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UniProtKB - P0DUB6 (AMY1A_HUMAN)

Entry version 6 (23 Feb 2022)
Sequence version 1 (02 Dec 2020)
Previous versions | rss
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Protein

Alpha-amylase 1A

Gene

AMY1A

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

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Calcium-binding enzyme that initiates starch digestion in the oral cavity (PubMed:12527308).

Catalyzes the hydrolysis of internal (1->4)-alpha-D-glucosidic bonds, yielding a mixture of maltose, isomaltose, small amounts of glucose as well as small linear and branched oligosaccharides called dextrins (PubMed:12527308).

1 Publication

Caution

Three distinct genes (AMY1A, AMY1B and AMY1C), located in a gene cluster on 1p21, encode proteins sharing the same peptidic sequence.Curated

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

  • Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha-linked D-glucose units.1 Publication EC:3.2.1.1

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Protein has several cofactor binding sites:

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi115CalciumCombined sources2 Publications1
Metal bindingi173Calcium; via carbonyl oxygenCombined sources2 Publications1
Metal bindingi182CalciumCombined sources2 Publications1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei210ChlorideCombined sources2 Publications1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei212Nucleophile1
Metal bindingi216Calcium; via carbonyl oxygenCombined sources2 Publications1
Active sitei248Proton donor1
Binding sitei313ChlorideCombined sources2 Publications1
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei315Transition state stabilizerBy similarity1
Binding sitei352ChlorideCombined sources2 Publications1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionGlycosidase, Hydrolase
Biological processCarbohydrate metabolism
LigandCalcium, Chloride, Metal-binding

Enzyme and pathway databases

Pathway Commons web resource for biological pathway data

More...PathwayCommonsi		P04745

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-HSA-189085, Digestion of dietary carbohydrate

Protein family/group databases

Carbohydrate-Active enZymes

More...CAZyi		GH13, Glycoside Hydrolase Family 13

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Alpha-amylase 1A (EC:3.2.1.11 Publication)
Alternative name(s):
1,4-alpha-D-glucan glucanohydrolase 1
Salivary alpha-amylase
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:AMY1AImported
Synonyms:AMY1
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 1

Organism-specific databases

Human Gene Nomenclature Database

More...HGNCi		HGNC:474, AMY1A

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		104702, gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_P0DUB6

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Keywords - Cellular componenti

Secreted

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Organism-specific databases

DisGeNET

More...DisGeNETi		276
277
278

Open Targets

More...OpenTargetsi		ENSG00000187733

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL2478

Genetic variation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		AMY1A

Domain mapping of disease mutations (DMDM)

More...DMDMi		1351933

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 15Sequence analysisAdd BLAST15
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000000140116 – 511Alpha-amylase 1AAdd BLAST496

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei16Pyrrolidone carboxylic acidBy similarity1
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi43 ↔ 101Combined sources2 Publications
Disulfide bondi85 ↔ 130Combined sources2 Publications
Disulfide bondi156 ↔ 175Combined sources2 Publications
Modified residuei365Deamidated asparagine; partial1 Publication1
Disulfide bondi393 ↔ 399Combined sources2 Publications
Modified residuei427Deamidated asparagine; partial; alternate1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi427N-linked (GlcNAc...) asparagine2 Publications1
Disulfide bondi465 ↔ 477Combined sources2 Publications
Modified residuei474Deamidated asparagine; partial1 Publication1
Glycosylationi476N-linked (GlcNAc...) asparagineSequence analysis1

Keywords - PTMi

Disulfide bond, Glycoprotein, Pyrrolidone carboxylic acid

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P04745

PaxDb, a database of protein abundance averages across all three domains of life

More...PaxDbi		P04745

PTM databases

GlyGen: Computational and Informatics Resources for Glycoscience

More...GlyGeni		P0DUB6, 2 sites

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P04745

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...PhosphoSitePlusi		P0DUB6

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		P04745, HS

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Monomer.

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		P0DUB6

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		P04745, protein

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1511
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		P0DUB6

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P04745

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the glycosyl hydrolase 13 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG2212, Eukaryota

Ensembl GeneTree

More...GeneTreei		ENSGT00940000154802

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_013336_2_1_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P04745

Identification of Orthologs from Complete Genome Data

More...OMAi		TWVETHD

Database of Orthologous Groups

More...OrthoDBi		665362at2759

TreeFam database of animal gene trees

More...TreeFami		TF312850

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		2.60.40.1180, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR006048, A-amylase/branching_C
IPR031319, A-amylase_C
IPR006046, Alpha_amylase
IPR006047, Glyco_hydro_13_cat_dom
IPR013780, Glyco_hydro_b
IPR017853, Glycoside_hydrolase_SF

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00128, Alpha-amylase, 1 hit
PF02806, Alpha-amylase_C, 1 hit

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR00110, ALPHAAMYLASE

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00642, Aamy, 1 hit
SM00632, Aamy_C, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF51445, SSF51445, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

