GenomeNet

Database: UniProt/SWISS-PROT
Entry: AMY2B_HUMAN
LinkDB: AMY2B_HUMAN
Original site: AMY2B_HUMAN 
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   12-SEP-2018, entry version 178.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; 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
RT   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
RT   gene, 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.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   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.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA   Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA   Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA   McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA   Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA   Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA   Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA   Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA   Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA   Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA   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.,
RA   Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA   Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA   Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA   Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA   Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA   Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA   Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA   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.,
RA   Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA   Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA   Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA   Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA   Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA   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.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   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
RT   project: 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;
RA   Gumucio D.L., Wiebauer K., Caldwell R.M., Samuelson L.C.,
RA   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.,
RA   Planta R.J., 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
RT   alpha-amylase encoded by the AMY2B gene.";
RL   Biochim. Biophys. Acta 1203:224-229(1993).
CC   -!- CATALYTIC ACTIVITY: Endohydrolysis of (1->4)-alpha-D-glucosidic
CC       linkages in polysaccharides containing three or more (1->4)-alpha-
CC       linked D-glucose units. {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.
CC       {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.
CC       {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         Note=No experimental confirmation available.;
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family.
CC       {ECO:0000305}.
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_066188.1; NM_020978.4. [P19961-1]
DR   UniGene; Hs.484588; -.
DR   ProteinModelPortal; P19961; -.
DR   SMR; P19961; -.
DR   BioGrid; 106777; 2.
DR   IntAct; P19961; 2.
DR   STRING; 9606.ENSP00000354610; -.
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; DB04417; P-Nitrophenol.
DR   DrugBank; DB03088; Pyroglutamic Acid.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   iPTMnet; P19961; -.
DR   PhosphoSitePlus; P19961; -.
DR   DMDM; 113789; -.
DR   MaxQB; P19961; -.
DR   PaxDb; P19961; -.
DR   PeptideAtlas; P19961; -.
DR   PRIDE; P19961; -.
DR   ProteomicsDB; 53704; -.
DR   TopDownProteomics; P19961-1; -. [P19961-1]
DR   Ensembl; ENST00000361355; ENSP00000354610; ENSG00000240038. [P19961-1]
DR   Ensembl; ENST00000477657; ENSP00000433347; ENSG00000240038. [P19961-2]
DR   Ensembl; ENST00000610648; ENSP00000481588; ENSG00000240038. [P19961-1]
DR   GeneID; 280; -.
DR   KEGG; hsa:280; -.
DR   UCSC; uc001duq.5; human. [P19961-1]
DR   CTD; 280; -.
DR   DisGeNET; 280; -.
DR   EuPathDB; HostDB:ENSG00000240038.6; -.
DR   GeneCards; AMY2B; -.
DR   HGNC; HGNC:478; AMY2B.
DR   HPA; HPA045394; -.
DR   HPA; HPA045399; -.
DR   HPA; HPA046980; -.
DR   MIM; 104660; gene.
DR   neXtProt; NX_P19961; -.
DR   OpenTargets; ENSG00000240038; -.
DR   PharmGKB; PA24785; -.
DR   eggNOG; KOG2212; Eukaryota.
DR   eggNOG; COG0366; LUCA.
DR   GeneTree; ENSGT00390000002882; -.
DR   HOGENOM; HOG000253313; -.
DR   HOVERGEN; HBG000061; -.
DR   InParanoid; P19961; -.
DR   KO; K01176; -.
DR   OMA; WKCQHAW; -.
DR   OrthoDB; EOG091G07V6; -.
DR   PhylomeDB; P19961; -.
DR   TreeFam; TF312850; -.
DR   Reactome; R-HSA-189085; Digestion of dietary carbohydrate.
DR   ChiTaRS; AMY2B; human.
DR   GeneWiki; AMY2B; -.
DR   GenomeRNAi; 280; -.
DR   PRO; PR:P19961; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   Bgee; ENSG00000240038; Expressed in 88 organ(s), highest expression level in body of pancreas.
DR   CleanEx; HS_AMY2B; -.
DR   ExpressionAtlas; P19961; baseline and differential.
DR   Genevisible; P19961; HS.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0004556; F:alpha-amylase activity; ISS:GO_Central.
DR   GO; GO:0103025; F:alpha-amylase activity (releasing maltohexaose); IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.40.1180; -; 1.
DR   InterPro; IPR006048; A-amylase/branching_C.
DR   InterPro; IPR031319; A-amylase_C.
DR   InterPro; IPR006046; Alpha_amylase.
DR   InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
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; SSF51445; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Calcium; Carbohydrate metabolism; Chloride;
KW   Complete proteome; Direct protein sequencing; Disulfide bond;
KW   Glycosidase; Hydrolase; Metal-binding; Pyrrolidone carboxylic acid;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL        1     15
FT   CHAIN        16    511       Alpha-amylase 2B.
FT                                /FTId=PRO_0000001402.
FT   ACT_SITE    212    212       Nucleophile.
FT                                {ECO:0000250|UniProtKB:P04746}.
FT   ACT_SITE    248    248       Proton donor.
FT                                {ECO:0000250|UniProtKB:P04746}.
FT   METAL       115    115       Calcium. {ECO:0000250|UniProtKB:P04746}.
FT   METAL       173    173       Calcium; via carbonyl oxygen.
FT                                {ECO:0000250|UniProtKB:P04746}.
FT   METAL       182    182       Calcium. {ECO:0000250|UniProtKB:P04746}.
FT   METAL       216    216       Calcium; via carbonyl oxygen.
FT                                {ECO:0000250|UniProtKB:P04746}.
FT   BINDING     210    210       Chloride. {ECO:0000250|UniProtKB:P04746}.
FT   BINDING     313    313       Chloride. {ECO:0000250|UniProtKB:P04746}.
FT   BINDING     352    352       Chloride. {ECO:0000250|UniProtKB:P04746}.
FT   SITE        315    315       Transition state stabilizer.
FT                                {ECO:0000250|UniProtKB:P04746}.
FT   MOD_RES      16     16       Pyrrolidone carboxylic acid.
FT                                {ECO:0000250|UniProtKB:P04746}.
FT   DISULFID     43    101       {ECO:0000250|UniProtKB:P04746}.
FT   DISULFID     85    130       {ECO:0000250|UniProtKB:P04746}.
FT   DISULFID    156    175       {ECO:0000250|UniProtKB:P04746}.
FT   DISULFID    393    399       {ECO:0000250|UniProtKB:P04746}.
FT   DISULFID    465    477       {ECO:0000250|UniProtKB:P04746}.
FT   VAR_SEQ     368    370       DVN -> EHG (in isoform 2).
FT                                {ECO:0000303|PubMed:14702039}.
FT                                /FTId=VSP_056932.
FT   VAR_SEQ     371    511       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:14702039}.
FT                                /FTId=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
//
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