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Overview

Uniprot IDP04843
Protein NameDolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 1
Gene NameRPN1
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
187 RNVESYTKLGNPTRS
281 ISSIRSFKTILPAAA
414 PVIVAYKKNLVEQHI
474 PAAEARMKVACITEQ
516 ISTLNSGKKSLETEH
538 ALLQSRLKTEGSDLC
553 DRVSEMQKLDAQVKE
559 QKLDAQVKELVLKSA
564 QVKELVLKSAVEAER
579 LVAGKLKKDTYIENE

Function

Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation (PubMed:31831667). N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity (By similarity)

Protein Sequence

10 MEAPAAGLFL 20 LLLLGTWAPA 30 PGSASSEAPP 40 LINEDVKRTV 50 DLSSHLAKVT 60 AEVVLAHLGG 70 GSTSRATSFL 80 LALEPELEAR 90 LAHLGVQVKG 100 EDEEENNLEV 110 RETKIKGKSG 120 RFFTVKLPVA 130 LDPGAKISVI 140 VETVYTHVLH 150 PYPTQITQSE 160 KQFVVFEGNH 170 YFYSPYPTKT 180 QTMRVKLASR 190 NVESYTKLGN 200 PTRSEDLLDY 210 GPFRDVPAYS 220 QDTFKVHYEN 230 NSPFLTITSM 240 TRVIEVSHWG 250 NIAVEENVDL 260 KHTGAVLKGP 270 FSRYDYQRQP 280 DSGISSIRSF 290 KTILPAAAQD 300 VYYRDEIGNV 310 STSHLLILDD 320 SVEMEIRPRF 330 PLFGGWKTHY 340 IVGYNLPSYE 350 YLYNLGDQYA 360 LKMRFVDHVF 370 DEQVIDSLTV 380 KIILPEGAKN 390 IEIDSPYEIS 400 RAPDELHYTY 410 LDTFGRPVIV 420 AYKKNLVEQH 430 IQDIVVHYTF 440 NKVLMLQEPL 450 LVVAAFYILF 460 FTVIIYVRLD 470 FSITKDPAAE 480 ARMKVACITE 490 QVLTLVNKRI 500 GLYRHFDETV 510 NRYKQSRDIS 520 TLNSGKKSLE 530 TEHKALTSEI 540 ALLQSRLKTE 550 GSDLCDRVSE 560 MQKLDAQVKE 570 LVLKSAVEAE 580 RLVAGKLKKD 590 TYIENEKLIS 600 GKRQELVTKI DHILDAL

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005829 cytosol
Cellular Component GO:0005783 endoplasmic reticulum
Cellular Component GO:0005789 endoplasmic reticulum membrane
Cellular Component GO:0042470 melanosome
Cellular Component GO:0016020 membrane
Cellular Component GO:0008250 oligosaccharyltransferase complex
Cellular Component GO:0160226 oligosaccharyltransferase complex A
Cellular Component GO:0160227 oligosaccharyltransferase complex B
Cellular Component GO:0005791 rough endoplasmic reticulum
Molecular Function GO:0003723 RNA binding
Biological Process GO:0006487 protein N-linked glycosylation

Reference

[1] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.

[2] Hong H, Chen X, Wang H, Gu X, Yuan Y et al.. Global profiling of protein lysine lactylation and potential target modified protein analysis in hepatocellular carcinoma.. Proteomics 23(9):e2200432. 2023 May. PMID: 36625413.

[3] He C, Zhang J, Bai X, Lu C, Zhang K. Lysine lactylation-based insight to understanding the characterization of cervical cancer.. Biochim Biophys Acta Mol Basis Dis 1870(7):167356. 2024 Oct. PMID: 39025375.

[4] He J, Lai T, Zhou Z, Yang H, Lei Z et al.. Multiomics profiling reveals the involvement of protein lactylation in nonhomologous end joining pathway conferring radioresistance in lung adenocarcinoma cell.. Sci Rep 15(1):24651. 2025 Jul 9. PMID: 40634431.

[5] Wu Q, Li Z, Gong T, Zheng X, Zhou X et al.. Porphyromonas gingivalis infection induces lysine lactylation reprogramming in human umbilical vein endothelial cells.. Front Cell Infect Microbiol 16:1706727. 2026. PMID: 41696360.