dbPTM

ADK_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ADK_HUMAN
UniProt AC	P55263
Protein Name	Adenosine kinase
Gene Name	ADK
Organism	Homo sapiens (Human).
Sequence Length	362
Subcellular Localization	Isoform 1: Nucleus . Isoform 2: Cytoplasm .
Protein Description	ATP dependent phosphorylation of adenosine and other related nucleoside analogs to monophosphate derivatives. Serves as a potential regulator of concentrations of extracellular adenosine and intracellular adenine nucleotides..
Protein Sequence	MAAAEEEPKPKKLKVEAPQALRENILFGMGNPLLDISAVVDKDFLDKYSLKPNDQILAEDKHKELFDELVKKFKVEYHAGGSTQNSIKVAQWMIQQPHKAATFFGCIGIDKFGEILKRKAAEAHVDAHYYEQNEQPTGTCAACITGDNRSLIANLAAANCYKKEKHLDLEKNWMLVEKARVCYIAGFFLTVSPESVLKVAHHASENNRIFTLNLSAPFISQFYKESLMKVMPYVDILFGNETEAATFAREQGFETKDIKEIAKKTQALPKMNSKRQRIVIFTQGRDDTIMATESEVTAFAVLDQDQKEIIDTNGAGDAFVGGFLSQLVSDKPLTECIRAGHYAASIIIRRTGCTFPEKPDFH

