NUP98 | ENSG00000110713 | NCBI 4928

Details for: NUP98

Gene ID: 4928

Symbol: NUP98

Ensembl ID: ENSG00000110713

Description: nucleoporin 98 and 96 precursor

Associated with

Amplification of signal from the kinetochores
(R-HSA-141424)
Amplification of signal from unattached kinetochores via a mad2 inhibitory signal
(R-HSA-141444)
Antiviral mechanism by ifn-stimulated genes
(R-HSA-1169410)
Cell cycle
(R-HSA-1640170)
Cell cycle, mitotic
(R-HSA-69278)
Cell cycle checkpoints
(R-HSA-69620)
Cellular responses to stimuli
(R-HSA-8953897)
Cellular responses to stress
(R-HSA-2262752)
Cellular response to heat stress
(R-HSA-3371556)
Cytokine signaling in immune system
(R-HSA-1280215)
Defective tpr may confer susceptibility towards thyroid papillary carcinoma (tpc)
(R-HSA-5619107)
Disease
(R-HSA-1643685)
Disorders of transmembrane transporters
(R-HSA-5619115)
Eml4 and nudc in mitotic spindle formation
(R-HSA-9648025)
Export of viral ribonucleoproteins from nucleus
(R-HSA-168274)
Gene expression (transcription)
(R-HSA-74160)
Gene silencing by rna
(R-HSA-211000)
Glucose metabolism
(R-HSA-70326)
Glycolysis
(R-HSA-70171)
Hcmv early events
(R-HSA-9609690)
Hcmv infection
(R-HSA-9609646)
Hcmv late events
(R-HSA-9610379)
Hiv infection
(R-HSA-162906)
Hiv life cycle
(R-HSA-162587)
Host interactions of hiv factors
(R-HSA-162909)
Immune system
(R-HSA-168256)
Infectious disease
(R-HSA-5663205)
Influenza infection
(R-HSA-168255)
Influenza viral rna transcription and replication
(R-HSA-168273)
Interactions of rev with host cellular proteins
(R-HSA-177243)
Interactions of vpr with host cellular proteins
(R-HSA-176033)
Interferon signaling
(R-HSA-913531)
Isg15 antiviral mechanism
(R-HSA-1169408)
Late phase of hiv life cycle
(R-HSA-162599)
Metabolism
(R-HSA-1430728)
Metabolism of carbohydrates
(R-HSA-71387)
Metabolism of non-coding rna
(R-HSA-194441)
Metabolism of proteins
(R-HSA-392499)
Metabolism of rna
(R-HSA-8953854)
Mitotic anaphase
(R-HSA-68882)
Mitotic metaphase and anaphase
(R-HSA-2555396)
Mitotic prometaphase
(R-HSA-68877)
Mitotic prophase
(R-HSA-68875)
Mitotic spindle checkpoint
(R-HSA-69618)
M phase
(R-HSA-68886)
Nep/ns2 interacts with the cellular export machinery
(R-HSA-168333)
Ns1 mediated effects on host pathways
(R-HSA-168276)
Nuclear envelope (ne) reassembly
(R-HSA-2995410)
Nuclear envelope breakdown
(R-HSA-2980766)
Nuclear import of rev protein
(R-HSA-180746)
Nuclear pore complex (npc) disassembly
(R-HSA-3301854)
Post-translational protein modification
(R-HSA-597592)
Postmitotic nuclear pore complex (npc) reformation
(R-HSA-9615933)
Processing of capped intron-containing pre-mrna
(R-HSA-72203)
Regulation of glucokinase by glucokinase regulatory protein
(R-HSA-170822)
Regulation of hsf1-mediated heat shock response
(R-HSA-3371453)
Resolution of sister chromatid cohesion
(R-HSA-2500257)
Rev-mediated nuclear export of hiv rna
(R-HSA-165054)
Rho gtpase effectors
(R-HSA-195258)
Rho gtpases activate formins
(R-HSA-5663220)
Sars-cov-2 activates/modulates innate and adaptive immune responses
(R-HSA-9705671)
Sars-cov-2 infection
(R-HSA-9694516)
Sars-cov-2-host interactions
(R-HSA-9705683)
Sars-cov infections
(R-HSA-9679506)
Separation of sister chromatids
(R-HSA-2467813)
Signaling by rho gtpases
(R-HSA-194315)
Signaling by rho gtpases, miro gtpases and rhobtb3
(R-HSA-9716542)
Signal transduction
(R-HSA-162582)
Slc transporter disorders
(R-HSA-5619102)
Snrnp assembly
(R-HSA-191859)
Sumo e3 ligases sumoylate target proteins
(R-HSA-3108232)
Sumoylation
(R-HSA-2990846)
Sumoylation of chromatin organization proteins
(R-HSA-4551638)
Sumoylation of dna damage response and repair proteins
(R-HSA-3108214)
Sumoylation of dna replication proteins
(R-HSA-4615885)
Sumoylation of rna binding proteins
(R-HSA-4570464)
Sumoylation of sumoylation proteins
(R-HSA-4085377)
Sumoylation of ubiquitinylation proteins
(R-HSA-3232142)
Transcriptional regulation by small rnas
(R-HSA-5578749)
Transport of mature mrna derived from an intron-containing transcript
(R-HSA-159236)
Transport of mature mrna derived from an intronless transcript
(R-HSA-159231)
Transport of mature mrnas derived from intronless transcripts
(R-HSA-159234)
Transport of mature transcript to cytoplasm
(R-HSA-72202)
Transport of ribonucleoproteins into the host nucleus
(R-HSA-168271)
Transport of the slbp dependant mature mrna
(R-HSA-159230)
Transport of the slbp independent mature mrna
(R-HSA-159227)
Trna processing
(R-HSA-72306)
Trna processing in the nucleus
(R-HSA-6784531)
Viral infection pathways
(R-HSA-9824446)
Viral messenger rna synthesis
(R-HSA-168325)
Vpr-mediated nuclear import of pics
(R-HSA-180910)
Mrna binding
(GO:0003729)
Nuclear localization sequence binding
(GO:0008139)
Protein binding
(GO:0005515)
Rna binding
(GO:0003723)
Serine-type peptidase activity
(GO:0008236)
Structural constituent of nuclear pore
(GO:0017056)
Transcription coactivator activity
(GO:0003713)

