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P04746

- AMYP_HUMAN

UniProt

P04746 - AMYP_HUMAN

Protein

Pancreatic alpha-amylase

Gene

AMY2A

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
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    • History
      Entry version 164 (01 Oct 2014)
      Sequence version 2 (01 Jul 1989)
      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.
    Binds 1 chloride ion per subunit.

    Sites

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

    GO - Molecular functioni

    1. alpha-amylase activity Source: UniProtKB
    2. calcium ion binding Source: UniProtKB
    3. cation binding Source: InterPro
    4. chloride ion binding Source: UniProtKB

    GO - Biological processi

    1. carbohydrate catabolic process Source: UniProtKB
    2. carbohydrate metabolic process Source: Reactome
    3. polysaccharide digestion Source: Reactome
    4. small molecule metabolic process Source: Reactome

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Biological processi

    Carbohydrate metabolism

    Keywords - Ligandi

    Calcium, Chloride, Metal-binding

    Enzyme and pathway databases

    BRENDAi3.2.1.1. 5538.
    ReactomeiREACT_9472. Digestion of dietary carbohydrate.
    SABIO-RKP04746.

    Protein family/group databases

    CAZyiGH13. Glycoside Hydrolase Family 13.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Pancreatic alpha-amylase (EC:3.2.1.1)
    Short name:
    PA
    Alternative name(s):
    1,4-alpha-D-glucan glucanohydrolase
    Gene namesi
    Name:AMY2A
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

    Organism-specific databases

    HGNCiHGNC:477. AMY2A.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: Reactome
    2. extracellular space Source: UniProtKB
    3. extracellular vesicular exosome Source: UniProt

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi210 – 2101R → A or Q: Abolishes chloride binding; strongly reduces activity. 1 Publication
    Mutagenesisi212 – 2121D → A or N: Abolishes activity. 2 Publications
    Mutagenesisi248 – 2481E → A or Q: Reduces activity. 1 Publication
    Mutagenesisi313 – 3131N → S: Reduces affinity for chloride; reduces activity. 1 Publication
    Mutagenesisi315 – 3151D → A or N: Strongly reduces activity. 1 Publication
    Mutagenesisi352 – 3521R → A: Abolishes chloride binding; has only slight effect on activity. 1 Publication

    Organism-specific databases

    PharmGKBiPA24784.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1515Add
    BLAST
    Chaini16 – 511496Pancreatic alpha-amylasePRO_0000001397Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei16 – 161Pyrrolidone carboxylic acid1 Publication
    Disulfide bondi43 ↔ 101
    Disulfide bondi85 ↔ 130
    Disulfide bondi156 ↔ 175
    Disulfide bondi393 ↔ 399
    Disulfide bondi465 ↔ 477
    Glycosylationi476 – 4761N-linked (GlcNAc...)

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Pyrrolidone carboxylic acid

    Proteomic databases

    PRIDEiP04746.

    PTM databases

    PhosphoSiteiP04746.

    Expressioni

    Gene expression databases

    BgeeiP04746.
    CleanExiHS_AMY2A.
    GenevestigatoriP04746.

    Organism-specific databases

    HPAiCAB045960.

    Interactioni

    Subunit structurei

    Monomer.

    Protein-protein interaction databases

    BioGridi106776. 3 interactions.
    IntActiP04746. 3 interactions.
    STRINGi9606.ENSP00000377509.

