dbPTM

NUDT5_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	NUDT5_MOUSE
UniProt AC	Q9JKX6
Protein Name	ADP-sugar pyrophosphatase {ECO:0000250\|UniProtKB:Q9UKK9}
Gene Name	Nudt5 {ECO:0000312\|MGI:MGI:1858232}
Organism	Mus musculus (Mouse).
Sequence Length	218
Subcellular Localization	Nucleus .
Protein Description	Enzyme that can either act as an ADP-sugar pyrophosphatase in absence of diphosphate or catalyze the synthesis of ATP in presence of diphosphate (By similarity). In absence of diphosphate, hydrolyzes with similar activities various modified nucleoside diphosphates such as ADP-ribose, ADP-mannose, ADP-glucose, 8-oxo-GDP and 8-oxo-dGDP. [PubMed: 10722730 Can also hydrolyze other nucleotide sugars with low activity]
Protein Sequence	METRESTESSPGKHLVTSEELISEGKWVKFEKTTYMDPTGKTRTWETVKLTTRKGKSADAVSVIPVLQRTLHHECVILVKQFRPPMGSYCLEFPAGFIEDGESPEAAALRELEEETGYKGEVAECSPAVCMDPGLSNCTTHVVTVTINGDDAGNVRPKPKPGDGEFMEVISLPKNDLLTRLDALGAEQHLTVDAKVYAYGLALKHANSKPFEVPFLKF

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------METRESTE -------CCCCCCCC	12.23	-
3	Phosphorylation	-----METRESTESS -----CCCCCCCCCC	38.14	24759943
6	Phosphorylation	--METRESTESSPGK --CCCCCCCCCCCCC	33.90	22942356
7	Phosphorylation	-METRESTESSPGKH -CCCCCCCCCCCCCE	34.82	22942356
9	Phosphorylation	ETRESTESSPGKHLV CCCCCCCCCCCCEEE	41.75	27087446
10	Phosphorylation	TRESTESSPGKHLVT CCCCCCCCCCCEEEC	31.29	27087446
13	Acetylation	STESSPGKHLVTSEE CCCCCCCCEEECHHH	36.83	23806337
17	Phosphorylation	SPGKHLVTSEELISE CCCCEEECHHHHHHC	36.46	25619855
18	Phosphorylation	PGKHLVTSEELISEG CCCEEECHHHHHHCC	22.92	25619855
23	Phosphorylation	VTSEELISEGKWVKF ECHHHHHHCCCCEEE	53.58	25619855
26	Ubiquitination	EELISEGKWVKFEKT HHHHHCCCCEEEEEE	44.77	22790023
29	Acetylation	ISEGKWVKFEKTTYM HHCCCCEEEEEEEEE	46.84	7713529
42	Phosphorylation	YMDPTGKTRTWETVK EECCCCCEEEEEEEE	34.38	26643407
44	Phosphorylation	DPTGKTRTWETVKLT CCCCCEEEEEEEEEE	32.65	26643407
56	Acetylation	KLTTRKGKSADAVSV EEEECCCCCCCCEEH	45.57	23806337
62	Phosphorylation	GKSADAVSVIPVLQR CCCCCCEEHHHHHHH	18.95	20495213
75	Glutathionylation	QRTLHHECVILVKQF HHHHCCCEEEEEEEC	1.68	24333276
75	S-nitrosylation	QRTLHHECVILVKQF HHHHCCCEEEEEEEC	1.68	21278135
75	S-nitrosocysteine	QRTLHHECVILVKQF HHHHCCCEEEEEEEC	1.68	-
209	Acetylation	ALKHANSKPFEVPFL HHHHCCCCCCCCCCC	54.24	-
217	Ubiquitination	PFEVPFLKF------ CCCCCCCCC------	49.78	-
217	Acetylation	PFEVPFLKF------ CCCCCCCCC------	49.78	-

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 NUDT5_MOUSE !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
44	T	Phosphorylation	-
Dephosphorylation at Thr-44 promotes the ATP-synthesis activity.
44	T	Phosphorylation	-
Phosphorylation at Thr-44 is required for homodimer stability; dephosphorylation results in destabilization of the homodimer.

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 NUDT5_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of NUDT5_MOUSE !!

Drug and Disease Associations

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

Regulatory Network of NUDT5_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-10, 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-9, AND MASSSPECTROMETRY.	17242355 [Abstract]