Both urinary proteome and its glycoproteome can reflect human health status, and more directly, functions of kidney and urinary tracts. Since high abundant protein albumin is not N-glycosylated, the urine N-glycoprotein enrichment procedure could deplete it and urine proteome could thus provide a more detailed protein profile in addition to glycosylation information, especially when albuminuria occurrs in some kidney diseases. In terms of describing the details of urinary proteins, urine glycoproteome is even a better choice than proteome itself. Pooled urine samples from healthy volunteers were collected and acetone precipitated for proteins. N-linked glycoproteins enriched with Concanavalin A affinity purification were separated and analyzed by SDS-PAGE-RPLC/MS/MS or 2D-LC/MS/MS. A total of 225 urinary proteins were identified based on 2-hit criteria with reliability over 97% for each peptide. Among these proteins, 94 were identified in previous urine proteome works; 150 were annotated as glycoproteins in SWISS-PROT, and 43 were predicted as glycoproteins by NetNGlyc 1.0. A number of known biomarkers and disease related glycoproteins were identified. Since changes of protein quantity or the glycosylation status can lead to changes of the Con A captured glycoprotein profile, specific urine glycoproteome patterns might be observed for specific pathological conditions as multiplex urinary biomarkers. The knowledge of urine glycoproteome is important in understanding kidney and body function.