    Structurei

    Secondary structure

    1
    511
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi27 – 315
    Helixi36 – 4510
    Turni46 – 516
    Beta strandi54 – 574
    Turni67 – 704
    Helixi73 – 775
    Beta strandi78 – 803
    Helixi91 – 10313
    Beta strandi107 – 1126
    Beta strandi115 – 1195
    Beta strandi124 – 1263
    Beta strandi128 – 1303
    Turni136 – 1394
    Turni142 – 1454
    Helixi148 – 1503
    Turni153 – 1553
    Beta strandi158 – 1625
    Helixi169 – 1746
    Helixi177 – 1793
    Beta strandi180 – 1834
    Helixi188 – 20417
    Beta strandi208 – 2114
    Helixi214 – 2163
    Helixi219 – 2268
    Turni234 – 2363
    Beta strandi244 – 2474
    Beta strandi253 – 2564
    Helixi259 – 2624
    Turni263 – 2653
    Beta strandi266 – 2694
    Helixi271 – 28111
    Helixi284 – 2863
    Helixi289 – 2946
    Helixi297 – 2993
    Helixi304 – 3063
    Beta strandi307 – 3093
    Helixi316 – 3183
    Beta strandi319 – 3213
    Helixi324 – 3263
    Helixi330 – 3323
    Helixi333 – 34513
    Beta strandi348 – 3558
    Beta strandi363 – 3664
    Turni369 – 3724
    Beta strandi375 – 3784
    Helixi400 – 4023
    Helixi404 – 41512
    Turni416 – 4183
    Beta strandi421 – 4266
    Beta strandi428 – 4369
    Turni437 – 4393
    Beta strandi440 – 4456
    Beta strandi447 – 4493
    Beta strandi451 – 4566
    Beta strandi461 – 4655
    Turni467 – 4693
    Beta strandi476 – 4794
    Beta strandi481 – 4844
    Beta strandi488 – 4947
    Beta strandi498 – 5069
    Helixi507 – 5093

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1B2YX-ray3.20A16-511[»]
    1BSIX-ray2.00A17-511[»]
    1CPUX-ray2.00A16-511[»]
    1HNYX-ray1.80A17-511[»]
    1KB3X-ray2.10A16-511[»]
    1KBBX-ray1.90A16-511[»]
    1KBKX-ray1.90A16-511[»]
    1KGUX-ray2.00A16-511[»]
    1KGWX-ray2.10A16-511[»]
    1KGXX-ray2.00A16-511[»]
    1U2YX-ray1.95A16-511[»]
    1U30X-ray1.90A16-511[»]
    1U33X-ray1.95A16-511[»]
    1XCWX-ray2.00A16-511[»]
    1XCXX-ray1.90A16-511[»]
    1XD0X-ray2.00A16-511[»]
    1XD1X-ray2.20A16-511[»]
    1XGZX-ray2.00A16-511[»]
    1XH0X-ray2.00A16-511[»]
    1XH1X-ray2.03A16-511[»]
    1XH2X-ray2.20A16-511[»]
    2CPUX-ray2.00A17-511[»]
    2QMKX-ray2.30A16-511[»]
    2QV4X-ray1.97A16-511[»]
    3BAIX-ray1.90A16-511[»]
    3BAJX-ray2.10A16-511[»]
    3BAKX-ray1.90A16-511[»]
    3BAWX-ray2.00A16-511[»]
    3BAXX-ray1.90A16-511[»]
    3BAYX-ray1.99A16-511[»]
    3CPUX-ray2.00A17-511[»]
    3IJ7X-ray2.00A17-511[»]
    3IJ8X-ray1.43A17-511[»]
    3IJ9X-ray1.85A17-511[»]
    3OLDX-ray2.00A16-511[»]
    3OLEX-ray1.55A16-511[»]
    3OLGX-ray2.30A16-511[»]
    3OLIX-ray1.50A16-511[»]
    4GQQX-ray1.35A17-511[»]
    4GQRX-ray1.20A17-511[»]
    ProteinModelPortaliP04746.
    SMRiP04746. Positions 16-511.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP04746.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 13 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    HOGENOMiHOG000253313.
    HOVERGENiHBG000061.
    InParanoidiP04746.
    KOiK01176.
    OMAiSNTYITA.
    OrthoDBiEOG7RJPR2.
    PhylomeDBiP04746.
    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.
    ProtoNetiSearch...

