ID AMY2B_HUMAN Reviewed; 511 AA. AC P19961; B3KTI1; B3KXB7; D3DT76; Q9UBH3; DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1991, sequence version 1. DT 02-SEP-2026, entry version 218. DE RecName: Full=Alpha-amylase 2B; DE EC=3.2.1.1 {ECO:0000250|UniProtKB:P04746}; DE AltName: Full=1,4-alpha-D-glucan glucanohydrolase 2B; DE AltName: Full=Carcinoid alpha-amylase; DE Flags: Precursor; GN Name=AMY2B; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=2701942; DOI=10.1016/0378-1119(89)90003-6; RA Tomita N., Horii A., Doi S., Yokouchi H., Shiosaki K., Higashiyama M., RA Matsuura N., Ogawa M., Mori T., Matsubara K.; RT "A novel type of human alpha-amylase produced in lung carcinoid tumor."; RL Gene 76:11-18(1989). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=2401405; DOI=10.1016/0378-1119(90)90191-s; RA Yokouchi H., Horii A., Emi M., Tomita N., Doi S., Ogawa M., Mori T., RA Matsubara K.; RT "Cloning and characterization of a third type of human alpha-amylase gene, RT AMY2B."; RL Gene 90:281-286(1990). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Brain; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Brain, and Kidney; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [7] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-56. RX PubMed=2452973; DOI=10.1128/mcb.8.3.1197-1205.1988; RA Gumucio D.L., Wiebauer K., Caldwell R.M., Samuelson L.C., Meisler M.H.; RT "Concerted evolution of human amylase genes."; RL Mol. Cell. Biol. 8:1197-1205(1988). RN [8] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-56. RC TISSUE=Pancreas; RX PubMed=3260028; DOI=10.1093/nar/16.10.4724; RA Groot P.C., Bleeker M.J., Pronk J.C., Arwert F., Mager W.H., Planta R.J., RA Eriksson A.W., Frants R.R.; RT "Human pancreatic amylase is encoded by two different genes."; RL Nucleic Acids Res. 16:4724-4724(1988). RN [9] RP PARTIAL PROTEIN SEQUENCE. RC TISSUE=Urine; RX PubMed=8268204; DOI=10.1016/0167-4838(93)90087-8; RA Omichi K., Hase S.; RT "Identification of the characteristic amino-acid sequence for human alpha- RT amylase encoded by the AMY2B gene."; RL Biochim. Biophys. Acta 1203:224-229(1993). CC -!- CATALYTIC ACTIVITY: CC Reaction=Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in CC polysaccharides containing three or more (1->4)-alpha-linked D- CC glucose units.; EC=3.2.1.1; Evidence={ECO:0000250|UniProtKB:P04746}; CC -!- COFACTOR: CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; CC Evidence={ECO:0000250|UniProtKB:P04746}; CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250|UniProtKB:P04746}; CC -!- COFACTOR: CC Name=chloride; Xref=ChEBI:CHEBI:17996; CC Evidence={ECO:0000250|UniProtKB:P04746}; CC Note=Binds 1 Cl(-) ion per subunit. {ECO:0000250|UniProtKB:P04746}; CC -!- SUBUNIT: Monomer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P19961-1; Sequence=Displayed; CC Name=2; CC IsoId=P19961-2; Sequence=VSP_056932, VSP_056933; CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M24895; AAA35525.1; -; mRNA. DR EMBL; D90097; BAA14130.1; -; Genomic_DNA. DR EMBL; AK095605; BAG53093.1; -; mRNA. DR EMBL; AK127047; BAG54429.1; -; mRNA. DR EMBL; AC105272; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471097; EAW72902.1; -; Genomic_DNA. DR EMBL; CH471097; EAW72903.1; -; Genomic_DNA. DR EMBL; CH471097; EAW72904.1; -; Genomic_DNA. DR