of precursor mRNA is a key step in gene expression regulation, and its dysregulation is common in tumors. The serine/arginine-rich splicing factor (SRSF) family, a core protein family in splicing regulation, has been confirmed to play oncogenic roles in various cancers. However, systematic research on the SRSF family in NSCLC remains insufficient. This study aims to systematically analyze the specific expression patterns, clinical prognostic value, collaborative mechanisms and potential biological functions of SRSF individual members in NSCLC by the combination of bioinformatics analysis and experimental verification. - Source: PubMed
Tu ShuqiChen YuhaoZhang YalongChen QiangFan YaguangWang YixuanZhang YangLi SinuoChen JunPan HongliZhou XuexiaLi Xuebing - Sperm flagellar axoneme comprises microtubules (MT) and associated machinery and is an integral determinant of sperm motility. Reports from our lab show reduced levels of acetyl α-tubulin, and HDAC6, along with compromised axoneme polymerization in sperm of asthenozoospermic men. These observations prompted us to identify the sperm repertoire of HDAC6-interacting proteins(HIPs) associated with the MTs. HIPs and Microtubule associated protein (MAP) fractions, respectively, were isolated from sperm of normozoospermic individuals, subjected to tandem mass spectrometry(MS) using a bottom-up approach and proteins in the two groups were identified. 1224 and 315 proteins were identified in the respective groups. Seven clusters of HIPs were among the top 20 significant clusters. Proteins were manually curated from these relevant clusters and overlapped with the MAPs dataset which identified 14 HDAC6 interacting proteins to be associated with MTs (HMAPs). On further analysis with MAP analyzer-LZTFL1, RAB7A, AIFM1 demonstrated low specificity toward MT whereas MYH10 and CFAP53 demonstrated high specificity. Among these HMAPs, EEF1A2, MYH10, ANXA1, TUFM, SOD1, and SRSF7 are known to interact with HDAC6 as documented in the BioGRID database. Interaction of CFAP53 with HDAC6 was validated by double immunofluorescence staining and co-immunoprecipitation in rat sperm. LFQ-DDA analysis of these HMAPs, revealed significantly lower abundance of CFAP53 and TUFM with higher abundance of MYH10 in asthenozoospermic men. Their differential expression in men with poor sperm motility as well as enrichment of acetylation on these HMAPs highlights their association with HDAC6 in maintaining axonemal stability/dynamicity and acetylation-deacetylation to the extent required for sperm motility, although interpretation is limited by the small sample size, restricted availability of human sperm for experimental validation, and reliance on acetylation predictions. - Source: PubMed
Publication date: 2026/02/27
Chawan VeenaPatankar AniketYevate SmitaGajbhiye RahulKushte SinetraGanla KedarParte Priyanka - Ossifying spindled and epithelioid tumour (OSET) is a recently defined soft tissue neoplasm with characteristic features, including a peripheral shell of bone or pseudocapsule, keratin expression, and indolent behaviour. Here, we present five unique cases of OSET with novel clinical and morphologic features. - Source: PubMed
Publication date: 2026/02/23
Sibira Rayan MSmith Benjamin FDavis AmyDavis Jessica LMohamed NadaZreik RiyamPapke David JMichal MichaelWangsiricharoen SintawatFritchie Karen J - How RIF1 (RAP1 interacting factor 1) fulfills its diverse roles in DNA double-strand break repair, DNA replication, and nuclear organization remains elusive. Here, we show that alternative splicing of a cassette exon (Ex32) encoding a Ser/Lys-rich cassette in the RIF1 C-terminal domain (CTD) gives rise to RIF1-Long (RIF1-L) and RIF1-Short (RIF1-S) isoforms with different functional characteristics. We demonstrate that RIF1-Ex32 splice-in is mediated by an exonic splicing enhancer that is recognized by the serine and arginine rich splicing factor 1 (SRSF1) and antagonized by SRSF3 and SRSF7. Exposure to DNA damage inhibited Ex32 splice-in, potentiated the association of SRSF3 and SRSF7 with RIF1 pre-mRNA, and caused an increase in RIF1-S protein expression, which was also observed across a diverse set of primary cancers. Isoform-specific proteomic analyses revealed RIF1-L preferentially associated with mediator of DNA damage checkpoint 1 (MDC1) and sustained MDC1 focus formation to a greater extent than RIF1-S. We further show that the Ser/Lys-rich cassette stabilized a novel phase separation activity of the RIF1 CTD and enhanced RIF1-L chromatin retention, which was reversed by cyclin-dependent kinase 1-dependent phosphorylation of the RIF1 CTD in response to G DNA damage checkpoint inhibition. These combined findings suggest DNA damage-dependent RIF1 alternative splicing contributes to RIF1 functional diversification in genome protection. - Source: PubMed
Publication date: 2025/10/24
Koo Adenine Si-HuiJia WeiyanKim Sang HwaScalf MarkBoos Claire EChen YuhongWang DeminVoter Andrew FBajaj AdityaSmith Lloyd MKeck James LBakkenist Christopher JGuo LinTibbetts Randal S - Malignant tumors, as one of the leading causes of mortality, pose great threats to global public health. Serine/Arginine-rich Splicing Factor 7 (SRSF7), a core splicing regulatory protein of the SRSF family, plays a crucial role in maintaining RNA stability, facilitating alternative splicing, and assisting RNA nuclear export. It also exhibits significantly aberrant expression among various cancers, including lung, colorectal, liver, and oral cancer. This review examines the molecular mechanisms of SRSF7 in tumorigenesis, with a focus on its role in the epigenetic reprogramming of related tumors. Specifically, it explores the abnormal regulation of the cell cycle, the regulation of non-coding RNA, the control of RNA methylation, and the reprogramming of glucose metabolism. Additionally, this review examines the role of SRSF7 in the tumor immune microenvironment through alternative splicing and immune evasion through the immune checkpoint PD-1. It also highlights the role of SRSF family members in tumor resistance, illustrating how alternative splicing contributes to tumor chemoresistance. Although SRSF7 shows significant promise in tumor intervention therapies, more experimental and clinical studies are still needed to evaluate its clinical application. This review enhances our understanding of the molecular landscape of SRSF7 in tumorigenesis with great potential to become a key node in tumor-targeted therapy and companion diagnostics, driving translational potential from mechanisms to clinical applications. - Source: PubMed
Publication date: 2025/12/30
Li YuanGao HuimengZhang XuanyuSun FuliGuo YanQiao Xue