Comprehensive analysis of human protein N-termini enables assessment of various protein forms

Abstract Various forms of protein (proteoforms) are generated by genetic variations, alternative splicing, alternative translation initiation, co- or post-translational modification and proteolysis. Different proteoforms are in part discovered by characterizing their N-terminal sequences. Here, we i...

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Autores principales:	Jeonghun Yeom, Shinyeong Ju, YunJin Choi, Eunok Paek, Cheolju Lee
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/b48742968cde47cb918ada2680e8d341
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spelling	oai:doaj.org-article:b48742968cde47cb918ada2680e8d3412021-12-02T15:05:50ZComprehensive analysis of human protein N-termini enables assessment of various protein forms10.1038/s41598-017-06314-92045-2322https://doaj.org/article/b48742968cde47cb918ada2680e8d3412017-07-01T00:00:00Zhttps://doi.org/10.1038/s41598-017-06314-9https://doaj.org/toc/2045-2322Abstract Various forms of protein (proteoforms) are generated by genetic variations, alternative splicing, alternative translation initiation, co- or post-translational modification and proteolysis. Different proteoforms are in part discovered by characterizing their N-terminal sequences. Here, we introduce an N-terminal-peptide-enrichment method, Nrich. Filter-aided negative selection formed the basis for the use of two N-blocking reagents and two endoproteases in this method. We identified 6,525 acetylated (or partially acetylated) and 6,570 free protein N-termini arising from 5,727 proteins in HEK293T human cells. The protein N-termini included translation initiation sites annotated in the UniProtKB database, putative alternative translational initiation sites, and N-terminal sites exposed after signal/transit/pro-peptide removal or unknown processing, revealing various proteoforms in cells. In addition, 46 novel protein N-termini were identified in 5′ untranslated region (UTR) sequence with pseudo start codons. Our data showing the observation of N-terminal sequences of mature proteins constitutes a useful resource that may provide information for a better understanding of various proteoforms in cells.Jeonghun YeomShinyeong JuYunJin ChoiEunok PaekCheolju LeeNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 7, Iss 1, Pp 1-13 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Jeonghun Yeom Shinyeong Ju YunJin Choi Eunok Paek Cheolju Lee Comprehensive analysis of human protein N-termini enables assessment of various protein forms
description	Abstract Various forms of protein (proteoforms) are generated by genetic variations, alternative splicing, alternative translation initiation, co- or post-translational modification and proteolysis. Different proteoforms are in part discovered by characterizing their N-terminal sequences. Here, we introduce an N-terminal-peptide-enrichment method, Nrich. Filter-aided negative selection formed the basis for the use of two N-blocking reagents and two endoproteases in this method. We identified 6,525 acetylated (or partially acetylated) and 6,570 free protein N-termini arising from 5,727 proteins in HEK293T human cells. The protein N-termini included translation initiation sites annotated in the UniProtKB database, putative alternative translational initiation sites, and N-terminal sites exposed after signal/transit/pro-peptide removal or unknown processing, revealing various proteoforms in cells. In addition, 46 novel protein N-termini were identified in 5′ untranslated region (UTR) sequence with pseudo start codons. Our data showing the observation of N-terminal sequences of mature proteins constitutes a useful resource that may provide information for a better understanding of various proteoforms in cells.
format	article
author	Jeonghun Yeom Shinyeong Ju YunJin Choi Eunok Paek Cheolju Lee
author_facet	Jeonghun Yeom Shinyeong Ju YunJin Choi Eunok Paek Cheolju Lee
author_sort	Jeonghun Yeom
title	Comprehensive analysis of human protein N-termini enables assessment of various protein forms
title_short	Comprehensive analysis of human protein N-termini enables assessment of various protein forms
title_full	Comprehensive analysis of human protein N-termini enables assessment of various protein forms
title_fullStr	Comprehensive analysis of human protein N-termini enables assessment of various protein forms
title_full_unstemmed	Comprehensive analysis of human protein N-termini enables assessment of various protein forms
title_sort	comprehensive analysis of human protein n-termini enables assessment of various protein forms
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/b48742968cde47cb918ada2680e8d341
work_keys_str_mv	AT jeonghunyeom comprehensiveanalysisofhumanproteinnterminienablesassessmentofvariousproteinforms AT shinyeongju comprehensiveanalysisofhumanproteinnterminienablesassessmentofvariousproteinforms AT yunjinchoi comprehensiveanalysisofhumanproteinnterminienablesassessmentofvariousproteinforms AT eunokpaek comprehensiveanalysisofhumanproteinnterminienablesassessmentofvariousproteinforms AT cheoljulee comprehensiveanalysisofhumanproteinnterminienablesassessmentofvariousproteinforms
_version_	1718388726771482624

Comprehensive analysis of human protein N-termini enables assessment of various protein forms

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