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P04746-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MKFFLLLFTI GFCWAQYSPN TQQGRTSIVH LFEWRWVDIA LECERYLAPK    50
    GFGGVQVSPP NENVAIYNPF RPWWERYQPV SYKLCTRSGN EDEFRNMVTR 100
    CNNVGVRIYV DAVINHMCGN AVSAGTSSTC GSYFNPGSRD FPAVPYSGWD 150
    FNDGKCKTGS GDIENYNDAT QVRDCRLTGL LDLALEKDYV RSKIAEYMNH 200
    LIDIGVAGFR LDASKHMWPG DIKAILDKLH NLNSNWFPAG SKPFIYQEVI 250
    DLGGEPIKSS DYFGNGRVTE FKYGAKLGTV IRKWNGEKMS YLKNWGEGWG 300
    FVPSDRALVF VDNHDNQRGH GAGGASILTF WDARLYKMAV GFMLAHPYGF 350
    TRVMSSYRWP RQFQNGNDVN DWVGPPNNNG VIKEVTINPD TTCGNDWVCE 400
    HRWRQIRNMV IFRNVVDGQP FTNWYDNGSN QVAFGRGNRG FIVFNNDDWS 450
    FSLTLQTGLP AGTYCDVISG DKINGNCTGI KIYVSDDGKA HFSISNSAED 500
    PFIAIHAESK L 511
    Length:511
    Mass (Da):57,707
    Last modified:July 1, 1989 - v2
    Checksum:iA77B1A34EACB3C2A
    GO
    Isoform 2 (identifier: P04746-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         250-265: IDLGGEPIKSSDYFGN → HQYLYAYKISSYSLEN
         266-511: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:265
    Mass (Da):30,302
    Checksum:iEDF2723EC07BF231
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei250 – 26516IDLGG…DYFGN → HQYLYAYKISSYSLEN in isoform 2. 1 PublicationVSP_055822Add
    BLAST
    Alternative sequencei266 – 511246Missing in isoform 2. 1 PublicationVSP_055823Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M18785
    , M18714, M18716, M18718, M18720, M18722, M18724, M18726, M18783 Genomic DNA. Translation: AAA52280.1.
    M28443 mRNA. Translation: AAA51724.1.
    BC007060 mRNA. Translation: AAH07060.1.
    BC146997 mRNA. Translation: AAI46998.1.
    M18669 Genomic DNA. Translation: AAA51723.1.
    X07056 Genomic DNA. Translation: CAA30099.1.
    CCDSiCCDS783.1.
    PIRiA29614. ALHUP.
    RefSeqiNP_000690.1. NM_000699.2.
    UniGeneiHs.654437.

    Genome annotation databases

    EnsembliENST00000414303; ENSP00000397582; ENSG00000243480. [P04746-1]
    GeneIDi279.
    KEGGihsa:279.
    UCSCiuc001dut.3. human.