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: 278.7614
Cell Significance Index: -43.3600
Cell Name: hematopoietic oligopotent progenitor cell (CL0002032)
Fold Change: 171.5401
Cell Significance Index: -43.5100
Cell Name: embryonic stem cell (CL0002322)
Fold Change: 105.7659
Cell Significance Index: -43.5700
Cell Name: smooth muscle fiber of ileum (CL1000278)
Fold Change: 100.3129
Cell Significance Index: -47.3600
Cell Name: mucosal type mast cell (CL0000485)
Fold Change: 98.4844
Cell Significance Index: -40.0100
Cell Name: peripheral blood mononuclear cell (CL2000001)
Fold Change: 87.1040
Cell Significance Index: -44.8100
Cell Name: ileal goblet cell (CL1000326)
Fold Change: 70.6385
Cell Significance Index: -47.4000
Cell Name: ciliated cell of the bronchus (CL0002332)
Fold Change: 42.0375
Cell Significance Index: -40.1400
Cell Name: orthochromatic erythroblast (CL0000552)
Fold Change: 36.5220
Cell Significance Index: -45.0300
Cell Name: CD8-alpha-beta-positive, alpha-beta intraepithelial T cell (CL0000796)
Fold Change: 16.3726
Cell Significance Index: -43.8600
Cell Name: CD8-positive, alpha-beta regulatory T cell (CL0000795)
Fold Change: 13.0752
Cell Significance Index: -40.1600
Cell Name: stromal cell of bone marrow (CL0010001)
Fold Change: 11.8144
Cell Significance Index: -46.6200
Cell Name: epidermal Langerhans cell (CL0002457)
Fold Change: 10.2029
Cell Significance Index: -22.3300
Cell Name: colon goblet cell (CL0009039)
Fold Change: 2.4730
Cell Significance Index: 244.6300
Cell Name: placental villous trophoblast (CL2000060)
Fold Change: 1.7763
Cell Significance Index: 47.4300
Cell Name: L2/3-6 intratelencephalic projecting glutamatergic neuron (CL4023040)
Fold Change: 1.7115
Cell Significance Index: 343.3200
Cell Name: skeletal muscle fiber (CL0008002)
Fold Change: 1.6351
Cell Significance Index: 42.0300
Cell Name: neoplastic cell (CL0001063)
Fold Change: 1.6050
Cell Significance Index: 318.5200
Cell Name: cardiac muscle myoblast (CL0000513)
Fold Change: 1.5700
Cell Significance Index: 120.4800
Cell Name: retinal progenitor cell (CL0002672)
Fold Change: 1.1915
Cell Significance Index: 66.8600
Cell Name: obsolete caudal ganglionic eminence derived GABAergic cortical interneuron (CL4023070)
Fold Change: 0.9666
Cell Significance Index: 346.7200
Cell Name: basal epithelial cell of tracheobronchial tree (CL0002329)
Fold Change: 0.9275
Cell Significance Index: 25.9200
Cell Name: GABAergic interneuron (CL0011005)
Fold Change: 0.7967
Cell Significance Index: 551.0000
Cell Name: intestinal crypt stem cell of colon (CL0009043)
Fold Change: 0.7587
Cell Significance Index: 82.5200
Cell Name: leptomeningeal cell (CL0000708)
Fold Change: 0.7420
Cell Significance Index: 15.8600
Cell Name: preadipocyte (CL0002334)
Fold Change: 0.6978
Cell Significance Index: 13.6200
Cell Name: enteroendocrine cell of small intestine (CL0009006)
Fold Change: 0.6933
Cell Significance Index: 17.3300
Cell Name: epithelial cell of small intestine (CL0002254)
Fold Change: 0.5460
Cell Significance Index: 88.8000
Cell Name: paneth cell of epithelium of small intestine (CL1000343)
Fold Change: 0.5073
Cell Significance Index: 10.9900
Cell Name: basal cell of urothelium (CL1000486)
Fold Change: 0.4764
Cell Significance Index: 58.5800
Cell Name: intermediate cell of urothelium (CL4030055)
Fold Change: 0.4727
Cell Significance Index: 85.2100
Cell Name: indirect pathway medium spiny neuron (CL4023029)
Fold Change: 0.3647
Cell Significance Index: 16.1300
Cell Name: bladder urothelial cell (CL1001428)
Fold Change: 0.2882
Cell Significance Index: 14.9700
Cell Name: non-pigmented ciliary epithelial cell (CL0002304)
Fold Change: 0.2841
Cell Significance Index: 180.4600
Cell Name: pigmented epithelial cell (CL0000529)
Fold Change: 0.2571
Cell Significance Index: 484.1100
Cell Name: tonsil germinal center B cell (CL2000006)
Fold Change: 0.2499
Cell Significance Index: 29.4700
Cell Name: stromal cell of ovary (CL0002132)
Fold Change: 0.2138
Cell Significance Index: 29.3600
Cell Name: type I muscle cell (CL0002211)
Fold Change: 0.2074
Cell Significance Index: 5.0600
Cell Name: cell in vitro (CL0001034)
Fold Change: 0.2064
Cell Significance Index: 112.7200
Cell Name: direct pathway medium spiny neuron (CL4023026)
Fold Change: 0.2060
Cell Significance Index: 7.8000
Cell Name: basal cell of prostate epithelium (CL0002341)
Fold Change: 0.1980
Cell Significance Index: 5.3900
Cell Name: cardiac endothelial cell (CL0010008)
Fold Change: 0.1836
Cell Significance Index: 2.6400
Cell Name: hair follicular keratinocyte (CL2000092)
Fold Change: 0.1821
Cell Significance Index: 80.5200
Cell Name: enterocyte of epithelium of large intestine (CL0002071)
Fold Change: 0.1800
Cell Significance Index: 8.1600
Cell Name: ciliary muscle cell (CL1000443)
Fold Change: 0.1669
Cell Significance Index: 75.7600
Cell Name: lens epithelial cell (CL0002224)
Fold Change: 0.1573
Cell Significance Index: 242.1000
Cell Name: tuft cell of colon (CL0009041)
Fold Change: 0.1563
Cell Significance Index: 141.1700
Cell Name: luminal adaptive secretory precursor cell of mammary gland (CL4033057)
Fold Change: 0.1329
Cell Significance Index: 6.2500
Cell Name: anterior lens cell (CL0002223)
Fold Change: 0.1256
Cell Significance Index: 231.6000
Cell Name: acinar cell of salivary gland (CL0002623)
Fold Change: 0.1008
