NUP214 | ENSG00000126883 | NCBI 8021

Details for: NUP214

Gene ID: 8021

Symbol: NUP214

Ensembl ID: ENSG00000126883

Description: nucleoporin 214

Associated with

Antiviral mechanism by ifn-stimulated genes
(R-HSA-1169410)
Cell cycle
(R-HSA-1640170)
Cell cycle, mitotic
(R-HSA-69278)
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)
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)
Hur (elavl1) binds and stabilizes mrna
(R-HSA-450520)
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 prophase
(R-HSA-68875)
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 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)
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)
Regulation of mrna stability by proteins that bind au-rich elements
(R-HSA-450531)
Rev-mediated nuclear export of hiv rna
(R-HSA-165054)
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)
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)
Cytoplasmic side of nuclear pore
(GO:1990876)
Cytosol
(GO:0005829)
Mrna export from nucleus
(GO:0006406)
Nuclear envelope
(GO:0005635)
Nuclear export signal receptor activity
(GO:0005049)
Nuclear localization sequence binding
(GO:0008139)
Nuclear pore
(GO:0005643)
Nucleocytoplasmic transport
(GO:0006913)
Nucleoplasm
(GO:0005654)
Protein binding
(GO:0005515)
Protein export from nucleus
(GO:0006611)
Protein import into nucleus
(GO:0006606)
Regulation of cell cycle
(GO:0051726)
Regulation of nucleocytoplasmic transport
(GO:0046822)
Rna export from nucleus
(GO:0006405)
Structural constituent of nuclear pore
(GO:0017056)

