One study showed that TLR9 proteolysis is a multistep process with the initial cleavage that can be mediated by AEP or multiple members of the cathepsin family. The second event is mediated exclusively by cathepsins. TLR7 and TLR3 were reported to be cleaved in a similar manner (Ewald SE et al 2011). Cleavage of TLR3 is not shown in this reaction, since other studies demonstrated that the N-terminal region of TLR3 ectodomain was implicated in ligand binding, suggesting that TLR3 may function as a full-length receptor (Liu L et al 2008, Tokisue T et al 2008).
Both full-length receptor and cleaved fragment corresponding to the C-terminal part of TLR9 were capable to bind ligand, however only the processed form (TLR9 C-ter, aa 471-1032) was shown to bind MyD88 and induce signaling in different mouse cells (Ewald SE et al 2008).",
"cellular_location": "endolysosome membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P07858-1",
"P07711-1",
"P43235-1",
"P25774-1",
"Q99538-1"
],
"evidence": [
{
"id": "R-HSA-1678920",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-1678920"
}
]
},
{
"id": "R-HSA-2130349",
"name": "Generation of CLIP from lip10",
"equation": "",
"summary": "The lip10 fragments bound in the nonameric complex are processed leaving only the CLIP fragment (81-105) bound to the MHC II peptide binding groove. Three cysteine proteases have been shown to be capable of digesting lip10, each with a different expression pattern among different APC. Cathepsin (Cat) S digests Ii in B cells and dendritic cells, thymic epithelial cells use Cat L and Cat L, while Cat S and F are active in macrophages (Villadangos, 2001; Bryant et al, 2002). Cat S appears to be the major enzyme involved as demonstrated by the use of specific inhibitors and of knockout experiments (Stumptner-Cuvelette et al. 2002). Following lip10 digestion, the MHC-like molecule HLA-DM induces the exchange of CLIP fragment for a highly diverse array of antigens (Denzin & Cresswell. 1995).",
"cellular_location": "lysosomal membrane, lysosomal lumen",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q9UBX1-1",
"P10619-1",
"P07339-1",
"P07858-1",
"P07711-1",
"P14091-1",
"P43234-1",
"P53634-1",
"P43235-1",
"O60911-1",
"P25774-1"
],
"evidence": [
{
"id": "R-HSA-2130349",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-2130349"
}
]
},
{
"id": "R-HSA-2130504",
"name": "Cleavage of lip22 to lip10",
"equation": "",
"summary": "The cleavage of lip22 occurs in residues 115-125, closer to the C-terminus than CLIP (residues 81-105). The resulting lip10 fragment is approximately 100 residues long and extends just through the C-terminus of the Ii CLIP. The proteases responsible for generating lip10 in vivo are not determined. Cysteine proteases like cathepsin S (CatS) are capable of degrading lip22 to lip10 (Bania et al. 2003) but in the presence of LHVS, an inhibitor of CatS, lip22 degradation is still observed, suggesting that other proteases are involved (Villadangos et al. 1997), possibly aspartic proteinases such as cathepsins D and E (Kageyama et al. 1996). The degradation of lip22 may depend on cell type (Bania et al. 2003). The lip22 and lip10 intermediate forms are still maintained as a nonameric complex due to the existence of the last trimerisation domain in the transmembrane region.",
"cellular_location": "lysosomal membrane, lysosomal lumen",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q9UBX1-1",
"P10619-1",
"P07339-1",
"P07858-1",
"P07711-1",
"P14091-1",
"P43234-1",
"P53634-1",
"P43235-1",
"O60911-1",
"P25774-1"
],
"evidence": [
{
"id": "R-HSA-2130504",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-2130504"
}
]
},
{
"id": "R-HSA-2130706",
"name": "MHC class II antigen processing",
"equation": "",
"summary": "Antigen processing and loading on to MHC class II molecules occurs in late endocytic/lysosomal vesicles, where epitopes which require extensive proteolytic processing are generated (Bryant & Ploegh 2003). These late endosome/lysosomal-like compartments are enriched in MHC II and are referred to as MIICs (MHC class II compartments) (Peters et al. 1991). A variety of lysosomal proteases like cathepsins S, D, B etc. and Asparaginyl endopeptidase (AEP) are suggested to be involved in the processing of antigens to generate CD4+ T cell epitopes (Deusing et al. 1998, Shi et al. 1999, Pluger et al. 2002, Watts et al. 2005). An initial cleavage by endopeptidases (AEP) would be necessary to unlock the antigen and allow further trimming of the ends by exopeptidases (Cathepsins). In the acidic environment of the lysosome, cathepsins are generally activated by autocatalytic cleavage of a propeptide which otherwise blocks the active site.",
"cellular_location": "lysosomal lumen",
"input_participant_list": [],
"output_participant_list": [
"R-ALL-2213226"
],
"enzyme_list": [
"Q9UBX1-1",
"P10619-1",
"P07339-1",
"P07858-1",
"P07711-1",
"P14091-1",
"P43234-1",
"P53634-1",
"P43235-1",
"O60911-1",
"P25774-1"
],
"evidence": [
{
"id": "R-HSA-2130706",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-2130706"
}
]
},
{
"id": "R-HSA-2168923",
"name": "Collagen type XVIII endostatin release",
"equation": "",
"summary": "Collagen type XVIII is a heparan sulfate proteoglycan associated with the basement membranes of almost all epithelia and endothelia. It has a large C-terminal noncollagenous domain. Mouse knockouts suggest that it may have a role in maintaining the structural integrity of the extracellular matrix (Utriainen et al. 2004).
