Go Annotations as Summary Text (Tabular View) (GO Graph)

GO curators for mouse genes have assigned the following annotations to the gene product of Npm1. (This text reflects annotations as of Tuesday, May 21, 2013.) MGI curation of this mouse gene is considered complete, including annotations derived from the biomedical literature as of December 8, 2008. If you know of any additional information regarding this mouse gene please let us know. Please supply mouse gene symbol and a PubMed ID.

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Summary from NCBI RefSeq

[Summary is not available for the mouse gene. This summary is for the human ortholog.] This gene encodes a phosphoprotein which moves between the nucleus and the cytoplasm. The gene product is thought to be involved in several processes including regulation of the ARF/p53 pathway. A number of genes are fusion partners have been characterized, in particular the anaplastic lymphoma kinase gene on chromosome 2. Mutations in this gene are associated with acute myeloid leukemia. More than a dozen pseudogenes of this gene have been identified. Alternative splicing results in multiple transcript variants.[provided by RefSeq, Nov 2009]

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Summary text based on GO annotations supported by experimental evidence in mouse

• Researchers have inferred from direct assay, that the gene product of Npm1
  • participates in the following biological processes:
    • cell growth ^[12]
    • cell volume homeostasis ^[12]
    • negative regulation of mRNA splicing, via spliceosome ^[18]
    • nucleocytoplasmic transport ^[3]
    • positive regulation of cell proliferation ^[12]
    • positive regulation of cellular biosynthetic process ^[12]
    • positive regulation of protein kinase activity ^[11]
    • ribosomal large subunit biogenesis ^[12]
    • ribosomal small subunit biogenesis ^[12]
    • ribosomal small subunit export from nucleus ^[12]
    • rRNA export from nucleus ^[12]
  • performs the following molecular functions:
    • RNA binding ^[18]
    • rRNA binding ^{[8, 12]}
  • is located in the following cellular components:
    • centrosome ^[17]
    • cytoplasm ^[20]
    • cytosol ^[12]
    • granular component ^[3]
    • large ribosomal subunit ^[12]
    • nuclear speck ^[18]
    • nucleolus ^{[1, 3, 4, 8, 10, 12, 13, 14, 16, 17, 19, 20, 21]}
    • nucleoplasm ^{[12, 17, 19]}
    • nucleus ^[20]
    • small ribosomal subunit ^[12]
• The gene product of Npm1 has been shown to bind to the gene products of Cdkn2a, Gpank1, Npm3, Rpl5, Rps15, Rrp1b, Vim, Ybx1. ^{[2, 3, 6, 8, 9, 11, 20]}
• Researchers have inferred, based on phenotypic analysis of mouse mutants, that the gene product of Npm1
  • participates in the following biological processes:
    • cell volume homeostasis ^[12]
    • positive regulation of cell proliferation ^[12]
    • positive regulation of cellular biosynthetic process ^[12]
    • protein destabilization ^[15]
    • protein localization ^[5]
    • regulation of cell cycle ^[3]
    • regulation of centrosome duplication ^[7]
    • ribosomal large subunit biogenesis ^[12]
    • ribosomal large subunit export from nucleus ^[12]
    • ribosomal small subunit biogenesis ^[12]
    • rRNA export from nucleus ^[12]
• Researchers have inferred, based on genetic interactions, that the gene product of Npm1
  • participates in the following biological processes:
    • positive regulation of centrosome duplication based on interactions with ^[11]
    • regulation of DNA damage response, signal transduction by p53 class mediator based on interactions with Trp53 ^[5]

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Summary text based on GO annotations supported by experimental evidence in other organisms

• From comparative sequence analysis (see table for details), MGI curators have determined that the gene product of Npm1:
  • participates in the following biological processes:
    • cell aging
    • centrosome cycle
    • DNA repair
    • negative regulation of apoptotic process
    • negative regulation of cell proliferation
    • negative regulation of centrosome duplication
    • negative regulation of protein kinase activity by regulation of protein phosphorylation
    • nucleocytoplasmic transport
    • nucleosome assembly
    • positive regulation of catalytic activity
    • positive regulation of DNA metabolic process
    • positive regulation of DNA replication
    • positive regulation of NF-kappaB transcription factor activity
    • positive regulation of translation
    • protein homooligomerization
    • protein localization
    • protein oligomerization
    • regulation of centriole replication
    • regulation of eIF2 alpha phosphorylation by dsRNA
    • regulation of endodeoxyribonuclease activity
    • regulation of endoribonuclease activity
    • regulation of neuron apoptotic process
    • response to stress
  • performs the following molecular functions:
    • DNA binding
    • enzyme binding
    • histone binding
    • NF-kappaB binding
    • phosphatidylinositol-3,4,5-trisphosphate binding
    • protein heterodimerization activity
    • protein homodimerization activity
    • protein kinase binding
    • protein kinase inhibitor activity
    • ribosomal large subunit binding
    • ribosomal small subunit binding
    • RNA binding
    • Tat protein binding
    • transcription coactivator activity
    • unfolded protein binding
  • is located in the following cellular components:
    • centrosome
    • cytoplasm
    • nucleolus
    • nucleoplasm
    • nucleus
    • ribonucleoprotein complex
    • spindle pole centrosome

