The cleavage of GSDMD by human neutrophil lysate was inhibited by ELANE\u2011specific inhibitors in a dose\u2011dependent manner (Kambara H et al. 2018). The identified ELANE cleavage site C268 in human GSDMD is different from the caspase cleavage site D275 and is not conserved between humans and mice (Kambara H et al. 2018). The N\u2011terminal fragment of GSDMD (1\u2011268) formed oligomers and induced lytic cell death upon overexpression in human embryonic kidney HEK293 cells (Kambara H et al. 2018). High\u2011resolution total internal reflection fluorescence (TIRF) microscopy showed that after NET formation GSDMD localized to the plasma membrane in human primary neutrophils (Sollberger G et al. 2018). These data suggest that GSDMD cleavage by ELANE at D268 induces lytic cell death in neutrophils (Sollberger G et al. 2018; Kambara H et al. 2018). In addition, the N\u2011terminal fragment of GSDMD was shown to target azurophilic (primary) granules and autophagosomes in human and murine neutrophils (Karmakar M et al. 2020). In this study the N\u2011terminal fragment of GSDMD facilitated release of ELANE into the cytosol by permeabilization of azurophilic granules and secretion of IL\u20111\u03b2 via an autophagy machinery\u2011dependent pathway (Karmakar M et al. 2020).;", "cellular_location": "cytosol", "input_participant_list": [], "output_participant_list": [ "R-HSA-9710104", "R-HSA-9710116" ], "enzyme_list": [ "P08246-1" ], "evidence": [ { "id": "R-HSA-9710106", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9710106" } ] }, { "id": "R-NUL-2482182", "name": "Cleavage of collagen type VIII by ELANE", "equation": "", "summary": "Collagen type VIII is a short chain, network-forming collagen,thought to play a role in tissue remodeling and repair (Shuttleworth 1997, Weitkamp et al. 1999). There are two alpha chain subtypes, found in a ratio of two alpha-1 to one alpha-2 chains (Mann et al. 1990) in the typical collagen heterotrimer. Studies suggest that type VIII collagen is a major component of the hexagonal lattice seen in Descemet's membrane (Mann et al. 1990). Mutations in both alpha chains have been associated with Fuchs endothelial corneal dystrophy (FECD), a degenerative disease of the corneal endothelium (Jun et al. 2012).; ; Collagen type VIII can be degraded by neutrophil elastase (ELANE, ELA2; Kittelberger et al. 1992).", "cellular_location": "extracellular region", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "P08246-1" ], "evidence": [ { "id": "R-NUL-2482182", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-NUL-2482182" } ] }, { "id": "R-NUL-2533972", "name": "Nid1 degradation by MMP1, 9, 12, ELANE", "equation": "", "summary": "Nidogen-1 (entactin) is a member of the nidogen family of basement membrane glycoproteins. It interacts with several other components of basement membranes, notably it connects the collagen and laminin networks to each other (Yurchenko & Patton 2009). 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Targets", "url": "" } ] }, { "participant_id": "R-HSA-9710104", "participant_name": "GSDMD(1-268) [cytosol]", "crossref": [ { "id": "6KN0", "database": "PDB", "url": "" }, { "id": "ENSP00000482096", "database": "Ensembl", "url": "" }, { "id": "NP_079012.3", "database": "RefSeq", "url": "" }, { "id": "6VFE", "database": "PDB", "url": "" }, { "id": "ENSG00000104518", "database": "OpenTargets", "url": "" }, { "id": "ENST00000615119", "database": "Ensembl", "url": "" }, { "id": "P57764", "database": "Pharos - Targets", "url": "" }, { "id": "5WQT", "database": "PDB", "url": "" }, { "id": "ENSG00000278718", "database": "Ensembl", "url": "" }, { "id": "NP_001159709.1", "database": "RefSeq", "url": "" }, { "id": "ENSG00000104518-GSDMD", "database": "HPA", "url": "" }, { "id": "ENST00000262580", "database": "Ensembl", "url": "" }, { "id": "P57764", "database": "UniProt", "url": "" }, { "id": "5NH1", "database": "PDB", "url": "" }, { "id": "ENSP00000488012", "database": "Ensembl", "url": "" }, { "id": "ENST00000526406", "database": "Ensembl", "url": "" }, { "id": "P57764", "database": "PRO", "url": "" }, { "id": "ENSP00000262580", "database": "Ensembl", "url": "" }, { "id": "6N9O", "database": "PDB", "url": "" }, { "id": "ENSP00000433209", "database": "Ensembl", "url": "" }, { "id": "6AO4", "database": "PDB", "url": "" }, { "id": "P57764", "database": "GeneCards", "url": "" }, { "id": "ENSG00000104518", "database": "Ensembl", "url": "" }, { "id": "ENST00000631751", "database": "Ensembl", "url": "" } ] }, { "participant_id": "R-HSA-9710116", "participant_name": "GSDMD(269-484) [cytosol]", "crossref": [ { "id": "ENSG00000278718", "database": "Ensembl", "url": "" }, { "id": "5WQT", "database": "PDB", "url": "" }, { "id": "P57764", "database": "Pharos - Targets", "url": "" }, { "id": "ENST00000262580", "database": "Ensembl", "url": "" }, { "id": "NP_001159709.1", "database": "RefSeq", "url": "" }, { "id": "ENSG00000104518-GSDMD", "database": "HPA", "url": "" }, { "id": "NP_079012.3", "database": "RefSeq", "url": "" }, { "id": "ENSP00000482096", "database": "Ensembl", "url": "" }, { "id": "6KN0", "database": "PDB", "url": "" }, { "id": "6VFE", "database": "PDB", "url": "" }, { "id": "ENSG00000104518", "database": "OpenTargets", "url": "" }, { "id": "ENST00000615119", "database": "Ensembl", "url": "" }, { "id": "P57764", "database": "UniProt", "url": "" }, { "id": "5NH1", "database": "PDB", "url": "" }, { "id": "ENSP00000488012", "database": "Ensembl", "url": "" }, { "id": "ENST00000526406", "database": "Ensembl", "url": "" }, { "id": "P57764", "database": "PRO", "url": "" }, { "id": "ENSP00000262580", "database": "Ensembl", "url": "" }, { "id": "6N9O", "database": "PDB", "url": "" }, { "id": "ENSP00000433209", "database": "Ensembl", "url": "" }, { "id": "6AO4", "database": "PDB", "url": "" }, { "id": "P57764", "database": "GeneCards", "url": "" }, { "id": "ENST00000631751", "database": "Ensembl", "url": "" }, { "id": "ENSG00000104518", "database": "Ensembl", "url": "" } ] } ], "reaction_enzymes": [ { "uniprot_ac": "O00391", "gene_name": "QSOX1", "activity": [ { "ec_number": "1.8.3.2", "activity": "O2 + 2 R'C(R)SH = H2O2 + R'C(R)S-S(R)CR'.", "evidence": [ { "id": "O00391", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/O00391" } ] }, { "ec_number": "1.8.3.2", "activity": "", "evidence": [ { "id": "O00391", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/O00391" } ] } ] }, { "uniprot_ac": "O00584", "gene_name": "RNASET2", "activity": [ { "ec_number": "4.6.1.19", "activity": "a ribonucleotidyl-ribonucleotide-RNA + H2O = a 3'-end 3'-phospho-ribonucleotide-RNA + a 5'-end dephospho-ribonucleoside-RNA + H(+).", "evidence": [ { "id": "O00584", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/O00584" } ] }, { "ec_number": "4.6.1.19", "activity": "", "evidence": [ { "id": "O00584", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/O00584" } ] } ] }, { "uniprot_ac": "O00754", "gene_name": "MAN2B1", "activity": [ { "ec_number": "3.2.1.24", "activity": "Hydrolysis of terminal, non-reducing alpha-D-mannose residues in alpha-D-mannosides.", "evidence": [ { "id": "O00754", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/O00754" } ] }, { "ec_number": "3.2.1.24", "activity": "", "evidence": [ { "id": "O00754", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/O00754" } ] } ] }, { "uniprot_ac": "O00764", "gene_name": "PDXK", "activity": [ { "ec_number": "2.7.1.35", "activity": "ATP + pyridoxal = ADP + H(+) + pyridoxal 5'-phosphate.", "evidence": [ { "id": "O00764", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/O00764" } ] }, { "ec_number": "2.7.1.35", "activity": "", "evidence": [ { "id": "O00764", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/O00764" } ] } ] }, { "uniprot_ac": "P00387", "gene_name": "CYB5R3", "activity": [ { "ec_number": "1.6.2.2", "activity": "2 Fe(III)-[cytochrome b5] + NADH = 2 Fe(II)-[cytochrome b5] + H(+) + NAD(+).", "evidence": [ { "id": "P00387", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P00387" } ] }, { "ec_number": "1.6.2.2", "activity": "", "evidence": [ { "id": "P00387", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P00387" } ] } ] }, { "uniprot_ac": "P00734", "gene_name": "F2", "activity": [ { "ec_number": "3.4.21.5", "activity": "Selective cleavage of Arg-|-Gly bonds in fibrinogen to form fibrin and release fibrinopeptides A and B.", "evidence": [ { "id": "P00734", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P00734" } ] }, { "ec_number": "3.4.21.5", "activity": "", "evidence": [ { "id": "P00734", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P00734" } ] } ] }, { "uniprot_ac": "P00747", "gene_name": "PLG", "activity": [ { "ec_number": "3.4.21.7", "activity": "Preferential cleavage: Lys-|-Xaa > Arg-|-Xaa, higher selectivity than trypsin. Converts fibrin into soluble products.", "evidence": [ { "id": "P00747", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P00747" } ] }, { "ec_number": "3.4.21.7", "activity": "", "evidence": [ { "id": "P00747", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P00747" } ] } ] }, { "uniprot_ac": "P02788", "gene_name": "LTF", "activity": [ { "ec_number": "3.4.21.