Proteolytic cleavage of the C-terminal noncollagenous domain by matrix metalloproteinases (Heljasvaara et al. 2005) releases 18 to 38 kDa C-terminal proteolytic fragments, collectively named endostatin. They have anti-angiogenic activity (O'Reilly et al. 1997, St\u00e4ndker et al. 1997) and suppress primary tumor and metastasis growth in experimental animal models (Ortega & Werb 2002). It is not clear whether this collagen subtype forms supramolecular assemblies (Myllyharju & Kivirikko, 2004) but thought likely, via a similar mechanism to the related collagen XV (Hurskainen et al. 2010).
Endostatin-like fragments are released from collagen type XVIII by MMP 7 (Lin et al. 2001), 3, 9, 12, 13 (Ferreras et al. 2000) and 20 (Heljasvaara et al. 2005). Several cathepsins and elastase can bring about endostatin release (Ferreras et al. 2000, Felbor et al. 2000).",
"cellular_location": "extracellular region",
"input_participant_list": [
"R-HSA-2172281"
],
"output_participant_list": [
"R-HSA-2470858"
],
"enzyme_list": [
"P39900-1",
"P07858-1",
"P07711-1",
"P14780-1",
"P43235-1",
"P45452-1",
"P09237-1",
"P08254-1",
"O60882-1"
],
"evidence": [
{
"id": "R-HSA-2168923",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-2168923"
}
]
},
{
"id": "R-HSA-2213200",
"name": "Release of endostatin-like peptides",
"equation": "",
"summary": "Collagens XV and XVIII are basement membrane associated collagens that can be cleaved to generate the antiangiogenic peptides restin (endostatin-XV) and endostatin (endostatin-XVIII), respectively (O'Reilly et al. 1997, Ramachandran et al. 1997, Sasaki et al. 2000). Endostatin fragments of differing molecular size (14-30 kDa) have been identified in vivo. Furthermore the C-terminal domains of several other collagens (IV, VIII, XIX) have anti-angiogenic and anti-tumoral activities (Ricard-Blum & Ballut 2011). Several proteases are able to generate endostatin from collagen XVIII including MMP-3, -7, -9, -13 and -20 and cathepsins B, V, S and L (Heljasvaara et al. 2005, Ma et al. 2007, Veillard et al. 2011). Endostatin inhibits proliferation of endothelial cells, angiogenesis and tumor growth in vivo (O'Reilly et al. 1997).",
"cellular_location": "extracellular region",
"input_participant_list": [
"R-HSA-2152295"
],
"output_participant_list": [
"R-HSA-2225571",
"R-HSA-2225572",
"R-HSA-2225575",
"R-HSA-2225576"
],
"enzyme_list": [
"P07858-1",
"P07711-1",
"P14780-1",
"O60911-1",
"P25774-1",
"P45452-1",
"P09237-1",
"P08254-1",
"O60882-1"
],
"evidence": [
{
"id": "R-HSA-2213200",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-2213200"
}
]
},
{
"id": "R-HSA-2471621",
"name": "Endostatin degradation by cathepsins",
"equation": "",
"summary": "As well as generating endostatin from collagen XVIII, cathepsins L and B quickly degrade it, as do cathepsins D and K. In contrast MMPs that produce endostatin do not cleave it further (Ferreras et al. 2000).",
"cellular_location": "extracellular region",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P07339-1",
"P07858-1",
"P07711-1",
"P43235-1"
],
"evidence": [
{
"id": "R-HSA-2471621",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-2471621"
}
]
},
{
"id": "R-HSA-6800434",
"name": "Exocytosis of ficolin-rich granule lumen proteins",
"equation": "",
"summary": "Ficoli-1 rich granules are a relatively new fourth neutrophil granule population that is enriched in the microbial lectin ficolin-1. Ficolin-1 is present in tertiary granules, but ficolin-1 rich granules can be differentiated by having low levels of gelatinases and an elevated exocytosis propensity (Rorvig et al. 2009, 2013). The importance of these granules may be to provide rapid release of pattern recognition molecules to activate the lectin complement pathway (Rorvig et al. 2009).",
"cellular_location": "extracellular region, ficolin-1-rich granule lumen",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q9UBR2-1",
"P18669-1",
"P32320-1",
"P09917-1",
"O00487-1",
"P13639-1",
"P12268-1",
"P62937-1",
"P15586-1",
"Q96G03-1",
"Q9P0J7-1",
"P68402-1",
"P36871-1",
"Q99436-1",
"P07339-1",
"P13798-1",
"P53396-1",
"P55072-1",
"P68104-1",
"P11142-1",
"Q9Y315-1",
"P04075-1",
"P09972-1",
"P07900-1",
"P09211-1",
"Q16539-1",
"P07858-1",
"P14618-1",
"P28482-1",
"Q01432-1",
"P12956-1",
"Q7Z6Z7-1",
"Q9UNP9-1",
"Q13510-1",
"P14174-1",
"P15848-1",
"P16278-1",
"Q8WVQ1-1",
"P04040-1",
"O00571-1",
"P14780-1",
"P06744-1",
"P52790-1",
"P00491-1",
"P06737-1",
"Q16769-1",
"P08236-1",
"P02794-1",
"P07384-1",
"Q14004-1",
"P00746-1",
"P98066-1",
"P25774-1",
"Q13162-1",
"P17858-1",
"P46976-1",
"P09960-1",
"P22392-1",
"P13716-1",
"O75874-1",
"P20839-1"
],
"evidence": [
{
"id": "R-HSA-6800434",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-6800434"
}
]
}
],
"reaction_participants": [
{
"participant_id": "R-ALL-2213226",
