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Walter"],"technology_type":["Data-dependent acquisition","Affinity purification coupled with mass spectrometry proteomics","Mass Spectrometry","Bottom-up proteomics"],"disease":["Colon Cancer"],"software":[""],"submitter_keywords":["Human","Ap-ms","Ribosome","Spata5l1","55lcc","Cinp. c1orf109","Spata5"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD065526"],"tissue":["Permanent Cell Line Cell"],"sample_protocol":["Silac-labeled cells containing POIs of interest fused to GFP/mCherry/FLAG/HaloTag were cultured in 15 cm dishes until ~80% confluency. Wild-type (or for GFP, free GFP-containing cells) labeled with ‘light’ isotopes were used as background controls. Depending on the experimental setup, tagged cell lines were labeled with ‘heavy’ isotopes. To compare treatments, untreated cells were labeled with ‘medium’ isotopes, while the same cells with treatment of interest were labeled with heavy isotopes before the assay. Cells were washed three times with ice-cold 1x PBS, scraped off, pelleted at 1,000rcf for 1 minute at 4 °C, and lysed in RIPA buffer (50 mM Tris-HCl pH 7.5, 150 mM NaCl, 1% NP40, 0.1% sodium deoxycholate, 1 mM EDTA pH 7.5, 5 mM β-glycerophosphate, 5 mM sodium fluoride, 1 mM sodium orthovanadate, and cOmplete Inhibitor cocktail EDTA Free (Roche) while rotating at 4 °C for 30 min. Next, lysates were sonicated three times for 30 sec at high intensity at 4 °C using a Diagenode Bioruptor Plus, followed by centrifugation at 16 000 rcf for 10 min at 4 °C. Supernatants were transferred to new tubes, and protein concentrations were measured using the Pierce BCA assay on a Tecan Spark system. Protein concentrations were adjusted to a maximum of 2 mg/mL, and 2 mg of protein were used for each affinity purification (AP) condition. Next, prewashed beads specific for the fusion proteins were added to the lysates (15 µL GFP-trap, 15 µL RFP-traps, 20 µL anti-FLAG and 15 µL HaloTrap-beads), and AP was carried out for 90 min at 4 °C with rotation at 10 rpm. Beads were washed once with 1 mL of RIPA buffer, and control and POI-tagged samples were combined at this step. After two additional washes with AP-MS wash buffer proteins were digested on-bead using 50 µL of elution buffer 1 (50 mM Tris-HCl pH 7.5, 2 M urea, 5 µg/mL trypsin, 1 mM DTT) for 30 min at 30 °C with shaking at 800 rpm. The supernatants were collected together with two additional washes using 100 µL of elution buffer 2 (50 mM Tris-HCl pH 7.5, 2 M urea, 5.5 mM CAA). The eluted protein mixtures were incubated overnight at 37 °C with shaking at 1 000 rpm. The next day, peptides were purified using stage tips with three C18 discs, vacuum-concentrated at 60 °C, and finally dissolved in 0.15% TFA at 30 °C with shaking at 1 500 rpm for 15 min. Peptide concentrations were measured using a NanoDrop One (Abs1 = 1 mg/mL), and 300 ng of peptides per sample were used for subsequent MS analysis.  In gel sample preparation AP of tagged POIs and their interactors was performed the same, but the post-AP processing differed significantly and is described here. After AP, the beads were washed three times with ice-cold RIPA lysis buffer. Proteins bound to the beads were then eluted by heating the beads at 95 °C for 15 min in 50 µL of 4x NuPAGE LDS sample buffer (Invitrogen) containing 1mM DTT. Afterward, 1 µL of 550 mM chloroacetamide (CAA) was added, and the samples were incubated at room temperature (RT) for 30 min. The eluted proteins were then subjected to in-gel digestion for MS analysis. First, the proteins were separated on a NuPAGE Novex Bis-Tris 4%-12% gel (Invitrogen). The gel was stained with Novex colloidal blue stain (Invitrogen) and destained with water. Each lane was cut into four