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Protein

Adenosine deaminase

Gene

ADA

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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

Catalytic activityi

Adenosine + H2O = inosine + NH3.3 Publications

Cofactori

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

Enzyme 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

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
Metal bindingi15Zinc; catalytic1 Publication1
Metal bindingi17Zinc; catalytic1 Publication1
Binding sitei17SubstrateCombined sources1 Publication1
Binding sitei19SubstrateCombined sources1 Publication1
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
Active sitei217Proton donorBy similarity1
Sitei238Important for catalytic activityBy similarity1
Metal bindingi295Zinc; catalytic1 Publication1
Binding sitei296SubstrateCombined sources1 Publication1

GO - Molecular functioni

  • adenosine deaminase activity Source: UniProtKB
  • purine nucleoside binding Source: Ensembl
  • zinc ion binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Cell adhesion, Nucleotide metabolism

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciMetaCyc:HS02191-MONOMER.
ZFISH:HS02191-MONOMER.
BRENDAi3.5.4.4. 2681.
ReactomeiR-HSA-74217. Purine salvage.
SABIO-RKP00813.
SignaLinkiP00813.

Names & Taxonomyi

Protein namesi
Recommended name:
Adenosine deaminase (EC:3.5.4.43 Publications)
Alternative name(s):
Adenosine aminohydrolase
Gene namesi
Name:ADA
Synonyms:ADA1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 20

Organism-specific databases

HGNCiHGNC:186. ADA.

Subcellular locationi

GO - Cellular componenti

  • cell junction Source: UniProtKB-SubCell
  • cell surface Source: UniProtKB
  • cytoplasm Source: HPA
  • cytoplasmic membrane-bounded vesicle lumen Source: UniProtKB-SubCell
  • cytosol Source: GO_Central
  • dendrite cytoplasm Source: Ensembl
  • external side of plasma membrane Source: UniProtKB
  • extracellular space Source: Ensembl
  • lysosome Source: UniProtKB
  • membrane Source: UniProtKB
  • neuronal cell body Source: Ensembl
  • plasma membrane Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

