{ "uniprot_canonical_ac": "P0DUB6-1", "uniprot_ac": "P0DUB6", "uniprot_id": "AMY1A_HUMAN", "mass": { "chemical_mass": 57768.0, "monoisotopic_mass": 57768.0 }, "refseq": { "ac": "NP_001008219", "name": "alpha-amylase 1B precursor", "url": "https://www.ncbi.nlm.nih.gov/protein/NP_001008219" }, "gene_names": [ { "name": "AMY1A", "resource": "UniProtKB", "type": "recommended", "url": "https://www.uniprot.org/uniprot/P0DUB6", "id": "P0DUB6" }, { "name": "AMY1", "resource": "UniProtKB", "type": "synonym", "url": "https://www.uniprot.org/uniprot/P0DUB6", "id": "P0DUB6" } ], "protein_names": [ { "name": "Alpha-amylase 1A", "resource": "UniProtKB", "type": "recommended", "url": "", "id": "P0DUB6" }, { "name": "1,4-alpha-D-glucan glucanohydrolase 1", "resource": "UniProtKB", "type": "synonym", "url": "", "id": "P0DUB6" }, { "name": "3.2.1.1", "resource": "UniProtKB", "type": "synonym", "url": "", "id": "P0DUB6" }, { "name": "Salivary alpha-amylase", "resource": "UniProtKB", "type": "synonym", "url": "", "id": "P0DUB6" }, { "name": "alpha-amylase 1B precursor", "resource": "RefSeq", "type": "synonym", "url": "https://www.ncbi.nlm.nih.gov/protein/NP_001008219", "id": "NP_001008219" }, { "name": "glycogenase; amylase, salivary, alpha-1B; salivary amylase alpha 1B; alpha-amylase 1; salivary alpha-amylase; 1,4-alpha-D-glucan glucanohydrolase 1; amylase alpha 1B (salivary); alpha-amylase 1A; alpha-amylase 1B", "resource": "RefSeq", "type": "synonym", "url": "https://www.ncbi.nlm.nih.gov/protein/NP_001008219", "id": "NP_001008219" } ], "function": [ { "annotation": "Calcium-binding enzyme that initiates starch digestion in the oral cavity (PubMed:12527308). 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"A", "alt_nt": "null", "minor_allelic_frequency": "", "site_lbl": "S429", "keywords": [ "ebi", "germline" ] } ], "mutagenesis": [], "expression_tissue": [], "expression_disease": [], "species": [ { "name": "Homo sapiens", "taxid": 9606, "evidence": [ { "database": "UniProtKB", "id": "P0DUB6", "url": "https://www.uniprot.org/uniprot/P0DUB6" } ], "common_name": "Human" } ], "gene": [ { "name": "AMY1A", "url": "https://www.uniprot.org/uniprot/P0DUB6", "locus": { "chromosome": "1", "start_pos": 103664554, "end_pos": 103655760, "strand": "-", "evidence": [ { "database": "Ensembl Gene", "id": "ENSG00000237763", "url": "https://www.ensembl.org/id/ENSG00000237763" } ] } } ], "crossref": [ { "id": "ENSG00000237763", "url": "https://bgee.org/?page=gene&gene_id=ENSG00000237763", "database": "Bgee", "categories": [ "Gene Expression" ] }, { "id": "cd11317", "url": "https://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=cd11317", "database": "CDD", "categories": [ "Protein Classification" ] }, { "id": "CHEMBL2478", "url": "https://www.ebi.ac.uk/chembldb/target/inspect/CHEMBL2478", "database": "ChEMBL", "categories": [ "Other" ] }, { "id": "AMY1A", "url": "http://www.genecards.org/cgi-bin/carddisp.pl?gene=AMY1A", "database": "GeneCards", "categories": [ "Gene Annotation", "Organism-specific" ] }, { "id": "276", "url": "https://www.ncbi.nlm.nih.gov/gene/276", "database": "GeneID", "categories": [ "Genome Annotation" ] }, { "id": "277", "url": "https://www.ncbi.nlm.nih.gov/gene/277", "database": "GeneID", "categories": [ "Genome Annotation" ] }, { "id": "278", "url": "https://www.ncbi.nlm.nih.gov/gene/278", "database": "GeneID", "categories": [ "Genome Annotation" ] }, { "id": "474", "url": "https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=474", "database": "HGNC", "categories": [ "Organism-specific" ] }, { "id": "IPR006046", "url": "https://www.ebi.ac.uk/interpro/entry/IPR006046", "database": "InterPro", "categories": [ "Protein Classification" ] }, { "id": "IPR006047", "url": "https://www.ebi.ac.uk/interpro/entry/IPR006047", "database": "InterPro", "categories": [ "Protein Classification" ] }, { "id": "IPR006048", "url": "https://www.ebi.ac.uk/interpro/entry/IPR006048", "database": "InterPro", "categories": [ "Protein Classification" ] }, { "id": "IPR013780", "url": "https://www.ebi.ac.uk/interpro/entry/IPR013780", "database": "InterPro", "categories": [ "Protein Classification" ] }, { "id": "IPR017853", "url": "https://www.ebi.ac.uk/interpro/entry/IPR017853", "database": "InterPro", "categories": [ "Protein Classification" ] }, { "id": "IPR031319", "url": "https://www.ebi.ac.uk/interpro/entry/IPR031319", "database": "InterPro", "categories": [ "Protein Classification" ] }, { "id": "hsa:276", "url": "https://www.genome.jp/dbget-bin/get_linkdb?