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Protein

Pancreatic alpha-amylase

Gene

AMY2A

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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.4 Publications

Cofactori

Protein has several cofactor binding sites:

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi115CalciumCombined sources4 Publications1
Metal bindingi173Calcium; via carbonyl oxygenCombined sources4 Publications1
Metal bindingi182CalciumCombined sources4 Publications1
Binding sitei210ChlorideCombined sources4 Publications1
Active sitei212Nucleophile3 Publications1
Metal bindingi216Calcium; via carbonyl oxygenCombined sources4 Publications1
Active sitei248Proton donor4 Publications1
Binding sitei313ChlorideCombined sources4 Publications1
Sitei315Transition state stabilizer3 Publications1
Binding sitei352ChlorideCombined sources4 Publications1

GO - Molecular functioni

  • alpha-amylase activity Source: UniProtKB
  • calcium ion binding Source: UniProtKB
  • chloride ion binding Source: UniProtKB

GO - Biological processi

  • carbohydrate catabolic process Source: UniProtKB
  • carbohydrate metabolic process Source: ProtInc
  • polysaccharide digestion 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

BioCyciZFISH:HS10841-MONOMER.
BRENDAi3.2.1.1. 2681.
ReactomeiR-HSA-189085. 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:3.2.1.14 Publications)
Short name:
PA
Alternative name(s):
1,4-alpha-D-glucan glucanohydrolase
Gene namesi
Name:AMY2A
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:477. AMY2A.

Subcellular locationi

GO - Cellular componenti

  • extracellular exosome Source: UniProtKB
  • extracellular region Source: Reactome
  • extracellular space Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi210R → A or Q: Abolishes chloride binding; strongly reduces activity. 1 Publication1
Mutagenesisi212D → A or N: Abolishes activity. 3 Publications1
Mutagenesisi248E → A or Q: Reduces activity. 2 Publications1
Mutagenesisi313N → S: Reduces affinity for chloride; reduces activity. 1 Publication1
Mutagenesisi315D → A or N: Strongly reduces activity. 2 Publications1
Mutagenesisi352R → A: Abolishes chloride binding; has only slight effect on activity. 1 Publication1

Organism-specific databases

DisGeNETi279.
OpenTargetsiENSG00000243480.
PharmGKBiPA24784.

Chemistry databases

ChEMBLiCHEMBL2045.
DrugBankiDB00284. Acarbose.
DB00702. Icodextrin.
DB00491. Miglitol.

Polymorphism and mutation databases

BioMutaiAMY2A.
DMDMi113803.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 15Add BLAST15
ChainiPRO_000000139716 – 511Pancreatic alpha-amylaseAdd BLAST496

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei16Pyrrolidone carboxylic acid2 Publications1
Disulfide bondi43 ↔ 101Combined sources4 Publications
Disulfide bondi85 ↔ 130Combined sources4 Publications
Disulfide bondi156 ↔ 175Combined sources4 Publications
Disulfide bondi393 ↔ 399Combined sources4 Publications
Disulfide bondi465 ↔ 477Combined sources4 Publications
Glycosylationi476N-linked (GlcNAc...)3 Publications1

Keywords - PTMi

Disulfide bond, Glycoprotein, Pyrrolidone carboxylic acid

Proteomic databases

MaxQBiP04746.
PaxDbiP04746.
PeptideAtlasiP04746.
PRIDEiP04746.

PTM databases

iPTMnetiP04746.
PhosphoSitePlusiP04746.

Expressioni

Tissue specificityi

Detected in pancreas (at protein level).1 Publication

Gene expression databases

BgeeiENSG00000243480.
CleanExiHS_AMY2A.
ExpressionAtlasiP04746. baseline and differential.
GenevisibleiP04746. HS.

Organism-specific databases

HPAiCAB045960.
HPA045394.
HPA045399.
HPA046980.

Interactioni

Subunit structurei

Monomer.

