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P03958 (ADA_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 150. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·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
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length352 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 By similarity. HAMAP-Rule MF_00540

Catalytic activity

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

Cofactor

Binds 1 zinc ion per subunit. Ref.9 Ref.12 Ref.15

Subunit structure

Interacts with DPP4 (extracellular domain) By similarity.

Subcellular location

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

Tissue specificity

Detected in brain neurons in the median emninence (at protein level). Found in all tissues, occurs in large amounts in T-lymphocytes and, at the time of weaning, in gastrointestinal tissues. Ref.10

Disruption phenotype

Lethal at perinatal stages. Fetuses are viable up to 18 dpc, but after this survival decreases rapidly. Fewer that 10% of mutant pups are born live, and these die within hours after birth. Mutant fetuses display much higher than normal levels of adenosine and dATP, respiratory distress, hepatocellular degeneration and necrosis. Prenatal lethality can be avoided using an ADA expression vector with a trophoblast-specific promoter. Mutant mice die after about three weeks due to immunodeficiency, disturbances in purine metabolism and severe lung inflammation. Ref.7 Ref.8 Ref.11

Sequence similarities

Belongs to the adenosine and AMP deaminases family.

Biophysicochemical properties

Kinetic parameters:

KM=20 µM for adenosine Ref.9 Ref.13

pH dependence:

Optimum pH is 6-8.5.

Ontologies

Keywords
   Biological processCell adhesion
Nucleotide metabolism
   Cellular componentCell junction
Cell membrane
Cytoplasm
Cytoplasmic vesicle
Membrane
   LigandMetal-binding
Zinc
   Molecular functionHydrolase
   PTMAcetylation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processPeyer's patch development

Inferred from mutant phenotype PubMed 10720488. Source: MGI

T cell activation

Inferred from electronic annotation. Source: Ensembl

adenosine catabolic process

Inferred from direct assay Ref.13. Source: UniProtKB

aging

Inferred from electronic annotation. Source: Ensembl

cell adhesion

Inferred from electronic annotation. Source: UniProtKB-KW

dATP catabolic process

Inferred from direct assay PubMed 7592575. Source: MGI

deoxyadenosine catabolic process

Inferred from direct assay PubMed 7592575. Source: MGI

embryonic digestive tract development

Inferred from mutant phenotype Ref.7. Source: MGI

germinal center B cell differentiation

Inferred from mutant phenotype PubMed 14607964. Source: MGI

histamine secretion

Inferred from electronic annotation. Source: Ensembl

hypoxanthine biosynthetic process

Inferred from mutant phenotype PubMed 10720488. Source: MGI

hypoxanthine salvage

Inferred from Biological aspect of Ancestor. Source: RefGenome

in utero embryonic development

Inferred from mutant phenotype Ref.8PubMed 9272950. Source: MGI

inosine biosynthetic process

Inferred from direct assay Ref.13. Source: UniProtKB

liver development

Inferred from mutant phenotype Ref.7Ref.8. Source: MGI

lung alveolus development

Inferred from mutant phenotype Ref.11. Source: MGI

lung development

Inferred from mutant phenotype Ref.7. Source: MGI

negative regulation of adenosine receptor signaling pathway

Inferred from Biological aspect of Ancestor. Source: RefGenome

negative regulation of apoptotic process

Inferred from mutant phenotype Ref.7PubMed 8171392. Source: MGI

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

Inferred from electronic annotation. Source: Ensembl

negative regulation of inflammatory response

Inferred from mutant phenotype Ref.11PubMed 11591798PubMed 15240734PubMed 15630442PubMed 17601796. Source: MGI

negative regulation of leukocyte migration

Inferred from mutant phenotype PubMed 15240734PubMed 15630442. Source: MGI

negative regulation of mature B cell apoptotic process

Inferred from mutant phenotype PubMed 14607964. Source: MGI

negative regulation of mucus secretion

Inferred from mutant phenotype PubMed 15240734PubMed 15630442. Source: MGI

negative regulation of penile erection

Inferred from mutant phenotype PubMed 18340377. Source: MGI

negative regulation of thymocyte apoptotic process

Inferred from mutant phenotype PubMed 11067867PubMed 16670300. Source: MGI

placenta development

Inferred from mutant phenotype PubMed 9272950. Source: MGI

positive regulation of B cell proliferation

Inferred from mutant phenotype PubMed 14607964. Source: MGI

positive regulation of T cell activation

Inferred from mutant phenotype PubMed 10845921PubMed 11435465. Source: MGI

positive regulation of T cell differentiation

Inferred from mutant phenotype Ref.8PubMed 9478961. Source: MGI

positive regulation of T cell differentiation in thymus

Inferred from mutant phenotype PubMed 11067867PubMed 11435465PubMed 12163459PubMed 16670300. Source: MGI