-", "activity": "", "evidence": [ { "id": "P02788", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P02788" } ] } ] }, { "uniprot_ac": "P03952", "gene_name": "KLKB1", "activity": [ { "ec_number": "3.4.21.34", "activity": "Cleaves selectively Arg-|-Xaa and Lys-|-Xaa bonds, including Lys-|-Arg and Arg-|-Ser bonds in (human) kininogen to release bradykinin.", "evidence": [ { "id": "P03952", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P03952" } ] }, { "ec_number": "3.4.21.34", "activity": "", "evidence": [ { "id": "P03952", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P03952" } ] } ] }, { "uniprot_ac": "P03956", "gene_name": "MMP1", "activity": [ { "ec_number": "3.4.24.7", "activity": "Cleavage of the triple helix of collagen at about three-quarters of the length of the molecule from the N-terminus, at 775-Gly-|-Ile-776 in the alpha1(I) chain. Cleaves synthetic substrates and alpha-macroglobulins at bonds where P1' is a hydrophobic residue.", "evidence": [ { "id": "P03956", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P03956" } ] }, { "ec_number": "3.4.24.7", "activity": "", "evidence": [ { "id": "P03956", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P03956" } ] } ] }, { "uniprot_ac": "P04066", "gene_name": "FUCA1", "activity": [ { "ec_number": "3.2.1.51", "activity": "an alpha-L-fucoside + H2O = an alcohol + L-fucose.", "evidence": [ { "id": "P04066", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P04066" } ] }, { "ec_number": "3.2.1.51", "activity": "", "evidence": [ { "id": "P04066", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P04066" } ] } ] }, { "uniprot_ac": "P05089", "gene_name": "ARG1", "activity": [ { "ec_number": "3.5.3.1", "activity": "H2O + L-arginine = L-ornithine + urea.", "evidence": [ { "id": "P05089", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P05089" } ] }, { "ec_number": "3.5.3.1", "activity": "", "evidence": [ { "id": "P05089", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P05089" } ] } ] }, { "uniprot_ac": "P05164", "gene_name": "MPO", "activity": [ { "ec_number": "1.11.2.2", "activity": "chloride + H(+) + H2O2 = H2O + hypochlorous acid.", "evidence": [ { "id": "P05164", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P05164" } ] }, { "ec_number": "1.11.2.2", "activity": "", "evidence": [ { "id": "P05164", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P05164" } ] } ] }, { "uniprot_ac": "P06280", "gene_name": "GLA", "activity": [ { "ec_number": "3.2.1.-", "activity": "", "evidence": [ { "id": "P06280", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P06280" } ] }, { "ec_number": "3.2.1.22", "activity": "a globoside Gb3Cer (d18:1(4E)) + H2O = a beta-D-Gal-(1->4)-beta-D-Glc-(1<->1)-Cer(d18:1(4E)) + D-galactose.", "evidence": [ { "id": "P06280", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P06280" } ] }, { "ec_number": "3.2.1.22", "activity": "", "evidence": [ { "id": "P06280", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P06280" } ] } ] }, { "uniprot_ac": "P07339", "gene_name": "CTSD", "activity": [ { "ec_number": "3.4.23.5", "activity": "Specificity similar to, but narrower than, that of pepsin A. Does not cleave the 4-Gln-|-His-5 bond in B chain of insulin.", "evidence": [ { "id": "P07339", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P07339" } ] }, { "ec_number": "3.4.23.5", "activity": "", "evidence": [ { "id": "P07339", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P07339" } ] } ] }, { "uniprot_ac": "P07477", "gene_name": "PRSS1", "activity": [ { "ec_number": "3.4.21.4", "activity": "Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa.", "evidence": [ { "id": "P07477", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P07477" } ] }, { "ec_number": "3.4.21.4", "activity": "", "evidence": [ { "id": "P07477", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P07477" } ] } ] }, { "uniprot_ac": "P07478", "gene_name": "PRSS2", "activity": [ { "ec_number": "3.4.21.4", "activity": "Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa.", "evidence": [ { "id": "P07478", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P07478" } ] }, { "ec_number": "3.4.21.4", "activity": "", "evidence": [ { "id": "P07478", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P07478" } ] } ] }, { "uniprot_ac": "P07686", "gene_name": "HEXB", "activity": [ { "ec_number": "3.2.1.52", "activity": "Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine residues in N-acetyl-beta-D-hexosaminides.", "evidence": [ { "id": "P07686", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P07686" } ] }, { "ec_number": "3.2.1.52", "activity": "", "evidence": [ { "id": "P07686", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P07686" } ] } ] }, { "uniprot_ac": "P08236", "gene_name": "GUSB", "activity": [ { "ec_number": "3.2.1.31", "activity": "a beta-D-glucuronoside + H2O = an alcohol + D-glucuronate.", "evidence": [ { "id": "P08236", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P08236" } ] }, { "ec_number": "3.2.1.31", "activity": "", "evidence": [ { "id": "P08236", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P08236" } ] } ] }, { "uniprot_ac": "P08246", "gene_name": "ELANE", "activity": [ { "ec_number": "3.4.21.37", "activity": "Hydrolysis of proteins, including elastin. Preferential cleavage: Val-|-Xaa > Ala-|-Xaa.", "evidence": [ { "id": "P08246", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P08246" } ] }, { "ec_number": "3.4.21.37", "activity": "", "evidence": [ { "id": "P08246", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P08246" } ] } ] }, { "uniprot_ac": "P08253", "gene_name": "MMP2", "activity": [ { "ec_number": "3.4.24.24", "activity": "Cleavage of gelatin type I and collagen types IV, V, VII, X. Cleaves the collagen-like sequence Pro-Gln-Gly-|-Ile-Ala-Gly-Gln.", "evidence": [ { "id": "P08253", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P08253" } ] }, { "ec_number": "3.4.24.24", "activity": "", "evidence": [ { "id": "P08253", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P08253" } ] } ] }, { "uniprot_ac": "P08254", "gene_name": "MMP3", "activity": [ { "ec_number": "3.4.24.17", "activity": "Preferential cleavage where P1', P2' and P3' are hydrophobic residues.", "evidence": [ { "id": "P08254", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P08254" } ] }, { "ec_number": "3.4.24.17", "activity": "", "evidence": [ { "id": "P08254", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P08254" } ] } ] }, { "uniprot_ac": "P08311", "gene_name": "CTSG", "activity": [ { "ec_number": "3.4.21.20", "activity": "Specificity similar to chymotrypsin C.", "evidence": [ { "id": "P08311", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P08311" } ] }, { "ec_number": "3.4.21.20", "activity": "", "evidence": [ { "id": "P08311", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P08311" } ] } ] }, { "uniprot_ac": "P09110", "gene_name": "ACAA1", "activity": [ { "ec_number": "2.3.1.9", "activity": "2 acetyl-CoA = acetoacetyl-CoA + CoA.", "evidence": [ { "id": "P09110", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P09110" } ] }, { "ec_number": "2.3.1.9", "activity": "", "evidence": [ { "id": "P09110", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P09110" } ] }, { "ec_number": "2.3.1.16", "activity": "acetyl-CoA + an acyl-CoA = a 3-oxoacyl-CoA + CoA.", "evidence": [ { "id": "P09110", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P09110" } ] }, { "ec_number": "2.3.1.155", "activity": "acetyl-CoA + tetradecanoyl-CoA = 3-oxohexadecanoyl-CoA + CoA.", "evidence": [ { "id": "P09110", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P09110" } ] }, { "ec_number": "2.3.1.16", "activity": "", "evidence": [ { "id": "P09110", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P09110" } ] } ] }, { "uniprot_ac": "P09237", "gene_name": "MMP7", "activity": [ { "ec_number": "3.4.24.23", "activity": "Cleavage of 14-Ala-|-Leu-15 and 16-Tyr-|-Leu-17 in B chain of insulin. No action on collagen types I, II, IV, V. Cleaves gelatin chain alpha2(I) > alpha1(I).", "evidence": [ { "id": "P09237", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P09237" } ] }, { "ec_number": "3.4.24.23", "activity": "", "evidence": [ { "id": "P09237", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P09237" } ] } ] }, { "uniprot_ac": "P09238", "gene_name": "MMP10", "activity": [ { "ec_number": "3.4.24.22", "activity": "Similar to stromelysin 1, but action on collagen types III, IV and V is weak.", "evidence": [ { "id": "P09238", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P09238" } ] }, { "ec_number": "3.4.24.22", "activity": "", "evidence": [ { "id": "P09238", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P09238" } ] } ] }, { "uniprot_ac": "P10153", "gene_name": "RNASE2", "activity": [ { "ec_number": "4.6.1.18", "activity": "an [RNA] containing cytidine + H2O = an [RNA]-3'-cytidine-3'-phosphate + a 5'-hydroxy-ribonucleotide-3'-[RNA].", "evidence": [ { "id": "P10153", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P10153" } ] }, { "ec_number": "4.6.1.18", "activity": "", "evidence": [ { "id": "P10153", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P10153" } ] } ] }, { "uniprot_ac": "P10619", "gene_name": "CTSA", "activity": [ { "ec_number": "3.4.16.-", "activity": "", "evidence": [ { "id": "P10619", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P10619" } ] }, { "ec_number": "3.4.16.5", "activity": "Release of a C-terminal amino acid with broad specificity.", "evidence": [ { "id": "P10619", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P10619" } ] }, { "ec_number": "3.4.16.5", "activity": "", "evidence": [ { "id": "P10619", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P10619" } ] } ] }, { "uniprot_ac": "P11216", "gene_name": "PYGB", "activity": [ { "ec_number": "2.4.1.1", "activity": "[(1->4)-alpha-D-glucosyl](n) + phosphate = [(1->4)-alpha-D-glucosyl](n-1) + alpha-D-glucose 1-phosphate.", "evidence": [ { "id": "P11216", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P11216" } ] }, { "ec_number": "2.4.1.1", "activity": "", "evidence": [ { "id": "P11216", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P11216" } ] } ] }, { "uniprot_ac": "P12724", "gene_name": "RNASE3", "activity": [ { "ec_number": "3.1.27.-", "activity": "", "evidence": [ { "id": "P12724", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P12724" } ] } ] }, { "uniprot_ac": "P14780", "gene_name": "MMP9", "activity": [ { "ec_number": "3.4.24.35", "activity": "Cleavage of gelatin types I and V and collagen types IV and V.", "evidence": [ { "id": "P14780", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P14780" } ] }, { "ec_number": "3.4.24.35", "activity": "", "evidence": [ { "id": "P14780", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P14780" } ] } ] }, { "uniprot_ac": "P15289", "gene_name": "ARSA", "activity": [ { "ec_number": "3.1.6.8", "activity": "H2O + N-acyl-1-beta-D-(3-O-sulfo)-galactosyl-sphing-4-enine = a beta-D-galactosyl-(1<->1')-N-acylsphing-4-enine + H(+) + sulfate.", "evidence": [ { "id": "P15289", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P15289" } ] }, { "ec_number": "3.1.6.8", "activity": "", "evidence": [ { "id": "P15289", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P15289" } ] } ] }, { "uniprot_ac": "P15586", "gene_name": "GNS", "activity": [ { "ec_number": "3.1.6.14", "activity": "Hydrolysis of the 6-sulfate groups of the N-acetyl-D-glucosamine 6-sulfate units of heparan sulfate and keratan sulfate.", "evidence": [ { "id": "P15586", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P15586" } ] }, { "ec_number": "3.1.6.14", "activity": "", "evidence": [ { "id": "P15586", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P15586" } ] } ] }, { "uniprot_ac": "P15848", "gene_name": "ARSB", "activity": [ { "ec_number": "3.1.6.12", "activity": "Hydrolysis of the 4-sulfate groups of the N-acetyl-D-galactosamine 4-sulfate units of chondroitin sulfate and dermatan sulfate.", "evidence": [ { "id": "P15848", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P15848" } ] }, { "ec_number": "3.1.6.12", "activity": "", "evidence": [ { "id": "P15848", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P15848" } ] } ] }, { "uniprot_ac": "P16278", "gene_name": "GLB1", "activity": [ { "ec_number": "3.2.1.23", "activity": "Hydrolysis of terminal non-reducing beta-D-galactose residues in beta-D-galactosides.", "evidence": [ { "id": "P16278", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P16278" } ] }, { "ec_number": "3.2.1.23", "activity": "", "evidence": [ { "id": "P16278", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P16278" } ] } ] }, { "uniprot_ac": "P19801", "gene_name": "AOC1", "activity": [ { "ec_number": "1.4.3.22", "activity": "H2O + histamine + O2 = H2O2 + imidazole-4-acetaldehyde + NH4(+).", "evidence": [ { "id": "P19801", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P19801" } ] }, { "ec_number": "1.4.3.22", "activity": "", "evidence": [ { "id": "P19801", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P19801" } ] }, { "ec_number": "1.4.3.