EXT1

From Wikipedia, the free encyclopedia

Exostoses (multiple) 1

Identifiers

EXT1; EXT; ttv

External IDs

OMIM: 608177 MGI: 894663 HomoloGene: 30957

Gene ontology
Molecular Function:	• transferase activity, transferring glycosyl groups • glucuronosyl-N-acetylglucosaminyl-proteoglycan 4-alpha-N-acetylglucosaminyltransferase activity • N-acetylglucosaminyl-proteoglycan 4-beta-glucuronosyltransferase activity
Cellular Component:	• endoplasmic reticulum • endoplasmic reticulum membrane • Golgi apparatus • membrane • integral to membrane • integral to endoplasmic reticulum membrane
Biological Process:	• skeletal development • glycosaminoglycan biosynthetic process • cell cycle • signal transduction • gastrulation • endoderm development • mesoderm development • heparan sulfate proteoglycan biosynthetic process • negative regulation of progression through cell cycle

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_000127 (mRNA)
NP_000118 (protein)

NM_010162 (mRNA)
NP_034292 (protein)

Location

Chr 8: 118.88 - 119.19 Mb

Chr 15: 52.9 - 53.18 Mb

Pubmed search

[1]

[2]

Exostoses (multiple) 1, also known as EXT1, is a human gene.^[1]

This gene encodes an endoplasmic reticulum-resident type II transmembrane glycosyltransferase involved in the chain elongation step of heparan sulfate biosynthesis. Mutations in this gene cause the type I form of multiple exostoses.^[1]

[edit] References

^ ^a ^b Entrez Gene: EXT1 exostoses (multiple) 1.

[edit] Further reading

Wuyts W, Van Hul W (2000). "Molecular basis of multiple exostoses: mutations in the EXT1 and EXT2 genes.". Hum. Mutat. 15 (3): 220–7. doi:10.1002/(SICI)1098-1004(200003)15:3<220::AID-HUMU2>3.0.CO;2-K. PMID 10679937.
Duncan G, McCormick C, Tufaro F (2001). "The link between heparan sulfate and hereditary bone disease: finding a function for the EXT family of putative tumor suppressor proteins.". J. Clin. Invest. 108 (4): 511–6. PMID 11518722.
Ogle RF, Dalzell P, Turner G, et al. (1992). "Multiple exostoses in a patient with t(8;11)(q24.11;p15.5).". J. Med. Genet. 28 (12): 881–3. PMID 1757967.
Ahn J, Lüdecke HJ, Lindow S, et al. (1995). "Cloning of the putative tumour suppressor gene for hereditary multiple exostoses (EXT1).". Nat. Genet. 11 (2): 137–43. doi:10.1038/ng1095-137. PMID 7550340.
Cook A, Raskind W, Blanton SH, et al. (1993). "Genetic heterogeneity in families with hereditary multiple exostoses.". Am. J. Hum. Genet. 53 (1): 71–9. PMID 8317501.
Hou J, Parrish J, Lüdecke HJ, et al. (1996). "A 4-megabase YAC contig that spans the Langer-Giedion syndrome region on human chromosome 8q24.1: use in refining the location of the trichorhinophalangeal syndrome and multiple exostoses genes (TRPS1 and EXT1).". Genomics 29 (1): 87–97. PMID 8530105.
Hecht JT, Hogue D, Wang Y, et al. (1997). "Hereditary multiple exostoses (EXT): mutational studies of familial EXT1 cases and EXT-associated malignancies.". Am. J. Hum. Genet. 60 (1): 80–6. PMID 8981950.
Lüdecke HJ, Ahn J, Lin X, et al. (1997). "Genomic organization and promoter structure of the human EXT1 gene.". Genomics 40 (2): 351–4. doi:10.1006/geno.1996.4577. PMID 9119404.
Philippe C, Porter DE, Emerton ME, et al. (1997). "Mutation screening of the EXT1 and EXT2 genes in patients with hereditary multiple exostoses.". Am. J. Hum. Genet. 61 (3): 520–8. PMID 9326317.
Wuyts W, Van Hul W, De Boulle K, et al. (1998). "Mutations in the EXT1 and EXT2 genes in hereditary multiple exostoses.". Am. J. Hum. Genet. 62 (2): 346–54. PMID 9463333.
Raskind WH, Conrad EU, Matsushita M, et al. (1998). "Evaluation of locus heterogeneity and EXT1 mutations in 34 families with hereditary multiple exostoses.". Hum. Mutat. 11 (3): 231–9. doi:10.1002/(SICI)1098-1004(1998)11:3<231::AID-HUMU8>3.0.CO;2-K. PMID 9521425.
McCormick C, Leduc Y, Martindale D, et al. (1998). "The putative tumour suppressor EXT1 alters the expression of cell-surface heparan sulfate.". Nat. Genet. 19 (2): 158–61. doi:10.1038/514. PMID 9620772.
Lin X, Gan L, Klein WH, Wells D (1998). "Expression and functional analysis of mouse EXT1, a homolog of the human multiple exostoses type 1 gene.". Biochem. Biophys. Res. Commun. 248 (3): 738–43. doi:10.1006/bbrc.1998.9050. PMID 9703997.
Lind T, Tufaro F, McCormick C, et al. (1998). "The putative tumor suppressors EXT1 and EXT2 are glycosyltransferases required for the biosynthesis of heparan sulfate.". J. Biol. Chem. 273 (41): 26265–8. PMID 9756849.
Bovée JV, Cleton-Jansen AM, Wuyts W, et al. (1999). "EXT-mutation analysis and loss of heterozygosity in sporadic and hereditary osteochondromas and secondary chondrosarcomas.". Am. J. Hum. Genet. 65 (3): 689–98. PMID 10441575.
Xu L, Xia J, Jiang H, et al. (1999). "Mutation analysis of hereditary multiple exostoses in the Chinese.". Hum. Genet. 105 (1-2): 45–50. PMID 10480354.
Simmons AD, Musy MM, Lopes CS, et al. (1999). "A direct interaction between EXT proteins and glycosyltransferases is defective in hereditary multiple exostoses.". Hum. Mol. Genet. 8 (12): 2155–64. PMID 10545594.
McCormick C, Duncan G, Goutsos KT, Tufaro F (2000). "The putative tumor suppressors EXT1 and EXT2 form a stable complex that accumulates in the Golgi apparatus and catalyzes the synthesis of heparan sulfate.". Proc. Natl. Acad. Sci. U.S.A. 97 (2): 668–73. PMID 10639137.
Kobayashi S, Morimoto K, Shimizu T, et al. (2000). "Association of EXT1 and EXT2, hereditary multiple exostoses gene products, in Golgi apparatus.". Biochem. Biophys. Res. Commun. 268 (3): 860–7. doi:10.1006/bbrc.2000.2219. PMID 10679296.