Ask about this productRelated genes to: SFRS17A antibody
- Gene:
- AKAP17A NIH gene
- Name:
- A-kinase anchoring protein 17A
- Previous symbol:
- CXYorf3, SFRS17A
- Synonyms:
- XE7, XE7Y, DXYS155E, MGC39904, 721P, CCDC133
- Chromosome:
- Xp22.33 and Yp11.32
- Locus Type:
- gene with protein product
- Date approved:
- 2006-09-22
- Date modifiied:
- 2015-11-17
Related products to: SFRS17A antibody
Related articles to: SFRS17A antibody
- Identify genetic variants associated with amblyopia in African American (AFR) and Admixed American (AMR) ancestry groups, expanding upon a previous studies conducted in European ancestry. - Source: PubMed
Publication date: 2026/07/27
Lee Kyoung A VWhitman Mary C - Renal cell carcinoma (RCC) remains a clinically challenging malignancy characterized by high heterogeneity, limited early biomarkers, and suboptimal response rates to current targeted and immune-based therapies. Increasing evidence highlights that dysregulated epigenetic mechanisms, particularly altered histone methylation, contribute to tumor progression, metabolic reprogramming, and immune escape in RCC. However, the specific regulatory networks linking epigenetic modifiers with transcriptomic rewiring and therapeutic vulnerabilities in clear cell RCC (ccRCC) remain poorly defined. In this multi-omics in silico study, we systematically screened all histone methyltransferases and identified SUV420H2 (also known as KMT5C) as the most consistently overexpressed gene associated with adverse clinical outcomes in ccRCC. SUV420H2 showed stepwise upregulation with tumor stage and grade, while promoter analysis revealed multiple significantly hypomethylated CpG sites, suggesting a potential epigenetic deregulation. Complementarily, six predicted SUV420H2-targeting miRNAs were significantly downregulated in ccRCC consistent with post-transcriptional regulatory control. SUV420H2 overexpression correlated with increased CD4⁺/CD8⁺ T-cell infiltration, indicating an association with altered immune infiltration patterns. Co-expression and enrichment analyses revealed strong associations with chromatin organization, mitotic regulation, RNA metabolic processes, and RNA splicing, from which a five-gene RNA-processing signature (KAT2A, SNRNP70, CCNL2, CLK2, AKAP17A) was derived. This signature was strongly correlated with SUV420H2 and was associated with poorer overall survival specifically in ccRCC. Drug-sensitivity profiling further showed that high SUV420H2/RNA-processing signature expression conferred increased sensitivity to FK866 (NAMPT inhibitor), topoisomerase inhibitors, and apoptosis-inducing agents, identifying potential therapeutic associations that warrant further investigation. Collectively, our findings suggest that SUV420H2 is a multi-layer dysregulated epigenetic regulator associated with ccRCC progression and highlight its RNA-processing network as a promising prognostic and therapeutic axis. - Source: PubMed
Publication date: 2026/07/14
Kundu SubhadipTripathi RupalMehta AnuragSingh AmitabhKhanna AshishRawal Sudhir Kumar - Transposable elements (TEs) threaten genomic integrity, yet their pervasive presence indicates the limitations of existing silencing mechanisms. A recent paper in (Zhao . 2025) discovered the SOS splicing system, which provides an RNA-level defense that excises DNA transposons from mRNAs, thereby restoring gene sequence. This spliceosome-independent pathway, mediated by AKAP17A, CAAP1, and RTCB, recognizes dsRNA hairpins formed by inverted terminal repeats (ITRs) and religates the resulting RNA fragments. From an evolutionary perspective, SOS splicing exemplifies a post-transcriptional error-correction mechanism that mitigates the deleterious consequence of TE insertions, paralleling the Constructive Neutral Evolution (CNE) framework. In contrast, ADAR-mediated A-to-I RNA editing suppresses the MDA5-triggered innate immune responses to TE-derived dsRNAs, effectively tolerating rather than eliminating TEs. There may be partial overlap between ADAR and SOS substrates. ADAR editing may delay but not prevent SOS splicing, while SOS excision removes ADAR substrates. The lethality of ADAR loss underscores its role as the mechanism mitigating purifying selection on TEs and thus may contribute to their genomic tolerance and proliferation. Collectively, while ADAR masks the harm of TEs, SOS splicing actively repairs the resulting damage, together illustrating a delicate evolutionary balance between TE tolerance and transcriptomic rescue. - Source: PubMed
Publication date: 2026/02/26
Cao QiDuan Yuange - Hypoxia-inducible factor 1α (HIF1α) is the master transcriptional regulator of cellular adaptation to low oxygen microenvironment, essential for oxygen homeostasis and promoting tumorigenesis. We report that AKAP17A, an A-kinase anchoring protein, activates HIF1α signaling through a protein kinase A (PKA)-independent mechanism. Depletion of AKAP17A in mammalian cells reduced HIF1α abundance and attenuated the transcriptional activation of HIF target genes. Consistently, akap17a-null zebrafish exhibited compromised HIF signaling, impaired hypoxia tolerance, and diminished hypoxia-induced erythropoiesis. Functionally, knocking out AKAP17A suppressed cancer cell proliferation in vitro and impeded tumor growth in vivo. Mechanistic investigations revealed that AKAP17A augments HIF1α protein synthesis. Collectively, this work identifies AKAP17A as a pivotal regulator of the HIF1α, providing novel insights into its role in hypoxic adaptation and oncogenesis. - Source: PubMed
Publication date: 2025/12/13
Zhang BoqiWang ZifanTang YanfeiMa GuanboLiu YunzhangLi YunHao JiejieYe JunliSun XiangrongLu Ling - All genomes have mobile genetic segments called transposable elements (TEs). Here we describe a system, which we term SOS splicing, that protects Caenorhabditis elegans and human genes against DNA-transposon-mediated disruption by excising these TEs from host mRNAs. SOS splicing, which seems to operate independently of the spliceosome, is a pattern-recognition system triggered by the base-pairing of inverted terminal repeat elements, which are a defining feature of DNA transposons. We identify three factors required for SOS splicing in both C. elegans and human cells: AKAP17A, which binds TE-containing mRNAs; the RNA ligase RTCB; and CAAP1, which bridges RTCB and AKAP17A to allow RTCB to ligate mRNA fragments generated by TE excision. We propose that SOS splicing is a previously undescribed conserved and RNA-structure-directed mode of mRNA splicing, and that an identified function of SOS splicing is to genetically buffer animals from the deleterious effects of DNA-transposon-mediated gene perturbation. - Source: PubMed
Publication date: 2025/12/10
Zhao Long-WenNardone ChristopherChang CindyPaulo Joao AElledge Stephen JKennedy Scott