P0DUB6-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MKLFWLLFTI GFCWAQYSSN TQQGRTSIVH LFEWRWVDIA LECERYLAPK 
        60         70         80         90        100
GFGGVQVSPP NENVAIHNPF RPWWERYQPV SYKLCTRSGN EDEFRNMVTR 
       110        120        130        140        150
CNNVGVRIYV DAVINHMCGN AVSAGTSSTC GSYFNPGSRD FPAVPYSGWD 
       160        170        180        190        200
FNDGKCKTGS GDIENYNDAT QVRDCRLSGL LDLALGKDYV RSKIAEYMNH 
       210        220        230        240        250
LIDIGVAGFR IDASKHMWPG DIKAILDKLH NLNSNWFPEG SKPFIYQEVI 
       260        270        280        290        300
DLGGEPIKSS DYFGNGRVTE FKYGAKLGTV IRKWNGEKMS YLKNWGEGWG 
       310        320        330        340        350
FMPSDRALVF VDNHDNQRGH GAGGASILTF WDARLYKMAV GFMLAHPYGF 
       360        370        380        390        400
TRVMSSYRWP RYFENGKDVN DWVGPPNDNG VTKEVTINPD TTCGNDWVCE 
       410        420        430        440        450
HRWRQIRNMV NFRNVVDGQP FTNWYDNGSN QVAFGRGNRG FIVFNNDDWT 
       460        470        480        490        500
FSLTLQTGLP AGTYCDVISG DKINGNCTGI KIYVSDDGKA HFSISNSAED 
       510 
PFIAIHAESK L
Length:511
Mass (Da):57,768
Last modified:December 2, 2020 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i7710BCAC83EBE8B2
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti285N → T in AAA57345 (PubMed:2442579).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
M18786 M18784 Genomic DNA Translation: AAA52279.1
AK292341 mRNA Translation: BAF85030.1
AC105272 Genomic DNA No translation available.
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.

The Consensus CDS (CCDS) project

More...CCDSi		CCDS30782.1

Protein sequence database of the Protein Information Resource

More...PIRi		A91543, ALHUS

NCBI Reference Sequences

More...RefSeqi		NP_001008219.1, NM_001008218.1
NP_001008220.1, NM_001008219.2
NP_001008222.1, NM_001008221.1
NP_001333709.1, NM_001346780.1
NP_004029.2, NM_004038.3
XP_011539564.1, XM_011541262.1
XP_016856547.1, XM_017001058.1

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000370083; ENSP00000359100; ENSG00000237763

Database of genes from NCBI RefSeq genomes

More...GeneIDi		276
277
278

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:276
hsa:277
hsa:278

Matched Annotation from NCBI and EMBL-EBI (MANE) - Phase one

More...MANE-Selecti		ENST00000330330.10; ENSP00000330484.5; NM_001008218.2; NP_001008219.1
ENST00000370083.9; ENSP00000359100.4; NM_004038.4; NP_004029.2
ENST00000622339.5; ENSP00000481450.2; NM_001008219.3; NP_001008220.1

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross%5Freferences%5Fsection">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Wikipedia

Amylase entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M18786 M18784 Genomic DNA Translation: AAA52279.1
AK292341 mRNA Translation: BAF85030.1
AC105272 Genomic DNA No translation available.
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
PIRiA91543, ALHUS
RefSeqiNP_001008219.1, NM_001008218.1
NP_001008220.1, NM_001008219.2
NP_001008222.1, NM_001008221.1
NP_001333709.1, NM_001346780.1
NP_004029.2, NM_004038.3
XP_011539564.1, XM_011541262.1
XP_016856547.1, XM_017001058.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB 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[»]
SMRiP0DUB6
ModBaseiSearch...
PDBe-KBiSearch...

Chemistry databases

BindingDBiP0DUB6
ChEMBLiCHEMBL2478

Protein family/group databases

CAZyiGH13, Glycoside Hydrolase Family 13

PTM databases

GlyGeniP0DUB6, 2 sites
iPTMnetiP04745
PhosphoSitePlusiP0DUB6

Genetic variation databases

BioMutaiAMY1A
DMDMi1351933

Proteomic databases

jPOSTiP04745
PaxDbiP04745

Genome annotation databases

EnsembliENST00000370083; ENSP00000359100; ENSG00000237763
GeneIDi276
277
278
KEGGihsa:276
hsa:277
hsa:278
MANE-SelectiENST00000330330.10; ENSP00000330484.5; NM_001008218.2; NP_001008219.1
ENST00000370083.9; ENSP00000359100.4; NM_004038.4; NP_004029.2
ENST00000622339.5; ENSP00000481450.2; NM_001008219.3; NP_001008220.1

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		276
277
278
DisGeNETi276
277
278

GeneCards: human genes, protein and diseases

More...GeneCardsi		AMY1A
HGNCiHGNC:474, AMY1A
MIMi104702, gene
neXtProtiNX_P0DUB6
OpenTargetsiENSG00000187733

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiKOG2212, Eukaryota
GeneTreeiENSGT00940000154802
HOGENOMiCLU_013336_2_1_1
InParanoidiP04745
OMAiTWVETHD
OrthoDBi665362at2759
TreeFamiTF312850

Enzyme and pathway databases

PathwayCommonsiP04745
ReactomeiR-HSA-189085, Digestion of dietary carbohydrate

Miscellaneous databases

EvolutionaryTraceiP04745

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		AMY1A
RNActiP04745, protein

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

GenevisibleiP04745, HS

Family and domain databases

Gene3Di2.60.40.1180, 1 hit
InterProiView protein in InterPro
IPR006048, A-amylase/branching_C
IPR031319, A-amylase_C
IPR006046, Alpha_amylase
IPR006047, Glyco_hydro_13_cat_dom
IPR013780, Glyco_hydro_b
IPR017853, Glycoside_hydrolase_SF
PfamiView protein in Pfam
PF00128, Alpha-amylase, 1 hit
PF02806, Alpha-amylase_C, 1 hit
PRINTSiPR00110, ALPHAAMYLASE
SMARTiView protein in SMART
SM00642, Aamy, 1 hit
SM00632, Aamy_C, 1 hit
SUPFAMiSSF51445, SSF51445, 1 hit

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiAMY1A_HUMAN
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P0DUB6
Secondary accession number(s): A6NJS5
, A8K8H6, P04745, Q13763, Q5T083
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 2, 2020
Last sequence update: December 2, 2020
Last modified: February 23, 2022
This is version 6 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>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.

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, 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
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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