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: 229.9653
Cell Significance Index: -35.7700
Cell Name: hematopoietic oligopotent progenitor cell (CL0002032)
Fold Change: 133.6128
Cell Significance Index: -33.8900
Cell Name: mucosal type mast cell (CL0000485)
Fold Change: 86.9892
Cell Significance Index: -35.3400
Cell Name: smooth muscle fiber of ileum (CL1000278)
Fold Change: 85.8252
Cell Significance Index: -40.5200
Cell Name: peripheral blood mononuclear cell (CL2000001)
Fold Change: 76.0714
Cell Significance Index: -39.1300
Cell Name: ileal goblet cell (CL1000326)
Fold Change: 60.3855
Cell Significance Index: -40.5200
Cell Name: ciliated cell of the bronchus (CL0002332)
Fold Change: 37.3504
Cell Significance Index: -35.6600
Cell Name: orthochromatic erythroblast (CL0000552)
Fold Change: 30.5120
Cell Significance Index: -37.6200
Cell Name: CD8-alpha-beta-positive, alpha-beta intraepithelial T cell (CL0000796)
Fold Change: 13.8492
Cell Significance Index: -37.1000
Cell Name: CD8-positive, alpha-beta regulatory T cell (CL0000795)
Fold Change: 11.4929
Cell Significance Index: -35.3000
Cell Name: epidermal Langerhans cell (CL0002457)
Fold Change: 10.3034
Cell Significance Index: -22.5500
Cell Name: stromal cell of bone marrow (CL0010001)
Fold Change: 9.6704
Cell Significance Index: -38.1600
Cell Name: CD14-positive, CD16-negative classical monocyte (CL0002057)
Fold Change: 1.9353
Cell Significance Index: 35.7700
Cell Name: colon goblet cell (CL0009039)
Fold Change: 1.7530
Cell Significance Index: 173.4100
Cell Name: neoplastic cell (CL0001063)
Fold Change: 1.5671
Cell Significance Index: 310.9900
Cell Name: L2/3-6 intratelencephalic projecting glutamatergic neuron (CL4023040)
Fold Change: 1.4983
Cell Significance Index: 300.5500
Cell Name: retinal progenitor cell (CL0002672)
Fold Change: 1.1699
Cell Significance Index: 65.6500
Cell Name: basal epithelial cell of tracheobronchial tree (CL0002329)
Fold Change: 0.9160
Cell Significance Index: 25.6000
Cell Name: early pro-B cell (CL0002046)
Fold Change: 0.8905
Cell Significance Index: 57.4500
Cell Name: obsolete caudal ganglionic eminence derived GABAergic cortical interneuron (CL4023070)
Fold Change: 0.8547
Cell Significance Index: 306.5800
Cell Name: gut absorptive cell (CL0000677)
Fold Change: 0.8391
Cell Significance Index: 50.3800
Cell Name: preadipocyte (CL0002334)
Fold Change: 0.6820
Cell Significance Index: 13.3100
Cell Name: cardiac muscle myoblast (CL0000513)
Fold Change: 0.6622
Cell Significance Index: 50.8200
Cell Name: GABAergic interneuron (CL0011005)
Fold Change: 0.5651
Cell Significance Index: 390.8300
Cell Name: granulosa cell (CL0000501)
Fold Change: 0.4885
Cell Significance Index: 12.8500
Cell Name: indirect pathway medium spiny neuron (CL4023029)
Fold Change: 0.4332
Cell Significance Index: 19.1600
Cell Name: forebrain neuroblast (CL1000042)
Fold Change: 0.3923
Cell Significance Index: 24.1100
Cell Name: direct pathway medium spiny neuron (CL4023026)
Fold Change: 0.3832
Cell Significance Index: 14.5100
Cell Name: enterocyte of epithelium of large intestine (CL0002071)
Fold Change: 0.3451
Cell Significance Index: 15.6400
Cell Name: skeletal muscle fiber (CL0008002)
Fold Change: 0.3268
Cell Significance Index: 8.4000
Cell Name: basal cell of urothelium (CL1000486)
Fold Change: 0.3204
Cell Significance Index: 39.4000
Cell Name: lung endothelial cell (CL1001567)
Fold Change: 0.3198
Cell Significance Index: 16.6600
Cell Name: intermediate cell of urothelium (CL4030055)
Fold Change: 0.3156
Cell Significance Index: 56.8900
Cell Name: stromal cell of ovary (CL0002132)
Fold Change: 0.2567
Cell Significance Index: 35.2500
Cell Name: conjunctival epithelial cell (CL1000432)
Fold Change: 0.2345
Cell Significance Index: 3.2000
Cell Name: cell in vitro (CL0001034)
Fold Change: 0.1784
Cell Significance Index: 97.4500
Cell Name: hair follicular keratinocyte (CL2000092)
Fold Change: 0.1687
Cell Significance Index: 74.5700
Cell Name: enteroendocrine cell of colon (CL0009042)
Fold Change: 0.1428
Cell Significance Index: 27.1800
Cell Name: pigmented epithelial cell (CL0000529)
Fold Change: 0.1236
Cell Significance Index: 232.7000
Cell Name: tonsil germinal center B cell (CL2000006)
Fold Change: 0.1228
Cell Significance Index: 14.4800
Cell Name: paneth cell of epithelium of small intestine (CL1000343)
Fold Change: 0.1182
Cell Significance Index: 2.5600
Cell Name: microfold cell of epithelium of small intestine (CL1000353)
Fold Change: 0.1152
Cell Significance Index: 7.9700
Cell Name: hippocampal granule cell (CL0001033)
Fold Change: 0.0950
Cell Significance Index: 6.3900
Cell Name: anterior lens cell (CL0002223)
Fold Change: 0.0858
Cell Significance Index: 158.2800
Cell Name: enterocyte of epithelium of small intestine (CL1000334)
Fold Change: 0.0751
Cell Significance Index: 2.1700
Cell Name: lens epithelial cell (CL0002224)
Fold Change: 0.0732
Cell Significance Index: 112.7500
Cell Name: non-pigmented ciliary epithelial cell (CL0002304)
Fold Change: 0.0610
Cell Significance Index: 38.7300
Cell Name: ciliary muscle cell (CL1000443)
Fold Change: 0.0602
Cell Significance Index: 27.3100
Cell Name: pancreatic acinar cell (CL0002064)
Fold Change: 0.0534
Cell Significance Index: 9.1100
Cell Name: tuft cell of colon (CL0009041)
Fold Change: 0.0231
