Search Results
Overview
| Uniprot ID | P04406 |
|---|---|
| Protein Name | Glyceraldehyde-3-phosphate dehydrogenase |
| Gene Name | GAPDH |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 117 | AHLQGGAKRVIISAP |
| 139 | VMGVNHEKYDNSLKI |
| 145 | EKYDNSLKIISNASC |
| 162 | NCLAPLAKVIHDNFG |
| 186 | HAITATQKTVDGPSG |
| 194 | TVDGPSGKLWRDGRG |
| 215 | PASTGAAKAVGKVIP |
| 219 | GAAKAVGKVIPELNG |
| 227 | VIPELNGKLTGMAFR |
| 251 | DLTCRLEKPAKYDDI |
| 254 | CRLEKPAKYDDIKKV |
| 263 | DDIKKVVKQASEGPL |
| 27 | RAAFNSGKVDIVAIN |
| 334 | LMAHMASKE****** |
| 5 | ***MGKVKVGVNGFG |
| 61 | GKFHGTVKAENGKLV |
| 66 | TVKAENGKLVINGNP |
Function
Catalyzes the conversion of D-glyceraldehyde 3-phosphate (G3P) into 3-phospho-D-glyceroyl phosphate in glycolysis and the reverse reaction in gluconeogenesis (PubMed:11724794, PubMed:3170585). Also shows nitrosylase activity, thereby playing a role in nuclear functions (PubMed:11724794, PubMed:3170585). Modulates the organization and assembly of the cytoskeleton (By similarity). Facilitates the CHP1-dependent microtubule and membrane associations through its ability to stimulate the binding of CHP1 to microtubules (By similarity). Component of the GAIT (gamma interferon-activated inhibitor of translation) complex which mediates interferon-gamma-induced transcript-selective translation inhibition in inflammation processes (PubMed:23071094). Upon interferon-gamma treatment assembles into the GAIT complex which binds to stem loop-containing GAIT elements in the 3'-UTR of diverse inflammatory mRNAs (such as ceruplasmin) and suppresses their translation (PubMed:23071094). Also plays a role in innate immunity by promoting TNF-induced NF-kappa-B activation and type I interferon production, via interaction with TRAF2 and TRAF3, respectively (PubMed:23332158, PubMed:27387501). Participates in nuclear events including transcription, RNA transport, DNA replication and apoptosis (By similarity). Nuclear functions are probably due to the nitrosylase activity that mediates cysteine S-nitrosylation of nuclear target proteins such as SIRT1, HDAC2 and PRKDC (By similarity)
Protein Sequence
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:0097452 | GAIT complex |
| Cellular Component | GO:0005811 | lipid droplet |
| Cellular Component | GO:0016020 | membrane |
| Cellular Component | GO:0015630 | microtubule cytoskeleton |
| Cellular Component | GO:0005634 | nucleus |
| Cellular Component | GO:0048471 | perinuclear region of cytoplasm |
| Cellular Component | GO:0005886 | plasma membrane |
| Cellular Component | GO:1990904 | ribonucleoprotein complex |
| Cellular Component | GO:0031982 | vesicle |
| Molecular Function | GO:0019828 | aspartic-type endopeptidase inhibitor activity |
| Molecular Function | GO:0097718 | disordered domain specific binding |
| Molecular Function | GO:0004365 | glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity |
| Molecular Function | GO:0042802 | identical protein binding |
| Molecular Function | GO:0008017 | microtubule binding |
| Molecular Function | GO:0051287 | NAD binding |
| Molecular Function | GO:0050661 | NADP binding |
| Molecular Function | GO:0035605 | peptidyl-cysteine S-nitrosylase activity |
| Biological Process | GO:0061844 | antimicrobial humoral immune response mediated by antimicrobial peptide |
| Biological Process | GO:0061621 | canonical glycolysis |
| Biological Process | GO:0071346 | cellular response to type II interferon |
| Biological Process | GO:0050832 | defense response to fungus |
| Biological Process | GO:0006096 | glycolytic process |
| Biological Process | GO:0051873 | killing by host of symbiont cells |
| Biological Process | GO:0031640 | killing of cells of another organism |
| Biological Process | GO:0000226 | microtubule cytoskeleton organization |
| Biological Process | GO:0010951 | negative regulation of endopeptidase activity |
| Biological Process | GO:1901194 | negative regulation of formation of translation preinitiation complex |
| Biological Process | GO:0017148 | negative regulation of translation |
| Biological Process | GO:0051402 | neuron apoptotic process |
| Biological Process | GO:0035606 | peptidyl-cysteine S-trans-nitrosylation |
| Biological Process | GO:0043123 | positive regulation of canonical NF-kappaB signal transduction |
| Biological Process | GO:0001819 | positive regulation of cytokine production |
| Biological Process | GO:0032481 | positive regulation of type I interferon production |
| Biological Process | GO:0050821 | protein stabilization |
| Biological Process | GO:0016241 | regulation of macroautophagy |
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] Lin Y, Chen M, Wang D, Yu Y, Chen R et al.. Multi-Proteomic Analysis Reveals the Effect of Protein Lactylation on Matrix and Cholesterol Metabolism in Tendinopathy.. J Proteome Res 22(6):1712-1722. 2023 Jun 2. PMID: 37159428.
[5] 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.
[6] 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.
[7] 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.
[8] Bao Q, Wan N, He Z, Cao J, Yuan W et al.. Subcellular Proteomic Mapping of Lysine Lactylation.. J Am Soc Mass Spectrom 35(12):3221-3232. 2024 Dec 4. PMID: 39569522.
[9] 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.
[10] 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.
[11] 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.
[12] Yan M, Tu H, Tang S, Gai Z, Shi Q et al.. Lactylated Proteomic Analysis Reveals Functional Implications of Lysine Lactylation In Asthenozoospermia.. Mol Cell Proteomics 24(12):101439. 2025 Dec. PMID: 41192556.
[13] 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.