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Entry version 223 (18 Sep 2019)
Sequence version 3 (23 Jan 2007)
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Protein

Adenosine deaminase

Gene

ADA

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

Catalyzes the hydrolytic deamination of adenosine and 2-deoxyadenosine (PubMed:8452534, PubMed:16670267). Plays an important role in purine metabolism and in adenosine homeostasis. Modulates signaling by extracellular adenosine, and so contributes indirectly to cellular signaling events. Acts as a positive regulator of T-cell coactivation, by binding DPP4 (PubMed:20959412). Its interaction with DPP4 regulates lymphocyte-epithelial cell adhesion (PubMed:11772392). Enhances dendritic cell immunogenicity by affecting dendritic cell costimulatory molecule expression and cytokines and chemokines secretion (By similarity). Enhances CD4+ T-cell differentiation and proliferation (PubMed:20959412). Acts as a positive modulator of adenosine receptors ADORA1 and ADORA2A, by enhancing their ligand affinity via conformational change (PubMed:23193172). Stimulates plasminogen activation (PubMed:15016824). Plays a role in male fertility (PubMed:21919946, PubMed:26166670). Plays a protective role in early postimplantation embryonic development (By similarity).By similarity8 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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

<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

Zn2+1 PublicationNote: Binds 1 zinc ion per subunit.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Inhibited by Cu2+ and Hg2+, coformycin, deoxycoformycin (dCF), 2-deoxyadenosine, 6-methylaminopurine riboside, 2-3-iso-propylidene-adenosine and erythro-9-(2-hydroxy-3-nonyl)adenine.2 Publications

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=37 µM for adenosine (at 25 degrees Celsius and pH 5.5)1 Publication
  1. Vmax=41 µmol/min/mg enzyme1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 bindingi15Zinc; catalytic1 Publication1
Metal bindingi17Zinc; catalytic1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 sitei17SubstrateCombined sources1 Publication1
Binding sitei19SubstrateCombined sources1 Publication1
<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>Sitei58Important for interaction with adenosine receptors and increasing their affinity for agonists1 Publication1
Sitei62Important for interaction with adenosine receptors and increasing their affinity for agonists1 Publication1
Binding sitei184Substrate; via amide nitrogenCombined sources1 Publication1
Metal bindingi214Zinc; catalytic1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 sitei217Proton donorBy similarity1
Sitei238Important for catalytic activityBy similarity1
Metal bindingi295Zinc; catalytic1 Publication1
Binding sitei296SubstrateCombined sources1 Publication1

<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

GO - Biological processi

<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 functionHydrolase
Biological processCell adhesion, Nucleotide metabolism
LigandMetal-binding, Zinc

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

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BioCyci
MetaCyc:HS02191-MONOMER

BRENDA Comprehensive Enzyme Information System

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BRENDAi
3.5.4.4 2681

Reactome - a knowledgebase of biological pathways and processes

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Reactomei
R-HSA-74217 Purine salvage

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
P00813

SignaLink: a signaling pathway resource with multi-layered regulatory networks

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SignaLinki
P00813

SIGNOR Signaling Network Open Resource

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SIGNORi
P00813

<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_and_taxonomy_section">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:
Adenosine deaminase (EC:3.5.4.43 Publications)
Alternative name(s):
Adenosine aminohydrolase
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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:ADA
Synonyms:ADA1
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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_and_taxonomy_section">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_and_taxonomy_section">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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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_manual">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 20

Organism-specific databases

Human Gene Nomenclature Database

More...
HGNCi
HGNC:186 ADA

Online Mendelian Inheritance in Man (OMIM)

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MIMi
608958 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_P00813

<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

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell junction, Cell membrane, Cytoplasm, Cytoplasmic vesicle, Lysosome, Membrane

