{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD066596/checksum.txt"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD066596/2322_14_B.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD066596/2322_07.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD066596/2322_03.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD066596/2322_01_B.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD066596/2322_16.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD066596/2322_08.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD066596/2322_04.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD066596/2322_13_B.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD066596/2322_05.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD066596/2322_06.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD066596/2322_02.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD066596/2322_15.raw"],"Mztab":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD066596/2322_01_B.mzTab","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD066596/2322_05.mzTab","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD066596/2322_15.mzTab","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD066596/2322_02.mzTab","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD066596/2322_07.mzTab","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD066596/new_cons_12.mzTab","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD066596/2322_04.mzTab","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD066596/2322_13_B.mzTab","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD066596/2322_16.mzTab","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD066596/2322_06.mzTab","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD066596/2322_14_B.mzTab","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD066596/2322_03.mzTab","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD066596/2322_08.mzTab"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["pflum@wayne.edu"],"submitter":["Mary Kay Pflum"],"technology_type":["Data-dependent acquisition","Mass Spectrometry","Bottom-up proteomics"],"disease":["Disease Free"],"software":[""],"submitter_keywords":["Substrate profiling","Kinase activity","Histone deacetylase","Hdac11","Proteomics","Braf"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD066596"],"tissue":["Epithelial Cell"],"sample_protocol":["HEK293 cells (ATCC, CRL-1573) were grown at 37°C in 5% CO2 in growth media containing high glucose DMEM (Gibco™, 12430104), 10% FBS (Gibco™, 16170086), and 1% antibiotics (Gibco™, 15240062). For HDAC11-FLAG overexpression, HEK293 cells at 60% confluency (approximately 2 X 10^6 cells) were transfected with mammalian expression plasmids encoding wild type or F152A mutant (pcDNA3+HDAC11-FLAG, 5 μg) using jetPRIME reagent (Avantor, 89129-924). After 4 hr of incubation at 37°C in 5% CO2 with jetPRIME reagent and plasmid DNA, media was replaced with fresh growth media and incubated for 24 hr at 37°C in 5% CO2. Then, HDAC inhibitor SAHA (30 μM in ≤ 2% DMSO, final concentration after dilution) was added to the growth media and incubated for another 24 hr to induce acetylation of cellular proteins. After cell harvest, the cell pellet was lysed in lysis buffer (500 μL; 50 mM Tris-Cl at pH 8.0, 150 mM NaCl, 10% glycerol, and 0.5% triton-X100) with 1× protease inhibitor cocktail (5 μL; genDEPOT, P3100-020) at 4°C for 40 min with rocking. The soluble cell lysate was collected after centrifugation at 4°C at 16800 rcf for 10 min, and total protein concentration was measured using Bradford reagent (Biorad, 5000205). For immunoprecipitation, the transfected lysates (3 mg total protein) were incubated with the FLAG antibody conjugated M2 affinity agarose beads (40 μL bead slurry, Sigma Aldrich, A2220, prewashed twice with cold Tris Buffered Saline (TBS); 500 μL; 20 mM Tris-Cl at pH 8.0, 150 mM NaCl) at 4 °C overnight with rocking in lysis buffer at 500 µL total volume in the presence of either a DMSO vehicle (≤ 2%) or Trapoxin A (1 uM in ≤ 2% DMSO). After incubation, beads were washed three times with lysis buffer containing high salt (500 mM NaCl) with centrifugation at 5000 rcf for 1 min at 4 °C to collect the bound beads between washes. After removal of the final wash buffer, the washed beads were incubated with 2X Laemmli sample buffer (40 uL; diluted from 4X Laemmli sample buffer; Bio-Rad, 1610747, with fresh -mercaptoethanol, 10% v/v) at 95°C in a sand bath for 2 minutes to denature and elute the bound HDAC11-FLAG. After elution, 80% of the eluate for LC-MS/MS analysis was desalted using 10% SDS-PAGE with electrophoresis for only 10 min at 100 V, which allowed the proteins to enter the first 1 cm of the separating layer. Proteins in the gel were visualized with Sypro Ruby stain (Invitrogen, S12000) and