slices, which were further destained using 25 mM ammonium bicarbonate buffer containing 50% ethanol. The gel pieces were then dehydrated with 100% ethanol before being digested in-gel with trypsin (Sigma-Aldrich) at 37 °C for 16 h. Following digestion, the gel pieces were treated with trifluoroacetic acid (TFA) to stop the reaction, and the resulting peptides were eluted using increasing concentrations of acetonitrile. These peptides were desalted using C18 StageTips. For elution from the StageTips, 50 µL of a 60% acetonitrile and 0.1% TFA solution was used. The peptides were then vacuum-dried at 60 °C until at least 50% of the initial volume evaporated. Dried peptides were resuspended in 0.15% TFA buffer at 30 °C and shaken at 1 500 rpm for 15 min. The resulting peptide concentration was estimated using a NanoDrop, and 300 ng of the sample was used for subsequent MS analysis."],"repository":["Pride"],"quantification_method":[""],"modification":[""],"data_protocol":["For DDA experiments raw data were processed using MaxQuant74 (v. 2.0.1.0), with searches conducted against the UniProt databases for  Homo sapiens (as indicated in the sample sheets). The false discovery rate (FDR) for both peptides and proteins was maintained at 1%. Cysteine carbamidomethylation was applied as a fixed modification, while methionine oxidation, N-terminal acetylation, and lysine acetylation were set as variable modifications. Re-quantification was enabled, and the number of allowed missed cleavages was set to two. All other parameters were left at their default settings. In R (v. 4.3.1), the ProteinGroups table from the MaxQuant output was filtered to exclude entries originating from the reverse decoy database, contaminants, and proteins identified solely by a modification site. Relative quantification of protein fold changes was determined using SILAC ratios extracted from the ProteinGroups table, normalized to the median ratio of all identified proteins. Statistical significance was assessed for proteins identified in at least three biological replicates. Differential protein abundance was estimated using the two-sided limma package. P-values below machine were automatically set to 0 by limma, so all p-values of 0 were replaced by machine (2.220446e-16). The Benjamini-Hochberg method was applied for multiple comparison correction. Scatter plots were generated by plotting the negative log10-transformed p-values against the log2-transformed fold changes between the perturbation and control. Proteins with a fold change of ≥1 and a p-value ≤0.05 were considered significantly enriched."],"omics_type":["Proteomics"],"labhead":["Chunaram Choudhary"],"instrument_platform":[""],"labhead_affiliation":["University of Copenhagen, Novo Nordisk Center for Protein Research, Proteomics Department, Proteomics and Cell Signaling Lab"],"submission_type":["PARTIAL"],"species":["Homo Sapiens (human)"],"publication":["Not available"],"submitter_mail":["jonaswalter@posteo.de"],"submitter_affiliation":["University of Bonn"],"submitter_country":["Germany"],"additional_accession":[]},"is_claimable":false,"name":"AP-MS Screening for novel Ribosome Biogenesis factors revealing 55LCC","description":"Data from our initital screening for novel biogenesis factors in human ribosome biogenesis, revealing 55LCC interaction and interaction within 55LCC. Further, the dataset includes 55LCC depletion data trapping the pre-60S, enriching non-released biogenesis factors on the pre-60S. In addition transgene variants were tested and the dependency of SPATA5L1 ATPase activity for Ribosome-55LCC interaction via GTPBP4-FLAG silac interactome in the presence of dual ATPase dead mutant while endogen was