CHST10

From Wikipedia, the free encyclopedia

Carbohydrate sulfotransferase 10

Identifiers

CHST10; HNK-1ST; HNK1ST; MGC17148

External IDs

OMIM: 606376 MGI: 2138283 HomoloGene: 21013

Gene ontology
Molecular Function:	• sulfotransferase activity • transferase activity
Cellular Component:	• membrane fraction • Golgi apparatus • membrane • integral to membrane
Biological Process:	• carbohydrate metabolic process • cell adhesion • learning • long-term memory

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_004854 (mRNA)
NP_004845 (protein)

NM_145142 (mRNA)
NP_660124 (protein)

Location

Chr 2: 100.37 - 100.4 Mb

Chr 1: 38.81 - 38.84 Mb

Pubmed search

[1]

[2]

Carbohydrate sulfotransferase 10, also known as CHST10, is a human gene.^[1]

Cell surface carbohydrates modulate a variety of cellular functions and are typically synthesized in a stepwise manner. HNK1ST plays a role in the biosynthesis of HNK1 (see MIM 151290), a neuronally expressed carbohydrate that contains a sulfoglucuronyl residue.[supplied by OMIM]^[1]

[edit] References

^ ^a ^b Entrez Gene: CHST10 carbohydrate sulfotransferase 10.

[edit] Further reading

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. PMID 16344560.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121-7. doi:10.1101/gr.2596504. PMID 15489334.
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.
Kang HG, Evers MR, Xia G, et al. (2002). "Molecular cloning and characterization of chondroitin-4-O-sulfotransferase-3. A novel member of the HNK-1 family of sulfotransferases.". J. Biol. Chem. 277 (38): 34766-72. doi:10.1074/jbc.M204907200. PMID 12080076.
Ong E, Yeh JC, Ding Y, et al. (1999). "Structure and function of HNK-1 sulfotransferase. Identification of donor and acceptor binding sites by site-directed mutagenesis.". J. Biol. Chem. 274 (36): 25608-12. PMID 10464296.
Ong E, Yeh JC, Ding Y, et al. (1998). "Expression cloning of a human sulfotransferase that directs the synthesis of the HNK-1 glycan on the neural cell adhesion molecule and glycolipids.". J. Biol. Chem. 273 (9): 5190-5. PMID 9478973.
Yu W, Andersson B, Worley KC, et al. (1997). "Large-scale concatenation cDNA sequencing.". Genome Res. 7 (4): 353-8. PMID 9110174.
Andersson B, Wentland MA, Ricafrente JY, et al. (1996). "A "double adaptor" method for improved shotgun library construction.". Anal. Biochem. 236 (1): 107-13. doi:10.1006/abio.1996.0138. PMID 8619474.
Shilatifard A, Merkle RK, Helland DE, et al. (1993). "Complex-type N-linked oligosaccharides of gp120 from human immunodeficiency virus type 1 contain sulfated N-acetylglucosamine.". J. Virol. 67 (2): 943-52. PMID 8419650.
Bernstein HB, Compans RW (1992). "Sulfation of the human immunodeficiency virus envelope glycoprotein.". J. Virol. 66 (12): 6953-9. PMID 1433500.