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Gene Review:

GGTA1P - glycoprotein, alpha-galactosyltransferase...

Homo sapiens

Synonyms: GGTA, GGTA1, GLYT2, Glycoprotein alpha-galactosyltransferase 1 pseudogene, Inactive N-acetyllactosaminide alpha-1,3-galactosyltransferase, ...

Ponce, J. et al., Shaper, N.L. et al., Koike, C. et al., Ebihara, S. et al., Jamra, R.A. et al.

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Psychiatry related information on GGTA1

No association between genetic variants at the GLYT2 gene and bipolar affective disorder and schizophrenia [1].

High impact information on GGTA1

Here, we question the primacy of this immune defense hypothesis with results that elucidate the evolutionary history of GGTA1 gene and pseudogene loci [2].
Transmembrane domain III plays an important role in ion binding and permeation in the glycine transporter GLYT2 [3].
The neuronal glycine transporter GLYT2 takes up glycine from the extracellular space by an electrogenic process where this neurotransmitter is co-transported with sodium and chloride ions [3].
We have now established that the former sequence (GGTA1P) is localized to 12q14-q15 and the latter sequence (GGTA1) is localized to 9q33-q34 [corrected] [4].

Biological context of GGTA1

Assignment of two human alpha-1,3-galactosyltransferase gene sequences (GGTA1 and GGTA1P) to chromosomes 9q33-q34 and 12q14-q15 [4].

Analytical, diagnostic and therapeutic context of GGTA1

These data will be useful for investigating the function of GLYT2 proteins and glycinergic neurons by gene targeting experiments [5].

References

No association between genetic variants at the GLYT2 gene and bipolar affective disorder and schizophrenia. Jamra, R.A., Villela, A.W., Klein, K., Becker, T., Schulze, T.G., Schmael, C., Deschner, M., Klopp, N., Illig, T., Propping, P., Cichon, S., Rietschel, M., Nöthen, M.M., Schumacher, J. Psychiatr. Genet. (2006) [Pubmed]
Functionally important glycosyltransferase gain and loss during catarrhine primate emergence. Koike, C., Uddin, M., Wildman, D.E., Gray, E.A., Trucco, M., Starzl, T.E., Goodman, M. Proc. Natl. Acad. Sci. U.S.A. (2007) [Pubmed]
Transmembrane domain III plays an important role in ion binding and permeation in the glycine transporter GLYT2. Ponce, J., Biton, B., Benavides, J., Avenet, P., Aragon, C. J. Biol. Chem. (2000) [Pubmed]
Assignment of two human alpha-1,3-galactosyltransferase gene sequences (GGTA1 and GGTA1P) to chromosomes 9q33-q34 and 12q14-q15. Shaper, N.L., Lin, S.P., Joziasse, D.H., Kim, D.Y., Yang-Feng, T.L. Genomics (1992) [Pubmed]
Gene structure and alternative splicing of the mouse glycine transporter type-2. Ebihara, S., Yamamoto, T., Obata, K., Yanagawa, Y. Biochem. Biophys. Res. Commun. (2004) [Pubmed]

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