<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

<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Severe combined immunodeficiency autosomal recessive T-cell-negative/B-cell-negative/NK-cell-negative due to adenosine deaminase deficiency (ADASCID)11 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn autosomal recessive disorder accounting for about 50% of non-X-linked SCIDs. SCID refers to a genetically and clinically heterogeneous group of rare congenital disorders characterized by impairment of both humoral and cell-mediated immunity, leukopenia, and low or absent antibody levels. Patients with SCID present in infancy with recurrent, persistent infections by opportunistic organisms. The common characteristic of all types of SCID is absence of T-cell-mediated cellular immunity due to a defect in T-cell development. ADA deficiency has been diagnosed in chronically ill teenagers and adults (late or adult onset). Population and newborn screening programs have also identified several healthy individuals with normal immunity who have partial ADA deficiency.
Related information in OMIM
Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_00221015H → D in ADASCID; loss of activity. 1 PublicationCorresponds to variant dbSNP:rs121908725EnsemblClinVar.1
Natural variantiVAR_00221120G → R in ADASCID; loss of activity. 1 PublicationCorresponds to variant dbSNP:rs121908724EnsemblClinVar.1
Natural variantiVAR_00221274G → C in ADASCID; delayed-onset. 1 PublicationCorresponds to variant dbSNP:rs121908730EnsemblClinVar.1
Natural variantiVAR_00221376R → W in ADASCID. 1 PublicationCorresponds to variant dbSNP:rs121908736EnsemblClinVar.1
Natural variantiVAR_00221583A → D in ADASCID; loss of activity. 1 PublicationCorresponds to variant dbSNP:rs121908726EnsemblClinVar.1
Natural variantiVAR_07695497Y → C in ADASCID; unknown pathological significance; loss of activity on its own; total loss of activity; when associated with V-106. 1 PublicationCorresponds to variant dbSNP:rs267606634EnsemblClinVar.1
Natural variantiVAR_002216101R → L in ADASCID. 1 PublicationCorresponds to variant dbSNP:rs121908714EnsemblClinVar.1
Natural variantiVAR_002218101R → Q in ADASCID; loss of activity. 1 PublicationCorresponds to variant dbSNP:rs121908714EnsemblClinVar.1
Natural variantiVAR_002217101R → W in ADASCID. 1 PublicationCorresponds to variant dbSNP:rs121908717EnsemblClinVar.1
Natural variantiVAR_076955106L → V in ADASCID; unknown pathological significance; 30% of activity; total loss of activity; when associated with C-97. 1 PublicationCorresponds to variant dbSNP:rs267606635EnsemblClinVar.1
Natural variantiVAR_002219107L → P in ADASCID. 1 PublicationCorresponds to variant dbSNP:rs121908739EnsemblClinVar.1
Natural variantiVAR_002220129V → M in ADASCID; delayed-onset. 1 PublicationCorresponds to variant dbSNP:rs121908731EnsemblClinVar.1
Natural variantiVAR_002221140G → E in ADASCID. 1 PublicationCorresponds to variant dbSNP:rs121908732EnsemblClinVar.1
Natural variantiVAR_002223149R → Q in ADASCID. 1 PublicationCorresponds to variant dbSNP:rs121908737EnsemblClinVar.1
Natural variantiVAR_002224149R → W in ADASCID. 1 PublicationCorresponds to variant dbSNP:rs121908733EnsemblClinVar.1
Natural variantiVAR_002226156R → C in ADASCID. 1 PublicationCorresponds to variant dbSNP:rs121908735EnsemblClinVar.1
Natural variantiVAR_002227156R → H in ADASCID; loss of activity. 1 PublicationCorresponds to variant dbSNP:rs121908722EnsemblClinVar.1
