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Fiedler, Rashna Bhandari"],"species":["Homo Sapiens (human)"],"full_dataset_link":["https://repository.jpostdb.org/entry/JPST001934"],"submitter_affiliation":["Leibniz Institut für Molekulare Pharmakologie, Berlin"],"sample_protocol":[""],"repository":["jPOST"],"data_protocol":[""],"name_synonyms":["dTAF[[II]]230, TAF[[II]]250, d230, human being, protein complex, Modern, Proteins, TAF200, Gene, l(3)84Ab, dTAFII250, protein, BG:DS00004.13, TAFII-250, protein-containing complex, TAF250/230, EfW1, Cell, Human, dTAF230, dmTAF[[II]]230, TAFII250, native protein, Homo sapiens, dmTAF1, Taf230, p230, Protein, Gene Products, TAF[[II]]250/230, TFIID, protein aggregate, Man, TAF250, Taf[[II]]250, Taf200, dTAF[[II]]250, TAF[[II]]230, Man (Taxonomy), TFIID TAF250, cel, cell, Taf1p, TAF[II]250, CG17603, TAF[[II]], human, Protein Gene Products, Gene Proteins, dTAF250, DmelCG17603, TAF1., Taf250, SR3-5, Modern Man, TAF, TAF230"],"description_synonyms":["AA408847, Dambose, Progress Reports, protein, AW209012, phosphorylation, dmTAF[[II]]230, Meat sugar, Techniques, Mesoinositol, i-inositol, NOR-90, Method, Summary Report, Nucleolar Protein, Line, 1, 2, 3, 4, 5, Work Flow, protein aggregate, Summary Reports, WMS, multicellular organismal biosynthetic process, D-myo-Inositol, inosite, single-organism biosynthetic process, Nuclear Protein, Man (Taxonomy), TFIID TAF250, Progress Report, cel, anabolism, L-myo-Inositol, hypoplasia, Predictions and Projections., Futurology, 2R, Progress, Field Reports, AA408077, Methodological Studies, UBF-1, GPHYSD2, transcription from bacterial-type RNA polymerase promoter, single organism signaling, SGS, 3S, dTAF[[II]]230, (1r, Data Set, 6S)-cyclohexane-1, Modern, TAF200, cis-1, Tcfubf, TAFII-250, Procedure, TAF250/230, mKIAA0035, ACMICD, 6-hexol, Workflows, TAFII250, Investigative Report, NOPP130, 5R, 4s, Lines, Nopp140, 1L-myo-Inositol, 1D-myo-Inositol, TCS1, NOPP140, Field, MASS, Methodological, CG17603, 5/4, TAF[[II]], Methodological Study, rRNA gene, human, 3230402K17Rik, Report, meso-Inositol, Taf250, SR3-5, bacterial transcription, Cells, 6-HEXAHYDROXY-CYCLOHEXANE, Work Flows, TAF230, Eukaryotic, d230, human being, 6-cyclohexanehexol, bioformation, Procedures, Peptidomics, myo-inositol, FBN, Gene, dTAFII250, protein-containing complex, EfW1, Human, protein amino acid phosphorylation, NS5ATP13, method, Investigative, Homo sapiens, reduced, dmTAF1, ECTOL1, Taf230, method used in an experiment, Gene Products, AU046071, Studies, Projections and Predictions, tiny, Man, Technique, TAF250, Cyclohexitol, Chiro Inositol, Taf200, dTAF[[II]]250, cell, Taf1p, myo-Inositol, UBF, OCTD, Study, dTAF250, Bios I, rDNA, Investigative Reports, TAF, small, TAF[[II]]250, protein complex, Proteins, Phosphorylations, 5-trans-4, Cell Lines, l(3)84Ab, BG:DS00004.13, Cell, dTAF230, Inositol, native protein, inositol, p230, Research Reports, Protein, TAF[[II]]250/230, TFIID, MFS1, Nuclear, background, WMS2, Taf[[II]]250, TCS, TAF[[II]]230, Ribosomal DNA, underdeveloped, Ins, Chiro-Inositol, Myoinositol, TAF[II]250, Nucleolar Proteins, treacle, P130, AA536818, UBF2, introduction, UBF1, Protein Gene Products, plan specification, Eukaryotic Cell, Gene Proteins, MFD1, inositols, DmelCG17603, signalling process, Reports, Modern Man, A930005G04Rik, SSKS, Summary, Nucleolar, Future, Field Report, TAF1"],"additional_accession":[]},"is_claimable":false,"name":"Pyrophosphoproteomics: extensive protein pyrophosphorylation revealed in human cell lines","description":"Reversible protein phosphorylation is a central signaling mechanism in eukaryotic cells. While the identification of canonical phosphorylation sites using mass-spectrometry (MS) based proteomics has become routine, annotation of non-canonical phosphorylation has remained a challenge. Here, we report a tailored pyrophosphoproteomics workflow to detect and reliably assign protein pyrophosphorylation in two human cell lines, providing the first direct evidence of endogenous protein pyrophosphorylation. Detection of protein pyrophosphorylation was reproducible, specific and consistent with previous biochemical evidence relating the installation of the modification to inositol pyrophosphates (PP-InsPs). We manually validated 148 pyrophosphosites across 71 human proteins, the most heavily pyrophosphorylated of which were the nucleolar proteins NOLC1 and TCOF1. A predictive workflow based on the MS data set was established to recognize putative pyrophosphorylation sequences, and UBF1, a nucleolar protein incompatible with the proteomics method, was biochemically shown to undergo pyrophosphorylation. When the biosynthesis of PP-InsPs was perturbed in a model cell line, proteins expressed in this background exhibited lower levels of pyrophosphorylation. Disruption of PP-InsP biosynthesis also significantly reduced rDNA transcription, potentially by lowering pyrophosphorylation on regulatory proteins NOLC1, TCOF1, and UBF1. Overall, protein pyrophosphorylation emerges as an archetype of non-canonical phosphorylation, and should be considered in future phosphoproteomic analyses.","dates":{"publication":"Tue Mar 12 00:00:00 GMT 2024"},"accession":"PXD038963","cross_references":{"TAXONOMY":["9606"]}}