Cell Significance Index: 20.8400
Cell Name: secondary lens fiber (CL0002225)
Fold Change: 0.0164
Cell Significance Index: 22.2700
Cell Name: cerebellar granule cell (CL0001031)
Fold Change: 0.0000
Cell Significance Index: 0.0000
Cell Name: placental villous trophoblast (CL2000060)
Fold Change: -0.0026
Cell Significance Index: -0.0700
Cell Name: leptomeningeal cell (CL0000708)
Fold Change: -0.0150
Cell Significance Index: -0.3200
Cell Name: pancreatic A cell (CL0000171)
Fold Change: -0.0154
Cell Significance Index: -11.4000
Cell Name: cardiac endothelial cell (CL0010008)
Fold Change: -0.0202
Cell Significance Index: -0.2900
Cell Name: kidney loop of Henle cortical thick ascending limb epithelial cell (CL1001109)
Fold Change: -0.0236
Cell Significance Index: -17.2800
Cell Name: pancreatic PP cell (CL0002275)
Fold Change: -0.0301
Cell Significance Index: -18.8200
Cell Name: acinar cell of salivary gland (CL0002623)
Fold Change: -0.0307
Cell Significance Index: -1.4300
Cell Name: luminal adaptive secretory precursor cell of mammary gland (CL4033057)
Fold Change: -0.0389
Cell Significance Index: -1.8300
Cell Name: type B pancreatic cell (CL0000169)
Fold Change: -0.0392
Cell Significance Index: -22.1100
Cell Name: pulmonary alveolar epithelial cell (CL0000322)
Fold Change: -0.0433
Cell Significance Index: -32.8000
Cell Name: epithelial cell of small intestine (CL0002254)
Fold Change: -0.0451
Cell Significance Index: -7.3300
Cell Name: cortical cell of adrenal gland (CL0002097)
Fold Change: -0.0539
Cell Significance Index: -1.4400
Cell Name: abnormal cell (CL0001061)
Fold Change: -0.0559
Cell Significance Index: -5.7100
Cell Name: odontoblast (CL0000060)
Fold Change: -0.0570
Cell Significance Index: -7.3100
Cell Name: cortical interneuron (CL0008031)
Fold Change: -0.0919
Cell Significance Index: -2.2100
Cell Name: pancreatic ductal cell (CL0002079)
Fold Change: -0.0959
Cell Significance Index: -10.9900
Cell Name: pancreatic D cell (CL0000173)
Fold Change: -0.1157
Cell Significance Index: -24.3600
Cell Name: dopaminergic neuron (CL0000700)
Fold Change: -0.1187
Cell Significance Index: -34.1400
Cell Name: bladder urothelial cell (CL1001428)
Fold Change: -0.1297
Cell Significance Index: -6.7400
Cell Name: pigmented ciliary epithelial cell (CL0002303)
Fold Change: -0.1412
Cell Significance Index: -20.5200
Cell Name: lactocyte (CL0002325)
Fold Change: -0.1487
Cell Significance Index: -19.2100
Cell Name: small intestine goblet cell (CL1000495)
Fold Change: -0.1947
Cell Significance Index: -6.8400
Cell Name: neutrophil progenitor cell (CL0000834)
Fold Change: -0.2198
Cell Significance Index: -5.8800
Cell Name: pancreatic endocrine cell (CL0008024)
Fold Change: -0.2209
Cell Significance Index: -25.2200
Cell Name: eye photoreceptor cell (CL0000287)
Fold Change: -0.2213
Cell Significance Index: -13.9500
Cell Name: transit amplifying cell of small intestine (CL0009012)
Fold Change: -0.2374
Cell Significance Index: -4.9300
Cell Name: sebum secreting cell (CL0000317)
Fold Change: -0.2449
Cell Significance Index: -17.3200
Cell Name: epithelial cell of stomach (CL0002178)
Fold Change: -0.2591
Cell Significance Index: -30.1900
Cell Name: smooth muscle cell of sphincter of pupil (CL0002243)
Fold Change: -0.2669
Cell Significance Index: -27.7900
Cell Name: progenitor cell of mammary luminal epithelium (CL0009116)
Fold Change: -0.3227
Cell Significance Index: -24.0500
Cell Name: fibroblast of cardiac tissue (CL0002548)
Fold Change: -0.3517
Cell Significance Index: -5.0500
Cell Name: GABAergic amacrine cell (CL4030027)
Fold Change: -0.3830
Cell Significance Index: -4.7500
Cell Name: transit amplifying cell of colon (CL0009011)
Fold Change: -0.3975
Cell Significance Index: -12.7300
Cell Name: fibro/adipogenic progenitor cell (CL0009099)
Fold Change: -0.4045
Cell Significance Index: -20.4400
Cell Name: kidney loop of Henle descending limb epithelial cell (CL1001021)
Fold Change: -0.4513
Cell Significance Index: -35.7400
Cell Name: retinal rod cell (CL0000604)
Fold Change: -0.4580
Cell Significance Index: -5.4600
Cell Name: glycinergic neuron (CL1001509)
Fold Change: -0.4687
Cell Significance Index: -24.6100
Cell Name: Purkinje cell (CL0000121)
Fold Change: -0.4905
Cell Significance Index: -10.7400
Cell Name: intestinal tuft cell (CL0019032)
Fold Change: -0.5537
Cell Significance Index: -33.9500
Cell Name: cardiac muscle cell (CL0000746)
Fold Change: -0.5947
Cell Significance Index: -8.7800
Cell Name: hippocampal pyramidal neuron (CL1001571)
Fold Change: -0.6083
Cell Significance Index: -17.3600
Cell Name: intestinal crypt stem cell of small intestine (CL0009017)
Fold Change: -0.6388
Cell Significance Index: -13.6100
Cell Name: BEST4+ enteroycte (CL4030026)
Fold Change: -0.6589
Cell Significance Index: -9.9300
Cell Name: type I muscle cell (CL0002211)
Fold Change: -0.6594
Cell Significance Index: -16.0900
Cell Name: basal cell of prostate epithelium (CL0002341)
Fold Change: -0.6617
Cell Significance Index: -18.0100
Cell Name: corticothalamic-projecting glutamatergic cortical neuron (CL4023013)
Fold Change: -0.6776
Cell Significance Index: -21.5800
Cell Name: mesenchymal cell (CL0008019)
Fold Change: -0.6782
Cell Significance Index: -11.3500
Cell Name: peg cell (CL4033014)
Fold Change: -0.6865
Cell Significance Index: -15.8600

