Details for: NPM1

Gene ID: 4869

Symbol: NPM1

Ensembl ID: ENSG00000181163

Description: nucleophosmin 1

Associated with

Cells (max top 100)

(Cell Significance Index and respective Thresholds are uniquely calculated using our advanced thresholding algorithms to reveal cell-specific gene markers)

  • Cell Name: polychromatophilic erythroblast (CL0000550)
    Fold Change: 904.5601
    Cell Significance Index: -140.7000
  • Cell Name: embryonic stem cell (CL0002322)
    Fold Change: 431.2199
    Cell Significance Index: -177.6400
  • Cell Name: hematopoietic oligopotent progenitor cell (CL0002032)
    Fold Change: 416.4114
    Cell Significance Index: -105.6200
  • Cell Name: mucosal type mast cell (CL0000485)
    Fold Change: 392.9285
    Cell Significance Index: -159.6300
  • Cell Name: smooth muscle fiber of ileum (CL1000278)
    Fold Change: 368.8025
    Cell Significance Index: -174.1200
  • Cell Name: peripheral blood mononuclear cell (CL2000001)
    Fold Change: 340.9312
    Cell Significance Index: -175.3700
  • Cell Name: ileal goblet cell (CL1000326)
    Fold Change: 260.3342
    Cell Significance Index: -174.6900
  • Cell Name: ciliated cell of the bronchus (CL0002332)
    Fold Change: 168.5480
    Cell Significance Index: -160.9200
  • Cell Name: orthochromatic erythroblast (CL0000552)
    Fold Change: 131.2780
    Cell Significance Index: -161.8600
  • Cell Name: stromal cell of bone marrow (CL0010001)
    Fold Change: 44.2062
    Cell Significance Index: -174.4400
  • Cell Name: CD8-positive, alpha-beta regulatory T cell (CL0000795)
    Fold Change: 33.7495
    Cell Significance Index: -103.6600
  • Cell Name: CD8-alpha-beta-positive, alpha-beta intraepithelial T cell (CL0000796)
    Fold Change: 28.3964
    Cell Significance Index: -76.0700
  • Cell Name: epidermal Langerhans cell (CL0002457)
    Fold Change: 20.0175
    Cell Significance Index: -43.8100
  • Cell Name: theca cell (CL0000503)
    Fold Change: 19.2084
    Cell Significance Index: 112.8500
  • Cell Name: interstitial cell of ovary (CL0002094)
    Fold Change: 16.3473
    Cell Significance Index: 209.3600
  • Cell Name: skeletal muscle myoblast (CL0000515)
    Fold Change: 12.1209
    Cell Significance Index: 131.7700
  • Cell Name: fibroblast of dermis (CL0002551)
    Fold Change: 11.2251
    Cell Significance Index: 234.9600
  • Cell Name: mesonephric nephron tubule epithelial cell (CL1000022)
    Fold Change: 9.8292
    Cell Significance Index: 341.5600
  • Cell Name: granulosa cell (CL0000501)
    Fold Change: 9.7351
    Cell Significance Index: 255.9800
  • Cell Name: kidney cell (CL1000497)
    Fold Change: 9.7254
    Cell Significance Index: 77.6500
  • Cell Name: luminal adaptive secretory precursor cell of mammary gland (CL4033057)
    Fold Change: 8.7899
    Cell Significance Index: 413.1200
  • Cell Name: fibroblast of mammary gland (CL0002555)
    Fold Change: 7.9946
    Cell Significance Index: 229.1700
  • Cell Name: peg cell (CL4033014)
    Fold Change: 7.8220
    Cell Significance Index: 180.7200
  • Cell Name: stromal cell of ovary (CL0002132)
    Fold Change: 6.7102
    Cell Significance Index: 921.5000
  • Cell Name: sebum secreting cell (CL0000317)
    Fold Change: 6.1762
    Cell Significance Index: 436.8100
  • Cell Name: vascular lymphangioblast (CL0005022)
    Fold Change: 5.9673
    Cell Significance Index: 105.4500
  • Cell Name: lactocyte (CL0002325)
    Fold Change: 5.9507
    Cell Significance Index: 768.7900
  • Cell Name: tonsil germinal center B cell (CL2000006)
    Fold Change: 5.8568
    Cell Significance Index: 690.7000
  • Cell Name: basal cell of urothelium (CL1000486)
    Fold Change: 5.8444
    Cell Significance Index: 718.6200
  • Cell Name: cell in vitro (CL0001034)
    Fold Change: 5.7526
    Cell Significance Index: 3141.6300
  • Cell Name: oral mucosa squamous cell (CL1001576)
    Fold Change: 5.5091
    Cell Significance Index: 47.3400
  • Cell Name: CD4-positive, alpha-beta memory T cell, CD45RO-positive (CL0001204)
    Fold Change: 5.0073
    Cell Significance Index: 147.0600
