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P00813 (ADA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 174. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Adenosine deaminase

EC=3.5.4.4
Alternative name(s):
Adenosine aminohydrolase
Gene names
Name:ADA
Synonyms:ADA1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length363 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the hydrolytic deamination of adenosine and 2-deoxyadenosine. 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. Its interaction with DPP4 regulates lymphocyte-epithelial cell adhesion. Ref.13

Catalytic activity

Adenosine + H2O = inosine + NH3. HAMAP-Rule MF_00540

Cofactor

Binds 1 zinc ion per subunit. Ref.18

Subunit structure

Interacts with DPP4 (extracellular domain). Ref.10 Ref.11 Ref.12 Ref.14

Subcellular location

Cell membrane; Peripheral membrane protein; Extracellular side. Cell junction. Cytoplasmic vesicle lumen By similarity. Cytoplasm By similarity. Note: Colocalized with DPP4 at the cell junction in lymphocyte-epithelial cell adhesion. Ref.10 Ref.13

Tissue specificity

Found in all tissues, occurs in large amounts in T-lymphocytes and, at the time of weaning, in gastrointestinal tissues.

Polymorphism

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. HAMAP-Rule MF_00540

Involvement in disease

Severe combined immunodeficiency autosomal recessive T-cell-negative/B-cell-negative/NK-cell-negative due to adenosine deaminase deficiency (ADASCID) [MIM:102700]: An 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.19 Ref.21 Ref.22 Ref.23 Ref.24 Ref.25 Ref.26 Ref.27 Ref.29 Ref.31

Sequence similarities

Belongs to the adenosine and AMP deaminases family.

Ontologies

Keywords
   Biological processCell adhesion
Nucleotide metabolism
   Cellular componentCell junction
Cell membrane
Cytoplasm
Cytoplasmic vesicle
Membrane
   Coding sequence diversityPolymorphism
   DiseaseDisease mutation
Hereditary hemolytic anemia
SCID
   LigandMetal-binding
Zinc
   Molecular functionHydrolase
   PTMAcetylation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processPeyer's patch development

Inferred from electronic annotation. Source: Ensembl

T cell activation

Inferred from direct assay PubMed 7594462. Source: UniProtKB

adenosine catabolic process

Inferred from direct assay PubMed 16670267. Source: UniProtKB

aging

Inferred from electronic annotation. Source: Ensembl

cell adhesion

Inferred from electronic annotation. Source: UniProtKB-KW

dATP catabolic process

Inferred from electronic annotation. Source: Ensembl

deoxyadenosine catabolic process

Inferred from electronic annotation. Source: Ensembl

embryonic digestive tract development

Inferred from electronic annotation. Source: Ensembl

germinal center B cell differentiation

Inferred from electronic annotation. Source: Ensembl

histamine secretion

Inferred from electronic annotation. Source: Ensembl

hypoxanthine salvage

Inferred from Biological aspect of Ancestor. Source: RefGenome

inosine biosynthetic process

Inferred from sequence or structural similarity. Source: UniProtKB

liver development

Inferred from electronic annotation. Source: Ensembl

lung alveolus development

Inferred from electronic annotation. Source: Ensembl

negative regulation of adenosine receptor signaling pathway

Inferred from direct assay PubMed 16670267. Source: UniProtKB

negative regulation of circadian sleep/wake cycle, non-REM sleep

Inferred from electronic annotation. Source: Ensembl

negative regulation of inflammatory response

Inferred from electronic annotation. Source: Ensembl

negative regulation of leukocyte migration

Inferred from electronic annotation. Source: Ensembl

negative regulation of mature B cell apoptotic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of mucus secretion

Inferred from electronic annotation. Source: Ensembl

negative regulation of penile erection

Inferred from electronic annotation. Source: Ensembl

negative regulation of thymocyte apoptotic process

Inferred from electronic annotation. Source: Ensembl

placenta development

Inferred from electronic annotation. Source: Ensembl

positive regulation of B cell proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of T cell differentiation in thymus

