Ask about this productRelated genes to: TPST2 antibody
- Gene:
- TPST2 NIH gene
- Name:
- tyrosylprotein sulfotransferase 2
- Previous symbol:
- -
- Synonyms:
- TANGO13B
- Chromosome:
- 22q12.1
- Locus Type:
- gene with protein product
- Date approved:
- 1998-10-14
- Date modifiied:
- 2015-12-11
Related products to: TPST2 antibody
Related articles to: TPST2 antibody
- Adaptive immune responses play a critical role in the pathogenesis of amyotrophic lateral sclerosis (ALS). In this study, we investigated the functional mechanisms of T cell subtypes and assessed the causal links between CD4+ cytotoxic T cell-related genes and ALS risk. - Source: PubMed
Pang Xin YuanWang Hong FenBai Jiong MingHuang Xu Sheng - Tyrosine sulfation is a widespread posttranslational modification in mammals and is known to influence protein function and signaling. However, its functional significance during porcine preimplantation development remains poorly understood. - Source: PubMed
Publication date: 2026/01/22
Gao JiazeWang ChengpengXie HongshuangYang GuangYang QingboHuang ChengLi ShijieLiu ZhonghuaHe TianyaoYin ZhiJin Jun-XueWang Jiaqiang - Tyrosylprotein sulfotransferases (TPSTs) catalyze O-sulfation of tyrosine residues on secreted and membrane proteins, but the molecular basis for their stimulation by metal ions remains unclear. We determined the structures of the catalytic domain of human TPST2 with PAP and Na (1.75 Å) or Mn (2.00 Å) bound and identified two conserved octahedral metal-binding sites. Anomalous diffraction at metal absorption edges confirmed the identity of the bound metals and demonstrated specific Mn binding. The Na- and Mn-bound structures closely superimposed, suggesting activation without large conformational changes. Structural comparison with the apo structure and ensemble refinement revealed differences in local dynamics around the metal binding sites. The flexible α3-helix and α12-α13 loop in the apo structure were stabilized by Na binding and further rigidified by Mn binding. These findings support an activation-by-ordering mechanism in which Na binding generates a pre-activated state, with Mn subsequently establishing a catalytically competent ordering that lowers the entropic barrier at the active-site entrance. This framework reconciles longstanding biochemical observations and suggests that Mn availability within the Golgi can tune TPST2-dependent signaling. - Source: PubMed
Publication date: 2026/01/23
Jin MinwooNoh ChaeminYang JihyeongKim HyunwooPark Soo BinKim Yong-ChulEom Soo Hyun - Multiple myeloma (MM), a malignancy of plasma cells in the bone marrow, urgently requires novel prognostic biomarkers. However, the prognostic significance of disulfidptosis-related genes and their association with treatment response in MM remain unclear. - Source: PubMed
Publication date: 2025/12/01
Zang YunkeZhou PeipeiDong HaotianWang JingfeiCao RongxuanYang GuimaoWu QianqianSun YanhuaSun Yanli - Protein tyrosine sulfation is of growing scientific interest due to its biological and clinical significance, yet it remains an underexplored post-translational modification (PTM). Catalyzed by Golgi-localized TPST1 and TPST2, tyrosine sulfation modulates protein-protein interactions and receptor-ligand binding in inflammation, hemostasis, immunity, and viral entry. Despite functional relevance, this modification is underrepresented in databases such as UniProt (accessed July 2025), in large part due to a lack of robust analytical strategies. Advances in mass spectrometry (MS)-based analyses have recently improved sensitivity of detection, expanding the known tyrosine 'sulfome.' Systematic profiling of sulfated residues can now be undertaken, expanding knowledge of their regulatory roles in both health and disease, and for pioneering new sulfation-targeted therapeutics. - Source: PubMed
Publication date: 2025/12/15
Oswald Sally ODaly Leonard AMesdaghi ShahramJones SarahRigden Daniel JEyers Patrick AEyers Claire E