{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Tabular":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD076503/report.pg_matrix.tsv","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD076503/report.pr_matrix.tsv","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD076503/report.tsv"],"Xlsx":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD076503/UP_JC_Peptide_Quant_100424.xlsx"],"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD076503/checksum.txt"],"Pdf":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD076503/diann_report.pdf"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD076503/ESC-rep2_soluble_100724_3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD076503/ESC-rep1_soluble_100724_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD076503/ESC-rep2_insoluble_100724_3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD076503/ESC-rep1_insoluble_100724_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD076503/ESC-rep1_soluble_100724_2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD076503/ESC-rep1_insoluble_100724_2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD076503/TSC_soluble_100724_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD076503/TSC_insoluble_100724_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD076503/ESC-rep2_soluble_100724_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD076503/ESC-rep1_soluble_100724_3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD076503/ESC-rep1_insoluble_100724_3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD076503/ESC-rep2_insoluble_100724_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD076503/TSC_soluble_100724_2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD076503/TSC_insoluble_100724_2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD076503/TSC_insoluble_100724_3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD076503/ESC-rep2_insoluble_100724_2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD076503/ESC-rep2_soluble_100724_2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD076503/TSC_soluble_100724_3.raw"],"Fasta":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD076503/uniprotkb_H_sapiens_w_Hao_Contams.fasta"]},"type":"primary"},"statusCodeValue":200,"statusCode":"OK"}],"scores":null,"additional":{"labhead_mail":["marcotte@utexas.edu"],"submitter":["Ujwal Punyamurtula"],"technology_type":["Mass Spectrometry","Bottom-up proteomics","Data-independent acquisition"],"software":[""],"submitter_keywords":[""],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD076503"],"tissue":["Embryo","Placenta","Cell Culture","Placental Villous Trophoblast","Embryonic Stem Cell"],"sample_protocol":["H9 human ES cells (WiCell) were cultured on plates coated with Matrigel (Corning, 354234) in mTeSR Plus medium (Stemcell Technologies, 100-0276). Cells were maintained at 37°C in a humidified incubator with 5% CO₂ and passaged every 4–5 days using ReLeSR (Stemcell technologies, 100-0483). CT27 human trophoblast stem cells (TSCs; kindly provided by Dr. Takahiro Arima, Tohoku University). The cells were cultured on plates coated with 0.05% iMatrix-511 (Iwai North America, N-892012). The medium consisted of DMEM/F12 medium (Thermo Fisher Scientific, 11320082) supplemented with 0.15% BSA (MilliporeSigma, A7906), 0.6% Penicillin-Streptomycin (Thermo Fisher Scientific, 15140-122), 1% ITS-X supplement (Thermo Fisher Scientific, 5150056), 1% KnockOut Serum Replacement (Thermo Fisher Scientific, 10828028), 0.2 mM L-ascorbic acid (Wako, 013-12061), 2.5 µM Y27632 (Selleck Chemicals, S1049), 25 ng/ml EGF (PeproTech, AF-100-15), 0.8 mM VPA (Wako, 227-01071), 2 µM CHIR99021 (Selleck Chemicals, S2924), and 5 μM A83-01 (MilliporeSigma, SML0788). Cells were maintained at 37°C in a humidified incubator with 5% CO₂ and passaged every 3–4 days with TrypLE Select Enzyme (Thermo Fisher Scientific, A1217701). H9 and CT27 were washed three times with ice cold PBS. The cells were then scrapped off the plates with a cell lifter (Corning, 3008) then centrifuged (5 min, 4,226g, 4°C). Remaining PBS supernatant was aspirated and the pellet was kept in -80°C until protein analysis. Harvested human trophoblast stem cell (hTSC; CT27) and human embryonic stem cell (hESC; H9) pellets were lysed by resuspending in Pierce IP Lysis buffer (3:1 v/v ratio of lysis buffer:sample; 25mM Tris-HCl pH 7.4, 150mM NaCl, 1mM EDTA, 1% NP-40 and 5% glycerol; Thermo Fisher) containing 1x cOmplete mini EDTA-free protease inhibitor (Roche) and 1x PhosSTOP EASYpack phosphatase inhibitor (Roche). These resuspended samples were incubated on ice for 5 minutes and vortexed