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GlycoBiology-FMA

Id Subject Object Predicate Lexical cue
_T1 28-35 FMAID:67257 denotes protein
_T2 28-35 FMAID:165447 denotes protein
_T3 254-261 FMAID:67257 denotes protein
_T4 254-261 FMAID:165447 denotes protein
_T5 377-390 FMAID:167256 denotes glycoproteins
_T6 377-390 FMAID:62925 denotes glycoproteins
_T7 398-405 FMAID:67257 denotes Protein
_T8 398-405 FMAID:165447 denotes Protein
_T9 592-602 FMAID:196728 denotes amino acid
_T10 592-602 FMAID:82739 denotes amino acid
_T11 603-614 FMAID:146309 denotes composition
_T12 603-614 FMAID:50603 denotes composition
_T13 641-652 FMAID:82750 denotes asparagines
_T14 641-652 FMAID:196739 denotes asparagines
_T15 723-733 FMAID:82750 denotes asparagine
_T16 723-733 FMAID:196739 denotes asparagine
_T17 738-747 FMAID:82765 denotes threonine
_T18 738-747 FMAID:196754 denotes threonine
_T19 789-799 FMAID:82750 denotes asparagine
_T20 789-799 FMAID:196739 denotes asparagine
_T21 1016-1023 FMAID:67257 denotes protein
_T22 1016-1023 FMAID:165447 denotes protein
_T23 1024-1031 FMAID:50594 denotes surface
_T24 1024-1031 FMAID:146300 denotes surface
_T25 1134-1142 FMAID:50594 denotes surfaces
_T26 1134-1142 FMAID:146300 denotes surfaces
_T27 1151-1155 FMAID:179288 denotes deep
_T28 1151-1155 FMAID:74551 denotes deep
_T29 1156-1164 FMAID:211293 denotes recesses
_T30 1188-1195 FMAID:180723 denotes grooves
_T31 1188-1195 FMAID:75037 denotes grooves
_T32 1275-1285 FMAID:82750 denotes asparagine
_T33 1275-1285 FMAID:196739 denotes asparagine
_T34 1347-1358 FMAID:196728 denotes amino acids
_T35 1347-1358 FMAID:82739 denotes amino acids
_T36 1467-1474 FMAID:50594 denotes surface
_T37 1467-1474 FMAID:146300 denotes surface
_T38 1485-1492 FMAID:165447 denotes protein
_T39 1485-1492 FMAID:67257 denotes protein
_T40 1669-1676 FMAID:165447 denotes protein
_T41 1669-1676 FMAID:67257 denotes protein
_T42 1696-1708 FMAID:179750 denotes and regional
_T43 1728-1735 FMAID:67257 denotes protein
_T44 1728-1735 FMAID:165447 denotes protein
_T45 1757-1764 FMAID:67257 denotes protein
_T46 1757-1764 FMAID:165447 denotes protein
_T47 1837-1852 FMAID:165911 denotes folded proteins
_T48 1837-1852 FMAID:62376 denotes folded proteins
_T49 1844-1852 FMAID:67257 denotes proteins
_T50 1844-1852 FMAID:165447 denotes proteins

GlycoBiology-NCBITAXON

Id Subject Object Predicate Lexical cue
T1 903-910 http://purl.bioontology.org/ontology/STY/T033 denotes finding
T2 1032-1040 http://purl.bioontology.org/ontology/NCBITAXON/1369226 denotes geometry
T3 1643-1651 http://purl.bioontology.org/ontology/NCBITAXON/353209 denotes relation
T4 1655-1665 http://purl.bioontology.org/ontology/NCBITAXON/127244 denotes mechanisms

