cDNA cloning of a human 100 kDa de‐ubiquitinating enzyme: the 100 kDa human de‐ubiquitinase belongs to the ubiquitin C‐terminal hydrolase family 2 (UCH2)

FEBS Letters

Frutiger, Séverine¹  Paquet, Nicole¹  Hoang-Van, Khan¹  Hughes, Graham J.¹  Falquet, Laurent¹  Jaton, Jean-Claude¹ 

[1] Department of Medical Biochemistry, Faculty of Medicine, University of Geneva, Medical Center, 1 rue Michel-Servet, CH-1211 Geneva 4, Switzerland

关键词: De-ubiquitinase;    Isopeptidase;    cDNA;    Ub;    ubiquitin;    UCH;    ubiquitin C-terminal hydrolase;    PVDF;    polyvinylidene difluoride;    sp;    Swissprot;    gb;    Genbank;    gp;    Genpept;    pir;    protein identification resource;    RACE-PCR;    rapid amplification of cDNA ends-PCR;   

DOI  :  10.1016/0014-5793(95)01287-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The full length cDNA encoding a 100 kDa human de-ubiquitinating enzyme, referred to as de-ubiquitinase was obtained using one clone selected from a randomly sequenced human brain cDNA library and specific primers. The sequence of 18 peptides generated from the de-ubiquitinase isolated from outdated human erythrocytes matched perfectly with the predicted amino acid sequence, which would encode a protein containing 858 amino acids (calculated M _r = 95,743 Da). Homology search disclosed that the protein is a member of a large family of ubiquitin C-terminal hydrolases (UCH2), that was defined on the basis of the presence of two specific patterns, ‘the Cys- and His-domains’, which are likely to be involved in the de-ubiquitinating activity [7]. An additional conserved region, ‘the aspartic acid domain’, was also identified, the functional role of which is unknown.

【 授权许可】

Unknown