-", "activity": "", "evidence": [ { "id": "P19801", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P19801" } ] } ] }, { "uniprot_ac": "P20151", "gene_name": "KLK2", "activity": [ { "ec_number": "3.4.21.35", "activity": "Preferential cleavage of Arg-|-Xaa bonds in small molecule substrates. Highly selective action to release kallidin (lysyl-bradykinin) from kininogen involves hydrolysis of Met-|-Xaa or Leu-|-Xaa.", "evidence": [ { "id": "P20151", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P20151" } ] }, { "ec_number": "3.4.21.35", "activity": "", "evidence": [ { "id": "P20151", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P20151" } ] } ] }, { "uniprot_ac": "P20839", "gene_name": "IMPDH1", "activity": [ { "ec_number": "1.1.1.205", "activity": "H2O + IMP + NAD(+) = H(+) + NADH + XMP.", "evidence": [ { "id": "P20839", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P20839" } ] }, { "ec_number": "1.1.1.205", "activity": "", "evidence": [ { "id": "P20839", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P20839" } ] } ] }, { "uniprot_ac": "P20933", "gene_name": "AGA", "activity": [ { "ec_number": "3.5.1.26", "activity": "H2O + N(4)-(beta-N-acetyl-D-glucosaminyl)-L-asparagine = H(+) + L-aspartate + N-acetyl-beta-D-glucosaminylamine.", "evidence": [ { "id": "P20933", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P20933" } ] }, { "ec_number": "3.5.1.26", "activity": "", "evidence": [ { "id": "P20933", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P20933" } ] } ] }, { "uniprot_ac": "P22894", "gene_name": "MMP8", "activity": [ { "ec_number": "3.4.24.34", "activity": "Cleavage of interstitial collagens in the triple helical domain. Unlike EC 3.4.24.7, this enzyme cleaves type III collagen more slowly than type I.", "evidence": [ { "id": "P22894", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P22894" } ] }, { "ec_number": "3.4.24.34", "activity": "", "evidence": [ { "id": "P22894", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P22894" } ] } ] }, { "uniprot_ac": "P23946", "gene_name": "CMA1", "activity": [ { "ec_number": "3.4.21.39", "activity": "Preferential cleavage: Phe-|-Xaa > Tyr-|-Xaa > Trp-|-Xaa > Leu-|-Xaa.", "evidence": [ { "id": "P23946", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P23946" } ] }, { "ec_number": "3.4.21.39", "activity": "", "evidence": [ { "id": "P23946", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P23946" } ] } ] }, { "uniprot_ac": "P24158", "gene_name": "PRTN3", "activity": [ { "ec_number": "3.4.21.76", "activity": "Hydrolysis of proteins, including elastin, by preferential cleavage: -Ala-|-Xaa- > -Val-|-Xaa-.", "evidence": [ { "id": "P24158", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P24158" } ] }, { "ec_number": "3.4.21.76", "activity": "", "evidence": [ { "id": "P24158", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P24158" } ] } ] }, { "uniprot_ac": "P28482", "gene_name": "MAPK1", "activity": [ { "ec_number": "2.7.11.24", "activity": "ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein].", "evidence": [ { "id": "P28482", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P28482" } ] }, { "ec_number": "2.7.11.24", "activity": "", "evidence": [ { "id": "P28482", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P28482" } ] } ] }, { "uniprot_ac": "P29350", "gene_name": "PTPN6", "activity": [ { "ec_number": "3.1.3.48", "activity": "H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate.", "evidence": [ { "id": "P29350", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P29350" } ] }, { "ec_number": "3.1.3.48", "activity": "", "evidence": [ { "id": "P29350", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P29350" } ] } ] }, { "uniprot_ac": "P30041", "gene_name": "PRDX6", "activity": [ { "ec_number": "1.11.1.27", "activity": "a hydroperoxide + 2 glutathione = an alcohol + glutathione disulfide + H2O.", "evidence": [ { "id": "P30041", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P30041" } ] }, { "ec_number": "3.1.1.4", "activity": "1-O-alkyl-2-acyl-sn-glycero-3-phosphocholine + H2O = 1-O-alkyl-sn-glycero-3-phosphocholine + a fatty acid + H(+).", "evidence": [ { "id": "P30041", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P30041" } ] }, { "ec_number": "2.3.1.23", "activity": "a 1-acyl-sn-glycero-3-phosphocholine + an acyl-CoA = a 1,2-diacyl-sn-glycero-3-phosphocholine + CoA.", "evidence": [ { "id": "P30041", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P30041" } ] }, { "ec_number": "1.11.1.27", "activity": "", "evidence": [ { "id": "P30041", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P30041" } ] } ] }, { "uniprot_ac": "P34059", "gene_name": "GALNS", "activity": [ { "ec_number": "3.1.6.4", "activity": "Hydrolysis of the 6-sulfate groups of the N-acetyl-D-galactosamine 6-sulfate units of chondroitin sulfate and of the D-galactose 6-sulfate units of keratan sulfate.", "evidence": [ { "id": "P34059", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P34059" } ] }, { "ec_number": "3.1.6.4", "activity": "", "evidence": [ { "id": "P34059", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P34059" } ] } ] }, { "uniprot_ac": "P39900", "gene_name": "MMP12", "activity": [ { "ec_number": "3.4.24.65", "activity": "Hydrolysis of soluble and insoluble elastin. Specific cleavages are also produced at 14-Ala-|-Leu-15 and 16-Tyr-|-Leu-17 in the B chain of insulin.", "evidence": [ { "id": "P39900", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P39900" } ] }, { "ec_number": "3.4.24.65", "activity": "", "evidence": [ { "id": "P39900", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P39900" } ] } ] }, { "uniprot_ac": "P42685", "gene_name": "FRK", "activity": [ { "ec_number": "2.7.10.2", "activity": "ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein].", "evidence": [ { "id": "P42685", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P42685" } ] }, { "ec_number": "2.7.10.2", "activity": "", "evidence": [ { "id": "P42685", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P42685" } ] } ] }, { "uniprot_ac": "P49184", "gene_name": "DNASE1L1", "activity": [ { "ec_number": "3.1.21.-", "activity": "", "evidence": [ { "id": "P49184", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P49184" } ] } ] }, { "uniprot_ac": "P51159", "gene_name": "RAB27A", "activity": [ { "ec_number": "3.6.5.2", "activity": "GTP + H2O = GDP + H(+) + phosphate.", "evidence": [ { "id": "P51159", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P51159" } ] }, { "ec_number": "3.6.5.2", "activity": "", "evidence": [ { "id": "P51159", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P51159" } ] } ] }, { "uniprot_ac": "P53396", "gene_name": "ACLY", "activity": [ { "ec_number": "2.3.3.8", "activity": "acetyl-CoA + ADP + oxaloacetate + phosphate = ATP + citrate + CoA.", "evidence": [ { "id": "P53396", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P53396" } ] }, { "ec_number": "2.3.3.8", "activity": "", "evidence": [ { "id": "P53396", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P53396" } ] } ] }, { "uniprot_ac": "P53634", "gene_name": "CTSC", "activity": [ { "ec_number": "3.4.14.1", "activity": "Release of an N-terminal dipeptide, Xaa-Yaa-|-Zaa-, except when Xaa is Arg or Lys, or Yaa or Zaa is Pro.", "evidence": [ { "id": "P53634", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P53634" } ] }, { "ec_number": "3.4.14.1", "activity": "", "evidence": [ { "id": "P53634", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P53634" } ] } ] }, { "uniprot_ac": "P55072", "gene_name": "VCP", "activity": [ { "ec_number": "3.6.4.6", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "P55072", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P55072" } ] }, { "ec_number": "3.6.4.6", "activity": "", "evidence": [ { "id": "P55072", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P55072" } ] } ] }, { "uniprot_ac": "P61626", "gene_name": "LYZ", "activity": [ { "ec_number": "3.2.1.17", "activity": "Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrins.", "evidence": [ { "id": "P61626", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P61626" } ] }, { "ec_number": "3.2.1.17", "activity": "", "evidence": [ { "id": "P61626", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P61626" } ] } ] }, { "uniprot_ac": "Q05655", "gene_name": "PRKCD", "activity": [ { "ec_number": "2.7.10.2", "activity": "ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein].", "evidence": [ { "id": "Q05655", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q05655" } ] }, { "ec_number": "2.7.11.13", "activity": "ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein].", "evidence": [ { "id": "Q05655", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q05655" } ] }, { "ec_number": "2.7.11.13", "activity": "", "evidence": [ { "id": "Q05655", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q05655" } ] } ] }, { "uniprot_ac": "Q13231", "gene_name": "CHIT1", "activity": [ { "ec_number": "3.2.1.14", "activity": "Random endo-hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins.", "evidence": [ { "id": "Q13231", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q13231" } ] }, { "ec_number": "3.2.1.14", "activity": "", "evidence": [ { "id": "Q13231", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q13231" } ] } ] }, { "uniprot_ac": "Q15661", "gene_name": "TPSAB1", "activity": [ { "ec_number": "3.4.21.59", "activity": "Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa, but with more restricted specificity than trypsin.", "evidence": [ { "id": "Q15661", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q15661" } ] }, { "ec_number": "3.4.21.59", "activity": "", "evidence": [ { "id": "Q15661", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q15661" } ] } ] }, { "uniprot_ac": "Q16769", "gene_name": "QPCT", "activity": [ { "ec_number": "2.3.2.5", "activity": "N-terminal L-glutaminyl-[peptide] = N-terminal 5-oxo-L-prolyl-[peptide] + NH4(+).", "evidence": [ { "id": "Q16769", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q16769" } ] }, { "ec_number": "2.3.2.5", "activity": "", "evidence": [ { "id": "Q16769", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q16769" } ] } ] }, { "uniprot_ac": "Q6XQN6", "gene_name": "NAPRT", "activity": [ { "ec_number": "6.3.4.21", "activity": "5-phospho-alpha-D-ribose 1-diphosphate + ATP + H2O + nicotinate = ADP + diphosphate + nicotinate beta-D-ribonucleotide + phosphate.", "evidence": [ { "id": "Q6XQN6", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q6XQN6" } ] }, { "ec_number": "6.3.4.21", "activity": "", "evidence": [ { "id": "Q6XQN6", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q6XQN6" } ] } ] }, { "uniprot_ac": "Q8NBS9", "gene_name": "TXNDC5", "activity": [ { "ec_number": "1.8.4.-", "activity": "", "evidence": [ { "id": "Q8NBS9", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q8NBS9" } ] }, { "ec_number": "5.3.4.1", "activity": "Catalyzes the rearrangement of -S-S- bonds in proteins.", "evidence": [ { "id": "Q8NBS9", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q8NBS9" } ] }, { "ec_number": "5.3.4.1", "activity": "", "evidence": [ { "id": "Q8NBS9", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q8NBS9" } ] } ] }, { "uniprot_ac": "Q8WVQ1", "gene_name": "CANT1", "activity": [ { "ec_number": "3.6.1.6", "activity": "ADP + H2O = AMP + H(+) + phosphate.", "evidence": [ { "id": "Q8WVQ1", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q8WVQ1" } ] }, { "ec_number": "3.6.1.6", "activity": "", "evidence": [ { "id": "Q8WVQ1", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q8WVQ1" } ] } ] }, { "uniprot_ac": "Q92820", "gene_name": "GGH", "activity": [ { "ec_number": "3.4.19.9", "activity": "(6S)-5,6,7,8-tetrahydrofolyl-(gamma-L-Glu)(n) + (n-1) H2O = (6S)-5,6,7,8-tetrahydrofolate + (n-1) L-glutamate.", "evidence": [ { "id": "Q92820", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q92820" } ] }, { "ec_number": "3.4.19.9", "activity": "", "evidence": [ { "id": "Q92820", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q92820" } ] } ] }, { "uniprot_ac": "Q99519", "gene_name": "NEU1", "activity": [ { "ec_number": "3.2.1.18", "activity": "Hydrolysis of alpha-(2->3)-, alpha-(2->6)-, alpha-(2->8)- glycosidic linkages of terminal sialic acid residues in oligosaccharides, glycoproteins, glycolipids, colominic acid and synthetic substrates.", "evidence": [ { "id": "Q99519", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q99519" } ] }, { "ec_number": "3.2.1.18", "activity": "", "evidence": [ { "id": "Q99519", "database": "UniProtKB", "url": 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