Natural variantiVAR_002228177V → M in ADASCID; loss of activity. 1 PublicationCorresponds to variant dbSNP:rs121908719EnsemblClinVar.1
Natural variantiVAR_002229179A → D in ADASCID; loss of activity. 1 PublicationCorresponds to variant dbSNP:rs121908727EnsemblClinVar.1
Natural variantiVAR_002230199Q → P in ADASCID; delayed-onset. 1 PublicationCorresponds to variant dbSNP:rs121908734EnsemblClinVar.1
Natural variantiVAR_002231211R → C in ADASCID; late onset; 4% of activity. 2 PublicationsCorresponds to variant dbSNP:rs121908740EnsemblClinVar.1
Natural variantiVAR_002232211R → H in ADASCID. 1 PublicationCorresponds to variant dbSNP:rs121908716EnsemblClinVar.1
Natural variantiVAR_002233215A → T in ADASCID; 8% of activity. 2 PublicationsCorresponds to variant dbSNP:rs114025668EnsemblClinVar.1
Natural variantiVAR_002234216G → R in ADASCID; severe. 1 PublicationCorresponds to variant dbSNP:rs121908723EnsemblClinVar.1
Natural variantiVAR_002236274P → L in ADASCID. 1 PublicationCorresponds to variant dbSNP:rs121908738EnsemblClinVar.1
Natural variantiVAR_002237291S → L in ADASCID. 2 PublicationsCorresponds to variant dbSNP:rs121908721EnsemblClinVar.1
Natural variantiVAR_002238297P → Q in ADASCID. 1 PublicationCorresponds to variant dbSNP:rs121908718EnsemblClinVar.1
Natural variantiVAR_002239304L → R in ADASCID; loss of activity. Corresponds to variant dbSNP:rs199422327EnsemblClinVar.1
Natural variantiVAR_002240329A → V in ADASCID. 1 PublicationCorresponds to variant dbSNP:rs121908715EnsemblClinVar.1
Natural variantiVAR_002241337Missing in ADASCID. 1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi58L → A: Decreases enzyme activity by reducing substrate affinity and maximum velocity; abolishes ADORA1 and ADORA2A modulator function. 1 Publication1
Mutagenesisi60D → A: Moderately reduces enzyme activity; reduces ADORA1 and ADORA2A modulation. 1 Publication1
Mutagenesisi61F → A: Decreases enzyme activity by reducing maximum velocity; reduces ADORA1 modulation. 1 Publication1
Mutagenesisi62L → A: Decreases enzyme activity by reducing substrate affinity and maximum velocity; abolishes ADORA1 and ADORA2A modulator function. 1 Publication1
Mutagenesisi64K → A: Moderately reduces enzyme activity; no change in ADORA1 and ADORA2A modulation. 1 Publication1
Mutagenesisi65F → A: Decreases enzyme activity by reducing substrate affinity and maximum velocity; reduces ADORA1 and ADORA2A modulation. 1 Publication1
Mutagenesisi66D → A: No change in enzyme activity; no change in ADORA1 and ADORA2A modulation. 1 Publication1
Mutagenesisi69M → A: Decreases enzyme activity by reducing maximum velocity; reduces ADORA2A modulation. 1 Publication1
Mutagenesisi115I → A: No change in enzyme activity; no change in ADORA1 and ADORA2A modulation. 1 Publication1
Mutagenesisi118N → A: Moderately reduces enzyme activity; no change in ADORA1 and ADORA2A modulation. 1 Publication1
Mutagenesisi155M → A: Decreases enzyme activity by reducing substrate affinity and maximum velocity. 1 Publication1
Mutagenesisi157H → A: Moderately reduces enzyme activity; no change in ADORA1 and ADORA2A modulation. 1 Publication1
Mutagenesisi184G → Q: Moderately reduces enzyme activity. 1 Publication1
Mutagenesisi185D → A: Moderately reduces enzyme activity. 1 Publication1
Mutagenesisi194L → A: No change in enzyme activity. 1 Publication1

