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P04745

- AMY1_HUMAN

UniProt

P04745 - AMY1_HUMAN

Protein

Alpha-amylase 1

Gene

AMY1A

more
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 171 (01 Oct 2014)
      Sequence version 2 (01 Feb 1996)
      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: ProtInc
    2. metal ion binding Source: UniProtKB-KW
    3. protein binding Source: IntAct

    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

    BRENDAi3.2.1.1. 2681.
    ReactomeiREACT_9472. Digestion of dietary carbohydrate.

    Protein family/group databases

    CAZyiGH13. Glycoside Hydrolase Family 13.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Alpha-amylase 1 (EC:3.2.1.1)
    Alternative name(s):
    1,4-alpha-D-glucan glucanohydrolase 1
    Salivary alpha-amylase
    Gene namesi
    Name:AMY1A
    Synonyms:AMY1
    AND
    Name:AMY1B
    Synonyms:AMY1
    AND
    Name:AMY1C
    Synonyms:AMY1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:474. AMY1A.
    HGNC:475. AMY1B.
    HGNC:476. AMY1C.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular space Source: UniProt
    2. extracellular vesicular exosome Source: UniProt

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA24783.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1515Sequence AnalysisAdd
    BLAST
    Chaini16 – 511496Alpha-amylase 1PRO_0000001401Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei16 – 161Pyrrolidone carboxylic acidBy similarity
    Disulfide bondi43 ↔ 101
    Disulfide bondi85 ↔ 130
    Disulfide bondi156 ↔ 175
    Modified residuei365 – 3651Deamidated asparagine; partial
    Disulfide bondi393 ↔ 399
    Modified residuei427 – 4271Deamidated asparagine; partial
    Glycosylationi427 – 4271N-linked (GlcNAc...); alternate1 Publication
    Disulfide bondi465 ↔ 477
    Modified residuei474 – 4741Deamidated asparagine; partial
    Glycosylationi476 – 4761N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Pyrrolidone carboxylic acid

    Proteomic databases

    MaxQBiP04745.
    PaxDbiP04745.
    PeptideAtlasiP04745.
    PRIDEiP04745.

    PTM databases

    PhosphoSiteiP04745.
    UniCarbKBiP04745.

    Expressioni

    Gene expression databases

    BgeeiP04745.
    CleanExiHS_AMY1A.
    GenevestigatoriP04745.

    Organism-specific databases

    HPAiCAB004310.
    HPA045394.
    HPA045399.
    HPA046980.

    Interactioni

    Subunit structurei

    Monomer.

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    MUC7Q8TAX72EBI-738586,EBI-738582

    Protein-protein interaction databases

    BioGridi106773. 4 interactions.
    106774. 1 interaction.
    106775. 1 interaction.
    IntActiP04745. 2 interactions.
    STRINGi9606.ENSP00000330484.

    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
    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
    Helixi272 – 28211
    Helixi289 – 2946
    Helixi297 – 2993
    Turni304 – 3063
    Beta strandi307 – 3093
    Helixi316 – 3183
    Beta strandi321 – 3233
    Helixi324 – 3263
    Helixi330 – 3323
    Helixi333 – 34513
    Beta strandi348 – 3558
    Beta strandi363 – 3686
    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 – 5003
    Beta strandi502 – 5065
    Helixi507 – 5093

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1C8QX-ray2.30A16-511[»]
    1JXJX-ray1.99A16-511[»]
    1JXKX-ray1.90A16-511[»]
    1MFUX-ray2.00A17-511[»]
    1MFVX-ray2.00A17-511[»]
    1NM9X-ray2.10A16-511[»]
    1Q4NX-ray2.07X16-511[»]
    1SMDX-ray1.60A17-511[»]
    1XV8X-ray3.00A/B16-511[»]
    1Z32X-ray1.60X16-511[»]
    3BLKX-ray2.00A16-511[»]
    3BLPX-ray1.60X16-511[»]
    3DHPX-ray1.50A16-511[»]
    ProteinModelPortaliP04745.
    SMRiP04745. Positions 16-511.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP04745.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 13 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG0366.
    HOGENOMiHOG000253313.
    HOVERGENiHBG000061.
    InParanoidiP04745.
    KOiK01176.
    OMAiVAINHES.
    OrthoDBiEOG7RJPR2.
    PhylomeDBiP04745.
    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.