-t+pathway+hsa:276", "database": "KEGG Pathway", "categories": [ "Enzyme and Pathway" ] }, { "id": "hsa:277", "url": "https://www.genome.jp/dbget-bin/get_linkdb?-t+pathway+hsa:277", "database": 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"http://www.pantherdb.org/panther/family.do?clsAccession=PTHR43447:SF50", "database": "PANTHER", "categories": [ "Protein Classification" ] }, { "id": "1C8Q", "url": "https://www.rcsb.org/structure/1C8Q", "database": "PDB", "categories": [ "3D Structure" ] }, { "id": "1JXJ", "url": "https://www.rcsb.org/structure/1JXJ", "database": "PDB", "categories": [ "3D Structure" ] }, { "id": "1JXK", "url": "https://www.rcsb.org/structure/1JXK", "database": "PDB", "categories": [ "3D Structure" ] }, { "id": "1MFU", "url": "https://www.rcsb.org/structure/1MFU", "database": "PDB", "categories": [ "3D Structure" ] }, { "id": "1MFV", "url": "https://www.rcsb.org/structure/1MFV", "database": "PDB", "categories": [ "3D Structure" ] }, { "id": "1NM9", "url": "https://www.rcsb.org/structure/1NM9", "database": "PDB", "categories": [ "3D Structure" ] }, { "id": "1Q4N", "url": "https://www.rcsb.org/structure/1Q4N", "database": "PDB", "categories": [ "3D Structure" ] }, { "id": "1SMD", "url": "https://www.rcsb.org/structure/1SMD", "database": "PDB", "categories": [ "3D Structure" ] }, { "id": "1XV8", "url": "https://www.rcsb.org/structure/1XV8", "database": "PDB", "categories": [ "3D Structure" ] }, { "id": "1Z32", "url": "https://www.rcsb.org/structure/1Z32", "database": "PDB", "categories": [ "3D Structure" ] }, { "id": "3BLK", "url": "https://www.rcsb.org/structure/3BLK", "database": "PDB", "categories": [ "3D Structure" ] }, { "id": "3BLP", "url": "https://www.rcsb.org/structure/3BLP", "database": "PDB", "categories": [ "3D Structure" ] }, { "id": "3DHP", "url": "https://www.rcsb.org/structure/3DHP", "database": "PDB", "categories": [ "3D Structure" ] }, { "id": "PF00128", "url": "http://pfam.xfam.org/family/PF00128", "database": "Pfam", "categories": [ "Protein Classification" ] }, { "id": "PF02806", "url": "http://pfam.xfam.org/family/PF02806", "database": "Pfam", "categories": [ "Protein Classification" ] }, { "id": "PR_P0DUB6", "url": "http://purl.obolibrary.org/obo/PR_P0DUB6", "database": "PRO", "categories": [ "Protein" ] }, { "id": "R-HSA-189085", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-189085", "database": "Reactome", "categories": [ "Protein Classification" ] }, { "id": "NP_001008219", "url": "https://www.ncbi.nlm.nih.gov/protein/NP_001008219", "database": "RefSeq", "categories": [ "Protein" ] }, { "id": "P0DUB6", "url": "https://www.uniprot.org/uniprot/P0DUB6", "database": "UniProtKB", "categories": [ "Protein" ] }, { "id": "P0DUB6-1", "url": "https://www.uniprot.org/uniprot/P0DUB6-1", "database": "UniProtKB", "categories": [ "Protein" ] } ], "sequence": { "sequence": "MKLFWLLFTIGFCWAQYSSNTQQGRTSIVHLFEWRWVDIALECERYLAPKGFGGVQVSPPNENVAIHNPFRPWWERYQPVSYKLCTRSGNEDEFRNMVTRCNNVGVRIYVDAVINHMCGNAVSAGTSSTCGSYFNPGSRDFPAVPYSGWDFNDGKCKTGSGDIENYNDATQVRDCRLSGLLDLALGKDYVRSKIAEYMNHLIDIGVAGFRIDASKHMWPGDIKAILDKLHNLNSNWFPEGSKPFIYQEVIDLGGEPIKSSDYFGNGRVTEFKYGAKLGTVIRKWNGEKMSYLKNWGEGWGFMPSDRALVFVDNHDNQRGHGAGGASILTFWDARLYKMAVGFMLAHPYGFTRVMSSYRWPRYFENGKDVNDWVGPPNDNGVTKEVTINPDTTCGNDWVCEHRWRQIRNMVNFRNVVDGQPFTNWYDNGSNQVAFGRGNRGFIVFNNDDWTFSLTLQTGLPAGTYCDVISGDKINGNCTGIKIYVSDDGKAHFSISNSAEDPFIAIHAESKL", "length": 511, "header": "sp|P0DUB6-1|AMY1A_HUMAN Isoform 1 of Alpha-amylase 1A OS=Homo sapiens OX=9606 GN=AMY1A PE=1 SV=1 CANONICAL=P0DUB6-1" }, "isoforms": [ { "isoform_ac": "P0DUB6-1", "url": "", "sequence": { "sequence": "MKLFWLLFTIGFCWAQYSSNTQQGRTSIVHLFEWRWVDIALECERYLAPKGFGGVQVSPPNENVAIHNPFRPWWERYQPVSYKLCTRSGNEDEFRNMVTRCNNVGVRIYVDAVINHMCGNAVSAGTSSTCGSYFNPGSRDFPAVPYSGWDFNDGKCKTGSGDIENYNDATQVRDCRLSGLLDLALGKDYVRSKIAEYMNHLIDIGVAGFRIDASKHMWPGDIKAILDKLHNLNSNWFPEGSKPFIYQEVIDLGGEPIKSSDYFGNGRVTEFKYGAKLGTVIRKWNGEKMSYLKNWGEGWGFMPSDRALVFVDNHDNQRGHGAGGASILTFWDARLYKMAVGFMLAHPYGFTRVMSSYRWPRYFENGKDVNDWVGPPNDNGVTKEVTINPDTTCGNDWVCEHRWRQIRNMVNFRNVVDGQPFTNWYDNGSNQVAFGRGNRGFIVFNNDDWTFSLTLQTGLPAGTYCDVISGDKINGNCTGIKIYVSDDGKAHFSISNSAEDPFIAIHAESKL", "length": 511, "header": "sp|P0DUB6-1|AMY1A_HUMAN Isoform 1 of Alpha-amylase 1A OS=Homo sapiens OX=9606 GN=AMY1A PE=1 SV=1 