dbPTM

AMPD2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	AMPD2_HUMAN
UniProt AC	Q01433
Protein Name	AMP deaminase 2
Gene Name	AMPD2
Organism	Homo sapiens (Human).
Sequence Length	879
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..
Protein Sequence	MRNRGQGLFRLRSRCFLHQSLPLGAGRRKGLDVAEPGPSRCRSDSPAVAAVVPAMASYPSGSGKPKAKYPFKKRASLQASTAAPEARGGLGAPPLQSARSLPGPAPCLKHFPLDLRTSMDGKCKEIAEELFTRSLAESELRSAPYEFPEESPIEQLEERRQRLERQISQDVKLEPDILLRAKQDFLKTDSDSDLQLYKEQGEGQGDRSLRERDVLEREFQRVTISGEEKCGVPFTDLLDAAKSVVRALFIREKYMALSLQSFCPTTRRYLQQLAEKPLETRTYEQGPDTPVSADAPVHPPALEQHPYEHCEPSTMPGDLGLGLRMVRGVVHVYTRREPDEHCSEVELPYPDLQEFVADVNVLMALIINGPIKSFCYRRLQYLSSKFQMHVLLNEMKELAAQKKVPHRDFYNIRKVDTHIHASSCMNQKHLLRFIKRAMKRHLEEIVHVEQGREQTLREVFESMNLTAYDLSVDTLDVHADRNTFHRFDKFNAKYNPIGESVLREIFIKTDNRVSGKYFAHIIKEVMSDLEESKYQNAELRLSIYGRSRDEWDKLARWAVMHRVHSPNVRWLVQVPRLFDVYRTKGQLANFQEMLENIFLPLFEATVHPASHPELHLFLEHVDGFDSVDDESKPENHVFNLESPLPEAWVEEDNPPYAYYLYYTFANMAMLNHLRRQRGFHTFVLRPHCGEAGPIHHLVSAFMLAENISHGLLLRKAPVLQYLYYLAQIGIAMSPLSNNSLFLSYHRNPLPEYLSRGLMVSLSTDDPLQFHFTKEPLMEEYSIATQVWKLSSCDMCELARNSVLMSGFSHKVKSHWLGPNYTKEGPEGNDIRRTNVPDIRVGYRYETLCQELALITQAVQSEMLETIPEEAGITMSPGPQ

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Dimethylation	------MRNRGQGLF ------CCCCCCCHH	41.37	-
3 (in isoform 2)	Phosphorylation	-	51.65	29514088
4	Dimethylation	----MRNRGQGLFRL ----CCCCCCCHHHH	28.57	-
6	Methylation	--MRNRGQGLFRLRS --CCCCCCCHHHHHH	42.02	26797129
13	Phosphorylation	QGLFRLRSRCFLHQS CCHHHHHHHHHEECC	37.68	20068231
16 (in isoform 2)	Phosphorylation	-	7.11	29514088
19 (in isoform 2)	Phosphorylation	-	49.13	29514088
39	Phosphorylation	DVAEPGPSRCRSDSP CCCCCCCCCCCCCCH	50.34	24275569
43	Phosphorylation	PGPSRCRSDSPAVAA CCCCCCCCCCHHHHH	46.17	46163015
45	Phosphorylation	PSRCRSDSPAVAAVV CCCCCCCCHHHHHHH	18.92	46163019
58	Phosphorylation	VVPAMASYPSGSGKP HHHHHHCCCCCCCCC	7.59	24275569
60	Phosphorylation	PAMASYPSGSGKPKA HHHHCCCCCCCCCCC	37.04	46163023
76	Phosphorylation	YPFKKRASLQASTAA CCCCHHHCCHHHCCC	25.66	23401153
79 (in isoform 3)	Ubiquitination	-	17.72	21906983
80	Phosphorylation	KRASLQASTAAPEAR HHHCCHHHCCCHHHC	12.96	30266825
81	Phosphorylation	RASLQASTAAPEARG HHCCHHHCCCHHHCC	29.83	30266825
87	Methylation	STAAPEARGGLGAPP HCCCHHHCCCCCCCC	37.74	-
97	Phosphorylation	LGAPPLQSARSLPGP CCCCCCCCCCCCCCC	33.08	22199227
99	Methylation	APPLQSARSLPGPAP CCCCCCCCCCCCCCC	43.93	-
100	Phosphorylation	PPLQSARSLPGPAPC CCCCCCCCCCCCCCC	38.34	26846344
109	Acetylation	PGPAPCLKHFPLDLR CCCCCCHHCCCCEEC	50.33	25953088
109	Ubiquitination	PGPAPCLKHFPLDLR CCCCCCHHCCCCEEC	50.33	-
117	Phosphorylation	HFPLDLRTSMDGKCK CCCCEECCCCCCHHH	35.38	23401153
117 (in isoform 2)	Ubiquitination	-	35.38	21906983
118	Phosphorylation	FPLDLRTSMDGKCKE CCCEECCCCCCHHHH	14.40	28355574