sentences

Id Subject Object Predicate Lexical cue
TextSentencer_T1 0-125 Sentence denotes Statistical analysis of the protein environment of N-glycosylation sites: implications for occupancy, structure, and folding.
TextSentencer_T2 126-210 Sentence denotes We recently reported statistical analysis of structural data on glycosidic linkages.
TextSentencer_T3 211-360 Sentence denotes Here we extend this analysis to the glycan-protein linkage, and the peptide primary, secondary, and tertiary structures around N-glycosylation sites.
TextSentencer_T4 361-564 Sentence denotes We surveyed 506 glycoproteins in the Protein Data Bank crystallographic database, giving 2592 glycosylation sequons (1683 occupied) and generated a database of 626 nonredundant sequons with 386 occupied.
TextSentencer_T5 565-763 Sentence denotes Deviations in the expected amino acid composition were seen around occupied asparagines, particularly an increased occurrence of aromatic residues before the asparagine and threonine at position +2.
TextSentencer_T6 764-866 Sentence denotes Glycosylation alters the asparagine side chain torsion angle distribution and reduces its flexibility.
TextSentencer_T7 867-968 Sentence denotes There is an elevated probability of finding glycosylation sites in which secondary structure changes.
TextSentencer_T8 969-1068 Sentence denotes An 11-class taxonomy was developed to describe protein surface geometry around glycosylation sites.
TextSentencer_T9 1069-1230 Sentence denotes Thirty-three percent of the occupied sites are on exposed convex surfaces, 10% in deep recesses and 20% on the edge of grooves with the glycan filling the cleft.
TextSentencer_T10 1231-1320 Sentence denotes A surprisingly large number of glycosylated asparagine residues have a low accessibility.
TextSentencer_T11 1321-1498 Sentence denotes The incidence of aromatic amino acids brought into close contact with the glycan by the folding process is higher than their normal levels on the surface or in the protein core.
TextSentencer_T12 1499-1744 Sentence denotes These data have significant implications for control of sequon occupancy and evolutionary selection of glycosylation sites and are discussed in relation to mechanisms of protein fold stabilization and regional quality control of protein folding.
TextSentencer_T13 1745-1922 Sentence denotes Hydrophobic protein-glycan interactions and the low accessibility of glycosylation sites in folded proteins are common features and may be critical in mediating these functions.
T1 0-125 Sentence denotes Statistical analysis of the protein environment of N-glycosylation sites: implications for occupancy, structure, and folding.
T2 126-210 Sentence denotes We recently reported statistical analysis of structural data on glycosidic linkages.
T3 211-360 Sentence denotes Here we extend this analysis to the glycan-protein linkage, and the peptide primary, secondary, and tertiary structures around N-glycosylation sites.
T4 361-564 Sentence denotes We surveyed 506 glycoproteins in the Protein Data Bank crystallographic database, giving 2592 glycosylation sequons (1683 occupied) and generated a database of 626 nonredundant sequons with 386 occupied.
T5 565-763 Sentence denotes Deviations in the expected amino acid composition were seen around occupied asparagines, particularly an increased occurrence of aromatic residues before the asparagine and threonine at position +2.
T6 764-866 Sentence denotes Glycosylation alters the asparagine side chain torsion angle distribution and reduces its flexibility.
T7 867-968 Sentence denotes There is an elevated probability of finding glycosylation sites in which secondary structure changes.
T8 969-1068 Sentence denotes An 11-class taxonomy was developed to describe protein surface geometry around glycosylation sites.
T9 1069-1230 Sentence denotes Thirty-three percent of the occupied sites are on exposed convex surfaces, 10% in deep recesses and 20% on the edge of grooves with the glycan filling the cleft.
T10 1231-1320 Sentence denotes A surprisingly large number of glycosylated asparagine residues have a low accessibility.
T11 1321-1498 Sentence denotes The incidence of aromatic amino acids brought into close contact with the glycan by the folding process is higher than their normal levels on the surface or in the protein core.
T12 1499-1744 Sentence denotes These data have significant implications for control of sequon occupancy and evolutionary selection of glycosylation sites and are discussed in relation to mechanisms of protein fold stabilization and regional quality control of protein folding.
T13 1745-1922 Sentence denotes Hydrophobic protein-glycan interactions and the low accessibility of glycosylation sites in folded proteins are common features and may be critical in mediating these functions.
T1 0-125 Sentence denotes Statistical analysis of the protein environment of N-glycosylation sites: implications for occupancy, structure, and folding.
T2 126-210 Sentence denotes We recently reported statistical analysis of structural data on glycosidic linkages.
T3 211-360 Sentence denotes Here we extend this analysis to the glycan-protein linkage, and the peptide primary, secondary, and tertiary structures around N-glycosylation sites.
T4 361-564 Sentence denotes We surveyed 506 glycoproteins in the Protein Data Bank crystallographic database, giving 2592 glycosylation sequons (1683 occupied) and generated a database of 626 nonredundant sequons with 386 occupied.
T5 565-763 Sentence denotes Deviations in the expected amino acid composition were seen around occupied asparagines, particularly an increased occurrence of aromatic residues before the asparagine and threonine at position +2.
T6 764-866 Sentence denotes Glycosylation alters the asparagine side chain torsion angle distribution and reduces its flexibility.
T7 867-968 Sentence denotes There is an elevated probability of finding glycosylation sites in which secondary structure changes.
T8 969-1068 Sentence denotes An 11-class taxonomy was developed to describe protein surface geometry around glycosylation sites.
T9 1069-1230 Sentence denotes Thirty-three percent of the occupied sites are on exposed convex surfaces, 10% in deep recesses and 20% on the edge of grooves with the glycan filling the cleft.
T10 1231-1320 Sentence denotes A surprisingly large number of glycosylated asparagine residues have a low accessibility.
T11 1321-1498 Sentence denotes The incidence of aromatic amino acids brought into close contact with the glycan by the folding process is higher than their normal levels on the surface or in the protein core.
T12 1499-1744 Sentence denotes These data have significant implications for control of sequon occupancy and evolutionary selection of glycosylation sites and are discussed in relation to mechanisms of protein fold stabilization and regional quality control of protein folding.
T13 1745-1922 Sentence denotes Hydrophobic protein-glycan interactions and the low accessibility of glycosylation sites in folded proteins are common features and may be critical in mediating these functions.