CANONICAL=P0DUB6-1" }, "locus": { "chromosome": "1", "start_pos": 103664517, "end_pos": 103656331, "strand": "-", "evidence": [ { "database": "Ensembl Transcript", "id": "ENST00000370083.9", "url": "https://www.ensembl.org/id/ENST00000370083.9" }, { "database": "Ensembl Peptide", "id": "ENSP00000359100.4", "url": "https://www.ensembl.org/id/ENSP00000359100.4" } ] } } ], "glycosylation": [ { "glytoucan_ac": "", "type": "N-linked", "subtype": "", "site_category": "reported", "site_seq": "N", "relation": "attached", "comment": "N-linked (GlcNAc...) asparagine", "start_pos": 427, "start_aa": "Asn", "end_pos": 427, "end_aa": "Asn", "residue": "Asn", "site_lbl": "Asn427", "evidence": [ { "id": "P0DUB6", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P0DUB6#ptm_processing" }, { "id": "16740002", "database": "PubMed", "url": "https://glygen.org/publication/PubMed/16740002" }, { "id": "1710976", "database": "PubMed", "url": "https://glygen.org/publication/PubMed/1710976" } ] }, { "glytoucan_ac": "", "type": "N-linked", "subtype": "", "site_category": "predicted", "site_seq": "N", "relation": "attached", "comment": "N-linked (GlcNAc...) asparagine", "start_pos": 476, "start_aa": "Asn", "end_pos": 476, "end_aa": "Asn", "residue": "Asn", "site_lbl": "Asn476", "evidence": [ { "id": "P0DUB6", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P0DUB6#ptm_processing" } ] } ], "phosphorylation": [ { "start_pos": 189, "end_pos": 189, "kinase_uniprot_canonical_ac": "", "kinase_gene_name": "", "residue": "Tyr", "comment": "", "evidence": [ { "database": "iPTMnet", "id": "P0DUB6", "url": "http://research.bioinformatics.udel.edu/iptmnet/entry/P0DUB6" }, { "database": "PubMed", "id": "20068231", "url": "https://glygen.org/publication/PubMed/20068231" } ], "site_lbl": "Tyr189" } ], "glycation": [], "keywords": [ "enzyme", "glycoprotein", "glycoprotein_predicted", "glycoprotein_reported" ], "publication": [ { "title": "Subsite mapping of the human pancreatic alpha-amylase active site through structural, kinetic, and mutagenesis techniques.", "journal": "Biochemistry", "date": "2000", "authors": "Brayer GD, Sidhu G, Maurus R, Rydberg EH, Braun C, Wang Y, Nguyen NT, Overall CM, Withers SG", "evidence": [ { "database": "Reactome", "id": "R-HSA-189085", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-189085" } ], "reference": [ { "type": "PubMed", "id": "10769135", "url": "https://glygen.org/publication/PubMed/10769135" } ] }, { "title": "Identification of a novel acidic mammalian chitinase distinct from chitotriosidase.", "journal": "The Journal of biological chemistry", "date": "2001", "authors": "Boot RG, Blommaart EF, Swart E, Ghauharali-van der Vlugt K, Bijl N, Moe C, Place A, Aerts JM", "evidence": [ { "database": "Reactome", "id": "R-HSA-189085", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-189085" } ], "reference": [ { "type": "PubMed", "id": "11085997", "url": "https://glygen.org/publication/PubMed/11085997" } ] }, { "title": "Probing the role of a mobile loop in substrate binding and enzyme activity of human salivary amylase.", "journal": "Journal of molecular biology", "date": "2003", "authors": "Ramasubbu N, Ragunath C, Mishra PJ", "evidence": [ { "database": "UniProtKB", "id": "P0DUB6", "url": "https://www.uniprot.org/uniprot/P0DUB6" } ], "reference": [ { "type": "PubMed", "id": "12527308", "url": "https://glygen.org/publication/PubMed/12527308" } ] }, { "title": "The maltase-glucoamylase gene: common ancestry to sucrase-isomaltase with complementary starch digestion activities.", "journal": "Proceedings of the National Academy of Sciences of the United States of America", "date": "2003", "authors": "Nichols BL, Avery S, Sen P, Swallow DM, Hahn D, Sterchi E", "evidence": [ { "database": "Reactome", "id": "R-HSA-189085", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-189085" } ], "reference": [ { "type": "PubMed", "id": "12547908", "url": "https://glygen.org/publication/PubMed/12547908" } ] }, { "title": "Changing genes; losing lactase.", "journal": "Gut", "date": "2003", "authors": "Grand RJ, Montgomery RK, Chitkara DK, Hirschhorn JN", "evidence": [ { "database": "Reactome", "id": "R-HSA-189085", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-189085" } ], "reference": [ { "type": "PubMed", "id": "12692040", "url": "https://glygen.org/publication/PubMed/12692040" } ] }, { "title": "Genetics of lactase persistence and lactose intolerance.", "journal": "Annual review of genetics", "date": "2003", "authors": "Swallow DM", "evidence": [ { "database": "Reactome", "id": "R-HSA-189085", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-189085" } ], "reference": [ { "type": "PubMed", "id": "14616060", "url": "https://glygen.org/publication/PubMed/14616060" } ] }, { "title": "Structure of human salivary alpha-amylase at 1.6-A resolution: implications for its role in the oral cavity.", "journal": "Acta Crystallogr. D", "date": "1996", "authors": "Ramasubbu N, Paloth V, Luo Y, Brayer GD, Levine MJ", "evidence": [ { "database": "UniProtKB", "id": "P0DUB6", "url": "https://www.uniprot.org/uniprot/P0DUB6" }, { "database": "Reactome", "id": "R-HSA-189085", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-189085" } ], "reference": [ { "type": "PubMed", "id": "15299664", "url": "https://glygen.org/publication/PubMed/15299664" } ] }, { "title": "Kinetic characterization of recombinant human acidic mammalian chitinase.", "journal": "Biochemistry", "date": "2006", "authors": "Chou YT, Yao S, Czerwinski R, Fleming M, Krykbaev R, Xuan D, Zhou H, Brooks J, Fitz L, Strand J, Presman E, Lin L, Aulabaugh A, Huang X", "evidence": [ { "database": "Reactome", "id": "R-HSA-189085", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-189085" } ], "reference": [ { "type": "PubMed", "id": "16584180", "url": "https://glygen.org/publication/PubMed/16584180" } ] }, { "title": "Identification of N-linked glycoproteins in human saliva by glycoprotein capture and mass spectrometry.", "journal": "Journal of proteome research", "date": "2006", "authors": "Ramachandran P, Boontheung P, Xie Y, Sondej M, Wong DT, Loo JA", "evidence": [ { "database": "UniProtKB", "id": "P0DUB6", "url": "https://www.uniprot.org/uniprot/P0DUB6#ptm_processing" }, { "database": "UniProtKB", "id": "P0DUB6", "url": "https://www.uniprot.org/uniprot/P0DUB6" } ], "reference": [ { "type": "PubMed", "id": "16740002", "url": "https://glygen.org/publication/PubMed/16740002" } ] }, { "title": "Rabbit small intestinal trehalase. Purification, cDNA cloning, expression, and verification of glycosylphosphatidylinositol anchoring.", "journal": "The Journal of biological chemistry", "date": "1990", "authors": "Ruf J, Wacker H, James P, Maffia M, Seiler P, Galand G, von Kieckebusch A, Semenza G, Matei N", "evidence": [ { "database": "Reactome", "id": "R-HSA-189085", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-189085" } ], "reference": [ { "type": "PubMed", "id": "1697585", "url": "https://glygen.org/publication/PubMed/1697585" } ] }, { "title": "Electrophoretic characterization of posttranslational modifications of human parotid salivary alpha-amylase.", "journal": "Electrophoresis", "date": "1991", "authors": "Bank RA, Hettema EH, Arwert F, Amerongen AV, Pronk JC", "evidence": [ { "database": "UniProtKB", "id": "P0DUB6", "url": "https://www.uniprot.org/uniprot/P0DUB6#ptm_processing" }, { "database": "UniProtKB", "id": "P0DUB6", "url": "https://www.uniprot.org/uniprot/P0DUB6" } ], "reference": [ { "type": "PubMed", "id": "1710976", "url": "https://glygen.org/publication/PubMed/1710976" } ] }, { "title": "Acidic mammalian chitinase is secreted via an ADAM17/epidermal growth factor receptor-dependent pathway and stimulates chemokine production by pulmonary epithelial cells.", "journal": "The Journal of biological chemistry", "date": "2008", "authors": "Hartl D, He CH, Koller B, Da Silva CA, Homer R, Lee CG, Elias JA", "evidence": [ { "database": "Reactome", "id": "R-HSA-189085", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-189085" } ], "reference": [ { "type": "PubMed", "id": "18824549", "url": "https://glygen.org/publication/PubMed/18824549" } ] }, { "title": "Triad of polar residues implicated in pH specificity of acidic mammalian chitinase.", "journal": "Protein science : a publication of the Protein Society", "date": "2009", "authors": "Olland AM, Strand J, Presman E, Czerwinski R, Joseph-McCarthy D, Krykbaev R, Schlingmann G, Chopra R, Lin L, Fleming M, Kriz R, Stahl M, Somers W, Fitz L, Mosyak L", "evidence": [ { "database": "Reactome", "id": "R-HSA-189085", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-189085" } ], "reference": [ { "type": "PubMed", "id": "19241384", "url": "https://glygen.org/publication/PubMed/19241384" } ] }, { "title": "Differential