Proteomics plays a key and insightful role in meat research in the post-genomic era. This study aimed to unveil using a shotgun proteomics approach the temporal dynamic changes in early post-mortem proteome of goat Semitendinosus muscle. Therefore, the evolution and comparison of the muscle proteome over three post-mortem times (1, 8, and 24 h) was assessed. The temporal proteomics profiling quantified 748 proteins, from which 174 were differentially abundant (DAPs): n = 55 between 1 h versus 8 h, n = 52 between 8 h versus 24 h, and n = 154 between 1 h versus 24 h. The DAPs belong to myriad interconnected pathways. Binding, transport and calcium homeostasis, as well as muscle contraction and structure, exhibited an equivalent contribution during post-mortem, demonstrating their central role. Catalytic, metabolism and ATP metabolic process, and proteolysis were active pathways from the first hours of animal bleeding. Conversely, oxidative stress, response to hypoxia and cell redox homeostasis along chaperones and heat shock proteins accounted for the large proportion of the biochemical processes, more importantly after 8 h post-mortem. Overall, the conversion of muscle into meat is largely orchestrated by energy production as well as mitochondrial metabolism and homeostasis through calcium and permeability transition regulation. The study further evidenced the role of ribosomal proteins in goat post-mortem muscle, signifying that several proteins experiencing changes during storage, also undergo splicing modifications, which is for instance a mechanism known for mitochondrial proteins. Overall, temporal proteomics profiling of early post-mortem muscle proteome offers an unparalleled view of the sophisticated post-mortem biochemical and proteolytic events associated with goat meat quality determination.