    P04745-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKLFWLLFTI GFCWAQYSSN TQQGRTSIVH LFEWRWVDIA LECERYLAPK    50
    GFGGVQVSPP NENVAIHNPF RPWWERYQPV SYKLCTRSGN EDEFRNMVTR 100
    CNNVGVRIYV DAVINHMCGN AVSAGTSSTC GSYFNPGSRD FPAVPYSGWD 150
    FNDGKCKTGS GDIENYNDAT QVRDCRLSGL LDLALGKDYV RSKIAEYMNH 200
    LIDIGVAGFR IDASKHMWPG DIKAILDKLH NLNSNWFPEG SKPFIYQEVI 250
    DLGGEPIKSS DYFGNGRVTE FKYGAKLGTV IRKWNGEKMS YLKNWGEGWG 300
    FMPSDRALVF VDNHDNQRGH GAGGASILTF WDARLYKMAV GFMLAHPYGF 350
    TRVMSSYRWP RYFENGKDVN DWVGPPNDNG VTKEVTINPD TTCGNDWVCE 400
    HRWRQIRNMV NFRNVVDGQP FTNWYDNGSN QVAFGRGNRG FIVFNNDDWT 450
    FSLTLQTGLP AGTYCDVISG DKINGNCTGI KIYVSDDGKA HFSISNSAED 500
    PFIAIHAESK L 511
    Length:511
    Mass (Da):57,768
    Last modified:February 1, 1996 - v2
    Checksum:i7710BCAC83EBE8B2
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti285 – 2851N → T in AAA57345. (PubMed:2442579)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M18786
    , M18715, M18717, M18719, M18721, M18723, M18725, M18727, M18784 Genomic DNA. Translation: AAA52279.1.
    AK292341 mRNA. Translation: BAF85030.1.
    AL513482 Genomic DNA. Translation: CAI14928.1.
    AL513482 Genomic DNA. Translation: CAI14932.1.
    BC063129 mRNA. Translation: AAH63129.1.
    BC069347 mRNA. Translation: AAH69347.1.
    BC069463 mRNA. Translation: AAH69463.1.
    BC092444 mRNA. Translation: AAH92444.1.
    BC132985 mRNA. Translation: AAI32986.1.
    BC132987 mRNA. Translation: AAI32988.1.
    BC132995 mRNA. Translation: AAI32996.1.
    BC132997 mRNA. Translation: AAI32998.1.
    M18671 Genomic DNA. Translation: AAA58368.1.
    M18674 Genomic DNA. Translation: AAA16183.2.
    M19233, M17883 Genomic DNA. Translation: AAA57345.1. Different termination.
    M17884 Genomic DNA. No translation available.
    CCDSiCCDS30782.1.
    CCDS30783.1.
    CCDS30784.1.
    PIRiA91543. ALHUS.
    RefSeqiNP_001008219.1. NM_001008218.1.
    NP_001008220.1. NM_001008219.1.
    NP_001008222.1. NM_001008221.1.
    NP_004029.2. NM_004038.3.
    XP_005270812.1. XM_005270755.1.
    XP_005270815.1. XM_005270758.1.
    XP_005270818.1. XM_005270761.1.
    XP_006710642.1. XM_006710579.1.
    XP_006710643.1. XM_006710580.1.
    XP_006710644.1. XM_006710581.1.
    UniGeneiHs.599274.
    Hs.654437.
    Hs.655232.
    Hs.662103.