Cell Significance Index: 4.7000
Cell Name: enteroendocrine cell of colon (CL0009042)
Fold Change: 0.0916
Cell Significance Index: 17.4400
Cell Name: progenitor cell of mammary luminal epithelium (CL0009116)
Fold Change: 0.0812
Cell Significance Index: 6.0500
Cell Name: fibroblast of mammary gland (CL0002555)
Fold Change: 0.0726
Cell Significance Index: 2.0800
Cell Name: small intestine goblet cell (CL1000495)
Fold Change: 0.0706
Cell Significance Index: 2.4800
Cell Name: hippocampal granule cell (CL0001033)
Fold Change: 0.0647
Cell Significance Index: 4.3500
Cell Name: lactocyte (CL0002325)
Fold Change: 0.0449
Cell Significance Index: 5.8000
Cell Name: forebrain neuroblast (CL1000042)
Fold Change: 0.0423
Cell Significance Index: 2.6000
Cell Name: secondary lens fiber (CL0002225)
Fold Change: 0.0394
Cell Significance Index: 53.6000
Cell Name: cortical cell of adrenal gland (CL0002097)
Fold Change: 0.0360
Cell Significance Index: 0.9600
Cell Name: lung endothelial cell (CL1001567)
Fold Change: 0.0282
Cell Significance Index: 1.4700
Cell Name: early pro-B cell (CL0002046)
Fold Change: -0.0078
Cell Significance Index: -0.5000
Cell Name: pancreatic acinar cell (CL0002064)
Fold Change: -0.0156
Cell Significance Index: -2.6600
Cell Name: pigmented ciliary epithelial cell (CL0002303)
Fold Change: -0.0170
Cell Significance Index: -2.4700
Cell Name: pancreatic A cell (CL0000171)
Fold Change: -0.0179
Cell Significance Index: -13.2500
Cell Name: cerebellar granule cell (CL0001031)
Fold Change: -0.0210
Cell Significance Index: -0.3600
Cell Name: type B pancreatic cell (CL0000169)
Fold Change: -0.0293
Cell Significance Index: -16.5200
Cell Name: microfold cell of epithelium of small intestine (CL1000353)
Fold Change: -0.0395
Cell Significance Index: -2.7300
Cell Name: kidney loop of Henle cortical thick ascending limb epithelial cell (CL1001109)
Fold Change: -0.0446
Cell Significance Index: -32.7200
Cell Name: pulmonary alveolar epithelial cell (CL0000322)
Fold Change: -0.0477
Cell Significance Index: -36.0800
Cell Name: pancreatic PP cell (CL0002275)
Fold Change: -0.0498
Cell Significance Index: -31.0700
Cell Name: abnormal cell (CL0001061)
Fold Change: -0.0963
Cell Significance Index: -9.8400
Cell Name: umbrella cell of urothelium (CL4030056)
Fold Change: -0.1113
Cell Significance Index: -1.0300
Cell Name: odontoblast (CL0000060)
Fold Change: -0.1145
Cell Significance Index: -14.6800
Cell Name: pancreatic ductal cell (CL0002079)
Fold Change: -0.1243
Cell Significance Index: -14.2400
Cell Name: pancreatic D cell (CL0000173)
Fold Change: -0.1349
Cell Significance Index: -28.4100
Cell Name: dopaminergic neuron (CL0000700)
Fold Change: -0.1412
Cell Significance Index: -40.6200
Cell Name: sebum secreting cell (CL0000317)
Fold Change: -0.1996
Cell Significance Index: -14.1200
Cell Name: fibroblast of cardiac tissue (CL0002548)
Fold Change: -0.2235
Cell Significance Index: -3.2100
Cell Name: smooth muscle cell of sphincter of pupil (CL0002243)
Fold Change: -0.2246
Cell Significance Index: -23.3900
Cell Name: epithelial cell of stomach (CL0002178)
Fold Change: -0.2569
Cell Significance Index: -29.9400
Cell Name: conjunctival epithelial cell (CL1000432)
Fold Change: -0.2595
Cell Significance Index: -3.5400
Cell Name: centrilobular region hepatocyte (CL0019029)
Fold Change: -0.2781
Cell Significance Index: -4.6900
Cell Name: intestinal crypt stem cell of small intestine (CL0009017)
Fold Change: -0.2979
Cell Significance Index: -6.3500
Cell Name: eye photoreceptor cell (CL0000287)
Fold Change: -0.3089
Cell Significance Index: -19.4700
Cell Name: pancreatic endocrine cell (CL0008024)
Fold Change: -0.3282
Cell Significance Index: -37.4600
Cell Name: endothelial cell of placenta (CL0009092)
Fold Change: -0.3790
Cell Significance Index: -2.2900
Cell Name: hippocampal pyramidal neuron (CL1001571)
Fold Change: -0.4135
Cell Significance Index: -11.8000
Cell Name: cardiac muscle cell (CL0000746)
Fold Change: -0.4342
Cell Significance Index: -6.4100
Cell Name: kidney loop of Henle descending limb epithelial cell (CL1001021)
Fold Change: -0.5218
Cell Significance Index: -41.3300
Cell Name: Hofbauer cell (CL3000001)
Fold Change: -0.6009
Cell Significance Index: -4.9000
Cell Name: periportal region hepatocyte (CL0019026)
Fold Change: -0.6457
Cell Significance Index: -9.5300
Cell Name: intestinal tuft cell (CL0019032)
Fold Change: -0.6509
Cell Significance Index: -39.9100
Cell Name: enterocyte of epithelium of small intestine (CL1000334)
Fold Change: -0.6777
Cell Significance Index: -19.5300
Cell Name: cortical interneuron (CL0008031)
Fold Change: -0.7105
Cell Significance Index: -17.0400
Cell Name: glycinergic neuron (CL1001509)
Fold Change: -0.7110
Cell Significance Index: -37.3300
Cell Name: granulosa cell (CL0000501)
Fold Change: -0.7336
Cell Significance Index: -19.2900
Cell Name: thyroid follicular cell (CL0002258)
Fold Change: -0.7494
Cell Significance Index: -7.9600
Cell Name: CD4-positive, alpha-beta memory T cell, CD45RO-positive (CL0001204)
Fold Change: -0.7985
Cell Significance Index: -23.4500
Cell Name: corticothalamic-projecting glutamatergic cortical neuron (CL4023013)
Fold Change: -0.8405
Cell Significance Index: -26.7700
Cell Name: fibro/adipogenic progenitor cell (CL0009099)
Fold Change: -0.8476
Cell Significance Index: -42.8400