EMBL; BC011179; AAH11179.1; -; mRNA. DR EMBL; BC020861; AAH20861.1; -; mRNA. DR EMBL; X07057; CAA30100.1; -; Genomic_DNA. DR EMBL; M18670; AAA51725.1; -; Genomic_DNA. DR CCDS; CCDS782.1; -. [P19961-1] DR PIR; JS0165; ALHU2B. DR RefSeq; NP_001373038.1; NM_001386109.1. [P19961-1] DR RefSeq; NP_001374366.1; NM_001387437.1. [P19961-1] DR RefSeq; NP_066188.1; NM_020978.4. [P19961-1] DR AlphaFoldDB; P19961; -. DR SMR; P19961; -. DR BioGRID; 106777; 9. DR FunCoup; P19961; 117. DR IntAct; P19961; 9. DR STRING; 9606.ENSP00000354610; -. DR DrugBank; DB01870; 1,4-dithio-alpha-D-glucopyranose. DR DrugBank; DB02730; 4-Methylthio-Alpha-D-Mannose. DR DrugBank; DB03092; 5-Hydroxymethyl-Chonduritol. DR DrugBank; DB03277; alpha-maltotriose. DR DrugBank; DB02379; Beta-D-Glucose. DR DrugBank; DB03323; Maltose. DR DrugBank; DB02218; N-[4-hydroxymethyl-cyclohexan-6-yl-1,2,3-triol]-4,6-dideoxy-4-aminoglucopyranoside. DR DrugBank; DB04417; P-Nitrophenol. DR DrugBank; DB03088; Pidolic acid. DR CAZy; GH13; Glycoside Hydrolase Family 13. DR GlyGen; P19961; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P19961; -. DR PhosphoSitePlus; P19961; -. DR BioMuta; AMY2B; -. DR DMDM; 113789; -. DR jPOST; P19961; -. DR MassIVE; P19961; -. DR PaxDb; 9606-ENSP00000354610; -. DR PeptideAtlas; P19961; -. DR PRIDE; P19961; -. DR ProteomicsDB; 3680; -. DR ProteomicsDB; 53704; -. [P19961-1] DR Pumba; P19961; -. DR TopDownProteomics; P19961-1; -. [P19961-1] DR Antibodypedia; 34942; 244 antibodies from 27 providers. DR DNASU; 280; -. DR Ensembl; ENST00000361355.8; ENSP00000354610.4; ENSG00000240038.8. [P19961-1] DR Ensembl; ENST00000477657.5; ENSP00000433347.1; ENSG00000240038.8. [P19961-2] DR Ensembl; ENST00000684275.1; ENSP00000507176.1; ENSG00000240038.8. [P19961-1] DR GeneID; 280; -. DR KEGG; hsa:280; -. DR MANE-Select; ENST00000684275.1; ENSP00000507176.1; NM_001387437.1; NP_001374366.1. DR UCSC; uc001duq.5; human. [P19961-1] DR AGR; HGNC:478; -. DR ClinPGx; PA24785; -. DR CTD; 280; -. DR DisGeNET; 280; -. DR GeneCards; AMY2B; -. DR HGNC; HGNC:478; AMY2B. DR HPA; ENSG00000240038; Tissue enriched (pancreas). DR MIM; 104660; gene. DR OpenTargets; ENSG00000240038; -. DR VEuPathDB; HostDB:ENSG00000240038; -. DR eggNOG; KOG2212; Eukaryota. DR GeneTree; ENSGT00940000154802; -. DR HOGENOM; CLU_013336_2_1_1; -. DR InParanoid; P19961; -. DR OMA; FRYAYDL; -. DR OrthoDB; 550577at2759; -. DR PAN-GO; P19961; 3 GO annotations based on evolutionary models. DR PhylomeDB; P19961; -. DR PathwayCommons; P19961; -. DR Reactome; R-HSA-189085; Digestion of dietary carbohydrate. DR SignaLink; P19961; -. DR Agora; ENSG00000240038; -. DR BioGRID-ORCS; 280; 12 hits in 1042 CRISPR screens. DR ChiTaRS; AMY2B; human. DR GeneWiki; AMY2B; -. DR GenomeRNAi; 280; -. DR Pharos; P19961; Tbio. DR PRO; PR:P19961; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; P19961; protein. DR Bgee; ENSG00000240038; Expressed in body of pancreas and 98 other cell types or tissues. DR ExpressionAtlas; P19961; baseline and differential. