dbPTM

NUDT9_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	NUDT9_HUMAN
UniProt AC	Q9BW91
Protein Name	ADP-ribose pyrophosphatase, mitochondrial
Gene Name	NUDT9
Organism	Homo sapiens (Human).
Sequence Length	350
Subcellular Localization	Isoform 1: Mitochondrion.
Protein Description	Hydrolyzes ADP-ribose (ADPR) to AMP and ribose 5'-phosphate..
Protein Sequence	MAGRLLGKALAAVSLSLALASVTIRSSRCRGIQAFRNSFSSSWFHLNTNVMSGSNGSKENSHNKARTSPYPGSKVERSQVPNEKVGWLVEWQDYKPVEYTAVSVLAGPRWADPQISESNFSPKFNEKDGHVERKSKNGLYEIENGRPRNPAGRTGLVGRGLLGRWGPNHAADPIITRWKRDSSGNKIMHPVSGKHILQFVAIKRKDCGEWAIPGGMVDPGEKISATLKREFGEEALNSLQKTSAEKREIEEKLHKLFSQDHLVIYKGYVDDPRNTDNAWMETEAVNYHDETGEIMDNLMLEAGDDAGKVKWVDINDKLKLYASHSQFIKLVAEKRDAHWSEDSEADCHAL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
67	Phosphorylation	NSHNKARTSPYPGSK CCCCCCCCCCCCCCC	38.62	20068231
68	Phosphorylation	SHNKARTSPYPGSKV CCCCCCCCCCCCCCC	19.51	25159151
70	Phosphorylation	NKARTSPYPGSKVER CCCCCCCCCCCCCCH	21.72	20068231
73	Phosphorylation	RTSPYPGSKVERSQV CCCCCCCCCCCHHCC	29.08	20068231
74	Acetylation	TSPYPGSKVERSQVP CCCCCCCCCCHHCCC	54.77	22424773
116	Phosphorylation	RWADPQISESNFSPK CCCCCCCCCCCCCCC	29.71	30266825
118	Phosphorylation	ADPQISESNFSPKFN CCCCCCCCCCCCCCC	36.06	30266825
121	Phosphorylation	QISESNFSPKFNEKD CCCCCCCCCCCCCCC	31.28	19664994
127	Succinylation	FSPKFNEKDGHVERK CCCCCCCCCCCEEEC	70.84	23954790
127	2-Hydroxyisobutyrylation	FSPKFNEKDGHVERK CCCCCCCCCCCEEEC	70.84	-
140	Phosphorylation	RKSKNGLYEIENGRP ECCCCCCEEEECCCC	19.09	-
182	Phosphorylation	ITRWKRDSSGNKIMH HHCEEECCCCCEEEC	44.15	30001349
183	Phosphorylation	TRWKRDSSGNKIMHP HCEEECCCCCEEECC	51.15	30624053
203	Acetylation	ILQFVAIKRKDCGEW EEEEEEEEECCCCCC	43.59	26051181
228	Acetylation	EKISATLKREFGEEA CCCCHHHHHHHHHHH	45.59	25953088
228	2-Hydroxyisobutyrylation	EKISATLKREFGEEA CCCCHHHHHHHHHHH	45.59	-
258	Phosphorylation	EKLHKLFSQDHLVIY HHHHHHHCCCCEEEE	45.17	23186163
310	Acetylation	GDDAGKVKWVDINDK CCCCCCEEEEECCHH	45.01	23236377
310	2-Hydroxyisobutyrylation	GDDAGKVKWVDINDK CCCCCCEEEEECCHH	45.01	-
310	Malonylation	GDDAGKVKWVDINDK CCCCCCEEEEECCHH	45.01	26320211
319	Malonylation	VDINDKLKLYASHSQ EECCHHEEEEEEHHH	45.23	26320211
319	Acetylation	VDINDKLKLYASHSQ EECCHHEEEEEEHHH	45.23	25953088
321	Phosphorylation	INDKLKLYASHSQFI CCHHEEEEEEHHHHH	12.41	28152594
323	Phosphorylation	DKLKLYASHSQFIKL HHEEEEEEHHHHHHH	15.32	-
325	Phosphorylation	LKLYASHSQFIKLVA EEEEEEHHHHHHHHH	25.04	28857561
340	Phosphorylation	EKRDAHWSEDSEADC HHCCCCCCCCCCCCC	22.97	20873877
343	Phosphorylation	DAHWSEDSEADCHAL CCCCCCCCCCCCCCC	30.54	20873877

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 NUDT9_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of NUDT9_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 NUDT9_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
A4_HUMAN	APP	physical	21832049
DUT_HUMAN	DUT	physical	26344197
IMPA1_HUMAN	IMPA1	physical	26344197
IMPA2_HUMAN	IMPA2	physical	26344197
MA2A1_HUMAN	MAN2A1	physical	26344197
NIT1_HUMAN	NIT1	physical	26344197
PHP14_HUMAN	PHPT1	physical	26344197
WDR5B_HUMAN	WDR5B	physical	28514442
TRI11_HUMAN	TRIM11	physical	28514442

Drug and Disease Associations

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

Regulatory Network of NUDT9_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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-121, AND MASSSPECTROMETRY.	18669648 [Abstract]
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."; Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.; J. Proteome Res. 6:4150-4162(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-68, AND MASSSPECTROMETRY.	17924679 [Abstract]