Search Results
Overview
| Uniprot ID | P43490 |
|---|---|
| Protein Name | Nicotinamide phosphoribosyltransferase |
| Gene Name | NAMPT |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 228 | VAGLALIKKYYGTKD |
| 229 | AGLALIKKYYGTKDP |
| 331 | VLEILGKKFPVTENS |
| 339 | FPVTENSKGYKLLPP |
| 423 | DPVADPNKRSKKGRL |
| 469 | FKNGKVTKSYSFDEI |
| 478 | YSFDEIRKNAQLNIE |
| 48 | EKKTENSKLRKVKYE |
Function
Catalyzes the condensation of nicotinamide with 5-phosphoribosyl-1-pyrophosphate to yield nicotinamide mononucleotide, an intermediate in the biosynthesis of NAD. It is the rate limiting component in the mammalian NAD biosynthesis pathway. The secreted form behaves both as a cytokine with immunomodulating properties and an adipokine with anti-diabetic properties, it has no enzymatic activity, partly because of lack of activation by ATP, which has a low level in extracellular space and plasma. Plays a role in the modulation of circadian clock function. NAMPT-dependent oscillatory production of NAD regulates oscillation of clock target gene expression by releasing the core clock component: CLOCK-BMAL1 heterodimer from NAD-dependent SIRT1-mediated suppression (By similarity)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0005829 | cytosol |
| Cellular Component | GO:0070062 | extracellular exosome |
| Cellular Component | GO:0005759 | mitochondrial matrix |
| Cellular Component | GO:0005634 | nucleus |
| Molecular Function | GO:0005125 | cytokine activity |
| Molecular Function | GO:0042802 | identical protein binding |
| Molecular Function | GO:0047280 | nicotinamide phosphoribosyltransferase activity |
| Biological Process | GO:0007267 | cell-cell signaling |
| Biological Process | GO:0032922 | circadian regulation of gene expression |
| Biological Process | GO:0006954 | inflammatory response |
| Biological Process | GO:0009435 | NAD+ biosynthetic process |
| Biological Process | GO:0034355 | NAD+ biosynthetic process via the salvage pathway |
| Biological Process | GO:0006741 | NADP+ biosynthetic process |
| Biological Process | GO:1901847 | nicotinate metabolic process |
| Biological Process | GO:0043123 | positive regulation of canonical NF-kappaB signal transduction |
| Biological Process | GO:0008284 | positive regulation of cell population proliferation |
| Biological Process | GO:0070374 | positive regulation of ERK1 and ERK2 cascade |
| Biological Process | GO:0010628 | positive regulation of gene expression |
| Biological Process | GO:0045944 | positive regulation of transcription by RNA polymerase II |
| Biological Process | GO:0007165 | signal transduction |
Reference
[1] Yang D, Yin J, Shan L, Yi X, Zhang W et al.. Identification of lysine-lactylated substrates in gastric cancer cells.. iScience 25(7):104630. 2022 Jul 15. PMID: 35800753.
[2] 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.
[3] 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.
[4] Cheng Z, Huang H, Li M, Chen Y. Proteomic analysis identifies PFKP lactylation in SW480 colon cancer cells.. iScience 27(1):108645. 2024 Jan 19. PMID: 38155775.
[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.