"participant_name": "MHC class II epitopes [lysosomal lumen]",
"crossref": [
{
"id": "15841",
"database": "ChEBI",
"url": ""
},
{
"id": "15841",
"database": "ChEBI",
"url": ""
},
{
"id": "15841",
"database": "ChEBI",
"url": ""
},
{
"id": "15841",
"database": "ChEBI",
"url": ""
},
{
"id": "15841",
"database": "ChEBI",
"url": ""
},
{
"id": "15841",
"database": "ChEBI",
"url": ""
}
]
},
{
"participant_id": "R-HSA-2152295",
"participant_name": "Collagen type XVIII [extracellular region]",
"crossref": [
{
"id": "CPX-1759",
"database": "ComplexPortal",
"url": ""
}
]
},
{
"participant_id": "R-HSA-2172281",
"participant_name": "Collagen type XVIII multimer [extracellular region]",
"crossref": [
{
"id": "36080",
"database": "ChEBI",
"url": ""
}
]
},
{
"participant_id": "R-HSA-2225571",
"participant_name": "COL15A1(?-1211) [extracellular region]",
"crossref": [
{
"id": "ENST00000375001",
"database": "Ensembl",
"url": ""
},
{
"id": "ENSP00000364140",
"database": "Ensembl",
"url": ""
},
{
"id": "3N3F",
"database": "PDB",
"url": ""
},
{
"id": "P39059",
"database": "Pharos - Targets",
"url": ""
},
{
"id": "ENSG00000204291-COL15A1",
"database": "HPA",
"url": ""
},
{
"id": "P39059",
"database": "UniProt",
"url": ""
},
{
"id": "P39059",
"database": "PRO",
"url": ""
},
{
"id": "NP_001846.3",
"database": "RefSeq",
"url": ""
},
{
"id": "ENSG00000204291",
"database": "OpenTargets",
"url": ""
},
{
"id": "ENSG00000204291",
"database": "Ensembl",
"url": ""
},
{
"id": "P39059",
"database": "GeneCards",
"url": ""
},
{
"id": "XP_011516516.1",
"database": "RefSeq",
"url": ""
}
]
},
{
"participant_id": "R-HSA-2225572",
"participant_name": "COL15A1(1212-1388) [extracellular region]",
"crossref": [
{
"id": "ENSG00000204291",
"database": "Ensembl",
"url": ""
},
{
"id": "XP_011516516.1",
"database": "RefSeq",
"url": ""
},
{
"id": "P39059",
"database": "GeneCards",
"url": ""
},
{
"id": "P39059",
"database": "PRO",
"url": ""
},
{
"id": "NP_001846.3",
"database": "RefSeq",
"url": ""
},
{
"id": "ENSG00000204291",
"database": "OpenTargets",
"url": ""
},
{
"id": "ENSG00000204291-COL15A1",
"database": "HPA",
"url": ""
},
{
"id": "P39059",
"database": "Pharos - Targets",
"url": ""
},
{
"id": "3N3F",
"database": "PDB",
"url": ""
},
{
"id": "P39059",
"database": "UniProt",
"url": ""
},
{
"id": "ENST00000375001",
"database": "Ensembl",
"url": ""
},
{
"id": "ENSP00000364140",
"database": "Ensembl",
"url": ""
}
]
},
{
"participant_id": "R-HSA-2225575",
"participant_name": "COL18A1(1572-11754) [extracellular region]",
"crossref": [
{
"id": "ENSP00000498485",
"database": "Ensembl",
"url": ""
},
{
"id": "P39060",
"database": "PRO",
"url": ""
},
{
"id": "ENSG00000182871-COL18A1",
"database": "HPA",
"url": ""
},
{
"id": "ENST00000651438",
"database": "Ensembl",
"url": ""
},
{
"id": "NP_569711.2",
"database": "RefSeq",
"url": ""
},
{
"id": "3HSH",
"database": "PDB",
"url": ""
},
{
"id": "NP_569712.2",
"database": "RefSeq",
"url": ""
},
{
"id": "ENSG00000182871",
"database": "Ensembl",
"url": ""
},
{
"id": "3HON",
"database": "PDB",
"url": ""
},
{
"id": "P39060",
"database": "GeneCards",
"url": ""
},
{
"id": "P39060",
"database": "UniProt",
"url": ""
},
{
"id": "HMDBP13479",
"database": "HMDB Protein",
"url": ""
},
{
"id": "ENST00000355480",
"database": "Ensembl",
"url": ""
},
{
"id": "ENSP00000352798",
"database": "Ensembl",
"url": ""
},
{
"id": "NP_085059.2",
"database": "RefSeq",
"url": ""
},
{
"id": "P39060",
"database": "Pharos - Targets",
"url": ""
},
{
"id": "15766",
"database": "Orphanet",
"url": ""
},
{
"id": "ENST00000359759",
"database": "Ensembl",
"url": ""
},
{
"id": "ENSG00000182871",
"database": "OpenTargets",
"url": ""
},
{
"id": "ENSP00000347665",
"database": "Ensembl",
"url": ""
},
{
"id": "1BNL",
"database": "PDB",
"url": ""
}
]
},
{
"participant_id": "R-HSA-2225576",
"participant_name": "COL18A1(?-1571) [extracellular region]",
"crossref": [
{
"id": "ENSP00000498485",
"database": "Ensembl",
"url": ""
},
{
"id": "P39060",
"database": "PRO",
"url": ""
},
{
"id": "ENST00000651438",
"database": "Ensembl",
"url": ""
},
{
"id": "ENSG00000182871-COL18A1",
"database": "HPA",
"url": ""
},
{
"id": "NP_569711.2",
"database": "RefSeq",
"url": ""
},
{
"id": "3HSH",
"database": "PDB",
"url": ""
},
{
"id": "NP_569712.2",
"database": "RefSeq",
"url": ""
},
{
"id": "ENSG00000182871",
"database": "Ensembl",
"url": ""
},
{
"id": "3HON",
"database": "PDB",
"url": ""
},
{
"id": "P39060",
"database": "GeneCards",
"url": ""
},
{
"id": "15766",
"database": "Orphanet",
"url": ""
},
{
"id": "ENST00000355480",
"database": "Ensembl",
"url": ""
},
{
"id": "HMDBP13479",
"database": "HMDB Protein",
"url": ""
},
{
"id": "NP_085059.2",
"database": "RefSeq",
"url": ""
},
{
"id": "ENSP00000352798",
"database": "Ensembl",
"url": ""
},
{
"id": "P39060",
"database": "Pharos - Targets",
"url": ""
},
{
"id": "P39060",
"database": "UniProt",
"url": ""
