PubMed:10984485
Annnotations
GlyCosmos6-Glycan-Motif-Image
Id | Subject | Object | Predicate | Lexical cue | image |
---|---|---|---|---|---|
T1 | 25-49 | Glycan_Motif | denotes | N-acetyl-D-galactosamine | https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G61418DU |
sentences
Id | Subject | Object | Predicate | Lexical cue |
---|---|---|---|---|
T1 | 0-139 | Sentence | denotes | The lectin domain of UDP-N-acetyl-D-galactosamine: polypeptide N-acetylgalactosaminyltransferase-T4 directs its glycopeptide specificities. |
T2 | 140-316 | Sentence | denotes | The initiation step of mucin-type O-glycosylation is controlled by a large family of homologous UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferases (GalNAc-transferases). |
T3 | 317-498 | Sentence | denotes | Differences in kinetic properties, substrate specificities, and expression patterns of these isoenzymes provide for differential regulation of O-glycan attachment sites and density. |
T4 | 499-706 | Sentence | denotes | Recently, it has emerged that some GalNAc-transferase isoforms in vitro selectively function with partially GalNAc O-glycosylated acceptor peptides rather than with the corresponding unglycosylated peptides. |
T5 | 707-871 | Sentence | denotes | O-Glycan attachment to selected sites, most notably two sites in the MUC1 tandem repeat, is entirely dependent on the glycosylation-dependent function of GalNAc-T4. |
T6 | 872-1030 | Sentence | denotes | Here we present data that a putative lectin domain found in the C terminus of GalNAc-T4 functions as a GalNAc lectin and confers its glycopeptide specificity. |
T7 | 1031-1244 | Sentence | denotes | A single amino acid substitution in the lectin domain of a secreted form of GalNAc-T4 selectively blocked GalNAc-glycopeptide activity, while the general activity to peptides exerted by this enzyme was unaffected. |
T8 | 1245-1413 | Sentence | denotes | Furthermore, the GalNAc-glycopeptide activity of wild-type secreted GalNAc-T4 was selectively inhibited by free GalNAc, while the activity with peptides was unaffected. |
GlyCosmos6-Glycan-Motif-Structure
Id | Subject | Object | Predicate | Lexical cue |
---|---|---|---|---|
T1 | 25-49 | https://glytoucan.org/Structures/Glycans/G61418DU | denotes | N-acetyl-D-galactosamine |
Glycan-GlyCosmos
Id | Subject | Object | Predicate | Lexical cue | image |
---|---|---|---|---|---|
T1 | 295-301 | Glycan | denotes | GalNAc | https://api.glycosmos.org/wurcs2image/latest/png/binary/G39738WL |
T2 | 534-540 | Glycan | denotes | GalNAc | https://api.glycosmos.org/wurcs2image/latest/png/binary/G39738WL |
T3 | 607-613 | Glycan | denotes | GalNAc | https://api.glycosmos.org/wurcs2image/latest/png/binary/G39738WL |
T4 | 861-867 | Glycan | denotes | GalNAc | https://api.glycosmos.org/wurcs2image/latest/png/binary/G39738WL |
T5 | 950-956 | Glycan | denotes | GalNAc | https://api.glycosmos.org/wurcs2image/latest/png/binary/G39738WL |
T6 | 975-981 | Glycan | denotes | GalNAc | https://api.glycosmos.org/wurcs2image/latest/png/binary/G39738WL |
T7 | 1107-1113 | Glycan | denotes | GalNAc | https://api.glycosmos.org/wurcs2image/latest/png/binary/G39738WL |
T8 | 1137-1143 | Glycan | denotes | GalNAc | https://api.glycosmos.org/wurcs2image/latest/png/binary/G39738WL |
T9 | 1262-1268 | Glycan | denotes | GalNAc | https://api.glycosmos.org/wurcs2image/latest/png/binary/G39738WL |
T10 | 1313-1319 | Glycan | denotes | GalNAc | https://api.glycosmos.org/wurcs2image/latest/png/binary/G39738WL |
T11 | 1357-1363 | Glycan | denotes | GalNAc | https://api.glycosmos.org/wurcs2image/latest/png/binary/G39738WL |
