Function: 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'. Ref.8 Ref.9 Ref.15
Subunit structure: Interacts (via ZRF1-UBD region) with ID1
By similarity. Component of ribosome-associated complex (RAC), a heterodimer composed of Hsp70/DnaK-type chaperone HSPA14 and Hsp40/DnaJ-type chaperone DNAJC2. Ref.8
Subcellular location: Nucleus. Cytoplasm › cytosol Ref.8 Ref.15.
Tissue specificity: Widely expressed. Ref.5
Induction: Expression is repressed by CEBPA. Strongly overexpressed in leukemic cells. Ref.6 Ref.7 Ref.11
Domain: The ZRF1-UBD region specifically recognizes and binds H2AK119ub. The ZRF1-UBD region is also involved in protein-protein interactions with other proteins, suggesting that it may be masked by some regulator, thereby preventing its association with H2AK119ub. Ref.15
Post-translational modification: Phosphorylated in M (mitotic) phase. Ref.1
Miscellaneous: Constitutes a myeloid leukemia-associated antigen and might be a target for leukemia T-cell therapy.
Sequence similarities: Contains 1 J domain.Contains 2 SANT domains.
Sequence caution: The sequence AAI39752.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.The sequence CAA66913.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
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