http://purl.uniprot.org/citations/37219487 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/37219487 | http://www.w3.org/2000/01/rdf-schema#comment | "Phosphorylation is a ubiquitous post-translation modification that regulates protein function by promoting, inhibiting or modulating protein-protein interactions. Hundreds of thousands of phosphosites have been identified but the vast majority have not been functionally characterised and it remains a challenge to decipher phosphorylation events modulating interactions. We generated a phosphomimetic proteomic peptide-phage display library to screen for phosphosites that modulate short linear motif-based interactions. The peptidome covers ~13,500 phospho-serine/threonine sites found in the intrinsically disordered regions of the human proteome. Each phosphosite is represented as wild-type and phosphomimetic variant. We screened 71 protein domains to identify 248 phosphosites that modulate motif-mediated interactions. Affinity measurements confirmed the phospho-modulation of 14 out of 18 tested interactions. We performed a detailed follow-up on a phospho-dependent interaction between clathrin and the mitotic spindle protein hepatoma-upregulated protein (HURP), demonstrating the essentiality of the phospho-dependency to the mitotic function of HURP. Structural characterisation of the clathrin-HURP complex elucidated the molecular basis for the phospho-dependency. Our work showcases the power of phosphomimetic ProP-PD to discover novel phospho-modulated interactions required for cellular function."xsd:string |
http://purl.uniprot.org/citations/37219487 | http://purl.org/dc/terms/identifier | "doi:10.15252/msb.202211164"xsd:string |
http://purl.uniprot.org/citations/37219487 | http://purl.uniprot.org/core/author | "Nilsson J."xsd:string |
http://purl.uniprot.org/citations/37219487 | http://purl.uniprot.org/core/author | "Dobritzsch D."xsd:string |
http://purl.uniprot.org/citations/37219487 | http://purl.uniprot.org/core/author | "Ivarsson Y."xsd:string |
http://purl.uniprot.org/citations/37219487 | http://purl.uniprot.org/core/author | "Kliche J."xsd:string |
http://purl.uniprot.org/citations/37219487 | http://purl.uniprot.org/core/author | "Davey N.E."xsd:string |
http://purl.uniprot.org/citations/37219487 | http://purl.uniprot.org/core/author | "Simonetti L."xsd:string |
http://purl.uniprot.org/citations/37219487 | http://purl.uniprot.org/core/author | "Garvanska D.H."xsd:string |
http://purl.uniprot.org/citations/37219487 | http://purl.uniprot.org/core/author | "Badgujar D."xsd:string |
http://purl.uniprot.org/citations/37219487 | http://purl.uniprot.org/core/date | "2023"xsd:gYear |
http://purl.uniprot.org/citations/37219487 | http://purl.uniprot.org/core/name | "Mol Syst Biol"xsd:string |
http://purl.uniprot.org/citations/37219487 | http://purl.uniprot.org/core/pages | "e11164"xsd:string |
http://purl.uniprot.org/citations/37219487 | http://purl.uniprot.org/core/title | "Large-scale phosphomimetic screening identifies phospho-modulated motif-based protein interactions."xsd:string |
http://purl.uniprot.org/citations/37219487 | http://purl.uniprot.org/core/volume | "19"xsd:string |
http://purl.uniprot.org/citations/37219487 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/37219487 |
http://purl.uniprot.org/citations/37219487 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/37219487 |
http://purl.uniprot.org/uniprot/#_Q15398-mappedCitation-37219487 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/37219487 |
http://purl.uniprot.org/uniprot/#_Q00610-mappedCitation-37219487 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/37219487 |
http://purl.uniprot.org/uniprot/Q00610 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/37219487 |
http://purl.uniprot.org/uniprot/Q15398 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/37219487 |