NID2

From Wikipedia, the free encyclopedia

Nidogen 2 (osteonidogen)

Identifiers

NID2; NID-2

External IDs

OMIM: 605399 MGI: 1298229 HomoloGene: 40575 GeneCards: NID2 Gene

Gene Ontology
Molecular function	• calcium ion binding • protein binding • collagen binding
Cellular component	• basement membrane • cell surface • extracellular matrix
Biological process	• cell adhesion • cell-matrix adhesion
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

ENSG00000087303

ENSMUSG00000021806

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 14:
52.47 – 52.54 Mb

Chr 14:
19.75 – 19.81 Mb

PubMed search

Nidogen-2 is a protein that in humans is encoded by the NID2 gene.^[1]^[2]

Basement membranes, which are composed of type IV collagens (see MIM 120130), laminins (see LAMC1; MIM 150290), perlecan (HSPG2; MIM 142461), and nidogen (see NID1; MIM 131390), are thin pericellular protein matrices that control a large number of cellular activities, including adhesion, migration, differentiation, gene expression, and apoptosis.[supplied by OMIM]^[2]

References

↑ Kohfeldt E, Sasaki T, Gohring W, Timpl R (Oct 1998). "Nidogen-2: a new basement membrane protein with diverse binding properties". J Mol Biol 282 (1): 99–109. doi:10.1006/jmbi.1998.2004. PMID 9733643.
↑ 2.0 2.1 "Entrez Gene: NID2 nidogen 2 (osteonidogen)".

Further reading

Ulazzi L, Sabbioni S, Miotto E, et al. (2007). "Nidogen 1 and 2 gene promoters are aberrantly methylated in human gastrointestinal cancer.". Mol. Cancer 6 (1): 17. doi:10.1186/1476-4598-6-17. PMC 1831485. PMID 17328794.
Nischt R, Schmidt C, Mirancea N, et al. (2007). "Lack of nidogen-1 and -2 prevents basement membrane assembly in skin-organotypic coculture.". J. Invest. Dermatol. 127 (3): 545–54. doi:10.1038/sj.jid.5700562. PMID 17008882.
Kimura K, Wakamatsu A, Suzuki Y, et al. (2006). "Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes.". Genome Res. 16 (1): 55–65. doi:10.1101/gr.4039406. PMC 1356129. PMID 16344560.
Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network.". Nature 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
Miosge N, Sasaki T, Timpl R (2003). "Evidence of nidogen-2 compensation for nidogen-1 deficiency in transgenic mice.". Matrix Biol. 21 (7): 611–21. doi:10.1016/S0945-053X(02)00070-7. PMID 12475645.
Miosge N, Holzhausen S, Zelent C, et al. (2002). "Nidogen-1 and nidogen-2 are found in basement membranes during human embryonic development.". Histochem. J. 33 (9-10): 523–30. doi:10.1023/A:1014995523521. PMID 12005023.
Tu H, Sasaki T, Snellman A, et al. (2002). "The type XIII collagen ectodomain is a 150-nm rod and capable of binding to fibronectin, nidogen-2, perlecan, and heparin.". J. Biol. Chem. 277 (25): 23092–9. doi:10.1074/jbc.M107583200. PMID 11956183.
Sasaki T, Göhring W, Mann K, et al. (2002). "Short arm region of laminin-5 gamma2 chain: structure, mechanism of processing and binding to heparin and proteins.". J. Mol. Biol. 314 (4): 751–63. doi:10.1006/jmbi.2001.5176. PMID 11733994.
Sasaki T, Göhring W, Miosge N, et al. (1999). "Tropoelastin binding to fibulins, nidogen-2 and other extracellular matrix proteins.". FEBS Lett. 460 (2): 280–4. doi:10.1016/S0014-5793(99)01362-9. PMID 10544250.
Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery.". Genome Res. 6 (9): 791–806. doi:10.1101/gr.6.9.791. PMID 8889548.

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