},
{
"id": "ENST00000359759",
"database": "Ensembl",
"url": ""
},
{
"id": "ENSG00000182871",
"database": "OpenTargets",
"url": ""
},
{
"id": "1BNL",
"database": "PDB",
"url": ""
},
{
"id": "ENSP00000347665",
"database": "Ensembl",
"url": ""
}
]
},
{
"participant_id": "R-HSA-2470858",
"participant_name": "Cleaved collagen type XVIII multimer [extracellular region]",
"crossref": [
{
"id": "36080",
"database": "ChEBI",
"url": ""
}
]
}
],
"reaction_enzymes": [
{
"uniprot_ac": "O00487",
"gene_name": "PSMD14",
"activity": [
{
"ec_number": "3.4.19.-",
"activity": "",
"evidence": [
{
"id": "O00487",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/O00487"
}
]
}
]
},
{
"uniprot_ac": "O00571",
"gene_name": "DDX3X",
"activity": [
{
"ec_number": "3.6.4.13",
"activity": "ATP + H2O = ADP + H(+) + phosphate.",
"evidence": [
{
"id": "O00571",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/O00571"
}
]
},
{
"ec_number": "3.6.4.13",
"activity": "",
"evidence": [
{
"id": "O00571",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/O00571"
}
]
}
]
},
{
"uniprot_ac": "O60882",
"gene_name": "MMP20",
"activity": [
{
"ec_number": "3.4.24.-",
"activity": "",
"evidence": [
{
"id": "O60882",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/O60882"
}
]
}
]
},
{
"uniprot_ac": "O60911",
"gene_name": "CTSV",
"activity": [
{
"ec_number": "3.4.22.43",
"activity": "The recombinant enzyme hydrolyzes proteins (serum albumin, collagen) and synthetic substrates (Z-Phe-Arg-NHMec > Z-Leu-Arg-NHMec > Z-Val-Arg-NHMec).",
"evidence": [
{
"id": "O60911",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/O60911"
}
]
},
{
"ec_number": "3.4.22.43",
"activity": "",
"evidence": [
{
"id": "O60911",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/O60911"
}
]
}
]
},
{
"uniprot_ac": "O75874",
"gene_name": "IDH1",
"activity": [
{
"ec_number": "1.1.1.42",
"activity": "D-threo-isocitrate + NADP(+) = 2-oxoglutarate + CO2 + NADPH.",
"evidence": [
{
"id": "O75874",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/O75874"
}
]
},
{
"ec_number": "1.1.1.42",
"activity": "",
"evidence": [
{
"id": "O75874",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/O75874"
}
]
}
]
},
{
"uniprot_ac": "P00491",
"gene_name": "PNP",
"activity": [
{
"ec_number": "2.4.2.1",
"activity": "a purine 2'-deoxy-D-ribonucleoside + phosphate = 2-deoxy-alpha-D-ribose 1-phosphate + a purine nucleobase.",
"evidence": [
{
"id": "P00491",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P00491"
}
]
},
{
"ec_number": "2.4.2.1",
"activity": "",
"evidence": [
{
"id": "P00491",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P00491"
}
]
}
]
},
{
"uniprot_ac": "P00746",
"gene_name": "CFD",
"activity": [
{
"ec_number": "3.4.21.46",
"activity": "Selective cleavage of Arg-|-Lys bond in complement factor B when in complex with complement subcomponent C3b or with cobra venom factor.",
"evidence": [
{
"id": "P00746",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P00746"
}
]
},
{
"ec_number": "3.4.21.46",
"activity": "",
"evidence": [
{
"id": "P00746",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P00746"
}
]
}
]
},
{
"uniprot_ac": "P02794",
"gene_name": "FTH1",
"activity": [
{
"ec_number": "1.16.3.1",
"activity": "4 Fe(2+) + 4 H(+) + O2 = 4 Fe(3+) + 2 H2O.",
"evidence": [
{
"id": "P02794",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P02794"
}
]
},
{
"ec_number": "1.16.3.1",
"activity": "",
"evidence": [
{
"id": "P02794",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P02794"
}
]
}
]
},
{
"uniprot_ac": "P04040",
"gene_name": "CAT",
"activity": [
{
"ec_number": "1.11.1.6",
"activity": "2 H2O2 = 2 H2O + O2.",
"evidence": [
{
"id": "P04040",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P04040"
}
]
},
{
"ec_number": "1.11.1.6",
"activity": "",
"evidence": [
{
"id": "P04040",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P04040"
}
]
}
]
},
{
"uniprot_ac": "P04075",
"gene_name": "ALDOA",
"activity": [
{
"ec_number": "4.1.2.13",
"activity": "beta-D-fructose 1,6-bisphosphate = D-glyceraldehyde 3-phosphate + dihydroxyacetone phosphate.",
"evidence": [
{
"id": "P04075",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P04075"
}
]
},
{
"ec_number": "4.1.2.13",
"activity": "",
"evidence": [
{
"id": "P04075",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P04075"
}
]
}
]
},
{
"uniprot_ac": "P06737",
"gene_name": "PYGL",
"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": "P06737",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P06737"
}
]
},
{
"ec_number": "2.4.1.1",
"activity": "",
"evidence": [
{
"id": "P06737",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P06737"
}
]
}
]
},
{
"uniprot_ac": "P06744",
"gene_name": "GPI",
"activity": [
{
"ec_number": "5.3.1.9",
"activity": "alpha-D-glucose 6-phosphate = beta-D-fructose 6-phosphate.",
"evidence": [
{