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** NUP214 is a transmembrane protein that spans the nuclear envelope and is embedded in the NPC. It contains a nuclear localization sequence (NLS) and a nuclear export signal (NES), which allows it to regulate the transport of molecules in and out of the nucleus. NUP214 has been shown to interact with various proteins, including RNA-binding proteins and viral proteins, to regulate their transport and function. The protein has also been implicated in the regulation of cell cycle progression, transcription, and immune responses. **Pathways and Functions** NUP214 is involved in several cellular pathways, including: 1. **Nuclear transport**: NUP214 regulates the transport of molecules between the nucleus and cytoplasm by interacting with other NPC components and RNA-binding proteins. 2. **Cell cycle regulation**: NUP214 interacts with cyclin-dependent kinases and other cell cycle regulators to regulate cell cycle progression. 3. **Transcription regulation**: NUP214 interacts with transcription factors and RNA-binding proteins to regulate transcriptional activity. 4. **Immune responses**: NUP214 has been shown to interact with viral proteins, such as HIV-1 and SARS-CoV-2, to regulate their transport and function. 5. **Antiviral mechanisms**: NUP214 has been implicated in the regulation of antiviral mechanisms, including the export of viral RNA from the nucleus. **Clinical Significance** NUP214 has been linked to several diseases, including: 1. **Thyroid papillary carcinoma**: Abnormal expression of NUP214 has been observed in thyroid papillary carcinoma, suggesting a potential role in the development of this cancer. 2. **Viral infections**: NUP214 has been implicated in the regulation of viral infections, including HIV-1 and SARS-CoV-2, suggesting a potential role in the development of antiviral therapies. 3. **Immune system disorders**: NUP214 has been linked to immune system disorders, including autoimmune diseases and immunodeficiency syndromes, suggesting a potential role in the regulation of immune responses. 4. **Cancer**: NUP214 has been implicated in the regulation of cancer cell growth and survival, suggesting a potential role in the development of cancer therapies. In conclusion, NUP214 is a critical protein involved in various cellular processes, including nuclear transport, cell cycle regulation, transcription regulation, and immune responses. Abnormal expression or function of NUP214 has been linked to several diseases, suggesting a potential role in the development of antiviral therapies and cancer treatments.