Keywords - Diseasei

Disease mutation, Hereditary hemolytic anemia, SCID

Organism-specific databases

DisGeNET

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DisGeNETi
100

GeneReviews a resource of expert-authored, peer-reviewed disease descriptions.

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GeneReviewsi
ADA

MalaCards human disease database

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MalaCardsi
ADA
MIMi102700 phenotype

Open Targets

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OpenTargetsi
ENSG00000196839

Orphanet; a database dedicated to information on rare diseases and orphan drugs

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Orphaneti
39041 Omenn syndrome
277 Severe combined immunodeficiency due to adenosine deaminase deficiency

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA24503

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL1910

Drug and drug target database

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DrugBanki
DB07711 (2S,3R)-3-(6-amino-9H-purin-9-yl)nonan-2-ol
DB07783 1-((1R)-1-(HYDROXYMETHYL)-3-{6-[(3-PHENYLPROPANOYL)AMINO]-1H-INDOL-1-YL}PROPYL)-1H-IMIDAZOLE-4-CARBOXAMIDE
DB07786 1-((1R,2S)-1-{2-[2-(4-CHLOROPHENYL)-1,3-BENZOXAZOL-7-YL]ETHYL}-2-HYDROXYPROPYL)-1H-IMIDAZOLE-4-CARBOXAMIDE
DB04218 1-Deaza-Adenosine
DB07785 1-{(1R,2S)-2-HYDROXY-1-[2-(2-NAPHTHYLOXY)ETHYL]PROPYL}-1H-IMIDAZONE-4-CARBOXAMIDE
DB03015 6-Hydroxy-1,6-Dihydro Purine Nucleoside
DB02472 6-Hydroxy-7,8-Dihydro Purine Nucleoside
DB00640 Adenosine
DB00975 Dipyridamole
DB14600 Edetate disodium anhydrous
DB00974 Edetic Acid
DB05057 Erdosteine
DB02616 FR117016
DB02096 FR221647
DB03572 FR230513
DB03220 FR233623
DB02830 FR236913
DB03370 FR239087
DB04440 Nebularine
DB01280 Nelarabine
DB00552 Pentostatin
DB00277 Theophylline
DB00194 Vidarabine

IUPHAR/BPS Guide to PHARMACOLOGY

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GuidetoPHARMACOLOGYi
1230

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
ADA

Domain mapping of disease mutations (DMDM)

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DMDMi
113339

<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 <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved1 Publication
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001943522 – 363Adenosine deaminaseAdd BLAST362

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 residuei2N-acetylalanine1 Publication1
Modified residuei54N6-acetyllysineCombined sources1
Modified residuei232N6-acetyllysineCombined sources1

Keywords - PTMi

Acetylation

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
P00813

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
P00813

MassIVE - Mass Spectrometry Interactive Virtual Environment

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MassIVEi
P00813

MaxQB - The MaxQuant DataBase

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MaxQBi
P00813

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

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PaxDbi
P00813

PeptideAtlas

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PeptideAtlasi
P00813

PRoteomics IDEntifications database

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PRIDEi
P00813

ProteomicsDB human proteome resource

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ProteomicsDBi
51289

Consortium for Top Down Proteomics

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TopDownProteomicsi
P00813

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P00813

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

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PhosphoSitePlusi
P00813

SwissPalm database of S-palmitoylation events

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SwissPalmi
P00813

<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

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Found in all tissues, occurs in large amounts in T-lymphocytes (PubMed:20959412). Expressed at the time of weaning in gastrointestinal tissues.1 Publication

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Up-regulated by hypoxia.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000196839 Expressed in 158 organ(s), highest expression level in duodenum

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P00813 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P00813 HS

Organism-specific databases

Human Protein Atlas

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HPAi
CAB004307
HPA001399
HPA023884

<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_section">'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_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Interacts with DPP4 (via extracellular domain) (PubMed:10951221, PubMed:14691230, PubMed:7907293, PubMed:8101391, PubMed:15016824).

Interacts with PLG (via Kringle 4 domain); the interaction stimulates PLG activation when in complex with DPP4 (PubMed:15016824).

