9BGF
Structure of human GlcNAc-1-phosphotransferase complexed with the donor substrate UDP-GlcNAc
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000139 | cellular_component | Golgi membrane |
A | 0003976 | molecular_function | UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity |
A | 0005515 | molecular_function | protein binding |
A | 0005794 | cellular_component | Golgi apparatus |
A | 0007040 | biological_process | lysosome organization |
A | 0009306 | biological_process | protein secretion |
A | 0015031 | biological_process | protein transport |
A | 0016020 | cellular_component | membrane |
A | 0016256 | biological_process | N-glycan processing to lysosome |
A | 0016740 | molecular_function | transferase activity |
A | 0033299 | biological_process | secretion of lysosomal enzymes |
A | 0046835 | biological_process | carbohydrate phosphorylation |
A | 0046872 | molecular_function | metal ion binding |
A | 0051649 | biological_process | establishment of localization in cell |
B | 0000139 | cellular_component | Golgi membrane |
B | 0003976 | molecular_function | UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity |
B | 0005515 | molecular_function | protein binding |
B | 0005794 | cellular_component | Golgi apparatus |
B | 0007040 | biological_process | lysosome organization |
B | 0009306 | biological_process | protein secretion |
B | 0015031 | biological_process | protein transport |
B | 0016020 | cellular_component | membrane |
B | 0016256 | biological_process | N-glycan processing to lysosome |
B | 0016740 | molecular_function | transferase activity |
B | 0033299 | biological_process | secretion of lysosomal enzymes |
B | 0046835 | biological_process | carbohydrate phosphorylation |
B | 0046872 | molecular_function | metal ion binding |
B | 0051649 | biological_process | establishment of localization in cell |
Functional Information from PROSITE/UniProt
site_id | PS00018 |
Number of Residues | 13 |
Details | EF_HAND_1 EF-hand calcium-binding domain. DTDQSGVLSdrEI |
Chain | Residue | Details |
A | ASP1018-ILE1030 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00525 |
Chain | Residue | Details |
A | ASP449 | |
B | ASP516 | |
B | ASP531 | |
B | ASP534 | |
A | ASP464 | |
A | ASP467 | |
A | ASP516 | |
A | ASP531 | |
A | ASP534 | |
B | ASP449 | |
B | ASP464 | |
B | ASP467 |
site_id | SWS_FT_FI2 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00448 |
Chain | Residue | Details |
A | ASP1018 | |
A | ASP1020 | |
A | SER1022 | |
A | GLU1029 | |
B | ASP1018 | |
B | ASP1020 | |
B | SER1022 | |
B | GLU1029 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | SITE: Cleavage; by MBTPS1 |
Chain | Residue | Details |
A | ARG928 | |
B | ARG928 |
site_id | SWS_FT_FI4 |
Number of Residues | 20 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
Chain | Residue | Details |
A | ASN83 | |
A | ASN1129 | |
B | ASN83 | |
B | ASN114 | |
B | ASN148 | |
B | ASN179 | |
B | ASN250 | |
B | ASN614 | |
B | ASN729 | |
B | ASN829 | |
B | ASN1009 | |
A | ASN114 | |
B | ASN1129 | |
A | ASN148 | |
A | ASN179 | |
A | ASN250 | |
A | ASN614 | |
A | ASN729 | |
A | ASN829 | |
A | ASN1009 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218 |
Chain | Residue | Details |
A | ASN699 | |
B | ASN699 |