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P19961

- AMY2B_HUMAN

UniProt

P19961 - AMY2B_HUMAN

Protein

Alpha-amylase 2B

Gene

AMY2B

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 149 (01 Oct 2014)
      Sequence version 1 (01 Feb 1991)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha-linked D-glucose units.

    Cofactori

    Binds 1 calcium ion per subunit.By similarity
    Binds 1 chloride ion per subunit.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi115 – 1151CalciumBy similarity
    Metal bindingi173 – 1731Calcium; via carbonyl oxygenBy similarity
    Metal bindingi182 – 1821CalciumBy similarity
    Binding sitei210 – 2101ChlorideBy similarity
    Active sitei212 – 2121NucleophileBy similarity
    Metal bindingi216 – 2161Calcium; via carbonyl oxygenBy similarity
    Active sitei248 – 2481Proton donorBy similarity
    Binding sitei313 – 3131ChlorideBy similarity
    Sitei315 – 3151Transition state stabilizerBy similarity
    Binding sitei352 – 3521ChlorideBy similarity

    GO - Molecular functioni

    1. alpha-amylase activity Source: ProtInc
    2. metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    1. carbohydrate metabolic process Source: ProtInc
    2. digestion Source: ProtInc

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Biological processi

    Carbohydrate metabolism

    Keywords - Ligandi

    Calcium, Chloride, Metal-binding

    Enzyme and pathway databases

    ReactomeiREACT_9472. Digestion of dietary carbohydrate.

    Protein family/group databases

    CAZyiGH13. Glycoside Hydrolase Family 13.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Alpha-amylase 2B (EC:3.2.1.1)
    Alternative name(s):
    1,4-alpha-D-glucan glucanohydrolase 2B
    Carcinoid alpha-amylase
    Gene namesi
    Name:AMY2B
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:478. AMY2B.

    Subcellular locationi

    Secreted By similarity

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA24785.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1515Add
    BLAST
    Chaini16 – 511496Alpha-amylase 2BPRO_0000001402Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei16 – 161Pyrrolidone carboxylic acidBy similarity
    Disulfide bondi43 ↔ 101By similarity
    Disulfide bondi85 ↔ 130By similarity
    Disulfide bondi156 ↔ 175By similarity
    Disulfide bondi393 ↔ 399By similarity
    Disulfide bondi465 ↔ 477By similarity

    Keywords - PTMi

    Disulfide bond, Pyrrolidone carboxylic acid

    Proteomic databases

    MaxQBiP19961.
    PaxDbiP19961.
    PRIDEiP19961.

    PTM databases

    PhosphoSiteiP19961.

    Expressioni

    Gene expression databases

    BgeeiP19961.
    CleanExiHS_AMY2B.
    GenevestigatoriP19961.

    Interactioni

    Subunit structurei

    Monomer.By similarity

    Protein-protein interaction databases

    BioGridi106777. 1 interaction.
    IntActiP19961. 2 interactions.
    STRINGi9606.ENSP00000341734.

    Structurei

    3D structure databases

    ProteinModelPortaliP19961.
    SMRiP19961. Positions 17-511.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 13 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG0366.
    HOGENOMiHOG000253313.
    HOVERGENiHBG000061.
    InParanoidiP19961.
    KOiK01176.
    OMAiSQVRDCR.
    PhylomeDBiP19961.
    TreeFamiTF312850.

