{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["FitzHugh ZT"],"funding":["National Institutes of Health"],"pagination":["355"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9953674"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["13(2)"],"pubmed_abstract":["All proteins have a carboxyl terminus, and we previously summarized eight mutations in binding and trafficking sequence determinants in the C-terminus that, when disrupted, cause human diseases. These sequence elements for binding and trafficking sites, as well as post-translational modifications (PTMs), are called minimotifs or short linear motifs. We wanted to determine how frequently mutations in minimotifs in the C-terminus cause disease. We searched specifically for PTMs because mutation of a modified amino acid almost always changes the chemistry of the side chain and can be interpreted as loss-of-function. We analyzed data from ClinVar for disease variants, Minimotif Miner and the C-terminome for PTMs, and RefSeq for protein sequences, yielding 20 such potential disease-causing vari"],"journal":["Biomolecules"],"pubmed_title":["Systematic Assessment of Protein C-Termini Mutated in Human Disorders."],"pmcid":["PMC9953674"],"funding_grant_id":["R15GM107983","R01GM079689","P20GM121325","LM010101","GM103440"],"pubmed_authors":["Schiller MR","FitzHugh ZT"],"additional_accession":[]},"is_claimable":false,"name":"Systematic Assessment of Protein C-Termini Mutated in Human Disorders.","description":"All proteins have a carboxyl terminus, and we previously summarized eight mutations in binding and trafficking sequence determinants in the C-terminus that, when disrupted, cause human diseases. These sequence elements for binding and trafficking sites, as well as post-translational modifications (PTMs), are called minimotifs or short linear motifs. We wanted to determine how frequently mutations in minimotifs in the C-terminus cause disease. We searched specifically for PTMs because mutation of a modified amino acid almost always changes the chemistry of the side chain and can be interpreted as loss-of-function. We analyzed data from ClinVar for disease variants, Minimotif Miner and the C-terminome for PTMs, and RefSeq for protein sequences, yielding 20 such potential disease-causing vari","dates":{"release":"2023-01-01T00:00:00Z","publication":"2023 Feb","modification":"2025-04-05T13:21:01.528Z","creation":"2024-10-15T13:18:12.26Z"},"accession":"S-EPMC9953674","cross_references":{"pubmed":["36830724"],"doi":["10.3390/biom13020355"]}}