NUD16_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: NUD16_HUMAN
• UniProt AC: Q96DE0
• Protein Name: U8 snoRNA-decapping enzyme
• Gene Name: NUDT16
• Organism: Homo sapiens (Human).
• Sequence Length: 195
• Subcellular Localization: Nucleus . Nucleus, nucleoplasm . Nucleus, nucleolus . Cytoplasm . Localized predominantly in the cytoplasm (PubMed:21070968). Localized in nucleolus, and in a minor proportion in distinct foci in the nucleoplasm (By similarity).
• Protein Description: RNA-binding and decapping enzyme that catalyzes the cleavage of the cap structure of snoRNAs and mRNAs in a metal-dependent manner. Part of the U8 snoRNP complex that is required for the accumulation of mature 5.8S and 28S rRNA. Has diphosphatase activity and removes m7G and/or m227G caps from U8 snoRNA and leaves a 5'monophosphate on the RNA. Catalyzes also the cleavage of the cap structure on mRNAs. Does not hydrolyze cap analog structures like 7-methylguanosine nucleoside triphosphate (m7GpppG). Also hydrolysis m7G- and m227G U3-capped RNAs but with less efficiencies. Has broad substrate specificity with manganese or cobalt as cofactor and can act on various RNA species. Binds to the U8 snoRNA; metal is not required for RNA-binding. May play a role in the regulation of snoRNAs and mRNAs degradation. Acts also as a phosphatase; hydrolyzes the non-canonical purine nucleotides inosine diphosphate (IDP) and deoxyinosine diphosphate (dITP) as well as guanosine diphosphate (GDP), deoxyguanosine diphosphate (dGDP), xanthine diphosphate (XDP), inosine triphosphate (ITP) and deoxyinosine triphosphate (ITP) to their respective monophosphate derivatives and does not distinguish between the deoxy- and ribose forms. [PubMed: 20385596]
• Protein Sequence: MAGARRLELGEALALGSGWRHACHALLYAPDPGMLFGRIPLRYAILMQMRFDGRLGFPGGFVDTQDRSLEDGLNRELREELGEAAAAFRVERTDYRSSHVGSGPRVVAHFYAKRLTLEELLAVEAGATRAKDHGLEVLGLVRVPLYTLRDGVGGLPTFLENSFIGSAREQLLEALQDLGLLQSGSISGLKIPAHH

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
17	Phosphorylation	GEALALGSGWRHACH HHHHHHCCCHHHHHH	35.71	20068231
111	Phosphorylation	PRVVAHFYAKRLTLE HHHHHHHHHCCCCHH	11.01	-
116	Phosphorylation	HFYAKRLTLEELLAV HHHHCCCCHHHHHHH	35.84	-
147	Phosphorylation	LVRVPLYTLRDGVGG EEEEEEEECCCCCCC	24.01	24719451
183	Phosphorylation	QDLGLLQSGSISGLK HHCCCHHCCCCCCCC	34.18	25693802
185	Phosphorylation	LGLLQSGSISGLKIP CCCHHCCCCCCCCCC	20.87	25693802
187	Phosphorylation	LLQSGSISGLKIPAH CHHCCCCCCCCCCCC	39.51	25693802
190	Ubiquitination	SGSISGLKIPAHH-- CCCCCCCCCCCCC--	50.60	33845483

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

Oops, there are no upstream regulatory protein records of NUD16_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of NUD16_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 NUD16_HUMAN !!

Protein-Protein Interaction

Oops, there are no PPI records of NUD16_HUMAN !!

Drug and Disease Associations

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