{ "uniprot_canonical_ac": "P08311-1", "uniprot_ac": "P08311", "uniprot_id": "CATG_HUMAN", "mass": { "chemical_mass": 28837.0, "monoisotopic_mass": 28837.0 }, "refseq": { "ac": "NP_001902", "name": "cathepsin G preproprotein", "summary": "The protein encoded by this gene, a member of the peptidase S1 protein family, is found in azurophil granules of neutrophilic polymorphonuclear leukocytes. The encoded protease has a specificity similar to that of chymotrypsin C, and may participate in the killing and digestion of engulfed pathogens, and in connective tissue remodeling at sites of inflammation. In addition, the encoded protein is antimicrobial, with bacteriocidal activity against S. aureus and N. gonorrhoeae. Transcript variants utilizing alternative polyadenylation signals exist for this gene. [provided by RefSeq, Sep 2014].", "url": "https://www.ncbi.nlm.nih.gov/protein/NP_001902" }, "gene_names": [ { "name": "CTSG", "resource": "UniProtKB", "type": "recommended", "url": "https://www.uniprot.org/uniprot/P08311", "id": "P08311" }, { "name": "CATG; CG", "resource": "RefSeq", "type": "synonym", "url": "https://www.ncbi.nlm.nih.gov/protein/NP_001902", "id": "NP_001902" }, { "name": "CTSG", "resource": "RefSeq", "type": "synonym", "url": "https://www.ncbi.nlm.nih.gov/protein/NP_001902", "id": "NP_001902" } ], "protein_names": [ { "name": "Cathepsin G", "resource": "UniProtKB", "type": "recommended", "url": "", "id": "P08311" }, { "name": "3.4.21.20", "resource": "UniProtKB", "type": "synonym", "url": "", "id": "P08311" }, { "name": "CG", "resource": "UniProtKB", "type": "synonym", "url": "", "id": "P08311" }, { "name": "cathepsin G preproprotein", "resource": "RefSeq", "type": "synonym", "url": "https://www.ncbi.nlm.nih.gov/protein/NP_001902", "id": "NP_001902" } ], "function": [ { "annotation": "CTSG Suppresses Colorectal Cancer Progression through Negative Regulation of Akt/mTOR/Bcl2 Signaling Pathway. Publication Status: Online-Only", "evidence": [ { "database": "RefSeq", "id": "NP_001902", "url": "https://www.ncbi.nlm.nih.gov/protein/NP_001902" }, { "database": "PubMed", "id": "37151875", "url": "https://glygen.org/publication/PubMed/37151875" } ] }, { "annotation": "Cathepsin G is an antimicrobial protein with bacteriocidal activity against S. aureus and N. gonorrhoeae.", "evidence": [ { "database": "RefSeq", "id": "NP_001902", "url": "https://www.ncbi.nlm.nih.gov/protein/NP_001902" }, { "database": "PubMed", "id": "2116408", "url": "https://glygen.org/publication/PubMed/2116408" } ] }, { "annotation": "Cathepsin G-Induced Insulin-Like Growth Factor (IGF) Elevation in MCF-7 Medium Is Caused by Proteolysis of IGF Binding Protein (IGFBP)-2 but Not of IGF-1.", "evidence": [ { "database": "RefSeq", "id": "NP_001902", "url": "https://www.ncbi.nlm.nih.gov/protein/NP_001902" }, { "database": "PubMed", "id": "33132312", "url": "https://glygen.org/publication/PubMed/33132312" } ] }, { "annotation": "Cathepsin G-induced malignant progression of MCF-7 cells involves suppression of PAF signaling through induced expression of PAFAH1B2.", "evidence": [ { "database": "RefSeq", "id": "NP_001902", "url": "https://www.ncbi.nlm.nih.gov/protein/NP_001902" }, { "database": "PubMed", "id": "35462067", "url": "https://glygen.org/publication/PubMed/35462067" } ] }, { "annotation": "Downregulation of interleukin 36gamma and its cleaver cathepsin G following treatment with narrow-band ultraviolet B phototherapy in psoriasis vulgaris.", "evidence": [ { "database": "RefSeq", "id": "NP_001902", "url": "https://www.ncbi.nlm.nih.gov/protein/NP_001902" }, { "database": "PubMed", "id": "34376113", "url": "https://glygen.org/publication/PubMed/34376113" } ] }, { "annotation": "Gene body methylation facilitates the transcription of CTSG via antisense lncRNA AL136018.1 in dermatomyositic myoideum.", "evidence": [ { "database": "RefSeq", "id": "NP_001902", "url": "https://www.ncbi.nlm.nih.gov/protein/NP_001902" }, { "database": "PubMed", "id": "33245176", "url": "https://glygen.org/publication/PubMed/33245176" } ] }, { "annotation": "Serine protease with trypsin- and chymotrypsin-like specificity (PubMed:8194606, PubMed:29652924). Also displays antibacterial activity against Gram-negative and Gram-positive bacteria independent of its protease activity (PubMed:2116408, PubMed:2117044). Prefers Phe and Tyr residues in the P1 position of substrates but also cleaves efficiently after Trp and Leu (PubMed:29652924). Shows a preference for negatively charged amino acids in the P2' position and for aliphatic amino acids both upstream and downstream of the cleavage site (PubMed:29652924). Required for recruitment and activation of platelets which is mediated by the F2RL3/PAR4 platelet receptor (PubMed:3390156, PubMed:10702240). Binds reversibly to and stimulates B cells and CD4(+) and CD8(+) T cells (PubMed:7842483, PubMed:9000539). Also binds reversibly to natural killer (NK) cells and enhances NK cell cytotoxicity through its protease activity (PubMed:9000539, PubMed:9536127). Cleaves complement C3 (PubMed:1861080). Cleaves vimentin (By similarity). Cleaves thrombin receptor F2R/PAR1 and acts as either an agonist or an inhibitor, depending on the F2R cleavage site (PubMed:10702240, PubMed:7744748). Cleavage of F2R at '41-Arg-|-Ser-42' results in receptor activation while cleavage at '55-Phe-|-Trp-56' results in inhibition of receptor activation (PubMed:7744748). Cleaves the synovial mucin-type protein PRG4/lubricin (PubMed:32144329). Cleaves and activates IL36G which promotes expression of chemokines CXCL1 and CXLC8 in keratinocytes (PubMed:30804664). Cleaves IL33 into mature forms which have greater activity than the unprocessed form (PubMed:22307629). Cleaves coagulation factor F8 to produce a partially activated form (PubMed:18217133). Also cleaves and activates coagulation factor F10 (PubMed:8920993). Cleaves leukocyte cell surface protein SPN/CD43 to releases its extracellular domain and trigger its intramembrane proteolysis by gamma-secretase, releasing the CD43 cytoplasmic tail chain (CD43-ct) which translocates to the nucleus (PubMed:18586676). Cleaves CCL5/RANTES to produce RANTES(4-68) lacking the N-terminal three amino acids which exhibits reduced chemotactic and antiviral activities (PubMed:16963625). During apoptosis, cleaves SMARCA2/BRM to produce a 160 kDa cleavage product which localizes to the cytosol (PubMed:11259672). Cleaves myelin basic protein MBP in B cell lysosomes at '224-Phe-|-Lys-225' and '248-Phe-|-Ser-249', degrading the major immunogenic MBP epitope and preventing the activation of MBP-specific autoreactive T cells (PubMed:15100291). Cleaves annexin ANXA1 and antimicrobial peptide CAMP to produce peptides which act on neutrophil N-formyl peptide receptors to enhance the release of CXCL2 (PubMed:22879591). Acts as a ligand for the N-formyl peptide receptor FPR1, enhancing phagocyte chemotaxis (PubMed:15210802). Has antibacterial activity against the Gram-negative bacteria N.gonorrhoeae and P.aeruginosa (PubMed:2116408, PubMed:1937776). Likely to act against N.gonorrhoeae by interacting with N.gonorrhoeae penA/PBP2 (PubMed:2126324). Exhibits potent antimicrobial activity against the Gram-positive bacterium L.monocytogenes (PubMed:2117044). Has antibacterial activity against the Gram-positive bacterium S.aureus and degrades S.aureus biofilms, allowing polymorphonuclear leukocytes to penetrate the biofilm and phagocytose bacteria (PubMed:2117044, PubMed:32995850). Has antibacterial activity against M.tuberculosis (PubMed:15385470). Mediates CASP4 activation induced by the Td92 surface protein of the periodontal pathogen T.denticola, causing production and secretion of IL1A and leading to pyroptosis of gingival fibroblasts (PubMed:29077095).", "evidence": [ { "database": "UniProtKB", "id": "P08311", "url": "https://www.uniprot.org/uniprot/P08311#function" }, { "database": "PubMed", "id": "1861080", "url": "https://glygen.org/publication/PubMed/1861080" }, { "database": "PubMed", "id": "8194606", "url": "https://glygen.org/publication/PubMed/8194606" }, { "database": "PubMed", "id": "29077095", "url": "https://glygen.org/publication/PubMed/29077095" }, { "database": "PubMed", "id": "15100291", "url": "https://glygen.org/publication/PubMed/15100291" }, { "database": "PubMed", "id": "11259672", "url": "https://glygen.org/publication/PubMed/11259672" }, { "database": "PubMed", "id": "3390156", "url": "https://glygen.org/publication/PubMed/3390156" }, { "database": "UniProtKB", "id": "P28293", "url": "https://www.uniprot.org/uniprot/P28293#function" }, { "database": "PubMed", "id": "22307629", "url": "https://glygen.org/publication/PubMed/22307629" }, { "database": "PubMed", "id": "15210802", "url": "https://glygen.org/publication/PubMed/15210802" }, { "database": "PubMed", "id": "9000539", "url": "https://glygen.org/publication/PubMed/9000539" }, { "database": "PubMed", "id": "2117044", "url": "https://glygen.org/publication/PubMed/2117044" }, { "database": "PubMed", "id": "9536127", "url": "https://glygen.org/publication/PubMed/9536127" }, { "database": "PubMed", "id": "32995850", "url": "https://glygen.org/publication/PubMed/32995850" }, { "database": "PubMed", "id": "2126324", "url": "https://glygen.org/publication/PubMed/2126324" }, { "database": "PubMed", "id": "15385470", "url": "https://glygen.org/publication/PubMed/15385470" }, { "database": "PubMed", "id": "18217133", "url": "https://glygen.org/publication/PubMed/18217133" }, { "database": "PubMed", "id": "18586676", "url": "https://glygen.org/publication/PubMed/18586676" }, { "database": "PubMed", "id": "22879591", "url": "https://glygen.org/publication/PubMed/22879591" }, { "database": "PubMed", "id": "29652924", "url": "https://glygen.org/publication/PubMed/29652924" }, { "database": "PubMed", "id": "16963625", "url": "https://glygen.org/publication/PubMed/16963625" }, { "database": "PubMed", "id": "10702240", "url": "https://glygen.org/publication/PubMed/10702240" }, { "database": "PubMed", "id": "8920993", "url": "https://glygen.org/publication/PubMed/8920993" }, { "database": "PubMed", "id": "7744748", "url": "https://glygen.org/publication/PubMed/7744748" }, { "database": "PubMed", "id": "30804664", "url": "https://glygen.org/publication/PubMed/30804664" }, { "database": "PubMed", "id": "7842483", "url": "https://glygen.org/publication/PubMed/7842483" }, { "database": "PubMed", "id": "2116408", "url": "https://glygen.org/publication/PubMed/2116408" }, { "database": "PubMed", "id": "1937776", "url": "https://glygen.org/publication/PubMed/1937776" }, { "database": "PubMed", "id": "32144329", "url": "https://glygen.org/publication/PubMed/32144329" } ] }, { "annotation": "The protein encoded by this gene, a member of the peptidase S1 protein family, is found in azurophil granules of neutrophilic polymorphonuclear leukocytes. The encoded protease has a specificity similar to that of chymotrypsin C, and may participate in the killing and digestion of engulfed pathogens, and in connective tissue remodeling at sites of inflammation. In addition, the encoded protein is antimicrobial, with bacteriocidal activity against S. aureus and N. gonorrhoeae. Transcript variants utilizing alternative polyadenylation signals exist for this gene. [provided by RefSeq, Sep 2014].", "evidence": [ { "database": "RefSeq", "id": "NP_001902", "url": "https://www.ncbi.nlm.nih.gov/protein/NP_001902" } ] } ], "disease": [], "snv": [ { "evidence": [ { "id": "rs930621208", "database": "dbSNP", "url": "https://www.ncbi.nlm.nih.gov/SNP/snp_ref.cgi?type=rs&rs=rs930621208" }, { "id": "rs930621208", "database": "TOPMed", "url": "https://www.ncbi.nlm.nih.gov/snp/rs930621208#frequency_tab" } ], "glycoeffect": [ "n-glyco-sequon-loss", "n-glyco-sequon-gain" ], "start_pos": 71, "end_pos": 71, "sequence_org": "N", "sequence_mut": "S", "comment": "Germline mutation passed 1 out of 1 filters: n-glyco-sequon-loss (NVT->SVT); n-glyco-sequon-gain (NIN->NIS).", "chr_id": "14", "chr_pos": "24574802", "ref_nt": "C", "alt_nt": "null", "minor_allelic_frequency": "", "site_lbl": "N71", "keywords": [ "ebi", "germline" ] }, { "evidence": [ { "id": "rs930621208", "database": "dbSNP", "url": "https://www.ncbi.nlm.nih.gov/SNP/snp_ref.cgi?type=rs&rs=rs930621208" }, { "id": "rs930621208", "database": "TOPMed", "url": "https://www.ncbi.nlm.nih.gov/snp/rs930621208#frequency_tab" } ], "glycoeffect": [ "n-glyco-sequon-loss", "n-glyco-sequon-gain" ], "start_pos": 71, "end_pos": 71, "sequence_org": "N", "sequence_mut": "T", "comment": "Germline mutation passed 1 out of 1 filters: n-glyco-sequon-loss (NVT->TVT); n-glyco-sequon-gain (NIN->NIT).", "chr_id": "14", "chr_pos": "24574802", "ref_nt": "G", "alt_nt": "null", "minor_allelic_frequency": "", "site_lbl": "N71", "keywords": [ "ebi", "germline" ] }, { "evidence": [ { "id": "rs45567233", "database": "dbSNP", "url": "https://www.ncbi.nlm.nih.gov/SNP/snp_ref.cgi?type=rs&rs=rs45567233" }, { "id": "rs45567233", "database": "1000Genomes", "url": "https://www.ensembl.org/homo_sapiens/Variation/Explore?v=rs45567233" }, { "id": "rs45567233", "database": "ExAC", "url": "https://www.ncbi.nlm.nih.gov/SNP/snp_ref.cgi?type=rs&rs=rs45567233" }, { "id": "rs45567233", "database": "TOPMed", "url": "https://www.ncbi.nlm.nih.gov/snp/rs45567233#frequency_tab" }, { "id": "rs45567233", "database": "gnomAD", "url": "http://gnomad.broadinstitute.org/awesome?query=rs45567233" } ], "glycoeffect": [ "n-glyco-sequon-gain" ], "start_pos": 125, "end_pos": 125, "sequence_org": "N", "sequence_mut": "S", "comment": "Germline mutation passed 1 out of 1 filters: n-glyco-sequon-gain (NVN->NVS).", "chr_id": "14", "chr_pos": "24574465", "ref_nt": "C", "alt_nt": "null", "minor_allelic_frequency": "0.09086", "site_lbl": "N125", "keywords": [ "ebi", "germline" ] }, { "evidence": [ { "id": "P08311", "database": "BioMuta", "url": "https://hive.biochemistry.gwu.edu/biomuta/proteinview/P08311" } ], "glycoeffect": [ "n-glyco-sequon-gain" ], "start_pos": 211, "end_pos": 211, "subjects_tested": "0", "subjects_positive": "0", "frequency": "0.0", "sequence_org": "A", "sequence_mut": "T", "comment": "Somatic mutation passed 1 out of 6 filters: n-glyco-sequon-gain (NVA->NVT).", "chr_id": "14", "chr_pos": "24573774", "ref_nt": "C", "alt_nt": "T", "minor_allelic_frequency": "", "site_lbl": "A211", "disease": [ { "disease_id": "DOID:1324", "recommended_name": { "id": "DOID:1324", "resource": "Disease Ontology", "url": "http://disease-ontology.org/term/DOID:1324", "name": "lung cancer", "description": "A respiratory system cancer that is located_in the lung." }, "synonyms": [ { "id": "MONDO:0012159", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0012159", "name": "lung cancer susceptibility 1", "description": "" }, { "id": "MONDO:0012159", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0012159", "name": "LNCR1", "description": "" }, { "id": "MONDO:0012159", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0012159", "name": "lung cancer susceptibility", "description": "" }, { "id": "MONDO:0012159", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0012159", "name": "lung cancer susceptibility 1", "description": "" }, { "id": "MONDO:0012942", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0012942", "name": "lung cancer susceptibility 3", "description": "" }, { "id": "MONDO:0012942", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0012942", "name": "LNCR3", "description": "" }, { "id": "MONDO:0012942", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0012942", "name": "lung cancer susceptibility 3", "description": "" }, { "id": "MONDO:0012942", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0012942", "name": "adenocarcinoma of lung, susceptibility to", "description": "" }, { "id": "MONDO:0012955", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0012955", "name": "lung cancer susceptibility 4", "description": "" }, { "id": "MONDO:0012955", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0012955", "name": "LNCR4", "description": "" }, { "id": "MONDO:0012955", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0012955", "name": "lung cancer susceptibility 4", "description": "" }, { "id": "MONDO:0013631", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0013631", "name": "lung cancer susceptibility 5", "description": "" }, { "id": "MONDO:0013631", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0013631", "name": "LNCR5", "description": "" }, { "id": "MONDO:0013631", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0013631", "name": "lung cancer susceptibility 5", "description": "" }, { "id": "MONDO:0008903", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0008903", "name": "lung cancer", "description": "A malignant neoplasm involving the lung." }, { "id": "MONDO:0008903", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0008903", "name": "adenocarcinoma of lung, response to tyrosine kinase inhibitor in, autosomal dominant, somatic mutation", "description": "" }, { "id": "MONDO:0008903", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0008903", "name": "adenocarcinoma of