positive regulation of T cell receptor signaling pathway

Inferred from mutant phenotype PubMed 11435465. Source: MGI

positive regulation of alpha-beta T cell differentiation

Inferred from mutant phenotype PubMed 11067867PubMed 12163459PubMed 16670300. Source: MGI

positive regulation of calcium-mediated signaling

Inferred from mutant phenotype PubMed 11435465. Source: MGI

positive regulation of germinal center formation

Inferred from mutant phenotype PubMed 14607964. Source: MGI

positive regulation of heart rate

Inferred from mutant phenotype PubMed 16626672. Source: MGI

positive regulation of smooth muscle contraction

Inferred from mutant phenotype PubMed 18340377. Source: MGI

purine nucleotide salvage

Inferred from electronic annotation. Source: Ensembl

purine ribonucleoside monophosphate biosynthetic process

Inferred from electronic annotation. Source: InterPro

regulation of T cell differentiation

Inferred from mutant phenotype Ref.7. Source: MGI

regulation of cell-cell adhesion mediated by integrin

Inferred from electronic annotation. Source: Ensembl

response to drug

Inferred from electronic annotation. Source: Ensembl

response to hydrogen peroxide

Inferred from electronic annotation. Source: Ensembl

response to hypoxia

Inferred from electronic annotation. Source: Ensembl

response to morphine

Inferred from electronic annotation. Source: Ensembl

response to vitamin E

Inferred from electronic annotation. Source: Ensembl

trophectodermal cell differentiation

Inferred from mutant phenotype PubMed 9272950. Source: MGI

xanthine biosynthetic process

Inferred from mutant phenotype PubMed 10720488. Source: MGI

   Cellular_componentcell junction

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytoplasm

Inferred from direct assay PubMed 11940672PubMed 7691243. Source: MGI

cytoplasmic membrane-bounded vesicle lumen

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytosol

Inferred from Biological aspect of Ancestor. Source: RefGenome

dendrite cytoplasm

Inferred from electronic annotation. Source: Ensembl

external side of plasma membrane

Inferred from Biological aspect of Ancestor. Source: RefGenome

extracellular space

Inferred from electronic annotation. Source: Ensembl

lysosome

Inferred from electronic annotation. Source: Ensembl

neuronal cell body

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionadenosine deaminase activity

Inferred from direct assay Ref.13. Source: UniProtKB

purine nucleoside binding

Inferred from electronic annotation. Source: Ensembl

zinc ion binding

Inferred from direct assay Ref.13. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 352351Adenosine deaminase HAMAP-Rule MF_00540
PRO_0000194353

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 and carbonyl oxygen
Binding site2961Substrate
Site2381Important for catalytic activity

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue541N6-acetyllysine By similarity
Modified residue2321N6-acetyllysine By similarity

Experimental info

Mutagenesis2171E → D: Reduces catalytic activity 700-fold. No effect on affinity for adenosine. Ref.9
Mutagenesis2171E → G: Reduces catalytic activity 3200-fold. No effect on affinity for adenosine. Ref.9
Mutagenesis2171E → Q: Reduces catalytic activity 4800-fold, and slighly increases affinity for substrate. Ref.9
Mutagenesis2171E → S: Loss of activity. Ref.9
Mutagenesis2381H → A: Increases affinity for adenosine 20-fold. Reduces enzyme activity 500-fold. Ref.14
Mutagenesis2381H → E: Nearly abolishes enzyme activity. Ref.14
Mutagenesis2381H → R: Reduces enzyme activity 1500-fold. No effect on affinity for adenosine. Ref.14
Mutagenesis2951D → E: No effect on affinity for adenosine. Reduces enzyme activity 2750-fold. Ref.13
Mutagenesis2961D → A: Reduces affinity for adenosine 70-fold. Reduces enzyme activity 110000-fold. Ref.13
Mutagenesis2961D → N: Reduces affinity for adenosine 10-fold. Reduces enzyme activity 100-fold. Ref.13
Sequence conflict1411E → R in AAB07142. Ref.2

Secondary structure

.................................................................. 352
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P03958 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: E53A8A1FABA148CD

