Human Gene AMY2A (ENST00000414303.7) from GENCODE V44
  Description: Homo sapiens amylase alpha 2A (AMY2A), mRNA. (from RefSeq NM_000699)
RefSeq Summary (NM_000699): This gene encodes a member of the alpha-amylase family of proteins. Amylases are secreted proteins that hydrolyze 1,4-alpha-glucoside bonds in oligosaccharides and polysaccharides, catalyzing the first step in digestion of dietary starch and glycogen. This gene and several family members are present in a gene cluster on chromosome 1. This gene encodes an amylase isoenzyme produced by the pancreas. [provided by RefSeq, Jan 2015].
Gencode Transcript: ENST00000414303.7
Gencode Gene: ENSG00000243480.8
Transcript (Including UTRs)
   Position: hg38 chr1:103,617,427-103,625,780 Size: 8,354 Total Exon Count: 10 Strand: +
Coding Region
   Position: hg38 chr1:103,617,441-103,625,746 Size: 8,306 Coding Exon Count: 10 

Page IndexSequence and LinksUniProtKB CommentsPrimersMalaCardsCTD
RNA-Seq ExpressionRNA StructureProtein StructureOther SpeciesGO AnnotationsmRNA Descriptions
PathwaysOther NamesMethods
Data last updated at UCSC: 2023-08-18 00:09:47

-  Sequence and Links to Tools and Databases
 
Genomic Sequence (chr1:103,617,427-103,625,780)mRNA (may differ from genome)Protein (511 aa)
Gene SorterGenome BrowserOther Species FASTAGene interactionsTable SchemaAlphaFold
BioGPSEnsemblEntrez GeneExonPrimerGencodeGeneCards
HGNCHPRDMalacardsMGIneXtProtOMIM
PubMedReactomeUniProtKBWikipediaBioGrid CRISPR DB

-  Comments and Description Text from UniProtKB
  ID: AMYP_HUMAN
DESCRIPTION: RecName: Full=Pancreatic alpha-amylase; Short=PA; EC=3.2.1.1; AltName: Full=1,4-alpha-D-glucan glucanohydrolase; Flags: Precursor;
CATALYTIC ACTIVITY: Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha- linked D-glucose units.
COFACTOR: Binds 1 calcium ion per subunit.
COFACTOR: Binds 1 chloride ion per subunit.
SUBUNIT: Monomer.
SUBCELLULAR LOCATION: Secreted, extracellular space.
SIMILARITY: Belongs to the glycosyl hydrolase 13 family.
WEB RESOURCE: Name=Wikipedia; Note=Amylase entry; URL="http://en.wikipedia.org/wiki/Amylase";

-  Primer design for this transcript
 

Primer3Plus can design qPCR Primers that straddle exon-exon-junctions, which amplify only cDNA, not genomic DNA.
Click here to load the transcript sequence and exon structure into Primer3Plus

Exonprimer can design one pair of Sanger sequencing primers around every exon, located in non-genic sequence.
Click here to open Exonprimer with this transcript

To design primers for a non-coding sequence, zoom to a region of interest and select from the drop-down menu: View > In External Tools > Primer3


-  MalaCards Disease Associations
  MalaCards Gene Search: AMY2A
Diseases sorted by gene-association score: pancreatitis (4)

-  Comparative Toxicogenomics Database (CTD)
  The following chemicals interact with this gene           more ... click here to view the complete list

-  RNA-Seq Expression Data from GTEx (53 Tissues, 570 Donors)
  Highest median expression: 4299.33 RPKM in Pancreas
Total median expression: 4325.87 RPKM



View in GTEx track of Genome Browser    View at GTEx portal     View GTEx Body Map

-  mRNA Secondary Structure of 3' and 5' UTRs
 
RegionFold EnergyBasesEnergy/Base
Display As
3' UTR 0.00340.000 Picture PostScript Text

The RNAfold program from the Vienna RNA Package is used to perform the secondary structure predictions and folding calculations. The estimated folding energy is in kcal/mol. The more negative the energy, the more secondary structure the RNA is likely to have.

-  Protein Domain and Structure Information
  InterPro Domains: Graphical view of domain structure
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

Pfam Domains:
PF00128 - Alpha amylase, catalytic domain
PF02806 - Alpha amylase, C-terminal all-beta domain