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 Nup214
B7ZAV2_HUMAN

Genular Protein ID: 3843799611

Symbol: NU214_HUMAN

Name: Nuclear pore complex protein Nup214

UniProtKB Accession Codes:

P35658 A6NFQ0 Q15010 Q3KQZ0 Q5JUP7 Q75R47 Q86XD3

Database IDs:

Citations:

PubMed ID: 1549122

Title: The translocation (6;9), associated with a specific subtype of acute myeloid leukemia, results in the fusion of two genes, dek and can, and the expression of a chimeric, leukemia-specific dek-can mRNA.

PubMed ID: 1549122

DOI: 10.1128/mcb.12.4.1687-1697.1992

PubMed ID: 7584026

Title: Prediction of the coding sequences of unidentified human genes. I. The coding sequences of 40 new genes (KIAA0001-KIAA0040) deduced by analysis of randomly sampled cDNA clones from human immature myeloid cell line KG-1.

PubMed ID: 7584026

DOI: 10.1093/dnares/1.1.27

PubMed ID: 15164053

Title: DNA sequence and analysis of human chromosome 9.

PubMed ID: 15164053

DOI: 10.1038/nature02465

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: 1630450

Title: Can, a putative oncogene associated with myeloid leukemogenesis, may be activated by fusion of its 3' half to different genes: characterization of the set gene.

PubMed ID: 1630450

DOI: 10.1128/mcb.12.8.3346-3355.1992

PubMed ID: 8108440

Title: The human CAN protein, a putative oncogene product associated with myeloid leukemogenesis, is a nuclear pore complex protein that faces the cytoplasm.

PubMed ID: 8108440

DOI: 10.1073/pnas.91.4.1519

PubMed ID: 9049309

Title: The human homologue of yeast CRM1 is in a dynamic subcomplex with CAN/Nup214 and the novel nuclear pore component Nup88.

PubMed ID: 9049309

DOI: 10.1093/emboj/16.4.807

PubMed ID: 11777942

Title: Exportin-5, a novel karyopherin, mediates nuclear export of double-stranded RNA binding proteins.

PubMed ID: 11777942

DOI: 10.1083/jcb.200110082

PubMed ID: 14766228

Title: Direct association of tristetraprolin with the nucleoporin CAN/Nup214.

PubMed ID: 14766228

DOI: 10.1016/j.bbrc.2004.01.080

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: 16964243

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

PubMed ID: 16964243

DOI: 10.1038/nbt1240

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: 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: 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: 19386703

Title: Herpesvirus capsid association with the nuclear pore complex and viral DNA release involve the nucleoporin CAN/Nup214 and the capsid protein pUL25.

PubMed ID: 19386703

DOI: 10.1128/jvi.02655-08

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: 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: 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: 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: 25410864

Title: Nuclear import of adenovirus DNA involves direct interaction of hexon with an N-terminal domain of the nucleoporin Nup214.

PubMed ID: 25410864

DOI: 10.1128/jvi.02639-14

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: 31178128

Title: Pathogenic variants in NUP214 cause 'plugged' nuclear pore channels and acute febrile encephalopathy.

PubMed ID: 31178128

DOI: 10.1016/j.ajhg.2019.05.003

PubMed ID: 17264208

Title: Crystal structure of the N-terminal domain of the human protooncogene Nup214/CAN.

PubMed ID: 17264208

DOI: 10.1073/pnas.0610828104

PubMed ID: 19219046

Title: The mRNA export protein DBP5 binds RNA and the cytoplasmic nucleoporin NUP214 in a mutually exclusive manner.

PubMed ID: 19219046

DOI: 10.1038/nsmb.1561

PubMed ID: 19208808

Title: Structural and functional analysis of the interaction between the nucleoporin Nup214 and the DEAD-box helicase Ddx19.

PubMed ID: 19208808

DOI: 10.1073/pnas.0813267106

PubMed ID: 15361874

Title: Fusion of NUP214 to ABL1 on amplified episomes in T-cell acute lymphoblastic leukemia.

PubMed ID: 15361874

DOI: 10.1038/ng1425

PubMed ID: 16959974

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

PubMed ID: 16959974

DOI: 10.1126/science.1133427

PubMed ID: 20851865

Title: SQSTM1-NUP214: a new gene fusion in adult T-cell acute lymphoblastic leukemia.

PubMed ID: 20851865

DOI: 10.3324/haematol.2010.029769

PubMed ID: 30758658

Title: NUP214 deficiency causes severe encephalopathy and microcephaly in humans.

