EXTL2

From Wikipedia, the free encyclopedia

Exostoses (multiple)-like 2

Identifiers

External IDs

OMIM: 602411 MGI: 1889574 HomoloGene: 1102

Gene ontology
Molecular Function:	• glucuronyl-galactosyl-proteoglycan 4-alpha-N-acetylglucosaminyltransferase activity • transferase activity, transferring glycosyl groups • manganese ion binding • alpha-1,4-N-acetylgalactosaminyltransferase activity • metal ion binding
Cellular Component:	• endoplasmic reticulum • membrane • integral to membrane
Biological Process:	• N-acetylglucosamine metabolic process • UDP-N-acetylgalactosamine metabolic process

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_001033025 (mRNA)
NP_001028197 (protein)

NM_021388 (mRNA)
NP_067363 (protein)

Location

Chr 1: 101.11 - 101.13 Mb

Chr 3: 116 - 116.02 Mb

Pubmed search

[1]

[2]

Exostoses (multiple)-like 2, also known as EXTL2, is a human gene.^[1]

[edit] References

^ Entrez Gene: EXTL2 exostoses (multiple)-like 2.

[edit] Further reading

Sobhany M, Dong J, Negishi M (2005). "Two-step mechanism that determines the donor binding specificity of human UDP-N-acetylhexosaminyltransferase.". J. Biol. Chem. 280 (25): 23441–5. doi:10.1074/jbc.M413379200. PMID 15831490.
Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs.". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
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.
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.
Kitagawa H, Shimakawa H, Sugahara K (1999). "The tumor suppressor EXT-like gene EXTL2 encodes an alpha1, 4-N-acetylhexosaminyltransferase that transfers N-acetylgalactosamine and N-acetylglucosamine to the common glycosaminoglycan-protein linkage region. The key enzyme for the chain initiation of heparan sulfate.". J. Biol. Chem. 274 (20): 13933–7. PMID 10318803.
Saito T, Seki N, Yamauchi M, et al. (1998). "Structure, chromosomal location, and expression profile of EXTR1 and EXTR2, new members of the multiple exostoses gene family.". Biochem. Biophys. Res. Commun. 243 (1): 61–6. PMID 9473480.
Wuyts W, Van Hul W, Hendrickx J, et al. (1998). "Identification and characterization of a novel member of the EXT gene family, EXTL2.". Eur. J. Hum. Genet. 5 (6): 382–9. PMID 9450183.
Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery.". Genome Res. 6 (9): 791–806. PMID 8889548.