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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

Protein has several cofactor binding sites:
  • Ca2+Note: Binds 1 Ca(2+) ion per subunit.
  • chlorideNote: Binds 1 Cl(-) 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. 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: UniProtKB
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 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. 4 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 – 315Combined sources
Helixi36 – 4510Combined sources
Turni46 – 516Combined sources
Beta strandi54 – 574Combined sources
Turni67 – 704Combined sources
Helixi73 – 775Combined sources
Beta strandi78 – 803Combined sources
Helixi91 – 10313Combined sources
Beta strandi107 – 1126Combined sources
Beta strandi115 – 1195Combined sources
Beta strandi124 – 1263Combined sources
Beta strandi128 – 1303Combined sources
Turni136 – 1394Combined sources
Turni142 – 1454Combined sources
Helixi148 – 1503Combined sources
Turni153 – 1553Combined sources
Beta strandi158 – 1625Combined sources
Helixi169 – 1746Combined sources
Helixi177 – 1793Combined sources
Beta strandi180 – 1834Combined sources
Helixi188 – 20417Combined sources
Beta strandi208 – 2114Combined sources
Helixi214 – 2163Combined sources
Helixi219 – 2268Combined sources
Turni234 – 2363Combined sources
Beta strandi244 – 2474Combined sources
Beta strandi253 – 2564Combined sources
Helixi259 – 2624Combined sources
Turni263 – 2653Combined sources
Beta strandi266 – 2694Combined sources
Helixi271 – 28111Combined sources
Helixi284 – 2863Combined sources
Helixi289 – 2946Combined sources
Helixi297 – 2993Combined sources
Helixi304 – 3063Combined sources
Beta strandi307 – 3093Combined sources
Helixi316 – 3183Combined sources
Beta strandi319 – 3213Combined sources
Helixi324 – 3263Combined sources
Helixi330 – 3323Combined sources
Helixi333 – 34513Combined sources
Beta strandi348 – 3558Combined sources
Beta strandi363 – 3664Combined sources
Turni369 – 3724Combined sources
Beta strandi375 – 3784Combined sources
Helixi400 – 4023Combined sources
Helixi404 – 41512Combined sources
Turni416 – 4183Combined sources
Beta strandi421 – 4266Combined sources
Beta strandi428 – 4369Combined sources
Turni437 – 4393Combined sources
Beta strandi440 – 4456Combined sources
Beta strandi447 – 4493Combined sources
Beta strandi451 – 4566Combined sources
Beta strandi461 – 4655Combined sources
Turni467 – 4693Combined sources
Beta strandi476 – 4794Combined sources
Beta strandi481 – 4844Combined sources
Beta strandi488 – 4947Combined sources
Beta strandi498 – 5069Combined sources
Helixi507 – 5093Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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

GeneTreeiENSGT00390000002882.
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

        10         20         30         40         50
MKFFLLLFTI GFCWAQYSPN TQQGRTSIVH LFEWRWVDIA LECERYLAPK
60 70 80 90 100
GFGGVQVSPP NENVAIYNPF RPWWERYQPV SYKLCTRSGN EDEFRNMVTR
110 120 130 140 150
CNNVGVRIYV DAVINHMCGN AVSAGTSSTC GSYFNPGSRD FPAVPYSGWD
160 170 180 190 200
FNDGKCKTGS GDIENYNDAT QVRDCRLTGL LDLALEKDYV RSKIAEYMNH
210 220 230 240 250
LIDIGVAGFR LDASKHMWPG DIKAILDKLH NLNSNWFPAG SKPFIYQEVI
260 270 280 290 300
DLGGEPIKSS DYFGNGRVTE FKYGAKLGTV IRKWNGEKMS YLKNWGEGWG
310 320 330 340 350
FVPSDRALVF VDNHDNQRGH GAGGASILTF WDARLYKMAV GFMLAHPYGF
360 370 380 390 400
TRVMSSYRWP RQFQNGNDVN DWVGPPNNNG VIKEVTINPD TTCGNDWVCE
410 420 430 440 450
HRWRQIRNMV IFRNVVDGQP FTNWYDNGSN QVAFGRGNRG FIVFNNDDWS
460 470 480 490 500
FSLTLQTGLP AGTYCDVISG DKINGNCTGI KIYVSDDGKA HFSISNSAED
510
PFIAIHAESK L
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:
EMBLi
GenBanki
DDBJi
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. [P04746-1]
PIRiA29614. ALHUP.
RefSeqiNP_000690.1. NM_000699.2. [P04746-1]
UniGeneiHs.654437.

Genome annotation databases

EnsembliENST00000414303; ENSP00000397582; ENSG00000243480. [P04746-1]
ENST00000622339; ENSP00000481450; ENSG00000243480. [P04746-1]
GeneIDi279.
KEGGihsa:279.
UCSCiuc001dut.3. human. [P04746-1]

Polymorphism databases

DMDMi113803.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

Wikipedia

Amylase entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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. [P04746-1 ]
PIRi A29614. ALHUP.
RefSeqi NP_000690.1. NM_000699.2. [P04746-1 ]
UniGenei Hs.654437.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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. 4 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 ]
ENST00000622339 ; ENSP00000481450 ; ENSG00000243480 . [P04746-1 ]
GeneIDi 279.
KEGGi hsa:279.
UCSCi uc001dut.3. human. [P04746-1 ]

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

GeneTreei ENSGT00390000002882.
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: November 26, 2014
This is version 166 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