NPM1 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. Belongs to the nucleoplasmin family. 3 alternatively spliced human isoforms have been reported. Note: This description may include information from UniProtKB.
Protein type: Nucleolus; Oncoprotein; RNA-binding; Translation
Chromosomal Location of Human Ortholog: 10q12
Cellular Component:  centrosome; cytoplasm; cytosol; granular component; large ribosomal subunit; nuclear matrix; nuclear speck; nucleolus; nucleoplasm; nucleus; protein-containing complex; protein-DNA complex; ribonucleoprotein complex; small ribosomal subunit; spindle pole centrosome
Molecular Function:  activating transcription factor binding; ATP binding; chromatin binding; core promoter binding; DNA binding; enzyme binding; histone binding; NF-kappaB binding; p53 binding; phosphatidylinositol-3,4,5-trisphosphate binding; protein binding; protein heterodimerization activity; protein homodimerization activity; protein kinase B binding; protein kinase binding; protein kinase inhibitor activity; protein N-terminus binding; ribosomal large subunit binding; ribosomal small subunit binding; RNA binding; rRNA binding; Tat protein binding; transcription coactivator activity; transcription factor binding; unfolded protein binding
Biological Process:  cardiac muscle hypertrophy; cell aging; cell volume homeostasis; cellular response to hypoxia; cellular response to testosterone stimulus; cellular response to UV; centrosome cycle; chromatin remodeling; cleavage in ITS2 between 5.8S rRNA and LSU-rRNA of tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); DNA repair; liver regeneration; negative regulation of apoptotic process; negative regulation of cardiac muscle cell apoptotic process; negative regulation of cell proliferation; negative regulation of centrosome duplication; negative regulation of epithelial cell proliferation; negative regulation of gene expression; negative regulation of mRNA splicing, via spliceosome; negative regulation of neuron apoptotic process; negative regulation of protein kinase activity by regulation of protein phosphorylation; nucleocytoplasmic transport; nucleosome assembly; positive regulation of catalytic activity; positive regulation of cell cycle G2/M phase transition; positive regulation of cell proliferation; positive regulation of cellular biosynthetic process; positive regulation of centrosome duplication; positive regulation of DNA metabolic process; positive regulation of DNA replication; positive regulation of DNA-directed DNA polymerase activity; positive regulation of NF-kappaB transcription factor activity; positive regulation of protein kinase activity; positive regulation of protein localization to nucleolus; positive regulation of protein ubiquitination; positive regulation of transcription by RNA polymerase II; positive regulation of transcription, DNA-templated; positive regulation of translation; posttranscriptional regulation of gene expression; protein complex oligomerization; protein destabilization; protein homooligomerization; protein localization; protein stabilization; regulation of cell cycle; regulation of cell growth; regulation of centriole replication; regulation of centrosome duplication; regulation of DNA damage response, signal transduction by p53 class mediator; regulation of eIF2 alpha phosphorylation by dsRNA; regulation of endodeoxyribonuclease activity; regulation of endoribonuclease activity; regulation of mRNA stability involved in cellular response to UV; regulation of neuron apoptotic process; regulation of protein stability; ribosomal large subunit biogenesis; ribosomal large subunit export from nucleus; ribosomal small subunit biogenesis; ribosomal small subunit export from nucleus; rRNA export from nucleus; rRNA transcription
Reference #:  P13084 (UniProtKB)
Alt. Names/Synonyms: B23NP; MGC108517; NPM; Npm1; Nucleolar phosphoprotein B23; nucleolar protein B23.1; Nucleolar protein NO38; Nucleophosmin; nucleophosmin (nucleolar phosphoprotein B23, numatrin); nucleophosmin 1; Numatrin
Gene Symbols: Npm1
Molecular weight: 32,560 Da
Basal Isoelectric point: 4.62  Predict pI for various phosphorylation states
Protein-Specific Antibodies, siRNAs or Recombinant Proteins from Cell Signaling Technology® Total Proteins
Select Structure to View Below

NPM1

Protein Structure Not Found.


Cross-references to other databases:  STRING  |  Reactome  |  BioGPS  |  Pfam  |  Phospho.ELM  |  NetworKIN  |  UniProtKB  |  Entrez-Gene  |  Ensembl Gene