ID OST48_HUMAN Reviewed; 456 AA. AC P39656; B2RDQ4; B4DJE3; B4DLI2; O43244; Q5VWA5; Q8NI93; Q9BUI2; DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot. DT 16-JUN-2009, sequence version 4. DT 02-SEP-2026, entry version 226. DE RecName: Full=Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 48 kDa subunit {ECO:0000305}; DE Short=DDOST 48 kDa subunit; DE Short=Oligosaccharyl transferase 48 kDa subunit; DE Flags: Precursor; GN Name=DDOST {ECO:0000312|HGNC:HGNC:2728}; Synonyms=KIAA0115, OST48; GN ORFNames=OK/SW-cl.45; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT GLY-8. RX PubMed=9367678; DOI=10.1006/geno.1997.4966; RA Yamagata T., Tsuru T., Momoi M.Y., Suwa K., Nozaki Y., Mukasa T., RA Ohashi H., Fukushima Y., Momoi T.; RT "Genome organization of human 48-kDa oligosaccharyltransferase (DDOST)."; RL Genomics 45:535-540(1997). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT GLY-8. RC TISSUE=Bone marrow; RX PubMed=7788527; DOI=10.1093/dnares/2.1.37; RA Nagase T., Miyajima N., Tanaka A., Sazuka T., Seki N., Sato S., Tabata S., RA Ishikawa K., Kawarabayasi Y., Kotani H., Nomura N.; RT "Prediction of the coding sequences of unidentified human genes. III. The RT coding sequences of 40 new genes (KIAA0081-KIAA0120) deduced by analysis of RT cDNA clones from human cell line KG-1."; RL DNA Res. 2:37-43(1995). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3), AND VARIANT RP GLY-8. RC TISSUE=Subthalamic nucleus, Synovium, and Umbilical cord blood; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT GLY-8. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT GLY-8. RC TISSUE=Brain; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 9-456 (ISOFORM 1). RC TISSUE=Colon adenocarcinoma; RA Shichijo S., Itoh K.; RT "Identification of immuno-peptidmics that are recognized by tumor-reactive RT CTL generated from TIL of colon cancer patients."; RL Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases. RN [8] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [9] RP FUNCTION. RX PubMed=22467853; DOI=10.1242/jcs.103952; RA Roboti P., High S.; RT "The oligosaccharyltransferase subunits OST48, DAD1 and KCP2 function as RT ubiquitous and selective modulators of mammalian N-glycosylation."; RL J. Cell Sci. 125:3474-3484(2012). RN [10] RP IDENTIFICATION IN THE OLIGOSACCHARYLTRANSFERASE COMPLEX. RX PubMed=25135935; DOI=10.1083/jcb.201404083; RA Cherepanova N.A., Shrimal S., Gilmore R.; RT "Oxidoreductase activity is necessary for N-glycosylation of cysteine- RT proximal acceptor sites in glycoproteins."; RL J. Cell Biol. 206:525-539(2014). RN [11] RP IDENTIFICATION IN THE OLIGOSACCHARYLTRANSFERASE COMPLEX. RX PubMed=23606741; DOI=10.1242/jcs.115410; RA Dumax-Vorzet A., Roboti P., High S.; RT "OST4 is a subunit of the mammalian oligosaccharyltransferase required for RT efficient N-glycosylation."; RL J. Cell Sci. 126:2595-2606(2013). RN [12] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [13] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [14] RP INTERACTION WITH SMIM22. RX PubMed=29765154; DOI=10.1038/s41388-018-0281-5; RA Polycarpou-Schwarz M., Gross