Inferred from electronic annotation. Source: Ensembl

positive regulation of T cell receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

positive regulation of alpha-beta T cell differentiation

Inferred from electronic annotation. Source: Ensembl

positive regulation of calcium-mediated signaling

Inferred from electronic annotation. Source: Ensembl

positive regulation of germinal center formation

Inferred from electronic annotation. Source: Ensembl

positive regulation of heart rate

Inferred from electronic annotation. Source: Ensembl

positive regulation of smooth muscle contraction

Inferred from electronic annotation. Source: Ensembl

purine nucleotide salvage

Inferred from mutant phenotype PubMed 9361033. Source: UniProtKB

purine ribonucleoside monophosphate biosynthetic process

Inferred from electronic annotation. Source: InterPro

regulation of cell-cell adhesion mediated by integrin

Inferred from direct assay Ref.13. Source: UniProtKB

response to hydrogen peroxide

Inferred from electronic annotation. Source: Ensembl

response to hypoxia

Inferred from direct assay PubMed 16670267. Source: UniProtKB

response to morphine

Inferred from electronic annotation. Source: Ensembl

response to vitamin E

Inferred from electronic annotation. Source: Ensembl

trophectodermal cell differentiation

Inferred from electronic annotation. Source: Ensembl

xanthine biosynthetic process

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcell junction

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytoplasmic membrane-bounded vesicle lumen

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytosol

Traceable author statement. Source: Reactome

dendrite cytoplasm

Inferred from electronic annotation. Source: Ensembl

external side of plasma membrane

Inferred from direct assay PubMed 16670267PubMed 7759315. Source: UniProtKB

extracellular space

Inferred from electronic annotation. Source: Ensembl

lysosome

Inferred from direct assay PubMed 8452534. Source: UniProtKB

neuronal cell body

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionadenosine deaminase activity

Inferred from direct assay PubMed 11999881PubMed 16670267Ref.23PubMed 8452534PubMed 9361033. Source: UniProtKB

purine nucleoside binding

Inferred from electronic annotation. Source: Ensembl

zinc ion binding

Inferred from mutant phenotype Ref.29. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.8
Chain2 – 363362Adenosine deaminase HAMAP-Rule MF_00540
PRO_0000194352

Sites

Active site2171Proton donor Probable
Metal binding151Zinc; catalytic
Metal binding171Zinc; catalytic
Metal binding2141Zinc; catalytic
Metal binding2951Zinc; catalytic
Binding site171Substrate
Binding site191Substrate
Binding site1841Substrate; via amide nitrogen
Binding site2961Substrate
Site2381Important for catalytic activity By similarity

Amino acid modifications

Modified residue21N-acetylalanine Ref.8
Modified residue541N6-acetyllysine Ref.16
Modified residue2321N6-acetyllysine Ref.16