lung, somatic", "description": "" }, { "id": "MONDO:0008903", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0008903", "name": "cancer of lung", "description": "" }, { "id": "MONDO:0008903", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0008903", "name": "lung cancer", "description": "" }, { "id": "MONDO:0008903", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0008903", "name": "lung cancer, protection against, autosomal dominant, somatic mutation", "description": "" }, { "id": "MONDO:0008903", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0008903", "name": "lung cancer, resistance to, autosomal dominant, somatic mutation", "description": "" }, { "id": "MONDO:0008903", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0008903", "name": "lung cancer, somatic", "description": "" }, { "id": "MONDO:0008903", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0008903", "name": "lung cancer, susceptibility to, autosomal dominant, somatic mutation", "description": "" }, { "id": "MONDO:0008903", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0008903", "name": "malignant lung neoplasm", "description": "" }, { "id": "MONDO:0008903", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0008903", "name": "malignant lung tumor", "description": "" }, { "id": "MONDO:0008903", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0008903", "name": "malignant lung tumour", "description": "" }, { "id": "MONDO:0008903", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0008903", "name": "malignant neoplasm of lung", "description": "" }, { "id": "MONDO:0008903", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0008903", "name": "malignant neoplasm of the lung", "description": "" }, { "id": "MONDO:0008903", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0008903", "name": "malignant tumor of lung", "description": "" }, { "id": "MONDO:0008903", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0008903", "name": "malignant tumor of the lung", "description": "" }, { "id": "MONDO:0008903", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0008903", "name": "malignant tumour of lung", "description": "" }, { "id": "MONDO:0008903", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0008903", "name": "malignant tumour of the lung", "description": "" }, { "id": "MONDO:0008903", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0008903", "name": "nonsmall cell lung cancer, response to tyrosine kinase inhibitor in, autosomal dominant, somatic mutation", "description": "" }, { "id": "MONDO:0008903", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0008903", "name": "nonsmall cell lung cancer, somatic", "description": "" }, { "id": "MONDO:0008903", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0008903", "name": "nonsmall cell lung cancer, susceptibility to, autosomal dominant, somatic mutation", "description": "" }, { "id": "MONDO:0008903", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0008903", "name": "Nonsmall cell lung cancer", "description": "" }, { "id": "MONDO:0008903", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0008903", "name": "alveolar cell carcinoma", "description": "" }, { "id": "MONDO:0008903", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0008903", "name": "lung cancer, protection against", "description": "" }, { "id": "MONDO:0008903", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0008903", "name": "lung neoplasm", "description": "" }, { "id": "MIM:211980", "resource": "MIM", "url": "https://www.omim.org/entry/211980", "name": "Lung cancer", "description": "Lung cancer" } ] } ], "keywords": [ "biomuta", "somatic", "cancer", "disease" ] }, { "evidence": [ { "id": "P08311", "database": "BioMuta", "url": "https://hive.biochemistry.gwu.edu/biomuta/proteinview/P08311" } ], "glycoeffect": [ "n-glyco-sequon-loss" ], "start_pos": 71, "end_pos": 71, "subjects_tested": "0", "subjects_positive": "0", "frequency": "0.0", "sequence_org": "N", "sequence_mut": "K", "comment": "Somatic mutation passed 1 out of 6 filters: n-glyco-sequon-loss (NVT->KVT).", "chr_id": "14", "chr_pos": "24574801", "ref_nt": "A", "alt_nt": "C", "minor_allelic_frequency": "", "site_lbl": "N71", "disease": [ { "disease_id": "DOID:1781", "recommended_name": { "id": "DOID:1781", "resource": "Disease Ontology", "url": "http://disease-ontology.org/term/DOID:1781", "name": "thyroid cancer", "description": "An endocrine gland cancer located in the thryoid gland located in the neck below the thyroid cartilage." }, "synonyms": [ { "id": "DOID:1781", "resource": "Disease Ontology", "url": "http://disease-ontology.org/term/DOID:1781", "name": "thyroid gland cancer", "description": "" }, { "id": "DOID:1781", "resource": "Disease Ontology", "url": "http://disease-ontology.org/term/DOID:1781", "name": "Thyroid gland neoplasm", "description": "" }, { "id": "DOID:1781", "resource": "Disease Ontology", "url": "http://disease-ontology.org/term/DOID:1781", "name": "malignant neoplasm of thyroid gland", "description": "" }, { "id": "DOID:1781", "resource": "Disease Ontology", "url": "http://disease-ontology.org/term/DOID:1781", "name": "malignant tumour of thyroid gland", "description": "" }, { "id": "DOID:1781", "resource": "Disease Ontology", "url": 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(paucimannose) asparagine; alternate", "start_pos": 71, "start_aa": "Asn", "end_pos": 71, "end_aa": "Asn", "residue": "Asn", "site_lbl": "Asn71", "evidence": [ { "id": "P08311", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P08311#ptm_processing" }, { "id": "26274980", "database": "PubMed", "url": "https://glygen.org/publication/PubMed/26274980" } ] }, { "glytoucan_ac": "G49108TO", "type": "O-linked", "subtype": "O-GlcNAcylation", "site_category": "reported_with_glycan", "site_seq": "", "relation": "attached", "comment": "O-GlcNAcylation", "evidence": [ { "id": "P08311", "database": "O-GlcNAc Database", "url": "https://www.oglcnac.mcw.edu/search/?query_protein=P08311" }, { "id": "30379171", "database": "PubMed", "url": "https://glygen.org/publication/PubMed/30379171" } ] } ], "phosphorylation": [], "glycation": [], "keywords": [ "enzyme", "glycoprotein", "glycoprotein_reported", "glycoprotein_reported_with_glycan" ], "publication": [ { "title": "N-Linked glycosylation and sialylation of the acid-labile subunit. Role in complex formation with insulin-like growth factor (IGF)-binding protein-3 and the IGFs.", "journal": "The Journal of biological chemistry", "date": "1999", "authors": "Janosi JB, Firth SM, Bond JJ, Baxter RC, Delhanty PJ", "evidence": [ { "database": "Reactome", "id": "R-HSA-381426", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-381426" } ], "reference": [ { "type": "PubMed", "id": "10026136", "url": "https://glygen.org/publication/PubMed/10026136" } ] }, { "title": "The insulin-like growth factor (IGF)-dependent IGF binding protein-4 protease secreted by human fibroblasts is pregnancy-associated plasma protein-A.", "journal": "Proceedings of the National Academy of Sciences of the United States of America", "date": "1999", "authors": "Lawrence JB, Oxvig C, Overgaard MT, Sottrup-Jensen L, Gleich GJ, Hays LG, Yates JR 3rd, Conover CA", "evidence": [ { "database": "Reactome", "id": "R-HSA-381426", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-381426" } ], "reference": [ { "type": "PubMed", "id": "10077652", "url": "https://glygen.org/publication/PubMed/10077652" } ] }, { "title": "The cleavage site specificity of human prostate specific antigen for insulin-like growth factor binding protein-3.", "journal": "FEBS letters", "date": "1999", "authors": "Okabe E, Kajihara J, Usami Y, Hirano K", "evidence": [ { "database": "Reactome", "id": "R-HSA-381426", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-381426" } ], "reference": [ { "type": "PubMed", "id": "10218588", "url": "https://glygen.org/publication/PubMed/10218588" } ] }, { "title": "Fibrillin degradation by matrix metalloproteinases: implications for connective tissue remodelling.", "journal": "The Biochemical journal", "date": "1999", "authors": "Ashworth JL, Murphy G, Rock MJ, Sherratt MJ, Shapiro SD, Shuttleworth CA, Kielty CM", "evidence": [ { "database": "Reactome", "id": "R-HSA-1474228", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-1474228" } ], "reference": [ { "type": "PubMed", "id": "10229672", "url": "https://glygen.org/publication/PubMed/10229672" } ] }, { "title": "Fibrillin degradation by matrix metalloproteinases: identification of amino- and carboxy-terminal cleavage sites.", "journal": "FEBS letters", "date": "1999", "authors": "Hindson VJ, Ashworth JL, Rock