HCSGD entry for NPM1


1. General information

Official gene symbolNPM1
Entrez ID4869
Gene full namenucleophosmin (nucleolar phosphoprotein B23, numatrin)
Other gene symbolsB23 NPM
Links to Entrez GeneLinks to Entrez Gene

2. Neighbors in the network

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3. Gene ontology annotation

GO ID

GO term

Evidence

Category

GO:0003676Nucleic acid bindingIEAmolecular_function
GO:0003713Transcription coactivator activityIDAmolecular_function
GO:0003723RNA bindingIDAmolecular_function
GO:0004860Protein kinase inhibitor activityIDAmolecular_function
GO:0005515Protein bindingIPImolecular_function
GO:0005634NucleusIDA ISScellular_component
GO:0005654NucleoplasmIDA TAScellular_component
GO:0005730NucleolusIDAcellular_component
GO:0005737CytoplasmIDA ISScellular_component
GO:0005813CentrosomeIDA ISScellular_component
GO:0005829CytosolTAScellular_component
GO:0006281DNA repairIDAbiological_process
GO:0006334Nucleosome assemblyIDA TASbiological_process
GO:0006886Intracellular protein transportTASbiological_process
GO:0006913Nucleocytoplasmic transportIDA TASbiological_process
GO:0006950Response to stressIMPbiological_process
GO:0007098Centrosome cycleIMP ISSbiological_process
GO:0007165Signal transductionNASbiological_process
GO:0007569Cell agingIMP ISSbiological_process
GO:0008104Protein localizationIDAbiological_process
GO:0008285Negative regulation of cell proliferationIMP ISSbiological_process
GO:0010826Negative regulation of centrosome duplicationIMPbiological_process
GO:0016032Viral processTASbiological_process
GO:0019901Protein kinase bindingIPImolecular_function
GO:0030529Ribonucleoprotein complexIDAcellular_component
GO:0030957Tat protein bindingIDAmolecular_function
GO:0031616Spindle pole centrosomeIDAcellular_component
GO:0032071Regulation of endodeoxyribonuclease activityIDAbiological_process
GO:0034080CENP-A containing nucleosome assembly at centromereTASbiological_process
GO:0042255Ribosome assemblyTASbiological_process
GO:0042393Histone bindingIDAmolecular_function
GO:0042803Protein homodimerization activityIDAmolecular_function
GO:0043023Ribosomal large subunit bindingIDAmolecular_function
GO:0043024Ribosomal small subunit bindingIDAmolecular_function
GO:0043066Negative regulation of apoptotic processIDA NASbiological_process
GO:0044387Negative regulation of protein kinase activity by regulation of protein phosphorylationIDAbiological_process
GO:0045727Positive regulation of translationIDAbiological_process
GO:0046599Regulation of centriole replicationIMPbiological_process
GO:0046982Protein heterodimerization activityIMPmolecular_function
GO:0051059NF-kappaB bindingIDA ISSmolecular_function
GO:0051082Unfolded protein bindingIDA ISSmolecular_function
GO:0051092Positive regulation of NF-kappaB transcription factor activityIMPbiological_process
GO:0051259Protein oligomerizationIDAbiological_process
GO:0060699Regulation of endoribonuclease activityIDAbiological_process
GO:0060735Regulation of eIF2 alpha phosphorylation by dsRNAIDAbiological_process
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4. Expression levels in datasets

  • Meta-analysis result

p-value upp-value downFDR upFDR down
0.94535253980.06171528060.99999024730.4685341506

  • Individual experiment result
    ( "-" represent NA in the specific microarray platform )

Data sourceUp or downLog fold change
GSE11954Up0.0997938546
GSE13712_SHEARDown-0.3027288812
GSE13712_STATICDown-0.0319874960
GSE19018Down-0.5935569382
GSE19899_A1Down-0.0218058445
GSE19899_A2Down-0.0904331679
PubMed_21979375_A1Up0.0732625694
PubMed_21979375_A2Up0.0308581319
GSE35957Down-0.5135853821
GSE36640Down-0.4053811172
GSE54402Up0.1915739288
GSE9593Down-0.0360199680
GSE43922Down-0.0319573240
GSE24585Down-0.1347671339
GSE37065Down-0.2917459787
GSE28863_A1Up0.0724267922
GSE28863_A2Down-0.0191125208
GSE28863_A3Up0.0038307030
GSE28863_A4Down-0.1129247658
GSE48662Down-0.6928682766

