NUD10_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: NUD10_HUMAN
• UniProt AC: Q8NFP7
• Protein Name: Diphosphoinositol polyphosphate phosphohydrolase 3-alpha {ECO:0000303|PubMed:12105228}
• Gene Name: NUDT10
• Organism: Homo sapiens (Human).
• Sequence Length: 164
• Subcellular Localization: Cytoplasm .
• Protein Description: Cleaves a beta-phosphate from the diphosphate groups in PP-InsP5 (diphosphoinositol pentakisphosphate), suggesting that it may play a role in signal transduction. Also able to catalyze the hydrolysis of dinucleoside oligophosphates, with Ap6A and Ap5A being the preferred substrates. The major reaction products are ADP and p4a from Ap6A and ADP and ATP from Ap5A. Also able to hydrolyze 5-phosphoribose 1-diphosphate..
• Protein Sequence: MKCKPNQTRTYDPEGFKKRAACLCFRSEREDEVLLVSSSRYPDRWIVPGGGMEPEEEPGGAAVREVYEEAGVKGKLGRLLGVFEQNQDPKHRTYVYVLTVTELLEDWEDSVSIGRKREWFKVEDAIKVLQCHKPVHAEYLEKLKLGGSPTNGNSMAPSSPDSDP

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
4	Ubiquitination	----MKCKPNQTRTY ----CCCCCCCCCCC	41.29	24816145
11	Phosphorylation	KPNQTRTYDPEGFKK CCCCCCCCCCHHHHH	26.64	-
17	Ubiquitination	TYDPEGFKKRAACLC CCCCHHHHHHEEEEE	52.81	32142685
18	Ubiquitination	YDPEGFKKRAACLCF CCCHHHHHHEEEEEE	45.03	24816145
37	Phosphorylation	EDEVLLVSSSRYPDR CCEEEEEECCCCCCC	23.67	30206219
38	Phosphorylation	DEVLLVSSSRYPDRW CEEEEEECCCCCCCE	16.03	30206219
39	Phosphorylation	EVLLVSSSRYPDRWI EEEEEECCCCCCCEE	28.47	30206219
67	Phosphorylation	GAAVREVYEEAGVKG CHHHHHHHHHHCCCC	11.87	28796482
73	Ubiquitination	VYEEAGVKGKLGRLL HHHHHCCCCHHHHHH	49.78	30230243
73	Methylation	VYEEAGVKGKLGRLL HHHHHCCCCHHHHHH	49.78	-
75	Methylation	EEAGVKGKLGRLLGV HHHCCCCHHHHHHCE	41.89	-
127	Ubiquitination	FKVEDAIKVLQCHKP EEHHHHHHHHCCCCC	38.32	-
133	Acetylation	IKVLQCHKPVHAEYL HHHHCCCCCCCHHHH	57.26	26051181
133	Ubiquitination	IKVLQCHKPVHAEYL HHHHCCCCCCCHHHH	57.26	-
142	Ubiquitination	VHAEYLEKLKLGGSP CCHHHHHHHCCCCCC	48.61	-
148	Phosphorylation	EKLKLGGSPTNGNSM HHHCCCCCCCCCCCC	27.10	22617229
150	Phosphorylation	LKLGGSPTNGNSMAP HCCCCCCCCCCCCCC	58.41	22617229
154	Phosphorylation	GSPTNGNSMAPSSPD CCCCCCCCCCCCCCC	20.09	28450419
158	Phosphorylation	NGNSMAPSSPDSDP- CCCCCCCCCCCCCC-	44.99	30266825
159	Phosphorylation	GNSMAPSSPDSDP-- CCCCCCCCCCCCC--	31.50	30266825
162	Phosphorylation	MAPSSPDSDP----- CCCCCCCCCC-----	55.98	30266825

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of NUD10_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of NUD10_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of NUD10_HUMAN !!

Protein-Protein Interaction

Oops, there are no PPI records of NUD10_HUMAN !!

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.

Related Literatures of Post-Translational Modification

Phosphorylation

"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-148; THR-150; SER-154;SER-158; SER-159 AND SER-162, AND MASS SPECTROMETRY.
PubMed: 19413330