UV (365 nm) light, excised from each lane (1 cm × 2 cm area), cut into 1 mm small pieces, and washed with destaining buffer (100 μL; 1:1 (v/v) acetonitrile: freshly prepared 50 mM ammonium bicarbonate, AB) for 15 min at room temperature. After removal of the destaining buffer, samples were dehydrated in acetonitrile (100 μL) for 10 min at room temperature. After removing the acetonitrile, gel pieces were rehydrated with 50 mM AB (100 μL) for 5 min. An equal volume of acetonitrile (100 μL) was added, and the mixture was incubated for 15 min at room temperature. After removal of the solvent mixture, the gel pieces were again dehydrated in acetonitrile (100 μL) until the pieces turn white in color. The acetonitrile was removed, and the gel slices were dried using a speedvac concentrator (ThermoSavant). Next, the dried gel slices were swelled with reducing buffer (100 μL; 50 mM TCEP in 25 mM AB) for 10 min at 37°C. After removing the reducing buffer, proteins were alkylated by incubating the gel pieces with alkylation buffer (100 μL; 55 mM iodoacetamide in 25 mM AB) with gentle rocking for 1 hr at room temperature. The alkylation buffer was removed, and the gel pieces were washed twice with destaining buffer (100 μL; 1:1 (v/v) acetonitrile: freshly prepared 50 mM AB) for 5 min at room temperature before dehydration with acetonitrile (100 μL). After the removal of the acetonitrile, the gel pieces were dried using a speedvac. The digestion step was accomplished by incubating the dried gel pieces with digestion buffer (100 μL; 20 ng/μL trypsin, Promega, V5280) in 40 mM AB and 9% acetonitrile) overnight at 37°C. The digested solutions were collected into new LoBind eppendorf tubes (Fisher Scientific, 13-698-794), and the gel pieces were extracted using extraction buffer (50 μL; 50 % acetonitrile and 0.2 % formic acid; ProteoChem, LC6201). The combined digestion and extraction buffers containing digested peptides were dried using speedvac and stored at −20°C until LC-MS/MS analysis."],"repository":["Pride"],"quantification_method":[""],"modification":[""],"data_protocol":["LC-MS/MS analysis was performed at the Wayne State University and Karmanos Cancer Center Proteomics Core facility. Digested peptides were separated by reverse phase chromatography under acidic conditions (0.1% formic acid) using an Easy-nLC 1000 UHPLC system (Thermo) and a C-18 column and analyzed on an Orbitrap Q Exactive mass spectrometer (Thermo). MS1 profiling was carried out over a 375-1600 m/z range at a resolution of 70,000. MS2 fragmentation was performed using higher energy collision induced dissociation (HCD) on the top 15 ions using a 1.6 m/z window and normalized collision energy of 29. Dynamic exclusion was turned on (15 s). MS raw data was processed using Proteome Discoverer (version 3.0) against a human database from Uniprot (UP000005640 Homo sapiens (human), downloaded 2021.03.30, 16679 entries). Searches included up to 2 missed tryptic cleavages. Mass tolerances for parent ions were 20 ppm for the first search, 4.5 ppm for the second search, and 20 ppm for fragment ions. The S5 iodoacetamide derivative of cysteine was specified as a fixed modification. Oxidation of methionine and acetylation of protein N-termini were set as variable modifications. Minimum protein and peptide identification probabilities were set at ≤1% false discovery rate (FDR), as determined by a reversed database search, and proteins required at least 1 unique peptide. All other parameters were left at their default settings. Label-free quantitation was performed using Maxquant software."],"omics_type":["Proteomics"],"labhead":["Mary Kay Pflum"],"instrument_platform":[""],"submission_type":["COMPLETE"],"labhead_affiliation":["Department of Chemistry, Wayne State University, 5101 Cass Avenue, Detroit, MI 48202"],"species":["Homo Sapiens (human)"],"submitter_mail":["pflum@wayne.edu"],"publication":["41273269 Madueke AC, Andrade R, Pflum MKH. HDAC11 Deacetylates BRAF to Regulate Kinase Activity and Cell Proliferation. ACS Chem Biol. 2025 20(12):2873-2885 10.1021/acschembio.5c00631"],"submitter_affiliation":["Wayne State University Chemistry"],"submitter_country":["United States"],"doi":["10.6019/PXD066596"],"pubmed_abstract":["Histone acetylation, governed by histone deacetylase (HDAC) enzymes, plays a pivotal role in cell biology. Elevated HDAC expression is linked to a poor prognosis in various diseases, including cancer, making HDAC inhibitors clinically valuable. Among the 11 metal-dependent HDAC isoforms, the exceptional ability of HDAC11 to regulate both the deacetylation and defattyacylation of proteins suggests an expansive role in cellular processes. However, since HDAC11 is one of the least studied HDAC isoforms, the known roles for HDAC11 in cell biology are limited. In this