    Polymorphism databases

    DMDMi113803.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Web resourcesi

    Wikipedia

    Amylase entry

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M18785
    , M18714 , M18716 , M18718 , M18720 , M18722 , M18724 , M18726 , M18783 Genomic DNA. Translation: AAA52280.1 .
    M28443 mRNA. Translation: AAA51724.1 .
    BC007060 mRNA. Translation: AAH07060.1 .
    BC146997 mRNA. Translation: AAI46998.1 .
    M18669 Genomic DNA. Translation: AAA51723.1 .
    X07056 Genomic DNA. Translation: CAA30099.1 .
    CCDSi CCDS783.1.
    PIRi A29614. ALHUP.
    RefSeqi NP_000690.1. NM_000699.2.
    UniGenei Hs.654437.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1B2Y X-ray 3.20 A 16-511 [» ]
    1BSI X-ray 2.00 A 17-511 [» ]
    1CPU X-ray 2.00 A 16-511 [» ]
    1HNY X-ray 1.80 A 17-511 [» ]
    1KB3 X-ray 2.10 A 16-511 [» ]
    1KBB X-ray 1.90 A 16-511 [» ]
    1KBK X-ray 1.90 A 16-511 [» ]
    1KGU X-ray 2.00 A 16-511 [» ]
    1KGW X-ray 2.10 A 16-511 [» ]
    1KGX X-ray 2.00 A 16-511 [» ]
    1U2Y X-ray 1.95 A 16-511 [» ]
    1U30 X-ray 1.90 A 16-511 [» ]
    1U33 X-ray 1.95 A 16-511 [» ]
    1XCW X-ray 2.00 A 16-511 [» ]
    1XCX X-ray 1.90 A 16-511 [» ]
    1XD0 X-ray 2.00 A 16-511 [» ]
    1XD1 X-ray 2.20 A 16-511 [» ]
    1XGZ X-ray 2.00 A 16-511 [» ]
    1XH0 X-ray 2.00 A 16-511 [» ]
    1XH1 X-ray 2.03 A 16-511 [» ]
    1XH2 X-ray 2.20 A 16-511 [» ]
    2CPU X-ray 2.00 A 17-511 [» ]
    2QMK X-ray 2.30 A 16-511 [» ]
    2QV4 X-ray 1.97 A 16-511 [» ]
    3BAI X-ray 1.90 A 16-511 [» ]
    3BAJ X-ray 2.10 A 16-511 [» ]
    3BAK X-ray 1.90 A 16-511 [» ]
    3BAW X-ray 2.00 A 16-511 [» ]
    3BAX X-ray 1.90 A 16-511 [» ]
    3BAY X-ray 1.99 A 16-511 [» ]
    3CPU X-ray 2.00 A 17-511 [» ]
    3IJ7 X-ray 2.00 A 17-511 [» ]
    3IJ8 X-ray 1.43 A 17-511 [» ]
    3IJ9 X-ray 1.85 A 17-511 [» ]
    3OLD X-ray 2.00 A 16-511 [» ]
    3OLE X-ray 1.55 A 16-511 [» ]
    3OLG X-ray 2.30 A 16-511 [» ]
    3OLI X-ray 1.50 A 16-511 [» ]
    4GQQ X-ray 1.35 A 17-511 [» ]
    4GQR X-ray 1.20 A 17-511 [» ]
    ProteinModelPortali P04746.
    SMRi P04746. Positions 16-511.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 106776. 3 interactions.
    IntActi P04746. 3 interactions.
    STRINGi 9606.ENSP00000377509.

    Chemistry

    BindingDBi P04746.
    ChEMBLi CHEMBL2045.
    DrugBanki DB00284. Acarbose.
    DB00702. Icodextrin.
    DB00491. Miglitol.

    Protein family/group databases

    CAZyi GH13. Glycoside Hydrolase Family 13.

    PTM databases

    PhosphoSitei P04746.

    Polymorphism databases

    DMDMi 113803.

    Proteomic databases

    PRIDEi P04746.

    Protocols and materials databases

    DNASUi 279.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000414303 ; ENSP00000397582 ; ENSG00000243480 . [P04746-1 ]
    GeneIDi 279.
    KEGGi hsa:279.
    UCSCi uc001dut.3. human.

    Organism-specific databases

    CTDi 279.
    GeneCardsi GC01P104159.
    HGNCi HGNC:477. AMY2A.
    HPAi CAB045960.
    MIMi 104650. gene.
    neXtProti NX_P04746.
    PharmGKBi PA24784.
    GenAtlasi Search...

    Phylogenomic databases

    HOGENOMi HOG000253313.
    HOVERGENi HBG000061.
    InParanoidi P04746.
    KOi K01176.
    OMAi SNTYITA.
    OrthoDBi EOG7RJPR2.
    PhylomeDBi P04746.
    TreeFami TF312850.

    Enzyme and pathway databases

    BRENDAi 3.2.1.1. 5538.
    Reactomei REACT_9472. Digestion of dietary carbohydrate.
    SABIO-RK P04746.