5. Regulation relationships with compounds/drugs/microRNAs

  • Compounds

Not regulated by compounds

  • Drugs

Not regulated by drugs

  • MicroRNAs

  • mirTarBase

MiRNA_name

mirBase ID

miRTarBase ID

Experiment

Support type

References (Pubmed ID)

hsa-miR-296-3pMIMAT0004679MIRT038406CLASHFunctional MTI (Weak)23622248
hsa-miR-93-3pMIMAT0004509MIRT038792CLASHFunctional MTI (Weak)23622248
hsa-miR-421MIMAT0003339MIRT039386CLASHFunctional MTI (Weak)23622248
hsa-miR-625-5pMIMAT0003294MIRT039598CLASHFunctional MTI (Weak)23622248
hsa-miR-598-3pMIMAT0003266MIRT040495CLASHFunctional MTI (Weak)23622248
hsa-miR-92b-3pMIMAT0003218MIRT040565CLASHFunctional MTI (Weak)23622248
hsa-miR-193b-3pMIMAT0002819MIRT041488CLASHFunctional MTI (Weak)23622248
hsa-miR-320aMIMAT0000510MIRT044729CLASHFunctional MTI (Weak)23622248
hsa-miR-149-5pMIMAT0000450MIRT045680CLASHFunctional MTI (Weak)23622248
hsa-miR-125a-5pMIMAT0000443MIRT045754CLASHFunctional MTI (Weak)23622248
hsa-miR-125b-5pMIMAT0000423MIRT045923CLASHFunctional MTI (Weak)23622248
hsa-miR-23b-3pMIMAT0000418MIRT046377CLASHFunctional MTI (Weak)23622248
hsa-miR-15b-5pMIMAT0000417MIRT046385CLASHFunctional MTI (Weak)23622248
hsa-miR-93-5pMIMAT0000093MIRT048875CLASHFunctional MTI (Weak)23622248
hsa-miR-92a-3pMIMAT0000092MIRT049162CLASHFunctional MTI (Weak)23622248
hsa-miR-25-3pMIMAT0000081MIRT050209CLASHFunctional MTI (Weak)23622248
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  • mirRecord
No target information from mirRecord

6. Text-mining results about the gene

Gene occurances in abstracts of cellular senescence-associated articles: 5 abstracts the gene occurs.


PubMed ID of the article

Sentenece the gene occurs

24782448Interactions of two highly acetylated proteins, nucleophosmin (NPM1) and nucleolin, with SIRT6 and SIRT7 were confirmed by co-immunoprecipitation
24782448NPM1 was found to be deacetylated by both SIRT6 and SIRT7
24782448In senescent cells, the acetylation level of NPM1 was increased in conjunction with decreased levels of SIRT6 and SIRT7, suggesting that the acetylation of NPM1 could be regulated by SIRT6 and SIRT7 in the aging process
23536448Nucleophosmin 1, upregulated in adenomas and cancers of the colon, inhibits p53-mediated cellular senescence
23536448Dysregulation of nucleophosmin 1 (NPM1) has been found in numerous solid and hematological malignancies
23536448Our aims were to compare NPM1 expression in normal colon, adenoma and CRC, to correlate their expressions with clinico-pathological parameters, and to assess the biological role of aberrant NPM1 expression in CRC cells
23536448NPM1 transcript levels were studied in human CRC cell lines, whereas a tissue microarray of 57 normal human colon, 40 adenoma and 185 CRC samples were used to analyze NPM1 protein expression by immunohistochemistry
23536448NPM1 transcript levels were 7-11-folds higher in three different human CRC cell lines compared to normal colon cells
23536448NPM1 protein expression was found to be progressively and significantly upregulated in CRC compared to adenomas and in adenomas compared to normal mucosa
23536448Reducing NPM1 expression by siRNA had caused a significant decrease in cell viability, a concomitant increase in cellular senescence and cell cycle arrest
23536448Cellular senescence induced under conditions of forced NPM1 suppression could be prevented by knocking down p53
23536448The differential expression of NPM1 along the normal colon-adenoma-carcinoma progression and its involvement in resisting p53 related senescent growth arrest in CRC cell lines implicate its role in supporting CRC tumorigenesis
18316603Two nucleolar proteins, p14(ARF)/p19(ARF) and B23, were shown to translocate out of the nucleolus after exposure of cells to DNA-damaging agents
18316603We show that redistribution of B23 and p19(ARF) after the exposure to genotoxic stress occurs preferentially when the c-Jun-NH(2)-kinase (JNK) pathway is activated and is inhibited when the JNK pathway is impaired
18316603Instead, c-Jun interacts with B23 in a dose-dependent manner
18316603Hence, we suggest that c-Jun translocates B23 and ARF from the nucleolus after JNK activation by means of protein interactions
17967869However, little is known about how MLF1 functions upstream of the CSN3-COP1-p53 pathway and how its deregulation by the formation of the fusion protein nucleophosmin (NPM)-MLF1, generated by t(3;5)(q25
17967869Here we show that MLF1 is a cytoplasmic-nuclear-shuttling protein and that its nucleolar localization on fusing with NPM prevents the full induction of p53 by both genotoxic and oncogenic cellular stress
17967869The fusion of MLF1 with NPM translocated MLF1 to the nucleolus and abolished the growth-suppressing activity
17546053The leukemia-associated cytoplasmic nucleophosmin mutant is an oncogene with paradoxical functions: Arf inactivation and induction of cellular senescence
17546053Mutations leading to aberrant cytoplasmic localization of Nucleophosmin 1 (NPM1) have been recently identified as the most frequent genetic alteration in acute myelogenous leukemia
17546053However, the oncogenic potential of this nucleophosmin mutant (NPMc+) has never been established, which casts doubt on its role in leukemogenesis
17546053By performing classical transformation assays, we find that NPMc+, but not wild-type NPM, cooperates specifically with adenovirus E1A to transform primary mouse embryonic fibroblasts in soft agar
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