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

• BMSC-UbP localizes at chromosome 15q22.3-q23 as confirmed by blast search in human genome [2].
• Using large-scale screening of human bone marrow stromal cell (BMSC) cDNA library, we isolated a full-length cDNA of 1352 bp encoding 380 amino acids with a ubiquitin domain (UBQ), which was designed as bone marrow stromal cell-derived ubiquitin-like protein (BMSC-UbP) [2].
• Moreover, BMSC-UbP mRNA decreased in BMSC stimulated with PMA and increased in HL60 cells stimulated with LPS, suggesting that BMSC-UbP might play roles in regulation of BMSC function or cell differentiation through an evocator- and cell-specific pattern [2].

Anatomical context of UBL7

• BMSC-UbP mRNA is widely expressed in human multiple tissues and various tumor cell lines [2].

References