{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD057524/checksum.txt"],"Csv":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD057524/db.protein-peptides.csv"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD057524/231101_23SP030_3_260ng_4ul.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD057524/231101_23SP030_2_248ng_4ul.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD057524/231101_23SP030_1_236ng_4ul.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD057524/231101_23SP030_4_188ng_4ul.raw"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["lenka.hernychova@mou.cz"],"submitter":["Naina Verma"],"technology_type":["Mass Spectrometry","Bottom-up proteomics"],"software":["Not available"],"submitter_keywords":["Human","Rna splicing","P21l","Isoform","P21waf1","Cyclin-dependent kinase 11","Mass spectrometry","Sf3b1","P53"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD057524"],"sample_protocol":["LC-MS/MS analysis was carried out using an Orbitrap FusionTM mass spectrometer (Thermo Fisher Scientific) with a New Objective digital PicoView 565 nanospray source (Scientific Instrument Services) coupled to a DionexTM UltiMateTM 3000 RSLC Nanoliquid chromatograph. The peptides were loaded into an Acclaim PepMapTM 100 nano trap column (nanoViperTM C18, 0.3 × 5 mm, 5 µm particle size, 100 Å pore size; Thermo Fisher Scientific) with loading buffer (2% ACN with 0.05% aqueous TFA (v/v)) for 5 min desalting at a flow rate 5 µl/min. Next, the peptides were eluted onto an Acclaim PepMapTM RSLC C18 (nanoViperTM 75 µm × 25 cm, 2 µm particle size, 100 Å pore size, Thermo Fisher Scientific) kept at 50 °C and separated by linear gradient elution over 36-min from 2-25% B and 5-min gradient from 25-60% B, followed by a 6-min wash step with 98% B, and 27-min of equilibration with 2% B. Mobile phase A was composed of LC-MS grade water and 0.1% formic acid (FA) while B was 80% acetonitrile with 0.1% aqueous FA (v/v). The flow rate was 300 nl/min. The Orbitrap mass analyzer was operated in positive ion mode, with the static positive ion spray voltage set to 2.7 kV, and ion transfer tube temperature to 275 °C. The master scan was acquired at resolving power settings of 120,000 (FWHM @ m/z 200), precursor mass range was 350-1400 m/z. The MS/MS spectra of multiply charged ions were collected in data-dependent mode (fragment and measure most intensive precursors for 2 seconds). Dynamic exclusion was set to 30 s. The peptides were fragmented using high energy collision-induced dissociation (HCD) with the normalized collision energy setting at 30 % and isolation window of 4 Da. The peptide fragments generated via HCD were detected in an ion trap (rapid scan rate)."],"repository":["Pride"],"quantification_method":[""],"modification":[""],"data_protocol":["Data analysis was performed with Peaks Studio 11. The raw data were treated with mass correction and chimera associations. The data were then searched by Peaks search engine where the main database was homo sapiens proteins from SwissProt with alternative sequence of p21 and secondary database was common MS contaminants. Precursors were searched with 10 ppm mass tolerance and fragments with 0.6 Da mass tolerance. Enzyme was set as semi-specific trypsin with up to 3 missed cleavages. A total of 4 variable modifications were considered, acetylation on protein N-terminus, carbamidomethylation on cysteine, deamidation of asparagine or glutamine and methylation on methionine. Results were validated by decoy search used to set false discovery rate on peptide level to 1%."],"omics_type":["Proteomics"],"labhead":["Prof. Lenka Hernychova"],"instrument_platform":[""],"labhead_affiliation":["RECAMO, Masaryk Memorial Cancer Institute Zluty Kopec, Brno,  Czech Republic"],"submission_type":["PARTIAL"],"species":["Homo Sapiens (human)"],"publication":["41105927 Krejcir R, Arcimowicz L, Martinkova L, Hrabal V, Zavadil Kokas F, Henek T, Kucerikova M, Bonczek O, Zatloukalova P, Hernychova L, Coates PJ, Vojtesek B, Lane DP. CDK11 inhibition induces cytoplasmic p21&lt;sup&gt;WAF1&lt;/sup&gt; splice variant by p53 stabilisation and SF3B1 inactivation. Mol Oncol. 