UBL4A, also known as GDX, has been characterized as a ubiquitously expressed and highly conserved protein from humans to plants. The N-terminal region of UBL4A shares 43% sequence identity with ubiquitin, however the C-terminal region has no homology to ubiquitin and it is therefore unlikely that UBL4A plays any role in targeting cellular proteins for degradation.
Dephosphorylates 26S nuclear proteasomes, thereby decreasing their proteolytic activity. The dephosphorylation may prevent assembly of the core and regulatory particles (CP and RP) into mature 26S proteasome.
Acts as a novel regulator of senescence. Involved in the formation of senescence-associated heterochromatin foci (SAHF), which represses expression of proliferation-promoting genes. Binds to proliferation-promoting genes. May be required for replication-independent chromatin assembly.
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