    Genome annotation databases

    EnsembliENST00000330330; ENSP00000330484; ENSG00000174876.
    ENST00000370079; ENSP00000359096; ENSG00000187733.
    ENST00000370080; ENSP00000359097; ENSG00000174876.
    ENST00000370083; ENSP00000359100; ENSG00000237763.
    GeneIDi276.
    277.
    278.
    KEGGihsa:276.
    hsa:277.
    hsa:278.
    UCSCiuc001duu.3. human.

    Polymorphism databases

    DMDMi1351933.

    Cross-referencesi

    Web resourcesi

    Wikipedia

    Amylase entry

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M18786
    , M18715 , M18717 , M18719 , M18721 , M18723 , M18725 , M18727 , M18784 Genomic DNA. Translation: AAA52279.1 .
    AK292341 mRNA. Translation: BAF85030.1 .
    AL513482 Genomic DNA. Translation: CAI14928.1 .
    AL513482 Genomic DNA. Translation: CAI14932.1 .
    BC063129 mRNA. Translation: AAH63129.1 .
    BC069347 mRNA. Translation: AAH69347.1 .
    BC069463 mRNA. Translation: AAH69463.1 .
    BC092444 mRNA. Translation: AAH92444.1 .
    BC132985 mRNA. Translation: AAI32986.1 .
    BC132987 mRNA. Translation: AAI32988.1 .
    BC132995 mRNA. Translation: AAI32996.1 .
    BC132997 mRNA. Translation: AAI32998.1 .
    M18671 Genomic DNA. Translation: AAA58368.1 .
    M18674 Genomic DNA. Translation: AAA16183.2 .
    M19233 , M17883 Genomic DNA. Translation: AAA57345.1 . Different termination.
    M17884 Genomic DNA. No translation available.
    CCDSi CCDS30782.1.
    CCDS30783.1.
    CCDS30784.1.
    PIRi A91543. ALHUS.
    RefSeqi NP_001008219.1. NM_001008218.1.
    NP_001008220.1. NM_001008219.1.
    NP_001008222.1. NM_001008221.1.
    NP_004029.2. NM_004038.3.
    XP_005270812.1. XM_005270755.1.
    XP_005270815.1. XM_005270758.1.
    XP_005270818.1. XM_005270761.1.
    XP_006710642.1. XM_006710579.1.
    XP_006710643.1. XM_006710580.1.
    XP_006710644.1. XM_006710581.1.
    UniGenei Hs.599274.
    Hs.654437.
    Hs.655232.
    Hs.662103.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1C8Q X-ray 2.30 A 16-511 [» ]
    1JXJ X-ray 1.99 A 16-511 [» ]
    1JXK X-ray 1.90 A 16-511 [» ]
    1MFU X-ray 2.00 A 17-511 [» ]
    1MFV X-ray 2.00 A 17-511 [» ]
    1NM9 X-ray 2.10 A 16-511 [» ]
    1Q4N X-ray 2.07 X 16-511 [» ]
    1SMD X-ray 1.60 A 17-511 [» ]
    1XV8 X-ray 3.00 A/B 16-511 [» ]
    1Z32 X-ray 1.60 X 16-511 [» ]
    3BLK X-ray 2.00 A 16-511 [» ]
    3BLP X-ray 1.60 X 16-511 [» ]
    3DHP X-ray 1.50 A 16-511 [» ]
    ProteinModelPortali P04745.
    SMRi P04745. Positions 16-511.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 106773. 4 interactions.
    106774. 1 interaction.
    106775. 1 interaction.
    IntActi P04745. 2 interactions.
    STRINGi 9606.ENSP00000330484.

    Chemistry

    BindingDBi P04745.
    ChEMBLi CHEMBL2478.

    Protein family/group databases

    CAZyi GH13. Glycoside Hydrolase Family 13.

    PTM databases

    PhosphoSitei P04745.
    UniCarbKBi P04745.

    Polymorphism databases

    DMDMi 1351933.

    Proteomic databases

    MaxQBi P04745.
    PaxDbi P04745.
    PeptideAtlasi P04745.
    PRIDEi P04745.

