RIOX1_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: RIOX1_MOUSE
• UniProt AC: Q9JJF3
• Protein Name: Ribosomal oxygenase 1 {ECO:0000312|MGI:MGI:1919202}
• Gene Name: Riox1 {ECO:0000312|MGI:MGI:1919202}
• Organism: Mus musculus (Mouse).
• Sequence Length: 603
• Subcellular Localization: Nucleus, nucleolus. Nucleus, nucleoplasm .
• Protein Description: Oxygenase that can act as both a histone lysine demethylase and a ribosomal histidine hydroxylase Also catalyzes the hydroxylation of 60S ribosomal protein L8 on 'His-216'. Acts as a regulator of osteoblast differentiation via its interaction with SP7/OSX by demethylating H3K4me and H3K36me, thereby inhibiting SP7/OSX-mediated promoter activation. May also play a role in ribosome biogenesis and in the replication or remodeling of certain heterochromatic region. Participates in MYC-induced transcriptional activation (By similarity). Specifically demethylates 'Lys-4' (H3K4me) and 'Lys-36' (H3K36me) of histone H3, thereby playing a central role in histone code. Preferentially demethylates trimethylated H3 'Lys-4' (H3K4me3) and monomethylated H3 'Lys-4' (H3K4me1) residues, while it has weaker activity for dimethylated H3 'Lys-36' (H3K36me2)..
• Protein Sequence: MDELPNGNGAALLKRGRGRRRRHPQSQPRGASVLALPLRPRKIRRHRKSAAASRVAALRARALRSEDSDSKVAVASVRGKRKRPAELLEASRSAEPRPVSARPRSASATLPSRVEGWAALSRNLGTAAPPPPGSHADEPGRPRASPLQQVLTELNGIPSSRRRAARLFEWLLAPLPPDHFYRRLWEREAVLVRRQDRSYYEGLFSTADLDSMLRYEDVQFGQHLDAARYVDGRRETLNPPGRALPAAAWSLYRAGCSLRLLCPQAFSPTVWQFLAVLQEQFGSMAGSNVYLTPPDSQGFAPHYDDIEAFVLQLEGRKLWRVYRPRDPSEELALTSSPNFSQEDLGEPVLQTVLEPGDLLYFPRGFIHQAECQDGVHSLHLTLSTYQRNTWGDFLEAVLPLAVQAAIEENVEFRRGLPRDFMDYMGAQHSDSKDPRRTAFMEKVRVLVARLGHFAPVDAVADQRAKDFIHDSLPPVLTDRERALSVHGLPVRWEAGEPVNVGAQLTTETQVHMLQDGVARLVGEGGRLFLYHTVENSRVYHLEEPKCLEIHPQQADAMELLLRSYPEFVRVGDLPCDSVEDQLSLATMLYDKGLLLTKTPLVPS

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
1	Acetylation	-------MDELPNGN -------CCCCCCCC		-
32	Phosphorylation	QSQPRGASVLALPLR CCCCCCCEEEEEECC		26239621
65	Phosphorylation	LRARALRSEDSDSKV HHHHHHHCCCCCCCE		30635358
68	Phosphorylation	RALRSEDSDSKVAVA HHHHCCCCCCCEEEE		30635358
70	Phosphorylation	LRSEDSDSKVAVASV HHCCCCCCCEEEEEE		30635358
76	Phosphorylation	DSKVAVASVRGKRKR CCCEEEEEECCCCCC		29176673
91	Phosphorylation	PAELLEASRSAEPRP HHHHHHHHHCCCCCC		-
105	Phosphorylation	PVSARPRSASATLPS CCCCCCCCCCCCCCC		28833060
107	Phosphorylation	SARPRSASATLPSRV CCCCCCCCCCCCCHH		26824392
109	Phosphorylation	RPRSASATLPSRVEG CCCCCCCCCCCHHHH		28833060
112	Phosphorylation	SASATLPSRVEGWAA CCCCCCCCHHHHHHH		25367039
134	Phosphorylation	AAPPPPGSHADEPGR CCCCCCCCCCCCCCC		29514104
152	Phosphorylation	SPLQQVLTELNGIPS CHHHHHHHHHCCCCC		-

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

Oops, there are no upstream regulatory protein records of RIOX1_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of RIOX1_MOUSE !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of RIOX1_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of RIOX1_MOUSE !!

Drug and Disease Associations

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