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LysargiNase coupled with trypsin digestion enhanced the identification of protein ubiquitination sites

ABSTRACT: We used LysargiNase to enhance the identification of ubiquitinated sites

ORGANISM(S): Saccharomyces Cerevisiae

SUBMITTER: Ping Xu

PROVIDER: PXD009060 | iProX | Wed Jul 18 00:00:00 BST 2018

REPOSITORIES: iProX

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The Ubiquitin Interacting Motif-Like Domain of Met4 Selectively Binds K48 Polyubiquitin Chains.

Villamil Mark M Xiao Weidi W Yu Clinton C Huang Lan L Xu Ping P Kaiser Peter P

Molecular & cellular proteomics : MCP 20211109 1

Protein ubiquitylation is an important posttranslational modification that governs most cellular processes. Signaling functions of ubiquitylation are very diverse and involve proteolytic as well as nonproteolytic events, such as localization, regulation of protein interactions, and control of protein activity. The intricacy of ubiquitin signaling is further complicated by several different polyubiquitin chain types that are likely recognized and interpreted by different protein readers. For exam ...[more]

PMID: 34763062

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