  • Cell Name: hair follicular keratinocyte (CL2000092)
    Fold Change: 4.9517
    Cell Significance Index: 2189.2500
  • Cell Name: intermediate cell of urothelium (CL4030055)
    Fold Change: 4.9219
    Cell Significance Index: 887.2700
  • Cell Name: basal cell of prostate epithelium (CL0002341)
    Fold Change: 4.8620
    Cell Significance Index: 132.3400
  • Cell Name: progenitor cell of mammary luminal epithelium (CL0009116)
    Fold Change: 4.6182
    Cell Significance Index: 344.1900
  • Cell Name: early pro-B cell (CL0002046)
    Fold Change: 4.6159
    Cell Significance Index: 297.8000
  • Cell Name: endothelial cell of venule (CL1000414)
    Fold Change: 4.3898
    Cell Significance Index: 49.8700
  • Cell Name: umbrella cell of urothelium (CL4030056)
    Fold Change: 3.0428
    Cell Significance Index: 28.0200
  • Cell Name: odontoblast (CL0000060)
    Fold Change: 3.0313
    Cell Significance Index: 388.5900
  • Cell Name: microfold cell of epithelium of small intestine (CL1000353)
    Fold Change: 2.9638
    Cell Significance Index: 204.9700
  • Cell Name: acinar cell of salivary gland (CL0002623)
    Fold Change: 2.8356
    Cell Significance Index: 132.2100
  • Cell Name: glycinergic neuron (CL1001509)
    Fold Change: 2.8084
    Cell Significance Index: 147.4500
  • Cell Name: pancreatic acinar cell (CL0002064)
    Fold Change: 2.3489
    Cell Significance Index: 401.0900
  • Cell Name: placental villous trophoblast (CL2000060)
    Fold Change: 2.0508
    Cell Significance Index: 54.7600
  • Cell Name: luminal hormone-sensing cell of mammary gland (CL4033058)
    Fold Change: 1.9101
    Cell Significance Index: 11.7600
  • Cell Name: neoplastic cell (CL0001063)
    Fold Change: 1.7932
    Cell Significance Index: 355.8700
  • Cell Name: bladder urothelial cell (CL1001428)
    Fold Change: 1.0066
    Cell Significance Index: 52.2900
  • Cell Name: pancreatic endocrine cell (CL0008024)
    Fold Change: 0.9754
    Cell Significance Index: 111.3400
  • Cell Name: pulmonary alveolar epithelial cell (CL0000322)
    Fold Change: 0.8203
    Cell Significance Index: 620.8800
  • Cell Name: tuft cell of colon (CL0009041)
    Fold Change: 0.3426
    Cell Significance Index: 309.3400
  • Cell Name: kidney loop of Henle cortical thick ascending limb epithelial cell (CL1001109)
    Fold Change: 0.3227
    Cell Significance Index: 236.5800
  • Cell Name: L2/3-6 intratelencephalic projecting glutamatergic neuron (CL4023040)
    Fold Change: 0.3150
    Cell Significance Index: 63.1900
  • Cell Name: colon goblet cell (CL0009039)
    Fold Change: 0.3014
    Cell Significance Index: 29.8200
  • Cell Name: mesenchymal cell (CL0008019)
    Fold Change: 0.2575
    Cell Significance Index: 4.3100
  • Cell Name: obsolete caudal ganglionic eminence derived GABAergic cortical interneuron (CL4023070)
    Fold Change: 0.2518
    Cell Significance Index: 90.3000
  • Cell Name: enteroendocrine cell of colon (CL0009042)
    Fold Change: 0.0671
    Cell Significance Index: 12.7700
  • Cell Name: pigmented epithelial cell (CL0000529)
    Fold Change: -0.0008
    Cell Significance Index: -1.5100
  • Cell Name: abnormal cell (CL0001061)
    Fold Change: -0.0233
    Cell Significance Index: -2.3800
  • Cell Name: pancreatic A cell (CL0000171)
    Fold Change: -0.0536
    Cell Significance Index: -39.7300
  • Cell Name: anterior lens cell (CL0002223)
    Fold Change: -0.0812
    Cell Significance Index: -149.8100
  • Cell Name: lens epithelial cell (CL0002224)
    Fold Change: -0.1013
    Cell Significance Index: -155.9200
  • Cell Name: secondary lens fiber (CL0002225)
    Fold Change: -0.1211
    Cell Significance Index: -164.6300
  • Cell Name: pancreatic PP cell (CL0002275)
    Fold Change: -0.1272
    Cell Significance Index: -79.4300
  • Cell Name: paneth cell of epithelium of small intestine (CL1000343)
    Fold Change: -0.1288
    Cell Significance Index: -2.7900
  • Cell Name: non-pigmented ciliary epithelial cell (CL0002304)
    Fold Change: -0.1752
    Cell Significance Index: -111.3000