M., Mestdagh P., Schott J., Grund S.E., RA Hildenbrand C., Rom J., Aulmann S., Sinn H.P., Vandesompele J., RA Diederichs S.; RT "The cancer-associated microprotein CASIMO1 controls cell proliferation and RT interacts with squalene epoxidase modulating lipid droplet formation."; RL Oncogene 37:4750-4768(2018). RN [15] {ECO:0007744|PDB:6S7O, ECO:0007744|PDB:6S7T} RP STRUCTURE BY ELECTRON MICROSCOPY (3.50 ANGSTROMS), IDENTIFICATION OF THE RP OLIGOSACCHARYLTRANSFERASE (OST) COMPLEX, FUNCTION, AND PATHWAY. RX PubMed=31831667; DOI=10.1126/science.aaz3505; RA Ramirez A.S., Kowal J., Locher K.P.; RT "Cryo-electron microscopy structures of human oligosaccharyltransferase RT complexes OST-A and OST-B."; RL Science 366:1372-1375(2019). RN [16] {ECO:0007744|PDB:8B6L} RP STRUCTURE BY ELECTRON MICROSCOPY (7.60 ANGSTROMS) OF THE STT3A-CONTAINING RP OLIGOSACCHARYLTRANSFERASE (OST) AND TRANSLOCON COMPLEXES, AND SUBUNIT. RX PubMed=36697828; DOI=10.1038/s41586-022-05638-5; RA Gemmer M., Chaillet M.L., van Loenhout J., Cuevas Arenas R., Vismpas D., RA Grollers-Mulderij M., Koh F.A., Albanese P., Scheltema R.A., Howes S.C., RA Kotecha A., Fedry J., Forster F.; RT "Visualization of translation and protein biogenesis at the ER membrane."; RL Nature 614:160-167(2023). RN [17] {ECO:0007744|PDB:8PN9} RP STRUCTURE BY ELECTRON MICROSCOPY (3.61 ANGSTROMS) OF THE STT3A-CONTAINING RP OLIGOSACCHARYLTRANSFERASE (OST), AND SUBUNIT. RX PubMed=38670073; DOI=10.1016/j.cell.2024.03.022; RA Lampson B.L., Ramrez A.S., Baro M., He L., Hegde M., Koduri V., Pfaff J.L., RA Hanna R.E., Kowal J., Shirole N.H., He Y., Doench J.G., Contessa J.N., RA Locher K.P., Kaelin W.G.; RT "Positive selection CRISPR screens reveal a druggable pocket in an RT oligosaccharyltransferase required for inflammatory signaling to NF- RT kappaB."; RL Cell 187:2209-2223(2024). RN [18] RP VARIANT CDG1R ASP-217. RX PubMed=22305527; DOI=10.1016/j.ajhg.2011.12.024; RA Jones M.A., Ng B.G., Bhide S., Chin E., Rhodenizer D., He P., Losfeld M.E., RA He M., Raymond K., Berry G., Freeze H.H., Hegde M.R.; RT "DDOST mutations identified by whole-exome sequencing are implicated in RT congenital disorders of glycosylation."; RL Am. J. Hum. Genet. 90:363-368(2012). CC -!- FUNCTION: Subunit of the oligosaccharyl transferase (OST) complex that CC catalyzes the initial transfer of a defined glycan CC (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol- CC pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr CC consensus motif in nascent polypeptide chains, the first step in CC protein N-glycosylation (PubMed:31831667). N-glycosylation occurs CC cotranslationally and the complex associates with the Sec61 complex at CC the channel-forming translocon complex that mediates protein CC translocation across the endoplasmic reticulum (ER). All subunits are CC required for a maximal enzyme activity (By similarity). Required for CC the assembly of both SST3A- and SS3B-containing OST complexes CC (PubMed:22467853). {ECO:0000250|UniProtKB:Q05052, CC ECO:0000269|PubMed:22467853, ECO:0000269|PubMed:31831667}. CC -!