study, proteomics-based mutant trapping was performed to identify nonhistone substrates of HDAC11 and link HDAC11 activity to specific cellular events. Proteomics revealed 64 putative substrates, with follow-up studies documenting that HDAC11 deacetylates the BRAF kinase on K680 to suppress kinase activity and cell proliferation. Given the established role of BRAF in cancer, HDAC11-mediated deacetylation likely influences signaling pathways in tumor progression, underscoring the diverse regulatory role of HDAC11 in cellular events."],"pubmed_title":["HDAC11 Deacetylates BRAF to Regulate Kinase Activity and Cell Proliferation."],"pubmed_authors":["Madueke Augustine C AC, Andrade Rafael R, Pflum Mary Kay H MKH"],"additional_accession":[]},"is_claimable":false,"name":"HDAC11 Deacetylates BRAF to Regulate Kinase Activity and Cell Proliferation","description":"Histone acetylation, governed by histone deacetylase (HDAC) enzymes, plays a pivotal role in cell biology. Elevated HDAC expression is linked to poor prognosis in various diseases, including cancer, making HDAC inhibitors clinically valuable. Among the 11 metal-dependent HDAC isoforms, the exceptional ability of HDAC11 to regulate both deacetylation and defattyacylation of proteins suggests an expansive role in cellular processes. However, since HDAC11 is one of the least studied HDAC isoforms, the known roles for HDAC11 in cell biology are limited. In this study, proteomics-based mutant trapping was performed to identify non-histone substrates of HDAC11 and link HDAC11 activity to specific cellular events. Proteomics analysis revealed 64 putative substrates, with follow-up studies documenting that HDAC11 deacetylates the BRAF kinase on K680 to suppress kinase activity and cell proliferation. Given the established role of BRAF in cancer, the data suggest that HDAC11-mediated deacetylation influences signaling pathways in tumor progression, underscoring the diverse regulatory role for HDAC11 in cellular events.","dates":{"publication":"2026-04-27","submission":"2025-07-25"},"accession":"PXD066596","cross_references":{"TAXONOMY":["NEWT:108018","NEWT:377960","NEWT:1131","NEWT:190486","NEWT:2042546","NEWT:148942","NEWT:295546","NEWT:258594","NEWT:1126","NEWT:1129","NEWT:89187","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:488003","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:641809","NEWT:44250","NEWT:317447","NEWT:5530","NEWT:868565","NEWT:135674","NEWT:1562698","NEWT:12637","NEWT:2164133","NEWT:1180","NEWT:2767846","NEWT:1343074","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: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:65121","NEWT:3715","NEWT:2065263","NEWT:1549675","NEWT:177437","NEWT:9014","NEWT:10891","NEWT:118221","NEWT:34869","NEWT:226126","NEWT:1616117","NEWT:34865","NEWT:550537","NEWT:284812","NEWT:3701","NEWT:3702","NEWT:1245466","NEWT:3704","NEWT:1246791","NEWT:34875","NEWT:9005","NEWT:34871","NEWT:9006","NEWT:33548","NEWT:1883426","NEWT:657321","NEWT:10886","NEWT:3708","NEWT:536231","NEWT:219813","NEWT:2305479","NEWT:215451","NEWT:460519","NEWT:272843","NEWT:272844","NEWT:1348799","NEWT:55784","NEWT:485","NEWT:2499525","NEWT:467144","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:272831","NEWT:987059","NEWT:491","NEWT:460523","NEWT:2423","NEWT:85694","NEWT:85692","NEWT:911045","NEWT:3750","NEWT:291146","NEWT:233271","NEWT:3745","NEWT:1715989","NCBITaxon:4751","NEWT:3747","NEWT:278161","NEWT:415978","NEWT:410289","NEWT:191701","NEWT:9054","NEWT:472","NEWT:29459","NEWT:28128","NEWT:470","NEWT:41122","NEWT:1328300","NEWT:748693","NCBITaxon:50557","NEWT:3735","NEWT:29491","NEWT:911022","NEWT:446","NEWT:153481","NEWT:714485","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:1325292","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:311339","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: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:941638","NEWT:7394","NEWT:6063","NEWT:404330","NEWT:1328388","NEWT:13064","NEWT:300641","NEWT:39655","NEWT:206411","NEWT:80869","NEWT:214053","NEWT:80863","NEWT:665890","NEWT:52639","NEWT:52638","NEWT:8697","NEWT:861109","NEWT:8695","NEWT:1196866","NEWT:6039","NEWT:1045775","NEWT:1123869","NCBITaxon:1335626","NEWT:7370","NEWT:280406","NEWT:83906","NEWT:99488","NEWT:99487","NEWT:1134506","NEWT:255470","NEWT:762903","NEWT:27697","NEWT:86185","NEWT:9935","NEWT:266940","NEWT:287889","NEWT:1028307","NEWT:52603","NEWT:92867","NEWT:92866","NEWT:1344414","NEWT:202950","NEWT:741158","NEWT:1293091","NEWT:202956","NEWT:483179","NEWT:315750","NEWT:99490","NEWT:632957","NEWT:9925","NCBITaxon:9606","NEWT:1436183","NEWT:1479235","NEWT:4232","NEWT:9922","NEWT:416348","NEWT:105812","NEWT:11298","NEWT:4233","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: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