{"database":"iProX","file_versions":[],"scores":null,"additional":{"omics_type":["Proteomics"],"submitter":["Han Wei"],"species":["Homo Sapiens"],"full_dataset_link":["http://www.iprox.org/page/project.html?id=IPX0017330000"],"submitter_email":["weihan548@126.com"],"submitter_affiliation":["Zhengzhou University"],"sample_protocol":[""],"repository":["iProX"],"data_protocol":[""],"additional_accession":[]},"is_claimable":false,"name":"Chemoproteomic profiling of SGPP-binding proteins","description":"S-guanylation is an endogenous post translational modification that has been implicated as a specific autophagic signal, yet its molecular mechanism and the identity of its binding proteins remain largely unknown. Here, we developed the first diazirine based photoaffinity probe for S-guanylation (SGPP) to capture and identify its interacting proteins in living cells. The SGPP efficiently labeled target proteins in a time , concentration , and UV crosslinking dependent manner, as demonstrated by in gel fluorescence scanning. Competitive labeling with excess FBnG, a known AUTAC warhead, confirmed the specificity of the probe. Using a chemoproteomic workflow combining SGPP mediated photocrosslinking, affinity enrichment, and mass spectrometry, we identified candidate binding proteins in HeLa cells","dates":{"publication":"Thu May 21 00:00:00 BST 2026"},"accession":"PXD078661","cross_references":{"TAXONOMY":["9606"]}}