5 Publications

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
106614, 24 interactors

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
P00813

Database of interacting proteins

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DIPi
DIP-371N

Protein interaction database and analysis system

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IntActi
P00813, 7 interactors

STRING: functional protein association networks

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STRINGi
9606.ENSP00000361965

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
P00813

<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

1363
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

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SMRi
P00813

Database of comparative protein structure models

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ModBasei
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
P00813

<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

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni126 – 143Required for binding to DDP41 PublicationAdd BLAST18

<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

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG1097 Eukaryota
COG1816 LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00950000183113

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000218816

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P00813

KEGG Orthology (KO)

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KOi
K01488

Identification of Orthologs from Complete Genome Data

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OMAi
HHVGSAS

Database of Orthologous Groups

More...
OrthoDBi
900867at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P00813

TreeFam database of animal gene trees

More...
TreeFami
TF314270

Family and domain databases

Conserved Domains Database

More...
CDDi
cd01320 ADA, 1 hit

HAMAP database of protein families

More...
HAMAPi
MF_00540 A_deaminase, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR006650 A/AMP_deam_AS
IPR001365 A/AMP_deaminase_dom
IPR028893 A_deaminase
IPR006330 Ado/ade_deaminase
IPR032466 Metal_Hydrolase

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00962 A_deaminase, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF51556 SSF51556, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR01430 aden_deam, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00485 A_DEAMINASE, 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_length">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>Sequence (1+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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.

This entry has 1 described isoform and 3 potential isoforms that are computationally mapped.Show allAlign All

P00813-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAQTPAFDKP KVELHVHLDG SIKPETILYY GRRRGIALPA NTAEGLLNVI
60 70 80 90 100
GMDKPLTLPD FLAKFDYYMP AIAGCREAIK RIAYEFVEMK AKEGVVYVEV
110 120 130 140 150
RYSPHLLANS KVEPIPWNQA EGDLTPDEVV ALVGQGLQEG ERDFGVKARS
160 170 180 190 200
ILCCMRHQPN WSPKVVELCK KYQQQTVVAI DLAGDETIPG SSLLPGHVQA
210 220 230 240 250
YQEAVKSGIH RTVHAGEVGS AEVVKEAVDI LKTERLGHGY HTLEDQALYN
260 270 280 290 300
RLRQENMHFE ICPWSSYLTG AWKPDTEHAV IRLKNDQANY SLNTDDPLIF
310 320 330 340 350
KSTLDTDYQM TKRDMGFTEE EFKRLNINAA KSSFLPEDEK RELLDLLYKA
360
YGMPPSASAG QNL
Length:363
Mass (Da):40,764
Last modified:January 23, 2007 - v3
<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:i786BC5085CA9AFCB
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
F5GWI4F5GWI4_HUMAN
Adenosine deaminase
ADA
339Annotation score:

Annotation score:1 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>
F5GXW0F5GXW0_HUMAN
Adenosine deaminase
ADA
263Annotation score:

Annotation score:1 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>
F5GYD4F5GYD4_HUMAN
Adenosine deaminase
ADA
75Annotation score:

Annotation score:1 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 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 conflicti340K → R in BAD97117 (Ref. 5) Curated1

<p>This subsection of the ‘Sequence’ section provides information on polymorphic variants. If the variant is associated with a disease state, the description of the latter can be found in the <a href="http://www.uniprot.org/manual/involvement_in_disease">'Involvement in disease'</a> subsection.<p><a href='/help/polymorphism' target='_top'>More...</a></p>Polymorphismi

There is a common allele, ADA*2, also known as the ADA 2 allozyme. It is associated with the reduced metabolism of adenosine to inosine. It specifically enhances deep sleep and slow-wave activity (SWA) during sleep.1 Publication