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

Pathology & Biotechi

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.
See also OMIM:102700
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_00221015H → D in ADASCID; loss of activity. 1 PublicationCorresponds to variant rs121908725dbSNPEnsembl.1
Natural variantiVAR_00221120G → R in ADASCID; loss of activity. 1 PublicationCorresponds to variant rs121908724dbSNPEnsembl.1
Natural variantiVAR_00221274G → C in ADASCID; delayed-onset. 1 PublicationCorresponds to variant rs121908730dbSNPEnsembl.1
Natural variantiVAR_00221376R → W in ADASCID. 1 PublicationCorresponds to variant rs121908736dbSNPEnsembl.1
Natural variantiVAR_00221583A → D in ADASCID; loss of activity. 1 PublicationCorresponds to variant rs121908726dbSNPEnsembl.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 rs267606634dbSNPEnsembl.1
Natural variantiVAR_002216101R → L in ADASCID. 1 PublicationCorresponds to variant rs121908720dbSNPEnsembl.1
Natural variantiVAR_002218101R → Q in ADASCID; loss of activity. 1 PublicationCorresponds to variant rs28930970dbSNPEnsembl.1
Natural variantiVAR_002217101R → W in ADASCID. 1 PublicationCorresponds to variant rs28930969dbSNPEnsembl.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 rs267606635dbSNPEnsembl.1
Natural variantiVAR_002219107L → P in ADASCID. 1 PublicationCorresponds to variant rs121908739dbSNPEnsembl.1
Natural variantiVAR_002220129V → M in ADASCID; delayed-onset. 1 PublicationCorresponds to variant rs121908731dbSNPEnsembl.1
Natural variantiVAR_002221140G → E in ADASCID. 1 PublicationCorresponds to variant rs121908732dbSNPEnsembl.1
Natural variantiVAR_002223149R → Q in ADASCID. 1 PublicationCorresponds to variant rs121908737dbSNPEnsembl.1
Natural variantiVAR_002224149R → W in ADASCID. 1 PublicationCorresponds to variant rs121908733dbSNPEnsembl.1
Natural variantiVAR_002226156R → C in ADASCID. 1 PublicationCorresponds to variant rs121908735dbSNPEnsembl.1
Natural variantiVAR_002227156R → H in ADASCID; loss of activity. 1 PublicationCorresponds to variant rs121908722dbSNPEnsembl.1
Natural variantiVAR_002228177V → M in ADASCID; loss of activity. 1 PublicationCorresponds to variant rs121908719dbSNPEnsembl.1
Natural variantiVAR_002229179A → D in ADASCID; loss of activity. 1 PublicationCorresponds to variant rs121908727dbSNPEnsembl.1
Natural variantiVAR_002230199Q → P in ADASCID; delayed-onset. 1 PublicationCorresponds to variant rs121908734dbSNPEnsembl.1
Natural variantiVAR_002231211R → C in ADASCID; late onset; 4% of activity. 2 PublicationsCorresponds to variant rs121908740dbSNPEnsembl.1
Natural variantiVAR_002232211R → H in ADASCID. 1 PublicationCorresponds to variant rs121908716dbSNPEnsembl.1
Natural variantiVAR_002233215A → T in ADASCID; 8% of activity. 2 PublicationsCorresponds to variant rs114025668dbSNPEnsembl.1
Natural variantiVAR_002234216G → R in ADASCID; severe. 1 PublicationCorresponds to variant rs121908723dbSNPEnsembl.1
Natural variantiVAR_002236274P → L in ADASCID. 1 PublicationCorresponds to variant rs121908738dbSNPEnsembl.1
Natural variantiVAR_002237291S → L in ADASCID. 2 PublicationsCorresponds to variant rs121908721dbSNPEnsembl.1
Natural variantiVAR_002238297P → Q in ADASCID. 1 PublicationCorresponds to variant rs121908718dbSNPEnsembl.1
Natural variantiVAR_002239304L → R in ADASCID; loss of activity. Corresponds to variant rs199422327dbSNPEnsembl.1
Natural variantiVAR_002240329A → V in ADASCID. 1 PublicationCorresponds to variant rs121908715dbSNPEnsembl.1
Natural variantiVAR_002241337Missing in ADASCID. 1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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

DisGeNETi100.
MalaCardsiADA.
MIMi102700. phenotype.
OpenTargetsiENSG00000196839.
Orphaneti39041. Omenn syndrome.
277. Severe combined immunodeficiency due to adenosine deaminase deficiency.
PharmGKBiPA24503.

Chemistry databases

ChEMBLiCHEMBL1910.
DrugBankiDB00640. Adenosine.
DB00975. Dipyridamole.
DB00974. Edetic Acid.
DB01280. Nelarabine.
DB00552. Pentostatin.
DB00277. Theophylline.
DB00194. Vidarabine.
GuidetoPHARMACOLOGYi1230.

Polymorphism and mutation databases

BioMutaiADA.
DMDMi113339.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001943522 – 363Adenosine deaminaseAdd BLAST362

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanine1 Publication1
Modified residuei54N6-acetyllysineCombined sources1
Modified residuei232N6-acetyllysineCombined sources1

Keywords - PTMi

Acetylation

Proteomic databases

EPDiP00813.
MaxQBiP00813.
PaxDbiP00813.
PeptideAtlasiP00813.
PRIDEiP00813.
TopDownProteomicsiP00813.

PTM databases

iPTMnetiP00813.
PhosphoSitePlusiP00813.
SwissPalmiP00813.

Expressioni

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

Inductioni

Up-regulated by hypoxia.1 Publication

Gene expression databases

BgeeiENSG00000196839.
CleanExiHS_ADA.
ExpressionAtlasiP00813. baseline and differential.
GenevisibleiP00813. HS.

Organism-specific databases

HPAiCAB004307.
HPA001399.
HPA023884.