periodically. To help separate subcellular components into insoluble and soluble fractions, the resulting cell lysates were homogenized using a 7mL KIMBLE Dounce tissue grinder set (Millipore) with 5 passes of pestle A and 45 passes of pestle B. To further clarify insoluble and soluble components, the homogenized cell lysates were flash-frozen with liquid nitrogen and thawed immediately by hand. Finally, to obtain separated insoluble and soluble fractions, the cell lysates were centrifuged at 14,000g for 20 min at 4oC. The pellet fraction samples (for hESC and hTSC samples) were resuspended in 100uL of Pierce IP lysis buffer and subjected to another freeze-thaw cycle to break apart insoluble material before flash-freezing for overnight storage. To solubilize the samples, SDS was added to 2% of the final volume, after which samples were heated to 95oC for 15 minutes. Subsequently, samples were diluted in a 6:1 acetone/sample volume ratio with ice-cold acetone (previously cooled to -20oC) and incubated overnight (~15 hours) at 4oC. Acetone-treated samples were centrifuged (16,600g, 15 min, 4oC) and the supernatant was discarded. Sample precipitates were washed twice with 400uL acetone (16,000g, 20 min, 4oC). To solubilize the proteins in the precipitate (and enable in-solution digestion), sample precipitates were resuspended in 50uL 1% SDC/50mM NH4HCO3 and sonicated twice for 10 min. Solubilized proteins were reduced with TCEP (final concentration: 5mM) at 56oC for 45 minutes and then alkylated with 25mM IAM for 45 minutes in the dark at RT. After quenching unreacted IAM with 12mM DTT, proteins were digested overnight (~15 hours at 37oC) with 2ug proteomics grade trypsin. After quenching the tryptic digestion with 1% formic acid, samples were centrifuged (16,000g, 10 min, 4oC) to remove the precipitated SDC. Samples were then filtered (14,000g, 20 min, 4oC) using Amicon Ultra 10kDa filters (Millipore) and dried via speed vacuum centrifugation for 1 hour. Samples were then processed using 6ug C18 ZipTip pipette tips (Millipore), eluted, dried once more by speed vacuum centrifugation, and resuspended in 5% acetonitrile/0.1% formic acid for LC-MS/MS analysis. Peptides were separated via reverse phase chromatography using a Dionex Ultimate 3000 RSLCnano UHPLC system (Thermo Scientific) on an EASY-Spray PepMap RSLC C18 column (Thermo Scientific, ES902). Peptides were eluted using a 3%-45% acetonitrile gradient in 0.1% formic acid over 120 minutes. The mass spectra of LC-separated peptides were acquired on a Thermo Orbitrap Fusion Lumos mass spectrometer configured to acquire DIA spectra using 42 x 12 m/z sequential precursor isolation windows at 15,000 resolution across a precursor mass range of 400 - 900 m/z. After each pass through the precursor mass range (i.e. after 42 DIA MS/MS scans) a full precursor MS scan was performed (400-1600 m/z, 120,000 resolution, AGC target 4e5)."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["Mass spectrometry data analysis DIA MS/MS experiments were searched using the DIA-NN platform [PMID: 31768060], with a predicted spectral library generated from a Uniprot protein FASTA file for Homo sapiens (downloaded 10/09/2023). The DIA-NN search utilized standard settings (trypsin digestion with up to one missed cleavage, deep learning-based spectra/RT/IM prediction, fixed cysteine carbamidomethylation, N-terminal methionine excision, and a precursor FDR of 1%). For each subcellular fraction in each cell type (i.e. TSC insoluble, TSC soluble, ESC insoluble, ESC soluble), three technical replicates were collected."],"omics_type":["Proteomics"],"labhead":["Edward Marcotte"],"instrument_platform":[""],"labhead_affiliation":["Edward M. Marcotte, PhD Center for Systems and Synthetic Biology Department of Molecular Biosciences University of Texas at Austin 2500 Speedway, MBB 3.148BA Austin, TX 78712-0159"],"submission_type":["PARTIAL"],"species":["Homo Sapiens (human)"],"submitter_mail":["usnpunyam@utexas.edu"],"publication":["42345196 Lee M, Jang Y, Guo Q, Punyamurtula U, Choi J, Kim J, Marcotte EM. Identifying membrane-bound transcriptional regulatory proteins from rare but evolutionarily conserved domain combinations. Nucleic Acids Res. 2026 54(12):gkag635 10.1093/nar/gkag635"],"submitter_affiliation":["The University of Texas at Austin"],"submitter_country":["United States"],"pubmed_abstract":["Transcriptional regulatory proteins, including transcription factors (TFs) and chromatin modifiers, must act inside cell nuclei, but membrane-bound transcription factors (MBTFs) are first anchored in membranes before nuclear translocation. Known