GO-BP

Id Subject Object Predicate Lexical cue
T1 53-66 http://purl.obolibrary.org/obo/GO_0070085 denotes glycosylation
T2 340-353 http://purl.obolibrary.org/obo/GO_0070085 denotes glycosylation
T3 455-468 http://purl.obolibrary.org/obo/GO_0070085 denotes glycosylation
T4 911-924 http://purl.obolibrary.org/obo/GO_0070085 denotes glycosylation
T5 1048-1061 http://purl.obolibrary.org/obo/GO_0070085 denotes glycosylation
T6 1602-1615 http://purl.obolibrary.org/obo/GO_0070085 denotes glycosylation
T7 764-777 http://purl.obolibrary.org/obo/GO_0070085 denotes Glycosylation
T8 1262-1274 http://purl.obolibrary.org/obo/GO_0070085 denotes glycosylated
T9 994-1003 http://purl.obolibrary.org/obo/GO_0032502 denotes developed
T10 1338-1358 http://purl.obolibrary.org/obo/GO_0015801 denotes aromatic amino acids
T11 1669-1681 http://purl.obolibrary.org/obo/GO_0006457 denotes protein fold
T12 1728-1743 http://purl.obolibrary.org/obo/GO_0006457 denotes protein folding
T13 1837-1852 http://purl.obolibrary.org/obo/GO_0006457 denotes folded proteins

GO-CC

Id Subject Object Predicate Lexical cue
T1 1188-1195 http://purl.obolibrary.org/obo/GO_0097610 denotes grooves
T2 1493-1497 http://purl.obolibrary.org/obo/GO_0019013 denotes core

EDAM-topics

Id Subject Object Predicate Lexical cue
T1 0-11 http://edamontology.org/topic_2269 denotes Statistical
T2 28-35 http://edamontology.org/topic_0078 denotes protein
T3 147-158 http://edamontology.org/topic_2269 denotes statistical
T4 171-186 http://edamontology.org/topic_3038 denotes structural data
T5 171-186 http://edamontology.org/topic_0081 denotes structural data
T6 201-209 http://edamontology.org/topic_0102 denotes linkages
T7 254-261 http://edamontology.org/topic_0078 denotes protein
T8 262-269 http://edamontology.org/topic_0102 denotes linkage
T9 279-286 http://edamontology.org/topic_0154 denotes peptide
T10 398-405 http://edamontology.org/topic_0078 denotes Protein
T11 398-410 http://edamontology.org/topic_2225 denotes Protein Data
T12 398-410 http://edamontology.org/topic_0078 denotes Protein Data
T13 416-432 http://edamontology.org/topic_2828 denotes crystallographic
T14 433-441 http://edamontology.org/topic_3489 denotes database
T15 497-517 http://edamontology.org/topic_2816 denotes generated a database
T16 509-517 http://edamontology.org/topic_3489 denotes database
T17 592-602 http://edamontology.org/topic_0154 denotes amino acid
T18 888-899 http://edamontology.org/topic_2269 denotes probability
T19 940-959 http://edamontology.org/topic_3542 denotes secondary structure
T20 940-959 http://edamontology.org/topic_0694 denotes secondary structure
T21 981-989 http://edamontology.org/topic_0637 denotes taxonomy
T22 1016-1023 http://edamontology.org/topic_0078 denotes protein
T23 1016-1031 http://edamontology.org/topic_0166 denotes protein surface
T24 1347-1358 http://edamontology.org/topic_0154 denotes amino acids
T25 1485-1492 http://edamontology.org/topic_0078 denotes protein
T26 1669-1676 http://edamontology.org/topic_0078 denotes protein
T27 1669-1681 http://edamontology.org/topic_0130 denotes protein fold
T28 1669-1681 http://edamontology.org/topic_0736 denotes protein fold
T29 1669-1695 http://edamontology.org/topic_0130 denotes protein fold stabilization
T30 1728-1735 http://edamontology.org/topic_0078 denotes protein
T31 1728-1743 http://edamontology.org/topic_0130 denotes protein folding
T32 1728-1743 http://edamontology.org/topic_0736 denotes protein folding
T33 1757-1764 http://edamontology.org/topic_0078 denotes protein
T34 1757-1784 http://edamontology.org/topic_0128 denotes protein-glycan interactions
T35 1772-1784 http://edamontology.org/topic_0602 denotes interactions
T36 1844-1852 http://edamontology.org/topic_0078 denotes proteins

