<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Wang J</submitter><funding>NIAID NIH HHS</funding><funding>NHGRI NIH HHS</funding><funding>U.S. Department of Health &amp;amp;amp; Human Services | NIH | National Institute of General Medical Sciences</funding><funding>Wellcome Trust</funding><funding>NIGMS NIH HHS</funding><funding>National Science Foundation</funding><pagination>16177</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC6212499</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>8(1)</volume><pubmed_abstract>Protein arginylation mediated by arginyltransferase ATE1 is a key regulatory process essential for mammalian embryogenesis, cell migration, and protein regulation. Despite decades of studies, very little is known about the specificity of ATE1-mediated target site recognition. Here, we used in vitro assays and computational analysis to dissect target site specificity of mouse arginyltransferases and gain insights into the complexity of the mammalian arginylome. We found that the four ATE1 isoforms have different, only partially overlapping target site specificity that includes more variability in the target residues than previously believed. Based on all the available data, we generated an algorithm for identifying potential arginylation consensus motif and used this algorithm for global pr</pubmed_abstract><journal>Scientific reports</journal><pubmed_title>Target site specificity and in vivo complexity of the mammalian arginylome.</pubmed_title><pmcid>PMC6212499</pmcid><funding_grant_id>R01 GM104003</funding_grant_id><funding_grant_id>DBI-1458477</funding_grant_id><funding_grant_id>R01 GM108744</funding_grant_id><funding_grant_id>R35GM122505</funding_grant_id><funding_grant_id>R01GM108744</funding_grant_id><funding_grant_id>R35 GM122505</funding_grant_id><funding_grant_id>R01GM104003</funding_grant_id><funding_grant_id>U41 HG007234</funding_grant_id><funding_grant_id>R01 AI118891</funding_grant_id><funding_grant_id>R01 GM110174</funding_grant_id><pubmed_authors>Dann GP</pubmed_authors><pubmed_authors>Wolf MY</pubmed_authors><pubmed_authors>Huang Y</pubmed_authors><pubmed_authors>Radivojac P</pubmed_authors><pubmed_authors>Garcia BA</pubmed_authors><pubmed_authors>Kashina A</pubmed_authors><pubmed_authors>Wang J</pubmed_authors><pubmed_authors>Kellis M</pubmed_authors><pubmed_authors>Pejaver VR</pubmed_authors></additional><is_claimable>false</is_claimable><name>Target site specificity and in vivo complexity of the mammalian arginylome.</name><description>Protein arginylation mediated by arginyltransferase ATE1 is a key regulatory process essential for mammalian embryogenesis, cell migration, and protein regulation. Despite decades of studies, very little is known about the specificity of ATE1-mediated target site recognition. Here, we used in vitro assays and computational analysis to dissect target site specificity of mouse arginyltransferases and gain insights into the complexity of the mammalian arginylome. We found that the four ATE1 isoforms have different, only partially overlapping target site specificity that includes more variability in the target residues than previously believed. Based on all the available data, we generated an algorithm for identifying potential arginylation consensus motif and used this algorithm for global pr</description><dates><release>2018-01-01T00:00:00Z</release><publication>2018 Nov</publication><modification>2025-04-04T21:37:38.931Z</modification><creation>2019-03-27T00:06:10Z</creation></dates><accession>S-EPMC6212499</accession><cross_references><pubmed>30385798</pubmed><doi>10.1038/s41598-018-34639-6</doi></cross_references></HashMap>