MJ, Cunliffe S, Shuttleworth CA, Kielty CM", "evidence": [ { "database": "Reactome", "id": "R-HSA-1474228", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-1474228" } ], "reference": [ { "type": "PubMed", "id": "10386589", "url": "https://glygen.org/publication/PubMed/10386589" } ] }, { "title": "Inflammation-related neutrophil proteases, cathepsin G and elastase, function as insulin-like growth factor binding protein proteases.", "journal": "Growth hormone & IGF research : official journal of the Growth Hormone Research Society and the International IGF Research Society", "date": "1999", "authors": "Gibson TL, Cohen P", "evidence": [ { "database": "Reactome", "id": "R-HSA-381426", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-381426" } ], "reference": [ { "type": "PubMed", "id": "10512690", "url": "https://glygen.org/publication/PubMed/10512690" } ] }, { "title": "Mixed-type inhibition of pulmonary angiotensin I-converting enzyme by captopril, enalaprilat and ramiprilat.", "journal": "Journal of enzyme inhibition", "date": "1999", "authors": "Baudin B, Beneteau-Burnat B", "evidence": [ { "database": "Reactome", "id": "R-HSA-2022377", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-2022377" } ], "reference": [ { "type": "PubMed", "id": "10536878", "url": "https://glygen.org/publication/PubMed/10536878" } ] }, { "title": "A central domain binding site in insulin-like growth factor binding protein-5 for the acid-labile subunit.", "journal": "Endocrinology", "date": "2000", "authors": "Twigg SM, Kiefer MC, Zapf J, Baxter RC", "evidence": [ { "database": "Reactome", "id": "R-HSA-381426", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-381426" } ], "reference": [ { "type": "PubMed", "id": "10614670", "url": "https://glygen.org/publication/PubMed/10614670" } ] }, { "title": "Insulin-like growth factor binding protein (IGFBP)-3-bound IGF-I and IGFBP-3-bound IGF-II in growth hormone deficiency.", "journal": "Hormone research", "date": "1999", "authors": "Belgorosky A, Rivarola MA", "evidence": [ { "database": "Reactome", "id": "R-HSA-381426", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-381426" } ], "reference": [ { "type": "PubMed", "id": "10681634", "url": "https://glygen.org/publication/PubMed/10681634" } ] }, { "title": "Cathepsin G activates protease-activated receptor-4 in human platelets.", "journal": "The Journal of biological chemistry", "date": "2000-03-10", "authors": "Sambrano G R, Huang W, Faruqi T, Mahrus S, Craik C, Coughlin S R", "evidence": [ { "database": "UniProtKB", "id": "P08311", "url": "https://www.uniprot.org/uniprot/P08311" } ], "reference": [ { "type": "PubMed", "id": "10702240", "url": "https://glygen.org/publication/PubMed/10702240" } ] }, { "title": "EMMPRIN (CD147), an inducer of matrix metalloproteinase synthesis, also binds interstitial collagenase to the tumor cell surface.", "journal": "Cancer research", "date": "2000", "authors": "Guo H, Li R, Zucker S, Toole BP", "evidence": [ { "database": "Reactome", "id": "R-HSA-1474228", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-1474228" } ], "reference": [ { "type": "PubMed", "id": "10706100", "url": "https://glygen.org/publication/PubMed/10706100" } ] }, { "title": "Biochemical characterization of the catalytic domain of human matrix metalloproteinase 19. Evidence for a role as a potent basement membrane degrading enzyme.", "journal": "The Journal of biological chemistry", "date": "2000", "authors": "Stracke JO, Hutton M, Stewart M, Pendas AM, Smith B, Lopez-Otin C, Murphy G, Knauper V", "evidence": [ { "database": "Reactome", "id": "R-HSA-1474228", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-1474228" } ], "reference": [ { "type": "PubMed", "id": "10809722", "url": "https://glygen.org/publication/PubMed/10809722" } ] }, { "title": "Binding characteristics of pro-insulin-like growth factor-II from cancer patients: binary and ternary complex formation with IGF binding proteins-1 to -6.", "journal": "The Journal of endocrinology", "date": "2000", "authors": "Bond JJ, Meka S, Baxter RC", "evidence": [ { "database": "Reactome", "id": "R-HSA-381426", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-381426" } ], "reference": [ { "type": "PubMed", "id": "10810289", "url": "https://glygen.org/publication/PubMed/10810289" } ] }, { "title": "Evidence that the interaction between insulin-like growth factor (IGF)-II and IGF binding protein (IGFBP)-4 is essential for the action of the IGF-II-dependent IGFBP-4 protease.", "journal": "Archives of biochemistry and biophysics", "date": "2000", "authors": "Qin X, Byun D, Lau KH, Baylink DJ, Mohan S", "evidence": [ { "database": "Reactome", "id": "R-HSA-381426", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-381426" } ], "reference": [ { "type": "PubMed", "id": "10898936", "url": "https://glygen.org/publication/PubMed/10898936" } ] }, { "title": "Angiotensin II generation by mast cell alpha- and beta-chymases.", "journal": "Biochimica et biophysica acta", "date": "2000", "authors": "Caughey GH, Raymond WW, Wolters PJ", "evidence": [ { "database": "Reactome", "id": "R-HSA-2022377", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-2022377" } ], "reference": [ { "type": "PubMed", "id": "10899625", "url": "https://glygen.org/publication/PubMed/10899625" } ] }, { "title": "Effects of IGFBP-2 overexpression in vitro and in vivo.", "journal": "Pediatric nephrology (Berlin, Germany)", "date": "2000", "authors": "Wolf E, Lahm H, Wu M, Wanke R, Hoeflich A", "evidence": [ { "database": "Reactome", "id": "R-HSA-381426", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-381426" } ], "reference": [ { "type": "PubMed", "id": "10912521", "url": "https://glygen.org/publication/PubMed/10912521" } ] }, { "title": "A human homolog of angiotensin-converting enzyme. Cloning and functional expression as a captopril-insensitive carboxypeptidase.", "journal": "The Journal of biological chemistry", "date": "2000", "authors": "Tipnis SR, Hooper NM, Hyde R, Karran E, Christie G, Turner AJ", "evidence": [ { "database": "Reactome", "id": "R-HSA-2022377", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-2022377" } ], "reference": [ { "type": "PubMed", "id": "10924499", "url": "https://glygen.org/publication/PubMed/10924499" } ] }, { "title": "O-glycosylation of insulin-like growth factor (IGF) binding protein-6 maintains high IGF-II binding affinity by decreasing binding to glycosaminoglycans and susceptibility to proteolysis.", "journal": "European journal of biochemistry", "date": "2000", "authors": "Marinaro JA, Neumann GM, Russo VC, Leeding KS, Bach LA", "evidence": [ { "database": "Reactome", "id": "R-HSA-381426", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-381426" } ], "reference": [ { "type": "PubMed", "id": "10951195", "url": 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(Baltimore, Md. : 1950)", "date": "2000", "authors": "Ernst WA, Thoma-Uszynski S, Teitelbaum R, Ko C, Hanson DA, Clayberger C, Krensky AM, Leippe M, Bloom BR, Ganz T, Modlin RL", "evidence": [ { "database": "Reactome", "id": "R-HSA-6803157", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-6803157" } ], "reference": [ { "type": "PubMed", "id": "11120840", "url": "https://glygen.org/publication/PubMed/11120840" } ] }, { "title": "Pregnancy-associated plasma protein-A accounts for the insulin-like growth factor (IGF)-binding protein-4 (IGFBP-4) proteolytic activity in human pregnancy serum and enhances the mitogenic activity of IGF by degrading IGFBP-4 in vitro.", "journal": "The Journal of clinical endocrinology and metabolism", "date": "2001", "authors": "Byun D, Mohan S, Yoo M, Sexton C, Baylink DJ, Qin X", "evidence": [ { "database": "Reactome", "id": "R-HSA-381426", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-381426" } ], "reference": [ { "type": "PubMed", "id": 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"https://www.uniprot.org/uniprot/P08311" } ], "reference": [ { "type": "PubMed", "id": "11259672", "url": "https://glygen.org/publication/PubMed/11259672" } ] }, { "title": "Pregnancy-associated plasma protein-A2 (PAPP-A2), a novel insulin-like growth factor-binding protein-5 proteinase.", "journal": "The Journal of biological chemistry", "date": "2001", "authors": "Overgaard MT, Boldt HB, Laursen LS, Sottrup-Jensen L, Conover CA, Oxvig C", "evidence": [ { "database": "Reactome", "id": "R-HSA-381426", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-381426" } ], "reference": [ { "type": "PubMed", "id": "11264294", "url": "https://glygen.org/publication/PubMed/11264294" } ] }, { "title": "Differential