Search Results
Overview
| Uniprot ID | P06748 |
|---|---|
| Protein Name | Nucleophosmin |
| Gene Name | NPM1 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 141 | KLLSISGKRSAPGGG |
| 150 | SAPGGGSKVPQKKVK |
| 154 | GGSKVPQKKVKLAAD |
| 194 | EEKAPVKKSIRDTPA |
| 202 | SIRDTPAKNAQKSNQ |
| 206 | TPAKNAQKSNQNGKD |
| 212 | QKSNQNGKDSKPSST |
| 215 | NQNGKDSKPSSTPRS |
| 223 | PSSTPRSKGQESFKK |
| 229 | SKGQESFKKQEKTPK |
| 233 | ESFKKQEKTPKTPKG |
| 236 | KKQEKTPKTPKGPSS |
| 239 | EKTPKTPKGPSSVED |
| 248 | PSSVEDIKAKMQASI |
| 250 | SVEDIKAKMQASIEK |
| 257 | KMQASIEKGGSLPKV |
| 263 | EKGGSLPKVEAKFIN |
| 267 | SLPKVEAKFINYVKN |
| 27 | GCELKADKDYHFKVD |
| 273 | AKFINYVKNCFRMTD |
| 32 | ADKDYHFKVDNDENE |
| 80 | KVTLATLKMSVQPTV |
Function
Involved in diverse cellular processes such as ribosome biogenesis, centrosome duplication, protein chaperoning, histone assembly, cell proliferation, and regulation of tumor suppressors p53/TP53 and ARF. Binds ribosome presumably to drive ribosome nuclear export. Associated with nucleolar ribonucleoprotein structures and bind single-stranded nucleic acids. Acts as a chaperonin for the core histones H3, H2B and H4. Stimulates APEX1 endonuclease activity on apurinic/apyrimidinic (AP) double-stranded DNA but inhibits APEX1 endonuclease activity on AP single-stranded RNA. May exert a control of APEX1 endonuclease activity within nucleoli devoted to repair AP on rDNA and the removal of oxidized rRNA molecules. In concert with BRCA2, regulates centrosome duplication. Regulates centriole duplication: phosphorylation by PLK2 is able to trigger centriole replication. Negatively regulates the activation of EIF2AK2/PKR and suppresses apoptosis through inhibition of EIF2AK2/PKR autophosphorylation. Antagonizes the inhibitory effect of ATF5 on cell proliferation and relieves ATF5-induced G2/M blockade (PubMed:22528486). In complex with MYC enhances the transcription of MYC target genes (PubMed:25956029). May act as chaperonin or cotransporter in the nucleolar localization of transcription termination factor TTF1 (By similarity)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0005813 | centrosome |
| Molecular Function | GO:0051059 | NF-kappaB binding |
| Molecular Function | GO:0042803 | protein homodimerization activity |
| Molecular Function | GO:0019901 | protein kinase binding |
| Molecular Function | GO:0004860 | protein kinase inhibitor activity |
| Molecular Function | GO:0043023 | ribosomal large subunit binding |
| Molecular Function | GO:0043024 | ribosomal small subunit binding |
| Molecular Function | GO:0003723 | RNA binding |
| Molecular Function | GO:0019843 | rRNA binding |
| Molecular Function | GO:0030957 | Tat protein binding |
| Molecular Function | GO:0003713 | transcription coactivator activity |
| Molecular Function | GO:0051082 | unfolded protein binding |
| Biological Process | GO:0007249 | canonical NF-kappaB signal transduction |
| Biological Process | GO:0034644 | cellular response to UV |
| Biological Process | GO:0090398 | cellular senescence |
| Biological Process | GO:0007098 | centrosome cycle |
| Biological Process | GO:0006338 | chromatin remodeling |
| Biological Process | GO:0006281 | DNA repair |
| Biological Process | GO:0008104 | intracellular protein localization |
| Biological Process | GO:0006886 | intracellular protein transport |
| Biological Process | GO:0030225 | macrophage differentiation |
| Biological Process | GO:0043066 | negative regulation of apoptotic process |
| Biological Process | GO:0008285 | negative regulation of cell population proliferation |
| Biological Process | GO:0010826 | negative regulation of centrosome duplication |
| Biological Process | GO:0006913 | nucleocytoplasmic transport |
| Biological Process | GO:0006334 | nucleosome assembly |
| Biological Process | GO:1902751 | positive regulation of cell cycle G2/M phase transition |
| Biological Process | GO:0008284 | positive regulation of cell population proliferation |
| Biological Process | GO:2000767 | positive regulation of cytoplasmic translation |
| Biological Process | GO:0045893 | positive regulation of DNA-templated transcription |
| Biological Process | GO:1904751 | positive regulation of protein localization to nucleolus |
| Biological Process | GO:0045944 | positive regulation of transcription by RNA polymerase II |
| Biological Process | GO:0006606 | protein import into nucleus |
| Biological Process | GO:0046599 | regulation of centriole replication |
| Biological Process | GO:0010824 | regulation of centrosome duplication |
| Biological Process | GO:1902629 | regulation of mRNA stability involved in cellular response to UV |
| Biological Process | GO:0042273 | ribosomal large subunit biogenesis |
| Biological Process | GO:0000055 | ribosomal large subunit export from nucleus |
| Biological Process | GO:0042274 | ribosomal small subunit biogenesis |
| Biological Process | GO:0000056 | ribosomal small subunit export from nucleus |
| Biological Process | GO:0042255 | ribosome assembly |
| Biological Process | GO:0007165 | signal transduction |
| Cellular Component | GO:0005737 | cytoplasm |
| Cellular Component | GO:0005829 | cytosol |
| Cellular Component | GO:0005925 | focal adhesion |
| Cellular Component | GO:0001652 | granular component |
| Cellular Component | GO:0015934 | large ribosomal subunit |
| Cellular Component | GO:0016020 | membrane |
| Cellular Component | GO:0016607 | nuclear speck |
| Cellular Component | GO:0005730 | nucleolus |
| Cellular Component | GO:0005654 | nucleoplasm |
| Cellular Component | GO:0005634 | nucleus |
| Cellular Component | GO:0032991 | protein-containing complex |
| Cellular Component | GO:0032993 | protein-DNA complex |
| Cellular Component | GO:1990904 | ribonucleoprotein complex |
| Cellular Component | GO:0015935 | small ribosomal subunit |
| Cellular Component | GO:0031616 | spindle pole centrosome |
| Molecular Function | GO:0003682 | chromatin binding |
| Molecular Function | GO:0001046 | core promoter sequence-specific DNA binding |
| Molecular Function | GO:0140297 | DNA-binding transcription factor binding |
| Molecular Function | GO:0042393 | histone binding |
| Molecular Function | GO:0060090 | molecular adaptor activity |
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] 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.