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Chang"],"software":[""],"tissue":["Cell Suspension Culture","Epithelial Cell","Cell Culture"],"sample_protocol":["HeLa cells were either untreated, stimulated with serum and pervanadate or with epidermal growth factor. A timecourse was carried out for EGF treatment such that HeLa cells were starved for 6 hours then treated with 160 ng/mL EGF for 1 min, 3 min, 5 min, or 15 min. Samples were prepared with denaturing lysis, insolution digest with trypsin, and cartridge desalting. Dried peptides were subjected to phosphotyrosine peptide enrichment using the Halo-Src SH2 superbinder fusion protein introduced in this paper. Peptides from enrichment were cleaned up with a iron (III) immobilized metal affinity enrichment prior to measurement by data dependent acquisition on an Orbitrap Exploris 480 hooked up to an Easy nLC II liquid chromatography instrument. Measurements of total proteome and global phosphoproteome were performed in addition to tyrosine phosphoproteome for the EGF stimulation timecourse. Other experiments in this study evaluated impacts of different enrichment bead types, peptide input amounts, peptide concentration, and conjugated bead shelf life."],"repository":["Pride"],"labhead":["Judit Villen"],"instrument_platform":[""],"labhead_affiliation":["Department of Genome Sciences; Villen Lab; University of Washington; United States"],"submission_type":["COMPLETE"],"publication":["10.1038/S44318-026-00843-8"],"submitter_affiliation":["University of Washington"],"labhead_mail":["jvillen@uw.edu"],"technology_type":["Data-dependent acquisition","Mass Spectrometry","Bottom-up proteomics"],"disease":["Cervix Carcinoma","Disease Free"],"submitter_keywords":["Hela","Enrichment","High-throughput","Automated","Egf","Phosphotyrosine","Lc-ms/ms"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD062515"],"quantification_method":[""],"modification":[""],"data_protocol":["DDA-MS/MS spectra were searched with Comet (2019.01.2 52) against the human proteome downloaded from Uniprot.org on March 21st, 2024 including only reviewed entries and excluding isoforms (20,418 entries). The yeast samples were searched against the S. cerevisiae proteome downloaded from Uniprot on February 19th, 2021 with the yeast vSrc kinase sequence appended. Peptides were searched with trypsin digestion allowing up to two missed cleavages. The precursor m/z tolerance was set to 20 ppm. The fragment m/z mass tolerance was set to 0.02 Da. Constant modification of cysteine carbamidomethylation (57.02146372118 Da) and variable modification of methionine oxidation (15.9949146202 Da, max 2), and N-terminal acetylation (42.01056468472, max 1) were used for all searches. An additional variable modification of serine, threonine, and tyrosine phosphorylation (79.966331 Da, max 3) was used for global and tyrosine-specific phosphopeptide samples. Search results were filtered to a 1% FDR at PSM level using Percolator. Phosphorylation sites were localized using an in-house implementation of the Ascore algorithm. Phosphorylation sites with an Ascore ≥ 13 (P ≤ 0.05) were considered confidently localized. Peptides were quantified using in-house software measuring chromatographic peak maximum intensities."],"omics_type":["Proteomics"],"species":["Homo Sapiens (human)","Saccharomyces Cerevisiae (baker's Yeast)","Saccharomyces Cerevisiae"],"submitter_mail":["alexisn1@uw.edu"],"submitter_country":["United States"],"doi":["10.6019/PXD062515"],"additional_accession":[]},"is_claimable":false,"name":"Scalable Phosphotyrosine Enrichment with SH2 Superbinder Enables Deep Profiling of EGF Responses","description":"Phosphotyrosine signaling plays a critical role in many biological processes, from cell proliferation to immune response. Despite its importance, proteomic studies of tyrosine phosphorylation have been limited in scale and throughput by costly reagents and labor-intensive protocols. To address this, we developed R2HaPpY, a phosphotyrosine enrichment method combining simplified superbinder reagent preparation and automated high-throughput enrichment. Our new reagent binds phosphotyrosine peptides at higher efficiency than existing enrichment reagents and reduces both cost and preparation time by 20-fold. We generalized R2HaPpY to samples of low and high phosphotyrosine levels, and benchmarked it on EGF signaling dynamics in HeLa cells. Using only ~1 mg of input peptides, we quantify 1,651 unique phosphotyrosine sites, including 878 regulated phosphotyrosine sites, many novel or not previously annotated as EGF-responsive. Our results reveal differential temporal regulation and represent the largest phosphotyrosine dataset of EGF stimulation response to date. This streamlined, cost-effective, and sensitive method enables quantitative mapping of tyrosine phosphorylation dynamics at the scale of hundreds of samples, facilitating integration of phosphotyrosine signaling into multiomic studies across diverse biological systems.","dates":{"publication":"2026-07-03","submission":"2025-04-02"},"accession":"PXD062515","cross_references":{"TAXONOMY":["NEWT:68239","NEWT:108018","NEWT:377960","NEWT:1131","NEWT:2042546","NEWT:295546","NEWT:258594","NEWT:1126","NEWT:1129","NEWT:309807","NEWT:89184","NEWT:309800","NEWT:1323429","NEWT:876138","NEWT:44271","NEWT:193516","NEWT:2315688","NEWT:592321","NEWT:1073882","NEWT:6819","NEWT:428386","NEWT:1117","NEWT:498257","NEWT:10036","NEWT:32264","NEWT:10034","NEWT:661410","NEWT:224326","NEWT:376619","NEWT:3765","NEWT:3767","NEWT:433727","NEWT:135622","NEWT:672127","NEWT:656061","NEWT:37965","NEWT:656064","NEWT:3760","NEWT:36630","NEWT:381198","NEWT:418106","NEWT:10029","NEWT:913645","NEWT:2492962","NEWT:641809","NEWT:44250","NEWT:317447","NEWT:5530","NEWT:868565","NEWT:135674","NEWT:1562698","NEWT:12637","NEWT:2164133","NEWT:2767846","NEWT:314344","NEWT:108061","NEWT:224308","NEWT:49928","NEWT:160621","NEWT:110368","NEWT:1916073","NEWT:1310161","NEWT:1230383","NEWT:77133","NEWT:1310165","NEWT:114727","NEWT:5516","NEWT:498211","NEWT:347256","NEWT:5518","NEWT:398007","NEWT:1527468","NEWT:498217","NEWT:498216","NEWT:11320","NEWT:1310173","NEWT:161934","NEWT:156587","NEWT:1148","NEWT:5508","NEWT:419481","NEWT:5507","NEWT:1140","NCBITaxon:2157","NEWT:2066563","NEWT:1143","NEWT:1462472","NEWT:1336795","NEWT:644042","NEWT:709964","NEWT:3712","NEWT:3711","NEWT:3714","NEWT:3715","NEWT:2065263","NEWT:1549675","NEWT:177437","NEWT:9014","NEWT:10891","NEWT:226126","NEWT:1616117","NEWT:34865","NEWT:28174","NEWT:550537","NEWT:284812","NEWT:3701","NEWT:3702","NEWT:1245466","NEWT:3704","NEWT:1246791","NEWT:9005","NEWT:34871","NEWT:9006","NEWT:33548","NEWT:1883426","NEWT