Interactioni

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

BioGridi106614. 20 interactors.
DIPiDIP-371N.
IntActiP00813. 4 interactors.
MINTiMINT-5000852.
STRINGi9606.ENSP00000361965.

Chemistry databases

BindingDBiP00813.

Structurei

Secondary structure

1363
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi11 – 13Combined sources3
Helixi18 – 20Combined sources3
Helixi24 – 34Combined sources11
Helixi43 – 50Combined sources8
Helixi58 – 62Combined sources5
Helixi63 – 67Combined sources5
Helixi69 – 72Combined sources4
Helixi76 – 91Combined sources16
Turni92 – 94Combined sources3
Beta strandi95 – 102Combined sources8
Helixi104 – 107Combined sources4
Beta strandi109 – 111Combined sources3
Helixi116 – 118Combined sources3
Helixi126 – 144Combined sources19
Beta strandi147 – 155Combined sources9
Helixi159 – 161Combined sources3
Helixi162 – 171Combined sources10
Turni172 – 176Combined sources5
Beta strandi177 – 184Combined sources8
Helixi191 – 193Combined sources3
Helixi195 – 207Combined sources13
Beta strandi210 – 219Combined sources10
Helixi221 – 229Combined sources9
Beta strandi234 – 238Combined sources5
Helixi240 – 244Combined sources5
Helixi246 – 254Combined sources9
Beta strandi258 – 261Combined sources4
Helixi263 – 268Combined sources6
Beta strandi270 – 272Combined sources3
Helixi279 – 285Combined sources7
Beta strandi290 – 292Combined sources3
Helixi297 – 300Combined sources4
Helixi304 – 315Combined sources12
Helixi319 – 331Combined sources13
Beta strandi333 – 335Combined sources3
Helixi337 – 351Combined sources15
Helixi355 – 362Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1M7Mmodel-A1-363[»]
3IARX-ray1.52A5-363[»]
ProteinModelPortaliP00813.
SMRiP00813.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00813.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni126 – 143Required for binding to DDP41 PublicationAdd BLAST18

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG1097. Eukaryota.
COG1816. LUCA.
GeneTreeiENSGT00730000111151.
HOGENOMiHOG000218816.
HOVERGENiHBG001718.
InParanoidiP00813.
KOiK01488.
OMAiMPAIAGC.
OrthoDBiEOG091G0NL8.
PhylomeDBiP00813.
TreeFamiTF314270.

Family and domain databases

CDDicd01320. ADA. 1 hit.
HAMAPiMF_00540. A_deaminase. 1 hit.
InterProiIPR006650. A/AMP_deam_AS.
IPR001365. A/AMP_deaminase_dom.
IPR028893. A_deaminase.
IPR006330. Ado/ade_deaminase.
IPR032466. Metal_Hydrolase.
[Graphical view]
PfamiPF00962. A_deaminase. 1 hit.
[Graphical view]
SUPFAMiSSF51556. SSF51556. 1 hit.
TIGRFAMsiTIGR01430. aden_deam. 1 hit.
PROSITEiPS00485. A_DEAMINASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

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
Checksum:i786BC5085CA9AFCB
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti340K → R in BAD97117 (Ref. 5) Curated1