    Family and domain databases

    Gene3Di2.60.40.1180. 1 hit.
    3.20.20.80. 1 hit.
    InterProiIPR006048. A-amylase_b_C.
    IPR006046. Alpha_amylase.
    IPR015902. Glyco_hydro_13.
    IPR013780. Glyco_hydro_13_b.
    IPR006047. Glyco_hydro_13_cat_dom.
    IPR006589. Glyco_hydro_13_sub_cat_dom.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view]
    PANTHERiPTHR10357. PTHR10357. 1 hit.
    PfamiPF00128. Alpha-amylase. 1 hit.
    PF02806. Alpha-amylase_C. 1 hit.
    [Graphical view]
    PRINTSiPR00110. ALPHAAMYLASE.
    SMARTiSM00642. Aamy. 1 hit.
    SM00632. Aamy_C. 1 hit.
    [Graphical view]
    SUPFAMiSSF51445. SSF51445. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P19961-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKFFLLLFTI GFCWAQYSPN TQQGRTSIVH LFEWRWVDIA LECERYLAPK    50
    GFGGVQVSPP NENVAIHNPF RPWWERYQPV SYKLCTRSGN EDEFRNMVTR 100
    CNNVGVRIYV DAVINHMSGN AVSAGTSSTC GSYFNPGSRD FPAVPYSGWD 150
    FNDGKCKTGS GDIENYNDAT QVRDCRLVGL LDLALEKDYV RSKIAEYMNH 200
    LIDIGVAGFR LDASKHMWPG DIKAILDKLH NLNSNWFPAG SKPFIYQEVI 250
    DLGGEPIKSS DYFGNGRVTE FKYGAKLGTV IRKWNGEKMS YLKNWGEGWG 300
    FMPSDRALVF VDNHDNQRGH GAGGASILTF WDARLYKMAV GFMLAHPYGF 350
    TRVMSSYRWP RQFQNGNDVN DWVGPPNNNG VIKEVTINPD TTCGNDWVCE 400
    HRWRQIRNMV NFRNVVDGQP FTNWYDNGSN QVAFGRGNRG FIVFNNDDWT 450
    FSLTLQTGLP AGTYCDVISG DKINGNCTGI KIYVSDDGKA HFSISNSAED 500
    PFIAIHAESK L 511
    Length:511
    Mass (Da):57,710
    Last modified:February 1, 1991 - v1
    Checksum:i05FC3B1EC1143857
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M24895 mRNA. Translation: AAA35525.1.
    D90097 Genomic DNA. Translation: BAA14130.1.
    AK127047 mRNA. Translation: BAG54429.1.
    CH471097 Genomic DNA. Translation: EAW72902.1.
    CH471097 Genomic DNA. Translation: EAW72903.1.
    CH471097 Genomic DNA. Translation: EAW72904.1.
    BC011179 mRNA. Translation: AAH11179.1.
    BC020861 mRNA. Translation: AAH20861.1.
    X07057 Genomic DNA. Translation: CAA30100.1.
    M18670 Genomic DNA. Translation: AAA51725.1.
    CCDSiCCDS782.1.
    PIRiJS0165. ALHU2B.
    RefSeqiNP_066188.1. NM_020978.4.
    UniGeneiHs.484588.

    Genome annotation databases

    EnsembliENST00000361355; ENSP00000354610; ENSG00000240038.
    GeneIDi280.
    KEGGihsa:280.
    UCSCiuc001duq.3. human.

    Polymorphism databases

    DMDMi113789.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M24895 mRNA. Translation: AAA35525.1 .
    D90097 Genomic DNA. Translation: BAA14130.1 .
    AK127047 mRNA. Translation: BAG54429.1 .
    CH471097 Genomic DNA. Translation: EAW72902.1 .
    CH471097 Genomic DNA. Translation: EAW72903.1 .
    CH471097 Genomic DNA. Translation: EAW72904.1 .
    BC011179 mRNA. Translation: AAH11179.1 .
    BC020861 mRNA. Translation: AAH20861.1 .
    X07057 Genomic DNA. Translation: CAA30100.1 .
    M18670 Genomic DNA. Translation: AAA51725.1 .
    CCDSi CCDS782.1.
    PIRi JS0165. ALHU2B.
    RefSeqi NP_066188.1. NM_020978.4.
    UniGenei Hs.484588.

    3D structure databases

    ProteinModelPortali P19961.
    SMRi P19961. Positions 17-511.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 106777. 1 interaction.
    IntActi P19961. 2 interactions.
    STRINGi 9606.ENSP00000341734.