PubMed ID: 30758658

DOI: 10.1007/s00439-019-01979-w

Sequence Information:

Length: 2090
Mass: 213620
Checksum: EE6F0F3DE3D522C6
Sequence:

MGDEMDAMIP EREMKDFQFR ALKKVRIFDS PEELPKERSS LLAVSNKYGL VFAGGASGLQ 
IFPTKNLLIQ NKPGDDPNKI VDKVQGLLVP MKFPIHHLAL SCDNLTLSAC MMSSEYGSII 
AFFDVRTFSN EAKQQKRPFA YHKLLKDAGG MVIDMKWNPT VPSMVAVCLA DGSIAVLQVT 
ETVKVCATLP STVAVTSVCW SPKGKQLAVG KQNGTVVQYL PTLQEKKVIP CPPFYESDHP 
VRVLDVLWIG TYVFAIVYAA ADGTLETSPD VVMALLPKKE EKHPEIFVNF MEPCYGSCTE 
RQHHYYLSYI EEWDLVLAAS AASTEVSILA RQSDQINWES WLLEDSSRAE LPVTDKSDDS 
LPMGVVVDYT NQVEITISDE KTLPPAPVLM LLSTDGVLCP FYMINQNPGV KSLIKTPERL 
SLEGERQPKS PGSTPTTPTS SQAPQKLDAS AAAAPASLPP SSPAAPIATF SLLPAGGAPT 
VFSFGSSSLK SSATVTGEPP SYSSGSDSSK AAPGPGPSTF SFVPPSKASL APTPAASPVA 
PSAASFSFGS SGFKPTLEST PVPSVSAPNI AMKPSFPPST SAVKVNLSEK FTAAATSTPV 
SSSQSAPPMS PFSSASKPAA SGPLSHPTPL SAPPSSVPLK SSVLPSPSGR SAQGSSSPVP 
SMVQKSPRIT PPAAKPGSPQ AKSLQPAVAE KQGHQWKDSD PVMAGIGEEI AHFQKELEEL 
KARTSKACFQ VGTSEEMKML RTESDDLHTF LLEIKETTES LHGDISSLKT TLLEGFAGVE 
EAREQNERNR DSGYLHLLYK RPLDPKSEAQ LQEIRRLHQY VKFAVQDVND VLDLEWDQHL 
EQKKKQRHLL VPERETLFNT LANNREIINQ QRKRLNHLVD SLQQLRLYKQ TSLWSLSSAV 
PSQSSIHSFD SDLESLCNAL LKTTIESHTK SLPKVPAKLS PMKQAQLRNF LAKRKTPPVR 
STAPASLSRS AFLSQRYYED LDEVSSTSSV SQSLESEDAR TSCKDDEAVV QAPRHAPVVR 
TPSIQPSLLP HAAPFAKSHL VHGSSPGVMG TSVATSASKI IPQGADSTML ATKTVKHGAP 
SPSHPISAPQ AAAAAALRRQ MASQAPAVNT LTESTLKNVP QVVNVQELKN NPATPSTAMG 
SSVPYSTAKT PHPVLTPVAA NQAKQGSLIN SLKPSGPTPA SGQLSSGDKA SGTAKIETAV 
TSTPSASGQF SKPFSFSPSG TGFNFGIITP TPSSNFTAAQ GATPSTKESS QPDAFSSGGG 
SKPSYEAIPE SSPPSGITSA SNTTPGEPAA SSSRPVAPSG TALSTTSSKL ETPPSKLGEL 
LFPSSLAGET LGSFSGLRVG QADDSTKPTN KASSTSLTST QPTKTSGVPS GFNFTAPPVL 
GKHTEPPVTS SATTTSVAPP AATSTSSTAV FGSLPVTSAG SSGVISFGGT SLSAGKTSFS 
FGSQQTNSTV PPSAPPPTTA ATPLPTSFPT LSFGSLLSSA TTPSLPMSAG RSTEEATSSA 
LPEKPGDSEV SASAASLLEE QQSAQLPQAP PQTSDSVKKE PVLAQPAVSN SGTAASSTSL 
VALSAEATPA TTGVPDARTE AVPPASSFSV PGQTAVTAAA ISSAGPVAVE TSSTPIASST 
TSIVAPGPSA EAAAFGTVTS GSSVFAQPPA ASSSSAFNQL TNNTATAPSA TPVFGQVAAS 
TAPSLFGQQT GSTASTAAAT PQVSSSGFSS PAFGTTAPGV FGQTTFGQAS VFGQSASSAA 
SVFSFSQPGF SSVPAFGQPA SSTPTSTSGS VFGAASSTSS SSSFSFGQSS PNTGGGLFGQ 
SNAPAFGQSP GFGQGGSVFG GTSAATTTAA TSGFSFCQAS GFGSSNTGSV FGQAASTGGI 
VFGQQSSSSS GSVFGSGNTG RGGGFFSGLG GKPSQDAANK NPFSSASGGF GSTATSNTSN 
LFGNSGAKTF GGFASSSFGE QKPTGTFSSG GGSVASQGFG FSSPNKTGGF GAAPVFGSPP 
TFGGSPGFGG VPAFGSAPAF TSPLGSTGGK VFGEGTAAAS AGGFGFGSSS NTTSFGTLAS 
QNAPTFGSLS QQTSGFGTQS SGFSGFGSGT GGFSFGSNNS SVQGFGGWRS

