{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD047652/SampleKey.txt","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD047652/checksum.txt"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD047652/20220907_PHCOQEHF_PC1017-Mohlke_6.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD047652/20220907_PHCOQEHF_PC1017-Mohlke_2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD047652/20220614_PHCOQEHF_PC984-Mohlke_4.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD047652/20220907_PHCOQEHF_PC1017-Mohlke_9.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD047652/20220907_PHCOQEHF_PC1017-Mohlke_pooled2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD047652/20220614_PHCOQEHF_PC984-Mohlke_pooled_3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD047652/20220907_PHCOQEHF_PC1017-Mohlke_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD047652/20220614_PHCOQEHF_PC984-Mohlke_3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD047652/20220907_PHCOQEHF_PC1017-Mohlke_5.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD047652/20220907_PHCOQEHF_PC1017-Mohlke_pooled1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD047652/20220907_PHCOQEHF_PC1017-Mohlke_8.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD047652/20220614_PHCOQEHF_PC984-Mohlke_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD047652/20220614_PHCOQEHF_PC984-Mohlke_6.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD047652/20220614_PHCOQEHF_PC984-Mohlke_2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD047652/20220614_PHCOQEHF_PC984-Mohlke_pooled_2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD047652/20220907_PHCOQEHF_PC1017-Mohlke_4.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD047652/20220907_PHCOQEHF_PC1017-Mohlke_7.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD047652/20220614_PHCOQEHF_PC984-Mohlke_5.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD047652/20220907_PHCOQEHF_PC1017-Mohlke_3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD047652/20220614_PHCOQEHF_PC984-Mohlke_pooled_1.raw"],"Fasta":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD047652/Uniprot-Mouse-Rev_Jan2021_17051seq.fasta","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD047652/uniprot-Human-Mar2021_20396seq.fasta"],"Other":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD047652/PC1017txt.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD047652/PC984txt.zip"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["karen_mohlke@med.unc.edu"],"submitter":["Christine Mills"],"technology_type":["Affinity purification coupled with mass spectrometry proteomics","Mass Spectrometry"],"software":[""],"submitter_keywords":["Proinsulin","secretion","rab gtpase activating protein","insulin","Affinity purification-mass spectrometry","genome-wide association study","Proinsulin; insulin; secretion; genome-wide association study; rab gtpase activating protein"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD047652"],"sample_protocol":["We delivered purified TBC1D30-6xHis or empty vector (Zymo Quick-DNA Midiprep Plus kit) into HEK293T or MIN6 cells by transfection (Lipofectamine 2000) or electroporation (Neon system, 1300V/10ms/3 pulses, Thermo Fisher Scientific) respectively. Cell lysates were captured 48 hours after transfection or 72 hours after electroporation in NP-40 lysis buffer with protease and phosphatase inhibitors and total protein content quantified by BCA. To ensure we would capture interactions relevant to insulin secretion, we used glucose to stimulated MIN6 cells overexpressing TBC1D30-6xHis or a negative control empty vector. Specifically, 72 hours after electroporation, cells were stimulated with 18 mM glucose for 10 minutes or cultured in basal glucose for 90 minutes prior to lysis. We pulled down TBC1D30-6xHis and protein interactors in triplicate from total lysate using His-Tag Dynabeads (Thermo Fisher Scientific, 10104D), washed three times with lysis buffer containing protease and phosphatase inhibitors, incubated with either 5 mg (HEK293T) or 7.5 mg (MIN6) of lysate for 10 minutes, washed thoroughly to deplete nonspecific interactors, and resuspended beads in 100 µl ammonium bicarbonate per sample. Immunoprecipitated protein samples were subjected to on-bead trypsin digestion as previously described (Rank et al., J Bacteriol. Apr 2021). Briefly, on-bead digestion was performed by adding 1µg trypsin and incubated with shaking, overnight at 37ºC. The following day, 1µug trypsin (Promega) was added to each sample and incubated shaking, at 37ºC for 3 hours. Beads were pelleted and supernatants were transferred to fresh tubes. The beads were washed twice with 100µl LC-MS grade water, and washes were added to the original supernatants. Samples were acidified by adding trifluoroacetic acid (Thermo)TFA to final concentration of 2%, to pH ~2. Peptides were desalted using peptide desalting spin columns (Thermo), lyophilized, and stored at -80ºC until further analysis."