Entry - *615133 - UDP-N-ACETYL-ALPHA-D-GALACTOSAMINE:POLYPEPTIDE N-ACETYLGALACTOSAMINYLTRANSFERASE-LIKE 5; GALNTL5 - OMIM

 
 
* 615133

UDP-N-ACETYL-ALPHA-D-GALACTOSAMINE:POLYPEPTIDE N-ACETYLGALACTOSAMINYLTRANSFERASE-LIKE 5; GALNTL5


Alternative titles; symbols

GalNAc TRANSFERASE 19; GalNAcT19


HGNC Approved Gene Symbol: GALNTL5

Cytogenetic location: 7q36.1     Genomic coordinates (GRCh38): 7:151,956,446-152,019,929 (from NCBI)


TEXT

▼ Description

Membrane-bound polypeptide N-acetylgalactosaminyltransferases (EC 2.4.1.41), such as GALNTL5, catalyze the first step in mucin-type O-glycosylation of peptides in the Golgi apparatus. These enzymes transfer N-acetylgalactosamine (GalNAc) from UDP-GalNAc to the hydroxyl group of serine or threonine in target proteins (summary by Peng et al., 2010).


▼ Cloning and Expression

Peng et al. (2010) stated that GALNTL5 contains 443 amino acids.


▼ Gene Structure

Peng et al. (2010) determined that the GALNTL5 gene contains 8 exons.


▼ Mapping

Peng et al. (2010) reported that the GALNTL5 gene maps to chromosome 7q36.2. Hartz (2013) mapped the GALNTL5 gene to chromosome 7q36.1 based on an alignment of the GALNTL5 sequence (GenBank AF440400) with the genomic sequence (GRCh37).


▼ REFERENCES

  1. Hartz, P. A. Personal Communication. Baltimore, Md. 2/27/2013.

  2. Peng, C., Togayachi, A., Kwon, Y.-D., Xie, C., Wu, G., Zou, X., Sato, T., Ito, H., Tachibana, K., Kubota, T., Noce, T., Narimatsu, H., Zhang, Y. Identification of a novel human UDP-GalNAc transferase with unique catalytic activity and expression profile. Biochem. Biophys. Res. Commun. 402: 680-686, 2010. [PubMed: 20977886, related citations] [Full Text]


Creation Date:
Patricia A. Hartz : 3/25/2013
Edit History:
mgross : 03/25/2013

* 615133

UDP-N-ACETYL-ALPHA-D-GALACTOSAMINE:POLYPEPTIDE N-ACETYLGALACTOSAMINYLTRANSFERASE-LIKE 5; GALNTL5


Alternative titles; symbols

GalNAc TRANSFERASE 19; GalNAcT19


HGNC Approved Gene Symbol: GALNTL5

Cytogenetic location: 7q36.1     Genomic coordinates (GRCh38): 7:151,956,446-152,019,929 (from NCBI)


TEXT

Description

Membrane-bound polypeptide N-acetylgalactosaminyltransferases (EC 2.4.1.41), such as GALNTL5, catalyze the first step in mucin-type O-glycosylation of peptides in the Golgi apparatus. These enzymes transfer N-acetylgalactosamine (GalNAc) from UDP-GalNAc to the hydroxyl group of serine or threonine in target proteins (summary by Peng et al., 2010).


Cloning and Expression

Peng et al. (2010) stated that GALNTL5 contains 443 amino acids.


Gene Structure

Peng et al. (2010) determined that the GALNTL5 gene contains 8 exons.


Mapping

Peng et al. (2010) reported that the GALNTL5 gene maps to chromosome 7q36.2. Hartz (2013) mapped the GALNTL5 gene to chromosome 7q36.1 based on an alignment of the GALNTL5 sequence (GenBank AF440400) with the genomic sequence (GRCh37).


REFERENCES

  1. Hartz, P. A. Personal Communication. Baltimore, Md. 2/27/2013.

  2. Peng, C., Togayachi, A., Kwon, Y.-D., Xie, C., Wu, G., Zou, X., Sato, T., Ito, H., Tachibana, K., Kubota, T., Noce, T., Narimatsu, H., Zhang, Y. Identification of a novel human UDP-GalNAc transferase with unique catalytic activity and expression profile. Biochem. Biophys. Res. Commun. 402: 680-686, 2010. [PubMed: 20977886] [Full Text: https://doi.org/10.1016/j.bbrc.2010.10.084]


Creation Date:
Patricia A. Hartz : 3/25/2013

Edit History:
mgross : 03/25/2013



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OMIM® and Online Mendelian Inheritance in Man® are registered trademarks of the Johns Hopkins University.
Copyright® 1966-2024 Johns Hopkins University.

NOTE: OMIM is intended for use primarily by physicians and other professionals concerned with genetic disorders, by genetics researchers, and by advanced students in science and medicine. While the OMIM database is open to the public, users seeking information about a personal medical or genetic condition are urged to consult with a qualified physician for diagnosis and for answers to personal questions.
OMIM® and Online Mendelian Inheritance in Man® are registered trademarks of the Johns Hopkins University.
Copyright® 1966-2024 Johns Hopkins University.
Printed: June 12, 2024