Nidogen-2

Nidogen 2 (osteonidogen)
Identifiers
Symbols NID2 ; NID-2
External IDs OMIM: 605399 MGI: 1298229 HomoloGene: 40575 GeneCards: NID2 Gene
RNA expression pattern
More reference expression data
Orthologs
Species Human Mouse
Entrez 22795 18074
Ensembl ENSG00000087303 ENSMUSG00000021806
UniProt Q14112 O88322
RefSeq (mRNA) NM_007361 NM_008695
RefSeq (protein) NP_031387 NP_032721
Location (UCSC) Chr 14:
52 – 52.07 Mb
Chr 14:
19.75 – 19.81 Mb
PubMed search

Nidogen-2, also known as osteonidogen, is a basal lamina protein of the nidogen family. It was the second nidogen to be described after nidogen-1 (entactin). Both play key roles during late embryonic development.[1] In humans it is encoded by the NID2 gene.[2][3]

References

  1. Miosge N, Holzhausen S, Zelent C, Sprysch P, Herken R (2002). "Nidogen-1 and nidogen-2 are found in basement membranes during human embryonic development". The Histochemical Journal 33 (9-10): 523–30. doi:10.1023/A:1014995523521. PMID 12005023.
  2. Kohfeldt E, Sasaki T, Göhring W, Timpl R (Sep 1998). "Nidogen-2: a new basement membrane protein with diverse binding properties". Journal of Molecular Biology 282 (1): 99–109. doi:10.1006/jmbi.1998.2004. PMID 9733643.
  3. "Entrez Gene: NID2 nidogen 2 (osteonidogen)".

Further reading

  • Ulazzi L, Sabbioni S, Miotto E, Veronese A, Angusti A, Gafà R, Manfredini S, Farinati F, Sasaki T, Lanza G, Negrini M (2007). "Nidogen 1 and 2 gene promoters are aberrantly methylated in human gastrointestinal cancer". Molecular Cancer 6 (1): 17. doi:10.1186/1476-4598-6-17. PMC 1831485. PMID 17328794. 
  • Nischt R, Schmidt C, Mirancea N, Baranowsky A, Mokkapati S, Smyth N, Woenne EC, Stark HJ, Boukamp P, Breitkreutz D (Mar 2007). "Lack of nidogen-1 and -2 prevents basement membrane assembly in skin-organotypic coculture". The Journal of Investigative Dermatology 127 (3): 545–54. doi:10.1038/sj.jid.5700562. PMID 17008882. 
  • Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (Oct 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514. 
  • Miosge N, Sasaki T, Timpl R (Nov 2002). "Evidence of nidogen-2 compensation for nidogen-1 deficiency in transgenic mice". Matrix Biology 21 (7): 611–21. doi:10.1016/S0945-053X(02)00070-7. PMID 12475645. 
  • Tu H, Sasaki T, Snellman A, Göhring W, Pirilä P, Timpl R, Pihlajaniemi T (Jun 2002). "The type XIII collagen ectodomain is a 150-nm rod and capable of binding to fibronectin, nidogen-2, perlecan, and heparin". The Journal of Biological Chemistry 277 (25): 23092–9. doi:10.1074/jbc.M107583200. PMID 11956183. 
  • Sasaki T, Göhring W, Mann K, Brakebusch C, Yamada Y, Fässler R, Timpl R (Dec 2001). "Short arm region of laminin-5 gamma2 chain: structure, mechanism of processing and binding to heparin and proteins". Journal of Molecular Biology 314 (4): 751–63. doi:10.1006/jmbi.2001.5176. PMID 11733994. 
  • Sasaki T, Göhring W, Miosge N, Abrams WR, Rosenbloom J, Timpl R (Oct 1999). "Tropoelastin binding to fibulins, nidogen-2 and other extracellular matrix proteins". FEBS Letters 460 (2): 280–4. doi:10.1016/S0014-5793(99)01362-9. PMID 10544250. 
  • Bonaldo MF, Lennon G, Soares MB (Sep 1996). "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Research 6 (9): 791–806. doi:10.1101/gr.6.9.791. PMID 8889548. 
This article is issued from Wikipedia - version of the Wednesday, February 10, 2016. The text is available under the Creative Commons Attribution/Share Alike but additional terms may apply for the media files.