"id": "P06744",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P06744"
}
]
},
{
"ec_number": "5.3.1.9",
"activity": "",
"evidence": [
{
"id": "P06744",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P06744"
}
]
}
]
},
{
"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": "P07384",
"gene_name": "CAPN1",
"activity": [
{
"ec_number": "3.4.22.52",
"activity": "Broad endopeptidase specificity.",
"evidence": [
{
"id": "P07384",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P07384"
}
]
},
{
"ec_number": "3.4.22.52",
"activity": "",
"evidence": [
{
"id": "P07384",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P07384"
}
]
}
]
},
{
"uniprot_ac": "P07711",
"gene_name": "CTSL",
"activity": [
{
"ec_number": "3.4.22.15",
"activity": "Specificity close to that of papain. As compared to cathepsin B, cathepsin L exhibits higher activity toward protein substrates, but has little activity on Z-Arg-Arg-NHMec, and no peptidyl-dipeptidase activity.",
"evidence": [
{
"id": "P07711",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P07711"
}
]
},
{
"ec_number": "3.4.22.15",
"activity": "",
"evidence": [
{
"id": "P07711",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P07711"
}
]
}
]
},
{
"uniprot_ac": "P07858",
"gene_name": "CTSB",
"activity": [
{
"ec_number": "3.4.22.1",
"activity": "Hydrolysis of proteins with broad specificity for peptide bonds. Preferentially cleaves -Arg-Arg-|-Xaa bonds in small molecule substrates (thus differing from cathepsin L). In addition to being an endopeptidase, shows peptidyl-dipeptidase activity, liberating C-terminal dipeptides.",
"evidence": [
{
"id": "P07858",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P07858"
}
]
},
{
"ec_number": "3.4.22.1",
"activity": "",
"evidence": [
{
"id": "P07858",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P07858"
}
]
}
]
},
{
"uniprot_ac": "P07900",
"gene_name": "HSP90AA1",
"activity": [
{
"ec_number": "3.6.4.10",
"activity": "ATP + H2O = ADP + H(+) + phosphate.",
"evidence": [
{
"id": "P07900",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P07900"
}
]
},
{
"ec_number": "3.6.4.10",
"activity": "",
"evidence": [
{
"id": "P07900",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P07900"
}
]
}
]
},
{
"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": "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": "P09211",
"gene_name": "GSTP1",
"activity": [
{
"ec_number": "2.5.1.18",
"activity": "glutathione + RX = a halide anion + an S-substituted glutathione + H(+).",
"evidence": [
{
"id": "P09211",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P09211"
}
]
},
{
"ec_number": "2.5.1.18",
"activity": "",
"evidence": [
{
"id": "P09211",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P09211"
}
]
}
]
},
{
"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": "P09917",
"gene_name": "ALOX5",
"activity": [
{
"ec_number": "1.13.11.-",
"activity": "",
"evidence": [
{
"id": "P09917",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P09917"
}
]
},
{
"ec_number": "1.13.11.34",
"activity": "(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 = H2O + leukotriene A4.",
"evidence": [
{
"id": "P09917",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P09917"
}
]
}
]
},
{
"uniprot_ac": "P09960",
"gene_name": "LTA4H",
"activity": [
{
"ec_number": "3.3.2.6",
"activity": "H2O + leukotriene A4 = leukotriene B4.",
"evidence": [
{
"id": "P09960",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P09960"
}
]
},
{
"ec_number": "3.4.11.4",
"activity": "Release of the N-terminal residue from a tripeptide.",
"evidence": [
{
"id": "P09960",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P09960"
}
]
},
{
"ec_number": "3.3.2.6",
"activity": "",
"evidence": [
{
"id": "P09960",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P09960"
}
]
}
]
},
{
"uniprot_ac": "P09972",
"gene_name": "ALDOC",
"activity": [
{
"ec_number": "4.1.2.13",
"activity": "beta-D-fructose 1,6-bisphosphate = D-glyceraldehyde 3-phosphate + dihydroxyacetone phosphate.",
"evidence": [
{
"id": "P09972",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P09972"
}
]
},
{
"ec_number": "4.1.2.13",
"activity": "",
"evidence": [
{
"id": "P09972",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P09972"
}
]
}
]
},
{
"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": "P11142",
"gene_name": "HSPA8",
"activity": [
{
"ec_number": "3.6.4.10",
"activity": "ATP + H2O = ADP + H(+) + phosphate.",
"evidence": [
{
"id": "P11142",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P11142"
}
]
},
{
"ec_number": "3.6.4.10",
"activity": "",
"evidence": [
{
"id": "P11142",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P11142"
}
]
}
]
},
{
"uniprot_ac": "P12268",
"gene_name": "IMPDH2",
"activity": [
{
"ec_number": "1.1.1.205",
"activity": "H2O + IMP + NAD(+) = H(+) + NADH + XMP.",
"evidence": [
{
