Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Adenosine deaminase  

UniProtKB / Swiss-Prot ID :  ADA_HUMAN

Gene Name (Synonyms) : 
ADA, ADA1  

Species :  Homo sapiens (Human). 

Subcellular Localization :  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. 

Protein 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. 

Protein Sequence MAQTPAFDKPKVELHVHLDGSIKPETILYYGRRRGIALPANTAEGLLNVIGMDKPLTLPDFLAKFDYYMP...
Predicted Secondary Structure CCCCCCCCCCCEEEEECCCCCCCHHHHHHHHHHCCCCCCCCCHHHHHHHHHCCCCCCHHHHHHHHHHHHH...
Protein Variant
LocationDescription
8D -> N (in allele ADA*2; in about 10% ofthe population; 20% to 30% decrease in
15H -> D (in ADASCID; loss of activity;dbSNP:rs121908725).
20G -> R (in ADASCID; loss of activity;dbSNP:rs121908724).
74G -> C (in ADASCID; delayed-onset;dbSNP:rs121908730).
76R -> W (in ADASCID; dbSNP:rs121908736). VAR_002213
80K -> R (in dbSNP:rs11555566). VAR_002214
83A -> D (in ADASCID; loss of activity;dbSNP:rs121908726).
101R -> L (in ADASCID; dbSNP:rs121908720). VAR_002216
101R -> Q (in ADASCID; loss of activity;dbSNP:rs28930970).
101R -> W (in ADASCID; dbSNP:rs28930969). VAR_002217
107L -> P (in ADASCID; dbSNP:rs121908739). VAR_002219
129V -> M (in ADASCID; delayed-onset;dbSNP:rs121908731).
140G -> E (in ADASCID; dbSNP:rs121908732). VAR_002221
142R -> Q (in a pancreatic ductaladenocarcinoma sample; somatic mutation;
149R -> Q (in ADASCID; dbSNP:rs121908737). VAR_002223
149R -> W (in ADASCID; dbSNP:rs121908733). VAR_002224
152L -> M (in an individual with partial ADAdeficiency but no immunodeficiency; 1,5%
156R -> C (in ADASCID; dbSNP:rs121908735). VAR_002226
156R -> H (in ADASCID; dbSNP:rs121908722). VAR_002227
177V -> M (in ADASCID; loss of activity;dbSNP:rs121908719).
179A -> D (in ADASCID; loss of activity;dbSNP:rs121908727).
199Q -> P (in ADASCID; delayed-onset;dbSNP:rs121908734).
211R -> C (in ADASCID; late onset;dbSNP:rs121908740).
211R -> H (in ADASCID; dbSNP:rs121908716). VAR_002232
215A -> T (in ADASCID; dbSNP:rs114025668). VAR_002233
216G -> R (in ADASCID; severe;dbSNP:rs121908723).
233T -> I (in an individual with partial ADAdeficiency but no immunodeficiency; 20%
274P -> L (in ADASCID; dbSNP:rs121908738). VAR_002236
291S -> L (in ADASCID; dbSNP:rs121908721). VAR_002237
297P -> Q (in ADASCID; dbSNP:rs121908718). VAR_002238
304L -> R (in ADASCID; loss of activity). VAR_002239
329A -> V (in ADASCID; dbSNP:rs121908715). VAR_002240
337Missing (in ADASCID). VAR_002241
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
Protein Variant
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
2N-acetylalanine.---MAQTPA
---CCCCCC
23.19UniProtKB
Link
29PhosphotyrosineETILYYGRR
HHHHHHHHH
10.46Phosphositeplus
Link
54N6-acetyllysineIGMDKPLTL
HHCCCCCCH
32.79HPRD
Link
54N6-acetyllysineIGMDKPLTL
HHCCCCCCH
32.79Phosphositeplus
Link
54N6-acetyllysine.IGMDKPLTL
HHCCCCCCH
32.79UniProtKB
Link
67PhosphotyrosineAKFDYYMPA
HHHHHHHHH
12.56Phosphositeplus
Link
164N6-acetyllysineNWSPKVVEL
HHHHHHHHH
54.09HPRD
Link
164N6-acetyllysineNWSPKVVEL
HHHHHHHHH
54.09Phosphositeplus
Link
232N6-acetyllysineVDILKTERL
HHHHCCCEE
48.99HPRD
Link
232N6-acetyllysineVDILKTERL
HHHHCCCEE
48.99Phosphositeplus
Link
232N6-acetyllysine.VDILKTERL
HHHHCCCEE
48.99UniProtKB
Link
284Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)VIRLKNDQA
HHHHHHCCC
48.94Phosphositeplus
Link
348PhosphotyrosineLDLLYKAYG
HHHHHHHHC
10.81Phosphositeplus
Link
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
DPP4_HUMANphysical interactionDIP:664EDIP8568233
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Disease Reference
Kegg disease
H00092 T-B-Severe combined immunodeficiencies (SCIDs), including the following four diseases: Adenosine dea
OMIM disease
102700Severe combined immunodeficiency autosomal recessive T-cell-negative/B-cell-negative/NK-cell-negative due to adenosine deaminase deficiency (ADASCID)
Drug Reference
Kegg drug
D00155 Pentostatin (JAN/USAN/INN); Nipent (TN)
D05134 Nelarabine (JAN/USAN/INN); Nelzarabine (USAN); Arranon (TN)
D05384 Pegademase bovine (USAN); Pegademase (INN); Adagen (TN)
DrugBank
DB00640Adenosine
DB00975Dipyridamole
DB00974Edetic Acid
DB01280Nelarabine
DB00552Pentostatin
DB00277Theophylline
DB00194Vidarabine
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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-54 AND LYS-232, AND MASSSPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures