Search Results

Overview

Uniprot IDQ9NR45
Protein NameN-acetylneuraminate-9-phosphate synthase
Gene NameNANS
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
290 CEMACNEKLGKSVVA
355 ELVDNHGKKIKS***
356 LVDNHGKKIKS****
52 ECGADCAKFQKSELE
61 QKSELEFKFNRKALE
74 LERPYTSKHSWGKTY
79 TSKHSWGKTYGEHKR

Function

Catalyzes the condensation of phosphoenolpyruvate (PEP) and N-acetylmannosamine 6-phosphate (ManNAc-6-P) to synthesize N-acetylneuraminate-9-phosphate (Neu5Ac-9-P) (PubMed:10749855). Also catalyzes the condensation of PEP and D-mannose 6-phosphate (Man-6-P) to produce 3-deoxy-D-glycero-beta-D-galacto-non-2-ulopyranosonate 9-phosphate (KDN-9-P) (PubMed:10749855). Neu5Ac-9-P and KDN-9-P are the phosphorylated forms of sialic acids N-acetylneuraminic acid (Neu5Ac) and deaminoneuraminic acid (KDN), respectively (PubMed:10749855). Required for brain and skeletal development (PubMed:27213289)

Protein Sequence

10 MPLELELCPG 20 RWVGGQHPCF 30 IIAEIGQNHQ 40 GDLDVAKRMI 50 RMAKECGADC 60 AKFQKSELEF 70 KFNRKALERP 80 YTSKHSWGKT 90 YGEHKRHLEF 100 SHDQYRELQR 110 YAEEVGIFFT 120 ASGMDEMAVE 130 FLHELNVPFF 140 KVGSGDTNNF 150 PYLEKTAKKG 160 RPMVISSGMQ 170 SMDTMKQVYQ 180 IVKPLNPNFC 190 FLQCTSAYPL 200 QPEDVNLRVI 210 SEYQKLFPDI 220 PIGYSGHETG 230 IAISVAAVAL 240 GAKVLERHIT 250 LDKTWKGSDH 260 SASLEPGELA 270 ELVRSVRLVE 280 RALGSPTKQL 290 LPCEMACNEK 300 LGKSVVAKVK 310 IPEGTILTMD 320 MLTVKVGEPK 330 GYPPEDIFNL 340 VGKKVLVTVE 350 EDDTIMEELV DNHGKKIKS

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0005829 cytosol
Cellular Component GO:0070062 extracellular exosome
Cellular Component GO:0005654 nucleoplasm
Molecular Function GO:0047444 N-acylneuraminate-9-phosphate synthase activity
Biological Process GO:0016051 carbohydrate biosynthetic process
Biological Process GO:0006055 CMP-N-acetylneuraminate biosynthetic process
Biological Process GO:0046380 N-acetylneuraminate biosynthetic process

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] Yang YH, Wang QC, Kong J, Yang JT, Liu JF. Global profiling of lysine lactylation in human lungs.. Proteomics 23(15):e2200437. 2023 Aug. PMID: 37170646.

[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] Shi CM, Wang QC, Li XL, Yang YH, Tang XY et al.. Global Profiling of Protein Lactylation in Human Hippocampi.. Proteomics Clin Appl 19(2):e202400061. 2025 Mar. PMID: 39610256.

[5] 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.

[6] 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.