Genular Protein ID: 2552910486

Symbol: B7ZAV2_HUMAN

Name: N/A

UniProtKB Accession Codes:

B7ZAV2

Database IDs:

Citations:

PubMed ID: 11237011

Title: Initial sequencing and analysis of the human genome.

PubMed ID: 11237011

DOI: 10.1038/35057062

PubMed ID: 15164053

Title: DNA sequence and analysis of human chromosome 9.

PubMed ID: 15164053

DOI: 10.1038/nature02465

PubMed ID: 15496913

Title: Finishing the euchromatic sequence of the human genome.

PubMed ID: 15496913

DOI: 10.1038/nature03001

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: 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: 23186163

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

PubMed ID: 23186163

PubMed ID: 28112733

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

PubMed ID: 28112733

Sequence Information:

Length: 916
Mass: 87973
Checksum: B712583CB93F3592
Sequence:

MKSSLLLRGV HFCFHLPGTA KIETAVTSTP SASGQFSKPF SFSPSGTGFN FGIITPTPSS 
NFTAAQGATP STKESSQPDA FSSGGGSKPS YEAIPESSPP SGITSASNTT PGEPAASSSR 
PVAPSGTALS TTSSKLETPP SKLGELLFPS SLAGETLGSF SGLRVGQADD STKPTNKASS 
TSLTSTQPTK TSGVPSGFNF TAPPVLGKHT EPPVTSSATT TSVAPPAATS TSSTAVFGSL 
PVTSAGSSGV ISFGGTSLSA GKTSFSFGSQ QTNSTVPPSA PPPTTAATPL PTSFPTLSFG 
SLLSSATTPS LPMSAGRSTE EATSSALPEK PGDSEVSASA ASLLEEQQSA QLPQAPPQTS 
DSVKKEPVLA QPAVSNSGTA ASSTSLVALS AEATPATTGV PDARTEAVPP ASSFSVPGQT 
AVTAAAISSA GPVAVETSST PIASSTTSIV APGPSAEAAA FGTVTSGSSV FAQPPAASSS 
SAFNQLTNNT ATAPSATPVF GQVAASTAPS LFGQQTGSTA STAAATPQVS SSGFSSPAFG 
TTAPGVFGQT TFGQASVFGQ SASSAASVFS FSQPGFSSVP AFGQPASSTP TSTSGSVFGA 
ASSTSSSSSF SFGQSSPNTG GGLFGQSNAP AFGQSPGFGQ GGSVFGGTSA ATTTAATSGF 
SFCQASGFGS SNTGSVFGQA ASTGGIVFGQ QSSSSSGSVF GSGNTGRGGG FFSGLGGKPS 
QDAANKNPFS SASGGFGSTA TSNTSNLFGN SGAKTFGGFA SSSFGEQKPT GTFSSGGGSV 
ASQGFGFSSP NKTGGFGAAP VFGSPPTFGG SPGFGGVPAF GSAPAFTSPL GSTGGKVFGE 
GTAAASAGGF GFGSSSNTTS FGTLASQNAP TFGSLSQQTS GFGTQSSGFS GFGSGTGGFS 
FGSNNSSVQG FGGWRS