123	Glutathionylation	RTSMDGKCKEIAEEL CCCCCCHHHHHHHHH	6.13	22555962
123 (in isoform 4)	Ubiquitination	-	6.13	21906983
124	Ubiquitination	TSMDGKCKEIAEELF CCCCCHHHHHHHHHH	56.49	-
132	Phosphorylation	EIAEELFTRSLAESE HHHHHHHHHHHHHHH	31.79	23090842
134	Phosphorylation	AEELFTRSLAESELR HHHHHHHHHHHHHHH	28.95	25159151
138	Phosphorylation	FTRSLAESELRSAPY HHHHHHHHHHHHCCC	36.00	18636317
142	Phosphorylation	LAESELRSAPYEFPE HHHHHHHHCCCCCCC	46.34	21945579
145	Phosphorylation	SELRSAPYEFPEESP HHHHHCCCCCCCCCH	29.89	21945579
151	Phosphorylation	PYEFPEESPIEQLEE CCCCCCCCHHHHHHH	29.52	21945579
157 (in isoform 3)	Ubiquitination	-	49.50	21906983
168	O-linked_Glycosylation	QRLERQISQDVKLEP HHHHHHHHHCCCCCH	16.40	30379171
168	Phosphorylation	QRLERQISQDVKLEP HHHHHHHHHCCCCCH	16.40	22167270
182	Ubiquitination	PDILLRAKQDFLKTD HHHHHHHHHHHHHCC	43.92	-
187	Ubiquitination	RAKQDFLKTDSDSDL HHHHHHHHCCCCCCC	50.72	-
188	Phosphorylation	AKQDFLKTDSDSDLQ HHHHHHHCCCCCCCH	42.77	30266825
190	Phosphorylation	QDFLKTDSDSDLQLY HHHHHCCCCCCCHHH	44.22	25159151
192	Phosphorylation	FLKTDSDSDLQLYKE HHHCCCCCCCHHHHH	44.14	30266825
195 (in isoform 2)	Ubiquitination	-	47.97	21906983
197	Phosphorylation	SDSDLQLYKEQGEGQ CCCCCHHHHHCCCCC	10.26	23927012
198	Ubiquitination	DSDLQLYKEQGEGQG CCCCHHHHHCCCCCC	52.75	21906983
198 (in isoform 1)	Ubiquitination	-	52.75	21906983
201 (in isoform 4)	Ubiquitination	-	41.93	21906983
208	O-linked_Glycosylation	GEGQGDRSLRERDVL CCCCCCHHHHHHHHH	36.20	30379171
208	Phosphorylation	GEGQGDRSLRERDVL CCCCCCHHHHHHHHH	36.20	18668243
229	Ubiquitination	VTISGEEKCGVPFTD EEECCCCCCCCCHHH	31.80	-
230	S-nitrosocysteine	TISGEEKCGVPFTDL EECCCCCCCCCHHHH	8.21	-
230	Glutathionylation	TISGEEKCGVPFTDL EECCCCCCCCCHHHH	8.21	22555962
230	S-nitrosylation	TISGEEKCGVPFTDL EECCCCCCCCCHHHH	8.21	19483679
242	Ubiquitination	TDLLDAAKSVVRALF HHHHHHHHHHHHHHH	45.57	-
254	Phosphorylation	ALFIREKYMALSLQS HHHHHHHHHHHHHHH	5.27	20068231
258	Phosphorylation	REKYMALSLQSFCPT HHHHHHHHHHHHCHH	18.15	20068231
261	Phosphorylation	YMALSLQSFCPTTRR HHHHHHHHHCHHHHH	33.82	20068231
265	Phosphorylation	SLQSFCPTTRRYLQQ HHHHHCHHHHHHHHH	33.83	20068231
266	Phosphorylation	LQSFCPTTRRYLQQL HHHHCHHHHHHHHHH	9.78	20068231
276	Ubiquitination	YLQQLAEKPLETRTY HHHHHHHCCCCCCCC	49.66	21906983
276 (in isoform 1)	Ubiquitination	-	49.66	21906983
282	Phosphorylation	EKPLETRTYEQGPDT HCCCCCCCCCCCCCC	38.54	28796482
283	Phosphorylation	KPLETRTYEQGPDTP CCCCCCCCCCCCCCC	11.72	28796482
289	Phosphorylation	TYEQGPDTPVSADAP CCCCCCCCCCCCCCC	28.82	28348404
292	Phosphorylation	QGPDTPVSADAPVHP CCCCCCCCCCCCCCC	22.95	28796482
307	Phosphorylation	PALEQHPYEHCEPST CHHHCCCCCCCCCCC	19.04	28796482
313	Phosphorylation	PYEHCEPSTMPGDLG CCCCCCCCCCCCCCH	18.29	28796482
314	Phosphorylation	YEHCEPSTMPGDLGL CCCCCCCCCCCCCHH	37.79	28796482
