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Gene Review

UBL7  -  ubiquitin-like 7

Homo sapiens

Synonyms: BMSC-UbP, BMSCUBP, Bone marrow stromal cell ubiquitin-like protein, MGC14421, SB132, ...
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High impact information on UBL7

  • In the complex structure, three residues (Met76, Ile78, and Leu99) of BMSC-UbP UBA form a trident anchoring the domain to the hydrophobic concave surface of ubiquitin defined by residues Leu8, Ile44, His68, and Val70 [1].
  • The structure determination was facilitated by using a solubility-enhancement tag (SET) GB1, immunoglobulin G binding domain 1 of Streptococcal protein G. The results show that BMSC-UbP UBA domain is primarily comprised of three alpha-helices with a hydrophobic patch defined by residues within the C terminus of helix-1, loop-1, and helix-3 [1].
  • The previously identified BMSC-UbP protein derived from bone marrow stromal cells contains a ubiquitin-associated (UBA) domain at the C terminus that has been implicated in linking cellular processes and the ubiquitin system [1].
  • The structural model of BMSC-UbP UBA domain complexed with ubiquitin was constructed by chemical shift mapping combined with the program HADDOCK, which is in agreement with the result from mutagenesis studies [1].
  • Cloning and identification of a novel ubiquitin-like protein, BMSC-UbP, from human bone marrow stromal cells [2].

Biological context of UBL7


Anatomical context of UBL7


  1. Solution structure of the ubiquitin-associated domain of human BMSC-UbP and its complex with ubiquitin. Chang, Y.G., Song, A.X., Gao, Y.G., Shi, Y.H., Lin, X.J., Cao, X.T., Lin, D.H., Hu, H.Y. Protein Sci. (2006) [Pubmed]
  2. Cloning and identification of a novel ubiquitin-like protein, BMSC-UbP, from human bone marrow stromal cells. Liu, S., Yu, Y., An, H., Li, N., Lin, N., Wang, W., Zhang, W., Wan, T., Cao, X. Immunol. Lett. (2003) [Pubmed]
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