EDAM-DFO

Id Subject Object Predicate Lexical cue
T1 0-11 http://edamontology.org/operation_2238 denotes Statistical
T2 0-20 http://edamontology.org/operation_2238 denotes Statistical analysis
T3 12-20 http://edamontology.org/operation_2945 denotes analysis
T4 28-35 http://edamontology.org/format_1208 denotes protein
T5 28-35 http://edamontology.org/data_1467 denotes protein
T6 102-111 http://edamontology.org/data_0883 denotes structure
T7 138-146 http://edamontology.org/data_2048 denotes reported
T8 147-158 http://edamontology.org/operation_2238 denotes statistical
T9 147-167 http://edamontology.org/operation_2238 denotes statistical analysis
T10 159-167 http://edamontology.org/operation_2945 denotes analysis
T11 171-181 http://edamontology.org/data_0883 denotes structural
T12 171-186 http://edamontology.org/data_2053 denotes structural data
T13 171-186 http://edamontology.org/data_0883 denotes structural data
T14 182-186 http://edamontology.org/data_0006 denotes data
T15 231-239 http://edamontology.org/operation_2945 denotes analysis
T16 254-261 http://edamontology.org/format_1208 denotes protein
T17 254-261 http://edamontology.org/data_1467 denotes protein
T18 279-286 http://edamontology.org/data_2906 denotes peptide
T19 311-330 http://edamontology.org/format_2033 denotes tertiary structures
T20 311-330 http://edamontology.org/data_0884 denotes tertiary structures
T21 320-330 http://edamontology.org/data_0883 denotes structures
T22 398-405 http://edamontology.org/data_1467 denotes Protein
T23 398-405 http://edamontology.org/format_1208 denotes Protein
T24 398-441 http://edamontology.org/data_0937 denotes Protein Data Bank crystallographic database
T25 406-410 http://edamontology.org/data_0006 denotes Data
T26 406-415 http://edamontology.org/data_2831 denotes Data Bank
T27 433-441 http://edamontology.org/data_0581 denotes database
T28 497-506 http://edamontology.org/operation_3429 denotes generated
T29 509-517 http://edamontology.org/data_0581 denotes database
T30 703-711 http://edamontology.org/data_1756 denotes residues
T31 940-959 http://edamontology.org/data_2880 denotes secondary structure
T32 940-959 http://edamontology.org/data_2366 denotes secondary structure
T33 940-959 http://edamontology.org/data_2973 denotes secondary structure
T34 940-959 http://edamontology.org/operation_2488 denotes secondary structure
T35 940-959 http://edamontology.org/operation_2482 denotes secondary structure
T36 940-959 http://edamontology.org/operation_0500 denotes secondary structure
T37 940-959 http://edamontology.org/data_0880 denotes secondary structure
T38 940-959 http://edamontology.org/data_2881 denotes secondary structure
T39 940-959 http://edamontology.org/data_2081 denotes secondary structure
T40 950-959 http://edamontology.org/data_0883 denotes structure
T41 981-989 http://edamontology.org/data_3028 denotes taxonomy
T42 1016-1023 http://edamontology.org/format_1208 denotes protein
T43 1016-1023 http://edamontology.org/data_1467 denotes protein
T44 1286-1294 http://edamontology.org/data_1756 denotes residues
T45 1417-1424 http://edamontology.org/operation_0004 denotes process
T46 1417-1424 http://edamontology.org/operation_2409 denotes process
T47 1446-1452 http://edamontology.org/operation_3435 denotes normal
T48 1485-1492 http://edamontology.org/format_1208 denotes protein
T49 1485-1492 http://edamontology.org/data_1467 denotes protein
T50 1505-1509 http://edamontology.org/data_0006 denotes data
T51 1669-1676 http://edamontology.org/data_1467 denotes protein
T52 1669-1676 http://edamontology.org/format_1208 denotes protein
T53 1709-1724 http://edamontology.org/operation_2428 denotes quality control
T54 1728-1735 http://edamontology.org/format_1208 denotes protein
T55 1728-1735 http://edamontology.org/data_1467 denotes protein
T56 1757-1764 http://edamontology.org/format_1208 denotes protein
T57 1757-1764 http://edamontology.org/data_1467 denotes protein
T58 1844-1852 http://edamontology.org/data_1467 denotes proteins
T59 1844-1852 http://edamontology.org/format_1208 denotes proteins
T60 1844-1872 http://edamontology.org/data_1277 denotes proteins are common features
T61 1864-1872 http://edamontology.org/data_1255 denotes features
T62 1912-1921 http://edamontology.org/operation_0004 denotes functions