  • Cell Name: type B pancreatic cell (CL0000169)
    Fold Change: -0.1829
    Cell Significance Index: -103.1400
  • Cell Name: ciliary muscle cell (CL1000443)
    Fold Change: -0.2950
    Cell Significance Index: -133.8900
  • Cell Name: pancreatic D cell (CL0000173)
    Fold Change: -0.2973
    Cell Significance Index: -62.6200
  • Cell Name: pro-T cell (CL0000827)
    Fold Change: -0.4368
    Cell Significance Index: -11.1600
  • Cell Name: dopaminergic neuron (CL0000700)
    Fold Change: -0.4517
    Cell Significance Index: -129.9600
  • Cell Name: basal epithelial cell of tracheobronchial tree (CL0002329)
    Fold Change: -0.5103
    Cell Significance Index: -14.2600
  • Cell Name: kidney loop of Henle descending limb epithelial cell (CL1001021)
    Fold Change: -0.5439
    Cell Significance Index: -43.0800
  • Cell Name: epithelial cell of small intestine (CL0002254)
    Fold Change: -0.5785
    Cell Significance Index: -94.0800
  • Cell Name: small intestine goblet cell (CL1000495)
    Fold Change: -0.7281
    Cell Significance Index: -25.5900
  • Cell Name: pancreatic ductal cell (CL0002079)
    Fold Change: -0.8529
    Cell Significance Index: -97.7100
  • Cell Name: enterocyte of epithelium of large intestine (CL0002071)
    Fold Change: -0.8925
    Cell Significance Index: -40.4600
  • Cell Name: pigmented ciliary epithelial cell (CL0002303)
    Fold Change: -0.9244
    Cell Significance Index: -134.3700
  • Cell Name: epithelial cell of stomach (CL0002178)
    Fold Change: -0.9516
    Cell Significance Index: -110.9000
  • Cell Name: retinal progenitor cell (CL0002672)
    Fold Change: -0.9832
    Cell Significance Index: -55.1700
  • Cell Name: CD4-positive, alpha-beta thymocyte (CL0000810)
    Fold Change: -1.0111
    Cell Significance Index: -17.4300
  • Cell Name: neutrophil progenitor cell (CL0000834)
    Fold Change: -1.0531
    Cell Significance Index: -28.1700
  • Cell Name: forebrain neuroblast (CL1000042)
    Fold Change: -1.1162
    Cell Significance Index: -68.6100
  • Cell Name: transit amplifying cell of colon (CL0009011)
    Fold Change: -1.1184
    Cell Significance Index: -35.8200
  • Cell Name: eye photoreceptor cell (CL0000287)
    Fold Change: -1.2974
    Cell Significance Index: -81.7700
  • Cell Name: lung endothelial cell (CL1001567)
    Fold Change: -1.4437
    Cell Significance Index: -75.2000
  • Cell Name: enterocyte of epithelium of small intestine (CL1000334)
    Fold Change: -1.4447
    Cell Significance Index: -41.6300
  • Cell Name: gut absorptive cell (CL0000677)
    Fold Change: -1.4792
    Cell Significance Index: -88.8000
  • Cell Name: smooth muscle cell of sphincter of pupil (CL0002243)
    Fold Change: -1.6160
    Cell Significance Index: -168.2600
  • Cell Name: cardiac muscle myoblast (CL0000513)
    Fold Change: -1.6255
    Cell Significance Index: -124.7400
  • Cell Name: endothelial cell of placenta (CL0009092)
    Fold Change: -1.7445
    Cell Significance Index: -10.5400
  • Cell Name: CD14-positive, CD16-negative classical monocyte (CL0002057)
    Fold Change: -1.8390
    Cell Significance Index: -33.9900
  • Cell Name: fibro/adipogenic progenitor cell (CL0009099)
    Fold Change: -2.1416
    Cell Significance Index: -108.2300
  • Cell Name: conjunctival epithelial cell (CL1000432)
    Fold Change: -2.1754
    Cell Significance Index: -29.6800
  • Cell Name: hippocampal granule cell (CL0001033)
    Fold Change: -2.3190
    Cell Significance Index: -155.9300
  • Cell Name: intestinal tuft cell (CL0019032)
    Fold Change: -2.5592
    Cell Significance Index: -156.9100
  • Cell Name: perivascular cell (CL4033054)
    Fold Change: -2.6401
    Cell Significance Index: -12.1900
  • Cell Name: enteroendocrine cell of small intestine (CL0009006)
    Fold Change: -2.7351
    Cell Significance Index: -68.3700
  • Cell Name: germ cell (CL0000586)
    Fold Change: -2.8786
    Cell Significance Index: -21.7400
  • Cell Name: neuron associated cell (CL0000095)
    Fold Change: -3.0111
    Cell Significance Index: -123.3800

