title: Identification of ubiquitinated proteins from human multiple myeloma U266 cells by proteomics.
abstract: OBJECTIVE
  To identify ubiquitinated proteins from complex human multiple myeloma (MM) U266 cells, a malignant disorder of differentiated human B cells.
  
  
  METHODS
  Employing a globally proteomic strategy combining of immunoprecipitation, LC-MS/MS and SCX-LC-MS analysis to identified ubiquitination sites, which were identified by detecting signature peptides containing a GG-tag (114.1 Da) and an LRGG-tag (383.2 Da).
  
  
  RESULTS
  In total, 52 ubiquitinated proteins containing 73 ubiquitination sites of which 14 and 59 sites contained LRGG-tag and GG-tag were identified, respectively.
  
  
  CONCLUSIONS
  Classification analysis by of the proteins identified in the study based on the PANTHER showed that they were associated with multiple functional groups. This suggested the involvement of many endogenous proteins in the ubiquitination in MM.
authors: Jinan University, Guangdong, China.
authors: HongLing
authors: H
authors: Jia
authors: ChaoWu
authors: C
authors: Liu
authors: Feng
authors: F
authors: Ge
authors: ChuanLe
authors: C
authors: Xiao
authors: ChunHua
authors: C
authors: Lu
authors: Tong
authors: T
authors: Wang
authors: QingYu
authors: Q
authors: He
mesh_terms: D045744:Cell Line, Tumor; D020869:Gene Expression Profiling; D015972:Gene Expression Regulation, Neoplastic / Q000502:physiology*; D006801:Humans; D009101:Multiple Myeloma / Q000378:metabolism*; D009363:Neoplasm Proteins / Q000235:genetics / Q000378:metabolism*; D040901:Proteomics / Q000379:methods*; D054875:Ubiquitination
chemical_list: D009363:Neoplasm Proteins