assembly of rat purinergic P2X7 receptor in immune cells of the brain and periphery.", "journal": "The Journal of biological chemistry", "date": "2001", "authors": "Kim M, Spelta V, Sim J, North RA, Surprenant A", "evidence": [ { "database": "Reactome", "id": "R-HSA-9660826", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9660826" } ], "reference": [ { "type": "PubMed", "id": "11313357", "url": "https://glygen.org/publication/PubMed/11313357" } ] }, { "title": "Human intelectin is a novel soluble lectin that recognizes galactofuranose in carbohydrate chains of bacterial cell wall.", "journal": "The Journal of biological chemistry", "date": "2001", "authors": "Tsuji S, Uehori J, Matsumoto M, Suzuki Y, Matsuhisa A, Toyoshima K, Seya T", "evidence": [ { "database": "Reactome", "id": "R-HSA-6803157", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-6803157" } ], "reference": [ { "type": "PubMed", "id": "11313366", "url": "https://glygen.org/publication/PubMed/11313366" } ] }, { "title": "Mutagenesis of basic amino acids in the carboxyl-terminal region of insulin-like growth factor binding protein-5 affects acid-labile subunit binding.", "journal": "Endocrinology", "date": "2001", "authors": "Firth SM, Clemmons DR, Baxter RC", "evidence": [ { "database": 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Hiemstra PS, Borregaard N", "evidence": [ { "database": "Reactome", "id": "R-HSA-6803157", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-6803157" } ], "reference": [ { "type": "PubMed", "id": "11389039", "url": "https://glygen.org/publication/PubMed/11389039" } ] }, { "title": "Functional evidence for a role of vascular chymase in the production of angiotensin II in isolated human arteries.", "journal": "Circulation", "date": "2001", "authors": "Richard V, Hurel-Merle S, Scalbert E, Ferry G, Lallemand F, Bessou JP, Thuillez C", "evidence": [ { "database": "Reactome", "id": "R-HSA-2022377", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-2022377" } ], "reference": [ { "type": "PubMed", "id": "11502696", "url": "https://glygen.org/publication/PubMed/11502696" } ] }, { "title": "Pregnancy-associated plasma protein-A (PAPP-A) cleaves insulin-like growth factor binding protein (IGFBP)-5 independent of IGF: implications for the mechanism of IGFBP-4 proteolysis by PAPP-A.", "journal": "FEBS letters", "date": "2001", "authors": "Laursen LS, Overgaard MT, Soe R, Boldt HB, Sottrup-Jensen L, Giudice LC, Conover CA, Oxvig C", "evidence": [ { "database": "Reactome", "id": "R-HSA-381426", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-381426" } ], "reference": [ { "type": "PubMed", "id": "11522292", "url": "https://glygen.org/publication/PubMed/11522292" } ] }, { "title": "Insulin-like growth factor-binding protein-5 inhibits growth and induces differentiation of mouse osteosarcoma cells.", "journal": "Biochemical and biophysical research communications", "date": "2001", "authors": "Schneider MR, Zhou R, Hoeflich A, Krebs O, Schmidt J, Mohan S, Wolf E, Lahm H", "evidence": [ { "database": "Reactome", "id": "R-HSA-381426", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-381426" } ], "reference": [ { "type": "PubMed", "id": "11606061", "url": "https://glygen.org/publication/PubMed/11606061" } ] }, { "title": "IGFBP-3 binding to endothelial cells inhibits plasmin and thrombin proteolysis.", "journal": "American journal of physiology. 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"UniProtKB", "id": "P08311", "url": "https://www.uniprot.org/uniprot/P08311" } ], "pmid": "" }, { "name": "peptidase activity", "id": "GO:0008233", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0008233", "evidence": [ { "database": "UniProtKB", "id": "P08311", "url": "https://www.uniprot.org/uniprot/P08311" } ], "pmid": "" }, { "name": "receptor ligand activity", "id": "GO:0048018", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0048018", "evidence": [ { "database": "UniProtKB", "id": "P08311", "url": "https://www.uniprot.org/uniprot/P08311" } ], "pmid": "" }, { "name": "caspase binding", "id": "GO:0089720", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0089720", "evidence": [ { "database": "UniProtKB", "id": "P08311", "url": "https://www.uniprot.org/uniprot/P08311" } ], "pmid": "" }, { "name": "serine-type peptidase activity", "id": "GO:0008236", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0008236", "evidence": [ { "database": "UniProtKB", "id": "P08311", "url": "https://www.uniprot.org/uniprot/P08311" } ], "pmid": "" } ] }, { "name": "Cellular Component", "total": 14, "go_terms": [ { "name": "extracellular region", "id": "GO:0005576", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0005576", "evidence": [ { "database": "UniProtKB", "id": "P08311", "url": "https://www.uniprot.org/uniprot/P08311" } ], "pmid": "" }, { "name": "extracellular space", "id": "GO:0005615", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0005615", "evidence": [ { "database": "UniProtKB", "id": "P08311", "url": "https://www.uniprot.org/uniprot/P08311" } ], "pmid": "" }, { "name": "nucleus", "id": "GO:0005634", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0005634", "evidence": [ { "database": "UniProtKB", "id": "P08311", "url": "https://www.uniprot.org/uniprot/P08311" } ], "pmid": "" }, { "name": "cytoplasm", "id": "GO:0005737", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0005737", "evidence": [ { "database": "UniProtKB", "id": "P08311", "url": "https://www.uniprot.org/uniprot/P08311" } ], "pmid": "" }, { "name": "cytosol", "id": "GO:0005829", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0005829", "evidence": [ { "database": "UniProtKB", "id": "P08311", "url": "https://www.uniprot.org/uniprot/P08311" } ], "pmid": "" }, { "name": "plasma membrane", "id": "GO:0005886", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0005886", "evidence": [ { "database": "UniProtKB", "id": "P08311", "url": "https://www.uniprot.org/uniprot/P08311" } ], "pmid": "" }, { "name": "membrane", "id": "GO:0016020", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0016020", "evidence": [ { "database": "UniProtKB", "id": "P08311", "url": "https://www.uniprot.org/uniprot/P08311" } ], "pmid": "" }, { "name": "secretory granule", "id": "GO:0030141", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0030141", "evidence": [ { "database": "UniProtKB", "id": "P08311", "url": "https://www.uniprot.org/uniprot/P08311" } ], "pmid": "" }, { "name": "intracellular membrane-bounded organelle", "id": "GO:0043231", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0043231", "evidence": [ { "database": "UniProtKB", "id": "P08311", "url": "https://www.uniprot.org/uniprot/P08311" } ], "pmid": "" }, { "name": "extracellular exosome", "id": "GO:0070062", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0070062", "evidence": [ { "database": "UniProtKB", "id": "P08311", "url": "https://www.uniprot.org/uniprot/P08311" } ], "pmid": "" }, { "name": "lysosome", "id": "GO:0005764", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0005764", "evidence": [ { "database": "UniProtKB", "id": "P08311", "url": "https://www.uniprot.org/uniprot/P08311" } ], "pmid": "" }, { "name": "azurophil granule lumen", "id": "GO:0035578", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0035578", "evidence": [ { "database": "UniProtKB", "id": "P08311", "url": "https://www.uniprot.org/uniprot/P08311" } ], "pmid": "" }, { "name": "cytoplasmic stress granule", "id": "GO:0010494", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0010494", "evidence": [ { "database": "UniProtKB", "id": "P08311", "url": "https://www.uniprot.org/uniprot/P08311" } ], "pmid": "" }, { "name": "collagen-containing extracellular matrix", "id": "GO:0062023", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0062023", "evidence": [ { "database": "UniProtKB", "id": "P08311", "url": "https://www.uniprot.org/uniprot/P08311" } ], "pmid": "" } ] }, { "name": "Biological Process", "total": 22, "go_terms": [ { "name": "protein phosphorylation", "id": "GO:0006468", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0006468", "evidence": [ { "database": "UniProtKB", "id": "P08311", "url": "https://www.uniprot.org/uniprot/P08311" } ], "pmid": "" }, { "name": "proteolysis", "id": "GO:0006508", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0006508", "evidence": [ { "database": "UniProtKB", "id": "P08311", "url": "https://www.uniprot.org/uniprot/P08311" } ], "pmid": "" }, { "name": "immune response", "id": "GO:0006955", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0006955", "evidence": [ { "database": "UniProtKB", "id": "P08311", "url": "https://www.uniprot.org/uniprot/P08311" } ], "pmid": "" }, { "name": "protein processing", "id": "GO:0016485", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0016485", "evidence": [ { "database": "UniProtKB", "id": "P08311", "url": "https://www.uniprot.org/uniprot/P08311" } ], "pmid": "" }, { "name": "antibacterial humoral response", "id": "GO:0019731", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0019731", "evidence": [ { "database": "UniProtKB", "id": "P08311", "url": "https://www.uniprot.org/uniprot/P08311" } ], "pmid": "" }, { "name": "extracellular matrix disassembly", "id": "GO:0022617", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0022617", "evidence": [ { "database": "UniProtKB", "id": "P08311", "url": "https://www.uniprot.org/uniprot/P08311" } ], "pmid": "" }, { "name": "defense response to Gram-negative bacterium", "id": "GO:0050829", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0050829", "evidence": [ { "database": "UniProtKB", "id": "P08311", "url": "https://www.uniprot.org/uniprot/P08311" } ], "pmid": "" }, { "name": "defense response to Gram-positive bacterium", "id": "GO:0050830", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0050830", "evidence": [ { "database": "UniProtKB", "id": "P08311", "url": "https://www.uniprot.org/uniprot/P08311" } ], "pmid": "" }, { "name": "angiotensin maturation", "id": "GO:0002003", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0002003", "evidence": [ { "database": "UniProtKB", "id": "P08311", "url": "https://www.uniprot.org/uniprot/P08311" } ], "pmid": "" }, { "name": "cellular response to lipopolysaccharide", "id": "GO:0071222", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0071222", "evidence": [ { "database": "UniProtKB", "id": "P08311", "url": "https://www.uniprot.org/uniprot/P08311" } ], "pmid": "" }, { "name": "platelet activation", "id": "GO:0030168", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0030168", "evidence": [ { "database": "UniProtKB", "id": "P08311", "url": "https://www.uniprot.org/uniprot/P08311" } ], "pmid": "" }, { "name": "purinergic nucleotide receptor signaling pathway", "id": "GO:0035590", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0035590", "evidence": [ { "database": "UniProtKB", "id": "P08311", "url": "https://www.uniprot.org/uniprot/P08311" } ], "pmid": "" }, { "name": "monocyte chemotaxis", "id": "GO:0002548", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0002548", "evidence": [ { "database": "UniProtKB", "id": "P08311", "url": "https://www.uniprot.org/uniprot/P08311" } ], "pmid": "" }, { "name": "cytokine-mediated signaling pathway", "id": "GO:0019221", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0019221", "evidence": [ { "database": "UniProtKB", "id": "P08311", "url": "https://www.uniprot.org/uniprot/P08311" } ], "pmid": "" }, { "name": "positive regulation of immune response", "id": "GO:0050778", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0050778", "evidence": [ { "database": "UniProtKB", "id": "P08311", "url": "https://www.uniprot.org/uniprot/P08311" } ], "pmid": "" }, { "name": "defense response to fungus", "id": "GO:0050832", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0050832", "evidence": [ { "database": "UniProtKB", "id": "P08311", "url": "https://www.uniprot.org/uniprot/P08311" } ], "pmid": "" }, { "name": "neutrophil-mediated killing of gram-positive bacterium", "id": "GO:0070946", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0070946", "evidence": [ { "database": "UniProtKB", "id": "P08311", "url": "https://www.uniprot.org/uniprot/P08311" } ], "pmid": "" }, { "name": "negative regulation of T cell activation", "id": "GO:0050868", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0050868", "evidence": [ { "database": "UniProtKB", "id": "P08311", "url": "https://www.uniprot.org/uniprot/P08311" } ], "pmid": "" }, { "name": "neutrophil activation", "id": "GO:0042119", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0042119", "evidence": [ { "database": "UniProtKB", "id": "P08311", "url": "https://www.uniprot.org/uniprot/P08311" } ], "pmid": "" }, { "name": "positive regulation of platelet aggregation", "id": "GO:1901731", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:1901731", "evidence": [ { "database": "UniProtKB", "id": "P08311", "url": "https://www.uniprot.org/uniprot/P08311" } ], "pmid": "" }, { "name": "protein metabolic process", "id": "GO:0019538", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0019538", "evidence": [ { "database": "UniProtKB", "id": "P08311", "url": "https://www.uniprot.org/uniprot/P08311" } ], "pmid": "" }, { "name": "biofilm matrix disassembly", "id": "GO:0098786", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0098786", "evidence": [ { "database": "UniProtKB", "id": "P08311", "url": "https://www.uniprot.org/uniprot/P08311" } ], "pmid": "" } ] } ] }, "pro_annotation": [], "site_annotation": [ { "start_pos": 71, "end_pos": 73, "annotation": "n_glycosylation_sequon" } ], "ptm_annotation": [ { "annotation": "Two C-terminal truncation variants have been identified, one which ends at Arg-243 and one which ends at Ser-244.", "evidence": [ { "database": "UniProtKB", "id": "P08311", "url": "https://www.uniprot.org/uniprot/P08311" }, { "database": "PubMed", "id": "26274980", "url": "https://glygen.org/publication/PubMed/26274980" } ] } ], "interactions": [], "reactions": [ { "id": "R-HSA-1592316", "name": "Initial activation of proMMP1", "equation": "", "summary": "ProMMP1 has several activators including plasmin (Eeckhout & Vaes 1977, Werb et al. 1977, Santala et al. 1999), trypsin (Grant et al. 1987, Saunders et al. 2005), plasma kallikrein (Nagase et al. 1982, Saunders et al. 2005), chymase (Saarinen et al. 1994, Suzuki et al. 1995, Saunders et al. 2005), tryptase (Gruber et al. 1989, Suzuki et al. 1995, Saunders et al. 2005), neutrophil elastase, cathepsin G (Saunders et al. 2005) and trypsin-2 (Moilanen et al. 2003). Concanavalin A (ConA) was the first cellular treatment that yielded active MMPs in culture, inducing the cellular activation of MMP1 likely through MMP14 activity (Overall and Sodek 1990).Trypsin-like serine proteinases are believed to remove 34-36 residues from the N-terminus of the secreted pro-enzyme, equivalent to positions 53-55 of the UniProt cannonical sequence which includes a signal peptide. Removal of this region is sufficient to destabilize the Cys92-Zn2+ stabilizing bond (numbered according to the Uniprot canonical sequence, Cys73 when numbered from the N terminus of the secreted peptide as typically represented in the literature) and partially activate enzyme activity. This intermediate form then undergoes autocatalysis at Thr83-Leu84 producing an MMP1 with about 20% of full collagenase activity (Suzuki et al. 1990). Full activation is brought about by a further cleavage at Gln99-Phe100. When first reported, considerable debate surrounded the activation of this archetypical MMP. Divergence of opinion resulted when competing groups studied activation in vitro using chemicals (organomercurials such as aminophenylmecuricacetate), which yield a different autolytic cleavage site in the protease susceptible loop when compared with the site cut by serine proteases such as trypsin. Different specific activities result, but in general the final autolytic cleavage site for all MMPs is the homologous Phe or Tyr at position 100 or 101. When the active enzyme commences here, full activity is realised due to the salt bridge forming between the N-terminal primary amine of the conserved Phe or Tyr with an Asp on helix C that in turn salt bridges to the active site Glu. Termini either side of this position do not result in full activity.", "cellular_location": "extracellular region", "input_participant_list": [ "R-HSA-1602455" ], "output_participant_list": [ "R-HSA-1602470", "R-HSA-1602471" ], "enzyme_list": [ "P08246-1", "P03956-1", "P00747-1", "P08311-1", "Q15661-1", "P07478-1", "P03952-1", "P23946-1", "P07477-1" ], "evidence": [ { "id": "R-HSA-1592316", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-1592316" } ] }, { "id": "R-HSA-1604722", "name": "Activation of proMMP9 by proteases", "equation": "", "summary": "proMMP9 can be activated by trypsin and chymotrypsin (Sopata & Dancewicz 1974), tissue kallikrein (Tschesche et al. 1989, Desrivieres et al. 1993), cathepsin G (Murphy et al. 1980), and trypsin-2 (Sorsa et al. 1997). This appears to be a one-step activation; the single peptide bond cleaved by