depleted.","dates":{"publication":"2026-07-29","submission":"2025-06-26"},"accession":"PXD065526","cross_references":{"TAXONOMY":["NEWT:330879","NEWT:377960","NEWT:2042546","NEWT:259447","NEWT:295546","NCBITaxon:2719036","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:111205","NEWT:1117","NEWT:498257","NEWT:10036","NEWT:1590","NEWT:10034","NEWT:661410","NEWT:638632","NEWT:224326","NEWT:376619","NCBITaxon:79857","NEWT:1096976","NEWT:1589","NEWT:135622","NEWT:35786","NEWT:1580","NEWT:399784","NEWT:96731","NEWT:383379","NEWT:418106","NEWT:10029","NEWT:913645","NEWT:641809","NEWT:38815","NEWT:317447","NEWT:4688","NEWT:111225","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:1912919","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:1182590","NEWT:3712","NEWT:3711","NEWT:270643","NEWT:2065263","NEWT:177437","NEWT:10418","NEWT:118698","NEWT:1616117","NEWT:118696","NEWT:34865","NEWT:52283","NEWT:284812","NEWT:8175","NEWT:43330","NEWT:1603293","NEWT:44664","NEWT:43346","NEWT:3702","NEWT:1245466","NEWT:244366","NEWT:1246791","NEWT:118694","NEWT:2850","NEWT:118691","NEWT:34871","NEWT:33548","NEWT:52299","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:1303443","NEWT:9483","NEWT:485","NEWT:56636","NEWT:2709072","NEWT:2853422","NEWT:1679718","NEWT:480","NEWT:67767","NEWT:46835","NEWT:109757","NEWT:582580","NEWT:294607","NEWT:1502","NEWT:128017","NEWT:376686","NEWT:95486","NEWT:1883446","NEWT:1233435","NEWT:109760","NEWT:29031","NEWT:235443","NEWT:1757312","NEWT:85694","NEWT:108458","NEWT:5936","NEWT:320637","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:472","NEWT:940825","NEWT:529507","NEWT:1071661","NEWT:470","NEWT:5911","NCBITaxon:50557","NEWT:39251","NEWT:29491","NEWT:101841","NEWT:446","NEWT:153481","NEWT:2014887","NEWT:33952","NEWT:445","NEWT:153009","NEWT:261756","NEWT:63366","NEWT:63367","NEWT:215402","NEWT:1547","NEWT:9031","NEWT:27292","NEWT:1050722","NEWT:108931","NEWT:1293497","NEWT:1055524","NEWT:150475","NEWT:267872","NEWT:172269","NEWT:9534","NEWT:5180","NEWT:256737","NEWT:9541","NEWT:8694","NEWT:33936","NEWT:8692","NEWT:2903","NEWT:185579","NEWT:13076","NEWT:1006581","NEWT:8673","NEWT:33940","NEWT:550","NEWT:554","NEWT:451516","NEWT:552","NEWT:1325291","NEWT:36185","NEWT:1054211","NEWT:1225786","NEWT:51338","NEWT:575412","NEWT:28112","NEWT:6493","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:8655","NEWT:5147","NEWT:28104","NEWT:407821","NEWT:568703","NCBITaxon:2","NEWT:568708","NEWT:986","NEWT:52641","NEWT:28532","NEWT:353152","NEWT:40674","NEWT:1194669","NEWT:51329","NEWT:443906","NEWT:519","NEWT:2510939","NEWT:7394","NEWT:6063","NEWT:1328388","NEWT:1548728","NEWT:667127","NEWT:9557","NEWT:377586","NEWT:300641","NEWT:39655","NEWT:9554","NEWT:38323","NEWT:256318","NEWT:206411","NCBITaxon:6191","NEWT:229533","NEWT:214053","NEWT:80863","NEWT:90675","NEWT:52638","NEWT:57075","NEWT:1666905","NEWT:8697","NEWT:8695","NEWT:884204","NEWT:1123869","NEWT:9544","NEWT:9545","NEWT:979","NEWT:7370","NEWT:83906","NEWT:1134506","NEWT:255470","NEWT:38783","NEWT:6426","NEWT:33090","NEWT:9935","NEWT:287889","NEWT:305959","NEWT:13489","NEWT:92867","NEWT:92866","NCBITaxon:3055","NEWT:51750","NEWT:202950","NEWT:295027","NCBITaxon:11320","NEWT:632957","NEWT:9925","NCBITaxon:9606","NEWT:90690","NEWT:1436183","NEWT:4232","NEWT:416348","NEWT:11298","NEWT:7742","NEWT:196627","NEWT:200308","NEWT:200302","NEWT:870435","NEWT:9913","NEWT:9915","NEWT:105841","NEWT:2666255","NEWT:999810","NCBITaxon:5693","NEWT:28995","NEWT:1392998","NEWT:380394","NEWT:226900","NEWT:1266738","NEWT:231490","NEWT:244704","NEWT:7725","NEWT:9909","NEWT:9902","NEWT:430615","NEWT:563041","NEWT:72664","NEWT:36599","NEWT:41949","NEWT:326423","NEWT:452467","NEWT:198822","NEWT:36111","NEWT:326424","NEWT:1678078","NEWT:74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