{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Tabular":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD067808/PXD067808_community_annotated.sdrf.tsv"],"Xlsx":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD067808/SDRF.xlsx"],"Msf":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD067808/P1858-3-NF_3.msfView","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD067808/P1858-2-NF_2.msfView","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD067808/P1858-3-NF_3.msf","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD067808/P1858-1-NF_1.msfView","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD067808/P1858-2-NF_2.msf","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD067808/P1858-1-NF_1.msf"],"Mzml":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD067808/P1858-3-NF_3.mzML","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD067808/P1858-1-NF_1.mzML","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD067808/P1858-2-NF_2.mzML"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD067808/P1858-1-NF_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD067808/P1858-2-NF_2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD067808/P1858-3-NF_3.raw"],"Mzid":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD067808/P1858-2-NF_2.mzid","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD067808/P1858-1-NF_1.mzid","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD067808/P1858-3-NF_3.mzid"],"Other":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD067808/P1858-3-NF_3.pdResult","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD067808/P1858-2-NF_2.pdResultView","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD067808/P1858-3-NF_3.pdResultView","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD067808/P1858-2-NF_2.pdResult","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD067808/P1858-1-NF_1.pdResult","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD067808/P1858-1-NF_1.pdResultView"]},"type":"primary"},"statusCodeValue":200,"statusCode":"OK"}],"scores":null,"additional":{"labhead_mail":["acammar3@jhmi.edu"],"submitter":["Sogol Sedighi"],"technology_type":["Data-dependent acquisition","Mass Spectrometry"],"software":[""],"submitter_keywords":["Human","Actin","Acetylation"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD067808"],"tissue":["Heart"],"sample_protocol":["1) In-gel Trypsin-LysC digestion as per SOP-PS-6001 (Standard Operation of Procedure for in-gel Digestion).  2) The digested peptide mixture was then concentrated and desalted using C18 Zip-Tip as per SOP- PS-6005 (Standard Operation of Procedure for Desalting Digested Peptides).  3) Reconstituted desalted peptides in 16 μl of 0.1% formic acid. 14 μl of peptide sample was analyzed by one 60 min LC/MS/MS run."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["The MS raw files were analyzed using Proteome Discoverer 2.5 against human protein sequences database."],"omics_type":["Proteomics"],"labhead":["Anthony Cammarato"],"instrument_platform":[""],"labhead_affiliation":["Division of Cardiology Department of Medicine Johns Hopkins University Baltimore, MD 21205"],"submission_type":["COMPLETE"],"species":["Homo Sapiens (human)"],"submitter_mail":["ssedigh2@jh.edu"],"publication":["41443503 Chitre K, Karpicheva OE, King CJ, Rynkiewicz MJ, Fenwick AJ, Dawson JF, Foster DB, Lehman W, Cammarato A. Pseudo-acetylation of ACTC1 K326 and K328 promotes dysinhibition of reconstituted human cardiac thin filaments. J Mol Cell Cardiol. 2026 212:10-15 10.1016/j.yjmcc.2025.12.008"],"submitter_affiliation":["Division of Cardiology, Department of Medicine,  Johns Hopkins University School of Medicine, Baltimore, MD, USA"],"submitter_country":["United States"],"doi":["10.6019/PXD067808"],"pubmed_abstract":["Electrostatic interactions between actin residues K326 and K328 and tropomyosin bias tropomyosin to an F-actin location where it blocks myosin attachment. K326/328 acetylation neutralizes their charge, potentially disrupting thin filament-based contractile regulation. We verified acetylation of K326/328 on human cardiac actin (ACTC1) and generated recombinant K326/328Q, pseudo-acetylated ACTC1. Pseudo-acetylation reduced inhibition of myosin-driven motility of F-actin-tropomyosin and F-actin-tropomyosin-troponin at low Ca<sup>2+</sup>. Cryo-EM-based and computational modeling revealed that pseudo-acetylation did not alter tropomyosin positioning along F-actin but decreased local F-actin-tropomyosin interaction energy. Thus, by reducing the energetic demands required for myosin to displace tropomyosin, ACTC1 K326/328 acetylation may promote contractile activation."],"pubmed_title":["Pseudo-acetylation of ACTC1 K326 and K328 promotes dysinhibition of reconstituted human cardiac thin filaments."],"pubmed_authors":["Chitre Kripa K, Karpicheva Olga E OE, King Chloe J CJ, Rynkiewicz Michael J MJ, Fenwick Axel J AJ, Dawson John F JF, Foster D Brian DB, Lehman William W, Cammarato Anthony A"],"additional_accession":[]},"is_claimable":false,"name":"Pseudo-acetylation of ACTC1 K326 and K328 promotes dysinhibition of reconstituted human cardiac thin filaments","description":"Tropomyosin (Tpm) regulates cardiac thin filament function by restricting myosin access through electrostatic interactions with actin - particularly involving residues K326 and K328 on each actin monomer. Acetylation at these lysines neutralizes charge, destabilizing Tpm’s inhibitory position and favoring myosin engagement. We hypothesize that mimicking this modification via a K to Q mutation would enhance contractility due to Tpm’s disinhibition. To determine whether cardiac actin amino acids K326 and 328 are acetylated in human cardiac tissue, we performed in-gel tryptic digestion of the major 42 kDa SDS-PAGE band (actin) from non-failing, donor cardiac homogenate replicates, and subsequently subjected the peptides to 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