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Summary text based on GO annotations supported by structural data

• Npm1 encodes a protein or proteins that contain the following InterPro domains: Nucleoplasmin, Nucleoplasmin core domain, indicating that the gene product:
  • performs the following molecular functions:
    • nucleic acid binding

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Summary text for additional MGI annotations

• Automated translation to GO terms of SwissProt keywords that describe Npm1 indicates that it:
  • is located in the following cellular components:
    • cytoskeleton

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References

1. Biggiogera M et al. (1990) Nucleolar distribution of proteins B23 and nucleolin in mouse preimplantation embryos as visualized by immunoelectron microscopy. Development, 110:1263-70. (PubMed:2100262)
2. Borggrefe T et al. (1998) A B-cell-specific DNA recombination complex. J Biol Chem, 273:17025-35. (PubMed:9642267)
3. Brady SN et al. (2004) ARF impedes NPM/B23 shuttling in an Mdm2-sensitive tumor suppressor pathway. Mol Cell Biol, 24:9327-38. (PubMed:15485902)
4. Chen H et al. (2008) Early pre-implantation lethality in mice carrying truncated mutation in the RNA polymerase 1-2 gene. Biochem Biophys Res Commun, 365:636-42. (PubMed:18023416)
5. Colombo E et al. (2005) Nucleophosmin is required for DNA integrity and p19Arf protein stability. Mol Cell Biol, 25:8874-86. (PubMed:16199867)
6. Crawford NP et al. (2009) The metastasis efficiency modifier ribosomal RNA processing 1 homolog B (RRP1B) is a chromatin-associated factor. J Biol Chem, 284:28660-73. (PubMed:19710015)
7. Grisendi S et al. (2005) Role of nucleophosmin in embryonic development and tumorigenesis. Nature, 437:147-53. (PubMed:16007073)
8. Huang N et al. (2005) Protein NPM3 interacts with the multifunctional nucleolar protein B23/nucleophosmin and inhibits ribosome biogenesis. J Biol Chem, 280:5496-502. (PubMed:15596447)
9. Kurki S et al. (2004) Nucleolar protein NPM interacts with HDM2 and protects tumor suppressor protein p53 from HDM2-mediated degradation. Cancer Cell, 5:465-75. (PubMed:15144954)
10. Lorenzen JA et al. (2005) Rbm19 is a nucleolar protein expressed in crypt/progenitor cells of the intestinal epithelium. Gene Expr Patterns, 6:45-56. (PubMed:16027046)
11. Ma Z et al. (2006) Interaction between ROCK II and nucleophosmin/B23 in the regulation of centrosome duplication. Mol Cell Biol, 26:9016-34. (PubMed:17015463)
12. Maggi LB Jr et al. (2008) Nucleophosmin serves as a rate-limiting nuclear export chaperone for the Mammalian ribosome. Mol Cell Biol, 28:7050-65. (PubMed:18809582)
13. Meder VS et al. (2005) PARP-1 and PARP-2 interact with nucleophosmin/B23 and accumulate in transcriptionally active nucleoli. J Cell Sci, 118:211-222. (PubMed:15615785)
14. Misawa K et al. (2000) A method to identify cDNAs based on localization of green fluorescent protein fusion products. Proc Natl Acad Sci U S A, 97:3062-6. (PubMed:10716735)
15. Otto J. (1980) Submandibular gland esterproteases. Mouse News Lett, 63:12.
16. Romanova LG et al. (2006) Implication of Nucleolar Protein SURF6 in Ribosome Biogenesis and Preimplantation Mouse Development. Biol Reprod, 75:690-6. (PubMed:16855206)
17. Shinmura K et al. (2005) Characterization of centrosomal association of nucleophosmin/B23 linked to Crm1 activity. FEBS Lett, 579:6621-34. (PubMed:16297385)
18. Tarapore P et al. (2006) Thr199 phosphorylation targets nucleophosmin to nuclear speckles and represses pre-mRNA processing. FEBS Lett, 580:399-409. (PubMed:16376875)
19. Wu MH et al. (2002) UV stimulation of nucleophosmin/B23 expression is an immediate-early gene response induced by damaged DNA. J Biol Chem, 277:48234-40. (PubMed:12374805)
20. Yu Y et al. (2006) Nucleophosmin is essential for ribosomal protein L5 nuclear export. Mol Cell Biol, 26:3798-809. (PubMed:16648475)
21. Yuan X et al. (2005) Genetic inactivation of the transcription factor TIF-IA leads to nucleolar disruption, cell cycle arrest, and p53-mediated apoptosis. Mol Cell, 19:77-87. (PubMed:15989966)

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Gene Ontology Evidence Code Abbreviations:

EXP Inferred from experiment

IC Inferred by curator

IDA Inferred from direct assay

IEA Inferred from electronic annotation

IGI Inferred from genetic interaction

IMP Inferred from mutant phenotype

IPI Inferred from physical interaction

ISS Inferred from sequence or structural similarity

ISO Inferred from sequence orthology

ISA Inferred from sequence alignment

ISM Inferred from sequence model

NAS Non-traceable author statement

ND No biological data available

RCA Reviewed computational analysis

TAS Traceable author statement

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