NO66_DROME - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: NO66_DROME
• UniProt AC: Q7K4H4
• Protein Name: Bifunctional lysine-specific demethylase and histidyl-hydroxylase NO66
• Gene Name: CG2982
• Organism: Drosophila melanogaster (Fruit fly).
• Sequence Length: 653
• Subcellular Localization: Nucleus.
• Protein Description: Oxygenase that can act as both a histone lysine demethylase and a ribosomal histidine hydroxylase. Specifically demethylates 'Lys-4' (H3K4me) and 'Lys-36' (H3K36me) of histone H3, thereby playing a central role in histone code (By similarity)..
• Protein Sequence: MKKATTSAAAKSQGNSKMQKNANNGTAKDKKKPNLDKESNDSNSVSDMLAVTKDQEVHAFFSKLFDDDAGPSTSKKTQSGSAAAAKTADRKRRLQAEADANNNDTGKAGKLTKESEATQGARATKRKQARSLGLERTSPIQVNGAALACPLVRKSLPPGEANSCPQPPKKDPAAVNSLVKIIKAEPTEEGNNNNDEKETETIETHKADSVEEGRRVLQWILFPVQTKVFFKDFWEHTACLVQRSNPKYFQSMISFKMLDEILIRHHLDFTVNVDVTTYKNGKRETLNPEGRALPPAVWGFYSDGCSIRLLNPSTYLIRLRQVCTVLQEFFHCKVGANLYLTPPNSQGFAPHYDDIEAFVIQVEGRKRWLLYEPPKKADQLARISSGNYDQEQLGKPIIDEVLSAGDVLYFPRGAVHQAITEEQQHSLHITLSVYQQQAYANLLETLMPMVLKKAVDRSVALRRGLPLHTFQVLGNAYKGNDCGSRKQLVENVQKLVTNYLMPSEDDIDEAVDQMAKKFQHEALPPIVLPSEEVRTVHGARSDADEQGNCVCDYKFNKKTSVRLLRANILRLVTESDGSVRIYHHVDNGLDYCKYEPYFMEILPEEAKAVELLISAYPFYLTIDQLPLESSARKIEVATALWEHGLLMTEKPFK

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
39	Phosphorylation	KPNLDKESNDSNSVS CCCCCCCCCCCCCHH	52.24	19429919
42	Phosphorylation	LDKESNDSNSVSDML CCCCCCCCCCHHHHH	34.94	19429919
44	Phosphorylation	KESNDSNSVSDMLAV CCCCCCCCHHHHHHH	27.27	19429919
46	Phosphorylation	SNDSNSVSDMLAVTK CCCCCCHHHHHHHCC	19.68	19429919
52	Phosphorylation	VSDMLAVTKDQEVHA HHHHHHHCCHHHHHH	24.24	19429919
131	Phosphorylation	TKRKQARSLGLERTS HHHHHHHHCCCCCCC	29.79	25749252
137	Phosphorylation	RSLGLERTSPIQVNG HHCCCCCCCCCCCCC	29.49	19429919
138	Phosphorylation	SLGLERTSPIQVNGA HCCCCCCCCCCCCCC	26.65	19429919
155	Phosphorylation	ACPLVRKSLPPGEAN HCCHHHCCCCCCCCC	35.23	22817900
180	Acetylation	AAVNSLVKIIKAEPT HHHHHHHHHHHCCCC	43.96	21791702

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

Oops, there are no upstream regulatory protein records of NO66_DROME !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of NO66_DROME !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of NO66_DROME !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PP2A_DROME	mts	physical	14605208

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Phosphorylation

"Phosphoproteome analysis of Drosophila melanogaster embryos.";
Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
J. Proteome Res. 7:1675-1682(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-44; SER-131 AND SER-138,AND MASS SPECTROMETRY.
PubMed: 18327897

"An integrated chemical, mass spectrometric and computational strategyfor (quantitative) phosphoproteomics: application to Drosophilamelanogaster Kc167 cells.";
Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D.,Juenger M.A., Eng J.K., Aebersold R., Tao W.A.;
Mol. Biosyst. 3:275-286(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-137 AND SER-138, ANDMASS SPECTROMETRY.
PubMed: 17372656