2m2e
From Proteopedia
Jump to navigationJump to search
Solution NMR structure of the SANT domain of human DNAJC2, Northeast structural genomics consortium target HR8254a
| ||||||||||||
Structural highlights
FunctionDNJC2_HUMAN 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. Specifically binds DNA sequence 5'-GTCAAGC-3'.[1] [2] [3] See AlsoReferences
| ||||||||||||||||||
This page was last modified 05:58, 15 May 2024.