MGSSHHHHHH SSGLVPRGSH MGSMFGPAKG RHFGVHPAPG FPGGVSQQAA GTKAGPAGAW PVGSRTDTMW RLRCKAKDGT HVLQGLSSRT RVRELQGQIA AITGIAPGGQ RILVGYPPEC LDLSNGDTIL EDLPIQSGDM LIIEEDQTRP RSSPAFTKRG ASSYVRETLP VLTRTVVPAD NSCLFTSVYY VVEGGVLNPA CAPEMRRLIA QIVASDPDFY SEAILGKTNQ EYCDWIKRDD TWGGAIEISI LSKFYQCEIC VVDTQTVRID RFGEDAGYTK RVLLIYDGIH YDPLQRNFPD PDTPPLTIFS SNDDIVLVQA LELADEARRR RQFTDVNRFT LRCMVCQKGL TGQAEAREHA KETGHTNFGE V.
YOD1 is composed of 348 amino acids and is characterized by the presence of an OTU domain, which is essential for its deubiquitinating activity . The recombinant form of YOD1 is typically expressed in E. coli and purified using conventional chromatography techniques . The recombinant protein often includes an N-terminal His-tag to facilitate purification and detection.
YOD1’s primary function is to remove ubiquitin moieties from polyubiquitinated proteins, thereby regulating their stability and degradation . This activity is crucial for maintaining cellular homeostasis and preventing the accumulation of misfolded or damaged proteins. YOD1 is a component of a multiprotein complex centered around p97, suggesting its involvement in the dislocation of misfolded proteins from the endoplasmic reticulum .
Recent studies have highlighted the significance of YOD1 in various diseases, particularly cancer. For instance, YOD1 has been implicated in the progression of triple-negative breast cancer (TNBC) by regulating the stability of CDK1, a key cell cycle protein . Aberrant expression of YOD1 has been associated with poor prognosis in TNBC patients, making it a potential therapeutic target .
Additionally, YOD1 has been identified as a potential prognostic biomarker for pancreatic cancer . Its expression levels correlate with the aggressiveness of pancreatic ductal adenocarcinoma (PDAC), a highly malignant form of pancreatic cancer .
Recombinant YOD1 is widely used in research to study its biochemical properties and role in various cellular processes. It serves as a valuable tool for investigating the mechanisms of protein ubiquitination and deubiquitination, as well as their implications in disease.