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.

**Key Characteristics:** 1. **Multifunctionality:** NUP98 has been implicated in various cellular processes, including immune response, cell cycle regulation, and viral infection. 2. **Signaling Pathways:** NUP98 interacts with multiple signaling pathways, including interferon signaling, cytokine signaling, and Rho GTPase signaling. 3. **Cellular Localization:** NUP98 is localized to the nuclear envelope and the nuclear pore complex, where it regulates the export of proteins and RNAs. 4. **Disease Association:** Dysregulation of NUP98 has been associated with various diseases, including thyroid papillary carcinoma and disorders of transmembrane transporters. **Pathways and Functions:** 1. **Amplification of Signal from Kinetochores:** NUP98 regulates the amplification of signals from kinetochores, which is crucial for proper chromosome segregation during mitosis. 2. **Antiviral Mechanism:** NUP98 plays a role in the antiviral mechanism by interferon-stimulated genes, which helps to regulate viral replication. 3. **Cell Cycle Regulation:** NUP98 regulates the cell cycle checkpoints, ensuring proper cell cycle progression and preventing genomic instability. 4. **Viral Infection:** NUP98 is involved in the export of viral ribonucleoproteins from the nucleus, which is essential for viral replication and transcription. 5. **Immune Response:** NUP98 regulates the immune response by interacting with cytokine signaling pathways and Rho GTPase signaling. **Clinical Significance:** 1. **Thyroid Papillary Carcinoma:** Dysregulation of NUP98 has been associated with thyroid papillary carcinoma, highlighting the importance of this gene in cancer development. 2. **Disorders of Transmembrane Transporters:** NUP98 is involved in the regulation of transmembrane transporters, which is crucial for proper cellular function and development. 3. **Immune Disorders:** Dysregulation of NUP98 has been associated with various immune disorders, including autoimmune diseases and immunodeficiency syndromes. 4. **Cancer Therapy:** NUP98 may serve as a target for cancer therapy, as its dysregulation is associated with cancer development and progression. In conclusion, NUP98 is a multifunctional gene that plays a crucial role in various cellular processes, including immune response, cell cycle regulation, and viral infection. Its dysregulation has been associated with various diseases, including thyroid papillary carcinoma and disorders of transmembrane transporters. Further research is needed to fully understand the mechanisms of NUP98 and its role in human disease.

