Death-associated protein 1 (DAP1) is a proline-rich cytoplasmatic protein highly conserved in most eukaryotes. It has been reported to be involved in controlling cell growth and migration, autophagy and apoptosis. The presence of human DAP1 is associated to a favourable prognosis in different types of cancer. Here we describe the almost complete \({{^{1}}\text {H}}\), \({{^{13}}\text {C}}\), and \({{^{15}}\text {N}}\) chemical shift assignments of the human DAP1. The limited spectral dispersion, mainly in the \({{^{1}}\text {H}{^{\text{N}}}}\) region, and the lack of defined secondary structure elements, predicted based on chemical shifts, identifies human DAP1 as an intrinsically disordered protein (IDP). This work lays the foundation for further structural investigations, dynamic studies, mapping of potential interaction partners or drug screening and development.

死亡相关蛋白 1 (DAP1) 是一种富含脯氨酸的细胞质蛋白，在大多数真核生物中高度保守。据报道，它参与控制细胞生长和迁移、自噬和凋亡。人类 DAP1 的存在与不同类型癌症的良好预后相关。这里我们描述几乎完整的\({{^{1}}\text {H}}\) 、 \({{^{13}}\text {C}}\)和\({{^{15 }}\text {N}}\)人类 DAP1 的化学位移分配。基于化学预测，光谱色散有限，主要集中在\({{^{1}}\text {H}{^{\text{N}}}}\)区域，并且缺乏明确的二级结构元素转变，将人类 DAP1 识别为本质上无序的蛋白质 (IDP)。这项工作为进一步的结构研究、动态研究、潜在相互作用伙伴的绘图或药物筛选和开发奠定了基础。