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0022098D → N Polymorphism; allele ADA*2; found in about 10% of the population; affects duration and intensity of deep sleep; enhances negative effects of sleep loss during sleep deprivation; may have a protective role against male infertility; 20% to 30% decrease in activity. 4 PublicationsCorresponds to variant dbSNP:rs73598374EnsemblClinVar.1
Natural variantiVAR_00221015H → D in ADASCID; loss of activity. 1 PublicationCorresponds to variant dbSNP:rs121908725EnsemblClinVar.1
Natural variantiVAR_00221120G → R in ADASCID; loss of activity. 1 PublicationCorresponds to variant dbSNP:rs121908724EnsemblClinVar.1
Natural variantiVAR_00221274G → C in ADASCID; delayed-onset. 1 PublicationCorresponds to variant dbSNP:rs121908730EnsemblClinVar.1
Natural variantiVAR_00221376R → W in ADASCID. 1 PublicationCorresponds to variant dbSNP:rs121908736EnsemblClinVar.1
Natural variantiVAR_00221480K → R1 PublicationCorresponds to variant dbSNP:rs11555566EnsemblClinVar.1
Natural variantiVAR_00221583A → D in ADASCID; loss of activity. 1 PublicationCorresponds to variant dbSNP:rs121908726EnsemblClinVar.1
Natural variantiVAR_07695497Y → C in ADASCID; unknown pathological significance; loss of activity on its own; total loss of activity; when associated with V-106. 1 PublicationCorresponds to variant dbSNP:rs267606634EnsemblClinVar.1
Natural variantiVAR_002216101R → L in ADASCID. 1 PublicationCorresponds to variant dbSNP:rs121908714EnsemblClinVar.1
Natural variantiVAR_002218101R → Q in ADASCID; loss of activity. 1 PublicationCorresponds to variant dbSNP:rs121908714EnsemblClinVar.1
Natural variantiVAR_002217101R → W in ADASCID. 1 PublicationCorresponds to variant dbSNP:rs121908717EnsemblClinVar.1
Natural variantiVAR_076955106L → V in ADASCID; unknown pathological significance; 30% of activity; total loss of activity; when associated with C-97. 1 PublicationCorresponds to variant dbSNP:rs267606635EnsemblClinVar.1
Natural variantiVAR_002219107L → P in ADASCID. 1 PublicationCorresponds to variant dbSNP:rs121908739EnsemblClinVar.1
Natural variantiVAR_002220129V → M in ADASCID; delayed-onset. 1 PublicationCorresponds to variant dbSNP:rs121908731EnsemblClinVar.1
Natural variantiVAR_002221140G → E in ADASCID. 1 PublicationCorresponds to variant dbSNP:rs121908732EnsemblClinVar.1
Natural variantiVAR_002222142R → Q in a pancreatic ductal adenocarcinoma sample; somatic mutation. 2 PublicationsCorresponds to variant dbSNP:rs61732239EnsemblClinVar.1
Natural variantiVAR_002223149R → Q in ADASCID. 1 PublicationCorresponds to variant dbSNP:rs121908737EnsemblClinVar.1
Natural variantiVAR_002224149R → W in ADASCID. 1 PublicationCorresponds to variant dbSNP:rs121908733EnsemblClinVar.1
Natural variantiVAR_002225152L → M in an individual with partial ADA deficiency but no immunodeficiency; 1,5% of activity. 1 PublicationCorresponds to variant dbSNP:rs121908728EnsemblClinVar.1
Natural variantiVAR_002226156R → C in ADASCID. 1 PublicationCorresponds to variant dbSNP:rs121908735EnsemblClinVar.1
Natural variantiVAR_002227156R → H in ADASCID; loss of activity. 1 PublicationCorresponds to variant dbSNP:rs121908722EnsemblClinVar.1
Natural variantiVAR_002228177V → M in ADASCID; loss of activity. 1 PublicationCorresponds to variant dbSNP:rs121908719EnsemblClinVar.1
Natural variantiVAR_002229179A → D in ADASCID; loss of activity. 1 PublicationCorresponds to variant dbSNP:rs121908727EnsemblClinVar.1
Natural variantiVAR_002230199Q → P in ADASCID; delayed-onset. 1 PublicationCorresponds to variant dbSNP:rs121908734EnsemblClinVar.1
Natural variantiVAR_002231211R → C in ADASCID; late onset; 4% of activity. 2 PublicationsCorresponds to variant dbSNP:rs121908740EnsemblClinVar.1
Natural variantiVAR_002232211R → H in ADASCID. 1 PublicationCorresponds to variant dbSNP:rs121908716EnsemblClinVar.1
Natural variantiVAR_002233215A → T in ADASCID; 8% of activity. 2 PublicationsCorresponds to variant dbSNP:rs114025668EnsemblClinVar.1
Natural variantiVAR_002234216G → R in ADASCID; severe. 1 PublicationCorresponds to variant dbSNP:rs121908723EnsemblClinVar.1
Natural variantiVAR_002235233T → I in an individual with partial ADA deficiency but no immunodeficiency; 20% of activity. 2 PublicationsCorresponds to variant dbSNP:rs121908729EnsemblClinVar.1
Natural variantiVAR_002236274P → L in ADASCID. 1 PublicationCorresponds to variant dbSNP:rs121908738EnsemblClinVar.1
Natural variantiVAR_002237291S → L in ADASCID. 2 PublicationsCorresponds to variant dbSNP:rs121908721EnsemblClinVar.1
Natural variantiVAR_002238297P → Q in ADASCID. 1 PublicationCorresponds to variant dbSNP:rs121908718EnsemblClinVar.1
Natural variantiVAR_002239304L → R in ADASCID; loss of activity. Corresponds to variant dbSNP:rs199422327EnsemblClinVar.1
Natural variantiVAR_002240329A → V in ADASCID. 1 PublicationCorresponds to variant dbSNP:rs121908715EnsemblClinVar.1
Natural variantiVAR_002241337Missing in ADASCID. 1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
X02994 mRNA Translation: CAA26734.1
X02189
, X02190, X02191, X02192, X02193, X02194, X02195, X02196, X02197, X02198, X02199 Genomic DNA Translation: CAA26130.1 Sequence problems.
M13792 Genomic DNA Translation: AAA78791.1
AL139352 Genomic DNA No translation available.
Z97053 Genomic DNA No translation available.
AK223397 mRNA Translation: BAD97117.1
BC007678 mRNA Translation: AAH07678.1
BC040226 mRNA Translation: AAH40226.1