FASTA35239,992
        10         20         30         40         50         60 
MAQTPAFNKP KVELHVHLDG AIKPETILYF GKKRGIALPA DTVEELRNII GMDKPLSLPG 

        70         80         90        100        110        120 
FLAKFDYYMP VIAGCREAIK RIAYEFVEMK AKEGVVYVEV RYSPHLLANS KVDPMPWNQT 

       130        140        150        160        170        180 
EGDVTPDDVV DLVNQGLQEG EQAFGIKVRS ILCCMRHQPS WSLEVLELCK KYNQKTVVAM 

       190        200        210        220        230        240 
DLAGDETIEG SSLFPGHVEA YEGAVKNGIH RTVHAGEVGS PEVVREAVDI LKTERVGHGY 

       250        260        270        280        290        300 
HTIEDEALYN RLLKENMHFE VCPWSSYLTG AWDPKTTHAV VRFKNDKANY SLNTDDPLIF 

       310        320        330        340        350 
KSTLDTDYQM TKKDMGFTEE EFKRLNINAA KSSFLPEEEK KELLERLYRE YQ 

« Hide

References

« Hide 'large scale' references
[1]"Identification of functional murine adenosine deaminase cDNA clones by complementation in Escherichia coli."
Yeung C.-Y., Ingolia D.E., Roth D.B., Shoemaker C., Al-Ubaidi M.R., Yen J.-Y., Ching C., Bobonis C., Kaufman R.J., Kellems R.E.
J. Biol. Chem. 260:10299-10307(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Structural and functional analysis of the murine adenosine deaminase gene."
Al-Ubaidi M.R., Ramamurthy V., Maa M.C., Ingolia D.E., Chinsky J.M., Martin B.D., Kellems R.E.
Genomics 7:476-485(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"The comparative sequence analysis of murine and human ADA genes."
Xu P., Winston J.W., Lu J., Muzny D.M., Gibbs R.A., Kellems R.E.
Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"High-throughput sequence identification of gene coding variants within alcohol-related QTLs."
Ehringer M.A., Thompson J., Conroy O., Xu Y., Yang F., Canniff J., Beeson M., Gordon L., Bennett B., Johnson T.E., Sikela J.M.
Mamm. Genome 12:657-663(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: ILS and ISS.
[5]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Tongue.
[6]"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: Mammary tumor.
[7]"Adenosine-deaminase-deficient mice die perinatally and exhibit liver-cell degeneration, atelectasis and small intestinal cell death."
Migchielsen A.A., Breuer M.L., van Roon M.A., te Riele H., Zurcher C., Ossendorp F., Toutain S., Hershfield M.S., Berns A., Valerio D.
Nat. Genet. 10:279-287(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE.
[8]"Disruption of the adenosine deaminase gene causes hepatocellular impairment and perinatal lethality in mice."
Wakamiya M., Blackburn M.R., Jurecic R., McArthur M.J., Geske R.S., Cartwright J. Jr., Mitani K., Vaishnav S., Belmont J.W., Kellems R.E., Finegold M.J., Montgomery C.A. Jr., Bradley A., Caskey C.T.
Proc. Natl. Acad. Sci. U.S.A. 92:3673-3677(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE.
[9]"Site-directed mutagenesis of active site glutamate-217 in mouse adenosine deaminase."
Mohamedali K.A., Kurz L.C., Rudolph F.B.
Biochemistry 35:1672-1680(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF GLU-217, CIRCULAR DICHROISM, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, ACTIVE SITE, PROPOSED ENZYME MECHANISM.
[10]"Adenosine deaminase in rodent median eminence: detection by antibody to the mouse enzyme and co-localization with adenosine deaminase-complexing protein (CD26)."
Nagy J.I., Yamamoto T., Uemura H., Schrader W.P.
Neuroscience 73:459-471(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[11]"Metabolic consequences of adenosine deaminase deficiency in mice are associated with defects in alveogenesis, pulmonary inflammation, and airway obstruction."
Blackburn M.R., Volmer J.B., Thrasher J.L., Zhong H., Crosby J.R., Lee J.J., Kellems R.E.
J. Exp. Med. 192:159-170(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE.
[12]"Atomic structure of adenosine deaminase complexed with a transition-state analog: understanding catalysis and immunodeficiency mutations."
Wilson D.K., Rudolph F.B., Quiocho F.A.
Science 252:1278-1284(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH ZINC IONS AND TRANSITION STATE ANALOG 6-HYDROXYL-1,6-DIHYDROPURINE RIBONUCLEOTIDE, COFACTOR, PROPOSED ENZYME MECHANISM.
[13]"Probing the functional role of two conserved active site aspartates in mouse adenosine deaminase."
Sideraki V., Mohamedali K.A., Wilson D.K., Chang Z., Kellems R.E., Quiocho F.A., Rudolph F.B.
Biochemistry 35:7862-7872(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 4-352 OF MUTANTS GLU-295 AND ALA-296 IN COMPLEXES WITH ZINC IONS; 6-HYDROXYL-1,6-DIHYDROPURINE RIBONUCLEOTIDE AND PURINE RIBOSIDE, CIRCULAR DICHROISM, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ASP-295 AND ASP-296.
[14]"Site-directed mutagenesis of histidine 238 in mouse adenosine deaminase: substitution of histidine 238 does not impede hydroxylate formation."
Sideraki V., Wilson D.K., Kurz L.C., Quiocho F.A., Rudolph F.B.
Biochemistry 35:15019-15028(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF MUTANTS ALA-238 AND GLU-238 IN COMPLEXES WITH ZINC IONS; 6-HYDROXYL-1,6-DIHYDROPURINE RIBONUCLEOTIDE AND PURINE RIBOSIDE, MUTAGENESIS OF HIS-238.
[15]"Complexes of adenosine deaminase with two potent inhibitors: X-ray structures in four independent molecules at pH of maximum activity."
Wang Z., Quiocho F.A.
Biochemistry 37:8314-8324(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH ZINC IONS AND INHIBITOR, COFACTOR, ACTIVE SITE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M10319 mRNA. Translation: AAA37173.1.
M34251 expand/collapse EMBL AC list , M34242, M34243, M34244, M34246, M34247, M34248, M34249, M34250 Genomic DNA. Translation: AAB07142.1.
U73107 Genomic DNA. Translation: AAC08442.1.
AF483480 mRNA. Translation: AAL90754.1.
AF483481 mRNA. Translation: AAL90755.1.
AK075899 mRNA. Translation: BAC36039.1.
BC002075 mRNA. Translation: AAH02075.1.
CCDSCCDS17015.1.
PIRDUMSA. A01010.
RefSeqNP_001258981.1. NM_001272052.1.
NP_031424.1. NM_007398.4.
UniGeneMm.388.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1A4LX-ray2.60A/B/C/D4-352[»]
1A4MX-ray1.95A/B/C/D4-352[»]
1ADDX-ray2.40A4-352[»]
1FKWX-ray2.40A4-352[»]
1FKXX-ray2.40A4-352[»]
1UIOX-ray2.40A4-352[»]
1UIPX-ray2.40A4-352[»]
2ADAX-ray2.40A1-352[»]
3KM8X-ray2.00A/B1-352[»]
3MVIX-ray1.60A/B4-352[»]
3MVTX-ray2.20A/C4-352[»]
3T1GX-ray2.35A4-352[»]
ProteinModelPortalP03958.
SMRP03958. Positions 4-352.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP03958. 1 interaction.
MINTMINT-4087128.