:657321","NEWT:10886","NEWT:3708","NEWT:536231","NEWT:219813","NEWT:215451","NEWT:460519","NEWT:272844","NEWT:1348799","NEWT:55784","NEWT:485","NEWT:2709072","NEWT:2499525","NEWT:142786","NEWT:2853422","NEWT:487","NEWT:1679718","NEWT:480","NEWT:67767","NEWT:46835","NEWT:216778","NEWT:376686","NEWT:237610","EFO:0001352","NEWT:219809","NEWT:219808","NEWT:119562","NEWT:1883446","NEWT:1233435","NEWT:118223","NEWT:141469","NEWT:987059","NEWT:491","NEWT:460523","NEWT:85694","NEWT:85692","NEWT:3750","NEWT:291146","NEWT:3745","NEWT:1715989","NCBITaxon:4751","NEWT:3747","NEWT:278161","NEWT:415978","NEWT:410289","NEWT:191701","NEWT:9054","NEWT:472","NEWT:29459","NEWT:1380096","NEWT:28128","NEWT:470","NEWT:41122","NEWT:1328300","NEWT:748693","NCBITaxon:50557","NEWT:3735","NEWT:29491","NEWT:911022","NEWT:446","NEWT:153481","NEWT:445","NEWT:2003758","NEWT:63366","NEWT:63367","NEWT:29488","NEWT:215402","NEWT:3726","NEWT:30455","NEWT:28141","NEWT:9030","NEWT:9031","NEWT:3728","NEWT:108931","NEWT:219799","NEWT:219798","NEWT:548","NEWT:150475","NEWT:256737","NEWT:51350","NEWT:8694","NEWT:8692","NEWT:542","NEWT:394503","NEWT:13076","NEWT:219785","NEWT:451515","NEWT:8673","NEWT:550","NEWT:10804","NEWT:554","NEWT:451516","NEWT:552","NEWT:1325291","NEWT:42410","NEWT:1225786","NEWT:771870","NEWT:8665","NEWT:51338","NEWT:9995","NEWT:28112","NEWT:49012","NEWT:28110","NEWT:10832","NEWT:507601","NEWT:520","NEWT:64657","NEWT:186441","NEWT:2585209","NEWT:643680","NEWT:214092","NEWT:40697","NEWT:13095","NEWT:162425","NEWT:242124","NEWT:9986","NEWT:8654","NEWT:8658","NEWT:1268063","NEWT:8657","NEWT:9983","NEWT:8655","NEWT:595495","NEWT:80833","NEWT:479096","NEWT:28108","NEWT:28104","NEWT:1114957","NEWT:568703","NEWT:568708","NEWT:52641","NEWT:353152","NEWT:353153","NEWT:227377","NEWT:1774284","NEWT:27689","NEWT:207769","NEWT:40674","NEWT:51329","NCBITaxon:1763","NEWT:443906","NEWT:13037","NEWT:519","NEWT:7394","NEWT:6063","NEWT:404330","NEWT:1328388","NEWT:300641","NEWT:39655","NEWT:38323","NEWT:206411","NEWT:80869","NEWT:214053","NEWT:80863","NEWT:665890","NEWT:52639","NEWT:52638","NEWT:8697","NEWT:861109","NEWT:8695","NEWT:1196866","NEWT:510516","NEWT:1045775","NEWT:1123869","NCBITaxon:1335626","NEWT:7370","NEWT:83906","NEWT:99488","NEWT:1134506","NEWT:255470","NEWT:27697","NEWT:86185","NEWT:9935","NEWT:287889","NEWT:1028307","NEWT:52603","NEWT:92867","NEWT:92866","NEWT:1344414","NEWT:202950","NEWT:741158","NEWT:1293091","NEWT:202956","NEWT:315750","NEWT:632957","NEWT:9925","NCBITaxon:9606","NEWT:1436183","NEWT:4232","NEWT:9922","NEWT:416348","NEWT:105812","NEWT:11298","NEWT:4236","NEWT:398031","NEWT:196627","NEWT:523840","NEWT:1076878","NEWT:200308","NEWT:200302","NEWT:9913","NEWT:9915","NEWT:105841","NEWT:1170227","NEWT:2666255","NEWT:999810","NEWT:28995","NEWT:1392998","NEWT:1150621","NEWT:1085791","NEWT:745531","NEWT:226900","NEWT:231490","NEWT:590651","NEWT:449239","NEWT:244704","NEWT:9909","NEWT:9902","NEWT:430615","NEWT:563041","NEWT:36599","NEWT:41949","NEWT:9900","NEWT:326423","NEWT:326424","NEWT:13013","NEWT:749906","NEWT:418985","NEWT:749907","NEWT:431947","NEWT:142809","NEWT:1095183","NEWT:302409","NEWT:9979","NEWT:130821","NEWT:2320211","NEWT:27606","NEWT:290610","NEWT:1519788","NEWT:59202","NEWT:9975","NEWT:8643","NEWT:1801631","NEWT:1159899","NEWT:502780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