    Miscellaneous databases

    EvolutionaryTracei P04746.
    GeneWikii AMY2A.
    GenomeRNAii 279.
    NextBioi 1129.
    PROi P04746.
    SOURCEi Search...

    Gene expression databases

    Bgeei P04746.
    CleanExi HS_AMY2A.
    Genevestigatori P04746.

    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. "Corrected sequences of cDNAs for human salivary and pancreatic alpha-amylases."
      Nakamura Y., Ogawa M., Nishide T., Emi M., Kosaki G., Himeno S., Matsubara K.
      Gene 28:263-270(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. Cited for: SEQUENCE REVISION.
    3. "Primary structure of human pancreatic alpha-amylase gene: its comparison with human salivary alpha-amylase gene."
      Horii A., Emi M., Tomita N., Nishide T., Ogawa M., Mori T., Matsubara K.
      Gene 60:57-64(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Tissue: Pancreas.
    4. "A complementary DNA sequence that predicts a human pancreatic amylase primary structure consistent with the electrophoretic mobility of the common isozyme, Amy2 A."
      Wise R.J., Karn R.C., Larsen S.H., Hodes M.E., Gardell S.J., Rutter W.J.
      Mol. Biol. Med. 2:307-322(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Tissue: Pancreas.
    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] (ISOFORMS 1 AND 2).
      Tissue: Pancreas.
    6. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-56.
    7. "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.
    8. "The active center of a mammalian alpha-amylase. Structure of the complex of a pancreatic alpha-amylase with a carbohydrate inhibitor refined to 2.2-A resolution."
      Qian M., Haser R., Buisson G., Duee E., Payan F.
      Biochemistry 33:6284-6294(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
    9. "The structure of human pancreatic alpha-amylase at 1.8-A resolution and comparisons with related enzymes."
      Brayer G.D., Luo Y., Withers S.G.
      Protein Sci. 4:1730-1742(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS), PYROGLUTAMATE FORMATION AT GLU-16.
    10. "Cloning, mutagenesis, and structural analysis of human pancreatic alpha-amylase expressed in Pichia pastoris."
      Rydberg E.H., Sidhu G., Vo H.C., Hewitt J., Cote H.C.F., Wang Y., Numao S., MacGillivray R.T.A., Overall C.M., Brayer G.D., Withers S.G.
      Protein Sci. 8:635-643(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), MUTAGENESIS OF ASP-212.
    11. "Subsite mapping of the human pancreatic alpha-amylase active site through structural, kinetic, and mutagenesis techniques."
      Brayer G.D., Sidhu G., Maurus R., Rydberg E.H., Braun C., Wang Y., Nguyen N.T., Overall C.M., Withers S.G.
      Biochemistry 39:4778-4791(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
    12. "Probing the role of the chloride ion in the mechanism of human pancreatic alpha-amylase."
      Numao S., Maurus R., Sidhu G., Wang Y., Overall C.M., Brayer G.D., Withers S.G.
      Biochemistry 41:215-225(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS), MUTAGENESIS OF ARG-210; ASN-313 AND ARG-352.
    13. "Mechanistic analyses of catalysis in human pancreatic alpha-amylase: detailed kinetic and structural studies of mutants of three conserved carboxylic acids."
      Rydberg E.H., Li C., Maurus R., Overall C.M., Brayer G.D., Withers S.G.
      Biochemistry 41:4492-4502(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS), MUTAGENESIS OF ASP-212; GLU-248 AND ASP-315.

    Entry informationi

    Entry nameiAMYP_HUMAN
    AccessioniPrimary (citable) accession number: P04746
    Secondary accession number(s): B9EJG1, Q9UBH3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 13, 1987
    Last sequence update: July 1, 1989
    Last modified: October 1, 2014
    This is version 164 of the entry and version 2 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

    3D-structure, Complete proteome, 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3

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