{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD077030/proteinGroups.txt","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD077030/checksum.txt"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD077030/P001824_DIA_mycBioID2_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD077030/P001758_gamma_R1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD077030/P001758_mycBioID2_R2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD077030/P001758_alpha_R3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD077030/P001824_DIA_gamma_2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD077030/P001824_DIA_beta_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD077030/P001758_gamma_R2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD077030/P001824_DIA_mycBioID2_4.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD077030/P001758_mycBioID2_R3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD077030/P001758_alpha_R2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD077030/P001824_DIA_alpha_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD077030/P001824_DIA_gamma_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD077030/P001824_DIA_mycBioID2_3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD077030/P001758_gamma_R3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD077030/P001824_DIA_alpha_2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD077030/P001824_DIA_beta_3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD077030/P001758_beta_3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD077030/P001758_alpha_R1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD077030/P001824_DIA_mycBioID2_2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD077030/P001824_DIA_beta_2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD077030/P001824_DIA_alpha_3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD077030/P001824_DIA_gamma_4.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD077030/P001758_mycBioID2_R1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD077030/P001758_beta_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD077030/P001758_beta_2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD077030/P001824_DIA_gamma_3.raw"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["bemerling@sbpdiscovery.org"],"submitter":["Rabi Murad"],"technology_type":["Data-dependent acquisition","Mass Spectrometry","Data-independent acquisition"],"software":[""],"submitter_keywords":["Bioid","Hela","Pi5p4ks"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD077030"],"tissue":["Epithelial Cell"],"sample_protocol":["Pellet was dissolved in 8M urea, 50 mM ammonium bicarbonate (ABC) and benzonase and the solution was centrifuged at 14,000 x g for 15 minutes to remove cellular debris. Supernatant protein concentration was determined using a bicinchoninic acid (BCA) protein assay (Thermo Scientific). Disulfide bridges were reduced with 5 mM tris(2-carboxyethyl)phosphine (TCEP) at 30°C for 60 min, and cysteines were subsequently alkylated with 15 mM iodoacetamide (IAA) in the dark at room temperature for 30 min.  Affinity purification was carried out in a Bravo AssayMap platform (Agilent) using AssayMap streptavidin cartridges (Agilent). Briefly, cartridges were first primed with 50 mM ammonium bicarbonate, and then proteins were slowly loaded onto the streptavidin cartridge. Background contamination was removed with 8M urea, 50 mM ammonium bicarbonate. Finally, cartridges were washed with Rapid digestion buffer (Promega, Rapid digestion buffer kit) and proteins were subjected to on-cartridge digestion with mass spec grade Trypsin/Lys-C Rapid digestion enzyme (Promega, Madison, WI) at 70C for 1h. Digested peptides were then desalted in the Bravo platform using AssayMap C18 cartridges, and dried down in a SpeedVac concentrator.  Prior to LC-MS/MS analysis, dried peptides were reconstituted with 2% ACN, 0.1% FA and concentration was determined using a NanoDropTM spectrophometer (ThermoFisher). Samples were then analyzed by LC-MS/MS using a Proxeon EASY-nanoLC system (ThermoFisher) coupled to a Orbitrap Fusion Lumos Tribid mass spectrometer (Thermo Fisher Scientific). Peptides were separated using an analytical C18 Aurora column (75µm x 250 mm, 1.6 µm particles; IonOpticks) at a flow rate of 300 nL/min (60C) using a 75-min gradient: 2% to 6% B in 1 min, 6% to 23% B in 45 min, 23% to 34% B in 28 min, and 34% to 48% B in 1 min (A= FA 0.1%; B=80% ACN: 0.1% FA). The mass spectrometer was operated in positive data-dependent acquisition