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Overview

Uniprot IDQ9H6U8
Protein NameAlpha-1,2-mannosyltransferase ALG9
Gene NameALG9
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
11 RGARQRLKGSGASSG
26 DTAPAADKLRELLGS

Function

Mannosyltransferase that operates in the biosynthetic pathway of dolichol-linked oligosaccharides, the glycan precursors employed in protein asparagine (N)-glycosylation. The assembly of dolichol-linked oligosaccharides begins on the cytosolic side of the endoplasmic reticulum membrane and finishes in its lumen. The sequential addition of sugars to dolichol pyrophosphate produces dolichol-linked oligosaccharides containing fourteen sugars, including two GlcNAcs, nine mannoses and three glucoses. Once assembled, the oligosaccharide is transferred from the lipid to nascent proteins by oligosaccharyltransferases. In the lumen of the endoplasmic reticulum, catalyzes the addition of the seventh and ninth alpha-1,2-linked mannose residues to Man(6)GlcNAc(2)-PP-dolichol and Man(8)GlcNAc(2)-PP-dolichol respectively

Protein Sequence

10 MASRGARQRL 20 KGSGASSGDT 30 APAADKLREL 40 LGSREAGGAE 50 HRTELSGNKA 60 GQVWAPEGST 70 AFKCLLSARL 80 CAALLSNISD 90 CDETFNYWEP 100 THYLIYGEGF 110 QTWEYSPAYA 120 IRSYAYLLLH 130 AWPAAFHARI 140 LQTNKILVFY 150 FLRCLLAFVS 160 CICELYFYKA 170 VCKKFGLHVS 180 RMMLAFLVLS 190 TGMFCSSSAF 200 LPSSFCMYTT 210 LIAMTGWYMD 220 KTSIAVLGVA 230 AGAILGWPFS 240 AALGLPIAFD 250 LLVMKHRWKS 260 FFHWSLMALI 270 LFLVPVVVID 280 SYYYGKLVIA 290 PLNIVLYNVF 300 TPHGPDLYGT 310 EPWYFYLING 320 FLNFNVAFAL 330 ALLVLPLTSL 340 MEYLLQRFHV 350 QNLGHPYWLT 360 LAPMYIWFII 370 FFIQPHKEER 380 FLFPVYPLIC 390 LCGAVALSAL 400 QKCYHFVFQR 410 YRLEHYTVTS 420 NWLALGTVFL 430 FGLLSFSRSV 440 ALFRGYHGPL 450 DLYPEFYRIA 460 TDPTIHTVPE 470 GRPVNVCVGK 480 EWYRFPSSFL 490 LPDNWQLQFI 500 PSEFRGQLPK 510 PFAEGPLATR 520 IVPTDMNDQN 530 LEEPSRYIDI 540 SKCHYLVDLD 550 TMRETPREPK 560 YSSNKEEWIS 570 LAYRPFLDAS 580 RSSKLLRAFY 590 VPFLSDQYTV 600 YVNYTILKPR 610 KAKQIRKKSG G

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005789 endoplasmic reticulum membrane
Cellular Component GO:0098553 lumenal side of endoplasmic reticulum membrane
Cellular Component GO:0016020 membrane
Molecular Function GO:0000026 alpha-1,2-mannosyltransferase activity
Molecular Function GO:0052926 dol-P-Man:Man(6)GlcNAc(2)-PP-Dol alpha-1,2-mannosyltransferase activity
Molecular Function GO:0052918 dol-P-Man:Man(8)GlcNAc(2)-PP-Dol alpha-1,2-mannosyltransferase activity
Biological Process GO:0006488 dolichol-linked oligosaccharide biosynthetic process
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] Guo X, Ren X, Yan C, Huang H. Quantitative Proteomics Reveals the Role of Lysine Lactylation in Lenalidomide-Resistance in Multiple Myeloma Cells.. ACS Chem Biol 20(7):1728-1738. 2025 Jul 18. PMID: 40590393.

[3] 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.