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAAAEEEPK ------CCCCCCCCC	18.51	22814378
34 (in isoform 2)	Ubiquitination	-	6.07	21906983
42	Ubiquitination	DISAVVDKDFLDKYS EHHEEECHHHHHHCC	38.48	-
47	Ubiquitination	VDKDFLDKYSLKPND ECHHHHHHCCCCCCC	38.60	-
47	Acetylation	VDKDFLDKYSLKPND ECHHHHHHCCCCCCC	38.60	20167786
48	Phosphorylation	DKDFLDKYSLKPNDQ CHHHHHHCCCCCCCC	20.92	24732914
49	Phosphorylation	KDFLDKYSLKPNDQI HHHHHHCCCCCCCCC	35.34	24719451
51 (in isoform 1)	Ubiquitination	-	35.52	21906983
51	Ubiquitination	FLDKYSLKPNDQILA HHHHCCCCCCCCCCC	35.52	21906983
54 (in isoform 2)	Ubiquitination	-	45.48	21906983
61	2-Hydroxyisobutyrylation	DQILAEDKHKELFDE CCCCCHHHHHHHHHH	48.35	-
61	Acetylation	DQILAEDKHKELFDE CCCCCHHHHHHHHHH	48.35	26822725
61	Ubiquitination	DQILAEDKHKELFDE CCCCCHHHHHHHHHH	48.35	-
63	2-Hydroxyisobutyrylation	ILAEDKHKELFDELV CCCHHHHHHHHHHHH	62.95	-
63	Ubiquitination	ILAEDKHKELFDELV CCCHHHHHHHHHHHH	62.95	-
71 (in isoform 1)	Ubiquitination	-	66.18	21906983
71	Ubiquitination	ELFDELVKKFKVEYH HHHHHHHHHCCEEEE	66.18	21906983
71	2-Hydroxyisobutyrylation	ELFDELVKKFKVEYH HHHHHHHHHCCEEEE	66.18	-
74	Acetylation	DELVKKFKVEYHAGG HHHHHHCCEEEECCC	42.93	26051181
77	Phosphorylation	VKKFKVEYHAGGSTQ HHHCCEEEECCCCCH	10.43	21963049
82	Phosphorylation	VEYHAGGSTQNSIKV EEEECCCCCHHHHHH	26.38	28152594
83	Phosphorylation	EYHAGGSTQNSIKVA EEECCCCCHHHHHHH	34.74	20068231
86	Phosphorylation	AGGSTQNSIKVAQWM CCCCCHHHHHHHHHH	17.61	20068231
111	Ubiquitination	FGCIGIDKFGEILKR HHHEEEHHHHHHHHH	54.04	-
117	Ubiquitination	DKFGEILKRKAAEAH HHHHHHHHHHHHHHH	58.47	-
160	S-nitrosocysteine	ANLAAANCYKKEKHL HHHHHHHCCCHHCCC	4.52	-
160	S-nitrosylation	ANLAAANCYKKEKHL HHHHHHHCCCHHCCC	4.52	19483679
162	Ubiquitination	LAAANCYKKEKHLDL HHHHHCCCHHCCCCC	57.57	-
162	Sumoylation	LAAANCYKKEKHLDL HHHHHCCCHHCCCCC	57.57	-
162	Sumoylation	LAAANCYKKEKHLDL HHHHHCCCHHCCCCC	57.57	-
162	2-Hydroxyisobutyrylation	LAAANCYKKEKHLDL HHHHHCCCHHCCCCC	57.57	-
162	Acetylation	LAAANCYKKEKHLDL HHHHHCCCHHCCCCC	57.57	25953088
165	Ubiquitination	ANCYKKEKHLDLEKN HHCCCHHCCCCCCHH	59.35	-
171	Acetylation	EKHLDLEKNWMLVEK HCCCCCCHHHHHHHH	64.31	26822725
171	Ubiquitination	EKHLDLEKNWMLVEK HCCCCCCHHHHHHHH	64.31	-
178	2-Hydroxyisobutyrylation	KNWMLVEKARVCYIA HHHHHHHHHHEEEEE	33.73	-
183	Phosphorylation	VEKARVCYIAGFFLT HHHHHEEEEEEEEEE	7.31	26546556
239 (in isoform 2)	Ubiquitination	-	27.84	21906983
246	Phosphorylation	GNETEAATFAREQGF CCCHHHHHHHHHCCC	25.52	46159829
256	Ubiquitination	REQGFETKDIKEIAK HHCCCCCHHHHHHHH	50.70	2190698
256 (in isoform 1)	Ubiquitination	-	50.70	21906983
256	Acetylation	REQGFETKDIKEIAK HHCCCCCHHHHHHHH	50.70	26051181
259	Ubiquitination	GFETKDIKEIAKKTQ CCCCHHHHHHHHHHC	53.88	-
264	Ubiquitination	DIKEIAKKTQALPKM HHHHHHHHHCCCHHC	36.53	-
270	Acetylation	KKTQALPKMNSKRQR HHHCCCHHCCCCCCE	52.11	8242835
274	Acetylation	ALPKMNSKRQRIVIF CCHHCCCCCCEEEEE	47.77	19814873
290	Sulfoxidation	QGRDDTIMATESEVT CCCCCEEEEECCCEE	4.02	30846556
312	Phosphorylation	DQKEIIDTNGAGDAF CHHHHHCCCCCCCHH	25.74	22817901
329	Phosphorylation	GFLSQLVSDKPLTEC HHHHHHCCCCCHHHH	48.81	22817901
342	Phosphorylation	ECIRAGHYAASIIIR HHHHHHHHHHEEEHH	11.71	27642862
353	S-nitrosylation	IIIRRTGCTFPEKPD EEHHCCCCCCCCCCC	3.33	24105792
358	Acetylation	TGCTFPEKPDFH--- CCCCCCCCCCCC---	50.56	26822725

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 ADK_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of ADK_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 ADK_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
FICD_HUMAN	FICD	physical	21988832
PORED_HUMAN	SRD5A3	physical	21988832
NNMT_HUMAN	NNMT	physical	26344197
NQO1_HUMAN	NQO1	physical	26344197
PCBP1_HUMAN	PCBP1	physical	26344197
PIPNB_HUMAN	PITPNB	physical	26344197
RBM12_HUMAN	RBM12	physical	26344197

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
614300	Hypermethioninemia due to adenosine kinase deficiency (HMAKD)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB01048	Abacavir
DB00640	Adenosine
DB00131	Adenosine monophosphate
DB00171	Adenosine triphosphate
DB00811	Ribavirin

Regulatory Network of ADK_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.	19413330 [Abstract]
Phosphorylation
Reference	PubMed
"Identification of the phosphotyrosine proteome from thrombinactivated platelets."; Maguire P.B., Wynne K.J., Harney D.F., O'Donoghue N.M., Stephens G.,Fitzgerald D.J.; Proteomics 2:642-648(2002). Cited for: PHOSPHORYLATION AT TYR-77.	12112843 [Abstract]