中文摘要：

我们从人的树枝状的房间识别了新奇象 ubiquitin 一样分子 DULP。DULP 包含与 ubiquitin 分享 26% 身份和 34% 类似的一个领域，并且它拥有恐水病的补丁由 mono-ubiquitin 或 poly-ubiquitin 过去常与一个 ubiquitin 相互作用主题(UIM ) 或联系 ubiquitin 的领域(UBA ) 交往的相应 Ile-44。相应于 6 ubiquitin 的离氨酸残余，涉及能绑 proteasomal 子单元 Rpn10/S5a 的 multi-ubiquitin 链的形成，也在它的 ubiquitin 相同领域被保存。然而， DULP 不拥有 Gly-Gly 为要求让 polyubiquitin 链的形成为降级指向底层的 ubiquitin 变化形式或 Lys-48 要求的高度保存的 C 终点，建议它可能是新奇 ubiquitin 域蛋白质(UDP ) 。DULP 被发现广泛地在许多房间表示了， ubiquitin 相同领域没被劈开。我们也证实那 DULP 表情在原子核和在 cytosol 更弱的大部分被充实。而且，我们发现在 293T 房间的 DULP 的 overexpression 导致了 apoptosis，它可能没与 mitochondrial 或 proteasome 小径被联系，与特定的机制遗体不清楚。进一步的调查被需要识别 DULP 的精确生物功能。

英文摘要：

We identified a novel ubiquitin-like molecule DULP from human dendritic cells. DULP contains a domain that shares 26% identity and 34% similarity with ubiquitin, and it possesses the corresponding Ile-44 hydrophobic patch used by mono- or poly-ubiquitin to interact with a ubiquitin-interaction motif （UIM） or ubiquitin-associated domain （UBA）. Lysine residue corresponding to 6 of ubiquitin, which is involved in the formation of a multi-ubiquitin chain that can bind proteasomal subunit Rpn10/S5a, is also conserved in its ubiquitin-homology domain. However, DULP does not possess the highly conserved C-terminus Gly-Gly required for ubiquitin conjugation or the Lys-48 required for the formation of polyubiquitin chain to target substrates for degradation, suggesting it might be a novel ubiquitin-domain protein （UDP）. DULP was found widely expressed in many cells and the ubiquitin-homology domain was not cleaved. We also confirmed that DULP expression was enriched in the nucleus and much weaker in the cytosol. Besides, we found that overexpression of DULP in 293T cells induced apoptosis, which might not be associated with the mitochondrial or proteasome pathway, with the specific mechanism remain unclear. Further investigations are needed to identify the precise biological functions of DULP. Cellular ＆ Molecular Immunology.