dbPTM

AMPD2_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	AMPD2_MOUSE
UniProt AC	Q9DBT5
Protein Name	AMP deaminase 2
Gene Name	Ampd2
Organism	Mus musculus (Mouse).
Sequence Length	798
Subcellular Localization
Protein Description	AMP deaminase plays a critical role in energy metabolism. Catalyzes the deamination of AMP to IMP and plays an important role in the purine nucleotide cycle (By similarity)..
Protein Sequence	MASEARSGLGASPLQSARSLPGNAPCLKHFPLDLRTSMDGKCKEIAEELFSRSLAESELRSAPYEFPEESPIEQLEERRQRLERQISQDVKLEPDILLRAKQDFLKTDSDSDLQLYKEQGEGQGDRGLWERDVVLEREFQRVIISGEEKCGVPFTDLLDAAKSVVRALFIREKYMALSLQSFCPTTRRYLQQLAEKPLETRTYEQSPDTPVSADAPVHPPALEQHPYEHCEPSAMPGDLGLGLRMVRGVVHVYTRRDPDEHCPEVELPYPDLQEFVADVNVLMALIINGPIKSFCYRRLQYLSSKFQMHVLLNEMKELAAQKKVPHRDFYNIRKVDTHIHASSCMNQKHLLRFIKRAMKRHLEEIVHVEQGREQTLREVFESMNLTAYDLSVDTLDVHADRNTFHRFDKFNAKYNPIGESVLREIFIKTDNKISGKYFAHIIKEVMADLEESKYQNAELRLSIYGRSRDEWDKLARWAVNHKVHSPNVRWLVQVPRLFDVYRTKGQLANFQEMLENIFLPLFEATVHPASHPELHLFLEHVDGFDSVDDESKPENHVFNLESPLPEAWVEEDNPPYAYYLYYTFANMAMLNHLRRQRGFHTFVLRPHCGEAGPIHHLVSAFMLAENISHGLLLRKAPVLQYLYYLAQIGIAMSPLSNNSLFLSYHRNPLPEYLSRGLMVSLSTDDPLQFHFTKEPLMEEYSIATQVWKLSSCDMCELARNSVLMSGFSHKVKSHWLGPNYTKEGPEGNDIRRTNVPDIRVGYRYETLCQELALITQAVQSEMLETIPEEVGIVMSPGP

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
3	Phosphorylation	-----MASEARSGLG -----CCHHHHCCCC	30.41	26643407
7	Phosphorylation	-MASEARSGLGASPL -CCHHHHCCCCCCHH	45.47	25159016
12	Phosphorylation	ARSGLGASPLQSARS HHCCCCCCHHHHHHC	25.09	26824392
16	Phosphorylation	LGASPLQSARSLPGN CCCCHHHHHHCCCCC	33.08	25159016
18	Methylation	ASPLQSARSLPGNAP CCHHHHHHCCCCCCC	43.93	24129315
19	Phosphorylation	SPLQSARSLPGNAPC CHHHHHHCCCCCCCC	38.34	28725479
26	Glutathionylation	SLPGNAPCLKHFPLD CCCCCCCCHHCCCCE	8.00	24333276
36	Phosphorylation	HFPLDLRTSMDGKCK CCCCEECCCCCCHHH	35.38	23984901
37	Phosphorylation	FPLDLRTSMDGKCKE CCCEECCCCCCHHHH	14.40	26239621
51	Phosphorylation	EIAEELFSRSLAESE HHHHHHHHHHHHHHH	33.32	26239621
53	Phosphorylation	AEELFSRSLAESELR HHHHHHHHHHHHHHH	30.63	25521595
57	Phosphorylation	FSRSLAESELRSAPY HHHHHHHHHHHCCCC	36.00	26745281
61	Phosphorylation	LAESELRSAPYEFPE HHHHHHHCCCCCCCC	46.34	18636335
64	Phosphorylation	SELRSAPYEFPEESP HHHHCCCCCCCCCCH	29.89	17947660
70	Phosphorylation	PYEFPEESPIEQLEE CCCCCCCCHHHHHHH	29.52	23970565
87	Phosphorylation	QRLERQISQDVKLEP HHHHHHHHHCCCCCH	16.40	27087446
107	Phosphorylation	AKQDFLKTDSDSDLQ HHHHHHHCCCCCCCH	42.77	27087446
109	Phosphorylation	QDFLKTDSDSDLQLY HHHHHCCCCCCCHHH	44.22	25521595
111	Phosphorylation	FLKTDSDSDLQLYKE HHHCCCCCCCHHHHH	44.14	25521595
116	Phosphorylation	SDSDLQLYKEQGEGQ CCCCCHHHHHCCCCC	10.26	25619855
145	Phosphorylation	EFQRVIISGEEKCGV EEEEEEECCCCCCCC	29.09	51459763
155	Phosphorylation	EKCGVPFTDLLDAAK CCCCCCHHHHHHHHH	21.48	51459771
209	Phosphorylation	TYEQSPDTPVSADAP CCCCCCCCCCCCCCC	29.04	30456941
212	Phosphorylation	QSPDTPVSADAPVHP CCCCCCCCCCCCCCC	22.95	24453211
230	Glutathionylation	EQHPYEHCEPSAMPG HCCCCCCCCCCCCCC	5.70	24333276
453	Ubiquitination	MADLEESKYQNAELR HHHHHHHCCCCCEEE	54.88	-

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 AMPD2_MOUSE !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of AMPD2_MOUSE !!

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 AMPD2_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of AMPD2_MOUSE !!

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of AMPD2_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Large scale localization of protein phosphorylation by use ofelectron capture dissociation mass spectrometry."; Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.; Mol. Cell. Proteomics 8:904-912(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-87, AND MASSSPECTROMETRY.	19131326 [Abstract]
"Large-scale phosphorylation analysis of mouse liver."; Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-111, AND MASSSPECTROMETRY.	17242355 [Abstract]
"Quantitative time-resolved phosphoproteomic analysis of mast cellsignaling."; Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,Kawakami T., Salomon A.R.; J. Immunol. 179:5864-5876(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-64, AND MASSSPECTROMETRY.	17947660 [Abstract]