GlyCosmos15-UBERON
Id | Subject | Object | Predicate | Lexical cue | uberon_id |
---|---|---|---|---|---|
T1 | 469-485 | Body_part | denotes | attachment sites | http://purl.obolibrary.org/obo/UBERON_4200047 |
sentences
Id | Subject | Object | Predicate | Lexical cue |
---|---|---|---|---|
T1 | 0-139 | Sentence | denotes | The lectin domain of UDP-N-acetyl-D-galactosamine: polypeptide N-acetylgalactosaminyltransferase-T4 directs its glycopeptide specificities. |
T2 | 140-316 | Sentence | denotes | The initiation step of mucin-type O-glycosylation is controlled by a large family of homologous UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferases (GalNAc-transferases). |
T3 | 317-498 | Sentence | denotes | Differences in kinetic properties, substrate specificities, and expression patterns of these isoenzymes provide for differential regulation of O-glycan attachment sites and density. |
T4 | 499-706 | Sentence | denotes | Recently, it has emerged that some GalNAc-transferase isoforms in vitro selectively function with partially GalNAc O-glycosylated acceptor peptides rather than with the corresponding unglycosylated peptides. |
T5 | 707-871 | Sentence | denotes | O-Glycan attachment to selected sites, most notably two sites in the MUC1 tandem repeat, is entirely dependent on the glycosylation-dependent function of GalNAc-T4. |
T6 | 872-1030 | Sentence | denotes | Here we present data that a putative lectin domain found in the C terminus of GalNAc-T4 functions as a GalNAc lectin and confers its glycopeptide specificity. |
T7 | 1031-1244 | Sentence | denotes | A single amino acid substitution in the lectin domain of a secreted form of GalNAc-T4 selectively blocked GalNAc-glycopeptide activity, while the general activity to peptides exerted by this enzyme was unaffected. |
T8 | 1245-1413 | Sentence | denotes | Furthermore, the GalNAc-glycopeptide activity of wild-type secreted GalNAc-T4 was selectively inhibited by free GalNAc, while the activity with peptides was unaffected. |
GlyCosmos15-Sentences
Id | Subject | Object | Predicate | Lexical cue |
---|---|---|---|---|
T1 | 0-139 | Sentence | denotes | The lectin domain of UDP-N-acetyl-D-galactosamine: polypeptide N-acetylgalactosaminyltransferase-T4 directs its glycopeptide specificities. |
T2 | 140-316 | Sentence | denotes | The initiation step of mucin-type O-glycosylation is controlled by a large family of homologous UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferases (GalNAc-transferases). |
T3 | 317-498 | Sentence | denotes | Differences in kinetic properties, substrate specificities, and expression patterns of these isoenzymes provide for differential regulation of O-glycan attachment sites and density. |
T4 | 499-706 | Sentence | denotes | Recently, it has emerged that some GalNAc-transferase isoforms in vitro selectively function with partially GalNAc O-glycosylated acceptor peptides rather than with the corresponding unglycosylated peptides. |
T5 | 707-871 | Sentence | denotes | O-Glycan attachment to selected sites, most notably two sites in the MUC1 tandem repeat, is entirely dependent on the glycosylation-dependent function of GalNAc-T4. |
T6 | 872-1030 | Sentence | denotes | Here we present data that a putative lectin domain found in the C terminus of GalNAc-T4 functions as a GalNAc lectin and confers its glycopeptide specificity. |
T7 | 1031-1244 | Sentence | denotes | A single amino acid substitution in the lectin domain of a secreted form of GalNAc-T4 selectively blocked GalNAc-glycopeptide activity, while the general activity to peptides exerted by this enzyme was unaffected. |