Chemistry

BindingDBP03958.
ChEMBLCHEMBL3206.

PTM databases

PhosphoSiteP03958.

2D gel databases

REPRODUCTION-2DPAGEP03958.

Proteomic databases

MaxQBP03958.
PaxDbP03958.
PRIDEP03958.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000017841; ENSMUSP00000017841; ENSMUSG00000017697.
GeneID11486.
KEGGmmu:11486.
UCSCuc008ntl.1. mouse.

Organism-specific databases

CTD100.
MGIMGI:87916. Ada.

Phylogenomic databases

eggNOGCOG1816.
HOGENOMHOG000218816.
HOVERGENHBG001718.
InParanoidP03958.
KOK01488.
OMADWMVAVL.
OrthoDBEOG7GN2MZ.
PhylomeDBP03958.
TreeFamTF314270.

Gene expression databases

ArrayExpressP03958.
BgeeP03958.
CleanExMM_ADA.
GenevestigatorP03958.

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

ChiTaRSADA. mouse.
EvolutionaryTraceP03958.
NextBio278844.
PROP03958.
SOURCESearch...

Entry information

Entry nameADA_MOUSE
AccessionPrimary (citable) accession number: P03958
Entry history
Integrated into UniProtKB/Swiss-Prot: October 23, 1986
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 150 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot