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P03958

- ADA_MOUSE

UniProt

P03958 - ADA_MOUSE

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Protein

Adenosine deaminase

Gene

Ada

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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).By similarity

Catalytic activityi

Adenosine + H2O = inosine + NH3.

Cofactori

Binds 1 zinc ion per subunit.3 Publications

Kineticsi

  1. KM=20 µM for adenosine2 Publications

pH dependencei

Optimum pH is 6-8.5.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi15 – 151Zinc; catalytic
Metal bindingi17 – 171Zinc; catalytic
Binding sitei17 – 171Substrate
Binding sitei19 – 191Substrate
Binding sitei184 – 1841Substrate; via amide nitrogen and carbonyl oxygen
Metal bindingi214 – 2141Zinc; catalytic
Active sitei217 – 2171Proton donor2 Publications
Sitei238 – 2381Important for catalytic activity
Metal bindingi295 – 2951Zinc; catalytic
Binding sitei296 – 2961Substrate

GO - Molecular functioni

  1. adenosine deaminase activity Source: UniProtKB
  2. purine nucleoside binding Source: Ensembl
  3. zinc ion binding Source: UniProtKB

GO - Biological processi

  1. adenosine catabolic process Source: UniProtKB
  2. aging Source: Ensembl
  3. cell adhesion Source: UniProtKB-KW
  4. dATP catabolic process Source: MGI
  5. deoxyadenosine catabolic process Source: MGI
  6. embryonic digestive tract development Source: MGI
  7. germinal center B cell differentiation Source: MGI
  8. histamine secretion Source: Ensembl
  9. hypoxanthine biosynthetic process Source: MGI
  10. hypoxanthine salvage Source: RefGenome
  11. inosine biosynthetic process Source: UniProtKB
  12. in utero embryonic development Source: MGI
  13. liver development Source: MGI
  14. lung alveolus development Source: MGI
  15. lung development Source: MGI
  16. negative regulation of adenosine receptor signaling pathway Source: RefGenome
  17. negative regulation of apoptotic process Source: MGI
  18. negative regulation of circadian sleep/wake cycle, non-REM sleep Source: Ensembl
  19. negative regulation of inflammatory response Source: MGI
  20. negative regulation of leukocyte migration Source: MGI
  21. negative regulation of mature B cell apoptotic process Source: MGI
  22. negative regulation of mucus secretion Source: MGI
  23. negative regulation of penile erection Source: MGI
  24. negative regulation of thymocyte apoptotic process Source: MGI
  25. Peyer's patch development Source: MGI
  26. placenta development Source: MGI
  27. positive regulation of alpha-beta T cell differentiation Source: MGI
  28. positive regulation of B cell proliferation Source: MGI
  29. positive regulation of calcium-mediated signaling Source: MGI
  30. positive regulation of germinal center formation Source: MGI
  31. positive regulation of heart rate Source: MGI
  32. positive regulation of smooth muscle contraction Source: MGI
  33. positive regulation of T cell activation Source: MGI
  34. positive regulation of T cell differentiation Source: MGI
  35. positive regulation of T cell differentiation in thymus Source: MGI
  36. positive regulation of T cell receptor signaling pathway Source: MGI
  37. purine nucleotide salvage Source: Ensembl
  38. purine ribonucleoside monophosphate biosynthetic process Source: InterPro
  39. regulation of cell-cell adhesion mediated by integrin Source: Ensembl
  40. regulation of T cell differentiation Source: MGI
  41. response to drug Source: Ensembl
  42. response to hydrogen peroxide Source: Ensembl
  43. response to hypoxia Source: Ensembl
  44. response to morphine Source: Ensembl
  45. response to vitamin E Source: Ensembl
  46. T cell activation Source: Ensembl
  47. trophectodermal cell differentiation Source: MGI
  48. xanthine biosynthetic process Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Cell adhesion, Nucleotide metabolism

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Adenosine deaminase (EC:3.5.4.4)
Alternative name(s):
Adenosine aminohydrolase
Gene namesi
Name:Ada
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 2

Organism-specific databases

MGIiMGI:87916. Ada.