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["Raw data files were searched against the reviewed mouse database (containing 17,137 entries), appended with a contaminants database, using Andromeda within MaxQuant (version 1.6.15.0). Enzyme specificity was set to trypsin, up to two missed cleavage sites were allowed, and methionine oxidation and N-terminus acetylation were set as variable modifications. A 1% FDR was used to filter all data. Match between runs was enabled (5 min match time window, 20 min alignment window), and a minimum of two unique peptides was required for label-free quantitation using the LFQ intensities. Perseus was used for further processing (Tyanova et al. Nat Methods Sept 2016). Only proteins with >1 unique+razor peptide were used for LFQ analysis. Proteins with 50% missing values were removed and missing values were imputed from normal distribution within Perseus. Log2 fold change (FC) ratios were calculated using the averaged Log2 LFQ intensities of sample compared to control, and students t-test performed for each pairwise comparison, with p-values calculated. Proteins with significant p-values (<0.05) and Log2 FC >1 were considered biological interactors."],"omics_type":["Proteomics"],"labhead":["Karen Mohlke"],"instrument_platform":[""],"submission_type":["PARTIAL"],"labhead_affiliation":["Department of Genetics, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina 27599, USA"],"species":["Homo Sapiens (human)","Mus Musculus (mouse)"],"publication":["40064677 Parsons VA, Vadlamudi S, Voos KM, Rohy AE, Moxley AH, Cannon ME, Rosen JD, Mills CA, Herring LE, Broadaway KA, Lorenzo DN, Mohlke KL. TBC1D30 regulates proinsulin and insulin secretion and is the target of a genomic association signal for proinsulin. Diabetologia. 2025 68(6):1169-1183 10.1007/s00125-025-06391-w"],"submitter_mail":["allie.mills@unc.edu"],"submitter_affiliation":["University of North Carolina - Chapel Hill"],"submitter_country":["United States"],"pubmed_abstract":["<h4>Aims/hypothesis</h4>Components of the insulin processing and secretion pathways remain incompletely understood. Here, we examined a genome-wide association study (GWAS) signal for plasma proinsulin levels. Lead GWAS variant rs150781447-T encodes an Arg279Cys substitution in TBC1 domain family member 30 (TBC1D30), but no role for this protein in insulin processing or secretion has been established previously. This study aimed to evaluate whether TBC1D30 drives the GWAS association signal by determining whether TBC1D30 is involved in proinsulin secretion and, if so, to examine the effects of variant alleles and potential mechanisms.<h4>Methods</h4>Using CRISPR/Cas9 genome editing to create double-strand breaks and prime editing to install substitutions in INS1 832/13 insulinoma cells, we generated clonal cell lines with altered TBC1D30, as well as homozygous and heterozygous lines carrying the lead GWAS variant. We characterised lines by Sanger sequencing, quantitative PCR and ELISAs to measure glucose-stimulated proinsulin and insulin secretion. We also tested the effects of TBC1D30 knockdown on proinsulin and insulin secretion in human islets. We further assessed TBC1D30's contribution to secretory pathways by examining the effects of altered gene function on intracellular proinsulin and insulin content and insulin localisation, and by identifying potential proteins that interact with TBC1D30 using affinity purification mass spectrometry.<h4>Results</h4>Compared with mock-edited cells, cell lines with reduced TBC1D30 expression or altered Rab GTPase-activating protein (RabGAP) domain had significantly more secreted proinsulin, 1.8- and 2.6-fold more than controls, respectively. Similarly, cells expressing the variant substitution demonstrated increased proinsulin secretion. Cell lines with a partial deletion of a critical functional domain showed 1.8-fold higher expression of Tbc1d30 and at least 2.0-fold less secreted proinsulin. Cells with altered RabGAP domain sequence also demonstrated, to a lesser extent, changes in secreted insulin levels. TBC1D30 knockdown in human islets resulted in increased insulin secretion with no significant effect on proinsulin secretion. The effects of altered TBC1D30 on mislocalisation of insulin, intracellular proinsulin and insulin content and the identities of interacting proteins are consistent with a role for TBC1D30 in proinsulin and insulin secretion.