Natural variations

Natural variant81D → N in allele ADA*2; in about 10% of the population; 20% to 30% decrease in activity; affects duration and intensity of deep sleep. Ref.20 Ref.32
Corresponds to variant rs73598374 [ dbSNP | Ensembl ].
VAR_002209
Natural variant151H → D in ADASCID; loss of activity. Ref.29
Corresponds to variant rs121908725 [ dbSNP | Ensembl ].
VAR_002210
Natural variant201G → R in ADASCID; loss of activity. Ref.27
Corresponds to variant rs121908724 [ dbSNP | Ensembl ].
VAR_002211
Natural variant741G → C in ADASCID; delayed-onset. Ref.31
Corresponds to variant rs121908730 [ dbSNP | Ensembl ].
VAR_002212
Natural variant761R → W in ADASCID. Ref.19
Corresponds to variant rs121908736 [ dbSNP | Ensembl ].
VAR_002213
Natural variant801K → R. Ref.28
Corresponds to variant rs11555566 [ dbSNP | Ensembl ].
VAR_002214
Natural variant831A → D in ADASCID; loss of activity. Ref.29
Corresponds to variant rs121908726 [ dbSNP | Ensembl ].
VAR_002215
Natural variant1011R → L in ADASCID. Ref.26
Corresponds to variant rs121908720 [ dbSNP | Ensembl ].
VAR_002216
Natural variant1011R → Q in ADASCID; loss of activity. Ref.22
Corresponds to variant rs28930970 [ dbSNP | Ensembl ].
VAR_002218
Natural variant1011R → W in ADASCID. Ref.23
Corresponds to variant rs28930969 [ dbSNP | Ensembl ].
VAR_002217
Natural variant1071L → P in ADASCID. Ref.19
Corresponds to variant rs121908739 [ dbSNP | Ensembl ].
VAR_002219
Natural variant1291V → M in ADASCID; delayed-onset. Ref.31
Corresponds to variant rs121908731 [ dbSNP | Ensembl ].
VAR_002220
Natural variant1401G → E in ADASCID. Ref.31
Corresponds to variant rs121908732 [ dbSNP | Ensembl ].
VAR_002221
Natural variant1421R → Q in a pancreatic ductal adenocarcinoma sample; somatic mutation. Ref.28 Ref.33
Corresponds to variant rs61732239 [ dbSNP | Ensembl ].
VAR_002222
Natural variant1491R → Q in ADASCID. Ref.19
Corresponds to variant rs121908737 [ dbSNP | Ensembl ].
VAR_002223
Natural variant1491R → W in ADASCID. Ref.31
Corresponds to variant rs121908733 [ dbSNP | Ensembl ].
VAR_002224
Natural variant1521L → M in an individual with partial ADA deficiency but no immunodeficiency; 1,5% of activity. Ref.30
Corresponds to variant rs121908728 [ dbSNP | Ensembl ].
VAR_002225
Natural variant1561R → C in ADASCID. Ref.25
Corresponds to variant rs121908735 [ dbSNP | Ensembl ].
VAR_002226
Natural variant1561R → H in ADASCID. Ref.26
Corresponds to variant rs121908722 [ dbSNP | Ensembl ].
VAR_002227
Natural variant1771V → M in ADASCID; loss of activity. Ref.26
Corresponds to variant rs121908719 [ dbSNP | Ensembl ].
VAR_002228
Natural variant1791A → D in ADASCID; loss of activity. Ref.29
Corresponds to variant rs121908727 [ dbSNP | Ensembl ].
VAR_002229
Natural variant1991Q → P in ADASCID; delayed-onset. Ref.31
Corresponds to variant rs121908734 [ dbSNP | Ensembl ].
VAR_002230
Natural variant2111R → C in ADASCID; late onset. Ref.19
Corresponds to variant rs121908740 [ dbSNP | Ensembl ].
VAR_002231
Natural variant2111R → H in ADASCID. Ref.23
Corresponds to variant rs121908716 [ dbSNP | Ensembl ].
VAR_002232
Natural variant2151A → T in ADASCID. Ref.19
Corresponds to variant rs114025668 [ dbSNP | Ensembl ].
VAR_002233
Natural variant2161G → R in ADASCID; severe. Ref.26
Corresponds to variant rs121908723 [ dbSNP | Ensembl ].
VAR_002234
Natural variant2331T → I in an individual with partial ADA deficiency but no immunodeficiency; 20% of activity. Ref.30
Corresponds to variant rs121908729 [ dbSNP | Ensembl ].
VAR_002235
Natural variant2741P → L in ADASCID. Ref.19
Corresponds to variant rs121908738 [ dbSNP | Ensembl ].
VAR_002236
Natural variant2911S → L in ADASCID. Ref.25 Ref.26
Corresponds to variant rs121908721 [ dbSNP | Ensembl ].
VAR_002237
Natural variant2971P → Q in ADASCID. Ref.24
Corresponds to variant rs121908718 [ dbSNP | Ensembl ].
VAR_002238
Natural variant3041L → R in ADASCID; loss of activity.
VAR_002239
Natural variant3291A → V in ADASCID. Ref.23
Corresponds to variant rs121908715 [ dbSNP | Ensembl ].
VAR_002240
Natural variant3371Missing in ADASCID.
VAR_002241

Experimental info

Sequence conflict3401K → R in BAD97117. Ref.5

Secondary structure

..................................................................... 363
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P00813 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 786BC5085CA9AFCB

FASTA36340,764
        10         20         30         40         50         60 
MAQTPAFDKP KVELHVHLDG SIKPETILYY GRRRGIALPA NTAEGLLNVI GMDKPLTLPD 

        70         80         90        100        110        120 
FLAKFDYYMP AIAGCREAIK RIAYEFVEMK AKEGVVYVEV RYSPHLLANS KVEPIPWNQA 

       130        140        150        160        170        180 
EGDLTPDEVV ALVGQGLQEG ERDFGVKARS ILCCMRHQPN WSPKVVELCK KYQQQTVVAI 

       190        200        210        220        230        240 
DLAGDETIPG SSLLPGHVQA YQEAVKSGIH RTVHAGEVGS AEVVKEAVDI LKTERLGHGY 

       250        260        270        280        290        300 
HTLEDQALYN RLRQENMHFE ICPWSSYLTG AWKPDTEHAV IRLKNDQANY SLNTDDPLIF 

