DnaJ homolog subfamily C member 2

Definition:

Acts both as a chaperone in the cytosol and as a chromatin regulator in the nucleus. When cytosolic, acts as a molecular chaperone: component of the ribosome-associated complex (RAC), a complex involved in folding or maintaining nascent polypeptides in a folding-competent state. In the RAC complex, stimulates the ATPase activity of the ribosome-associated pool of Hsp70-type chaperones HSPA14 that bind to the nascent polypeptide chain. When nuclear, mediates the switching from polycomb-repressed genes to an active state: specifically recruited at histone H2A ubiquitinated at 'Lys-119' (H2AK119ub), and promotes the displacement of the polycomb PRC1 complex from chromatin, thereby facilitating transcription activation.

References:

[1]. Holger Richly, et al. Transcriptional activation of polycomb-repressed genes by ZRF1. Nature. 2010 Dec 23;468(7327):1124-8. [Content Brief]

[2]. Heather A Hundley, et al. Human Mpp11 J protein: ribosome-tethered molecular chaperones are ubiquitous. Science. 2005 May 13;308(5724):1032-4. [Content Brief]

[3]. Hendrik Otto, et al. The chaperones MPP11 and Hsp70L1 form the mammalian ribosome-associated complex. Proc Natl Acad Sci U S A. 2005 Jul 19;102(29):10064-9. [Content Brief]

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