Search Results

Overview

Uniprot IDQ61937
Protein NameNucleophosmin
Gene NameNpm1
OrganismMus musculus

Kla Sites from experimental identification

Position Flanking peptide
150 SAPGGGNKVPQKKVK
221 KPSTPRSKGQESFKK
237 EKTPKTPKGPSSVED

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. In complex with MYC enhances the transcription of MYC target genes. May act as chaperonin or cotransporter in the nucleolar localization of transcription termination factor TTF1 (PubMed:20513429)

Protein Sequence

10 MEDSMDMDMS 20 PLRPQNYLFG 30 CELKADKDYH 40 FKVDNDENEH 50 QLSLRTVSLG 60 AGAKDELHIV 70 EAEAMNYEGS 80 PIKVTLATLK 90 MSVQPTVSLG 100 GFEITPPVVL 110 RLKCGSGPVH 120 ISGQHLVAVE 130 EDAESEDEDE 140 EDVKLLGMSG 150 KRSAPGGGNK 160 VPQKKVKLDE 170 DDEDDDEDDE 180 DDEDDDDDDF 190 DEEETEEKVP 200 VKKSVRDTPA 210 KNAQKSNQNG 220 KDLKPSTPRS 230 KGQESFKKQE 240 KTPKTPKGPS 250 SVEDIKAKMQ 260 ASIEKGGSLP 270 KVEAKFINYV 280 KNCFRMTDQE 290 AIQDLWQWRK SL

Gene Ontology

Classification GO ID Description
Biological Process GO:1904751 positive regulation of protein localization to nucleolus
Cellular Component GO:0005813 centrosome
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0005829 cytosol
Cellular Component GO:0001652 granular component
Cellular Component GO:0015934 large ribosomal subunit
Cellular Component GO:0016363 nuclear matrix
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:0005524 ATP binding
Molecular Function GO:0003682 chromatin binding
Molecular Function GO:0001046 core promoter sequence-specific DNA binding
Molecular Function GO:0003677 DNA binding
Molecular Function GO:0140297 DNA-binding transcription factor binding
Molecular Function GO:0019899 enzyme binding
Molecular Function GO:0042393 histone binding
Molecular Function GO:0042802 identical protein binding
Molecular Function GO:0060090 molecular adaptor activity
Molecular Function GO:0051059 NF-kappaB binding
Molecular Function GO:0002039 p53 binding
Molecular Function GO:0005547 phosphatidylinositol-3,4,5-trisphosphate binding
Molecular Function GO:0042803 protein homodimerization activity
Molecular Function GO:0043422 protein kinase B binding
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:0006884 cell volume homeostasis
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:0000448 cleavage in ITS2 between 5.8S rRNA and LSU-rRNA of tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA)
Biological Process GO:0006281 DNA repair
Biological Process GO:0008104 intracellular protein localization
Biological Process GO:0030225 macrophage differentiation
Biological Process GO:0043066 negative regulation of apoptotic process
Biological Process GO:0010667 negative regulation of cardiac muscle cell apoptotic process
Biological Process GO:0008285 negative regulation of cell population proliferation
Biological Process GO:0010826 negative regulation of centrosome duplication
Biological Process GO:0050680 negative regulation of epithelial cell proliferation
Biological Process GO:0010629 negative regulation of gene expression
Biological Process GO:0048025 negative regulation of mRNA splicing, via spliceosome
Biological Process GO:0043524 negative regulation of neuron apoptotic process
Biological Process GO:0044387 negative regulation of protein kinase activity by regulation of protein phosphorylation
Biological Process GO:0006913 nucleocytoplasmic transport
Biological Process GO:0006334 nucleosome assembly
Biological Process GO:0009891 positive regulation of biosynthetic process
Biological Process GO:0043085 positive regulation of catalytic activity
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:0010825 positive regulation of centrosome duplication
Biological Process GO:2000767 positive regulation of cytoplasmic translation
Biological Process GO:0051054 positive regulation of DNA metabolic process
Biological Process GO:0045740 positive regulation of DNA replication
Biological Process GO:1900264 positive regulation of DNA-directed DNA polymerase activity
Biological Process GO:0045893 positive regulation of DNA-templated transcription
Biological Process GO:0045860 positive regulation of protein kinase activity
Biological Process GO:0031398 positive regulation of protein ubiquitination
Biological Process GO:0045944 positive regulation of transcription by RNA polymerase II
Biological Process GO:0045727 positive regulation of translation
Biological Process GO:0010608 post-transcriptional regulation of gene expression
Biological Process GO:0006606 protein import into nucleus
Biological Process GO:0050821 protein stabilization
Biological Process GO:0051726 regulation of cell cycle
Biological Process GO:0001558 regulation of cell growth
Biological Process GO:0046599 regulation of centriole replication
Biological Process GO:0010824 regulation of centrosome duplication
Biological Process GO:0043516 regulation of DNA damage response, signal transduction by p53 class mediator
Biological Process GO:0060735 regulation of eIF2 alpha phosphorylation by dsRNA
Biological Process GO:1902629 regulation of mRNA stability involved in cellular response to UV
Biological Process GO:0043523 regulation of neuron apoptotic process
Biological Process GO:0031647 regulation of protein stability
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:0009303 rRNA transcription

Reference

[1] Sung E, Sim H, Cho YC, Lee W, Bae JS et al.. Global Profiling of Lysine Acetylation and Lactylation in Kupffer Cells.. J Proteome Res 22(12):3683-3691. 2023 Dec 1. PMID: 37897433.

[2] Zhuo W, Zhang M, Tan J, Gao Y, Wang Y et al.. Lysine lactylation analysis of proteins in the heart of the Kawasaki disease mouse model.. Front Cell Dev Biol 13:1550220. 2025. PMID: 40114965.

[3] Wu D, Tang Y, Li X, Xiong S, Zhang Z et al.. Characterization of protein lactylation in healthy and ischemic mouse hearts.. Front Cardiovasc Med 12:1644886. 2025. PMID: 41089239.