4FYQ
Human aminopeptidase N (CD13)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0001525 | biological_process | angiogenesis |
| A | 0001618 | molecular_function | virus receptor activity |
| A | 0004177 | molecular_function | aminopeptidase activity |
| A | 0005615 | cellular_component | extracellular space |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005765 | cellular_component | lysosomal membrane |
| A | 0005793 | cellular_component | endoplasmic reticulum-Golgi intermediate compartment |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0006508 | biological_process | proteolysis |
| A | 0008237 | molecular_function | metallopeptidase activity |
| A | 0008270 | molecular_function | zinc ion binding |
| A | 0009897 | cellular_component | external side of plasma membrane |
| A | 0030154 | biological_process | cell differentiation |
| A | 0030667 | cellular_component | secretory granule membrane |
| A | 0038023 | molecular_function | signaling receptor activity |
| A | 0042277 | molecular_function | peptide binding |
| A | 0043171 | biological_process | peptide catabolic process |
| A | 0046718 | biological_process | symbiont entry into host cell |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0070006 | molecular_function | metalloaminopeptidase activity |
| A | 0070062 | cellular_component | extracellular exosome |
Functional Information from PROSITE/UniProt
| site_id | PS00142 |
| Number of Residues | 10 |
| Details | ZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. VIAHELAHQW |
| Chain | Residue | Details |
| A | VAL385-TRP394 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10095, ECO:0000269|PubMed:22932899 |
| Chain | Residue | Details |
| A | GLU389 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:22932899 |
| Chain | Residue | Details |
| A | GLY352 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 3 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:22932899, ECO:0007744|PDB:4FYQ, ECO:0007744|PDB:4FYR, ECO:0007744|PDB:4FYT |
| Chain | Residue | Details |
| A | HIS388 | |
| A | HIS392 | |
| A | GLU411 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | SITE: Transition state stabilizer => ECO:0000269|PubMed:22932899 |
| Chain | Residue | Details |
| A | TYR477 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | MOD_RES: Sulfotyrosine => ECO:0000255 |
| Chain | Residue | Details |
| A | TYR176 | |
| A | TYR419 | |
| A | TYR424 | |
| A | TYR913 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:22932899 |
| Chain | Residue | Details |
| A | ASN128 | |
| A | ASN234 | |
| A | ASN681 | |
| A | ASN818 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:15084671, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:22932899 |
| Chain | Residue | Details |
| A | ASN265 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 3 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:22932899 |
| Chain | Residue | Details |
| A | ASN319 | |
| A | ASN527 | |
| A | ASN625 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 1 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218 |
| Chain | Residue | Details |
| A | ASN573 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 1 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine |
| Chain | Residue | Details |
| A | ASN735 |