trypsin-2 in proMMP-9 is Arg106-Phe107. Modes of activation by other proteases are unclear. Activation is inhibited by endostatin (Nyberg et al. 2003).", "cellular_location": "extracellular region", "input_participant_list": [], "output_participant_list": [ "R-HSA-1604713", "R-HSA-668812" ], "enzyme_list": [ "P17538-1", "P08311-1", "P14780-1", "P07478-1", "P20151-1", "P07477-1" ], "evidence": [ { "id": "R-HSA-1604722", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-1604722" } ] }, { "id": "R-HSA-2022411", "name": "Cathepsin G hydrolyzes Angiotensin-(1-10) to Angiotensin-(1-8)", "equation": "", "summary": "Cathepsin G hydrolyzes angiotensin-(1-10) (angiotensin I) to yield angiotensin-(1-8) (angiotensin II) (Reilly et al. 1982, Owen and Campbell 1998, Raymond et al. 2010). Cathepsin bound to the plasma membrane of neutrophils has a higher activity than does soluble cathepsin G (Owen and Campbell 1998).", "cellular_location": "extracellular region, plasma membrane", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "P20718-1", "P08311-1" ], "evidence": [ { "id": "R-HSA-2022411", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-2022411" } ] }, { "id": "R-HSA-3785684", "name": "Fibronectin degradation by CTSG", "equation": "", "summary": "Plasma fibronectin (FN1) is degraded by cathepsin G (CTSG) into a characteristic pattern of gelatin-binding peptides of M, = 64000, 40000, and 30000 (Vartio et al. 1981, Vartio 1982). CTSG is activated by UV exposure and can activate matrix metalloproteinases MMP1 and MMP2, but increased levels of MMP activity did not correlate with increased FN degradation in normal human fibroblasts (NHFs) following exposure to UVB (50 mJ/cm2) irradiation, while addtion of CTSG inhibitor decreased FN degradation, suggesting that CTSG is directly responsible for FN1 degradation (Son et al. 2009).", "cellular_location": "plasma membrane", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "P08311-1" ], "evidence": [ { "id": "R-HSA-3785684", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-3785684" } ] }, { "id": "R-HSA-381500", "name": "Cathepsin G proteolyzes IGF:IGFBP3:ALS", "equation": "", "summary": "Cathepsin G cleaves IGFBP-3 between amino acids 168 and 169 and between amino acids 226 and 227, releasing IGF from the IGF:IGFBP-3:ALS Complex.", "cellular_location": "extracellular region, plasma membrane", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "P20718-1", "P08311-1" ], "evidence": [ { "id": "R-HSA-381500", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-381500" } ] }, { "id": "R-HSA-448678", "name": "CTSG cleaves CASP1(1-404)", "equation": "", "summary": "Caspase 1 is expressed as a precursor that is cleaved to generate the p10 and p20 subunits that subsequently form the active tetramer.", "cellular_location": "cytosol", "input_participant_list": [], "output_participant_list": [ "R-HSA-448674", "R-HSA-448680" ], "enzyme_list": [ "P29466-1", "P08311-1" ], "evidence": [ { "id": "R-HSA-448678", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-448678" } ] }, { "id": "R-HSA-6798751", "name": "Exocytosis of azurophil granule lumen proteins", "equation": "", "summary": "Azurophil or primary granules were originally defined by their high content of myeloperoxidase (MPO) and their affinity for the basic dye azure A (Spicer & Hardin 1969). Azurophil granules are generally described as spherical. Like lysosomes, they contain CD63 in their membrane (Cham et al. 1994) but are regarded as specialized secretory granules rather than lysosomes (Cieutat et al. 1998). Azurophil granules undergo limited exocytosis in response to stimulation (Sengelov et al. 1993, Faurschou et al. 2002), their primary role is believed to be killing and degradation of engulfed microbes in the phagolysosome (Joiner et al. 1989).; ; MPO reacts with H2O2 formed by NADPH oxidase, increasing its toxicity by formation of hypochlorous acid and other chlorination products, tyrosine radicals and reactive nitrogen intermediates which attack the surface of microbes (Klebanoff et al. 2013).;", "cellular_location": "extracellular region, azurophil granule lumen", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "Q05655-1", "P07686-1", "P12724-1", "P04066-1", "Q92820-1", "Q6XQN6-1", "Q99536-1", "Q9BRF8-1", "Q9UHL4-1", "P08246-1", "P34059-1", "P15586-1", "P24158-1", "Q9Y2J8-1", "P10619-1", "O00584-1", "P53396-1", "P55072-1", "P06280-1", "P28482-1", "Q9NZK5-1", "P20933-1", "P05089-1", "P15289-1", "P15848-1", "P16278-1", "Q9H7Z7-1", "P53634-1", "P08311-1", "Q9BTY2-1", "P00387-1", "P30041-1", "P05164-1", "Q8NBS9-1", "P11216-1", "P10153-1", "P61626-1", "P08236-1", "P42685-1", "P07478-1", "O00754-1", "P20839-1" ], "evidence": [ { "id": "R-HSA-6798751", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-6798751" } ] }, { "id": "R-HSA-6813659", "name": "ELANE, CTSG or PRTN3 binds bacteria", "equation": "", "summary": "Polymorphonuclear neutrophils (PMNs) are the most abundant circulating blood leukocytes that are rapidly recruited to sites of infection by host- and/or pathogen-derived components. PMNs provide the first-line defense against infection killing invading pathogens and resolving the inflammation they cause (Kobayashi SD et al. 2005). Activated neutrophils are known to release a variety of molecules, including the neutrophil serine proteases such as neutrophil elastase (ELINE), proteinase 3 (PRTN3) and cathepsin G (CTSG) (Garwicz D et al. 2005). Neutrophil serine proteases contribute to antimicrobial defense by ", "cellular_location": "extracellular region, plasma membrane", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "P08246-1", "P24158-1", "P08311-1" ], "evidence": [ { "id": "R-HSA-6813659", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-6813659" } ] }, { "id": "R-HSA-9635424", "name": "Rv3364c binds cathepsin G", "equation": "", "summary": "Mtb secretes serine protease inhibitor Rv3364c (Rv3364c) protein into the phagocyte's cytosol which blocks the serine protease activity of human cathepsin G (CTSG), inhibiting the cleavage of caspase-1 (Danelishvili et al. 2011).", "cellular_location": "cytosol", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "P08311-1" ], "evidence": [ { "id": "R-HSA-9635424", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9635424" } ] } ], "reaction_participants": [ { "participant_id": "R-HSA-1602455", "participant_name": "MMP1(20-469) [extracellular region]", "crossref": [ { "id": "P03956", "database": "UniProt", "url": "" }, { "id": "MMP1_HUMAN", "database": "ZINC - 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World Drugs", "url": "" }, { "id": "6ESM", "database": "PDB", "url": "" }, { "id": "5UE3", "database": "PDB", "url": "" }, { "id": "P14780", "database": "ZINC target", "url": "" }, { "id": "2OW2", "database": "PDB", "url": "" }, { "id": "MMP9_HUMAN", "database": "ZINC - Predictions - Purchasable", "url": "" }, { "id": "HMDBP02128", "database": "HMDB Protein", "url": "" }, { "id": "4HMA", "database": "PDB", "url": "" }, { "id": "P14780", "database": "GeneCards", "url": "" }, { "id": "18601", "database": "Orphanet", "url": "" }, { "id": "5TH9", "database": "PDB", "url": "" }, { "id": "P14780", "database": "UniProt", "url": "" }, { "id": "4H82", "database": "PDB", "url": "" }, { "id": "4JIJ", "database": "PDB", "url": "" }, { "id": "1633", "database": "Guide to Pharmacology - Targets", "url": "" }, { "id": "ENSG00000100985-MMP9", "database": "HPA", "url": "" }, { "id": "MMP9_HUMAN", "database": "ZINC - Metabolites", "url": "" }, { "id": "5I12", "database": "PDB", "url": "" }, { "id": "4JQG", "database": "PDB", "url": "" }, { "id": "1GKD", "database": "PDB", "url": "" }, { "id": "2OW0", "database": "PDB", "url": "" }, { "id": "ENSG00000100985", "database": "Ensembl", "url": "" }, { "id": "4H3X", "database": "PDB", "url": "" }, { "id": "4H1Q", "database": "PDB", "url": "" }, { "id": "MMP9_HUMAN", "database": "ZINC - Substances", "url": "" }, { "id": "5UE4", "database": "PDB", "url": "" }, { "id": "4WZV", "database": "PDB", "url": "" }, { "id": "ENSP00000361405", "database": "Ensembl", "url": "" }, { "id": "4H2E", "database": "PDB", "url": "" }, { "id": "MMP9_HUMAN", "database": "ZINC - Investigational", "url": "" }, { "id": "ENSG00000100985", "database": "OpenTargets", "url": "" }, { "id": "P14780", "database": "Pharos - Targets", "url": "" }, { "id": "P14780", "database": "PRO", "url": "" }, { "id": "2OW1", "database": "PDB", "url": "" }, { "id": "MMP9_HUMAN", "database": "ZINC - Biogenic", "url": "" } ] } ], "reaction_enzymes": [ { "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": "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": "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": "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": "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": "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": "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": "P17538", "gene_name": "CTRB1", "activity": [ { "ec_number": "3.4.21.1", "activity": "Preferential cleavage: Tyr-|-Xaa, Trp-|-Xaa, Phe-|-Xaa, Leu-|-Xaa.", "evidence": [ { "id": "P17538", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P17538" } ] }, { "ec_number": "3.4.21.1", "activity": "", "evidence": [ { "id": "P17538", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P17538" } ] } ] }, { "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": "P20718", "gene_name": "GZMH", "activity": [ { "ec_number": "3.4.21.