enzymatic activity of common haplotypic versions of the human acidic Mammalian chitinase protein.", "journal": "The Journal of biological chemistry", "date": "2009", "authors": "Seibold MA, Reese TA, Choudhry S, Salam MT, Beckman K, Eng C, Atakilit A, Meade K, Lenoir M, Watson HG, Thyne S, Kumar R, Weiss KB, Grammer LC, Avila P, Schleimer RP, Fahy JV, Rodriguez-Santana J, Rodriguez-Cintron W, Boot RG, Sheppard D, Gilliland FD, Locksley RM, Burchard EG", "evidence": [ { "database": "Reactome", "id": "R-HSA-189085", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-189085" } ], "reference": [ { "type": "PubMed", "id": "19435888", "url": "https://glygen.org/publication/PubMed/19435888" } ] }, { "title": "Structural hierarchy of regulatory elements in the folding and transport of an intestinal multidomain protein.", "journal": "The Journal of biological chemistry", "date": "2010", "authors": "Behrendt M, Polaina J, Naim HY", "evidence": [ { "database": "Reactome", "id": "R-HSA-189085", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-189085" } ], "reference": [ { "type": "PubMed", "id": "19955176", "url": "https://glygen.org/publication/PubMed/19955176" } ] }, { "title": "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.", "journal": "Science signaling", "date": "2010", "authors": "Olsen JV, Vermeulen M, Santamaria A, Kumar C, Miller ML, Jensen LJ, Gnad F, Cox J, Jensen TS, Nigg EA, Brunak S, Mann M", "evidence": [ { "database": "iPTMnet", "id": "P0DUB6", "url": "http://research.bioinformatics.udel.edu/iptmnet/entry/P0DUB6" } ], "reference": [ { "type": "PubMed", "id": "20068231", "url": "https://glygen.org/publication/PubMed/20068231" } ] }, { "title": "Structural basis for substrate selectivity in human maltase-glucoamylase and sucrase-isomaltase N-terminal domains.", "journal": "The Journal of biological chemistry", "date": "2010", "authors": "Sim L, Willemsma C, Mohan S, Naim HY, Pinto BM, Rose DR", "evidence": [ { "database": "Reactome", "id": "R-HSA-189085", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-189085" } ], "reference": [ { "type": "PubMed", "id": "20356844", "url": "https://glygen.org/publication/PubMed/20356844" } ] }, { "title": "Primary structure of human salivary alpha-amylase gene.", "journal": "Gene", "date": "1986", "authors": "Nishide T, Nakamura Y, Emi M, Yamamoto T, Ogawa M, Mori T, Matsubara K", "evidence": [ { "database": "UniProtKB", "id": "P0DUB6", "url": "https://www.uniprot.org/uniprot/P0DUB6" } ], "reference": [ { "type": "PubMed", "id": "2423416", "url": "https://glygen.org/publication/PubMed/2423416" } ] }, { "title": "Identification of a human salivary amylase gene. Partial sequence of genomic DNA suggests a mode of regulation different from that of mouse, Amy1.", "journal": "Mol. Biol. Med.", "date": "1987", "authors": "Handy D E, Larsen S H, Karn R C, Hodes M E", "evidence": [ { "database": "UniProtKB", "id": "P0DUB6", "url": "https://www.uniprot.org/uniprot/P0DUB6" } ], "reference": [ { "type": "PubMed", "id": "2442579", "url": "https://glygen.org/publication/PubMed/2442579" } ] }, { "title": "Concerted evolution of human amylase genes.", "journal": "Mol. Cell. Biol.", "date": "1988", "authors": "Gumucio DL, Wiebauer K, Caldwell RM, Samuelson LC, Meisler MH", "evidence": [ { "database": "UniProtKB", "id": "P0DUB6", "url": "https://www.uniprot.org/uniprot/P0DUB6" }, { "database": "Reactome", "id": "R-HSA-189085", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-189085" } ], "reference": [ { "type": "PubMed", "id": "2452973", "url": "https://glygen.org/publication/PubMed/2452973" } ] }, { "title": "Trehalase deficiency in Greenland.", "journal": "Scandinavian journal of gastroenterology", "date": "1988", "authors": "Gudmand-Hoyer E, Fenger HJ, Skovbjerg H, Kern-Hansen P, Madsen PR", "evidence": [ { "database": "Reactome", "id": "R-HSA-189085", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-189085" } ], "reference": [ { "type": "PubMed", "id": "3227291", "url": "https://glygen.org/publication/PubMed/3227291" } ] }, { "title": "Topology and quaternary structure of pro-sucrase/isomaltase and final-form sucrase/isomaltase.", "journal": "The Biochemical journal", "date": "1986", "authors": "Cowell GM, Tranum-Jensen J, Sjostrom H, Noren O", "evidence": [ { "database": "Reactome", "id": "R-HSA-189085", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-189085" } ], "reference": [ { "type": "PubMed", "id": "3800897", "url": "https://glygen.org/publication/PubMed/3800897" } ] }, { "title": "Expression and intracellular transport of microvillus membrane hydrolases in human intestinal epithelial cells.", "journal": "The Journal of cell biology", "date": "1985", "authors": "Hauri HP, Sterchi EE, Bienz D, Fransen JA, Marxer A", "evidence": [ { "database": "Reactome", "id": "R-HSA-189085", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-189085" } ], "reference": [ { "type": "PubMed", "id": "3897250", "url": "https://glygen.org/publication/PubMed/3897250" } ] }, { "title": "Trehalase deficiency in a family.", "journal": "Gastroenterology", "date": "1973", "authors": "Madzarovova-Nohejlova J", "evidence": [ { "database": "Reactome", "id": "R-HSA-189085", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-189085" } ], "reference": [ { "type": "PubMed", "id": "4737205", "url": "https://glygen.org/publication/PubMed/4737205" } ] }, { "title": "Trehalose malabsorption causing intolerance to mushrooms. Report of a probable case.", "journal": "Gastroenterology", "date": "1971", "authors": "Bergoz R", "evidence": [ { "database": "Reactome", "id": "R-HSA-189085", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-189085" } ], "reference": [ { "type": "PubMed", "id": "5104075", "url": "https://glygen.org/publication/PubMed/5104075" } ] }, { "title": "Purification and characterization of kidney and intestinal brush-border membrane trehalases from the rabbit.", "journal": "Biochimica et biophysica acta", "date": "1984", "authors": "Galand G", "evidence": [ { "database": "Reactome", "id": "R-HSA-189085", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-189085" } ], "reference": [ { "type": "PubMed", "id": "6466686", "url": "https://glygen.org/publication/PubMed/6466686" } ] }, { "title": "Corrected sequences of cDNAs for human salivary and pancreatic alpha-amylases.", "journal": "Gene", "date": "1984", "authors": "Nishide T, Emi M, Nakamura Y, Matsubara K", "evidence": [ { "database": "UniProtKB", "id": "P0DUB6", "url": "https://www.uniprot.org/uniprot/P0DUB6" } ], "reference": [ { "type": "PubMed", "id": "6610603", "url": "https://glygen.org/publication/PubMed/6610603" } ] }, { "title": "Human lactase-phlorizin hydrolase: evidence of dimerization in the endoplasmic reticulum.", "journal": "Archives of biochemistry and biophysics", "date": "1995", "authors": "Grunberg J, Sterchi EE", "evidence": [ { "database": "Reactome", "id": "R-HSA-189085", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-189085" } ], "reference": [ { "type": "PubMed", "id": "7487100", "url": "https://glygen.org/publication/PubMed/7487100" } ] }, { "title": "Purification and characterization of human chitotriosidase, a novel member of the chitinase family of proteins.", "journal": "The Journal of biological chemistry", "date": "1995", "authors": "Renkema GH, Boot RG, Muijsers AO, Donker-Koopman WE, Aerts JM", "evidence": [ { "database": "Reactome", "id": "R-HSA-189085", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-189085" } ], "reference": [ { "type": "PubMed", "id": "7836450", "url": "https://glygen.org/publication/PubMed/7836450" } ] }, { "title": "Dimeric assembly of enterocyte brush border enzymes.", "journal": "Biochemistry", "date": "1994", "authors": "Danielsen EM", "evidence": [ { "database": "Reactome", "id": "R-HSA-189085", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-189085" } ], "reference": [ { "type": "PubMed", "id": "7906143", "url": "https://glygen.org/publication/PubMed/7906143" } ] }, { "title": "Human intestinal sucrase-isomaltase. Identification of free sucrase and isomaltase and cleavage of the hybrid into active distinct subunits.", "journal": "The Journal of biological chemistry", "date": "1975", "authors": "Conklin KA, Yamashiro KM, Gray GM", "evidence": [ { "database": "Reactome", "id": "R-HSA-189085", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-189085" } ], "reference": [ { "type": "PubMed", "id": "807575", "url": "https://glygen.org/publication/PubMed/807575" } ] }, { "title": "Proteolytic processing of human lactase-phlorizin hydrolase is a two-step event: identification of the cleavage sites.", "journal": "Archives of biochemistry and biophysics", "date": "1996", "authors": "Wuthrich