Cell ID: Standard Cell Ontology term used for mapping and comparing cells across experiments. Ensures consistency in analyzing cellular functions across tissues.
Fold Change: Represents the ratio of the current Cell Significance Index to the Cell Significance Index Threshold, indicating how much the gene expression has changed compared to a baseline.
Cell Significance Index: Reflects how strongly a gene is expressed in this specific cell.

Cell ID: Standard Cell Ontology term used for mapping and comparing cells across experiments. Ensures consistency in analyzing cellular functions across tissues.
Fold Change: Represents the ratio of the current Cell Significance Index to the Cell Significance Index Threshold, indicating how much the gene expression has changed compared to a baseline.
Cell Significance Index: Reflects how strongly a gene is expressed in this cell type. Calculated using techniques like effect size estimation and bootstrapping for reliability.

Cell ID: Standard Cell Ontology term used for mapping and comparing cells across experiments. Ensures consistency in analyzing cellular functions across tissues.
Fold Change: Represents the ratio of the current Cell Significance Index to the Cell Significance Index Threshold, indicating how much the gene expression has changed compared to a baseline.
Cell Significance Index: Reflects how strongly a gene is expressed in this cell type. Calculated using techniques like effect size estimation and bootstrapping for reliability.

Other Information

**Key Characteristics** NPM1 is a 215-kDa protein that belongs to the nucleophosmin family. It is characterized by its high phosphoserine content, which allows it to interact with chromatin and other proteins. NPM1 is a multifunctional protein that regulates various cellular processes, including: 1. Cell cycle regulation: NPM1 promotes cell cycle progression by regulating the activity of cyclin-dependent kinases and the phosphatase activity of Wee1. 2. DNA repair: NPM1 regulates DNA repair processes, including nucleotide excision repair and base excision repair. 3. Transcriptional control: NPM1 regulates the activity of transcription factors, such as NF-κB and AP-2, which are involved in cell proliferation and differentiation. 4. Chromatin remodeling: NPM1 regulates chromatin remodeling by interacting with chromatin-modifying enzymes, such as histone deacetylases and histone acetyltransferases. **Pathways and Functions** NPM1 is involved in several signaling pathways, including: 1. Alk signaling pathway: NPM1 is a downstream effector of the Alk (Anaplastic Lymphoma Kinase) signaling pathway, which is involved in cell proliferation and survival. 2. NF-κB signaling pathway: NPM1 regulates the activity of NF-κB, a transcription factor involved in cell proliferation, differentiation, and survival. 3. AP-2 signaling pathway: NPM1 regulates the activity of AP-2, a transcription factor involved in cell proliferation and differentiation. 4. DNA damage response pathway: NPM1 regulates the activity of DNA damage response proteins, such as ATM and ATR. NPM1's functions include: 1. Cell cycle regulation: NPM1 promotes cell cycle progression by regulating the activity of cyclin-dependent kinases and the phosphatase activity of Wee1. 2. DNA repair: NPM1 regulates DNA repair processes, including nucleotide excision repair and base excision repair. 3. Transcriptional control: NPM1 regulates the activity of transcription factors, such as NF-κB and AP-2, which are involved in cell proliferation and differentiation. 4. Chromatin remodeling: NPM1 regulates chromatin remodeling by interacting with chromatin-modifying enzymes, such as histone deacetylases and histone acetyltransferases. **Clinical Significance** Mutations in the NPM1 gene have been associated with several diseases, including: 1. Acute myeloid leukemia (AML): NPM1 mutations are a common genetic alteration in AML and are associated with a poor prognosis. 2. Solid tumors: NPM1 mutations have been associated with an increased risk of solid tumors, including breast, lung, and colon cancer. 3. Leukemia: NPM1 mutations are a common genetic alteration in leukemia and are associated with a poor prognosis. 4. Cancer therapy: NPM1 is a target for cancer therapy, and inhibitors of NPM1 have been developed to treat AML and other cancers. In conclusion, NPM1 is a multifunctional protein that plays a crucial role in various cellular processes, including cell cycle regulation, DNA repair, and transcriptional control. Mutations in the NPM1 gene have been associated with several diseases, including leukemia and solid tumors, and NPM1 is a target for cancer therapy. Further research is needed to fully understand the mechanisms of NPM1's functions and its role in human disease.

Genular Protein ID: 2547930731

Symbol: NPM_HUMAN

Name: Nucleophosmin

UniProtKB Accession Codes:

P06748 A8K3N7 B5BU00 D3DQL6 P08693 Q12826 Q13440 Q13441 Q14115 Q5EU94 Q5EU95 Q5EU96 Q5EU97 Q5EU98 Q5EU99 Q6V962 Q8WTW5 Q96AT6 Q96DC4 Q96EA5 Q9BYG9 Q9UDJ7

Database IDs:

AGR 1 AlphaFoldDB 1 Antibodypedia 1 BMRB 1 Bgee 1 BindingDB 1 BioGRID 1 BioGRID-ORCS 1 BioMuta 1 CCDS 3 CORUM 1 CTD 1 ChEMBL 1 ChiTaRS 1 DIP 1 DMDM 1 DNASU 1 DisGeNET 1 DisProt 1 DrugBank 1 DrugCentral 1 EMBL 46 EMDB 1 Ensembl 5 EvolutionaryTrace 1 ExpressionAtlas 1 GO 59 Gene3D 2 GeneCards 1 GeneTree 1 GeneWiki 1 GenomeRNAi 1 GlyCosmos 1 GlyGen 1 HGNC 1 HOGENOM 1 HPA 1 IDEAL 1 InParanoid 1 IntAct 1 InterPro 4 KEGG 1 MANE-Select 1 MIM 1 MINT 1 MalaCards 1 MassIVE 1 MetOSite 1 NCBI Taxonomy 1 OMA 1 OpenTargets 1 Orphanet 7 OrthoDB 1 PANTHER 2 PDB 8 PDBsum 8 PIR 2 PRIDE 1 PRO 1 PathwayCommons 1 PaxDb 1 PeptideAtlas 1 Pfam 2 PharmGKB 1 Pharos 1 PhosphoSitePlus 1 PhylomeDB 1 Proteomes 1 ProteomicsDB 3 Pumba 1 REPRODUCTION-2DPAGE 1 RNAct 1 Reactome 10 RefSeq 3 SIGNOR 1 SMR 1 STRING 1 SUPFAM 1 SignaLink 1 SwissPalm 1 TopDownProteomics 3 TreeFam 1 UCSC 1 VEuPathDB 1 eggNOG 1 iPTMnet 1 jPOST 1 neXtProt 1

Citations:

PubMed ID: 2713355

Title: Characterization of the cDNA encoding human nucleophosmin and studies of its role in normal and abnormal growth.