       310        320        330        340        350        360 
KSTLDTDYQM TKRDMGFTEE EFKRLNINAA KSSFLPEDEK RELLDLLYKA YGMPPSASAG 


QNL 

« Hide

References

« Hide 'large scale' references
[1]"Human adenosine deaminase. cDNA and complete primary amino acid sequence."
Daddona P.E., Shewach D.S., Kelley W.N., Argos P., Markham A.F., Orkin S.H.
J. Biol. Chem. 259:12101-12106(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Sequence of human adenosine deaminase cDNA including the coding region and a small intron."
Wiginton D.A., Adrian G.S., Hutton J.J.
Nucleic Acids Res. 12:2439-2446(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Adenosine deaminase: characterization and expression of a gene with a remarkable promoter."
Valerio D., Duyvesteyn M.G.C., Dekker B.M.M., Weeda G., Berkvens T.M., van der Voorn L., van Ormondt H., van der Eb A.J.
EMBO J. 4:437-443(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"Complete sequence and structure of the gene for human adenosine deaminase."
Wiginton D.A., Kaplan D.J., States J.C., Akeson A.L., Perme C.M., Bilyk I.J., Vaughn A.J., Lattier D.L., Hutton J.J.
Biochemistry 25:8234-8244(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Thymus.
[6]"The DNA sequence and comparative analysis of human chromosome 20."
Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E. expand/collapse author list , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain and Placenta.
[8]Bienvenut W.V.
Submitted (AUG-2004) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-11, ACETYLATION AT ALA-2, MASS SPECTROMETRY.
Tissue: B-cell lymphoma.
[9]"Molecular cloning of human adenosine deaminase gene sequences."
Orkin S.H., Daddona P.E., Shewach D.S., Markham A.F., Bruns G.A., Goff S.C., Kelley W.N.
J. Biol. Chem. 258:12753-12756(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 141-363.
[10]"Direct association of adenosine deaminase with a T cell activation antigen, CD26."
Kameoka J., Tanaka T., Nojima Y., Schlossman S.F., Morimoto C.
Science 261:466-469(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DPP4, SUBCELLULAR LOCATION.
[11]"Binding of adenosine deaminase to the lymphocyte surface via CD26."
De Meester I., Vanham G., Kestens L., Vanhoof G., Bosmans E., Gigase P., Scharpe S.
Eur. J. Immunol. 24:566-570(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DPP4.
[12]"Molecular characterization of dipeptidyl peptidase activity in serum: soluble CD26/dipeptidyl peptidase IV is responsible for the release of X-Pro dipeptides."
Durinx C., Lambeir A.M., Bosmans E., Falmagne J.B., Berghmans R., Haemers A., Scharpe S., De Meester I.
Eur. J. Biochem. 267:5608-5613(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DPP4.
[13]"Regulation of epithelial and lymphocyte cell adhesion by adenosine deaminase-CD26 interaction."
Gines S., Marino M., Mallol J., Canela E.I., Morimoto C., Callebaut C., Hovanessian A., Casado V., Lluis C., Franco R.
Biochem. J. 361:203-209(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[14]"N-linked glycosylation of dipeptidyl peptidase IV (CD26): effects on enzyme activity, homodimer formation, and adenosine deaminase binding."
Aertgeerts K., Ye S., Shi L., Prasad S.G., Witmer D., Chi E., Sang B.C., Wijnands R.A., Webb D.R., Swanson R.V.
Protein Sci. 13:145-154(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH APP4.
[15]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[16]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-54 AND LYS-232, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]"The crystal structure of human adenosine deaminase."
Structural genomics consortium (SGC)
Submitted (AUG-2009) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (1.52 ANGSTROMS) OF 5-363 IN COMPLEX WITH NICKEL IONS AND 2-DEAOXYADENOSINE, COFACTOR.
[19]"Hot spot mutations in adenosine deaminase deficiency."
Hirschhorn R., Tzall S., Ellenbogen A.
Proc. Natl. Acad. Sci. U.S.A. 87:6171-6175(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ADASCID TRP-76; PRO-107; GLN-149; CYS-211; THR-215 AND LEU-274.
[20]"An Asp8Asn substitution results in the adenosine deaminase (ADA) genetic polymorphism (ADA 2 allozyme): occurrence on different chromosomal backgrounds and apparent intragenic crossover."
Hirschhorn R., Yang D.R., Israni A.
Ann. Hum. Genet. 58:1-9(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ADA*2 ASN-8.
[21]"Structure of adenosine deaminase mRNAs from normal and adenosine deaminase-deficient human cell lines."
Adrian G.S., Wiginton D.A., Hutton J.
Mol. Cell. Biol. 4:1712-1717(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ADASCID.