Protein-protein interaction databases

BioGridi106776. 4 interactors.
IntActiP04746. 4 interactors.
STRINGi9606.ENSP00000397582.

Chemistry databases

BindingDBiP04746.

Structurei

Secondary structure

1511
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi27 – 31Combined sources5
Helixi36 – 45Combined sources10
Turni46 – 51Combined sources6
Beta strandi54 – 57Combined sources4
Turni67 – 70Combined sources4
Helixi73 – 77Combined sources5
Beta strandi78 – 80Combined sources3
Helixi91 – 103Combined sources13
Beta strandi107 – 112Combined sources6
Beta strandi115 – 119Combined sources5
Beta strandi124 – 126Combined sources3
Beta strandi128 – 130Combined sources3
Helixi136 – 138Combined sources3
Turni142 – 145Combined sources4
Helixi148 – 150Combined sources3
Turni153 – 155Combined sources3
Beta strandi158 – 162Combined sources5
Helixi169 – 174Combined sources6
Helixi177 – 179Combined sources3
Beta strandi180 – 183Combined sources4
Helixi188 – 204Combined sources17
Beta strandi208 – 211Combined sources4
Helixi214 – 216Combined sources3
Helixi219 – 226Combined sources8
Turni234 – 236Combined sources3
Beta strandi244 – 247Combined sources4
Beta strandi253 – 256Combined sources4
Helixi259 – 262Combined sources4
Turni263 – 265Combined sources3
Beta strandi266 – 269Combined sources4
Helixi271 – 282Combined sources12
Helixi284 – 286Combined sources3
Helixi289 – 294Combined sources6
Helixi297 – 299Combined sources3
Helixi304 – 306Combined sources3
Beta strandi307 – 309Combined sources3
Helixi316 – 318Combined sources3
Beta strandi319 – 321Combined sources3
Helixi324 – 326Combined sources3
Helixi330 – 332Combined sources3
Helixi333 – 345Combined sources13
Beta strandi348 – 355Combined sources8
Beta strandi363 – 366Combined sources4
Turni369 – 372Combined sources4
Beta strandi375 – 378Combined sources4
Helixi400 – 402Combined sources3
Helixi404 – 415Combined sources12
Turni416 – 418Combined sources3
Beta strandi421 – 426Combined sources6
Beta strandi428 – 436Combined sources9
Turni437 – 439Combined sources3
Beta strandi440 – 445Combined sources6
Beta strandi447 – 449Combined sources3
Beta strandi451 – 456Combined sources6
Beta strandi461 – 465Combined sources5
Turni467 – 469Combined sources3
Beta strandi476 – 479Combined sources4
Beta strandi481 – 484Combined sources4
Beta strandi488 – 494Combined sources7
Beta strandi498 – 500Combined sources3
Beta strandi502 – 506Combined sources5
Helixi507 – 509Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4W93X-ray1.35A17-511[»]
4X9YX-ray1.07A17-511[»]
5E0FX-ray1.40A17-511[»]
5EMYX-ray1.23A17-511[»]
ProteinModelPortaliP04746.
SMRiP04746.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP04746.

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 13 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG2212. Eukaryota.
COG0366. LUCA.
GeneTreeiENSGT00390000002882.
HOGENOMiHOG000253313.
HOVERGENiHBG000061.
InParanoidiP04746.
KOiK01176.
OMAiDANDWIG.
OrthoDBiEOG091G07V6.
PhylomeDBiP04746.
TreeFamiTF312850.

Family and domain databases

Gene3Di2.60.40.1180. 1 hit.
3.20.20.80. 1 hit.
InterProiIPR006048. A-amylase/branching_C.
IPR031319. A-amylase_C.
IPR006046. Alpha_amylase.
IPR015902. Glyco_hydro_13.
IPR006047. Glyco_hydro_13_cat_dom.
IPR013780. Glyco_hydro_b.
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. AlignAdd to basket

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)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_055822250 – 265IDLGG…DYFGN → HQYLYAYKISSYSLEN in isoform 2. 1 PublicationAdd BLAST16
Alternative sequenceiVSP_055823266 – 511Missing in isoform 2. 1 PublicationAdd BLAST246

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_000699.3. [P04746-1]
UniGeneiHs.654437.