M, Grunberg J, Hahn D, Jacob R, Radebach I, Naim HY, Sterchi EE", "evidence": [ { "database": "Reactome", "id": "R-HSA-189085", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-189085" } ], "reference": [ { "type": "PubMed", "id": "8951031", "url": "https://glygen.org/publication/PubMed/8951031" } ] }, { "title": "Molecular cloning, sequencing and expression of cDNA encoding human trehalase.", "journal": "Gene", "date": "1997", "authors": "Ishihara R, Taketani S, Sasai-Takedatsu M, Kino M, Tokunaga R, Kobayashi Y", "evidence": [ { "database": "Reactome", "id": "R-HSA-189085", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-189085" } ], "reference": [ { "type": "PubMed", "id": "9427547", "url": "https://glygen.org/publication/PubMed/9427547" } ] }, { "title": "Human small intestinal maltase-glucoamylase cDNA cloning. Homology to sucrase-isomaltase.", "journal": "The Journal of biological chemistry", "date": "1998", "authors": "Nichols BL, Eldering J, Avery S, Hahn D, Quaroni A, Sterchi E", "evidence": [ { "database": "Reactome", "id": "R-HSA-189085", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-189085" } ], "reference": [ { "type": "PubMed", "id": "9446624", "url": "https://glygen.org/publication/PubMed/9446624" } ] } ], "pathway": [ { "id": "hsa:276", "name": "", "url": "https://www.genome.jp/dbget-bin/get_linkdb?-t+pathway+hsa:276", "resource": "KEGG Pathway" }, { "id": "hsa:277", "name": "", "url": "https://www.genome.jp/dbget-bin/get_linkdb?-t+pathway+hsa:277", "resource": "KEGG Pathway" }, { "id": "hsa:278", "name": "", "url": "https://www.genome.jp/dbget-bin/get_linkdb?-t+pathway+hsa:278", "resource": "KEGG Pathway" }, { "id": "R-HSA-189085", "name": "Digestion of dietary carbohydrate", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-189085", "resource": "Reactome", "description": "Digestion of dietary carbohydrate" } ], "orthologs": [], "go_annotation": { "categories": [ { "name": "Cellular Component", "total": 2, "go_terms": [ { "name": "extracellular space", "id": "GO:0005615", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0005615", "evidence": [ { "database": "UniProtKB", "id": "P0DUB6", "url": "https://www.uniprot.org/uniprot/P0DUB6" } ], "pmid": "" }, { "name": "extracellular exosome", "id": "GO:0070062", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0070062", "evidence": [ { "database": "UniProtKB", "id": "P0DUB6", "url": "https://www.uniprot.org/uniprot/P0DUB6" } ], "pmid": "" } ] }, { "name": "Biological Process", "total": 2, "go_terms": [ { "name": "carbohydrate metabolic process", "id": "GO:0005975", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0005975", "evidence": [ { "database": "UniProtKB", "id": "P0DUB6", "url": "https://www.uniprot.org/uniprot/P0DUB6" } ], "pmid": "" }, { "name": "oligosaccharide metabolic process", "id": "GO:0009311", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0009311", "evidence": [ { "database": "UniProtKB", "id": "P0DUB6", "url": "https://www.uniprot.org/uniprot/P0DUB6" } ], "pmid": "" } ] }, { "name": "Molecular Function", "total": 3, "go_terms": [ { "name": "chloride ion binding", "id": "GO:0031404", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0031404", "evidence": [ { "database": "UniProtKB", "id": "P0DUB6", "url": "https://www.uniprot.org/uniprot/P0DUB6" } ], "pmid": "" }, { "name": "calcium ion binding", "id": "GO:0005509", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0005509", "evidence": [ { "database": "UniProtKB", "id": "P0DUB6", "url": "https://www.uniprot.org/uniprot/P0DUB6" } ], "pmid": "" }, { "name": "alpha-amylase activity", "id": "GO:0004556", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0004556", "evidence": [ { "database": "UniProtKB", "id": "P0DUB6", "url": "https://www.uniprot.org/uniprot/P0DUB6" } ], "pmid": "" } ] } ] }, "pro_annotation": [], "site_annotation": [ { "start_pos": 427, "end_pos": 429, "annotation": "n_glycosylation_sequon" }, { "start_pos": 476, "end_pos": 478, "annotation": "n_glycosylation_sequon" } ], "ptm_annotation": [], "interactions": [], "reactions": [ { "id": "R-HSA-188979", "name": "Digestion of linear starch (amylose) by extracellular amylase", "equation": "", "summary": "Extracellular amylose starch, linear polymers of glucose joined by alpha-1,4 linkages, is digested by the endoglucosidase activity of alpha-amylases, yielding maltose, maltotriose, and longer maltosides. The human genome contains five functional alpha-amylase genes, encoding structurally closely related isoenzymes (Gumucio et al. 1988). Three of these genes encode proteins synthesized in the parotid glands and released into the saliva (amylase 1A, B, and C), and the other two encode proteins synthesized in the exocrine pancreas and released into the small intestine (amylase 2A and B). In the human body, starch digestion thus commences in the mouth, mediated by salivary amylases, and is continued in the small intestine, mediated by the pancreatic ones.