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; in allele ADA*2; in about 10% of the population; 20% to 30% decrease in activity; affects duration and intensity of deep sleep; enhances negative effects of sleep loss during sleep deprivation; may have a protective role against male infertility. 4 PublicationsCorresponds to variant rs73598374dbSNPEnsembl.1
Natural variantiVAR_00221015H → D in ADASCID; loss of activity. 1 PublicationCorresponds to variant rs121908725dbSNPEnsembl.1
Natural variantiVAR_00221120G → R in ADASCID; loss of activity. 1 PublicationCorresponds to variant rs121908724dbSNPEnsembl.1
Natural variantiVAR_00221274G → C in ADASCID; delayed-onset. 1 PublicationCorresponds to variant rs121908730dbSNPEnsembl.1
Natural variantiVAR_00221376R → W in ADASCID. 1 PublicationCorresponds to variant rs121908736dbSNPEnsembl.1
Natural variantiVAR_00221480K → R.1 PublicationCorresponds to variant rs11555566dbSNPEnsembl.1
Natural variantiVAR_00221583A → D in ADASCID; loss of activity. 1 PublicationCorresponds to variant rs121908726dbSNPEnsembl.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 rs267606634dbSNPEnsembl.1
Natural variantiVAR_002216101R → L in ADASCID. 1 PublicationCorresponds to variant rs121908720dbSNPEnsembl.1
Natural variantiVAR_002218101R → Q in ADASCID; loss of activity. 1 PublicationCorresponds to variant rs28930970dbSNPEnsembl.1
Natural variantiVAR_002217101R → W in ADASCID. 1 PublicationCorresponds to variant rs28930969dbSNPEnsembl.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 rs267606635dbSNPEnsembl.1
Natural variantiVAR_002219107L → P in ADASCID. 1 PublicationCorresponds to variant rs121908739dbSNPEnsembl.1
Natural variantiVAR_002220129V → M in ADASCID; delayed-onset. 1 PublicationCorresponds to variant rs121908731dbSNPEnsembl.1
Natural variantiVAR_002221140G → E in ADASCID. 1 PublicationCorresponds to variant rs121908732dbSNPEnsembl.1
Natural variantiVAR_002222142R → Q in a pancreatic ductal adenocarcinoma sample; somatic mutation. 2 PublicationsCorresponds to variant rs61732239dbSNPEnsembl.1
Natural variantiVAR_002223149R → Q in ADASCID. 1 PublicationCorresponds to variant rs121908737dbSNPEnsembl.1
Natural variantiVAR_002224149R → W in ADASCID. 1 PublicationCorresponds to variant rs121908733dbSNPEnsembl.1
Natural variantiVAR_002225152L → M in an individual with partial ADA deficiency but no immunodeficiency; 1,5% of activity. 1 PublicationCorresponds to variant rs121908728dbSNPEnsembl.1
Natural variantiVAR_002226156R → C in ADASCID. 1 PublicationCorresponds to variant rs121908735dbSNPEnsembl.1
Natural variantiVAR_002227156R → H in ADASCID; loss of activity. 1 PublicationCorresponds to variant rs121908722dbSNPEnsembl.1
Natural variantiVAR_002228177V → M in ADASCID; loss of activity. 1 PublicationCorresponds to variant rs121908719dbSNPEnsembl.1
Natural variantiVAR_002229179A → D in ADASCID; loss of activity. 1 PublicationCorresponds to variant rs121908727dbSNPEnsembl.1
Natural variantiVAR_002230199Q → P in ADASCID; delayed-onset. 1 PublicationCorresponds to variant rs121908734dbSNPEnsembl.1
Natural variantiVAR_002231211R → C in ADASCID; late onset; 4% of activity. 2 PublicationsCorresponds to variant rs121908740dbSNPEnsembl.1
Natural variantiVAR_002232211R → H in ADASCID. 1 PublicationCorresponds to variant rs121908716dbSNPEnsembl.1
Natural variantiVAR_002233215A → T in ADASCID; 8% of activity. 2 PublicationsCorresponds to variant rs114025668dbSNPEnsembl.1
Natural variantiVAR_002234216G → R in ADASCID; severe. 1 PublicationCorresponds to variant rs121908723dbSNPEnsembl.1
Natural variantiVAR_002235233T → I in an individual with partial ADA deficiency but no immunodeficiency; 20% of activity. 2 PublicationsCorresponds to variant rs121908729dbSNPEnsembl.1
Natural variantiVAR_002236274P → L in ADASCID. 1 PublicationCorresponds to variant rs121908738dbSNPEnsembl.1
Natural variantiVAR_002237291S → L in ADASCID. 2 PublicationsCorresponds to variant rs121908721dbSNPEnsembl.1
Natural variantiVAR_002238297P → Q in ADASCID. 1 PublicationCorresponds to variant rs121908718dbSNPEnsembl.1
Natural variantiVAR_002239304L → R in ADASCID; loss of activity. Corresponds to variant rs199422327dbSNPEnsembl.1
Natural variantiVAR_002240329A → V in ADASCID. 1 PublicationCorresponds to variant rs121908715dbSNPEnsembl.1
Natural variantiVAR_002241337Missing in ADASCID. 1