Protein Data Bank (PDB) 3-D Structure
MuPIT help
1B2Y - X-ray 1BSI - X-ray MuPIT 1CPU - X-ray MuPIT 1HNY - X-ray 1KB3 - X-ray MuPIT 1KBB - X-ray MuPIT 1KBK - X-ray MuPIT 1KGU - X-ray MuPIT 1KGW - X-ray MuPIT 1KGX - X-ray MuPIT 1U2Y - X-ray MuPIT 1U30 - X-ray MuPIT 1U33 - X-ray MuPIT 1XCW - X-ray MuPIT 1XCX - X-ray MuPIT 1XD0 - X-ray MuPIT 1XD1 - X-ray MuPIT 1XGZ - X-ray MuPIT 1XH0 - X-ray MuPIT 1XH1 - X-ray MuPIT 1XH2 - X-ray MuPIT 2CPU - X-ray MuPIT 2QMK - X-ray MuPIT 2QV4 - X-ray MuPIT 3BAI - X-ray MuPIT 3BAJ - X-ray MuPIT 3BAK - X-ray MuPIT 3BAW - X-ray MuPIT 3BAX - X-ray MuPIT 3BAY - X-ray MuPIT 3CPU - X-ray MuPIT 3IJ7 - X-ray MuPIT 3IJ8 - X-ray MuPIT 3IJ9 - X-ray MuPIT 3OLD - X-ray MuPIT 3OLE - X-ray MuPIT 3OLG - X-ray MuPIT 3OLI - X-ray MuPIT


ModBase Predicted Comparative 3D Structure on P04746
FrontTopSide
The pictures above may be empty if there is no ModBase structure for the protein. The ModBase structure frequently covers just a fragment of the protein. You may be asked to log onto ModBase the first time you click on the pictures. It is simplest after logging in to just click on the picture again to get to the specific info on that model.

-  Orthologous Genes in Other Species
  Orthologies between human, mouse, and rat are computed by taking the best BLASTP hit, and filtering out non-syntenic hits. For more distant species reciprocal-best BLASTP hits are used. Note that the absence of an ortholog in the table below may reflect incomplete annotations in the other species rather than a true absence of the orthologous gene.
MouseRatZebrafishD. melanogasterC. elegansS. cerevisiae
No orthologNo orthologGenome BrowserNo orthologNo orthologNo ortholog
      
      
  Ensembl   
  Protein Sequence   
  Alignment   

-  Gene Ontology (GO) Annotations with Structured Vocabulary
  Molecular Function:
GO:0003824 catalytic activity
GO:0004556 alpha-amylase activity
GO:0005509 calcium ion binding
GO:0016787 hydrolase activity
GO:0016798 hydrolase activity, acting on glycosyl bonds
GO:0031404 chloride ion binding
GO:0043169 cation binding
GO:0046872 metal ion binding

Biological Process:
GO:0005975 carbohydrate metabolic process
GO:0008152 metabolic process
GO:0016052 carbohydrate catabolic process
GO:0044245 polysaccharide digestion

Cellular Component:
GO:0005576 extracellular region
GO:0005615 extracellular space
GO:0070062 extracellular exosome


-  Descriptions from all associated GenBank mRNAs
  BC146997 - Homo sapiens amylase, alpha 2A (pancreatic), mRNA (cDNA clone MGC:182100 IMAGE:9056925), complete cds.
BC007060 - Homo sapiens amylase, alpha 2A (pancreatic), mRNA (cDNA clone MGC:12504 IMAGE:3949799), complete cds.
M28443 - Human pancreatic amylase (amy2A) mRNA, complete cds.
AK223463 - Homo sapiens mRNA for amylase, alpha 2A; pancreatic precursor variant, clone: FCC117B01.
CU675523 - Synthetic construct Homo sapiens gateway clone IMAGE:100017381 5' read AMY2A mRNA.
DQ896151 - Synthetic construct Homo sapiens clone IMAGE:100010611; FLH194735.01L; RZPDo839E0770D amylase, alpha 2A; pancreatic (AMY2A) gene, encodes complete protein.
DQ892901 - Synthetic construct clone IMAGE:100005531; FLH194739.01X; RZPDo839E0780D amylase, alpha 2A; pancreatic (AMY2A) gene, encodes complete protein.
KJ890671 - Synthetic construct Homo sapiens clone ccsbBroadEn_00065 AMY2A gene, encodes complete protein.

-  Biochemical and Signaling Pathways
  Reactome (by CSHL, EBI, and GO)

Protein P04746 (Reactome details) participates in the following event(s):

R-HSA-188979 Digestion of linear starch (amylose) by extracellular amylase
R-HSA-191114 Digestion of branched starch (amylopectin) by extracellular amylase
R-HSA-189085 Digestion of dietary carbohydrate
R-HSA-8935690 Digestion
R-HSA-8963743 Digestion and absorption

-  Other Names for This Gene
  Alternate Gene Symbols: AMYP_HUMAN, ENST00000414303.1, ENST00000414303.2, ENST00000414303.3, ENST00000414303.4, ENST00000414303.5, ENST00000414303.6, NM_000699, P04746, Q9UBH3, uc001dut.1, uc001dut.2, uc001dut.3, uc001dut.4, uc001dut.5
UCSC ID: ENST00000414303.7
RefSeq Accession: NM_000699
Protein: P04746 (aka AMYP_HUMAN)

-  Methods, Credits, and Use Restrictions
  Click here for details on how this gene model was made and data restrictions if any.