- PATHWAY: Protein modification; protein glycosylation. CC {ECO:0000269|PubMed:31831667}. CC -!- SUBUNIT: Component of the oligosaccharyltransferase (OST) complex CC (PubMed:31831667, PubMed:36697828, PubMed:38670073). OST exists in two CC different complex forms which contain common core subunits RPN1, RPN2, CC OST48, OST4, DAD1 and TMEM258, either STT3A or STT3B as catalytic CC subunits, and form-specific accessory subunits (PubMed:23606741, CC PubMed:25135935, PubMed:31831667, PubMed:36697828, PubMed:38670073). CC STT3A complex assembly occurs through the formation of 3 subcomplexes. CC Subcomplex 1 contains RPN1 and TMEM258, subcomplex 2 contains the CC STT3A-specific subunits STT3A, DC2/OSTC, and KCP2 as well as the core CC subunit OST4, and subcomplex 3 contains RPN2, DAD1, and OST48. The CC STT3A complex can form stable complexes with the Sec61 complex or with CC both the Sec61 and TRAP complexes (By similarity). Interacts with CC SMIM22 (PubMed:29765154). {ECO:0000250|UniProtKB:Q05052, CC ECO:0000269|PubMed:23606741, ECO:0000269|PubMed:25135935, CC ECO:0000269|PubMed:29765154, ECO:0000269|PubMed:31831667, CC ECO:0000269|PubMed:36697828, ECO:0000269|PubMed:38670073}. CC -!- INTERACTION: CC P39656; Q86WV6: STING1; NbExp=2; IntAct=EBI-358866, EBI-2800345; CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane CC {ECO:0000250|UniProtKB:Q29381}; Single-pass type I membrane protein CC {ECO:0000250|UniProtKB:Q29381}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=P39656-1; Sequence=Displayed; CC Name=2; CC IsoId=P39656-2; Sequence=VSP_055498; CC Name=3; CC IsoId=P39656-3; Sequence=VSP_055499; CC -!- DISEASE: Congenital disorder of glycosylation 1R (CDG1R) [MIM:614507]: CC A form of congenital disorder of glycosylation, a multisystem disorder CC caused by a defect in glycoprotein biosynthesis and characterized by CC under-glycosylated serum glycoproteins. Congenital disorders of CC glycosylation result in a wide variety of clinical features, such as CC defects in the nervous system development, psychomotor retardation, CC dysmorphic features, hypotonia, coagulation disorders, and CC immunodeficiency. The broad spectrum of features reflects the critical CC role of N-glycoproteins during embryonic development, differentiation, CC and maintenance of cell functions. {ECO:0000269|PubMed:22305527}. CC Note=The disease is caused by variants affecting the gene represented CC in this entry. CC -!- SIMILARITY: Belongs to the DDOST 48 kDa subunit family. {ECO:0000305}. CC -!- CAUTION: It is uncertain whether Met-1 or Met-18 is the initiator. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAB93478.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; D89060; BAA23670.1; -; Genomic_DNA. DR EMBL; D29643; BAA06126.1; -; mRNA. DR EMBL; AK296041; BAG58805.1; -; mRNA. DR EMBL; AK297009; BAG59544.1; -; mRNA. DR EMBL; AK315633; BAG38001.1; -; mRNA. DR EMBL; AL391357; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471134; EAW94938.1; -; Genomic_DNA. DR EMBL; BC002594; AAH02594.1; -; mRNA. DR EMBL; AB062391; BAB93478.1; ALT_INIT; mRNA. DR PIR; S66254; A44654. DR RefSeq; NP_005207.3; NM_005216.5. DR PDB; 6S7O; EM; 