The Consensus CDS (CCDS) project

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CCDSi
CCDS13335.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A91032 DUHUA

NCBI Reference Sequences

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RefSeqi
NP_000013.2, NM_000022.3

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000372874; ENSP00000361965; ENSG00000196839

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
100

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:100

UCSC genome browser

More...
UCSCi
uc002xmj.4 human

Keywords - Coding sequence diversityi

Polymorphism

<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_references_section">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

ADAbase

ADA mutation db

Wikipedia

Adenosine deaminase entry

Mendelian genes adenosine deaminase (ADA)

Leiden Open Variation Database (LOVD)

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X02994 mRNA Translation: CAA26734.1
X02189
, X02190, X02191, X02192, X02193, X02194, X02195, X02196, X02197, X02198, X02199 Genomic DNA Translation: CAA26130.1 Sequence problems.
M13792 Genomic DNA Translation: AAA78791.1
AL139352 Genomic DNA No translation available.
Z97053 Genomic DNA No translation available.
AK223397 mRNA Translation: BAD97117.1
BC007678 mRNA Translation: AAH07678.1
BC040226 mRNA Translation: AAH40226.1
CCDSiCCDS13335.1
PIRiA91032 DUHUA
RefSeqiNP_000013.2, NM_000022.3

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1M7Mmodel-A1-363[»]
3IARX-ray1.52A5-363[»]
SMRiP00813
ModBaseiSearch...

Protein-protein interaction databases

BioGridi106614, 24 interactors
CORUMiP00813
DIPiDIP-371N
IntActiP00813, 7 interactors
STRINGi9606.ENSP00000361965

