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Table 1 GBM proteins identified as potential CPZ targets

From: Chlorpromazine induces cytotoxic autophagy in glioblastoma cells via endoplasmic reticulum stress and unfolded protein response

Protein Name Gene Name UNIPROT Protein AC Main Cellular Localization Molecular function Biological role in UPR
BiP HSPA5 P11021 ER- Cytoplasm Molecular chaperone Master regulator of UPR [38,39,40]
Endoplasmin HSP90B1 P14625 ER lumen Molecular chaperone Protein folding [41];
ER-associated degradation (ERAD) [42]
Heat shock protein HSP 90-beta HSP90AB1 P08238 Cell membrane – Nucleus –Cytoplasm - Secreted Molecular chaperone Protein folding [43]
T-complex protein 1 (TRiC) TCP1 (subunit alpha) P17987 Cytoskeleton; cytosol Subunits of chaperone complex TRiC Protein folding [44, 45]
CCT5 (subunit epsilon) P48643 Cytoskeleton; cytoplasm
CCT6 (subunit zeta) P40227 Cytoplasm
CCT8 (subunit theta) P50990 Cytoskeleton - Cytoplasm
Heat shock protein 75 kDa TRAP1 Q12931 Mitocondrion Molecular chaperone Translational attenuation [46]
Elongation factor 1-alpha 1 EEF1A1 P68104 Cell membrane - nucleus Elongation factor Regulation of chaperone-mediated autophagy [47]
EF2; Elongation factor 2 EEF2 P13639 Cytoplasm - Nucleus Elongation factor Inhibition of protein synthesis [48]
TER ATPase; Transitional endoplasmic reticulum ATPase VCP P55072 Cytosol; ER; nucleus Hydrolase Elimination of misfolded proteins from the ER [51]; ERAD pathway
  1. GBM protein factors whose ability to bind ATP/GTP appeared modified by the presence of CPZ and thus recognized as potential targets of the drug. Their identification has been done via ABPP-MS, using a kinase enrichment procedure with an insoluble ATP probe