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DnaJ homolog subfamily B member 12 (DNAJB12) is an ER-localized Hsp40 co-chaperone that recruits Hsp70 to the ER surface to facilitate protein folding, triage, and degradation processes. It contains an N-terminal J-domain, a transmembrane domain, and a stress-sensitive DUF1977 domain, making it important for regulating ER homeostasis, especially under conditions of proteotoxic stress. DNAJB12 is important for the constitutive degradation of BOK, a pro-apoptotic BCL-2 family protein, thereby functioning as an ER stress sensor and influencing cell survival and apoptosis
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