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 | 0002003 | biological_process | angiotensin maturation |
A | 0004177 | molecular_function | aminopeptidase activity |
A | 0005615 | cellular_component | extracellular space |
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 | 0008233 | molecular_function | peptidase activity |
A | 0008237 | molecular_function | metallopeptidase activity |
A | 0008270 | molecular_function | zinc ion binding |
A | 0009897 | cellular_component | external side of plasma membrane |
A | 0016020 | cellular_component | membrane |
A | 0016285 | molecular_function | alanyl aminopeptidase activity |
A | 0016787 | molecular_function | hydrolase activity |
A | 0030154 | biological_process | cell differentiation |
A | 0030667 | cellular_component | secretory granule membrane |
A | 0038023 | molecular_function | signaling receptor activity |
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 | 7 |
Details | Region: {"description":"Necessary and sufficient to mediate interaction with HCoV-229E","evidences":[{"source":"PubMed","id":"1350662","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8887485","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU10095","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"22932899","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"22932899","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 3 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"22932899","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4FYQ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4FYR","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4FYT","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | Site: {"description":"Transition state stabilizer","evidences":[{"source":"PubMed","id":"22932899","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI6 |
Number of Residues | 4 |
Details | Modified residue: {"description":"Sulfotyrosine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI7 |
Number of Residues | 4 |
Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22932899","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI8 |
Number of Residues | 1 |
Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"15084671","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22932899","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI9 |
Number of Residues | 3 |
Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"22932899","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI10 |
Number of Residues | 1 |
Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI11 |
Number of Residues | 1 |
Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine"} |
Chain | Residue | Details |