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: NUP214

Associated with

Cells (max top 100)

Other Information

The translocation (6;9), associated with a specific subtype of acute myeloid leukemia, results in the fusion of two genes, dek and can, and the expression of a chimeric, leukemia-specific dek-can mRNA. PubMed ID: 1549122

Prediction of the coding sequences of unidentified human genes. I. The coding sequences of 40 new genes (KIAA0001-KIAA0040) deduced by analysis of randomly sampled cDNA clones from human immature myeloid cell line KG-1. PubMed ID: 7584026

DNA sequence and analysis of human chromosome 9. PubMed ID: 15164053

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

Can, a putative oncogene associated with myeloid leukemogenesis, may be activated by fusion of its 3' half to different genes: characterization of the set gene. PubMed ID: 1630450

The human CAN protein, a putative oncogene product associated with myeloid leukemogenesis, is a nuclear pore complex protein that faces the cytoplasm. PubMed ID: 8108440

The human homologue of yeast CRM1 is in a dynamic subcomplex with CAN/Nup214 and the novel nuclear pore component Nup88. PubMed ID: 9049309

Exportin-5, a novel karyopherin, mediates nuclear export of double-stranded RNA binding proteins. PubMed ID: 11777942

Direct association of tristetraprolin with the nucleoporin CAN/Nup214. PubMed ID: 14766228

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

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

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

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

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

Herpesvirus capsid association with the nuclear pore complex and viral DNA release involve the nucleoporin CAN/Nup214 and the capsid protein pUL25. PubMed ID: 19386703

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

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

Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features. PubMed ID: 22223895

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

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

Nuclear import of adenovirus DNA involves direct interaction of hexon with an N-terminal domain of the nucleoporin Nup214. PubMed ID: 25410864

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

Pathogenic variants in NUP214 cause 'plugged' nuclear pore channels and acute febrile encephalopathy. PubMed ID: 31178128

Crystal structure of the N-terminal domain of the human protooncogene Nup214/CAN. PubMed ID: 17264208

The mRNA export protein DBP5 binds RNA and the cytoplasmic nucleoporin NUP214 in a mutually exclusive manner. PubMed ID: 19219046

Structural and functional analysis of the interaction between the nucleoporin Nup214 and the DEAD-box helicase Ddx19. PubMed ID: 19208808

Fusion of NUP214 to ABL1 on amplified episomes in T-cell acute lymphoblastic leukemia. PubMed ID: 15361874

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

SQSTM1-NUP214: a new gene fusion in adult T-cell acute lymphoblastic leukemia. PubMed ID: 20851865

NUP214 deficiency causes severe encephalopathy and microcephaly in humans. PubMed ID: 30758658

Initial sequencing and analysis of the human genome. PubMed ID: 11237011

DNA sequence and analysis of human chromosome 9. PubMed ID: 15164053

Finishing the euchromatic sequence of the human genome. PubMed ID: 15496913

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

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

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

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

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

Database document:

PubMed ID: 1549122

PubMed ID: 7584026

PubMed ID: 15164053

PubMed ID: 15489334

PubMed ID: 1630450

PubMed ID: 8108440

PubMed ID: 9049309

PubMed ID: 11777942

PubMed ID: 14766228

PubMed ID: 17081983

PubMed ID: 16964243

PubMed ID: 17924679

PubMed ID: 18691976

PubMed ID: 18669648

PubMed ID: 19413330

PubMed ID: 19386703

PubMed ID: 19690332

PubMed ID: 20068231

PubMed ID: 21269460

PubMed ID: 21406692

PubMed ID: 22223895

PubMed ID: 23186163

PubMed ID: 24275569

PubMed ID: 25410864

PubMed ID: 28112733

PubMed ID: 30543681

PubMed ID: 31178128

PubMed ID: 17264208

PubMed ID: 19219046

PubMed ID: 19208808

PubMed ID: 15361874

PubMed ID: 16959974

PubMed ID: 20851865

PubMed ID: 30758658

PubMed ID: 11237011

PubMed ID: 15164053

PubMed ID: 15496913

PubMed ID: 18691976

PubMed ID: 18669648

PubMed ID: 20068231

PubMed ID: 21269460

PubMed ID: 23186163

PubMed ID: 28112733