    Chemistry

    BindingDBi P19961.

    Protein family/group databases

    CAZyi GH13. Glycoside Hydrolase Family 13.

    PTM databases

    PhosphoSitei P19961.

    Polymorphism databases

    DMDMi 113789.

    Proteomic databases

    MaxQBi P19961.
    PaxDbi P19961.
    PRIDEi P19961.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000361355 ; ENSP00000354610 ; ENSG00000240038 .
    GeneIDi 280.
    KEGGi hsa:280.
    UCSCi uc001duq.3. human.

    Organism-specific databases

    CTDi 280.
    GeneCardsi GC01P104096.
    HGNCi HGNC:478. AMY2B.
    MIMi 104660. gene.
    neXtProti NX_P19961.
    PharmGKBi PA24785.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0366.
    HOGENOMi HOG000253313.
    HOVERGENi HBG000061.
    InParanoidi P19961.
    KOi K01176.
    OMAi SQVRDCR.
    PhylomeDBi P19961.
    TreeFami TF312850.

    Enzyme and pathway databases

    Reactomei REACT_9472. Digestion of dietary carbohydrate.

    Miscellaneous databases

    ChiTaRSi AMY2B. human.
    GeneWikii AMY2B.
    GenomeRNAii 280.
    NextBioi 1133.
    PROi P19961.
    SOURCEi Search...

    Gene expression databases

    Bgeei P19961.
    CleanExi HS_AMY2B.
    Genevestigatori P19961.

    Family and domain databases

    Gene3Di 2.60.40.1180. 1 hit.
    3.20.20.80. 1 hit.
    InterProi IPR006048. A-amylase_b_C.
    IPR006046. Alpha_amylase.
    IPR015902. Glyco_hydro_13.
    IPR013780. Glyco_hydro_13_b.
    IPR006047. Glyco_hydro_13_cat_dom.
    IPR006589. Glyco_hydro_13_sub_cat_dom.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view ]
    PANTHERi PTHR10357. PTHR10357. 1 hit.
    Pfami PF00128. Alpha-amylase. 1 hit.
    PF02806. Alpha-amylase_C. 1 hit.
    [Graphical view ]
    PRINTSi PR00110. ALPHAAMYLASE.
    SMARTi SM00642. Aamy. 1 hit.
    SM00632. Aamy_C. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51445. SSF51445. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "A novel type of human alpha-amylase produced in lung carcinoid tumor."
      Tomita N., Horii A., Doi S., Yokouchi H., Shiosaki K., Higashiyama M., Matsuura N., Ogawa M., Mori T., Matsubara K.
      Gene 76:11-18(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Cloning and characterization of a third type of human alpha-amylase gene, AMY2B."
      Yokouchi H., Horii A., Emi M., Tomita N., Doi S., Ogawa M., Mori T., Matsubara K.
      Gene 90:281-286(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Brain.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Brain and Kidney.
    6. "Concerted evolution of human amylase genes."
      Gumucio D.L., Wiebauer K., Caldwell R.M., Samuelson L.C., Meisler M.H.
      Mol. Cell. Biol. 8:1197-1205(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-56.
    7. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-56.
      Tissue: Pancreas.
    8. "Identification of the characteristic amino-acid sequence for human alpha-amylase encoded by the AMY2B gene."
      Omichi K., Hase S.
      Biochim. Biophys. Acta 1203:224-229(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL PROTEIN SEQUENCE.
      Tissue: Urine.

    Entry informationi

    Entry nameiAMY2B_HUMAN
    AccessioniPrimary (citable) accession number: P19961
    Secondary accession number(s): B3KXB7, D3DT76, Q9UBH3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1991
    Last sequence update: February 1, 1991
    Last modified: October 1, 2014
    This is version 149 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    2. Human chromosome 1
      Human chromosome 1: entries, gene names and cross-references to MIM
    3. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3