2026 20(3):804-822 10.1002/1878-0261.70143"],"submitter_mail":["naina.verma@mou.cz"],"submitter_affiliation":["Masaryk Memorial Cancer Institute"],"submitter_country":["Czechia"],"pubmed_abstract":["CDK11 is a cyclin-dependent kinase with a role in transcription and RNA splicing and represents a potential target for cancer treatment. We show that blocking CDK11 activity with the OTS964 inhibitor causes p53 stabilisation through MDM2 downregulation. Under these conditions, p53 activates the expression of its downstream effector CDKN1A (p21<sup>WAF1</sup>), produced in two isoforms, the canonical p21<sup>C</sup> and the recently described p21<sup>L</sup>. We compared the ability of both isoforms to block proliferation and showed that p21<sup>L</sup> partially lost its inhibitory potential, likely due to the missing cyclin-binding Cy2 and PCNA-interacting motifs and its cytoplasmic localisation. We identified the epitopes of four p21<sup>WAF1</sup> antibodies using phage display to determine isoform specificity. Moreover, we show that the trigger for p21<sup>L</sup> induction is inhibition of the spliceosomal protein SF3B1. CDK11 activates SF3B1 by phosphorylation, and inhibition of either SF3B1 or CDK11 induces p21<sup>L</sup>. We discovered an isoform similar to human p21<sup>L</sup> in murine cells, suggesting evolutionary conservation of CDKN1A alternative splicing. Our results uncover an unknown link between RNA splicing and proliferation control involving a novel isoform of a key cell cycle inhibitor."],"pubmed_title":["CDK11 inhibition induces cytoplasmic p21&lt;sup&gt;WAF1&lt;/sup&gt; splice variant by p53 stabilisation and SF3B1 inactivation."],"pubmed_authors":["Krejcir Radovan R, Arcimowicz Lukasz L, Martinkova Lucia L, Hrabal Vaclav V, Zavadil Kokas Filip F, Henek Tomas T, Kucerikova Martina M, Bonczek Ondrej O, Zatloukalova Pavlina P, Hernychova Lenka L, Coates Philip J PJ, Vojtesek Borivoj B, Lane David P DP"],"additional_accession":[]},"is_claimable":false,"name":"CDK11 inhibition induces cytoplasmic p21WAF1 splice variant by p53 stabilisation and SF3B1 inactivation","description":"CDK11 is a cyclin-dependent kinase with a role in transcription and RNA splicing and represents a potential target of anticancer treatment. This study investigated the interconnection between CDK11 and the p53 tumour suppressor protein. We show that blocking CDK11 functions with selective OTS964 inhibitor leads to p53 stabilisation through MDM2 downregulation, while the low MDM2 levels are achieved by degradation of MDM2 mRNA. p53 activates the expression of its downstream effector p21WAF1, produced in two isoforms, canonical p21C and recently described alternative p21L. The difference between the two isoforms is in the C-terminus with p21L lacking several functional motifs including a nuclear localisation signal and a PCNA binding motif. Because of the lack of isoform-specific p21 antibodies, the identity of p21L was confirmed with mass spectrometry. Furthermore, we analysed the epitopes of three anti-p21 monoclonal antibodies and identified those that recognise both isoforms and an antibody specific to p21C, making it a valuable tool for future research of p21 isoforms. We compared the ability of both isoforms to block proliferation and showed that p21L partially lost its inhibitory potential and that p21L is also more stable than p21C. Furthermore, we discovered that the trigger for p21L induction is inhibiting the SF3B1 spliceosomal protein. CDK11 activates SF3B1 by phosphorylation and inhibition of both SF3B1 and CDK11 induces p21L. The inhibition of another spliceosomal component SF2/ASF only induces p21C. Moreover, p21L is only induced in the cells with functional p53 protein and p53 knock-out cells lose this ability. We also show that an isoform similar to human p21L is produced in murine