"id": "P12268",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P12268"
}
]
},
{
"ec_number": "1.1.1.205",
"activity": "",
"evidence": [
{
"id": "P12268",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P12268"
}
]
}
]
},
{
"uniprot_ac": "P12956",
"gene_name": "XRCC6",
"activity": [
{
"ec_number": "4.2.99.-",
"activity": "",
"evidence": [
{
"id": "P12956",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P12956"
}
]
},
{
"ec_number": "3.6.4.-",
"activity": "",
"evidence": [
{
"id": "P12956",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P12956"
}
]
}
]
},
{
"uniprot_ac": "P13639",
"gene_name": "EEF2",
"activity": [
{
"ec_number": "3.6.5.-",
"activity": "",
"evidence": [
{
"id": "P13639",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P13639"
}
]
}
]
},
{
"uniprot_ac": "P13716",
"gene_name": "ALAD",
"activity": [
{
"ec_number": "4.2.1.24",
"activity": "2 5-aminolevulinate = H(+) + 2 H2O + porphobilinogen.",
"evidence": [
{
"id": "P13716",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P13716"
}
]
},
{
"ec_number": "4.2.1.24",
"activity": "",
"evidence": [
{
"id": "P13716",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P13716"
}
]
}
]
},
{
"uniprot_ac": "P13798",
"gene_name": "APEH",
"activity": [
{
"ec_number": "3.4.19.1",
"activity": "Internal cleavage of oxidized and glycated proteins.",
"evidence": [
{
"id": "P13798",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P13798"
}
]
},
{
"ec_number": "3.4.19.1",
"activity": "",
"evidence": [
{
"id": "P13798",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P13798"
}
]
}
]
},
{
"uniprot_ac": "P14091",
"gene_name": "CTSE",
"activity": [
{
"ec_number": "3.4.23.34",
"activity": "Similar to cathepsin D, but slightly broader specificity.",
"evidence": [
{
"id": "P14091",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P14091"
}
]
},
{
"ec_number": "3.4.23.34",
"activity": "",
"evidence": [
{
"id": "P14091",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P14091"
}
]
}
]
},
{
"uniprot_ac": "P14174",
"gene_name": "MIF",
"activity": [
{
"ec_number": "5.3.2.1",
"activity": "3-phenylpyruvate = enol-phenylpyruvate.",
"evidence": [
{
"id": "P14174",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P14174"
}
]
},
{
"ec_number": "5.3.3.12",
"activity": "L-dopachrome = 5,6-dihydroxyindole-2-carboxylate.",
"evidence": [
{
"id": "P14174",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P14174"
}
]
},
{
"ec_number": "5.3.2.1",
"activity": "",
"evidence": [
{
"id": "P14174",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P14174"
}
]
}
]
},
{
"uniprot_ac": "P14618",
"gene_name": "PKM",
"activity": [
{
"ec_number": "2.7.1.40",
"activity": "CTP + pyruvate = CDP + H(+) + phosphoenolpyruvate.",
"evidence": [
{
"id": "P14618",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P14618"
}
]
},
{
"ec_number": "2.7.1.40",
"activity": "",
"evidence": [
{
"id": "P14618",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P14618"
}
]
},
{
"ec_number": "2.7.10.2",
"activity": "ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein].",
"evidence": [
{
"id": "P14618",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P14618"
}
]
},
{
"ec_number": "2.7.11.1",
"activity": "ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein].",
"evidence": [
{
"id": "P14618",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P14618"
}
]
}
]
},
{
"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": "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": "P17858",
"gene_name": "PFKL",
"activity": [
{
"ec_number": "2.7.1.11",
"activity": "ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 1,6-bisphosphate + H(+).",
"evidence": [
{
"id": "P17858",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P17858"
}
]
},
{
"ec_number": "2.7.1.11",
"activity": "",
"evidence": [
{
"id": "P17858",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P17858"
}
]
}
]
},
{
"uniprot_ac": "P18669",
"gene_name": "PGAM1",
"activity": [
{
"ec_number": "5.4.2.11",
"activity": "(2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate.",
"evidence": [
{
"id": "P18669",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P18669"
}
]
},
{
"ec_number": "5.4.2.4",
"activity": "(2R)-3-phospho-glyceroyl phosphate = (2R)-2,3-bisphosphoglycerate + H(+).",
"evidence": [
{
"id": "P18669",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P18669"
}
]
},
{
"ec_number": "5.4.2.4",
"activity": "",
"evidence": [
{
"id": "P18669",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P18669"
}
]
},
{
"ec_number": "5.4.2.11",
"activity": "",
"evidence": [
{
"id": "P18669",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P18669"
}
]
}
]
},
{
"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": "P22392",
"gene_name": "NME2",
"activity": [
{
"ec_number": "2.7.4.6",
"activity": "a ribonucleoside 5'-diphosphate + ATP = a ribonucleoside 5'-triphosphate + ADP.",