Subcellular locationi

Cell membrane By similarity; Peripheral membrane protein By similarity; Extracellular side By similarity. Cell junction By similarity. Cytoplasmic vesicle lumen 1 Publication. Cytoplasm By similarity
Note: Colocalized with DPP4 at the cell junction in lymphocyte-epithelial cell adhesion.By similarity

GO - Cellular componenti

  1. cell junction Source: UniProtKB-KW
  2. cytoplasm Source: MGI
  3. cytoplasmic vesicle Source: UniProtKB-KW
  4. cytosol Source: RefGenome
  5. dendrite cytoplasm Source: Ensembl
  6. external side of plasma membrane Source: RefGenome
  7. extracellular space Source: Ensembl
  8. lysosome Source: Ensembl
  9. neuronal cell body Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

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

Pathology & Biotechi

Disruption phenotypei

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.3 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi217 – 2171E → D: Reduces catalytic activity 700-fold. No effect on affinity for adenosine. 1 Publication
Mutagenesisi217 – 2171E → G: Reduces catalytic activity 3200-fold. No effect on affinity for adenosine. 1 Publication
Mutagenesisi217 – 2171E → Q: Reduces catalytic activity 4800-fold, and slighly increases affinity for substrate. 1 Publication
Mutagenesisi217 – 2171E → S: Loss of activity. 1 Publication
Mutagenesisi238 – 2381H → A: Increases affinity for adenosine 20-fold. Reduces enzyme activity 500-fold. 1 Publication
Mutagenesisi238 – 2381H → E: Nearly abolishes enzyme activity. 1 Publication
Mutagenesisi238 – 2381H → R: Reduces enzyme activity 1500-fold. No effect on affinity for adenosine. 1 Publication
Mutagenesisi295 – 2951D → E: No effect on affinity for adenosine. Reduces enzyme activity 2750-fold. 1 Publication
Mutagenesisi296 – 2961D → A: Reduces affinity for adenosine 70-fold. Reduces enzyme activity 110000-fold. 1 Publication
Mutagenesisi296 – 2961D → N: Reduces affinity for adenosine 10-fold. Reduces enzyme activity 100-fold. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 352351Adenosine deaminasePRO_0000194353Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei54 – 541N6-acetyllysineBy similarity
Modified residuei232 – 2321N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP03958.
PaxDbiP03958.
PRIDEiP03958.

2D gel databases

REPRODUCTION-2DPAGEP03958.

PTM databases

PhosphoSiteiP03958.

Expressioni

Tissue specificityi

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.1 Publication

Gene expression databases

BgeeiP03958.
CleanExiMM_ADA.
ExpressionAtlasiP03958. baseline and differential.
GenevestigatoriP03958.

Interactioni

Subunit structurei

Interacts with DPP4 (extracellular domain).By similarity

Protein-protein interaction databases

IntActiP03958. 1 interaction.
MINTiMINT-4087128.

Structurei

Secondary structure

1
352
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi11 – 133
Helixi18 – 203
Helixi24 – 3411
Helixi43 – 508
Helixi58 – 625
Helixi65 – 728
Helixi76 – 9217
Beta strandi95 – 1028
Helixi105 – 1073
Beta strandi109 – 1113
Helixi116 – 1183
Helixi126 – 14419
Beta strandi147 – 1559
Helixi159 – 1613
Helixi162 – 17110
Turni174 – 1763
Beta strandi177 – 1848
Helixi191 – 1933
Helixi195 – 20713
Beta strandi210 – 21910
Helixi221 – 2299
Beta strandi234 – 2385
Helixi240 – 2445
Helixi246 – 2549
Beta strandi258 – 2614
Helixi263 – 2686
Beta strandi270 – 2723
Helixi279 – 2857
Beta strandi289 – 2924
Helixi297 – 3004
Helixi304 – 31512
Helixi319 – 33214
Beta strandi333 – 3353
Helixi337 – 35014

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliP03958.
SMRiP03958. Positions 4-352.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP03958.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1816.
HOGENOMiHOG000218816.
HOVERGENiHBG001718.
InParanoidiP03958.
KOiK01488.
OMAiDWMVAVL.
OrthoDBiEOG7GN2MZ.
PhylomeDBiP03958.
TreeFamiTF314270.

Family and domain databases

HAMAPiMF_00540. A_deaminase.
InterProiIPR006650. A/AMP_deam_AS.
IPR001365. A/AMP_deaminase_dom.
IPR028893. A_deaminase.
IPR006330. Ado/ade_deaminase.
[Graphical view]
PfamiPF00962. A_deaminase. 1 hit.
[Graphical view]
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.

