KlaDB：A Multi‑species Database of Lysine Lactylation Sites with Benchmarking of Prediction Models

Lactylation, a novel lactate-derived lysine post-translational modification (PTM), has emerged as a critical mechanistic link between cellular metabolism and epigenetic regulation. With the development of mass spectrometry (MS) techniques, a large number of lactylation sites have been identified. However, no dedicated, comprehensive lysine lactylation (Kla)-specific database has been established to date.

Here, we constructed KlaDB (Lysine Lactylation Database)，which currently contains 64,072 experimentally validated lactylation sites in 17,759 proteins across 9 species. The database offers a user-friendly interactive interface that helps researchers to intuitively explore and retrieve comprehensive information associated with each Kla site. Furthermore, KlaDB incorporates a systematic multi-species benchmarking analysis of four published lysine lactylation (Kla) prediction models, offering guidance for users to select appropriate computational tools.