"evidence": [
{
"id": "P22392",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P22392"
}
]
},
{
"ec_number": "2.7.13.3",
"activity": "ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.",
"evidence": [
{
"id": "P22392",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P22392"
}
]
},
{
"ec_number": "2.7.4.6",
"activity": "",
"evidence": [
{
"id": "P22392",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P22392"
}
]
},
{
"ec_number": "2.7.13.3",
"activity": "",
"evidence": [
{
"id": "P22392",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P22392"
}
]
}
]
},
{
"uniprot_ac": "P25774",
"gene_name": "CTSS",
"activity": [
{
"ec_number": "3.4.22.27",
"activity": "Similar to cathepsin L, but with much less activity on Z-Phe-Arg-|-NHMec, and more activity on the Z-Val-Val-Arg-|-Xaa compound.",
"evidence": [
{
"id": "P25774",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P25774"
}
]
},
{
"ec_number": "3.4.22.27",
"activity": "",
"evidence": [
{
"id": "P25774",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P25774"
}
]
}
]
},
{
"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": "P32320",
"gene_name": "CDA",
"activity": [
{
"ec_number": "3.5.4.5",
"activity": "2'-deoxycytidine + H(+) + H2O = 2'-deoxyuridine + NH4(+).",
"evidence": [
{
"id": "P32320",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P32320"
}
]
},
{
"ec_number": "3.5.4.5",
"activity": "",
"evidence": [
{
"id": "P32320",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P32320"
}
]
}
]
},
{
"uniprot_ac": "P36871",
"gene_name": "PGM1",
"activity": [
{
"ec_number": "5.4.2.2",
"activity": "alpha-D-glucose 1-phosphate = alpha-D-glucose 6-phosphate.",
"evidence": [
{
"id": "P36871",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P36871"
}
]
},
{
"ec_number": "5.4.2.2",
"activity": "",
"evidence": [
{
"id": "P36871",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P36871"
}
]
}
]
},
{
"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": "P43234",
"gene_name": "CTSO",
"activity": [
{
"ec_number": "3.4.22.42",
"activity": "The recombinant human enzyme hydrolyzes synthetic endopeptidase substrates including Z-Phe-Arg-NHMec and Z-Arg-Arg-NHMec.",
"evidence": [
{
"id": "P43234",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P43234"
}
]
},
{
"ec_number": "3.4.22.42",
"activity": "",
"evidence": [
{
"id": "P43234",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P43234"
}
]
}
]
},
{
"uniprot_ac": "P43235",
"gene_name": "CTSK",
"activity": [
{
"ec_number": "3.4.22.38",
"activity": "Broad proteolytic activity. With small-molecule substrates and inhibitors, the major determinant of specificity is P2, which is preferably Leu, Met > Phe, and not Arg.",
"evidence": [
{
"id": "P43235",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P43235"
}
]
},
{
"ec_number": "3.4.22.38",
"activity": "",
"evidence": [
{
"id": "P43235",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P43235"
}
]
}
]
},
{
"uniprot_ac": "P45452",
"gene_name": "MMP13",
"activity": [
{
"ec_number": "3.4.24.-",
"activity": "",
"evidence": [
{
"id": "P45452",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P45452"
}
]
}
]
},
{
"uniprot_ac": "P46976",
"gene_name": "GYG1",
"activity": [
{
"ec_number": "2.4.1.186",
"activity": "[1,4-alpha-D-glucosyl](n)-L-tyrosyl-[glycogenin] + UDP-alpha-D-glucose = [1,4-alpha-D-glucosyl](n+1)-L-tyrosyl-[glycogenin] + H(+) + UDP.",
"evidence": [
{
"id": "P46976",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P46976"
}
]
},
{
"ec_number": "2.4.1.186",
"activity": "",
"evidence": [
{
"id": "P46976",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P46976"
}
]
}
]
},
{
"uniprot_ac": "P52790",
"gene_name": "HK3",
"activity": [
{
"ec_number": "2.7.1.1",
"activity": "ATP + D-fructose = ADP + D-fructose 6-phosphate + H(+).",
"evidence": [
{
"id": "P52790",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P52790"
}
]
},
{
"ec_number": "2.7.1.1",
"activity": "",
"evidence": [
{
"id": "P52790",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P52790"
}
]
},
{
"ec_number": "2.7.1.-",
"activity": "",
"evidence": [
{
"id": "P52790",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P52790"
}
]
}
]
},
{
"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": "P62937",
"gene_name": "PPIA",
"activity": [
{
"ec_number": "5.2.1.8",
"activity": "[protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0).",
"evidence": [
{
"id": "P62937",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P62937"
}
]
},
{
"ec_number": "5.2.1.8",
"activity": "",
"evidence": [
{
"id": "P62937",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P62937"
}
]
}
]
},
{
"uniprot_ac": "P68104",
"gene_name": "EEF1A1",
"activity": [
{
"ec_number": "3.6.5.-",
"activity": "",
"evidence": [
{
"id": "P68104",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P68104"
