ADA_HUMAN - dbPTM
ADA_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ADA_HUMAN
UniProt AC P00813
Protein Name Adenosine deaminase
Gene Name ADA
Organism Homo sapiens (Human).
Sequence Length 363
Subcellular Localization Cell membrane
Peripheral membrane protein
Extracellular side. Cell junction . Cytoplasmic vesicle lumen . Cytoplasm. Lysosome . Colocalized with DPP4 at the cell surface.
Protein Description Catalyzes the hydrolytic deamination of adenosine and 2-deoxyadenosine. [PubMed: 8452534]
Protein Sequence MAQTPAFDKPKVELHVHLDGSIKPETILYYGRRRGIALPANTAEGLLNVIGMDKPLTLPDFLAKFDYYMPAIAGCREAIKRIAYEFVEMKAKEGVVYVEVRYSPHLLANSKVEPIPWNQAEGDLTPDEVVALVGQGLQEGERDFGVKARSILCCMRHQPNWSPKVVELCKKYQQQTVVAIDLAGDETIPGSSLLPGHVQAYQEAVKSGIHRTVHAGEVGSAEVVKEAVDILKTERLGHGYHTLEDQALYNRLRQENMHFEICPWSSYLTGAWKPDTEHAVIRLKNDQANYSLNTDDPLIFKSTLDTDYQMTKRDMGFTEEEFKRLNINAAKSSFLPEDEKRELLDLLYKAYGMPPSASAGQNL
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
2Acetylation------MAQTPAFDK
------CCCCCCCCC		23.19-
4Phosphorylation----MAQTPAFDKPK
----CCCCCCCCCCC		13.6728464451
9AcetylationAQTPAFDKPKVELHV
CCCCCCCCCCEEEEE		40.0423749302
9UbiquitinationAQTPAFDKPKVELHV
CCCCCCCCCCEEEEE		40.04-
23UbiquitinationVHLDGSIKPETILYY
EEECCCCCCEEEEEE		38.20-
26PhosphorylationDGSIKPETILYYGRR
CCCCCCEEEEEEECC		25.4746158955
29PhosphorylationIKPETILYYGRRRGI
CCCEEEEEEECCCCE		10.4620090780
30PhosphorylationKPETILYYGRRRGIA
CCEEEEEEECCCCEE		10.747119995
54AcetylationLNVIGMDKPLTLPDF
HHHHCCCCCCCHHHH		32.7919608861
54UbiquitinationLNVIGMDKPLTLPDF
HHHHCCCCCCCHHHH		32.7919608861
67PhosphorylationDFLAKFDYYMPAIAG
HHHHHCCHHHHHHHH		12.5620090780
84PhosphorylationEAIKRIAYEFVEMKA
HHHHHHHHHHHHHHC		13.927451665
89SulfoxidationIAYEFVEMKAKEGVV
HHHHHHHHHCCCCEE		4.2621406390
90UbiquitinationAYEFVEMKAKEGVVY
HHHHHHHHCCCCEEE		42.68-
92UbiquitinationEFVEMKAKEGVVYVE
HHHHHHCCCCEEEEE		49.86-
111UbiquitinationPHLLANSKVEPIPWN
CCHHCCCCCCCCCCC		50.88-
147UbiquitinationGERDFGVKARSILCC
CCCCCCHHHHEEHHH		38.16-
147AcetylationGERDFGVKARSILCC
CCCCCCHHHHEEHHH		38.1625953088
162PhosphorylationMRHQPNWSPKVVELC
HHCCCCCCHHHHHHH		22.8324719451
164UbiquitinationHQPNWSPKVVELCKK
CCCCCCHHHHHHHHH		54.0919608861
164AcetylationHQPNWSPKVVELCKK
CCCCCCHHHHHHHHH		54.0923749302
170AcetylationPKVVELCKKYQQQTV
HHHHHHHHHHCCCEE		68.1123749302
170UbiquitinationPKVVELCKKYQQQTV
HHHHHHHHHHCCCEE		68.11-
171UbiquitinationKVVELCKKYQQQTVV
HHHHHHHHHCCCEEE		47.50-
206UbiquitinationQAYQEAVKSGIHRTV
HHHHHHHHHCCCCEE		50.44-
225UbiquitinationVGSAEVVKEAVDILK
CCCHHHHHHHHHHHH		45.17-
232UbiquitinationKEAVDILKTERLGHG
HHHHHHHHHHCCCCC		48.9919608861
232AcetylationKEAVDILKTERLGHG
HHHHHHHHHHCCCCC		48.9919608861
240PhosphorylationTERLGHGYHTLEDQA
HHCCCCCCCHHHHHH		5.9728796482
242PhosphorylationRLGHGYHTLEDQALY
