{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Xlsx":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD065214/experimental_design.xlsx","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD065214/Acetyl_K_Sites.xlsx","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD065214/MOF_interactors_results.xlsx"],"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD065214/checksum.txt"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD065214/MOF_Soluble_deacet_06.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD065214/MOF_Soluble_acet_07.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD065214/MOF_Chr_deacet_01.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD065214/3672_JB_AVAQ008_2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD065214/3595_CT_AVAQ003_MOFTM_3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD065214/3595_CT_AVAQ003_MOFWT_2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD065214/MOF_Chr_acet_04.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD065214/3636_CT_AVAQ003_3_01.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD065214/3636_CT_AVAQ003_5_01.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD065214/MOF_Soluble_acet_08.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD065214/3636_CT_AVAQ003_1_01.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD065214/MOF_Chr_deacet_02.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD065214/3672_JB_AVAQ008_3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD065214/MOF_Soluble_deacet_05.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD065214/3595_CT_AVAQ003_Ctrl_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD065214/MOF_Chr_acet_03.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD065214/3672_JB_AVAQ008_1.raw"],"Other":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD065214/MaxQuant.7z"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["avaquero@carrerasresearch.org"],"submitter":["Joan Josep Bech-Serra"],"technology_type":["Data-dependent acquisition","Mass Spectrometry","Bottom-up proteomics"],"software":[""],"submitter_keywords":["Fusion lumos","Plk1","Mof","Interactome","Sirt2","Label free"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD065214"],"sample_protocol":["HEK293F cells transfected with wild-type and mutated MOF (K113R/K116R/K175R) were immunoprecipitated with and specific antibody against MOF and the immune complexes were pulled down with protein A-agarose beads. Control cells transfected with the empty vector were added to the experimental design. The resulting material was then “In-Beads” digested with trypsin. Briefly, the beads were washed three times with 500 l of 200mM Ammonium Bicarbonate (ABC) and resuspended in 60 l of 6M Urea/200 mM ABC. Then the samples were reduced with 10 l of 10mM DTT (1h, 30ºC) and alkylated with 10 l of 20mM Iodoacetamide (30 minutes, room temperature and darkness). After that, the samples were diluted with 280 l of 200 mM ABC and digested with 5l of 0.2g/l Trypsin for 16h at 37ºC.  The beads were finally, pulled-down (5 minutes at 5000g); the supernatant transferred to new-cleaned tubes and finally acidified with 20 l of 100% Formic acid. The resulting peptides mixtures were desalted using C18 stage tips (UltraMicroSpin Column, The Nest Group, Inc., MA) and dried-down in a SpeedVac. Samples were loaded to 300 μm × 5 mm C18 PepMap100, 5mm, 100Å (Thermo Scientific) at a flow rate of 15 μL/min using a Thermo Scientific Dionex Ultimate 3000 chromatographic system (Thermo Scientific). Peptides were separated using a C18 analytical column (nanoEaseTM M/Z HSS C18 T3 (75 μm × 25 cm, 100Å, Waters) with a 150 min run, comprising three consecutive steps with linear gradients from 3% to 35 % B in 120 min, from 35 % to 50 % B in 5min, from 50 % to 85% B in 2min, followed by isocratic elution at 85 % B in 5 min and stabilization to initial conditions (A= 0.1% FA in water, B= 0.1% FA in CH3CN) at 250 nL/min flow rate. The column outlets were directly connected to an Advion TriVersa NanoMate (Advion) fitted on an Orbitrap Fusion Lumos™ Tribrid mass spectrometer (Thermo). The mass spectrometer was operated in a data-dependent acquisition (DDA) mode. Survey MS scans were acquired in the orbitrap with the resolution (defined at 200 m/z) set to 120,000. The lock mass was user-defined at 445.12 m/z in each Orbitrap scan. The top speed (most intense) ions per scan were fragmented by CID. The MSMS was detected in the Ion Trap (with Max Injection time of 35ms). The ion count target value was 400,000 for the survey scan and 10,000 (CID) for the MS/MS scan. Target ions already selected for MS/MS were dynamically excluded for 15 s. Spray voltage in the NanoMate source was set to 1.70 kV. RF Lens were tuned to 30%. Minimal signal required to trigger MS to MS/MS switch was set to 5000 and activation Q was 0.250. The spectrometer was working in positive polarity mode and singly charge state precursors were rejected for fragmentation. Data was acquired with Xcalibur software vs 4.0.27.10 (Thermo Scientific)."],"repository":["Pride"],"quantification_method":[""],"modification":[""],"data_protocol":["The .raw files will be analyzed with the MaxQuant(v.1.6.7.0) software using the built-in search engine Andromeda to search against the Swissprot Human database downloaded from UniprotKB website in October 25, 2019. The search parameters were set as follow: the enzyme was trypsin with a maximum of 2 allowed missed cleavages. Oxidation in methionines as well as Acetylation at protein N-terminal was set as variable modifications while carbamidomethylation in cysteines was set as fixed modification. The mass tolerances for the first and main search were set at 20 and 4.5 ppm, respectively. In addition, only peptides with more than 8 and up to 25 aminoacids were considered. The final list of identified peptides and proteins were filtered by using a 1% False Discovery Rate (FDR) both at peptide and protein level."],"omics_type":["Proteomics"],"labhead":["Alex Vaquero"],"instrument_platform":[""],"submission_type":["PARTIAL"],"labhead_affiliation":["Chromatin Biology Laboratory, Cancer Epigenetics and Biology Program (PEBC), Bellvitge Biomedical Research Institute (IDIBELL), L’Hospitalet de Llobregat, Barcelona, Spain.  Chromatin Biology Laboratory, Josep Carreras Leukaemia Research Institute (IJC), Badalona, Spain."],"species":["Homo Sapiens (human)"],"publication":["Not available"],"submitter_mail":["jbech@carrerasresearch.org"],"submitter_affiliation":["Proteomics Unit - Josep Carreras Leukaemia Research Institute"],"submitter_country":["Spain"],"additional_accession":[]},"is_claimable":false,"name":"The functional antagonism between SIRT2 and MOF regulates mitotic entry - MOF interactors","description":"Mitosis entry is tightly regulated by a complex network of interconnected mechanisms involving epigenetic modifications, signaling pathways, transcriptional control, and structural changes. While significant progress has been made in understanding these processes individually, the mechanisms integrating chromatin dynamics with key mitotic regulators are still not fully understood. Here, we identify a functional antagonism between the deacetylase SIRT2 and the acetyltransferase MOF in the G2/M transition and mitotic progression. This interplay, which involves MOF deacetylation by SIRT2, regulates key histone marks, including H4K16ac deacetylation and H4K20me1 deposition, condensin II loading, the stability of the key mitotic regulator PLK1 and has a major impact on the transcription control of mitosis regulated by the FOXM1. Our findings reveal a previously unrecognized layer of regulation in G2/M progression, shedding light on the intricate crosstalk between chromatin dynamics and mitotic control, with potential implications for understanding chromosomal stability and 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