3.50 A; G=1-456. DR PDB; 6S7T; EM; 3.50 A; G=1-456. DR PDB; 8B6L; EM; 7.60 A; N=1-456. DR PDB; 8PN9; EM; 3.61 A; G=1-452. DR PDB; 9N9J; EM; 3.20 A; N2=1-456. DR PDB; 9YGY; EM; 4.10 A; N2=1-456. DR AlphaFoldDB; P39656; -. DR EMDB; EMD-15870; -. DR EMDB; EMD-17779; -. DR EMDB; EMD-49171; -. DR EMDB; EMD-72945; -. DR SMR; P39656; -. DR BioGRID; 108017; 435. DR ComplexPortal; CPX-5621; Oligosaccharyltransferase complex A. DR ComplexPortal; CPX-5622; Oligosaccharyltransferase complex B, MAGT1 variant. DR ComplexPortal; CPX-8738; Oligosaccharyltransferase complex B, TUCS3 variant. DR CORUM; P39656; -. DR FunCoup; P39656; 3096. DR IntAct; P39656; 246. DR MINT; P39656; -. DR NDEx; IQUERY-CP-DDOST; 2 NDEx IQuery Curated Pathways. DR STRING; 9606.ENSP00000399457; -. DR BindingDB; P39656; -. DR ChEMBL; CHEMBL4239; -. DR TCDB; 9.B.142.3.17; the integral membrane glycosyltransferase family 39 (gt39) family. DR GlyGen; P39656; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P39656; -. DR PhosphoSitePlus; P39656; -. DR SwissPalm; P39656; -. DR BioMuta; DDOST; -. DR DMDM; 239938926; -. DR CPTAC; CPTAC-349; -. DR CPTAC; CPTAC-350; -. DR jPOST; P39656; -. DR MassIVE; P39656; -. DR PaxDb; 9606-ENSP00000399457; -. DR PeptideAtlas; P39656; -. DR ProteomicsDB; 55317; -. [P39656-1] DR Pumba; P39656; -. DR TopDownProteomics; P39656-1; -. [P39656-1] DR Antibodypedia; 29811; 243 antibodies from 26 providers. DR DNASU; 1650; -. DR Ensembl; ENST00000415136.6; ENSP00000399457.3; ENSG00000244038.11. [P39656-1] DR GeneID; 1650; -. DR KEGG; hsa:1650; -. DR UCSC; uc001bdo.1; human. [P39656-1] DR AGR; HGNC:2728; -. DR ClinPGx; PA27195; -. DR CTD; 1650; -. DR DisGeNET; 1650; -. DR GeneCards; DDOST; -. DR GeneReviews; DDOST; -. DR HGNC; HGNC:2728; DDOST. DR HPA; ENSG00000244038; Low tissue specificity. DR MalaCards; DDOST; -. DR MIM; 602202; gene. DR MIM; 614507; phenotype. DR OpenTargets; ENSG00000244038; -. DR Orphanet; 300536; DDOST-CDG. DR VEuPathDB; HostDB:ENSG00000244038; -. DR eggNOG; KOG2754; Eukaryota. DR GeneTree; ENSGT00390000017294; -. DR InParanoid; P39656; -. DR OMA; AHDEYPR; -. DR OrthoDB; 29105at2759; -. DR PAN-GO; P39656; 2 GO annotations based on evolutionary models. DR PhylomeDB; P39656; -. DR BRENDA; 2.4.99.18; 2681. DR PathwayCommons; P39656; -. DR Reactome; R-HSA-1799339; SRP-dependent cotranslational protein targeting to membrane. DR Reactome; R-HSA-446203; Asparagine N-linked glycosylation. DR Reactome; R-HSA-6798695; Neutrophil degranulation. DR Reactome; R-HSA-879415; Advanced glycosylation endproduct receptor signaling. DR Reactome; R-HSA-9694548; Maturation of spike protein. DR Reactome; R-HSA-9768727; Regulation of CDH1 posttranslational processing and trafficking to plasma membrane. DR Reactome; R-HSA-9918432; Maturation of DENV proteins. DR Reactome; R-HSA-9931295; PD-L1(CD274) glycosylation and translocation to plasma membrane. DR SignaLink; P39656; -. DR SIGNOR; P39656; -. DR UniPathway; UPA00378; -. DR Agora; ENSG00000244038; -. DR BioGRID-ORCS; 1650; 761 hits in 1132 CRISPR screens. DR CD-CODE; 91857CE7; Nucleolus. DR ChiTaRS; DDOST; human. DR GeneWiki; DDOST; -. DR