Chemistry databases

BindingDBiP00813
ChEMBLiCHEMBL1910
DrugBankiDB07711 (2S,3R)-3-(6-amino-9H-purin-9-yl)nonan-2-ol
DB07783 1-((1R)-1-(HYDROXYMETHYL)-3-{6-[(3-PHENYLPROPANOYL)AMINO]-1H-INDOL-1-YL}PROPYL)-1H-IMIDAZOLE-4-CARBOXAMIDE
DB07786 1-((1R,2S)-1-{2-[2-(4-CHLOROPHENYL)-1,3-BENZOXAZOL-7-YL]ETHYL}-2-HYDROXYPROPYL)-1H-IMIDAZOLE-4-CARBOXAMIDE
DB04218 1-Deaza-Adenosine
DB07785 1-{(1R,2S)-2-HYDROXY-1-[2-(2-NAPHTHYLOXY)ETHYL]PROPYL}-1H-IMIDAZONE-4-CARBOXAMIDE
DB03015 6-Hydroxy-1,6-Dihydro Purine Nucleoside
DB02472 6-Hydroxy-7,8-Dihydro Purine Nucleoside
DB00640 Adenosine
DB00975 Dipyridamole
DB14600 Edetate disodium anhydrous
DB00974 Edetic Acid
DB05057 Erdosteine
DB02616 FR117016
DB02096 FR221647
DB03572 FR230513
DB03220 FR233623
DB02830 FR236913
DB03370 FR239087
DB04440 Nebularine
DB01280 Nelarabine
DB00552 Pentostatin
DB00277 Theophylline
DB00194 Vidarabine

DrugCentral

More...
DrugCentrali
P00813
GuidetoPHARMACOLOGYi1230

PTM databases

iPTMnetiP00813
PhosphoSitePlusiP00813
SwissPalmiP00813

Polymorphism and mutation databases

BioMutaiADA
DMDMi113339

Proteomic databases

EPDiP00813
jPOSTiP00813
MassIVEiP00813
MaxQBiP00813
PaxDbiP00813
PeptideAtlasiP00813
PRIDEiP00813
ProteomicsDBi51289
TopDownProteomicsiP00813

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
100
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000372874; ENSP00000361965; ENSG00000196839
GeneIDi100
KEGGihsa:100
UCSCiuc002xmj.4 human

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
100
DisGeNETi100

GeneCards: human genes, protein and diseases

More...
GeneCardsi
ADA
GeneReviewsiADA
HGNCiHGNC:186 ADA
HPAiCAB004307
HPA001399
HPA023884
MalaCardsiADA
MIMi102700 phenotype
608958 gene
neXtProtiNX_P00813
OpenTargetsiENSG00000196839
Orphaneti39041 Omenn syndrome
277 Severe combined immunodeficiency due to adenosine deaminase deficiency
PharmGKBiPA24503

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG1097 Eukaryota
COG1816 LUCA
GeneTreeiENSGT00950000183113
HOGENOMiHOG000218816
InParanoidiP00813
KOiK01488
OMAiHHVGSAS
OrthoDBi900867at2759
PhylomeDBiP00813
TreeFamiTF314270

Enzyme and pathway databases

BioCyciMetaCyc:HS02191-MONOMER
BRENDAi3.5.4.4 2681
ReactomeiR-HSA-74217 Purine salvage
SABIO-RKiP00813
SignaLinkiP00813
SIGNORiP00813

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...
ChiTaRSi
ADA human
EvolutionaryTraceiP00813

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
Adenosine_deaminase

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...
GenomeRNAii
100

Pharos

More...
Pharosi
P00813

Protein Ontology

More...
PROi
PR:P00813

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000196839 Expressed in 158 organ(s), highest expression level in duodenum
ExpressionAtlasiP00813 baseline and differential
GenevisibleiP00813 HS

Family and domain databases

CDDicd01320 ADA, 1 hit
HAMAPiMF_00540 A_deaminase, 1 hit
InterProiView protein in InterPro
IPR006650 A/AMP_deam_AS
IPR001365 A/AMP_deaminase_dom
IPR028893 A_deaminase
IPR006330 Ado/ade_deaminase
IPR032466 Metal_Hydrolase
PfamiView protein in Pfam
PF00962 A_deaminase, 1 hit
SUPFAMiSSF51556 SSF51556, 1 hit
TIGRFAMsiTIGR01430 aden_deam, 1 hit
PROSITEiView protein in PROSITE
PS00485 A_DEAMINASE, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

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 nameiADA_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: P00813
Secondary accession number(s): Q53F92, Q6LA59
<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_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: September 18, 2019
This is version 223 of the entry and version 3 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, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Human chromosome 20
    Human chromosome 20: entries, gene names and cross-references to MIM
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
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