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Fujitani"],"software":[""],"tissue":["Epithelial Cell"],"sample_protocol":["Purified sFGFR3, with liquid chromatography AKTA GO system (Cytiva) with HisTrap HP for affinity chromatography, MonoQ 5/50 GL for anion exchange chromatography, and HiLoad 16/600 Superdex200pg for gel filtration, were reduced with 10 mM dithiothreitol (FUJIFILM Wako Pure Chemical) for 40 min at 56°C, followed by alkylation with 20 mM iodoacetamide (FUJIFILM Wako Pure Chemical) for 30 min at room temperature in the dark. The reductive alkylated samples were digested with 0.5 µg of sequence grade trypsin/Lys-C (Promega) for 16 h at 37°C. The resultant peptides were desalted with a styrene divinylbenzene polymer tip column (GL Science, Tokyo, Japan). Flow-through fractions that would contain more hydrophilic peptides, including glycopeptides, were further desalted on graphitized carbon tip columns (GL Science). The collected eluates were combined and evaporated on a centrifugal evaporator. Finally, the resulting desalted peptides were redissolved with 15 µL of ultrapure water containing 0.1% formic acid."],"repository":["Pride"],"labhead":["Motoko Takahashi"],"instrument_platform":[""],"submission_type":["COMPLETE"],"labhead_affiliation":["Sapporo Medical University School of Medicine"],"publication":["38244702 Hashimoto U, Fujitani N, Uehara Y, Okamoto H, Saitou A, Ito F, Ariki S, Shiratsuchi A, Hasegawa Y, Takahashi M. N-glycan on N262 of FGFR3 regulates the intracellular localization and phosphorylation of the receptor. Biochim Biophys Acta Gen Subj. 2024 1868(4):130565 10.1016/j.bbagen.2024.130565"],"submitter_affiliation":["Sapporo Medical University"],"labhead_mail":["takam@sapmed.ac.jp"],"technology_type":["Data-dependent acquisition","Mass Spectrometry","Bottom-up proteomics"],"disease":["Achondroplasia"],"submitter_keywords":["Fgfr3","N-glycoproteomics","Fibroblast growth factor receptor 3"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD047309"],"quantification_method":[""],"modification":[""],"data_protocol":["Acquired data were processed with MaxQuant software 1.6.3.3 (Cox and Mann 2008). The peptide searches referred to amino acid sequence data obtained from UniProt registration numbers P22607. Up to two trypsin miscleavage were allowed. For fragment ion match, a mass tolerance was set to 20 ppm. The false discovery rate was set to 0.01 for the identification of peptides. Methionine oxidation and acetylation of the protein N-terminus were set as variable modifications and carbamidomethyl on cysteine as a fixed modification. Glycopeptide identification was performed by manual analysis. First, the molecular weight values deconvolved on MaxQuant from the m/z and charge number of the precursor ions, along with the amino acid sequence of FGFR3, are entered into the GlycoMod Tool (https://web.expasy.org/glycomod/), molecular weight-based glycopeptide candidates are obtained. Then, to determine the authenticity of the proposed glycopeptides by GlycoMod Tool, all candidate precursor ions were visually confirmed with MaxQuant, referring to the oxonium ions (m/z 204.087 for HexNAc, m/z 274.092 for NeuAc-H2O, m/z 292.103 for NeuAc, and m/z 366.140 for Hex+HexNAc) and fragment ion for peptide+HexNAc in the MS/MS spectra. Relative abundance of glycopeptides and the glycosylation rate were estimated from the intensity of precursor ions."],"omics_type":["Proteomics"],"species":["Homo Sapiens (human)"],"submitter_mail":["fujitani@sapmed.ac.jp"],"curator_keywords":["Human proteome project","Biology/disease-driven human proteome project (b/d-hpp)","Glycoproteomics (b/d-hpp)"],"submitter_country":["Japan"],"doi":["10.6019/PXD047309"],"pubmed_abstract":["N-glycosylation and proper processing of N-glycans are required for the function of membrane proteins including cell surface receptors. Fibroblast growth factor receptor (FGFR) is involved in a wide variety of biological processes including embryonic development, osteogenesis, angiogenesis, and cell proliferation. Human FGFR3 contains six potential N-glycosylation sites, however, the roles of glycosylation have not been elucidated. The site-specific profiles of N-glycans of the FGFR3 extracellular domain expressed and secreted by CHO-K1 cells were examined, and glycan occupancies and structures of four sites were determined. The results indicated that most sites were fully occupied by glycans, and the dominant populations were the complex type. By examining single