GenomeRNAi; 1650; -. DR Pharos; P39656; Tchem. DR PRO; PR:P39656; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; P39656; protein. DR Bgee; ENSG00000244038; Expressed in corpus epididymis and 205 other cell types or tissues. DR ExpressionAtlas; P39656; baseline and differential. DR GO; GO:0035577; C:azurophil granule membrane; TAS:Reactome. DR GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA. DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:UniProtKB. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0008250; C:oligosaccharyltransferase complex; IDA:UniProtKB. DR GO; GO:0160226; C:oligosaccharyltransferase complex A; IDA:UniProtKB. DR GO; GO:0160227; C:oligosaccharyltransferase complex B; IDA:UniProtKB. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0008047; F:enzyme activator activity; IMP:ARUK-UCL. DR GO; GO:0009101; P:glycoprotein biosynthetic process; ISS:UniProtKB. DR GO; GO:0006487; P:protein N-linked glycosylation; IDA:UniProtKB. DR GO; GO:0031647; P:regulation of protein stability; IMP:ARUK-UCL. DR GO; GO:0034097; P:response to cytokine; IDA:UniProtKB. DR GO; GO:0042110; P:T cell activation; IDA:UniProtKB. DR InterPro; IPR005013; DDOST_48_kDa_subunit. DR InterPro; IPR055459; OST48_MD. DR InterPro; IPR055457; OST48_N. DR PANTHER; PTHR10830; DOLICHYL-DIPHOSPHOOLIGOSACCHARIDE--PROTEIN GLYCOSYLTRANSFERASE 48 KDA SUBUNIT; 1. DR PANTHER; PTHR10830:SF0; DOLICHYL-DIPHOSPHOOLIGOSACCHARIDE--PROTEIN GLYCOSYLTRANSFERASE 48 KDA SUBUNIT; 1. DR Pfam; PF23358; OST48_MD; 1. DR Pfam; PF03345; OST48_N; 1. DR PDBsum; 6S7O; -. DR PDBsum; 6S7T; -. DR PDBsum; 8B6L; -. DR PDBsum; 8PN9; -. DR PDBsum; 9N9J; -. DR PDBsum; 9YGY; -. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Congenital disorder of glycosylation; KW Disease variant; Endoplasmic reticulum; Membrane; KW Proteomics identification; Reference proteome; Signal; Transmembrane; KW Transmembrane helix. FT SIGNAL 1..42 FT /evidence="ECO:0000250" FT CHAIN 43..456 FT /note="Dolichyl-diphosphooligosaccharide--protein FT glycosyltransferase 48 kDa subunit" FT /id="PRO_0000021957" FT TOPO_DOM 43..427 FT /note="Lumenal" FT /evidence="ECO:0000255" FT TRANSMEM 428..447 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 448..456 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT VAR_SEQ 69..105 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_055498" FT VAR_SEQ 124..141 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_055499" FT VARIANT 8 FT /note="R -> G (in dbSNP:rs537816)" FT /evidence="ECO:0000269|PubMed:14702039, FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:7788527, FT ECO:0000269|PubMed:9367678, ECO:0000269|Ref.5" FT /id="VAR_047911" FT VARIANT 217 FT /note="G -> D (in CDG1R; dbSNP:rs387906831)" FT /evidence="ECO:0000269|PubMed:22305527" FT /id="VAR_067544" FT CONFLICT 229 FT /note="P -> R (in Ref. 3; BAG59544)" FT /evidence="ECO:0000305" FT CONFLICT 343 FT /note="G -> A (in Ref. 1; BAA23670)" FT /evidence="ECO:0000305" FT CONFLICT 434 FT /note="S -> P (in Ref. 1; BAA23670 and 2; BAA06126)" FT /evidence="ECO:0000305" FT STRAND 45..53 FT /evidence="ECO:0007829|PDB:6S7O" FT