P03958-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAQTPAFNKP KVELHVHLDG AIKPETILYF GKKRGIALPA DTVEELRNII
60 70 80 90 100
GMDKPLSLPG FLAKFDYYMP VIAGCREAIK RIAYEFVEMK AKEGVVYVEV
110 120 130 140 150
RYSPHLLANS KVDPMPWNQT EGDVTPDDVV DLVNQGLQEG EQAFGIKVRS
160 170 180 190 200
ILCCMRHQPS WSLEVLELCK KYNQKTVVAM DLAGDETIEG SSLFPGHVEA
210 220 230 240 250
YEGAVKNGIH RTVHAGEVGS PEVVREAVDI LKTERVGHGY HTIEDEALYN
260 270 280 290 300
RLLKENMHFE VCPWSSYLTG AWDPKTTHAV VRFKNDKANY SLNTDDPLIF
310 320 330 340 350
KSTLDTDYQM TKKDMGFTEE EFKRLNINAA KSSFLPEEEK KELLERLYRE

YQ
Length:352
Mass (Da):39,992
Last modified:January 23, 2007 - v3
Checksum:iE53A8A1FABA148CD
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti141 – 1411E → R in AAB07142. (PubMed:2387582)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M10319 mRNA. Translation: AAA37173.1.
M34251
, 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.
CCDSiCCDS17015.1.
PIRiA01010. DUMSA.
RefSeqiNP_001258981.1. NM_001272052.1.
NP_031424.1. NM_007398.4.
UniGeneiMm.388.

Genome annotation databases

EnsembliENSMUST00000017841; ENSMUSP00000017841; ENSMUSG00000017697.
GeneIDi11486.
KEGGimmu:11486.
UCSCiuc008ntl.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M10319 mRNA. Translation: AAA37173.1 .
M34251
, 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 .
CCDSi CCDS17015.1.
PIRi A01010. DUMSA.
RefSeqi NP_001258981.1. NM_001272052.1.
NP_031424.1. NM_007398.4.
UniGenei Mm.388.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1A4L X-ray 2.60 A/B/C/D 4-352 [» ]
1A4M X-ray 1.95 A/B/C/D 4-352 [» ]
1ADD X-ray 2.40 A 4-352 [» ]
1FKW X-ray 2.40 A 4-352 [» ]
1FKX X-ray 2.40 A 4-352 [» ]
1UIO X-ray 2.40 A 4-352 [» ]
1UIP X-ray 2.40 A 4-352 [» ]
2ADA X-ray 2.40 A 1-352 [» ]
3KM8 X-ray 2.00 A/B 1-352 [» ]
3MVI X-ray 1.60 A/B 4-352 [» ]
3MVT X-ray 2.20 A/C 4-352 [» ]
3T1G X-ray 2.35 A 4-352 [» ]
ProteinModelPortali P03958.
SMRi P03958. Positions 4-352.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P03958. 1 interaction.
MINTi MINT-4087128.

Chemistry

BindingDBi P03958.
ChEMBLi CHEMBL3206.

PTM databases

PhosphoSitei P03958.

2D gel databases

REPRODUCTION-2DPAGE P03958.

Proteomic databases

MaxQBi P03958.
PaxDbi P03958.
PRIDEi P03958.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000017841 ; ENSMUSP00000017841 ; ENSMUSG00000017697 .
GeneIDi 11486.
KEGGi mmu:11486.
UCSCi uc008ntl.1. mouse.

Organism-specific databases

CTDi 100.
MGIi MGI:87916. Ada.

Phylogenomic databases

eggNOGi COG1816.
HOGENOMi HOG000218816.
HOVERGENi HBG001718.
InParanoidi P03958.
KOi K01488.
OMAi DWMVAVL.
OrthoDBi EOG7GN2MZ.
PhylomeDBi P03958.
TreeFami TF314270.

Miscellaneous databases

ChiTaRSi ADA. mouse.
EvolutionaryTracei P03958.
NextBioi 278844.
PROi P03958.
SOURCEi Search...

Gene expression databases

Bgeei P03958.
CleanExi MM_ADA.
ExpressionAtlasi P03958. baseline and differential.
Genevestigatori P03958.

Family and domain databases

HAMAPi MF_00540. A_deaminase.
InterProi IPR006650. A/AMP_deam_AS.
IPR001365. A/AMP_deaminase_dom.
IPR028893. A_deaminase.
IPR006330. Ado/ade_deaminase.
[Graphical view ]
Pfami PF00962. A_deaminase. 1 hit.
[Graphical view ]
TIGRFAMsi TIGR01430. aden_deam. 1 hit.
PROSITEi PS00485. A_DEAMINASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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.

Entry informationi

Entry nameiADA_MOUSE
AccessioniPrimary (citable) accession number: P03958
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 23, 1986
Last sequence update: January 23, 2007
Last modified: October 29, 2014
This is version 152 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3