PubMed:12507512 JSONTXT

{"project":"GGDB-2020","denotations":[{"id":"T1","span":{"begin":101,"end":111},"obj":"https://acgg.asia/db/ggdb/info/gg100"},{"id":"T2","span":{"begin":271,"end":281},"obj":"https://acgg.asia/db/ggdb/info/gg100"},{"id":"T3","span":{"begin":417,"end":426},"obj":"https://acgg.asia/db/ggdb/info/gg088"},{"id":"T4","span":{"begin":538,"end":548},"obj":"https://acgg.asia/db/ggdb/info/gg100"},{"id":"T5","span":{"begin":681,"end":691},"obj":"https://acgg.asia/db/ggdb/info/gg100"},{"id":"T6","span":{"begin":840,"end":850},"obj":"https://acgg.asia/db/ggdb/info/gg100"},{"id":"T7","span":{"begin":913,"end":923},"obj":"https://acgg.asia/db/ggdb/info/gg100"}],"text":"Cloning and characterization of a novel UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase, pp-GalNAc-T14.\nA novel member of the human UDP-N-acetyl-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase (pp-GalNAc-T) gene family was cloned and designated pp-GalNAc-T14. This type II membrane protein contains all motifs that are conserved in the pp-GalNAc-T family proteins and forms a subfamily with pp-GalNAc-T2 on the phylogenetic tree. Quantitative real time PCR analysis revealed significantly high expression of the pp-GalNAc-T14 transcript in kidney, although the transcripts were ubiquitously expressed in all tissues examined. Furthermore, the recombinant pp-GalNAc-T14 transferred GalNAc to a panel of mucin-derived peptide substrates such as Muc2, Muc5AC, Muc7, and Muc13 (-58). Our results provide evidence that pp-GalNAc-T14 is a new member of the pp-GalNAc-T family and suggest that pp-GalNAc-T14 may be involved in the O-glycosylation in kidney."}

{"project":"ggdb-test","denotations":[{"id":"T1","span":{"begin":101,"end":111},"obj":"https://acgg.asia/db/ggdb/info/gg100"},{"id":"T2","span":{"begin":271,"end":281},"obj":"https://acgg.asia/db/ggdb/info/gg100"},{"id":"T3","span":{"begin":417,"end":426},"obj":"https://acgg.asia/db/ggdb/info/gg088"},{"id":"T4","span":{"begin":538,"end":548},"obj":"https://acgg.asia/db/ggdb/info/gg100"},{"id":"T5","span":{"begin":681,"end":691},"obj":"https://acgg.asia/db/ggdb/info/gg100"},{"id":"T6","span":{"begin":840,"end":850},"obj":"https://acgg.asia/db/ggdb/info/gg100"},{"id":"T7","span":{"begin":913,"end":923},"obj":"https://acgg.asia/db/ggdb/info/gg100"}],"text":"Cloning and characterization of a novel UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase, pp-GalNAc-T14.\nA novel member of the human UDP-N-acetyl-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase (pp-GalNAc-T) gene family was cloned and designated pp-GalNAc-T14. This type II membrane protein contains all motifs that are conserved in the pp-GalNAc-T family proteins and forms a subfamily with pp-GalNAc-T2 on the phylogenetic tree. Quantitative real time PCR analysis revealed significantly high expression of the pp-GalNAc-T14 transcript in kidney, although the transcripts were ubiquitously expressed in all tissues examined. Furthermore, the recombinant pp-GalNAc-T14 transferred GalNAc to a panel of mucin-derived peptide substrates such as Muc2, Muc5AC, Muc7, and Muc13 (-58). Our results provide evidence that pp-GalNAc-T14 is a new member of the pp-GalNAc-T family and suggest that pp-GalNAc-T14 may be involved in the O-glycosylation in kidney."}

{"project":"glycogenes","denotations":[{"id":"PD-GlycoGenes20190927-B_T1","span":{"begin":40,"end":96},"obj":"https://acgg.asia/db/ggdb/info/gg095"},{"id":"PD-GlycoGenes20190927-B_T2","span":{"begin":40,"end":96},"obj":"https://acgg.asia/db/ggdb/info/gg094"},{"id":"PD-GlycoGenes20190927-B_T3","span":{"begin":40,"end":96},"obj":"https://acgg.asia/db/ggdb/info/gg093"},{"id":"PD-GlycoGenes20190927-B_T4","span":{"begin":40,"end":96},"obj":"https://acgg.asia/db/ggdb/info/gg092"},{"id":"PD-GlycoGenes20190927-B_T5","span":{"begin":40,"end":96},"obj":"https://acgg.asia/db/ggdb/info/gg091"},{"id":"PD-GlycoGenes20190927-B_T6","span":{"begin":40,"end":96},"obj":"https://acgg.asia/db/ggdb/info/gg090"},{"id":"PD-GlycoGenes20190927-B_T7","span":{"begin":40,"end":96},"obj":"https://acgg.asia/db/ggdb/info/gg089"},{"id":"PD-GlycoGenes20190927-B_T8","span":{"begin":40,"end":96},"obj":"https://acgg.asia/db/ggdb/info/gg088"},{"id":"PD-GlycoGenes20190927-B_T9","span":{"begin":40,"end":96},"obj":"https://acgg.asia/db/ggdb/info/gg087"},{"id":"PD-GlycoGenes20190927-B_T10","span":{"begin":101,"end":111},"obj":"https://acgg.asia/db/ggdb/info/gg100"},{"id":"PD-GlycoGenes20190927-B_T11","span":{"begin":220,"end":228},"obj":"https://acgg.asia/db/ggdb/info/gg104"},{"id":"PD-GlycoGenes20190927-B_T12","span":{"begin":257,"end":267},"obj":"url"},{"id":"PD-GlycoGenes20190927-B_T13","span":{"begin":271,"end":281},"obj":"https://acgg.asia/db/ggdb/info/gg100"},{"id":"PD-GlycoGenes20190927-B_T14","span":{"begin":293,"end":295},"obj":"https://acgg.asia/db/ggdb/info/gg111"},{"id":"PD-GlycoGenes20190927-B_T15","span":{"begin":362,"end":370},"obj":"https://acgg.asia/db/ggdb/info/gg104"},{"id":"PD-GlycoGenes20190927-B_T16","span":{"begin":417,"end":426},"obj":"https://acgg.asia/db/ggdb/info/gg088"},{"id":"PD-GlycoGenes20190927-B_T17","span":{"begin":538,"end":548},"obj":"https://acgg.asia/db/ggdb/info/gg100"},{"id":"PD-GlycoGenes20190927-B_T18","span":{"begin":681,"end":691},"obj":"https://acgg.asia/db/ggdb/info/gg100"},{"id":"PD-GlycoGenes20190927-B_T19","span":{"begin":840,"end":850},"obj":"https://acgg.asia/db/ggdb/info/gg100"},{"id":"PD-GlycoGenes20190927-B_T20","span":{"begin":877,"end":885},"obj":"https://acgg.asia/db/ggdb/info/gg104"},{"id":"PD-GlycoGenes20190927-B_T21","span":{"begin":913,"end":923},"obj":"https://acgg.asia/db/ggdb/info/gg100"}],"text":"Cloning and characterization of a novel UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase, pp-GalNAc-T14.\nA novel member of the human UDP-N-acetyl-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase (pp-GalNAc-T) gene family was cloned and designated pp-GalNAc-T14. This type II membrane protein contains all motifs that are conserved in the pp-GalNAc-T family proteins and forms a subfamily with pp-GalNAc-T2 on the phylogenetic tree. Quantitative real time PCR analysis revealed significantly high expression of the pp-GalNAc-T14 transcript in kidney, although the transcripts were ubiquitously expressed in all tissues examined. Furthermore, the recombinant pp-GalNAc-T14 transferred GalNAc to a panel of mucin-derived peptide substrates such as Muc2, Muc5AC, Muc7, and Muc13 (-58). Our results provide evidence that pp-GalNAc-T14 is a new member of the pp-GalNAc-T family and suggest that pp-GalNAc-T14 may be involved in the O-glycosylation in kidney."}