Disclaimer: This summary is generated by an AI language model and may contain inaccuracies or hallucinations. However, it is cross-referenced with curated gene expression data from major biological sources. Please verify the information before use.

Nuclear pore complex protein Nup98

Genular Protein ID: 3200082497

Symbol: NUP98_HUMAN

Name: Nuclear pore complex protein Nup98

UniProtKB Accession Codes:

P52948 Q8IUT2 Q8WYB0 Q96E54 Q9H3Q4 Q9NT02 Q9UF57 Q9UHX0 Q9Y6J4 Q9Y6J5

Database IDs:

Citations:

PubMed ID: 8563754

Title: The t(7;11)(p15;p15) translocation in acute myeloid leukaemia fuses the genes for nucleoporin NUP98 and class I homeoprotein HOXA9.

PubMed ID: 8563754

DOI: 10.1038/ng0296-159

PubMed ID: 10087256

Title: A conserved biogenesis pathway for nucleoporins: proteolytic processing of a 186-kilodalton precursor generates Nup98 and the novel nucleoporin, Nup96.

PubMed ID: 10087256

DOI: 10.1083/jcb.144.6.1097

PubMed ID: 16554811

Title: Human chromosome 11 DNA sequence and analysis including novel gene identification.

PubMed ID: 16554811

DOI: 10.1038/nature04632

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: 17974005

Title: The full-ORF clone resource of the German cDNA consortium.

PubMed ID: 17974005

DOI: 10.1186/1471-2164-8-399

PubMed ID: 10556215

Title: The t(11;20)(p15;q11) chromosomal translocation associated with therapy-related myelodysplastic syndrome results in an NUP98-TOP1 fusion.

PubMed ID: 10556215

PubMed ID: 10209021

Title: RAE1 is a shuttling mRNA export factor that binds to a GLEBS-like NUP98 motif at the nuclear pore complex through multiple domains.

PubMed ID: 10209021

DOI: 10.1083/jcb.145.2.237

PubMed ID: 11106761

Title: Vesicular stomatitis virus matrix protein inhibits host cell gene expression by targeting the nucleoporin Nup98.

PubMed ID: 11106761

DOI: 10.1016/s1097-2765(00)00120-9

PubMed ID: 11493482

Title: A novel gene, NSD1, is fused to NUP98 in the t(5;11)(q35;p15.5) in de novo childhood acute myeloid leukemia.

PubMed ID: 11493482

DOI: 10.1182/blood.v98.4.1264

PubMed ID: 11684705

Title: Novel vertebrate nucleoporins Nup133 and Nup160 play a role in mRNA export.

PubMed ID: 11684705

DOI: 10.1083/jcb.200108007

PubMed ID: 11986249

Title: NUP98 is fused to the NSD3 gene in acute myeloid leukemia associated with t(8;11)(p11.2;p15).

PubMed ID: 11986249

DOI: 10.1182/blood.v99.10.3857

PubMed ID: 11839768

Title: Tpr is localized within the nuclear basket of the pore complex and has a role in nuclear protein export.

PubMed ID: 11839768

DOI: 10.1083/jcb.200106046

PubMed ID: 12802065

Title: Direct interaction with nup153 mediates binding of Tpr to the periphery of the nuclear pore complex.

PubMed ID: 12802065

DOI: 10.1091/mbc.e02-09-0620

PubMed ID: 15229283

Title: Nucleoporins as components of the nuclear pore complex core structure and Tpr as the architectural element of the nuclear basket.

PubMed ID: 15229283

DOI: 10.1091/mbc.e04-03-0165

PubMed ID: 16028218

Title: Characterization of 6q abnormalities in childhood acute myeloid leukemia and identification of a novel t(6;11)(q24.1;p15.5) resulting in a NUP98-C6orf80 fusion in a case of acute megakaryoblastic leukemia.

PubMed ID: 16028218

DOI: 10.1002/gcc.20233

PubMed ID: 15725483

Title: t(9;11)(p22;p15) with NUP98-LEDGF fusion gene in pediatric acute myeloid leukemia.

