{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD074496/checksum.txt"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD074496/ANG2-NVPD2-1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD074496/ANG2-NVPD2-5.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD074496/ANG2-4.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD074496/ANG2-NVPD2-4.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD074496/ANG2-6.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD074496/ANG2-NVPD2-2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD074496/ANG2-1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD074496/ANG2-5.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD074496/ANG2-3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD074496/ANG2-NVPD2-6.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD074496/ANG2-2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD074496/ANG2-NVPD2-3.raw"],"Xls":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD074496/CombineAnnotation.xls"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["wzmcliangguang@163.com"],"submitter":["仕炬 叶"],"technology_type":["Mass Spectrometry","Gel-based experiment"],"software":["Not available"],"submitter_keywords":["nf-κb p65","cardiomyocytes","cdk9","cardiac remodeling","Angiotensin ii; cdk9; nf-κb p65; cardiac remodeling; cardiomyocytes","Angiotensin ii"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD074496"],"tissue":["Heart"],"sample_protocol":["Quantitative phosphoproteomics was performed by MH BioTech Co.,Ltd (Shanghai, China). Briefly, the heart tissue samples were collected from three mice per group and pooled as one sample. The samples were preprocessed through protein extraction, protein digestion, TMT labeling, enrichment of modified peptides, fraction separation. The purified peptides were redissolved and analyzed by LC-MS/MS (Mass-Hub, Shanghai) using an Ultimate 3000 RSLCnano system (Thermo Fisher Scientific), which was online-connected to a Q Exactive HF mass spectrometer (Thermo Fisher) equipped with a Nanospray Flex ion source (Thermo Fisher)."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["For phosphoproteomic analysis, phosphorylation of serine (S), threonine (T), and tyrosine (Y), were specified as variable modifications. A total of 1298 phosphoproteins and 2396 phosphorylated modification sites were identified. Student’s t-test was then performed to compare the two groups, using a P value of < 0.05 and a fold-change threshold of 1.2 for upregulation or 0.83 for downregulation as criteria for significance. Proteins with a FC > 1.2 were considered upregulated, while those with a FC < 0.83 were considered downregulated.  KEGG and Reactome pathway enrichment analysis of NVP2-downregulated phosphoproteins according to their enrichment P-value (P < 0.05). For KEGG enrichment analysis and Reactome pathway enrichment analysis, the number of differentially expressed proteins (a) and the number of quantified proteins (b) are first calculated for each pathway. Subsequently, the total number of differentially expressed proteins (c) and the total number of quantified proteins (d) across all pathways are computed. Finally, using these four values (a, b, c, d), the Fisher's exact test P-value and enrichment fold are calculated. The enrichment fold is calculated using the formula: (a/c) / (b/d). For Protein interaction information, the PPI network was obtained from the STRING database (string-db.org). TOP 100 proteins were queried against protein interaction relationships in the STRING database to construct a network interaction diagram for these proteins. Core nodes within the protein interaction network were calculated using algorithms such as Degree, MCC, and MNC from the Cytoscope software."],"omics_type":["Proteomics"],"labhead":["Guang Liang"],"instrument_platform":[""],"labhead_affiliation":["Hangzhou Medical College"],"submission_type":["PARTIAL"],"species":["Mus Musculus (mouse)"],"submitter_mail":["3324111@zju.edu.cn"],"publication":["41876530 Ye S, Zhao Y, Tu H, Han X, Liu T, Gong Y, Lu J, Jin T, Luo W, Qu X, Lai D, Fu G, Liang G. Cardiomyocyte Cyclin-dependent kinase 9 directly binds to and phosphorylates NF-κB p65 subunit to drive cardiac inflammation and remodeling. Nat Commun. 2026 17(1):5036 10.1038/s41467-026-70410-6"],"submitter_affiliation":["Sir Run Run Shaw Hospital, School of Medicine, Zhejiang University"],"submitter_country":["China"],"pubmed_abstract":["Hypertensive heart failure highlights an urgent need for effective therapeutic strategies. Protein kinases regulate multiple pathways in cardiac pathophysiology and may provide promising therapeutic targets. Here, we identified a Cyclin-dependent kinase, CDK9, promoting inflammation and cardiac remodeling in terminally differentiated cardiomyocytes. Firstly, kinase enrichment analysis and experimental evidence revealed CDK9 phosphorylation at Thr-186 in both human and mouse hypertrophic heart tissues. CDK9 loss of function via T186A mutation in cardiomyocytes attenuated Ang II-induced heart remodeling and NF-κB-mediated inflammation, whereas CDK9 overactivation by T186E mutation induces. This regulatory function of CDK9 in cardiac remodeling is cell cycle-independent. Further studies demonstrate that the kinase domain of CDK9 directly binds to NF-κB P65 protein, which leads to the CDK9/P65 complex nuclear translocation, P65 phosphorylation, and transcription of inflammatory and hypertrophic genes in cardiomyocytes. This process requires CDK9 Thr-186 phosphorylation and Cyclin T1 presence, but is independent on IKKβ and CDK9-RNAPII pathways. Pharmacological inhibition of CDK9 phosphorylation significantly attenuated Ang II-induced cardiac inflammation, remodeling, and dysfunction in mice. Collectively, Ang II-activated CDK9 directly binds to and phosphorylates P65 to drive cardiac inflammation and remodeling. This study identifies CDK9 as a potential target in heart failure therapeutics."],"pubmed_title":["Cardiomyocyte Cyclin-dependent kinase 9 directly binds to and phosphorylates NF-κB p65 subunit to drive cardiac inflammation and remodeling."],"pubmed_authors":["Ye Shiju S, Zhao Yanbo Y, Tu Hanxiao H, Han Xue X, Liu Tong T, Gong Yingchao Y, Lu Jiangting J, Jin Tingting T, Luo Wu W, Qu Xuefeng X, Lai Dongwu D, Fu Guosheng G, Liang Guang G"],"additional_accession":[]},"is_claimable":false,"name":"Cardiomyocyte Cyclin-dependent kinase 9 directly binds to and phosphorylates NF-κB p65 subunit to drive cardiac inflammation and remodeling","description":"Hypertensive heart failure highlights an urgent need for effective therapeutic strategies. Protein kinases regulate multiple pathways in cardiac pathophysiology and may provide promising therapeutic targets. Here, we identified a Cyclin-dependent kinase, CDK9, promoting inflammation and cardiac remodeling in terminally differentiated cardiomyocytes. Firstly, kinase enrichment analysis and experimental evidence revealed CDK9 phosphorylation at Thr-186 in both human and mouse hypertrophic heart tissues. CDK9 loss of function via T186A mutation in cardiomyocytes attenuated Ang II-induced heart remodeling and NF-κB-mediated inflammation, whereas CDK9 overactivation by T186E mutation induces. This regulatory function of CDK9 in cardiac remodeling is cell cycle-independent. Further studies demonstrate that the kinase domain of CDK9 directly binds to NF-κB P65 protein, which leads to the CDK9/P65 complex nuclear translocation, P65 phosphorylation, and transcription of inflammatory and hypertrophic genes in cardiomyocytes. This process requires CDK9 Thr-186 phosphorylation and Cyclin T1 presence, but is independent on IKKβ and CDK9-RNAPII pathways. Pharmacological inhibition of CDK9 phosphorylation significantly attenuated Ang II-induced cardiac inflammation, remodeling, and dysfunction in mice. Collectively, Ang II-activated CDK9 directly binds to and phosphorylates P65 to drive cardiac inflammation and remodeling. This study identifies CDK9 as a potential target in heart failure 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