PubMed ID: 2713355

DOI: 10.1021/bi00429a017

PubMed ID: 2775293

Title: The nucleotide sequence of a human cDNA encoding the highly conserved nucleolar phosphoprotein B23.

PubMed ID: 2775293

DOI: 10.1016/0006-291x(89)92100-1

PubMed ID: 2478125

Title: Isolation and characterization of a molecular cDNA clone of a human mRNA from interferon-treated cells encoding nucleolar protein B23, numatrin.

PubMed ID: 2478125

DOI: 10.1016/0006-291x(89)91699-9

PubMed ID: 9092633

Title: Isolation and characterization of the human nucleophosmin/B23 (NPM) gene: identification of the YY1 binding site at the 5' enhancer region.

PubMed ID: 9092633

DOI: 10.1093/nar/25.6.1225

PubMed ID: 15659725

Title: Cytoplasmic nucleophosmin in acute myelogenous leukemia with a normal karyotype.

PubMed ID: 15659725

DOI: 10.1056/nejmoa041974

PubMed ID: 16574551

Title: Cytoplasmic nucleophosmin in myeloid sarcoma occurring 20 years after diagnosis of acute myeloid leukaemia.

PubMed ID: 16574551

DOI: 10.1016/s1470-2045(06)70661-1

PubMed ID: 14702039

Title: Complete sequencing and characterization of 21,243 full-length human cDNAs.

PubMed ID: 14702039

DOI: 10.1038/ng1285

PubMed ID: 19054851

Title: Human protein factory for converting the transcriptome into an in vitro-expressed proteome.

PubMed ID: 19054851

DOI: 10.1038/nmeth.1273

PubMed ID: 15489334

Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).

PubMed ID: 15489334

DOI: 10.1101/gr.2596504

PubMed ID: 8562957

Title: The t(5;17) variant of acute promyelocytic leukemia expresses a nucleophosmin-retinoic acid receptor fusion.

PubMed ID: 8562957

PubMed ID: 8122112

Title: Fusion of a kinase gene, ALK, to a nucleolar protein gene, NPM, in non-Hodgkin's lymphoma.

PubMed ID: 8122112

DOI: 10.1126/science.8122112

PubMed ID: 8633037

Title: Characterization of the transforming activity of p80, a hyperphosphorylated protein in a Ki-1 lymphoma cell line with chromosomal translocation t(2;5).

PubMed ID: 8633037

DOI: 10.1073/pnas.93.9.4181

PubMed ID: 2602120

Title: Nucleotide sequence of a cDNA clone representing a third allele of human protein B23.

PubMed ID: 2602120

PubMed ID: 9150948

Title: A two-dimensional gel database of human colon carcinoma proteins.

PubMed ID: 9150948

DOI: 10.1002/elps.1150180344

PubMed ID: 8314759

Title: Nucleolar targeting signal of Rex protein of human T-cell leukemia virus type I specifically binds to nucleolar shuttle protein B-23.

PubMed ID: 8314759

DOI: 10.1016/s0021-9258(19)85191-8

PubMed ID: 12882984

Title: Nucleophosmin interacts with and inhibits the catalytic function of eukaryotic initiation factor 2 kinase PKR.

PubMed ID: 12882984

DOI: 10.1074/jbc.m301392200

PubMed ID: 3944116

Title: Amino acid sequence of protein B23 phosphorylation site.

PubMed ID: 3944116

DOI: 10.1016/s0021-9258(17)36022-2

PubMed ID: 2429957

Title: Amino acid sequence of a specific antigenic peptide of protein B23.

PubMed ID: 2429957

DOI: 10.1016/s0021-9258(18)67023-1

PubMed ID: 8089149

Title: Identification of the nuclear and nucleolar localization signals of the protein p120. Interaction with translocation protein B23.

PubMed ID: 8089149

DOI: 10.1016/s0021-9258(17)31583-1

PubMed ID: 7631008

Title: Modification of nucleolar protein B23 after exposure to ionizing radiation.

PubMed ID: 7631008

DOI: 10.2307/3579152

PubMed ID: 8570204

Title: The t(3;5)(q25.1;q34) of myelodysplastic syndrome and acute myeloid leukemia produces a novel fusion gene, NPM-MLF1.

PubMed ID: 8570204

PubMed ID: 11051553

Title: Nucleophosmin/B23 is a target of CDK2/cyclin E in centrosome duplication.

PubMed ID: 11051553

DOI: 10.1016/s0092-8674(00)00093-3

PubMed ID: 11309377

Title: The nucleolar phosphoprotein B23 interacts with hepatitis delta antigens and modulates the hepatitis delta virus RNA replication.