cells in response to OTS964. We conclude that p21L might represent a possible mechanism for tumour cells to escape p21-induced mitotic arrest, especially for those with SF3B1 mutations and other alterations in spliceosome functions.","dates":{"publication":"2026-04-06","submission":"2024-11-05"},"accession":"PXD057524","cross_references":{"TAXONOMY":["NEWT:330879","NEWT:377960","NEWT:2042546","NEWT:259447","NEWT:295546","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:6819","NEWT:475174","NEWT:1117","NEWT:498257","NEWT:10036","NEWT:1590","NEWT:10034","NEWT:661410","NEWT:638632","NEWT:224326","NEWT:376619","NCBITaxon:79857","NEWT:1096976","NEWT:3765","NEWT:1589","NEWT:135622","NEWT:35786","NEWT:1580","NEWT:399784","NEWT:96731","NEWT:656064","NEWT:1582","NEWT:36630","NEWT:383379","NEWT:418106","NCBITaxon:12721","NEWT:10029","NEWT:913645","NEWT:641809","NEWT:1392488","NEWT:38815","NEWT:317447","NEWT:4688","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:410658","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:3714","NEWT:2065263","NEWT:177437","NEWT:10418","NEWT:118698","NEWT:1616117","NEWT:118696","NEWT:34865","NEWT:52283","NEWT:28174","NEWT:284812","NEWT:8175","NEWT:43330","NEWT:1603293","NEWT:44664","NEWT:43346","NEWT:3702","NEWT:1245466","NEWT:3704","NEWT:244366","NEWT:1246791","NEWT:118694","NEWT:2850","NEWT:118691","NEWT:34871","NEWT:33548","NEWT:52299","NEWT:8165","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:1348799","NEWT:33995","NEWT:55784","NEWT:1303443","NEWT:9483","NEWT:485","NEWT:56636","NEWT:2499525","NEWT:2853422","NEWT:487","NEWT:1679718","NEWT:480","NEWT:67767","NEWT:46835","NEWT:109757","NEWT:582580","NEWT:1185650","NEWT:216778","NEWT:1502","NEWT:128017","NEWT:376686","NEWT:237610","NEWT:95486","NEWT:1883446","NEWT:1233435","NEWT:118223","NEWT:109760","NEWT:29031","NEWT:317047","NEWT:491","NEWT:460523","NEWT:235443","NEWT:1757312","NEWT:85694","NEWT:109786","NEWT:108458","NEWT:5936","NEWT:320637","NEWT:1078283","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:1640278","NEWT:472","NEWT:940825","NEWT:529507","NEWT:1071661","NEWT:28128","NEWT:470","NEWT:5911","NEWT:748693","NCBITaxon:50557","NEWT:39251","NEWT:29491","NEWT:101841","NEWT:446","NEWT:153481","NEWT:2014887","NEWT:33952","NEWT:445","NEWT:153009","NEWT:261756","NEWT:166313","NEWT:63366","NEWT:63367","NEWT:215402","NEWT:1547","NEWT:906914","NEWT:9031","NEWT:27292","NEWT:1050722","NEWT:3728","NEWT:108931","NEWT:1293497","NEWT:1055524","NEWT:150475","NEWT:267872","NEWT:381666","NEWT:172269","NEWT:9534","NEWT:5180","NEWT:256737","NEWT:9541","NEWT:8694","NEWT:33936","NEWT:8692","NEWT:2903","NEWT:185579","NEWT:13076","NEWT:207340","NEWT:1006581","NEWT:8673","NEWT:33940","NEWT:550","NEWT:554","NEWT:451516","NEWT:552","NEWT:1325291","NEWT:36185","NEWT:1054211","NEWT:1225786","NEWT:771870","NEWT:51338","NEWT:575412","NEWT:28112","NEWT:6493","NEWT:10832","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:9983","NEWT:8655","NEWT:5147","NEWT:28108","NEWT:28104","NEWT:407821","NEWT:568703","NCBITaxon:2","NEWT:568708","NEWT:1613","NEWT:986","NEWT:52641","NEWT:28532","NEWT:353152","NEWT:298176","NEWT:227377","NEWT:1774284","NEWT:40674","NEWT:1194669","NEWT:443906","NEWT:519","NEWT:2510939","NEWT:7394","NEWT:6063","NEWT:1328388","NEWT:105487","NEWT:1548728","NEWT:667127","NEWT:9557","NEWT:377586","NEWT:300641","NEWT:39655","NEWT:9554","NEWT:38323","NEWT:475932","NEWT:256318","NEWT:206411","NCBITaxon:6191","NEWT:229533","NEWT:214053","NEWT:28550","NEWT:80863","NEWT:90675","NEWT:52639","NEWT:52638","NEWT:57075","NEWT:1666905","NEWT:8697","NEWT:8695","NEWT:884204","NEWT:1045775","NEWT:1123869","NEWT:9544","NEWT:9545","NEWT:979","NEWT:7370","NEWT:83906","NEWT:99488","NEWT:1134506","NEWT:255470","NEWT:38783","NEWT:6426","NEWT:33090","NEWT:9935","NEWT:287889","NEWT:305959","NEWT:1028307","NEWT:13489","NEWT:29829","NEWT:92867","NEWT:92866","NCBITaxon:3055","NEWT:51750","NEWT:202950","NEWT:441772",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