PubMed ID: 15725483

DOI: 10.1016/j.leukres.2004.09.002

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: 16467868

Title: NUP98 rearrangements in hematopoietic malignancies: a study of the Groupe Francophone de Cytogenetique Hematologique.

PubMed ID: 16467868

DOI: 10.1038/sj.leu.2404130

PubMed ID: 16964243

Title: A probability-based approach for high-throughput protein phosphorylation analysis and site localization.

PubMed ID: 16964243

DOI: 10.1038/nbt1240

PubMed ID: 17287853

Title: A novel NUP98-PHF23 fusion resulting from a cryptic translocation t(11;17)(p15;p13) in acute myeloid leukemia.

PubMed ID: 17287853

DOI: 10.1038/sj.leu.2404579

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: 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: 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: 20407419

Title: Protein Tpr is required for establishing nuclear pore-associated zones of heterochromatin exclusion.

PubMed ID: 20407419

DOI: 10.1038/emboj.2010.54

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: 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: 22058212

Title: Functional analysis of the NUP98-CCDC28A fusion protein.

PubMed ID: 22058212

DOI: 10.3324/haematol.2011.047969

PubMed ID: 23186163

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

PubMed ID: 23186163

DOI: 10.1021/pr300630k

PubMed ID: 23523133

Title: Nup153 and Nup98 bind the HIV-1 core and contribute to the early steps of HIV-1 replication.

PubMed ID: 23523133

DOI: 10.1016/j.virol.2013.02.008

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: 25944712

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

PubMed ID: 25944712

DOI: 10.1002/pmic.201400617

PubMed ID: 28221134

Title: Human Nup98 regulates the localization and activity of DExH/D-box helicase DHX9.

PubMed ID: 28221134

DOI: 10.7554/elife.18825

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: 30543681

Title: Biallelic mutations in nucleoporin NUP88 cause lethal fetal akinesia deformation sequence.

PubMed ID: 30543681

DOI: 10.1371/journal.pgen.1007845

PubMed ID: 33097660

Title: SARS-CoV-2 Orf6 hijacks Nup98 to block STAT nuclear import and antagonize interferon signaling.

PubMed ID: 33097660

DOI: 10.1073/pnas.2016650117

PubMed ID: 33360543

Title: Overexpression of SARS-CoV-2 protein ORF6 dislocates RAE1 and NUP98 from the nuclear pore complex.

PubMed ID: 33360543

DOI: 10.1016/j.bbrc.2020.11.115

PubMed ID: 33849972

Title: SARS-CoV-2 ORF6 Disrupts Bidirectional Nucleocytoplasmic Transport through Interactions with Rae1 and Nup98.

PubMed ID: 33849972

DOI: 10.1128/mbio.00065-21

PubMed ID: 12191480

Title: The three-dimensional structure of the autoproteolytic, nuclear pore-targeting domain of the human nucleoporin Nup98.

PubMed ID: 12191480

DOI: 10.1016/s1097-2765(02)00589-0

PubMed ID: 18287282

Title: Structural constraints on autoprocessing of the human nucleoporin Nup98.

PubMed ID: 18287282

DOI: 10.1110/ps.073311808

PubMed ID: 20498086

Title: Structural and functional analysis of the interaction between the nucleoporin Nup98 and the mRNA export factor Rae1.

PubMed ID: 20498086

DOI: 10.1073/pnas.1005389107

PubMed ID: 8563753

Title: Fusion of the nucleoporin gene NUP98 to HOXA9 by the chromosome translocation t(7;11)(p15;p15) in human myeloid leukaemia.

PubMed ID: 8563753

DOI: 10.1038/ng0296-154

PubMed ID: 10477737

Title: The (4;11)(q21;p15) translocation fuses the NUP98 and RAP1GDS1 genes and is recurrent in T-cell acute lymphocytic leukemia.

PubMed ID: 10477737

PubMed ID: 10929031

Title: t(4;11)(q21;p15) translocation involving NUP98 and RAP1GDS1 genes: characterization of a new subset of T acute lymphoblastic leukaemia.

PubMed ID: 10929031

DOI: 10.1046/j.1365-2141.2000.02106.x

PubMed ID: 16419055

Title: Identification of NUP98 abnormalities in acute leukemia: JARID1A (12p13) as a new partner gene.

PubMed ID: 16419055

DOI: 10.1002/gcc.20308

PubMed ID: 16959974

Title: The consensus coding sequences of human breast and colorectal cancers.

PubMed ID: 16959974

DOI: 10.1126/science.1133427

PubMed ID: 23531517

Title: NUP98/JARID1A is a novel recurrent abnormality in pediatric acute megakaryoblastic leukemia with a distinct HOX gene expression pattern.

PubMed ID: 23531517

DOI: 10.1038/leu.2013.87

PubMed ID: 34163069

Title: Phase separation drives aberrant chromatin looping and cancer development.