mode. MS1 spectra were measured in the Orbitrap in a mass-to-charge (m/z) of 375 – 1500 with a resolution of 60,000. Automatic gain control target was set to 4 x 10^5 with a maximum injection time of 50 ms. The instrument was set to run in top speed mode with 1-second cycles for the survey and the MS/MS scans. After a survey scan, the most abundant precursors (with charge state between +2 and +7) were isolated in the quadrupole with an isolation window of 0.7 m/z and fragmented with HCD at 30% normalized collision energy. Fragmented precursors were detected in the ion trap as rapid scan mode with automatic gain control target set to 1 x 10^4 and a maximum injection time set at 35 ms. The dynamic exclusion was set to 20 seconds with a 10 ppm mass tolerance around the precursor."],"repository":["pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["All mass spectra from were analyzed with MaxQuant software version 2.4.10.0 MS/MS spectra were searched against the Homo sapiens Uniprot protein sequence database (downloaded in Mar 2022), and GPM cRAP sequences (commonly known protein contaminants). Precursor mass tolerance was set to 20ppm and 4.5ppm for the first search where initial mass recalibration was completed and for the main search, respectively. Product ions were searched with a mass tolerance 0.5 Da. The maximum precursor ion charge state used for searching was 7. Carbamidomethylation of cysteine was searched as a fixed modification, while oxidation of methionine and acetylation of protein N-terminal were searched as variable modifications. Enzyme was set to trypsin in a specific mode and a maximum of two missed cleavages was allowed for searching. The target-decoy-based false discovery rate (FDR) filter for spectrum and protein identification was set to 1%.  Protein identification results were further processed using the Perseus software suite version 2.0.9.0 (https://www.nature.com/articles/s44161-023-00294-y#ref-CR62)."],"omics_type":["Proteomics"],"labhead":["Brooke Emerling"],"instrument_platform":[""],"submission_type":["PARTIAL"],"labhead_affiliation":["Cancer Metabolism and Microenvironment Program, NCI-Designated Cancer Center, Sanford Burnham Prebys Medical Discovery Institute"],"species":["Homo Sapiens (human)"],"publication":["10.1016/J.JBC.2026.113071"],"submitter_mail":["rmurad.geo03@gmail.com"],"submitter_affiliation":["Sanford Burnham Prebys Medical Discovery Institute"],"submitter_country":["United States"],"additional_accession":[]},"is_claimable":false,"name":"A proximity-labeling map of PI5P4K phosphoinositide kinases interaction networks","description":"Phosphatidylinositol-5-phosphate 4-kinases (PI5P4Ks) have emerged as candidate drug targets in cancer, neurological, inflammatory, and infectious diseases. Although their canonical function is to phosphorylate PI(5)P to generate PI(4,5)P2, growing evidence points to additional catalytic-independent roles, but how these functions are organized within protein interaction networks remains unclear. Here, we use proximity-dependent biotin identification (BioID) in HeLa cells to map isoform-resolved interactomes of human PI5P4Kα, PI5P4Kβ, and PI5P4Kγ. This approach captures PI5P4K-proximal proteins in intact cells and reveals interaction networks positioning these kinases within trafficking-associated signaling modules. Importantly, BioID analysis indicates that PI5P4Kγ has the most extensive set of proximal interactors among the three PI5P4Ks, consistent with its comparatively low catalytic activity and a prominent scaffold-like function. Among PI5P4Kγ-enriched partners, we highlight the endosomal cargo adaptor SNX17 as a proximal interactor that links PI5P4Kγ to β1-integrin recycling and to cell migration and invasion. By providing a proximity map for all three PI5P4Ks, this study offers a framework to help define contexts in which targeted protein degradation may offer advantages over catalytic inhibition and provides a resource for future mechanistic studies on these phosphoinositide