Genome annotation databases

EnsembliENST00000414303; ENSP00000397582; ENSG00000243480. [P04746-1]
ENST00000622339; ENSP00000481450; ENSG00000243480. [P04746-1]
GeneIDi279.
KEGGihsa:279.
UCSCiuc001dut.4. human. [P04746-1]

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.
CCDSiCCDS783.1. [P04746-1]
PIRiA29614. ALHUP.
RefSeqiNP_000690.1. NM_000699.3. [P04746-1]
UniGeneiHs.654437.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4W93X-ray1.35A17-511[»]
4X9YX-ray1.07A17-511[»]
5E0FX-ray1.40A17-511[»]
5EMYX-ray1.23A17-511[»]
ProteinModelPortaliP04746.
SMRiP04746.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi106776. 4 interactors.
IntActiP04746. 4 interactors.
STRINGi9606.ENSP00000397582.

Chemistry databases

BindingDBiP04746.
ChEMBLiCHEMBL2045.
DrugBankiDB00284. Acarbose.
DB00702. Icodextrin.
DB00491. Miglitol.

Protein family/group databases

CAZyiGH13. Glycoside Hydrolase Family 13.

PTM databases

iPTMnetiP04746.
PhosphoSitePlusiP04746.

Polymorphism and mutation databases

BioMutaiAMY2A.
DMDMi113803.

Proteomic databases

MaxQBiP04746.
PaxDbiP04746.
PeptideAtlasiP04746.
PRIDEiP04746.

Protocols and materials databases

DNASUi279.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000414303; ENSP00000397582; ENSG00000243480. [P04746-1]
ENST00000622339; ENSP00000481450; ENSG00000243480. [P04746-1]
GeneIDi279.
KEGGihsa:279.
UCSCiuc001dut.4. human. [P04746-1]

Organism-specific databases

CTDi279.
DisGeNETi279.
GeneCardsiAMY2A.
HGNCiHGNC:477. AMY2A.
HPAiCAB045960.
HPA045394.
HPA045399.
HPA046980.
MIMi104650. gene.
neXtProtiNX_P04746.
OpenTargetsiENSG00000243480.
PharmGKBiPA24784.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2212. Eukaryota.
COG0366. LUCA.
GeneTreeiENSGT00390000002882.
HOGENOMiHOG000253313.
HOVERGENiHBG000061.
InParanoidiP04746.
KOiK01176.
OMAiDANDWIG.
OrthoDBiEOG091G07V6.
PhylomeDBiP04746.
TreeFamiTF312850.

Enzyme and pathway databases

BioCyciZFISH:HS10841-MONOMER.
BRENDAi3.2.1.1. 2681.
ReactomeiR-HSA-189085. Digestion of dietary carbohydrate.
SABIO-RKP04746.

Miscellaneous databases

EvolutionaryTraceiP04746.
GeneWikiiAMY2A.
GenomeRNAii279.
PROiP04746.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000243480.
CleanExiHS_AMY2A.
ExpressionAtlasiP04746. baseline and differential.
GenevisibleiP04746. HS.

Family and domain databases

Gene3Di2.60.40.1180. 1 hit.
3.20.20.80. 1 hit.
InterProiIPR006048. A-amylase/branching_C.
IPR031319. A-amylase_C.
IPR006046. Alpha_amylase.
IPR015902. Glyco_hydro_13.
IPR006047. Glyco_hydro_13_cat_dom.
IPR013780. Glyco_hydro_b.
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...

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 30, 2016
This is version 185 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.