[22]"Identification of a point mutation in the adenosine deaminase gene responsible for immunodeficiency."
Bonthron D.T., Markham A.F., Ginsburg D., Orkin S.H.
J. Clin. Invest. 76:894-897(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ADASCID GLN-101.
[23]"Mutant human adenosine deaminase alleles and their expression by transfection into fibroblasts."
Akeson A.L., Wiginton D.A., Dusing M.R., States J.C., Hutton J.J.
J. Biol. Chem. 263:16291-16296(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ADASCID TRP-101; HIS-211 AND VAL-329.
[24]"Identification of a point mutation resulting in a heat-labile adenosine deaminase (ADA) in two unrelated children with partial ADA deficiency."
Hirschhorn R., Tzall S., Ellenbogen A., Orkin S.H.
J. Clin. Invest. 83:497-501(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ADASCID GLN-297.
[25]"Identification of two new missense mutations (R156C and S291L) in two ADA-SCID patients unusual for response to therapy with partial exchange transfusions."
Hirschhorn R.
Hum. Mutat. 1:166-168(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ADASCID CYS-156 AND LEU-291.
[26]"Novel splicing, missense, and deletion mutations in seven adenosine deaminase-deficient patients with late/delayed onset of combined immunodeficiency disease. Contribution of genotype to phenotype."
Santisteban I., Arredondo-Vega F.X., Kelly S., Mary A., Fischer A., Hummell D.S., Lawton A., Sorensen R.U., Stiehm E.R., Uribe L., Weinberg K., Hershfield M.S.
J. Clin. Invest. 92:2291-2302(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ADASCID LEU-101; HIS-156; MET-177; ARG-216 AND LEU-291.
[27]"Homozygosity for a missense mutation (G20R) associated with neonatal onset adenosine deaminase-deficient severe combined immunodeficiency (ADA-SCID)."
Yang D.R., Huie M.L., Hirschhorn R.
Clin. Immunol. Immunopathol. 70:171-175(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ADASCID ARG-20.
[28]"Three new adenosine deaminase mutations that define a splicing enhancer and cause severe and partial phenotypes: implications for evolution of a CpG hotspot and expression of a transduced ADA cDNA."
Santisteban I., Arredondo-Vega F.X., Kelly S., Loubser M., Meydan N., Roifman C., Howell P.L., Bowen T., Weinberg K.I., Schroeder M.L., Hershfield M.S.
Hum. Mol. Genet. 4:2081-2087(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ARG-80 AND GLN-142.
[29]"Four new adenosine deaminase mutations, altering a zinc-binding histidine, two conserved alanines, and a 5' splice site."
Santisteban I., Arredondo-Vega F.X., Kelly S., Debre M., Fisher A., Perignon J.L., Hilman B., Eldahr J., Dreyfus D.H., Gelfand E.W., Howell P.L., Hershfield M.S.
Hum. Mutat. 5:243-250(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ADASCID ASP-15; ASP-83 AND ASP-179.
[30]"Two newly identified mutations (Thr233Ile and Leu152Met) in partially adenosine deaminase-deficient (ADA-) individuals that result in differing biochemical and metabolic phenotypes."
Hirschhorn R., Borkowsky W., Jiang C.-K., Yang D.R., Jenkins T.
Hum. Genet. 100:22-29(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS MET-152 AND ILE-233.
[31]"Seven novel mutations in the adenosine deaminase (ADA) gene in patients with severe and delayed onset combined immunodeficiency: G74C, V129M, G140E, R149W, Q199P, 462delG, and E337del."
Arrendondo-Vega F.X., Santisteban I., Notarangelo L.D., El Dahr J., Buckley R., Roifman C., Conley M.E., Hershfield M.S.
Hum. Mutat. 11:482-482(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ADASCID CYS-74; MET-129; GLU-140; TRP-149 AND PRO-199.
[32]"A functional genetic variation of adenosine deaminase affects the duration and intensity of deep sleep in humans."
Retey J.V., Adam M., Honegger E., Khatami R., Luhmann U.F.O., Jung H.H., Berger W., Landolt H.-P.
Proc. Natl. Acad. Sci. U.S.A. 102:15676-15681(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: EFFECT OF VARIANT ADA*2 ASN-8 ON SLEEP.
[33]"Core signaling pathways in human pancreatic cancers revealed by global genomic analyses."
Jones S., Zhang X., Parsons D.W., Lin J.C., Leary R.J., Angenendt P., Mankoo P., Carter H., Kamiyama H., Jimeno A., Hong S.M., Fu B., Lin M.T., Calhoun E.S., Kamiyama M., Walter K., Nikolskaya T., Nikolsky Y. expand/collapse author list , Hartigan J., Smith D.R., Hidalgo M., Leach S.D., Klein A.P., Jaffee E.M., Goggins M., Maitra A., Iacobuzio-Donahue C., Eshleman J.R., Kern S.E., Hruban R.H., Karchin R., Papadopoulos N., Parmigiani G., Vogelstein B., Velculescu V.E., Kinzler K.W.
Science 321:1801-1806(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] GLN-142.
+Additional computationally mapped references.

