NOTCH2

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Notch homolog 2 (Drosophila)
File:PBB Protein NOTCH2 image.jpg
PDB rendering based on 2oo4.
Available structures
PDB Ortholog search: Template:Homologene2PDBe PDBe, Template:Homologene2uniprot RCSB
Identifiers
Symbols NOTCH2 ; AGS2; hN2
External IDs Template:OMIM5 Template:MGI HomoloGene7865
RNA expression pattern
File:PBB GE NOTCH2 212377 s at tn.png
File:PBB GE NOTCH2 202443 x at tn.png
File:PBB GE NOTCH2 202445 s at tn.png
More reference expression data
Orthologs
Template:GNF Ortholog box
Species Human Mouse
Entrez n/a n/a
Ensembl n/a n/a
UniProt n/a n/a
RefSeq (mRNA) n/a n/a
RefSeq (protein) n/a n/a
Location (UCSC) n/a n/a
PubMed search n/a n/a

Notch homolog 2 (Drosophila), also known as NOTCH2, is a human gene.

NOTCH2 is associated with Alagille syndrome.[1]

This gene encodes a member of the Notch family. Members of this Type 1 transmembrane protein family share structural characteristics including an extracellular domain consisting of multiple epidermal growth factor-like (EGF) repeats, and an intracellular domain consisting of multiple, different domain types. Notch family members play a role in a variety of developmental processes by controlling cell fate decisions. The Notch signaling network is an evolutionarily conserved intercellular signaling pathway which regulates interactions between physically adjacent cells. In Drosophilia, notch interaction with its cell-bound ligands (delta, serrate) establishes an intercellular signaling pathway that plays a key role in development. Homologues of the notch-ligands have also been identified in human, but precise interactions between these ligands and the human notch homologues remain to be determined. This protein is cleaved in the trans-Golgi network, and presented on the cell surface as a heterodimer. This protein functions as a receptor for membrane bound ligands, and may play a role in vascular, renal and hepatic development.[2]

References

  1. Samejima H, Torii C, Kosaki R; et al. (2007). "Screening for Alagille syndrome mutations in the JAG1 and NOTCH2 genes using denaturing high-performance liquid chromatography". Genet. Test. 11 (3): 216–27. doi:10.1089/gte.2006.0519. PMID 17949281.
  2. "Entrez Gene: NOTCH2 Notch homolog 2 (Drosophila)".

Further reading

  • Artavanis-Tsakonas S, Rand MD, Lake RJ (1999). "Notch signaling: cell fate control and signal integration in development". Science. 284 (5415): 770–6. PMID 10221902.
  • Kojika S, Griffin JD (2001). "Notch receptors and hematopoiesis". Exp. Hematol. 29 (9): 1041–52. PMID 11532344.
  • Schwarzmeier JD, Hubmann R, Düchler M; et al. (2005). "Regulation of CD23 expression by Notch2 in B-cell chronic lymphocytic leukemia". Leuk. Lymphoma. 46 (2): 157–65. doi:10.1080/10428190400010742. PMID 15621797.
  • Stifani S, Blaumueller CM, Redhead NJ; et al. (1993). "Human homologs of a Drosophila Enhancer of split gene product define a novel family of nuclear proteins". Nat. Genet. 2 (2): 119–27. doi:10.1038/ng1092-119. PMID 1303260.
  • Larsson C, Lardelli M, White I, Lendahl U (1995). "The human NOTCH1, 2, and 3 genes are located at chromosome positions 9q34, 1p13-p11, and 19p13.2-p13.1 in regions of neoplasia-associated translocation". Genomics. 24 (2): 253–8. doi:10.1006/geno.1994.1613. PMID 7698746.
  • Katsanis N, Fitzgibbon J, Fisher EM (1996). "Paralogy mapping: identification of a region in the human MHC triplicated onto human chromosomes 1 and 9 allows the prediction and isolation of novel PBX and NOTCH loci". Genomics. 35 (1): 101–8. doi:10.1006/geno.1996.0328. PMID 8661110.
  • Hsieh JJ, Nofziger DE, Weinmaster G, Hayward SD (1997). "Epstein-Barr virus immortalization: Notch2 interacts with CBF1 and blocks differentiation". J. Virol. 71 (3): 1938–45. PMID 9032325.
  • Blaumueller CM, Qi H, Zagouras P, Artavanis-Tsakonas S (1997). "Intracellular cleavage of Notch leads to a heterodimeric receptor on the plasma membrane". Cell. 90 (2): 281–91. PMID 9244302.
  • Bigas A, Martin DI, Milner LA (1998). "Notch1 and Notch2 inhibit myeloid differentiation in response to different cytokines". Mol. Cell. Biol. 18 (4): 2324–33. PMID 9528802.
  • Berezovska O, Xia MQ, Hyman BT (1998). "Notch is expressed in adult brain, is coexpressed with presenilin-1, and is altered in Alzheimer disease". J. Neuropathol. Exp. Neurol. 57 (8): 738–45. PMID 9720489.
  • Gray GE, Mann RS, Mitsiadis E; et al. (1999). "Human ligands of the Notch receptor". Am. J. Pathol. 154 (3): 785–94. PMID 10079256.
  • Shimizu K, Chiba S, Kumano K; et al. (2000). "Mouse jagged1 physically interacts with notch2 and other notch receptors. Assessment by quantitative methods". J. Biol. Chem. 274 (46): 32961–9. PMID 10551863.
  • Shimizu K, Chiba S, Hosoya N; et al. (2000). "Binding of Delta1, Jagged1, and Jagged2 to Notch2 rapidly induces cleavage, nuclear translocation, and hyperphosphorylation of Notch2". Mol. Cell. Biol. 20 (18): 6913–22. PMID 10958687.
  • Wu L, Aster JC, Blacklow SC; et al. (2001). "MAML1, a human homologue of Drosophila mastermind, is a transcriptional co-activator for NOTCH receptors". Nat. Genet. 26 (4): 484–9. doi:10.1038/82644. PMID 11101851.
  • Sriuranpong V, Borges MW, Ravi RK; et al. (2001). "Notch signaling induces cell cycle arrest in small cell lung cancer cells". Cancer Res. 61 (7): 3200–5. PMID 11306509.
  • Shimizu K, Chiba S, Saito T; et al. (2001). "Manic fringe and lunatic fringe modify different sites of the Notch2 extracellular region, resulting in different signaling modulation". J. Biol. Chem. 276 (28): 25753–8. doi:10.1074/jbc.M103473200. PMID 11346656.
  • Saxena MT, Schroeter EH, Mumm JS, Kopan R (2001). "Murine notch homologs (N1-4) undergo presenilin-dependent proteolysis". J. Biol. Chem. 276 (43): 40268–73. doi:10.1074/jbc.M107234200. PMID 11518718.
  • Inglés-Esteve J, Espinosa L, Milner LA; et al. (2002). "Phosphorylation of Ser2078 modulates the Notch2 function in 32D cell differentiation". J. Biol. Chem. 276 (48): 44873–80. doi:10.1074/jbc.M104703200. PMID 11577080.

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