X-ray crystallographic studies of amylase 1A and 2A proteins show them to be monomers, complexed with single calcium and chloride ions (Ramasubbu et al. 1996; Brayer et al. 2000). Biochemical characterization of amylase 2A indicates that the enzyme efficiently cleaves poly-glucose chains so as to release maltose - a glucose disaccharide - from the reducing end of the chain (Braun et al. 1993; Brayer et al. 2000).", "cellular_location": "extracellular region", "input_participant_list": [ "R-ALL-189075" ], "output_participant_list": [], "enzyme_list": [ "P04746-1", "P19961-1", "P0DTE7-1", "P0DUB6-1", "P0DTE8-1" ], "evidence": [ { "id": "R-HSA-188979", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-188979" } ] }, { "id": "R-HSA-191114", "name": "Digestion of branched starch (amylopectin) by extracellular amylase", "equation": "", "summary": "The 1-4 linkages of extracellular amylopectin starch, a glucose polymer containing linear segments formed by alpha-1,4 linkages and a smaller number of alpha-1,6 linkages forming branch points, are digested by the endoglucosidase activity of alpha-amylases, yielding maltose, maltotriose, and longer maltosides from the alpha-1,4 linear segments and alpha-limit dextrins from the branch points. Alpha-limit dextrins are glucose (G) oligomers linked by 1-4 and 1-6 bonds. 1-6 branch points make up about 5% of all amylopectin glucose bonds - the exact fraction depends on the source of the starch. Mass spectroscopic analysis of alpha-limit dextrin shows it to be a mixture of maltosides and isomaltosides containing two to forty G residues, but the most common contain fewer than seven. Maltose (G2) is the shortest 1-4 maltoside produced by alpha-amylase. Isomaltose (G2) is the shortest 1-6 isomaltoside.

The human genome contains five functional alpha-amylase genes, encoding structurally closely related isoenzymes (Gumucio et al. 1988). Three of these genes encode proteins synthesized in the parotid glands and released into the saliva (amylase 1A, B, and C), and the other two encode proteins synthesized in the exocrine pancreas and released into the small intestine (amylase 2A and B). In the human body, starch digestion thus commences in the mouth, mediated by salivary amylases, and is continued in the small intestine, mediated by the pancreatic ones.

X-ray crystallographic studies of amylase 1A and 2A proteins show them to be monomers, complexed with single calcium and chloride ions (Ramasubbu et al. 1996; Brayer et al. 2000). 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"subtype", "site_category", "site_seq", "relation", "comment", "start_pos", "start_aa", "end_pos", "end_aa", "residue", "site_lbl" ] }, { "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": 1 }, { "field": "total_sites", "count": 1 } ], "sort_fields": [ "start_pos", "end_pos", "kinase_uniprot_canonical_ac", "kinase_gene_name", "residue", "comment", "site_lbl" ] }, { "table_id": "snv", "table_stats": [ { "field": "total", "count": 1 }, { "field": "total_sites", "count": 1 } ], "sort_fields": [ "start_pos", "end_pos", "sequence_org", "sequence_mut", "comment", "chr_id", "chr_pos", "ref_nt", "alt_nt", "minor_allelic_frequency", "site_lbl" ] }, { "table_id": "snv_disease", "table_stats": [ { "field": "total", "count": 0 }, { "field": "total_sites", "count": 0 } ], "sort_fields": [] }, { "table_id": "snv_non_disease", "table_stats": [ { "field": "total", "count": 1 }, { "field": "total_sites", "count": 1 } ], "sort_fields": [ "start_pos", "end_pos", "sequence_org", "sequence_mut", "comment", "chr_id", "chr_pos", "ref_nt", "alt_nt", "minor_allelic_frequency", "site_lbl" ] }, { "table_id": "publication", "table_stats": [ { "field": "total", "count": 34 } ], "sort_fields": [ "title", "journal", "date", "authors" ] } ] }