PubMed ID: 34163069

DOI: 10.1038/s41586-021-03662-5

Sequence Information:

Length: 1817
Mass: 197579
Checksum: BC60E5456B936C79
Sequence:

MFNKSFGTPF GGGTGGFGTT STFGQNTGFG TTSGGAFGTS AFGSSNNTGG LFGNSQTKPG 
GLFGTSSFSQ PATSTSTGFG FGTSTGTANT LFGTASTGTS LFSSQNNAFA QNKPTGFGNF 
GTSTSSGGLF GTTNTTSNPF GSTSGSLFGP SSFTAAPTGT TIKFNPPTGT DTMVKAGVST 
NISTKHQCIT AMKEYESKSL EELRLEDYQA NRKGPQNQVG AGTTTGLFGS SPATSSATGL 
FSSSTTNSGF AYGQNKTAFG TSTTGFGTNP GGLFGQQNQQ TTSLFSKPFG QATTTQNTGF 
SFGNTSTIGQ PSTNTMGLFG VTQASQPGGL FGTATNTSTG TAFGTGTGLF GQTNTGFGAV 
GSTLFGNNKL TTFGSSTTSA PSFGTTSGGL FGNKPTLTLG TNTNTSNFGF GTNTSGNSIF 
GSKPAPGTLG TGLGAGFGTA LGAGQASLFG NNQPKIGGPL GTGAFGAPGF NTTTATLGFG 
APQAPVALTD PNASAAQQAV LQQHINSLTY SPFGDSPLFR NPMSDPKKKE ERLKPTNPAA 
QKALTTPTHY KLTPRPATRV RPKALQTTGT AKSHLFDGLD DDEPSLANGA FMPKKSIKKL 
VLKNLNNSNL FSPVNRDSEN LASPSEYPEN GERFSFLSKP VDENHQQDGD EDSLVSHFYT 
NPIAKPIPQT PESAGNKHSN SNSVDDTIVA LNMRAALRNG LEGSSEETSF HDESLQDDRE 
EIENNSYHMH PAGIILTKVG YYTIPSMDDL AKITNEKGEC IVSDFTIGRK GYGSIYFEGD 
VNLTNLNLDD IVHIRRKEVV VYLDDNQKPP VGEGLNRKAE VTLDGVWPTD KTSRCLIKSP 
DRLADINYEG RLEAVSRKQG AQFKEYRPET GSWVFKVSHF SKYGLQDSDE EEEEHPSKTS 
TKKLKTAPLP PASQTTPLQM ALNGKPAPPP QSQSPEVEQL GRVVELDSDM VDITQEPVLD 
TMLEESMPED QEPVSASTHI ASSLGINPHV LQIMKASLLT DEEDVDMALD QRFSRLPSKA 
DTSQEICSPR LPISASHSSK TRSLVGGLLQ SKFTSGAFLS PSVSVQECRT PRAASLMNIP 
STSSWSVPPP LTSVFTMPSP APEVPLKTVG TRRQLGLVPR EKSVTYGKGK LLMDMALFMG 
RSFRVGWGPN WTLANSGEQL NGSHELENHQ IADSMEFGFL PNPVAVKPLT ESPFKVHLEK 
LSLRQRKPDE DMKLYQTPLE LKLKHSTVHV DELCPLIVPN LGVAVIHDYA DWVKEASGDL 
PEAQIVKHWS LTWTLCEALW GHLKELDSQL NEPREYIQIL ERRRAFSRWL SCTATPQIEE 
EVSLTQKNSP VEAVFSYLTG KRISEACSLA QQSGDHRLAL LLSQFVGSQS VRELLTMQLV 
DWHQLQADSF IQDERLRIFA LLAGKPVWQL SEKKQINVCS QLDWKRSLAI HLWYLLPPTA 
SISRALSMYE EAFQNTSDSD RYACSPLPSY LEGSGCVIAE EQNSQTPLRD VCFHLLKLYS 
DRHYDLNQLL EPRSITADPL DYRLSWHLWE VLRALNYTHL SAQCEGVLQA SYAGQLESEG 
LWEWAIFVLL HIDNSGIREK AVRELLTRHC QLLETPESWA KETFLTQKLR VPAKWIHEAK 
AVRAHMESDK HLEALCLFKA EHWNRCHKLI IRHLASDAII NENYDYLKGF LEDLAPPERS 
SLIQDWETSG LVYLDYIRVI EMLRHIQQVD CSGNDLEQLH IKVTSLCSRI EQIQCYSAKD 
RLAQSDMAKR VANLLRVVLS LHHPPDRTSD STPDPQRVPL RLLAPHIGRL PMPEDYAMDE 
LRSLTQSYLR ELAVGSL

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.

Details for: NUP98

Associated with

Cells (max top 100)

Other Information

The t(7;11)(p15;p15) translocation in acute myeloid leukaemia fuses the genes for nucleoporin NUP98 and class I homeoprotein HOXA9. PubMed ID: 8563754

A conserved biogenesis pathway for nucleoporins: proteolytic processing of a 186-kilodalton precursor generates Nup98 and the novel nucleoporin, Nup96. PubMed ID: 10087256

Human chromosome 11 DNA sequence and analysis including novel gene identification. PubMed ID: 16554811

The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). PubMed ID: 15489334

The full-ORF clone resource of the German cDNA consortium. PubMed ID: 17974005

The t(11;20)(p15;q11) chromosomal translocation associated with therapy-related myelodysplastic syndrome results in an NUP98-TOP1 fusion. PubMed ID: 10556215