372	Sumoylation	LIINGPIKSFCYRRL HHHCCCHHHHHHHHH	40.38	-
372	Sumoylation	LIINGPIKSFCYRRL HHHCCCHHHHHHHHH	40.38	-
374 (in isoform 3)	Ubiquitination	-	3.45	21906983
389 (in isoform 3)	Ubiquitination	-	9.04	21906983
397	Acetylation	VLLNEMKELAAQKKV HHHHHHHHHHHCCCC	42.18	19608861
398	Acetylation	LLNEMKELAAQKKVP HHHHHHHHHHCCCCC	3.90	19608861
412 (in isoform 2)	Ubiquitination	-	2.84	21906983
414	Ubiquitination	RDFYNIRKVDTHIHA HHCCCEEECCCEEEH	40.44	-
414 (in isoform 3)	Ubiquitination	-	40.44	21906983
418 (in isoform 4)	Ubiquitination	-	12.84	21906983
427 (in isoform 2)	Ubiquitination	-	13.99	21906983
433 (in isoform 4)	Ubiquitination	-	8.56	21906983
435	Acetylation	KHLLRFIKRAMKRHL HHHHHHHHHHHHHHH	31.24	19608861
441	Acetylation	IKRAMKRHLEEIVHV HHHHHHHHHHHHHCH	31.88	19608861
452 (in isoform 2)	Ubiquitination	-	32.32	21906983
458 (in isoform 4)	Ubiquitination	-	55.46	21906983
489	Acetylation	NTFHRFDKFNAKYNP CCCCCHHHCCCCCCC	37.49	27452117
489	Ubiquitination	NTFHRFDKFNAKYNP CCCCCHHHCCCCCCC	37.49	-
493	Acetylation	RFDKFNAKYNPIGES CHHHCCCCCCCCCHH	46.82	27452117
493	Ubiquitination	RFDKFNAKYNPIGES CHHHCCCCCCCCCHH	46.82	21906983
493 (in isoform 1)	Ubiquitination	-	46.82	21906983
494	Phosphorylation	FDKFNAKYNPIGESV HHHCCCCCCCCCHHH	24.62	5051937
500	Phosphorylation	KYNPIGESVLREIFI CCCCCCHHHHHHHHH	22.65	19060867
508	Ubiquitination	VLREIFIKTDNRVSG HHHHHHHCCCCCCCH	38.79	21906983
508 (in isoform 1)	Ubiquitination	-	38.79	21906983
509	Phosphorylation	LREIFIKTDNRVSGK HHHHHHCCCCCCCHH	33.42	68701067
516	Acetylation	TDNRVSGKYFAHIIK CCCCCCHHHHHHHHH	29.68	23954790
526	Sulfoxidation	AHIIKEVMSDLEESK HHHHHHHHHHHHHHC	2.43	30846556
527	Phosphorylation	HIIKEVMSDLEESKY HHHHHHHHHHHHHCC	44.19	110748373
533	Ubiquitination	MSDLEESKYQNAELR HHHHHHHCCCCCEEE	54.88	2190698
533 (in isoform 1)	Ubiquitination	-	54.88	21906983
534	Phosphorylation	SDLEESKYQNAELRL HHHHHHCCCCCEEEE	19.11	18083107
544	Phosphorylation	AELRLSIYGRSRDEW CEEEEEEECCCHHHH	11.78	30576142
547	Phosphorylation	RLSIYGRSRDEWDKL EEEEECCCHHHHHHH	39.46	30576142
721	Phosphorylation	RKAPVLQYLYYLAQI HHHHHHHHHHHHHHH	7.78	23401153
723	Phosphorylation	APVLQYLYYLAQIGI HHHHHHHHHHHHHCC	7.47	23401153
724	Phosphorylation	PVLQYLYYLAQIGIA HHHHHHHHHHHHCCC	7.93	23401153
733	Phosphorylation	AQIGIAMSPLSNNSL HHHCCCCCCCCCCCE	17.42	23401153
736	Phosphorylation	GIAMSPLSNNSLFLS CCCCCCCCCCCEEHH	37.03	23401153
743	Phosphorylation	SNNSLFLSYHRNPLP CCCCEEHHCCCCCHH	16.14	23401153
777	Sulfoxidation	HFTKEPLMEEYSIAT CCCCCHHHCHHCHHH	5.56	30846556
780	Phosphorylation	KEPLMEEYSIATQVW CCHHHCHHCHHHHHH	7.65	27732954
781	Phosphorylation	EPLMEEYSIATQVWK CHHHCHHCHHHHHHH	14.71	27732954
784	Phosphorylation	MEEYSIATQVWKLSS HCHHCHHHHHHHHHC	23.22	27732954
794	Sulfoxidation	WKLSSCDMCELARNS HHHHCCCHHHHHHHH	1.93	21406390
