Journal
BIOLOGY DIRECT
Volume 8, Issue -, Pages -Publisher
BIOMED CENTRAL LTD
DOI: 10.1186/1745-6150-8-29
Keywords
eEF1A1; eEF1A2; Phosphorylation; Methylation; Acetylation; Ubiquitination; Post-translational modification
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Funding
- Wellcome Trust
- Medical Research Council [MRC 724GMM RA2389]
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Translation elongation factors eEF1A1 and eEF1A2 are 92% identical but exhibit non-overlapping expression patterns. While the two proteins are predicted to have similar tertiary structures, it is notable that the minor variations between their sequences are highly localised within their modelled structures. We used recently available high-throughput omics data to assess the spatial location of post-translational modifications and discovered that they are highly enriched on those surface regions of the protein that correspond to the clusters of sequence variation. This observation suggests how these two isoforms could be differentially regulated allowing them to perform distinct functions.
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