}
]
}
]
},
{
"uniprot_ac": "P68402",
"gene_name": "PAFAH1B2",
"activity": [
{
"ec_number": "3.1.1.47",
"activity": "a 1-O-alkyl-2-acetyl-sn-glycero-3-phosphocholine + H2O = 1-O-alkyl-sn-glycero-3-phosphocholine + acetate + H(+).",
"evidence": [
{
"id": "P68402",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P68402"
}
]
},
{
"ec_number": "3.1.1.47",
"activity": "",
"evidence": [
{
"id": "P68402",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P68402"
}
]
}
]
},
{
"uniprot_ac": "P98066",
"gene_name": "TNFAIP6",
"activity": [
{
"ec_number": "3.1.1.-",
"activity": "",
"evidence": [
{
"id": "P98066",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P98066"
}
]
}
]
},
{
"uniprot_ac": "Q01432",
"gene_name": "AMPD3",
"activity": [
{
"ec_number": "3.5.4.6",
"activity": "AMP + H(+) + H2O = IMP + NH4(+).",
"evidence": [
{
"id": "Q01432",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/Q01432"
}
]
},
{
"ec_number": "3.5.4.6",
"activity": "",
"evidence": [
{
"id": "Q01432",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/Q01432"
}
]
}
]
},
{
"uniprot_ac": "Q13162",
"gene_name": "PRDX4",
"activity": [
{
"ec_number": "1.11.1.24",
"activity": "[thioredoxin]-dithiol + a hydroperoxide = [thioredoxin]-disulfide + an alcohol + H2O.",
"evidence": [
{
"id": "Q13162",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/Q13162"
}
]
},
{
"ec_number": "1.11.1.24",
"activity": "",
"evidence": [
{
"id": "Q13162",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/Q13162"
}
]
}
]
},
{
"uniprot_ac": "Q13510",
"gene_name": "ASAH1",
"activity": [
{
"ec_number": "3.5.1.23",
"activity": "an N-acylsphing-4-enine + H2O = a fatty acid + sphing-4-enine.",
"evidence": [
{
"id": "Q13510",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/Q13510"
}
]
},
{
"ec_number": "3.5.1.23",
"activity": "",
"evidence": [
{
"id": "Q13510",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/Q13510"
}
]
},
{
"ec_number": "3.5.1.-",
"activity": "",
"evidence": [
{
"id": "Q13510",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/Q13510"
}
]
}
]
},
{
"uniprot_ac": "Q14004",
"gene_name": "CDK13",
"activity": [
{
"ec_number": "2.7.11.22",
"activity": "ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein].",
"evidence": [
{
"id": "Q14004",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/Q14004"
}
]
},
{
"ec_number": "2.7.11.23",
"activity": "[DNA-directed RNA polymerase] + ATP = ADP + H(+) + phospho-[DNA-directed RNA polymerase].",
"evidence": [
{
"id": "Q14004",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/Q14004"
}
]
},
{
"ec_number": "2.7.11.22",
"activity": "",
"evidence": [
{
"id": "Q14004",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/Q14004"
}
]
},
{
"ec_number": "2.7.11.23",
"activity": "",
"evidence": [
{
"id": "Q14004",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/Q14004"
}
]
}
]
},
{
"uniprot_ac": "Q16539",
"gene_name": "MAPK14",
"activity": [
{
"ec_number": "2.7.11.24",
"activity": "ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein].",
"evidence": [
{
"id": "Q16539",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/Q16539"
}
]
},
{
"ec_number": "2.7.11.24",
"activity": "",
"evidence": [
{
"id": "Q16539",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/Q16539"
}
]
}
]
},
{
"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": "Q7Z6Z7",
"gene_name": "HUWE1",
"activity": [
{
"ec_number": "2.3.2.26",
"activity": "S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.",
"evidence": [
{
"id": "Q7Z6Z7",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/Q7Z6Z7"
}
]
},
{
"ec_number": "2.3.2.26",
"activity": "",
"evidence": [
{
"id": "Q7Z6Z7",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/Q7Z6Z7"
}
]
}
]
},
{
"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": "Q96G03",
"gene_name": "PGM2",
"activity": [
{
"ec_number": "5.4.2.2",
"activity": "alpha-D-glucose 1-phosphate = alpha-D-glucose 6-phosphate.",
"evidence": [
{
"id": "Q96G03",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/Q96G03"
}
]
},
{
"ec_number": "5.4.2.7",
"activity": "2-deoxy-alpha-D-ribose 1-phosphate = 2-deoxy-D-ribose 5-phosphate.",
"evidence": [
{
"id": "Q96G03",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/Q96G03"
}
]
},
{
"ec_number": "5.4.2.7",
"activity": "",
"evidence": [
{
"id": "Q96G03",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/Q96G03"
}
]
}
]
},
{
"uniprot_ac": "Q99436",
"gene_name": "PSMB7",
"activity": [
{
"ec_number": "3.4.25.1",
"activity": "Cleavage of peptide bonds with very broad specificity.",
"evidence": [
{
"id": "Q99436",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/Q99436"
}
]
},
{
"ec_number": "3.4.25.1",
"activity": "",
"evidence": [
{
"id": "Q99436",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/Q99436"
}
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