PubMed ID: 11309377

DOI: 10.1074/jbc.m010087200

PubMed ID: 12058066

Title: The RNA binding activity of a ribosome biogenesis factor, nucleophosmin/B23, is modulated by phosphorylation with a cell cycle-dependent kinase and by association with its subtype.

PubMed ID: 12058066

DOI: 10.1091/mbc.02-03-0036

PubMed ID: 12429849

Title: Functional proteomic analysis of human nucleolus.

PubMed ID: 12429849

DOI: 10.1091/mbc.e02-05-0271

PubMed ID: 12214246

Title: The role of nucleophosmin in centrosome duplication.

PubMed ID: 12214246

DOI: 10.1038/sj.onc.1205708

PubMed ID: 14654843

Title: Proteomic characterization of the human centrosome by protein correlation profiling.

PubMed ID: 14654843

DOI: 10.1038/nature02166

PubMed ID: 15388344

Title: Nek2A kinase regulates the localization of numatrin to centrosome in mitosis.

PubMed ID: 15388344

DOI: 10.1016/j.febslet.2004.08.047

PubMed ID: 15190079

Title: B23/nucleophosmin serine 4 phosphorylation mediates mitotic functions of polo-like kinase 1.

PubMed ID: 15190079

DOI: 10.1074/jbc.m403264200

PubMed ID: 15772089

Title: RPGR ORF15 isoform co-localizes with RPGRIP1 at centrioles and basal bodies and interacts with nucleophosmin.

PubMed ID: 15772089

DOI: 10.1093/hmg/ddi129

PubMed ID: 16107701

Title: Human histone chaperone nucleophosmin enhances acetylation-dependent chromatin transcription.

PubMed ID: 16107701

DOI: 10.1128/mcb.25.17.7534-7545.2005

PubMed ID: 15897463

Title: Sumoylation induced by the Arf tumor suppressor: a p53-independent function.

PubMed ID: 15897463

DOI: 10.1073/pnas.0502978102

PubMed ID: 17081983

Title: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.

PubMed ID: 17081983

DOI: 10.1016/j.cell.2006.09.026

PubMed ID: 16916647

Title: Substrate and functional diversity of lysine acetylation revealed by a proteomics survey.

PubMed ID: 16916647

DOI: 10.1016/j.molcel.2006.06.026

PubMed ID: 17015463

Title: Interaction between ROCK II and nucleophosmin/B23 in the regulation of centrosome duplication.

PubMed ID: 17015463

DOI: 10.1128/mcb.01383-06

PubMed ID: 17924679

Title: Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.

PubMed ID: 17924679

DOI: 10.1021/pr070152u

PubMed ID: 17215513

Title: Aurora-B regulates RNA methyltransferase NSUN2.

PubMed ID: 17215513

DOI: 10.1091/mbc.e06-11-1021

PubMed ID: 18259216

Title: The nucleolar SUMO-specific protease SENP3 reverses SUMO modification of nucleophosmin and is required for rRNA processing.

PubMed ID: 18259216

DOI: 10.1038/embor.2008.3

PubMed ID: 19015314

Title: Nucleolar protein B23/nucleophosmin regulates the vertebrate SUMO pathway through SENP3 and SENP5 proteases.

PubMed ID: 19015314

DOI: 10.1083/jcb.200807185

PubMed ID: 18024471

Title: The structure and functions of NPM1/Nucleophosmin/B23, a multifunctional nucleolar acidic protein.

PubMed ID: 18024471

DOI: 10.1093/jb/mvm222

PubMed ID: 18220336

Title: Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis.

PubMed ID: 18220336

DOI: 10.1021/pr0705441

PubMed ID: 18691976

Title: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle.

PubMed ID: 18691976

DOI: 10.1016/j.molcel.2008.07.007

PubMed ID: 18809582

Title: Nucleophosmin serves as a rate-limiting nuclear export chaperone for the Mammalian ribosome.

PubMed ID: 18809582

DOI: 10.1128/mcb.01548-07

PubMed ID: 18669648

Title: A quantitative atlas of mitotic phosphorylation.

PubMed ID: 18669648

DOI: 10.1073/pnas.0805139105

PubMed ID: 18318008

Title: Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography.

PubMed ID: 18318008

DOI: 10.1002/pmic.200700884

PubMed ID: 19413330

Title: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.

PubMed ID: 19413330

DOI: 10.1021/ac9004309

PubMed ID: 19710015

Title: The metastasis efficiency modifier ribosomal RNA processing 1 homolog B (RRP1B) is a chromatin-associated factor.

PubMed ID: 19710015

DOI: 10.1074/jbc.m109.023457

PubMed ID: 19208757

Title: Nucleolar structure and function are regulated by the deubiquitylating enzyme USP36.

PubMed ID: 19208757

DOI: 10.1242/jcs.044461

PubMed ID: 19188445

Title: APE1/Ref-1 interacts with NPM1 within nucleoli and plays a role in the rRNA quality control process.

PubMed ID: 19188445

DOI: 10.1128/mcb.01337-08

PubMed ID: 19369195

Title: Large-scale proteomics analysis of the human kinome.

PubMed ID: 19369195

DOI: 10.1074/mcp.m800588-mcp200

PubMed ID: 19690332

Title: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions.