Web resources

ADAbase

ADA mutation db

GeneReviews
Wikipedia

Adenosine deaminase entry

Mendelian genes adenosine deaminase (ADA)

Leiden Open Variation Database (LOVD)

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X02994 mRNA. Translation: CAA26734.1.
X02189 expand/collapse EMBL AC list , 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.
PIRDUHUA. A91032.
RefSeqNP_000013.2. NM_000022.2.
UniGeneHs.654536.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1M7Mmodel-A1-363[»]
3IARX-ray1.52A5-363[»]
ProteinModelPortalP00813.
SMRP00813. Positions 5-363.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106614. 9 interactions.
DIPDIP-371N.
IntActP00813. 2 interactions.
MINTMINT-5000852.
STRING9606.ENSP00000361965.

Chemistry

BindingDBP00813.
ChEMBLCHEMBL1910.
DrugBankDB00640. Adenosine.
DB00242. Cladribine.
DB00975. Dipyridamole.
DB00199. Erythromycin.
DB01073. Fludarabine.
DB00249. Idoxuridine.
DB01280. Nelarabine.
DB00552. Pentostatin.
DB00277. Theophylline.
DB00194. Vidarabine.
GuidetoPHARMACOLOGY1230.

PTM databases

PhosphoSiteP00813.

Polymorphism databases

DMDM113339.

Proteomic databases

PaxDbP00813.
PeptideAtlasP00813.
PRIDEP00813.

Protocols and materials databases

DNASU100.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000372874; ENSP00000361965; ENSG00000196839.
GeneID100.
KEGGhsa:100.
UCSCuc002xmj.3. human.

Organism-specific databases

CTD100.
GeneCardsGC20M043248.
HGNCHGNC:186. ADA.
HPACAB004307.
HPA001399.
HPA023884.
MIM102700. phenotype.
608958. gene.
neXtProtNX_P00813.
Orphanet39041. Omenn syndrome.
277. Severe combined immunodeficiency due to adenosine deaminase deficiency.
PharmGKBPA24503.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1816.
HOGENOMHOG000218816.
HOVERGENHBG001718.
InParanoidP00813.
KOK01488.
OMALYKAYGM.
OrthoDBEOG7GN2MZ.
PhylomeDBP00813.
TreeFamTF314270.

Enzyme and pathway databases

BioCycMetaCyc:HS02191-MONOMER.
ReactomeREACT_111217. Metabolism.
SABIO-RKP00813.
SignaLinkP00813.

Gene expression databases

ArrayExpressP00813.
BgeeP00813.
CleanExHS_ADA.
GenevestigatorP00813.

Family and domain databases

HAMAPMF_00540. A_deaminase.
InterProIPR006650. A/AMP_deam_AS.
IPR001365. A/AMP_deaminase_dom.
IPR028893. A_deaminase.
IPR006330. Ado/ade_deaminase.
[Graphical view]
PfamPF00962. A_deaminase. 1 hit.
[Graphical view]
TIGRFAMsTIGR01430. aden_deam. 1 hit.
PROSITEPS00485. A_DEAMINASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP00813.
GeneWikiAdenosine_deaminase.
GenomeRNAi100.
NextBio377.
PROP00813.
SOURCESearch...

Entry information

Entry nameADA_HUMAN
AccessionPrimary (citable) accession number: P00813
Secondary accession number(s): Q53F92, Q6LA59
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: March 19, 2014
This is version 174 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 20

Human chromosome 20: entries, gene names and cross-references to MIM