UBX protein domain

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UBX
solution structure of the ubx domain of kiaa0794 protein
Identifiers
SymbolUBX
PfamPF00789
Pfam clanCL0072
InterProIPR001012
SMARTUBX
SCOP21i42 / SCOPe / SUPFAM
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

In molecular biology, the UBX protein domain is found in ubiquitin-regulatory proteins, which are members of the ubiquitination pathway, as well as a number of other ubiquitin-like proteins including FAF-1 (FAS-associated factor 1), the human Rep-8 reproduction protein and several hypothetical proteins from yeast. The function of the UBX domain is not known although the fragment of avian FAF-1 containing the UBX domain causes apoptosis of transfected cells.

Function[edit]

So far, as yet, no general function for the UBX domain has yet emerged.[1] Additionally, the absence of a carboxy-terminal di-glycine motif, however, indicates that UBX domains are not covalently attached to target proteins in a ubiquitin-like manner.[2]

Structure[edit]

The UBX domain comprises about 80 amino acid residues. They are distinct structural units defining a large family of proteins that often exhibit a modular domain architecture three-dimensional structures of UBX domains reveal a close structural relationship with ubiquitin despite the lack of significant sequence homology[2]

Homology[edit]

UBX domain is very similar to ubiquitin which gives us some indication of evolution. There are ubiquitin fusion which seem to be advantageous for ribosomal subunit folding.[2]

References[edit]

  1. ^ Buchberger A (May 2002). "From UBA to UBX: new words in the ubiquitin vocabulary". Trends in Cell Biology. 12 (5): 216–21. doi:10.1016/S0962-8924(02)02269-9. PMID 12062168.
  2. ^ a b c Schuberth C, Buchberger A (August 2008). "UBX domain proteins: major regulators of the AAA ATPase Cdc48/p97". Cellular and Molecular Life Sciences. 65 (15): 2360–71. doi:10.1007/s00018-008-8072-8. PMID 18438607.
This article incorporates text from the public domain Pfam and InterPro: IPR001012