<h4>Conclusions/interpretation</h4>These findings suggest that effects on TBC1D30 are responsible for the GWAS signal and that TBC1D30 plays a critical role in the secretion of mature insulin."],"pubmed_title":["TBC1D30 regulates proinsulin and insulin secretion and is the target of a genomic association signal for proinsulin."],"pubmed_authors":["Parsons Victoria A VA, Vadlamudi Swarooparani S, Voos Kayleigh M KM, Rohy Abigail E AE, Moxley Anne H AH, Cannon Maren E ME, Rosen Jonathan D JD, Mills Christine A CA, Herring Laura E LE, Broadaway K Alaine KA, Lorenzo Damaris N DN, Mohlke Karen L KL"],"additional_accession":[]},"is_claimable":false,"name":"Identification of TBC1D30 interactors in murine MIN6 insulinoma cells.","description":"Components of the insulin processing and secretion pathways remain incompletely understood. Here we examined a genome-wide association study (GWAS) locus associated with plasma proinsulin levels. Low-frequency GWAS variant rs150781447 encodes an Arg279Cys substitution in TBC1D30, but no role for this protein in insulin processing or secretion has been previously established. Using CRISPR/Cas9 genome editing in INS1 832/13 insulinoma cells, we generated clonal cell lines with altered TBC1D30. Compared to mock-edited cells, cell lines with reduced TBC1D30 expression or function showed significantly more secreted proinsulin, and to a lesser extent, secreted insulin. Cell lines with a partial deletion of a key functional domain showed increased expression of TBC1D30 and less secreted proinsulin. The effects on secretion corresponded to effects on intracellular proinsulin and insulin content. The interactome of TBC1D30, identified through affinity purification-mass spectrometry, was enriched in proteins involved in insulin trafficking and secretion. These findings suggest that the effects of rs150781447 on TBC1D30 are responsible for this GWAS signal and that TBC1D30 plays a critical role in the secretion of mature insulin.","dates":{"publication":"2026-06-08","submission":"2023-12-08"},"accession":"PXD047652","cross_references":{"TAXONOMY":["NEWT:330879","NEWT:377960","NEWT:1131","NEWT:35795","NEWT:2042546","NEWT:259447","NEWT:295546","NCBITaxon:2719036","NEWT:1334565","NEWT:625351","NEWT:258594","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:2315688","NEWT:1073882","NEWT:6819","NEWT:475174","NEWT:428386","NEWT:1117","NEWT:498257","NEWT:10036","NEWT:32264","NEWT:12215","NEWT:1590","NEWT:10034","NEWT:33114","NEWT:1596","NEWT:661410","NEWT:638632","NEWT:224326","NEWT:376619","NCBITaxon:79857","NEWT:1096976","NEWT:3765","NEWT:3767","NEWT:1589","NEWT:135622","NEWT:4615","NEWT:672127","NEWT:35786","NEWT:1580","NEWT:399784","NEWT:96731","NEWT:656064","NEWT:1582","NEWT:3760","NEWT:1584","NEWT:36630","NEWT:1585","NEWT:383379","NEWT:418106","NCBITaxon:12721","NEWT:10029","NEWT:913645","NEWT:2492962","NEWT:641809","NEWT:1392488","NEWT:38815","NEWT:317447","NEWT:4688","NEWT:7719","NEWT:5530","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:49928","NEWT:3349","NEWT:160621","NEWT:212790","NEWT:110368","NEWT:1310161","NEWT:77133","NEWT:145481","NEWT:1310165","NEWT:29058","NCBITaxon:79824","NEWT:410658","NEWT:5516","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:1310173","NEWT:44685","NEWT:161934","NEWT:156587","NEWT:1148","NEWT:5508","NEWT:3329","NEWT:419481","NEWT:5507","NEWT:260499","NEWT:410661","NEWT:1140","NCBITaxon:2157","NEWT:2066563","NEWT:1143","NEWT:1287689","NEWT:1094343","NEWT:1462472","NEWT:1336795","NEWT:644042","NEWT:150808","NEWT:1182590","NEWT:3712","NEWT:3711","NEWT:3714","NCBITaxon:37162","NEWT:270643","NEWT:2065263","NEWT:177437","NEWT:10891","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:176597","NEWT:118694","NEWT:2850","NEWT:118691","NEWT:34871","NEWT:33548","NEWT:52299","NEWT:8165","NEWT:96794","NEWT:3708","NEWT:332648","NEWT:44670","NEWT:926571","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:1538553","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","EFO:0001352","NEWT:119562","NEWT:1883446","NEWT:1233435","NEWT:118223","NEWT:11757","NEWT:987059","NEWT:109760","NEWT:29031","NEWT:317047","NEWT:1509","NEWT:491","NEWT:460523","NEWT:45954","NEWT:235443","NEWT:1579","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:191701","NEWT:373153","NEWT:1640278","NEWT:472","NEWT:940825","NEWT:29459","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:11723","NEWT:445","NEWT:153009","NEWT:261756","NEWT:166313","NEWT:63366","NEWT:63367","NEWT:215402","NEWT:1547","NEWT:1290454","NEWT:906914","NEWT:81231006","NEWT:28141","NEWT:9031","NEWT:27292","NEWT:1050722","NEWT:3728","NEWT:108931","NEWT:1293497","NEWT:1055524","NEWT:548","NEWT:150475","NEWT:267872","NEWT:381666","NEWT:172269","NEWT:9534","NEWT:2126348","NEWT:5180","NEWT:256737","NEWT:9541","NEWT:8694","NEWT:33936","NEWT:8692","NEWT:2903","NEWT:185579","NEWT:872227","NEWT:13076","NEWT:207340","NEWT:1006581","NEWT:8673","NEWT:33940","NEWT:2126337","NEWT:550","NEWT:33941","NEWT:554","NEWT:451516","NEWT:552","NEWT:1325291","NEWT:42410","NEWT:36185","NEWT:1054211","NEWT:1225786","NEWT:771870","NEWT:51338","NEWT:9995","NEWT:575412","NEWT:28112","NEWT:49012","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:353153","NEWT:227377","NEWT:1774284","NEWT:40674","NEWT:11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