CCCCCCCHHHHHHHH		24.2928796482
249PhosphorylationTLEDQALYNRLRQEN
HHHHHHHHHHHHHHC		10.9728796482
273UbiquitinationSYLTGAWKPDTEHAV
HHHCCCCCCCCCCEE		32.26-
284UbiquitinationEHAVIRLKNDQANYS
CCEEEEEECCCCCCC		48.9421906983
290PhosphorylationLKNDQANYSLNTDDP
EECCCCCCCCCCCCC		19.9728796482
291PhosphorylationKNDQANYSLNTDDPL
ECCCCCCCCCCCCCE		18.2346158949
301UbiquitinationTDDPLIFKSTLDTDY
CCCCEEEEHHCCCCC		35.22-
302PhosphorylationDDPLIFKSTLDTDYQ
CCCEEEEHHCCCCCC		24.3722210691
303PhosphorylationDPLIFKSTLDTDYQM
CCEEEEHHCCCCCCC		29.2822210691
306PhosphorylationIFKSTLDTDYQMTKR
EEEHHCCCCCCCCHH		39.4528796482
308PhosphorylationKSTLDTDYQMTKRDM
EHHCCCCCCCCHHHC		11.4128796482
311PhosphorylationLDTDYQMTKRDMGFT
CCCCCCCCHHHCCCC		13.8528796482
312UbiquitinationDTDYQMTKRDMGFTE
CCCCCCCHHHCCCCH		40.85-
312AcetylationDTDYQMTKRDMGFTE
CCCCCCCHHHCCCCH		40.8525953088
315SulfoxidationYQMTKRDMGFTEEEF
CCCCHHHCCCCHHHH		5.7421406390
323AcetylationGFTEEEFKRLNINAA
CCCHHHHHHCCCHHH		60.2923749302
323UbiquitinationGFTEEEFKRLNINAA
CCCHHHHHHCCCHHH		60.29-
331UbiquitinationRLNINAAKSSFLPED
HCCCHHHHHHCCCHH		44.19-
331AcetylationRLNINAAKSSFLPED
HCCCHHHHHHCCCHH		44.1925953088
340UbiquitinationSFLPEDEKRELLDLL
HCCCHHHHHHHHHHH		64.59-
340AcetylationSFLPEDEKRELLDLL
HCCCHHHHHHHHHHH		64.5925953088
348PhosphorylationRELLDLLYKAYGMPP
HHHHHHHHHHHCCCC		10.8125147952
351PhosphorylationLDLLYKAYGMPPSAS
HHHHHHHHCCCCCCC		15.146843299
356PhosphorylationKAYGMPPSASAGQNL
HHHCCCCCCCCCCCC		29.0526074081
358PhosphorylationYGMPPSASAGQNL--
HCCCCCCCCCCCC--		36.9526074081
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of ADA_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ADA_HUMAN !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of ADA_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
AA1R_HUMANADORA1physical
12150791
DRD1_HUMANDRD1physical
12150791
GCR_HUMANNR3C1physical
9154805
AA2AR_HUMANADORA2Aphysical
11125033
SGCD_HUMANSGCDphysical
21988832
PIAS2_HUMANPIAS2physical
21988832
POTEF_HUMANPOTEFphysical
26186194
ACTB_HUMANACTBphysical
26186194
PPAC_HUMANACP1physical
26344197
APT_HUMANAPRTphysical
26344197
ATX2_HUMANATXN2physical
26344197
ATX2L_HUMANATXN2Lphysical
26344197
SPB5_HUMANSERPINB5physical
26344197
CHK1_HUMANCHEK1genetic
28319113
PTEN_HUMANPTENgenetic
28319113
POTEF_HUMANPOTEFphysical
28514442
ACTBL_HUMANACTBL2physical
28514442
WEE1_HUMANWEE1genetic
27453043
CHK1_HUMANCHEK1genetic
27453043
BLM_HUMANBLMgenetic
27453043
Drug and Disease Associations
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)
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
Regulatory Network of ADA_HUMAN

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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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