PubMed ID: 19690332

DOI: 10.1126/scisignal.2000007

PubMed ID: 19608861

Title: Lysine acetylation targets protein complexes and co-regulates major cellular functions.

PubMed ID: 19608861

DOI: 10.1126/science.1175371

PubMed ID: 20075868

Title: Nucleolar retention of a translational C/EBPalpha isoform stimulates rDNA transcription and cell size.

PubMed ID: 20075868

DOI: 10.1038/emboj.2009.404

PubMed ID: 20159986

Title: Methylation of ribosomal protein S10 by protein-arginine methyltransferase 5 regulates ribosome biogenesis.

PubMed ID: 20159986

DOI: 10.1074/jbc.m110.103911

PubMed ID: 20926688

Title: RRP1B targets PP1 to mammalian cell nucleoli and is associated with pre-60S ribosomal subunits.

PubMed ID: 20926688

DOI: 10.1091/mbc.e10-04-0287

PubMed ID: 20352051

Title: Polo-like kinase 2-dependent phosphorylation of NPM/B23 on serine 4 triggers centriole duplication.

PubMed ID: 20352051

DOI: 10.1371/journal.pone.0009849

PubMed ID: 20333249

Title: Nucleophosmin phosphorylation by v-cyclin-CDK6 controls KSHV latency.

PubMed ID: 20333249

DOI: 10.1371/journal.ppat.1000818

PubMed ID: 20068231

Title: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.

PubMed ID: 20068231

DOI: 10.1126/scisignal.2000475

PubMed ID: 21269460

Title: Initial characterization of the human central proteome.

PubMed ID: 21269460

DOI: 10.1186/1752-0509-5-17

PubMed ID: 21084279

Title: BRCA2 and nucleophosmin coregulate centrosome amplification and form a complex with the Rho effector kinase ROCK2.

PubMed ID: 21084279

DOI: 10.1158/0008-5472.can-10-0030

PubMed ID: 22002061

Title: New centromeric component CENP-W is an RNA-associated nuclear matrix protein that interacts with nucleophosmin/B23 protein.

PubMed ID: 22002061

DOI: 10.1074/jbc.m111.228411

PubMed ID: 21406692

Title: System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation.

PubMed ID: 21406692

DOI: 10.1126/scisignal.2001570

PubMed ID: 22528486

Title: Nucleophosmin (NPM1/B23) interacts with activating transcription factor 5 (ATF5) protein and promotes proteasome- and caspase-dependent ATF5 degradation in hepatocellular carcinoma cells.

PubMed ID: 22528486

DOI: 10.1074/jbc.m112.363622

PubMed ID: 23019224

Title: DDX31 regulates the p53-HDM2 pathway and rRNA gene transcription through its interaction with NPM1 in renal cell carcinomas.

PubMed ID: 23019224

DOI: 10.1158/0008-5472.can-12-1645

PubMed ID: 22223895

Title: Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features.

PubMed ID: 22223895

DOI: 10.1074/mcp.m111.015131

PubMed ID: 22362753

Title: Function of homo- and hetero-oligomers of human nucleoplasmin/nucleophosmin family proteins NPM1, NPM2 and NPM3 during sperm chromatin remodeling.

PubMed ID: 22362753

DOI: 10.1093/nar/gks162

PubMed ID: 23972994

Title: ABH2 couples regulation of ribosomal DNA transcription with DNA alkylation repair.

PubMed ID: 23972994

DOI: 10.1016/j.celrep.2013.07.027

PubMed ID: 23186163

Title: Toward a comprehensive characterization of a human cancer cell phosphoproteome.

PubMed ID: 23186163

DOI: 10.1021/pr300630k

PubMed ID: 24275569

Title: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.

PubMed ID: 24275569

DOI: 10.1016/j.jprot.2013.11.014

PubMed ID: 25218447

Title: Uncovering global SUMOylation signaling networks in a site-specific manner.

PubMed ID: 25218447

DOI: 10.1038/nsmb.2890

PubMed ID: 25114211

Title: Mapping of SUMO sites and analysis of SUMOylation changes induced by external stimuli.

PubMed ID: 25114211

DOI: 10.1073/pnas.1413825111

PubMed ID: 25956029

Title: The nucleolar protein GLTSCR2 is an upstream negative regulator of the oncogenic Nucleophosmin-MYC axis.

PubMed ID: 25956029

DOI: 10.1016/j.ajpath.2015.03.016

PubMed ID: 25772364

Title: SUMO-2 orchestrates chromatin modifiers in response to DNA damage.

PubMed ID: 25772364

DOI: 10.1016/j.celrep.2015.02.033

PubMed ID: 25818168

Title: GLTSCR2 is an upstream negative regulator of nucleophosmin in cervical cancer.

PubMed ID: 25818168

DOI: 10.1111/jcmm.12474

PubMed ID: 25755297

Title: System-wide analysis of SUMOylation dynamics in response to replication stress reveals novel small ubiquitin-like modified target proteins and acceptor lysines relevant for genome stability.

PubMed ID: 25755297

DOI: 10.1074/mcp.o114.044792

PubMed ID: 25944712

Title: N-terminome analysis of the human mitochondrial proteome.

PubMed ID: 25944712

DOI: 10.1002/pmic.201400617

PubMed ID: 28190768

Title: Serine ADP-ribosylation depends on HPF1.

PubMed ID: 28190768

DOI: 10.1016/j.molcel.2017.01.003

PubMed ID: 28112733

Title: Site-specific mapping of the human SUMO proteome reveals co-modification with phosphorylation.

PubMed ID: 28112733

DOI: 10.1038/nsmb.3366

PubMed ID: 17879352

Title: Crystal structure of human nucleophosmin-core reveals plasticity of the pentamer-pentamer interface.

PubMed ID: 17879352

DOI: 10.1002/prot.21504

PubMed ID: 18511415

Title: Structural consequences of nucleophosmin mutations in acute myeloid leukemia.

PubMed ID: 18511415

DOI: 10.1074/jbc.m801706200

Sequence Information:

  • Length: 294
  • Mass: 32575
  • Checksum: 620BC7BA2E4A0054
  • Sequence:
    • MEDSMDMDMS PLRPQNYLFG CELKADKDYH FKVDNDENEH QLSLRTVSLG AGAKDELHIV 
EAEAMNYEGS PIKVTLATLK MSVQPTVSLG GFEITPPVVL RLKCGSGPVH ISGQHLVAVE 
EDAESEDEEE EDVKLLSISG KRSAPGGGSK VPQKKVKLAA DEDDDDDDEE DDDEDDDDDD 
FDDEEAEEKA PVKKSIRDTP AKNAQKSNQN GKDSKPSSTP RSKGQESFKK QEKTPKTPKG 
PSSVEDIKAK MQASIEKGGS LPKVEAKFIN YVKNCFRMTD QEAIQDLWQW RKSL

Genular Protein ID: 2825759989

Symbol: A0A0S2Z4G7_HUMAN

Name: N/A

UniProtKB Accession Codes:

A0A0S2Z4G7

Database IDs:

ARBA 9 AlphaFoldDB 1 Antibodypedia 1 BioGRID-ORCS 1 CTD 1 ChiTaRS 1 DNASU 1 DisGeNET 1 EMBL 4 ExpressionAtlas 1 GO 15 Gene3D 2 InterPro 4 NCBI Taxonomy 1 OrthoDB 1 PANTHER 2 Pfam 4 RefSeq 1 SAM 1 SMR 1 SUPFAM 1 VEuPathDB 1

Citations:

PubMed ID: 11181995

Title: The sequence of the human genome.

PubMed ID: 11181995

DOI: 10.1126/science.1058040

PubMed ID: 26871637

Title: Widespread Expansion of Protein Interaction Capabilities by Alternative Splicing.

PubMed ID: 26871637

DOI: 10.1016/j.cell.2016.01.029

Sequence Information:

  • Length: 265
  • Mass: 29465
  • Checksum: 932BEC3377692D91
  • Sequence:
    • MEDSMDMDMS PLRPQNYLFG CELKADKDYH FKVDNDENEH QLSLRTVSLG AGAKDELHIV 
EAEAMNYEGS PIKVTLATLK MSVQPTVSLG GFEITPPVVL RLKCGSGPVH ISGQHLVAVE 
EDAESEDEEE EDVKLLSISG KRSAPGGGSK VPQKKVKLAA DEDDDDDDEE DDDEDDDDDD 
FDDEEAEEKA PVKKGQESFK KQEKTPKTPK GPSSVEDIKA KMQASIEKGG SLPKVEAKFI 
NYVKNCFRMT DQEAIQDLWQ WRKSL

Genular Protein ID: 489050646

Symbol: A0A140VJQ2_HUMAN

Name: N/A

UniProtKB Accession Codes:

A0A140VJQ2

Database IDs:

ARBA 5 AlphaFoldDB 1 Antibodypedia 1 BioGRID-ORCS 1 CTD 1 DNASU 1 DisGeNET 1 EMBL 2 ExpressionAtlas 1 GO 15 Gene3D 1 InterPro 3 NCBI Taxonomy 1 OrthoDB 1 PANTHER 2 Pfam 2 RefSeq 1 SAM 1 SMR 1 SUPFAM 1 VEuPathDB 1

Sequence Information:

  • Length: 259
  • Mass: 28400
  • Checksum: 6AEAD2909EE0A47A
  • Sequence:
    • MEDSMDMDMS PLRPQNYLFG CELKADKDYH FKVDNDENEH QLSLRTVSLG AGAKDELHIV 
EAEAMNYEGS PIKVTLATLK MSVQPTVSLG GFEITPPVVL RLKCGSGPVH ISGQHLVAVE 
EDAESEDEEE EDVKLLSISG KRSAPGGGSK VPQKKVKLAA DEDDDDDDEE DDDEDDDDDD 
FDDEEAEEKA PVKKSIRDTP AKNAQKSNQN GKDSKPSSTP RSKGQESFKK QEKTPKTPKG 
PSSVEDIKAK MQASIEKAH

Database document:

This is a preview of the gene's schema. Only a few entries are kept for 'singleCellExpressions,' 'mRNAExpressions,' and other large data arrays for visualization purposes. You can zoom in with the mouse wheel for a closer view, and the text will adjust automatically if necessary. For the full schema, download it here.