dbPTM

NUDT5_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	NUDT5_HUMAN
UniProt AC	Q9UKK9
Protein Name	ADP-sugar pyrophosphatase
Gene Name	NUDT5
Organism	Homo sapiens (Human).
Sequence Length	219
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. [PubMed: 27257257 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]
Protein Sequence	MESQEPTESSQNGKQYIISEELISEGKWVKLEKTTYMDPTGKTRTWESVKRTTRKEQTADGVAVIPVLQRTLHYECIVLVKQFRPPMGGYCIEFPAGLIDDGETPEAAALRELEEETGYKGDIAECSPAVCMDPGLSNCTIHIVTVTINGDDAENARPKPKPGDGEFVEVISLPKNDLLQRLDALVAEEHLTVDARVYSYALALKHANAKPFEVPFLKF

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MESQEPTE -------CCCCCCCC	11.45	20068231
3	Phosphorylation	-----MESQEPTESS -----CCCCCCCCCC	38.25	25159151
7	Phosphorylation	-MESQEPTESSQNGK -CCCCCCCCCCCCCC	47.98	25159151
9	Phosphorylation	ESQEPTESSQNGKQY CCCCCCCCCCCCCEE	39.44	25159151
10	Phosphorylation	SQEPTESSQNGKQYI CCCCCCCCCCCCEEE	22.79	25159151
14	Ubiquitination	TESSQNGKQYIISEE CCCCCCCCEEEEEHH	47.69	-
16	Phosphorylation	SSQNGKQYIISEELI CCCCCCEEEEEHHHH	12.05	28152594
19	Phosphorylation	NGKQYIISEELISEG CCCEEEEEHHHHHCC	18.56	29759185
27	Ubiquitination	EELISEGKWVKLEKT HHHHHCCCCEEEEEE	44.77	29967540
27	Acetylation	EELISEGKWVKLEKT HHHHHCCCCEEEEEE	44.77	25953088
30	Ubiquitination	ISEGKWVKLEKTTYM HHCCCCEEEEEEEEE	50.22	-
33	Ubiquitination	GKWVKLEKTTYMDPT CCCEEEEEEEEECCC	57.51	-
33	Acetylation	GKWVKLEKTTYMDPT CCCEEEEEEEEECCC	57.51	23954790
36	Nitration	VKLEKTTYMDPTGKT EEEEEEEEECCCCCC	12.54	-
37	Sulfoxidation	KLEKTTYMDPTGKTR EEEEEEEECCCCCCC	4.71	30846556
42	Ubiquitination	TYMDPTGKTRTWESV EEECCCCCCCCHHHH	36.99	21906983
42	Sumoylation	TYMDPTGKTRTWESV EEECCCCCCCCHHHH	36.99	28112733
42	Acetylation	TYMDPTGKTRTWESV EEECCCCCCCCHHHH	36.99	23954790
43	Phosphorylation	YMDPTGKTRTWESVK EECCCCCCCCHHHHH	34.38	23927012
45	Phosphorylation	DPTGKTRTWESVKRT CCCCCCCCHHHHHHC	38.52	23927012
48	Phosphorylation	GKTRTWESVKRTTRK CCCCCHHHHHHCCCC	25.21	23927012
50	Ubiquitination	TRTWESVKRTTRKEQ CCCHHHHHHCCCCEE	53.99	27667366
55	Ubiquitination	SVKRTTRKEQTADGV HHHHCCCCEECCCCE	52.67	21906983
58	Phosphorylation	RTTRKEQTADGVAVI HCCCCEECCCCEEEE	28.01	21406692
71	Phosphorylation	VIPVLQRTLHYECIV EEHHHHHHEEEEEEE	12.62	28152594
74	Phosphorylation	VLQRTLHYECIVLVK HHHHHEEEEEEEEEE	18.66	27273156
75	Ubiquitination	LQRTLHYECIVLVKQ HHHHEEEEEEEEEEE	13.66	24816145
76	Glutathionylation	QRTLHYECIVLVKQF HHHEEEEEEEEEEEC	1.74	22555962
89	Ubiquitination	QFRPPMGGYCIEFPA ECCCCCCEEEEEECC	14.11	23000965
119	Ubiquitination	ELEEETGYKGDIAEC HHHHHHCCCCCHHHC	21.15	23000965
124	Neddylation	TGYKGDIAECSPAVC HCCCCCHHHCCCEEE	19.24	32015554