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0004556; F:alpha-amylase activity; ISS:UniProtKB. DR GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-ARBA. DR GO; GO:0031404; F:chloride ion binding; IEA:UniProtKB-ARBA. DR GO; GO:0005975; P:carbohydrate metabolic process; IBA:GO_Central. DR CDD; cd11317; AmyAc_bac_euk_AmyA; 1. DR FunFam; 2.60.40.1180:FF:000020; Pancreatic alpha-amylase; 1. DR FunFam; 3.20.20.80:FF:000056; Pancreatic alpha-amylase; 1. DR Gene3D; 3.20.20.80; Glycosidases; 1. DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1. DR InterPro; IPR006048; A-amylase/branching_C. DR InterPro; IPR031319; A-amylase_C. DR InterPro; IPR006046; Alpha_amylase. DR InterPro; IPR006047; GH13_cat_dom. DR InterPro; IPR017853; GH_hydrolase_sf. DR InterPro; IPR013780; Glyco_hydro_b. DR PANTHER; PTHR43447; ALPHA-AMYLASE; 1. DR Pfam; PF00128; Alpha-amylase; 1. DR Pfam; PF02806; Alpha-amylase_C; 1. DR PRINTS; PR00110; ALPHAAMYLASE. DR SMART; SM00642; Aamy; 1. DR SMART; SM00632; Aamy_C; 1. DR SUPFAM; SSF51445; (Trans)glycosidases; 1. DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1. PE 1: Evidence at protein level; KW Alternative splicing; Calcium; Carbohydrate metabolism; Chloride; KW Direct protein sequencing; Disulfide bond; Glycosidase; Hydrolase; KW Metal-binding; Proteomics identification; Pyrrolidone carboxylic acid; KW Reference proteome; Secreted; Signal. FT SIGNAL 1..15 FT CHAIN 16..511 FT /note="Alpha-amylase 2B" FT /id="PRO_0000001402" FT ACT_SITE 212 FT /note="Nucleophile" FT /evidence="ECO:0000250|UniProtKB:P04746" FT ACT_SITE 248 FT /note="Proton donor" FT /evidence="ECO:0000250|UniProtKB:P04746" FT BINDING 115 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250|UniProtKB:P04746" FT BINDING 173 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250|UniProtKB:P04746" FT BINDING 182 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250|UniProtKB:P04746" FT BINDING 210 FT /ligand="chloride" FT /ligand_id="ChEBI:CHEBI:17996" FT /evidence="ECO:0000250|UniProtKB:P04746" FT BINDING 216 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250|UniProtKB:P04746" FT BINDING 313 FT /ligand="chloride" FT /ligand_id="ChEBI:CHEBI:17996" FT /evidence="ECO:0000250|UniProtKB:P04746" FT BINDING 352 FT /ligand="chloride" FT /ligand_id="ChEBI:CHEBI:17996" FT /evidence="ECO:0000250|UniProtKB:P04746" FT SITE 315 FT /note="Transition state stabilizer" FT /evidence="ECO:0000250|UniProtKB:P04746" FT MOD_RES 16 FT /note="Pyrrolidone carboxylic acid" FT /evidence="ECO:0000250|UniProtKB:P04746" FT DISULFID 43..101 FT /evidence="ECO:0000250|UniProtKB:P04746" FT DISULFID 85..130 FT /evidence="ECO:0000250|UniProtKB:P04746" FT DISULFID 156..175 FT /evidence="ECO:0000250|UniProtKB:P04746" FT DISULFID 393..399 FT /evidence="ECO:0000250|UniProtKB:P04746" FT DISULFID 465..477 FT /evidence="ECO:0000250|UniProtKB:P04746" FT VAR_SEQ 368..370 FT /note="DVN -> EHG (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_056932" FT VAR_SEQ 371..511 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_056933" SQ SEQUENCE 511 AA; 57710 MW; 05FC3B1EC1143857 CRC64; MKFFLLLFTI GFCWAQYSPN TQQGRTSIVH LFEWRWVDIA LECERYLAPK GFGGVQVSPP NENVAIHNPF RPWWERYQPV SYKLCTRSGN EDEFRNMVTR CNNVGVRIYV DAVINHMSGN AVSAGTSSTC GSYFNPGSRD FPAVPYSGWD FNDGKCKTGS GDIENYNDAT QVRDCRLVGL LDLALEKDYV RSKIAEYMNH LIDIGVAGFR LDASKHMWPG DIKAILDKLH NLNSNWFPAG SKPFIYQEVI DLGGEPIKSS DYFGNGRVTE FKYGAKLGTV IRKWNGEKMS YLKNWGEGWG FMPSDRALVF VDNHDNQRGH GAGGASILTF WDARLYKMAV GFMLAHPYGF TRVMSSYRWP RQFQNGNDVN DWVGPPNNNG VIKEVTINPD TTCGNDWVCE HRWRQIRNMV NFRNVVDGQP FTNWYDNGSN QVAFGRGNRG FIVFNNDDWT FSLTLQTGLP AGTYCDVISG DKINGNCTGI KIYVSDDGKA HFSISNSAED PFIAIHAESK L //