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P04746

- AMYP_HUMAN

UniProt

P04746 - AMYP_HUMAN

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Protein

Pancreatic alpha-amylase

Gene
AMY2A
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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 stabilizer By similarity
Binding sitei352 – 3521Chloride

GO - Molecular functioni

  1. alpha-amylase activity Source: UniProtKB
  2. calcium ion binding Source: UniProtKB
  3. 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
Complete GO annotation...

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
ProteomesiUP000005640: Chromosome 1

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
Complete GO annotation...

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 acid
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.

Miscellaneous databases

EvolutionaryTraceiP04746.

Family & Domainsi

Sequence similaritiesi

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.

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. VSP_055822Add
BLAST
Alternative sequencei266 – 511246Missing in isoform 2. VSP_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.
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.
DB00522. Bentiromide.
DB00702. Icodextrin.
DB00491. Miglitol.
DB00085. Pancrelipase.

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 .
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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 163 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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