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UBA Domain
Class:Ubiquitin processes

No ImageNMR data reveals that the UBA domains of the human homologue of yeast Rad23A (HHR23A) form three-helix bundles with a hydrophobic core that stabilizes the protein. These domains also possess a conserved surface patch of hydrophobic amino acids that likely interact with hydrophobic regions of ubiquitin and other target proteins.

Structure Reference:
Mueller, TD. and Feigon, J. (2002) J. Mol. Biol. 319(5): 1243-1255. PDB: 1IFY.

Domain binding and function:
The ubiquitin-associated (UBA) domain is an approximately 40 amino acid motif that was first recognized in proteins associated with ubiquitination but is also found in proteins involved in DNA nucleotide excision-repair and other proteins. UBA domains have been shown to bind mono-, di-, tri-, and tetra-ubiquitin in vitro but appear to bind to polyubiquitin with a higher affinity and it is thought that polyubiquitinated proteins represent the true in vivo binding substrates. As well, some UBA domains appear to homo and heterodimerize and to bind other substrates. Functionally, the UBA domain has been proposed to limit ubiquitin chain elongation and to target ubiquitinated proteins to the 26S proteasome for degradation.
Examples of Proteins: 
UBA Domain Proteins
Binding Partners
HHR23A mono and polyubiquitin
Rad23 (homodimerization)
HHR23A (heterodimerization)
c-Cbl unknown
HIP-2 E2 unknown

No Image

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