HELIX 56..59 FT /evidence="ECO:0007829|PDB:6S7O" FT HELIX 61..69 FT /evidence="ECO:0007829|PDB:6S7O" FT STRAND 73..78 FT /evidence="ECO:0007829|PDB:6S7O" FT STRAND 88..90 FT /evidence="ECO:0007829|PDB:6S7O" FT STRAND 95..100 FT /evidence="ECO:0007829|PDB:6S7O" FT STRAND 103..106 FT /evidence="ECO:0007829|PDB:6S7T" FT HELIX 113..121 FT /evidence="ECO:0007829|PDB:6S7O" FT STRAND 125..130 FT /evidence="ECO:0007829|PDB:6S7O" FT HELIX 136..143 FT /evidence="ECO:0007829|PDB:6S7O" FT TURN 144..146 FT /evidence="ECO:0007829|PDB:6S7O" FT STRAND 155..157 FT /evidence="ECO:0007829|PDB:6S7T" FT STRAND 158..163 FT /evidence="ECO:0007829|PDB:6S7O" FT STRAND 168..170 FT /evidence="ECO:0007829|PDB:6S7O" FT STRAND 173..175 FT /evidence="ECO:0007829|PDB:6S7O" FT STRAND 177..180 FT /evidence="ECO:0007829|PDB:6S7O" FT TURN 184..186 FT /evidence="ECO:0007829|PDB:6S7O" FT STRAND 195..197 FT /evidence="ECO:0007829|PDB:6S7O" FT STRAND 202..204 FT /evidence="ECO:0007829|PDB:6S7T" FT STRAND 209..211 FT /evidence="ECO:0007829|PDB:6S7T" FT STRAND 212..215 FT /evidence="ECO:0007829|PDB:6S7O" FT HELIX 216..218 FT /evidence="ECO:0007829|PDB:6S7O" FT STRAND 222..224 FT /evidence="ECO:0007829|PDB:6S7T" FT STRAND 226..228 FT /evidence="ECO:0007829|PDB:6S7T" FT STRAND 243..248 FT /evidence="ECO:0007829|PDB:6S7O" FT STRAND 254..259 FT /evidence="ECO:0007829|PDB:6S7O" FT HELIX 261..264 FT /evidence="ECO:0007829|PDB:6S7O" FT HELIX 266..269 FT /evidence="ECO:0007829|PDB:6S7O" FT TURN 276..279 FT /evidence="ECO:0007829|PDB:6S7O" FT STRAND 283..285 FT /evidence="ECO:0007829|PDB:6S7O" FT HELIX 288..299 FT /evidence="ECO:0007829|PDB:6S7O" FT STRAND 302..304 FT /evidence="ECO:0007829|PDB:6S7O" FT STRAND 306..308 FT /evidence="ECO:0007829|PDB:6S7T" FT STRAND 312..315 FT /evidence="ECO:0007829|PDB:6S7O" FT STRAND 318..320 FT /evidence="ECO:0007829|PDB:6S7T" FT STRAND 323..328 FT /evidence="ECO:0007829|PDB:6S7O" FT STRAND 330..334 FT /evidence="ECO:0007829|PDB:6S7O" FT STRAND 337..341 FT /evidence="ECO:0007829|PDB:6S7T" FT STRAND 344..347 FT /evidence="ECO:0007829|PDB:6S7T" FT STRAND 354..367 FT /evidence="ECO:0007829|PDB:6S7O" FT STRAND 369..371 FT /evidence="ECO:0007829|PDB:6S7T" FT STRAND 377..380 FT /evidence="ECO:0007829|PDB:6S7O" FT STRAND 386..394 FT /evidence="ECO:0007829|PDB:6S7O" FT STRAND 397..399 FT /evidence="ECO:0007829|PDB:6S7T" FT STRAND 402..411 FT /evidence="ECO:0007829|PDB:6S7O" FT STRAND 415..418 FT /evidence="ECO:0007829|PDB:6S7T" FT HELIX 423..425 FT /evidence="ECO:0007829|PDB:6S7O" FT HELIX 426..445 FT /evidence="ECO:0007829|PDB:6S7O" SQ SEQUENCE 456 AA; 50801 MW; 2707ABAC8FF158CB CRC64; MGYFRCARAG SFGRRRKMEP STAARAWALF WLLLPLLGAV CASGPRTLVL LDNLNVRETH SLFFRSLKDR GFELTFKTAD DPSLSLIKYG EFLYDNLIIF SPSVEDFGGN INVETISAFI DGGGSVLVAA SSDIGDPLRE LGSECGIEFD EEKTAVIDHH NYDISDLGQH TLIVADTENL LKAPTIVGKS SLNPILFRGV GMVADPDNPL VLDILTGSST SYSFFPDKPI TQYPHAVGKN TLLIAGLQAR NNARVIFSGS LDFFSDSFFN SAVQKAAPGS QRYSQTGNYE LAVALSRWVF KEEGVLRVGP VSHHRVGETA PPNAYTVTDL VEYSIVIQQL SNGKWVPFDG DDIQLEFVRI DPFVRTFLKK KGGKYSVQFK LPDVYGVFQF KVDYNRLGYT HLYSSTQVSV RPLQHTQYER FIPSAYPYYA SAFSMMLGLF IFSIVFLHMK EKEKSD //