RAE1 is a shuttling mRNA export factor that binds to a GLEBS-like NUP98 motif at the nuclear pore complex through multiple domains. PubMed ID: 10209021

Vesicular stomatitis virus matrix protein inhibits host cell gene expression by targeting the nucleoporin Nup98. PubMed ID: 11106761

A novel gene, NSD1, is fused to NUP98 in the t(5;11)(q35;p15.5) in de novo childhood acute myeloid leukemia. PubMed ID: 11493482

Novel vertebrate nucleoporins Nup133 and Nup160 play a role in mRNA export. PubMed ID: 11684705

NUP98 is fused to the NSD3 gene in acute myeloid leukemia associated with t(8;11)(p11.2;p15). PubMed ID: 11986249

Tpr is localized within the nuclear basket of the pore complex and has a role in nuclear protein export. PubMed ID: 11839768

Direct interaction with nup153 mediates binding of Tpr to the periphery of the nuclear pore complex. PubMed ID: 12802065

Nucleoporins as components of the nuclear pore complex core structure and Tpr as the architectural element of the nuclear basket. PubMed ID: 15229283

Characterization of 6q abnormalities in childhood acute myeloid leukemia and identification of a novel t(6;11)(q24.1;p15.5) resulting in a NUP98-C6orf80 fusion in a case of acute megakaryoblastic leukemia. PubMed ID: 16028218

t(9;11)(p22;p15) with NUP98-LEDGF fusion gene in pediatric acute myeloid leukemia. PubMed ID: 15725483

Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. PubMed ID: 17081983

NUP98 rearrangements in hematopoietic malignancies: a study of the Groupe Francophone de Cytogenetique Hematologique. PubMed ID: 16467868

A probability-based approach for high-throughput protein phosphorylation analysis and site localization. PubMed ID: 16964243

A novel NUP98-PHF23 fusion resulting from a cryptic translocation t(11;17)(p15;p13) in acute myeloid leukemia. PubMed ID: 17287853

Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis. PubMed ID: 18220336

Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. PubMed ID: 18691976

A quantitative atlas of mitotic phosphorylation. PubMed ID: 18669648

Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography. PubMed ID: 18318008

Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. PubMed ID: 19413330

Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. PubMed ID: 19690332

Lysine acetylation targets protein complexes and co-regulates major cellular functions. PubMed ID: 19608861

Protein Tpr is required for establishing nuclear pore-associated zones of heterochromatin exclusion. PubMed ID: 20407419

Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis. PubMed ID: 20068231

Initial characterization of the human central proteome. PubMed ID: 21269460

System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation. PubMed ID: 21406692

Functional analysis of the NUP98-CCDC28A fusion protein. PubMed ID: 22058212

Toward a comprehensive characterization of a human cancer cell phosphoproteome. PubMed ID: 23186163

Nup153 and Nup98 bind the HIV-1 core and contribute to the early steps of HIV-1 replication. PubMed ID: 23523133

An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. PubMed ID: 24275569

N-terminome analysis of the human mitochondrial proteome. PubMed ID: 25944712

Human Nup98 regulates the localization and activity of DExH/D-box helicase DHX9. PubMed ID: 28221134

Site-specific mapping of the human SUMO proteome reveals co-modification with phosphorylation. PubMed ID: 28112733

Biallelic mutations in nucleoporin NUP88 cause lethal fetal akinesia deformation sequence. PubMed ID: 30543681

SARS-CoV-2 Orf6 hijacks Nup98 to block STAT nuclear import and antagonize interferon signaling. PubMed ID: 33097660

Overexpression of SARS-CoV-2 protein ORF6 dislocates RAE1 and NUP98 from the nuclear pore complex. PubMed ID: 33360543

SARS-CoV-2 ORF6 Disrupts Bidirectional Nucleocytoplasmic Transport through Interactions with Rae1 and Nup98. PubMed ID: 33849972

The three-dimensional structure of the autoproteolytic, nuclear pore-targeting domain of the human nucleoporin Nup98. PubMed ID: 12191480

Structural constraints on autoprocessing of the human nucleoporin Nup98. PubMed ID: 18287282

Structural and functional analysis of the interaction between the nucleoporin Nup98 and the mRNA export factor Rae1. PubMed ID: 20498086

Fusion of the nucleoporin gene NUP98 to HOXA9 by the chromosome translocation t(7;11)(p15;p15) in human myeloid leukaemia. PubMed ID: 8563753

The (4;11)(q21;p15) translocation fuses the NUP98 and RAP1GDS1 genes and is recurrent in T-cell acute lymphocytic leukemia. PubMed ID: 10477737

t(4;11)(q21;p15) translocation involving NUP98 and RAP1GDS1 genes: characterization of a new subset of T acute lymphoblastic leukaemia. PubMed ID: 10929031

Identification of NUP98 abnormalities in acute leukemia: JARID1A (12p13) as a new partner gene. PubMed ID: 16419055

The consensus coding sequences of human breast and colorectal cancers. PubMed ID: 16959974

NUP98/JARID1A is a novel recurrent abnormality in pediatric acute megakaryoblastic leukemia with a distinct HOX gene expression pattern. PubMed ID: 23531517

Phase separation drives aberrant chromatin looping and cancer development. PubMed ID: 34163069