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| N-ter acetylation | Mature Ntermini position start | Subcellular localization |
Protein N-terminal status is crucial in protein fate and protein half-life. Some of the most frequent protein N-termini modifications are co-translational and associated to Met excision and/or N-terminal acetylation. Some others occur post-translationally such as the excision of a targeting/transit peptide as observed for nuclear coded proteins targeting to the mitochondrial or the chloroplast organelles.
Our large-scale N-terminomics analyses provide some highly relevant data that have been integrated in a dedicated database i.e., NTerdb.
Such collected data were curated for subcellular localisation, protein N-terminus status and mature N-terminal starting position using the data redundancy and the annotations available in various databases.
The NTerdb contains more than 200.000 mature experimental N-termini related to 35.000 distinct non-redundant proteins. Nearly 8.000 proteins have been manually curated for subcellular localization and/or mature protein position start. The process of validation is still in progress...
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| Proteins with experimental data | Proteins curated (subcell. localization, N-termini position start) |
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