MBTFs are vital for processes from myelin expression (MYRF) to cholesterol homeostasis (SREBP), yet their overall diversity remains uncharted. We hypothesized that additional membrane-bound transcriptional regulators (MBTRs) might exist, so we developed a bioinformatics screen to prioritize membrane proteins that are likely to regulate transcription. Our approach leverages domain composition by positing that unusual domain combinations suggest novel biological functions. We searched for rare but evolutionarily conserved pairings of transmembrane domains with domains likely involved in transcriptional regulation. Our method rediscovered known MBTFs and membrane-bound histone kinases, and identified novel MBTR candidates, including transmembrane histone N-acetyltransferases, a putative new subclass of MBTFs that shares the DNA-binding domain of MYRF, and the prolactin regulatory element-binding protein PREB (SEC12). Assays using recombinant PREB demonstrated that the transmembrane domain is the determinant of PREB subcellular localization, governing its distribution between the membrane and the nucleus in mouse embryonic stem cells. These findings underscore the utility of our method and provide a framework for investigating MBTRs that likely facilitate the integration of extracellular signals with transcriptional responses."],"pubmed_title":["Identifying membrane-bound transcriptional regulatory proteins from rare but evolutionarily conserved domain combinations."],"pubmed_authors":["Lee Muyoung M, Jang Yeejin Y, Guo Qingqing Q, Punyamurtula Ujwal U, Choi Joonhyuk J, Kim Jonghwan J, Marcotte Edward M EM"],"additional_accession":[]},"is_claimable":false,"name":"Identifying membrane-bound transcriptional regulatory proteins from rare but evolutionarily conserved domain combinations","description":"Transcriptional regulatory proteins, including transcription factors (TFs) and chromatin modifiers, must act inside cell nuclei, but membrane-bound transcription factors (MBTFs) are first anchored in membranes before nuclear translocation. Known MBTFs are vital for processes from myelin expression (MYRF) to cholesterol homeostasis (SREBP), yet their overall diversity remains uncharted. We hypothesized that additional membrane-bound transcriptional regulators (MBTRs) might exist, so we developed a bioinformatics screen to prioritize membrane proteins that are likely to regulate transcription. Our approach leverages domain composition by positing that surprising domain combinations suggest novel biological functions. We searched for rare but evolutionarily conserved pairings of transmembrane domains with domains likely involved in transcriptional regulation. Our method rediscovered known MBTFs and membrane-bound histone kinases, and identified novel MBTR candidates, including transmembrane histone N-acetyltransferases, a putative new subclass of MBTFs that share MYRF's DNA-binding domain, and the prolactin regulatory element-binding protein PREB (SEC12). Assays using recombinant PREB demonstrated that the transmembrane domain is the determinant of PREB subcellular localization, governing its distribution between the membrane and the nucleus in mouse embryonic stem cells. These findings underscore the utility of our method and provide a framework for investigating MBTRs that likely facilitate the integration of extracellular signals with transcriptional responses.","dates":{"publication":"2026-06-29","submission":"2026-04-02"},"accession":"PXD076503","cross_references":{"TAXONOMY":["NEWT:68239","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:2433","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:2492962","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:156587","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:28174","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:2709072","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:1380096","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:29486","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:536","NEWT:8658","NEWT:1268063","NEWT:8657","NEWT:9983","NEWT:8655","NEWT:595495","NEWT:80833","NEWT:479096","NEWT:28108","NEWT:28104","NEWT:1114957","NEWT:568703","NEWT:568708","NEWT:52641","NEWT:353152","NEWT:116597","NEWT:353153","NEWT:116598","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:38323","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:510516","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:9938","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:11294","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:1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