4EB1
Hyperstable in-frame insertion variant of antithrombin
Functional Information from GO Data
Chain | GOid | namespace | contents |
I | 0004867 | molecular_function | serine-type endopeptidase inhibitor activity |
I | 0005615 | cellular_component | extracellular space |
I | 0030193 | biological_process | regulation of blood coagulation |
L | 0002020 | molecular_function | protease binding |
L | 0004867 | molecular_function | serine-type endopeptidase inhibitor activity |
L | 0005515 | molecular_function | protein binding |
L | 0005576 | cellular_component | extracellular region |
L | 0005615 | cellular_component | extracellular space |
L | 0005788 | cellular_component | endoplasmic reticulum lumen |
L | 0005886 | cellular_component | plasma membrane |
L | 0007596 | biological_process | blood coagulation |
L | 0007599 | biological_process | hemostasis |
L | 0008201 | molecular_function | heparin binding |
L | 0030193 | biological_process | regulation of blood coagulation |
L | 0030414 | molecular_function | peptidase inhibitor activity |
L | 0031012 | cellular_component | extracellular matrix |
L | 0042802 | molecular_function | identical protein binding |
L | 0070062 | cellular_component | extracellular exosome |
L | 0072562 | cellular_component | blood microparticle |
Functional Information from PROSITE/UniProt
site_id | PS00284 |
Number of Residues | 11 |
Details | SERPIN Serpins signature. FKANRPFLVfI |
Chain | Residue | Details |
I | PHE410-ILE420 | |
L | PHE402-ILE412 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 6 |
Details | Binding site: {} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | Site: {"description":"Reactive bond","evidences":[{"source":"PubMed","id":"7238875","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"14760718","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"book","publicationDate":"1979","firstPage":"43","lastPage":"54","publisher":"Elsevier","address":"Amsterdam","bookName":"The physiological inhibitors of blood coagulation and fibrinolysis","title":"Primary structure of antithrombin-III (heparin cofactor). Partial homology between alpha-1-antitrypsin and antithrombin-III.","editors":["Collen D.","Wiman B.","Verstraete M."],"authors":["Petersen T.E.","Dudek-Wojciechowska G.","Sottrup-Jensen L.","Magnusson S."]}}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"book","publicationDate":"1979","firstPage":"43","lastPage":"54","publisher":"Elsevier","address":"Amsterdam","bookName":"The physiological inhibitors of blood coagulation and fibrinolysis","title":"Primary structure of antithrombin-III (heparin cofactor). Partial homology between alpha-1-antitrypsin and antithrombin-III.","editors":["Collen D.","Wiman B.","Verstraete M."],"authors":["Petersen T.E.","Dudek-Wojciechowska G.","Sottrup-Jensen L.","Magnusson S."]}}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | Glycosylation: {"description":"N-linked (GlcNAc...) (complex) asparagine","evidences":[{"source":"PubMed","id":"14760718","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15084671","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19838169","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"book","publicationDate":"1979","firstPage":"43","lastPage":"54","publisher":"Elsevier","address":"Amsterdam","bookName":"The physiological inhibitors of blood coagulation and fibrinolysis","title":"Primary structure of antithrombin-III (heparin cofactor). Partial homology between alpha-1-antitrypsin and antithrombin-III.","editors":["Collen D.","Wiman B.","Verstraete M."],"authors":["Petersen T.E.","Dudek-Wojciechowska G.","Sottrup-Jensen L.","Magnusson S."]}}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI6 |
Number of Residues | 2 |
Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"16263699","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"book","publicationDate":"1979","firstPage":"43","lastPage":"54","publisher":"Elsevier","address":"Amsterdam","bookName":"The physiological inhibitors of blood coagulation and fibrinolysis","title":"Primary structure of antithrombin-III (heparin cofactor). Partial homology between alpha-1-antitrypsin and antithrombin-III.","editors":["Collen D.","Wiman B.","Verstraete M."],"authors":["Petersen T.E.","Dudek-Wojciechowska G.","Sottrup-Jensen L.","Magnusson S."]}}]} |
Chain | Residue | Details |