    Protocols and materials databases

    DNASUi 277.
    278.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000330330 ; ENSP00000330484 ; ENSG00000174876 .
    ENST00000370079 ; ENSP00000359096 ; ENSG00000187733 .
    ENST00000370080 ; ENSP00000359097 ; ENSG00000174876 .
    ENST00000370083 ; ENSP00000359100 ; ENSG00000237763 .
    GeneIDi 276.
    277.
    278.
    KEGGi hsa:276.
    hsa:277.
    hsa:278.
    UCSCi uc001duu.3. human.

    Organism-specific databases

    CTDi 276.
    277.
    278.
    GeneCardsi GC01M104230.
    GC01P104197.
    GC01P104292.
    HGNCi HGNC:474. AMY1A.
    HGNC:475. AMY1B.
    HGNC:476. AMY1C.
    HPAi CAB004310.
    HPA045394.
    HPA045399.
    HPA046980.
    MIMi 104700. gene.
    104701. gene.
    104702. gene.
    neXtProti NX_P04745.
    PharmGKBi PA24783.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0366.
    HOGENOMi HOG000253313.
    HOVERGENi HBG000061.
    InParanoidi P04745.
    KOi K01176.
    OMAi VAINHES.
    OrthoDBi EOG7RJPR2.
    PhylomeDBi P04745.
    TreeFami TF312850.

    Enzyme and pathway databases

    BRENDAi 3.2.1.1. 2681.
    Reactomei REACT_9472. Digestion of dietary carbohydrate.

    Miscellaneous databases

    EvolutionaryTracei P04745.
    GeneWikii AMY1A.
    NextBioi 1113.
    PROi P04745.
    SOURCEi Search...

    Gene expression databases

    Bgeei P04745.
    CleanExi HS_AMY1A.
    Genevestigatori P04745.

    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. "Primary structure of human salivary alpha-amylase gene."
      Nishide T., Nakamura Y., Emi M., Yamamoto T., Ogawa M., Mori T., Matsubara K.
      Gene 41:299-304(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "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].
    3. Cited for: SEQUENCE REVISION.
    4. "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].
    5. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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: Thyroid.
    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 AND 408-448.
    8. "Identification of a human salivary amylase gene. Partial sequence of genomic DNA suggests a mode of regulation different from that of mouse, Amy1."
      Handy D.E., Larsen S.H., Karn R.C., Hodes M.E.
      Mol. Biol. Med. 4:145-155(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-293 AND 450-511.
    9. "Electrophoretic characterization of posttranslational modifications of human parotid salivary alpha-amylase."
      Bank R.A., Hettema E.H., Arwert F., Amerongen A.V., Pronk J.C.
      Electrophoresis 12:74-79(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: POST-TRANSLATIONAL MODIFICATIONS.
    10. "Identification of N-linked glycoproteins in human saliva by glycoprotein capture and mass spectrometry."
      Ramachandran P., Boontheung P., Xie Y., Sondej M., Wong D.T., Loo J.A.
      J. Proteome Res. 5:1493-1503(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-427.
      Tissue: Saliva.
    11. "Structure of human salivary alpha-amylase at 1.6-A resolution: implications for its role in the oral cavity."
      Ramasubbu N., Paloth V., Luo Y., Brayer G.D., Levine M.J.
      Acta Crystallogr. D 52:435-446(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
    12. "Probing the role of a mobile loop in substrate binding and enzyme activity of human salivary amylase."
      Ramasubbu N., Ragunath C., Mishra P.J.
      J. Mol. Biol. 325:1061-1076(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF WILD-TYPE AND MUTANT 321-GLY--ALA-325 DEL.

    Entry informationi

    Entry nameiAMY1_HUMAN
    AccessioniPrimary (citable) accession number: P04745
    Secondary accession number(s): A6NJS5
    , A8K8H6, Q13763, Q5T083
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 13, 1987
    Last sequence update: February 1, 1996
    Last modified: October 1, 2014
    This is version 171 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