NOG (gene)

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File:PBB Protein NOG image.jpg
PDB rendering based on 1m4u.
Available structures
PDB Ortholog search: Template:Homologene2PDBe PDBe, Template:Homologene2uniprot RCSB
Symbols NOG ; SYM1; SYNS1
External IDs Template:OMIM5 Template:MGI HomoloGene3979
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

Noggin, also known as NOG, is a human gene.[1]

The secreted polypeptide noggin, encoded by the NOG gene, binds and inactivates members of the transforming growth factor-beta (TGF-beta) superfamily signaling proteins, such as bone morphogenetic protein-4 (BMP4). By diffusing through extracellular matrices more efficiently than members of the TGF-beta superfamily, noggin may have a principal role in creating morphogenic gradients. Noggin appears to have pleiotropic effect, both early in development as well as in later stages. It was originally isolated from Xenopus based on its ability to restore normal dorsal-ventral body axis in embryos that had been artificially ventralized by UV treatment. The results of the mouse knockout of noggin suggest that it is involved in numerous developmental processes, such as neural tube fusion and joint formation. Recently, several dominant human NOG mutations in unrelated families with proximal symphalangism (SYM1) and multiple synostoses syndrome (SYNS1) were identified; both SYM1 and SYNS1 have multiple joint fusion as their principal feature, and map to the same region (17q22) as NOG. All NOG mutations altered evolutionarily conserved amino acid residues. The amino acid sequence of human noggin is highly homologous to that of Xenopus, rat and mouse.[1]


  1. 1.0 1.1 "Entrez Gene: NOG noggin".

Further reading

  • Smith WC (1999). "TGF beta inhibitors. New and unexpected requirements in vertebrate development". Trends Genet. 15 (1): 3–5. PMID 10087923.
  • Polymeropoulos MH, Poush J, Rubenstein JR, Francomano CA (1995). "Localization of the gene (SYM1) for proximal symphalangism to human chromosome 17q21-q22". Genomics. 27 (2): 225–9. doi:10.1006/geno.1995.1035. PMID 7557985.
  • Valenzuela DM, Economides AN, Rojas E; et al. (1995). "Identification of mammalian noggin and its expression in the adult nervous system". J. Neurosci. 15 (9): 6077–84. PMID 7666191.
  • McMahon JA, Takada S, Zimmerman LB; et al. (1998). "Noggin-mediated antagonism of BMP signaling is required for growth and patterning of the neural tube and somite". Genes Dev. 12 (10): 1438–52. PMID 9585504.
  • Brunet LJ, McMahon JA, McMahon AP, Harland RM (1998). "Noggin, cartilage morphogenesis, and joint formation in the mammalian skeleton". Science. 280 (5368): 1455–7. PMID 9603738.
  • Krakow D, Reinker K, Powell B; et al. (1998). "Localization of a multiple synostoses-syndrome disease gene to chromosome 17q21-22". Am. J. Hum. Genet. 63 (1): 120–4. PMID 9634519.
  • Gong Y, Krakow D, Marcelino J; et al. (1999). "Heterozygous mutations in the gene encoding noggin affect human joint morphogenesis". Nat. Genet. 21 (3): 302–4. doi:10.1038/6821. PMID 10080184.
  • Li W, LoTurco JJ (2000). "Noggin is a negative regulator of neuronal differentiation in developing neocortex". Dev. Neurosci. 22 (1–2): 68–73. PMID 10657699.
  • Dixon ME, Armstrong P, Stevens DB, Bamshad M (2002). "Identical mutations in NOG can cause either tarsal/carpal coalition syndrome or proximal symphalangism". Genet. Med. 3 (5): 349–53. PMID 11545688.
  • Marcelino J, Sciortino CM, Romero MF; et al. (2001). "Human disease-causing NOG missense mutations: effects on noggin secretion, dimer formation, and bone morphogenetic protein binding". Proc. Natl. Acad. Sci. U.S.A. 98 (20): 11353–8. doi:10.1073/pnas.201367598. PMID 11562478.
  • Beck HN, Drahushuk K, Jacoby DB; et al. (2003). "Bone morphogenetic protein-5 (BMP-5) promotes dendritic growth in cultured sympathetic neurons". BMC neuroscience. 2: 12. PMID 11580864.
  • Paine-Saunders S, Viviano BL, Economides AN, Saunders S (2002). "Heparan sulfate proteoglycans retain Noggin at the cell surface: a potential mechanism for shaping bone morphogenetic protein gradients". J. Biol. Chem. 277 (3): 2089–96. doi:10.1074/jbc.M109151200. PMID 11706034.
  • Takahashi T, Takahashi I, Komatsu M; et al. (2002). "Mutations of the NOG gene in individuals with proximal symphalangism and multiple synostosis syndrome". Clin. Genet. 60 (6): 447–51. PMID 11846737.
  • Mangino M, Flex E, Digilio MC; et al. (2002). "Identification of a novel NOG gene mutation (P35S) in an Italian family with symphalangism". Hum. Mutat. 19 (3): 308. doi:10.1002/humu.9016. PMID 11857750.
  • Brown DJ, Kim TB, Petty EM; et al. (2002). "Autosomal dominant stapes ankylosis with broad thumbs and toes, hyperopia, and skeletal anomalies is caused by heterozygous nonsense and frameshift mutations in NOG, the gene encoding noggin". Am. J. Hum. Genet. 71 (3): 618–24. PMID 12089654.
  • Hall AK, Burke RM, Anand M, Dinsio KJ (2002). "Activin and bone morphogenetic proteins are present in perinatal sensory neuron target tissues that induce neuropeptides". J. Neurobiol. 52 (1): 52–60. doi:10.1002/neu.10068. PMID 12115893.
  • 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. PMID 12477932.
  • Groppe J, Greenwald J, Wiater E; et al. (2003). "Structural basis of BMP signalling inhibition by the cystine knot protein Noggin". Nature. 420 (6916): 636–42. doi:10.1038/nature01245. PMID 12478285.
  • Brown DJ, Kim TB, Petty EM; et al. (2003). "Characterization of a stapes ankylosis family with a NOG mutation". Otol. Neurotol. 24 (2): 210–5. PMID 12621334.

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