about
Macrophage migration inhibitory factorInsulin IITransformation related protein 53Fibronectin 1Serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1Serine (or cysteine) peptidase inhibitor, clade A, member 1AB cell leukemia/lymphoma 2Von Willebrand factorBreast cancer 2, early onsetSerine (or cysteine) peptidase inhibitor, clade F, member 2Heat shock protein 1 (chaperonin)Aldolase A, fructose-bisphosphateSolute carrier family 6 (neurotransmitter transporter, dopamine), member 3Low density lipoprotein receptorMyelin basic proteinCoagulation factor IIIPrion proteinCollagen, type I, alpha 1Perlecan (heparan sulfate proteoglycan 2)Selectin, lymphocyteDipeptidylpeptidase 4Elastase, neutrophil expressedCollagen, type III, alpha 1Fas (TNFRSF6)-associated via death domainMannose-binding lectin (protein C) 2Serine (or cysteine) peptidase inhibitor, clade A, member 5Annexin A2Integrin beta 1 (fibronectin receptor beta)Integrin alpha 3Cell adhesion molecule L1-likeCST3Cystatin CIntegrin beta 3ProsaposinCaspase 3FURINFurin (paired basic amino acid cleaving enzyme)Macrophage migration inhibitory factor (glycosylation-inhibiting factor)Collagen, type I, alpha 2Cartilage oligomeric matrix protein
P680
In vitro degradation of insulin-like peptide 3 by insulin-degrading enzymeMesotrypsin and caspase-14 participate in prosaposin processing: potential relevance to epidermal permeability barrier formationAffinity purification of human tissue factor: interaction of factor VII and tissue factor in detergent micellesBinding of ADAMTS13 to von Willebrand factorMatriptase-3 is a novel phylogenetically preserved membrane-anchored serine protease with broad serpin reactivityRegulation of carcinoma cell invasion by protein C inhibitor whose expression is decreased in renal cell carcinomaADAMTS-13 metalloprotease interacts with the endothelial cell-derived ultra-large von Willebrand factorDNA and RNA binding by the mitochondrial lon protease is regulated by nucleotide and protein substrateFunctional defects of a muscle-specific calpain, p94, caused by mutations associated with limb-girdle muscular dystrophy type 2ACasper is a FADD- and caspase-related inducer of apoptosisRole of the single cysteine residue, Cys 3, of human and bovine cystatin B (stefin B) in the inhibition of cysteine proteinases
P921
Q133582-3B612FE8-8534-47B9-833E-ADE433D6C34CQ14762286-2A89C9DD-4662-4F77-B079-6765E8B4C6C3Q14818136-673541C9-02D5-47C9-B5F5-F1A8B6B47A13Q14818136-CFF9F7C8-45A8-4E14-9D2D-79BD0E9A26B0Q14819493-2E4B6580-BE0C-49C7-B03C-8DB035AA96E4Q14861065-19768886-BFF8-4758-B754-8088349F7865Q14861844-B164EA45-C7BF-4674-AAEA-99C305C40757Q14863583-C732EC76-7DAB-470E-BCA2-51533DCFBBAEQ14863680-40E34101-0656-413A-9419-9B7407C48E27Q14864740-0647DF7B-746E-42DA-BB48-20524FED4466Q14864740-22AA930E-5199-4A79-8595-5B03A1AA8BFDQ14864957-4A1FF6EF-87FC-4ECD-A7F7-E1CC2CFD36ECQ14865001-7CB2BB5F-72D9-4CDD-BD1C-61D11DC9D7F0Q14865001-FBF9B9E2-FE51-4DE3-8235-C8D0B1C89460Q14865094-F4183616-C867-4ACA-9F7E-E3224688B217Q14865375-DD4FB47A-1442-4F6C-9F36-173452CB4290Q14872730-26CCC1A9-64C8-460D-83B0-CE2DFB2D85ADQ14876145-803D137A-F93A-4FB6-8A1B-69B74D12D668Q14877239-C0011B25-679B-4B88-A544-7720E3ADEE17Q14881308-EDE917F3-7FBC-4C5C-ADB6-48FDA10B5047Q14881727-1DC9FC2B-6BC2-4EB1-B265-0339B6CD4023Q14890113-F9278334-23BC-47CF-858D-369D63141E73Q14901674-369F504A-735C-4500-8EC3-F72053F31DAEQ14904807-42FE80F1-AB2C-4F19-A4EE-6428AB613D86Q14905650-6CAFB0F8-06D5-48D7-81F0-D25EA3FDB83EQ14906850-DC14279E-256F-4E23-A855-4F83E8391C2CQ14907140-3337309A-8E84-4244-B7E6-32E3D0BC5892Q14907668-416DD4D4-8A12-44D8-9811-1635702D6FE0Q14907929-FA6FAA40-F668-4151-83E9-C1241086289CQ14908237-CDE8AE25-7B46-432F-A74D-EE7A562A6024Q14908237-F86C9C91-8248-476D-8F5E-BBB1E3E26492Q14912087-0A0A34F2-72FB-4E19-ABC7-D29440CB6596Q14912141-3E5808C7-775B-441F-A581-E6B2EF882DB9Q14912971-3F3CFBF6-C45C-4464-ACCB-C5B868B499A8Q14913588-CEEC0FDD-B371-428E-A7DD-CC333A5D27D2Q14913600-5A449871-5BF0-435D-85C4-FEA22134B7ADQ14913600-95D11B69-9414-465D-BFD9-F47EDED5ED56Q14913644-E1D91626-B81E-4132-855B-658B49A69B7DQ14914245-1E879A09-3772-4B7A-AEB8-F310EBEAAADAQ14914375-CCEBF9B9-B2B9-4F36-89B3-0295E8AE991D
P680
Q24296243-3FC0A527-1336-48EE-9B09-FB261EDE63AFQ24298476-EACEA73D-38E9-4A7C-B83C-26D52D0B394DQ24298644-A5E6A113-D423-4296-B432-C98934F2C17FQ24299876-5D278540-D96A-4E61-A12D-A02F5A184307Q24300747-81640705-FAE7-44E0-9032-10105FA292C7Q24303401-98BD11BF-6763-4A78-99A6-DAC432A3A941Q24303587-DF71C443-A3D8-444D-AC96-384C78E11D3FQ24305946-B50F858B-E146-4AFA-A55B-7ADA99512423Q24310208-33AF8BA6-9114-4F05-9CE7-E89BD13B2573Q24315042-878AD4FF-CE5A-4431-84FF-CFB6E05EA235Q24644675-0B6F13D4-2850-4E38-8DE7-995C142647B2
P921
description
Interacting selectively and non-covalently with any protease or peptidase.
@en
moleculaire functie
@nl
name
liaison de protéase
@fr
protease binding
@en
proteasebinding
@nn
unió de proteasa
@ca
type
label
liaison de protéase
@fr
protease binding
@en
proteasebinding
@nn
unió de proteasa
@ca
altLabel
GO:0002020
@en
prefLabel
liaison de protéase
@fr
protease binding
@en
proteasebinding
@nn
unió de proteasa
@ca
P279
P2888
P686
GO:0002020