A mass-spectrometry draft of the human proteome
A mass-spectrometry survey drafted the human proteome across tissues, cell lines, and body fluids, capturing protein information that genomics alone cannot.
What the study found
Proteomes carry information — large differences in protein abundance, tissue- and time-dependent expression, and post-translational modifications — that genomics and transcriptomics do not capture. In this 2014 Nature study, researchers used mass spectrometry to assemble a draft of the human proteome from human tissues, cell lines, and body fluids, and released a public database (ProteomicsDB) for real-time analysis. The data allowed estimation of the size of the protein-coding genome and identified organ-specific proteins and translated products of some long non-coding RNAs.
Why it matters
Genes are the same in every cell; which proteins are actually made, where, and in what form is what defines a tissue and how disease arises. A mass-spectrometry map measures proteins directly rather than inferring them from RNA, so it can catch abundance differences and modifications, and even flag protein evidence for regions of the genome once thought non-coding.
Analysis — the pattern
Placed beside antibody-based atlases and structure prediction (this is analysis): mass spectrometry, imaging, and computation are converging into a systems-level view of proteins rather than one-protein-at-a-time study. A live direction is single-cell and spatial proteomics, resolving expression far more finely than a tissue average.
What is still uncertain
Mass-spectrometry coverage is uneven, low-abundance proteins are hard to detect, and identifications require careful statistical control. It is a reference resource for research, not a diagnosis, and drafts are revised as methods improve.