kinases.","dates":{"publication":"2026-05-05","submission":"2026-04-11"},"accession":"PXD077030","cross_references":{"TAXONOMY":["NEWT:330879","NEWT:377960","NEWT:2042546","NEWT:259447","NEWT:295546","NCBITaxon:2719036","NEWT:625351","NCBITaxon:1280","NEWT:112503","NEWT:1129","NEWT:309807","NEWT:59753","NEWT:89184","NEWT:309800","NEWT:281395","NEWT:1211601","NEWT:876138","NEWT:44271","NEWT:193516","NEWT:1073882","NEWT:6819","NEWT:475174","NEWT:1117","NEWT:498257","NEWT:10036","NEWT:1590","NEWT:10034","NEWT:661410","NEWT:638632","NEWT:224326","NEWT:376619","NCBITaxon:79857","NEWT:1096976","NEWT:3765","NEWT:1589","NEWT:135622","NEWT:35786","NEWT:1580","NEWT:399784","NEWT:96731","NEWT:656064","NEWT:1582","NEWT:36630","NEWT:383379","NEWT:418106","NCBITaxon:12721","NEWT:10029","NEWT:913645","NEWT:641809","NEWT:1392488","NEWT:38815","NEWT:317447","NEWT:4688","NEWT:7719","NEWT:868565","NEWT:135674","NEWT:79329","NEWT:30069","NEWT:12637","NEWT:59729","NEWT:2164133","NEWT:295105","NEWT:108061","NEWT:60711","NEWT:224308","NEWT:3347","NEWT:160621","NEWT:212790","NEWT:110368","NEWT:1310161","NEWT:77133","NEWT:145481","NEWT:1310165","NEWT:29058","NCBITaxon:79824","NEWT:410658","NEWT:44688","NEWT:44689","NEWT:498211","NEWT:347256","NEWT:5518","NEWT:398007","NEWT:1527468","NEWT:498217","NEWT:498216","NEWT:11320","NEWT:246196","NEWT:246197","NEWT:145458","NEWT:44685","NEWT:161934","NEWT:1148","NEWT:5508","NEWT:3329","NEWT:419481","NEWT:5507","NEWT:410661","NEWT:1140","NCBITaxon:2157","NEWT:1143","NEWT:1287689","NEWT:1094343","NEWT:1462472","NEWT:1336795","NEWT:644042","NEWT:150808","NEWT:1182590","NEWT:3712","NEWT:3711","NEWT:3714","NEWT:270643","NEWT:2065263","NEWT:177437","NEWT:10418","NEWT:118698","NEWT:1616117","NEWT:118696","NEWT:34865","NEWT:52283","NEWT:28174","NEWT:284812","NEWT:8175","NEWT:43330","NEWT:1603293","NEWT:44664","NEWT:43346","NEWT:3702","NEWT:1245466","NEWT:3704","NEWT:244366","NEWT:1246791","NEWT:176597","NEWT:118694","NEWT:2850","NEWT:118691","NEWT:34871","NEWT:33548","NEWT:52299","NEWT:8165","NEWT:96794","NEWT:3708","NEWT:332648","NEWT:44670","NEWT:536231","NEWT:376219","NEWT:219813","NEWT:1510","NEWT:460519","NEWT:1515","NEWT:572307","NEWT:1432138","NEWT:1424507","NEWT:1194599","NEWT:272844","NEWT:1348799","NEWT:33995","NEWT:55784","NEWT:1303443","NEWT:9483","NEWT:485","NEWT:56636","NEWT:2499525","NEWT:2853422","NEWT:487","NEWT:1538553","NEWT:1679718","NEWT:480","NEWT:67767","NEWT:46835","NEWT:109757","NEWT:582580","NEWT:1185650","NEWT:216778","NEWT:1502","NEWT:128017","NEWT:376686","NEWT:237610","NEWT:95486","NEWT:1883446","NEWT:1233435","NEWT:118223","NEWT:11757","NEWT:109760","NEWT:29031","NEWT:317047","NEWT:491","NEWT:460523","NEWT:45954","NEWT:235443","NEWT:1757312","NEWT:85694","NEWT:109786","NEWT:108458","NEWT:5936","NEWT:320637","NEWT:1078283","NEWT:3750","NEWT:983964","NEWT:11706","NEWT:32644","NEWT:527796","NEWT:499175","NEWT:109779","NEWT:3745","NEWT:1715989","NCBITaxon:4751","NEWT:3747","NEWT:1116234","NEWT:1255228","NEWT:410289","NEWT:373153","NEWT:1640278","NEWT:472","NEWT:940825","NEWT:529507","NEWT:1071661","NEWT:28128","NEWT:470","NEWT:5911","NEWT:748693","NCBITaxon:50557","NEWT:39251","NEWT:29491","NEWT:101841","NEWT:446","NEWT:153481","NEWT:2014887","NEWT:33952","NEWT:445","NEWT:153009","NEWT:261756","NEWT:166313","NEWT:63366","NEWT:63367","NEWT:215402","NEWT:1547","NEWT:906914","NEWT:9031","NEWT:27292","NEWT:1050722","NEWT:3728","NEWT:108931","NEWT:1293497","NEWT:1055524","NEWT:150475","NEWT:267872","NEWT:381666","NEWT:172269","NEWT:9534","NEWT:5180","NEWT:256737","NEWT:9541","NEWT:8694","NEWT:33936","NEWT:8692","NEWT:2903","NEWT:185579","NEWT:13076","NEWT:207340","NEWT:1006581","NEWT:8673","NEWT:33940","NEWT:550","NEWT:554","NEWT:451516","NEWT:552","NEWT:1325291","NEWT:36185","NEWT:1054211","NEWT:1225786","NEWT:771870","NEWT:51338","NEWT:575412","NEWT:28112","NEWT:6493","NEWT:10832","NEWT:6494","NEWT:6491","NEWT:507601","NEWT:520","NEWT:186441","NEWT:643680","NEWT:214092","NCBITaxon:6157","NEWT:13095","NEWT:162425","NEWT:104105","NEWT:216257","NEWT:9986","NEWT:8654","NEWT:8658","NEWT:1268063","NEWT:8657","NEWT:9983","NEWT:8655","NEWT:5147","NEWT:28108","NEWT:28104","NEWT:407821","NEWT:568703","NCBITaxon:2","NEWT:568708","NEWT:1613","NEWT:986","NEWT:52641","NEWT:28532","NEWT:353152","NEWT:298176","NEWT:353153","NEWT:227377","NEWT:1774284","NEWT:40674","NEWT:1194669","NEWT:443906","NEWT:519","NEWT:2510939","NEWT:7394","NEWT:6063","NEWT:1328388","NEWT:105487","NEWT:1548728","NEWT:667127","NEWT:9557","NEWT:377586","NEWT:300641","NEWT:39655","NEWT:9554","NEWT:38323","NEWT:475932","NEWT:256318","NEWT:206411","NCBITaxon:6191","NEWT:229533","NEWT:214053","NEWT:28550","NEWT:80863","NEWT:90675","NEWT:52639","NEWT:52638","NEWT:57075","NEWT:1666905","NEWT:8697","NEWT:8695","NEWT:884204","NEWT:1045775","NEWT:1123869","NEWT:9544","NEWT:9545","NEWT:979","NEWT:7370","NEWT:83906","NEWT:99488","NEWT:1134506","NEWT:255470","NEWT:38783","NEWT:6426","NEWT:33090","NEWT:9935","NEWT:287889","NEWT:3059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