810	Acetylation	LMSGFSHKVKSHWLG HHHCCCCCCCCCCCC	50.59	25953088
810	Malonylation	LMSGFSHKVKSHWLG HHHCCCCCCCCCCCC	50.59	26320211
812	Ubiquitination	SGFSHKVKSHWLGPN HCCCCCCCCCCCCCC	41.21	-
839	Methylation	RTNVPDIRVGYRYET CCCCCCCCCCCHHHH	24.16	-
844	Phosphorylation	DIRVGYRYETLCQEL CCCCCCHHHHHHHHH	12.55	20068231
846	Phosphorylation	RVGYRYETLCQELAL CCCCHHHHHHHHHHH	24.73	20068231
855	Phosphorylation	CQELALITQAVQSEM HHHHHHHHHHHHHHH	16.01	20068231
860	Phosphorylation	LITQAVQSEMLETIP HHHHHHHHHHHHHCC	20.55	20068231
865	Phosphorylation	VQSEMLETIPEEAGI HHHHHHHHCCHHHCC	37.56	20068231
873	Phosphorylation	IPEEAGITMSPGPQ- CCHHHCCCCCCCCC-	15.64	26074081
875	Phosphorylation	EEAGITMSPGPQ--- HHHCCCCCCCCC---	20.32	20068231

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_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
6	Q	Methylation		26797129
Methylated at Gln-6 by N6AMT1.

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_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PP4R2_HUMAN	PPP4R2	physical	22863883
AMPD2_HUMAN	AMPD2	physical	25416956
CCDB1_HUMAN	CCNDBP1	physical	25416956
TBC9B_HUMAN	TBC1D9B	physical	26344197
NDK7_HUMAN	NME7	physical	27173435
TBG1_HUMAN	TUBG1	physical	27173435
GCP4_HUMAN	TUBGCP4	physical	27173435
TCHP_HUMAN	TCHP	physical	27173435

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
615809	Pontocerebellar hypoplasia 9 (PCH9)
615686	Spastic paraplegia 63, autosomal recessive (SPG63)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of AMPD2_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"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-516, AND MASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-76 AND SER-190, AND MASSSPECTROMETRY.	19690332 [Abstract]
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-100; SER-118; SER-151;SER-168 AND SER-190, AND MASS SPECTROMETRY.	18669648 [Abstract]
"Phosphoproteome of resting human platelets."; Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,Schuetz C., Walter U., Gambaryan S., Sickmann A.; J. Proteome Res. 7:526-534(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-190, AND MASSSPECTROMETRY.	18088087 [Abstract]
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column."; Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.; Anal. Sci. 24:161-166(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-494 AND SER-500, ANDMASS SPECTROMETRY.	18187866 [Abstract]
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization."; Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; Nat. Biotechnol. 24:1285-1292(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-100, AND MASSSPECTROMETRY.	16964243 [Abstract]
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-168, AND MASSSPECTROMETRY.	17081983 [Abstract]

show