T8 | 1245-1413 | Sentence | denotes | Furthermore, the GalNAc-glycopeptide activity of wild-type secreted GalNAc-T4 was selectively inhibited by free GalNAc, while the activity with peptides was unaffected. |
GlyCosmos15-Glycan
Id | Subject | Object | Predicate | Lexical cue | image |
---|---|---|---|---|---|
T1 | 295-301 | Glycan | denotes | GalNAc | https://api.glycosmos.org/wurcs2image/latest/png/binary/G39738WL |
T2 | 534-540 | Glycan | denotes | GalNAc | https://api.glycosmos.org/wurcs2image/latest/png/binary/G39738WL |
T3 | 607-613 | Glycan | denotes | GalNAc | https://api.glycosmos.org/wurcs2image/latest/png/binary/G39738WL |
T4 | 861-867 | Glycan | denotes | GalNAc | https://api.glycosmos.org/wurcs2image/latest/png/binary/G39738WL |
T5 | 950-956 | Glycan | denotes | GalNAc | https://api.glycosmos.org/wurcs2image/latest/png/binary/G39738WL |
T6 | 975-981 | Glycan | denotes | GalNAc | https://api.glycosmos.org/wurcs2image/latest/png/binary/G39738WL |
T7 | 1107-1113 | Glycan | denotes | GalNAc | https://api.glycosmos.org/wurcs2image/latest/png/binary/G39738WL |
T8 | 1137-1143 | Glycan | denotes | GalNAc | https://api.glycosmos.org/wurcs2image/latest/png/binary/G39738WL |
T9 | 1262-1268 | Glycan | denotes | GalNAc | https://api.glycosmos.org/wurcs2image/latest/png/binary/G39738WL |
T10 | 1313-1319 | Glycan | denotes | GalNAc | https://api.glycosmos.org/wurcs2image/latest/png/binary/G39738WL |
T11 | 1357-1363 | Glycan | denotes | GalNAc | https://api.glycosmos.org/wurcs2image/latest/png/binary/G39738WL |
Lectin-Jamboree-Sentence
Id | Subject | Object | Predicate | Lexical cue |
---|---|---|---|---|
T1 | 0-139 | Sentence | denotes | The lectin domain of UDP-N-acetyl-D-galactosamine: polypeptide N-acetylgalactosaminyltransferase-T4 directs its glycopeptide specificities. |
T2 | 140-316 | Sentence | denotes | The initiation step of mucin-type O-glycosylation is controlled by a large family of homologous UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferases (GalNAc-transferases). |
T3 | 317-498 | Sentence | denotes | Differences in kinetic properties, substrate specificities, and expression patterns of these isoenzymes provide for differential regulation of O-glycan attachment sites and density. |
T4 | 499-706 | Sentence | denotes | Recently, it has emerged that some GalNAc-transferase isoforms in vitro selectively function with partially GalNAc O-glycosylated acceptor peptides rather than with the corresponding unglycosylated peptides. |
T5 | 707-871 | Sentence | denotes | O-Glycan attachment to selected sites, most notably two sites in the MUC1 tandem repeat, is entirely dependent on the glycosylation-dependent function of GalNAc-T4. |
T6 | 872-1030 | Sentence | denotes | Here we present data that a putative lectin domain found in the C terminus of GalNAc-T4 functions as a GalNAc lectin and confers its glycopeptide specificity. |
T7 | 1031-1244 | Sentence | denotes | A single amino acid substitution in the lectin domain of a secreted form of GalNAc-T4 selectively blocked GalNAc-glycopeptide activity, while the general activity to peptides exerted by this enzyme was unaffected. |
T8 | 1245-1413 | Sentence | denotes | Furthermore, the GalNAc-glycopeptide activity of wild-type secreted GalNAc-T4 was selectively inhibited by free GalNAc, while the activity with peptides was unaffected. |
Anatomy-UBERON
Id | Subject | Object | Predicate | Lexical cue | uberon_id |
---|---|---|---|---|---|
T1 | 469-485 | Body_part | denotes | attachment sites | http://purl.obolibrary.org/obo/UBERON_4200047 |