Abundant proteins of human multiple myeloma (MM) were globally analyzed and identified by using two- dimensional gel electrophoresis (2DE) and MALDI-TOF/TOF mass spectrometry (MS). Spots of 517 corresponding to 268 different proteins were detected on 2DE gels of protein lysate from plasma cells isolated from eight newly diagnosed MM patients. These identified proteins were classified into different categories based on their molecular functions and biological processes. The detailed experimental procedures and MS spectra of all the identified proteins have been deposited in the Proteomics Identifications Database (PRIDE) (http://www.ebi.ac.uk/pride) with Accession No. 8846 & 8847. This 2DE map of MM proteins will be an invaluable resource for further proteomics research that investigates proteomic changes associated with biomarker identification and carcinogenesis analysis of multiple myeloma.