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, Z97053 Genomic DNA. Translation: CAH73885.1.
Z97053, AL139352 Genomic DNA. Translation: CAB09782.2.
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.
UniGeneiHs.654536.

Genome annotation databases

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

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

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, Z97053 Genomic DNA. Translation: CAH73885.1.
Z97053, AL139352 Genomic DNA. Translation: CAB09782.2.
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.
UniGeneiHs.654536.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1M7Mmodel-A1-363[»]
3IARX-ray1.52A5-363[»]
ProteinModelPortaliP00813.
SMRiP00813.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi106614. 20 interactors.
DIPiDIP-371N.
IntActiP00813. 4 interactors.
MINTiMINT-5000852.
STRINGi9606.ENSP00000361965.

Chemistry databases

BindingDBiP00813.
ChEMBLiCHEMBL1910.
DrugBankiDB00640. Adenosine.
DB00975. Dipyridamole.
DB00974. Edetic Acid.
DB01280. Nelarabine.
DB00552. Pentostatin.
DB00277. Theophylline.
DB00194. Vidarabine.
GuidetoPHARMACOLOGYi1230.

PTM databases

iPTMnetiP00813.
PhosphoSitePlusiP00813.
SwissPalmiP00813.

Polymorphism and mutation databases

BioMutaiADA.
DMDMi113339.

Proteomic databases

EPDiP00813.
MaxQBiP00813.
PaxDbiP00813.
PeptideAtlasiP00813.
PRIDEiP00813.
TopDownProteomicsiP00813.

Protocols and materials databases

DNASUi100.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi100.
DisGeNETi100.
GeneCardsiADA.
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.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1097. Eukaryota.
COG1816. LUCA.
GeneTreeiENSGT00730000111151.
HOGENOMiHOG000218816.
HOVERGENiHBG001718.
InParanoidiP00813.
KOiK01488.
OMAiMPAIAGC.
OrthoDBiEOG091G0NL8.
PhylomeDBiP00813.
TreeFamiTF314270.

Enzyme and pathway databases

BioCyciMetaCyc:HS02191-MONOMER.
ZFISH:HS02191-MONOMER.
BRENDAi3.5.4.4. 2681.
ReactomeiR-HSA-74217. Purine salvage.
SABIO-RKP00813.
SignaLinkiP00813.

Miscellaneous databases

ChiTaRSiADA. human.
EvolutionaryTraceiP00813.
GeneWikiiAdenosine_deaminase.
GenomeRNAii100.
PROiP00813.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000196839.
CleanExiHS_ADA.
ExpressionAtlasiP00813. baseline and differential.
GenevisibleiP00813. HS.

Family and domain databases

CDDicd01320. ADA. 1 hit.
HAMAPiMF_00540. A_deaminase. 1 hit.
InterProiIPR006650. A/AMP_deam_AS.
IPR001365. A/AMP_deaminase_dom.
IPR028893. A_deaminase.
IPR006330. Ado/ade_deaminase.
IPR032466. Metal_Hydrolase.
[Graphical view]
PfamiPF00962. A_deaminase. 1 hit.
[Graphical view]
SUPFAMiSSF51556. SSF51556. 1 hit.
TIGRFAMsiTIGR01430. aden_deam. 1 hit.
PROSITEiPS00485. A_DEAMINASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiADA_HUMAN
AccessioniPrimary (citable) accession number: P00813
Secondary accession number(s): Q53F92, Q6LA59
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: November 30, 2016
This is version 202 of the entry and version 3 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, Direct protein sequencing, Reference proteome

Documents

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