N-glycan deletion mutants of FGFR3, it was found that N262Q mutation significantly increased the population with oligomannose-type N-glycans, which was localized in the endoplasmic reticulum. Protein stability assay suggested that fraction with oligomannose-type N-glycans in the N262Q mutant is more stable than those in the wild type and other mutants. Furthermore, it was found that ligand-independent phosphorylation was significantly upregulated in N262Q mutants with complex type N-glycans. The findings suggest that N-glycans on N262 of FGFR3 affect the intracellular localization and phosphorylation status of the receptor."],"pubmed_title":["N-glycan on N262 of FGFR3 regulates the intracellular localization and phosphorylation of the receptor."],"pubmed_authors":["Hashimoto Ukichiro U, Fujitani Naoki N, Uehara Yasuaki Y, Okamoto Hiromi H, Saitou Atsushi A, Ito Fumie F, Ariki Shigeru S, Shiratsuchi Akiko A, Hasegawa Yoshihiro Y, Takahashi Motoko M"],"additional_accession":[]},"is_claimable":false,"name":"N-glycoproteomics of CHO cell-expressed FGFR3","description":"Receptor tyrosine kinases (RTKs) that undergo N-linked glycosylation undergo protein quality control in the endoplasmic reticulum (ER) and subsequently transfer to the Golgi apparatus, where they acquire a diverse array of glycan structures. The family of receptor tyrosine kinases (RTKs) known as FGFR (Fibroblast Growth Factor Receptor) possesses N-glycosylation potential sites within their extracellular domains. Mutations in the modification site of FGFR3 have been documented in conditions such as Achondroplasia (ACH) and hypochondroplasia (HCH). While it is believed that ACH and HCH are associated with the overactivity of FGFR3 and accumulation in the ER, there has yet to be a case where the root cause has been explained from the perspective of glycosylation. This study furnishes a site-specific profile of N-glycans on FGFR3 through structural analysis of the extracellular domain of FGFR3 containing N-glycosylation potential sites, conducted via nLC-MS/MS. Moreover, we generated mutants of FGFR3 with a single glycan deficiency at each site and examined the impact of N-glycans at these sites on the receptor. The findings demonstrated reduced phosphorylation in the N98 glycosylation deficient mutant and accumulation in the ER in the N262 glycosylation deficient mutant, indicating ligand-independent autophosphorylation of the receptor. Hence, it is proposed that N-glycans in FGFR3 may play a role in functional regulation, offering fresh perspectives on disease etiology from a glycosylation standpoint.","dates":{"publication":"2026-08-05","submission":"2023-11-28"},"accession":"PXD047309","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:247480","NEWT:1211601","NEWT:876138","NEWT:44271","NEWT:193516","NEWT:2315688","NEWT:1073882","NEWT:6819","NEWT:112509","NEWT:475174","NEWT:111205","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:381198","NEWT:418106","NCBITaxon:12721","NEWT:10029","NEWT:913645","NEWT:2492962","NEWT:641809","NEWT:1392488","NEWT:38815","NEWT:317447","NEWT:4688","NEWT:111225","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:55350","NEWT:1310161","NEWT:77133","NEWT:145481","NEWT:1310165","NEWT:29058","NCBITaxon:79824","NEWT:1912919","NEWT:410658","NEWT:5516","NEWT:44688","NEWT:44689","NEWT:498211","NEWT:345076","NEWT:347256","NEWT:5518","NEWT:398007","NEWT:1527468","NEWT:498217","NEWT:498216","NEWT:11320","NEWT:246196","NEWT:246197","NEWT:145458","NEWT:1310173","NEWT:200795","NEWT:2579791","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:717966","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:9006","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:2709072","NEWT:2499525","NEWT:2853422","NEWT:487","NEWT:1538553","NEWT:1679718","NEWT:480","NEWT:67767","NEWT:45972","NEWT:46835","NEWT:109757","NEWT:582580","NEWT:1185650","NEWT:216778","NEWT:294607","NEWT:1502","NEWT:128017","NEWT:2836","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:321967","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:29488","NEWT:215402","NEWT:1547","NEWT:1290454","NEWT:3726","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:542","NEWT:2903","NEWT:185579","NEWT:872227","NEWT:13076","NEWT:2587410","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:64657","NEWT:186441","NEWT:643680","NEWT:214092","NCBITaxon:6157","NEWT:13095","NEWT:162425","NEWT:104105","NEWT:216257","NEWT:9986","NEWT:86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