124	Ubiquitination	TGYKGDIAECSPAVC HCCCCCHHHCCCEEE	19.24	23000965
132	Ubiquitination	ECSPAVCMDPGLSNC HCCCEEEECCCCCCC	5.83	23000965
161	Ubiquitination	ENARPKPKPGDGEFV HHCCCCCCCCCCCEE	68.69	24816145
172	Phosphorylation	GEFVEVISLPKNDLL CCEEEEEEECHHHHH	43.74	24719451
172	Ubiquitination	GEFVEVISLPKNDLL CCEEEEEEECHHHHH	43.74	23000965
175	Ubiquitination	VEVISLPKNDLLQRL EEEEEECHHHHHHHH	69.27	23000965
198	Phosphorylation	LTVDARVYSYALALK CCCCHHHHHHHHHHH	7.15	28152594
199	Phosphorylation	TVDARVYSYALALKH CCCHHHHHHHHHHHH	10.89	28152594
200	Phosphorylation	VDARVYSYALALKHA CCHHHHHHHHHHHHC	6.48	28152594
202	Ubiquitination	ARVYSYALALKHANA HHHHHHHHHHHHCCC	4.33	23000965
205	Ubiquitination	YSYALALKHANAKPF HHHHHHHHHCCCCCC	34.76	23000965
205	Methylation	YSYALALKHANAKPF HHHHHHHHHCCCCCC	34.76	115974303
207	Ubiquitination	YALALKHANAKPFEV HHHHHHHCCCCCCCC	18.98	23000965
207	Neddylation	YALALKHANAKPFEV HHHHHHHCCCCCCCC	18.98	32015554
210	Ubiquitination	ALKHANAKPFEVPFL HHHHCCCCCCCCCCC	50.47	23000965
210	Neddylation	ALKHANAKPFEVPFL HHHHCCCCCCCCCCC	50.47	32015554
210	Acetylation	ALKHANAKPFEVPFL HHHHCCCCCCCCCCC	50.47	19608861
215	Ubiquitination	NAKPFEVPFLKF--- CCCCCCCCCCCC---	22.96	23000965
218	Methylation	PFEVPFLKF------ CCCCCCCCC------	49.78	19608861
218	Acetylation	PFEVPFLKF------ CCCCCCCCC------	49.78	19608861
218	Ubiquitination	PFEVPFLKF------ CCCCCCCCC------	49.78	23000965

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_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
45	T	Phosphorylation	27257257
Dephosphorylation at Thr-45 promotes the ATP-synthesis activity.
45	T	Phosphorylation	27257257
Phosphorylation at Thr-45 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_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
GANP_HUMAN	MCM3AP	physical	16169070
SKA3_HUMAN	SKA3	physical	22939629
RFA2_HUMAN	RPA2	physical	22939629
CUL1_HUMAN	CUL1	physical	22863883
TRI47_HUMAN	TRIM47	physical	22863883
NHRF2_HUMAN	SLC9A3R2	physical	27173435
YAP1_HUMAN	YAP1	physical	27173435
CTNB1_HUMAN	CTNNB1	physical	27173435

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 NUDT5_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 MET-1, AND MASS SPECTROMETRY.	19413330 [Abstract]
"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-42; LYS-210 AND LYS-218, ANDMASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells."; Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.; Nat. Biotechnol. 23:94-101(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-74, AND MASSSPECTROMETRY.	15592455 [Abstract]

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