-", "activity": "", "evidence": [ { "id": "P20718", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P20718" } ] } ] }, { "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": "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": "P29466", "gene_name": "CASP1", "activity": [ { "ec_number": "3.4.22.36", "activity": "Strict requirement for an Asp residue at position P1 and has a preferred cleavage sequence of Tyr-Val-Ala-Asp-|-.", "evidence": [ { "id": "P29466", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P29466" } ] }, { "ec_number": "3.4.22.36", "activity": "", "evidence": [ { "id": "P29466", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P29466" } ] } ] }, { "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": "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": "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": "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": "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": "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": "Q99536", "gene_name": "VAT1", "activity": [ { "ec_number": "1.-.-.-", "activity": "", "evidence": [ { "id": "Q99536", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q99536" } ] } ] }, { "uniprot_ac": "Q9BRF8", "gene_name": "CPPED1", "activity": [ { "ec_number": "3.1.3.16", "activity": "H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] + phosphate.", "evidence": [ { "id": "Q9BRF8", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q9BRF8" } ] }, { "ec_number": "3.1.3.16", "activity": "", "evidence": [ { "id": "Q9BRF8", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q9BRF8" } ] } ] }, { "uniprot_ac": "Q9BTY2", "gene_name": "FUCA2", "activity": [ { "ec_number": "3.2.1.51", "activity": "an alpha-L-fucoside + H2O = an alcohol + L-fucose.", "evidence": [ { "id": "Q9BTY2", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q9BTY2" } ] }, { "ec_number": "3.2.1.51", "activity": "", "evidence": [ { "id": "Q9BTY2", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q9BTY2" } ] } ] }, { "uniprot_ac": "Q9H7Z7", "gene_name": "PTGES2", "activity": [ { "ec_number": "5.3.99.3", "activity": "prostaglandin H2 = prostaglandin E2.", "evidence": [ { "id": "Q9H7Z7", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q9H7Z7" } ] }, { "ec_number": "5.3.99.3", "activity": "", "evidence": [ { "id": "Q9H7Z7", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q9H7Z7" } ] } ] }, { "uniprot_ac": "Q9NZK5", "gene_name": "ADA2", "activity": [ { "ec_number": "3.5.4.4", "activity": "2'-deoxyadenosine + H(+) + H2O = 2'-deoxyinosine + NH4(+).", "evidence": [ { "id": "Q9NZK5", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q9NZK5" } ] }, { "ec_number": "3.5.4.4", "activity": "", "evidence": [ { "id": "Q9NZK5", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q9NZK5" } ] } ] }, { "uniprot_ac": "Q9UHL4", "gene_name": "DPP7", "activity": [ { "ec_number": "3.4.14.2", "activity": "Release of an N-terminal dipeptide, Xaa-Yaa-|-, preferentially when Yaa is Ala or Pro. Substrates are oligopeptides, preferentially tripeptides.", "evidence": [ { "id": "Q9UHL4", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q9UHL4" } ] }, { "ec_number": "3.4.14.2", "activity": "", "evidence": [ { "id": "Q9UHL4", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q9UHL4" } ] } ] }, { "uniprot_ac": "Q9Y2J8", "gene_name": "PADI2", "activity": [ { "ec_number": "3.5.3.15", "activity": "H2O + L-arginyl-[protein] = L-citrullyl-[protein] + NH4(+).", "evidence": [ { "id": "Q9Y2J8", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q9Y2J8" } ] }, { "ec_number": "3.5.3.15", "activity": "", "evidence": [ { "id": "Q9Y2J8", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q9Y2J8" } ] } ] } ], "biomarkers": [], "synthesized_glycans": [], "cluster_types": [ { "name": "homologset.mgi", "label": "MGI Homologs" }, { "name": "homologset.oma", "label": "OMA Homologs" } ], "sequence_features": { "n_linked_sites": [ 71 ], "o_linked_sites": [], "snv_sites": [ 71, 73, 125, 211 ], "glycation_sites": [], "phosphorylation_sites": [], "sequon_annotation_sites": [ { "start_pos": 71, "end_pos": 73 } ] }, "section_stats": [ { "table_id": "glycosylation", "table_stats": [ { "field": "total", "count": 2 }, { "field": "total_sites", "count": 2 }, { "field": "n_linked_glycans", "count": 0 }, { "field": "n_linked_glycan_sites", "count": 1 }, { "field": "o_linked_glycans", "count": 1 }, { "field": "o_linked_glycan_sites", "count": 1 } ], "sort_fields": [ "glytoucan_ac", "type", "subtype", "site_category", "site_seq", "relation", "comment", "start_pos", "start_aa", "end_pos", "end_aa", "residue", "site_lbl" ] }, { "table_id": "glycosylation_reported", "table_stats": [ { "field": "total", "count": 1 }, { "field": "total_sites", "count": 1 }, { "field": "n_linked_glycans", "count": 0 }, { "field": "n_linked_glycan_sites", "count": 1 }, { "field": "o_linked_glycans", "count": 0 }, { "field": "o_linked_glycan_sites", "count": 0 } ], "sort_fields": [ "glytoucan_ac", "type", "subtype", "site_category", "site_seq", "relation", "comment", "start_pos", "start_aa", "end_pos", "end_aa", "residue", "site_lbl" ] }, { "table_id": "glycosylation_reported_with_glycan", "table_stats": [ { "field": "total", "count": 1 }, { "field": "total_sites", "count": 1 }, { "field": "n_linked_glycans", "count": 0 }, { "field": "n_linked_glycan_sites", "count": 0 }, { "field": "o_linked_glycans", "count": 1 }, { "field": "o_linked_glycan_sites", "count": 1 } ], "sort_fields": [ "glytoucan_ac", "type", "subtype", "site_category", "site_seq", "relation", "comment", "start_pos", "start_aa", "end_pos", "end_aa", "residue", "site_lbl" ] }, { "table_id": "glycosylation_predicted", "table_stats": [ { "field": "total", "count": 0 }, { "field": "total_sites", "count": 0 }, { "field": "n_linked_glycans", "count": 0 }, { "field": "n_linked_glycan_sites", "count": 0 }, { "field": "o_linked_glycans", "count": 0 }, { "field": "o_linked_glycan_sites", "count": 0 } ], "sort_fields": [] }, { "table_id": "glycosylation_automatic_literature_mining", "table_stats": [ { "field": "total", "count": 0 }, { "field": "total_sites", "count": 0 }, { "field": "n_linked_glycans", "count": 0 }, { "field": "n_linked_glycan_sites", "count": 0 }, { "field": "o_linked_glycans", "count": 0 }, { "field": "o_linked_glycan_sites", "count": 0 } ], "sort_fields": [] }, { "table_id": "phosphorylation", "table_stats": [ { "field": "total", "count": 0 }, { "field": "total_sites", "count": 0 } ], "sort_fields": [] }, { "table_id": "snv", "table_stats": [ { "field": "total", "count": 7 }, { "field": "total_sites", "count": 4 } ], "sort_fields": [ "start_pos", "end_pos", "sequence_org", "sequence_mut", "comment", "chr_id", "chr_pos", "ref_nt", "alt_nt", "minor_allelic_frequency", "site_lbl", "subjects_tested", "subjects_positive", "frequency" ] }, { "table_id": "snv_disease", "table_stats": [ { "field": "total", "count": 2 }, { "field": "total_sites", "count": 2 } ], "sort_fields": [ "start_pos", "end_pos", "sequence_org", "sequence_mut", "comment", "chr_id", "chr_pos", "ref_nt", "alt_nt", "minor_allelic_frequency", "site_lbl", "subjects_tested", "subjects_positive", "frequency" ] }, { "table_id": "snv_non_disease", "table_stats": [ { "field": "total", "count": 5 }, { "field": "total_sites", "count": 3 } ], "sort_fields": [ "start_pos", "end_pos", "sequence_org", "sequence_mut", "comment", "chr_id", "chr_pos", "ref_nt", "alt_nt", "minor_allelic_frequency", "site_lbl", "subjects_tested", "subjects_positive", "frequency" ] }, { "table_id": "publication", "table_stats": [ { "field": "total", "count": 307 } ], "sort_fields": [ "title", "journal", "date", "authors" ] } ] }