UniProt ID | RIOX1_HUMAN | |
---|---|---|
UniProt AC | Q9H6W3 | |
Protein Name | Ribosomal oxygenase 1 {ECO:0000312|HGNC:HGNC:20968} | |
Gene Name | RIOX1 {ECO:0000312|HGNC:HGNC:20968} | |
Organism | Homo sapiens (Human). | |
Sequence Length | 641 | |
Subcellular Localization | Nucleus, nucleolus. Nucleus, nucleoplasm. Granular part of nucleoli. Nucleoplasm, nucleoplasmic foci, some of them associated with nucleoli. | |
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. 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). 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 (By similarity). May also play a role in ribosome biogenesis and in the replication or remodeling of certain heterochromatic region. Participates in MYC-induced transcriptional activation.. | |
Protein Sequence | MDGLQASAGPLRRGRPKRRRKPQPHSGSVLALPLRSRKIRKQLRSVVSRMAALRTQTLPSENSEESRVESTADDLGDALPGGAAVAAVPDAARREPYGHLGPAELLEASPAARSLQTPSARLVPASAPPARLVEVPAAPVRVVETSALLCTAQHLAAVQSSGAPATASGPQVDNTGGEPAWDSPLRRVLAELNRIPSSRRRAARLFEWLIAPMPPDHFYRRLWEREAVLVRRQDHTYYQGLFSTADLDSMLRNEEVQFGQHLDAARYINGRRETLNPPGRALPAAAWSLYQAGCSLRLLCPQAFSTTVWQFLAVLQEQFGSMAGSNVYLTPPNSQGFAPHYDDIEAFVLQLEGRKLWRVYRPRVPTEELALTSSPNFSQDDLGEPVLQTVLEPGDLLYFPRGFIHQAECQDGVHSLHLTLSTYQRNTWGDFLEAILPLAVQAAMEENVEFRRGLPRDFMDYMGAQHSDSKDPRRTAFMEKVRVLVARLGHFAPVDAVADQRAKDFIHDSLPPVLTDRERALSVYGLPIRWEAGEPVNVGAQLTTETEVHMLQDGIARLVGEGGHLFLYYTVENSRVYHLEEPKCLEIYPQQADAMELLLGSYPEFVRVGDLPCDSVEDQLSLATTLYDKGLLLTKMPLALN | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
1 | Acetylation | -------MDGLQASA -------CCCCCCCC | 22814378 | ||
26 | Phosphorylation | RRKPQPHSGSVLALP CCCCCCCCCCCCCHH | 21712546 | ||
28 | Phosphorylation | KPQPHSGSVLALPLR CCCCCCCCCCCHHCC | 28555341 | ||
48 | Phosphorylation | KQLRSVVSRMAALRT HHHHHHHHHHHHHHH | - | ||
55 | Phosphorylation | SRMAALRTQTLPSEN HHHHHHHHCCCCCCC | - | ||
60 | Phosphorylation | LRTQTLPSENSEESR HHHCCCCCCCCHHHH | 28348404 | ||
63 | Phosphorylation | QTLPSENSEESRVES CCCCCCCCHHHHCCC | 21815630 | ||
66 | Phosphorylation | PSENSEESRVESTAD CCCCCHHHHCCCCHH | 21815630 | ||
70 | Phosphorylation | SEESRVESTADDLGD CHHHHCCCCHHHHHH | - | ||
97 | Phosphorylation | DAARREPYGHLGPAE HHHHCCCCCCCCHHH | 29255136 | ||
109 | Phosphorylation | PAELLEASPAARSLQ HHHHHHHCHHHHHCC | 30266825 | ||
114 | Phosphorylation | EASPAARSLQTPSAR HHCHHHHHCCCCCCC | 24114839 | ||
117 | Phosphorylation | PAARSLQTPSARLVP HHHHHCCCCCCCCCC | 24114839 | ||
119 | Phosphorylation | ARSLQTPSARLVPAS HHHCCCCCCCCCCCC | 24114839 | ||
126 | Phosphorylation | SARLVPASAPPARLV CCCCCCCCCCCCCEE | 24114839 | ||
197 | Phosphorylation | AELNRIPSSRRRAAR HHHCCCCCHHHHHHH | 20860994 | ||
198 | Phosphorylation | ELNRIPSSRRRAARL HHCCCCCHHHHHHHH | 20860994 | ||
236 | Phosphorylation | LVRRQDHTYYQGLFS EEECCCCCCEECCCC | 24043423 | ||
237 | Phosphorylation | VRRQDHTYYQGLFST EECCCCCCEECCCCH | 24043423 | ||
238 | Phosphorylation | RRQDHTYYQGLFSTA ECCCCCCEECCCCHH | 24043423 | ||
243 | Phosphorylation | TYYQGLFSTADLDSM CCEECCCCHHCHHHH | 24043423 | ||
244 | Phosphorylation | YYQGLFSTADLDSML CEECCCCHHCHHHHH | 24043423 | ||
249 | Phosphorylation | FSTADLDSMLRNEEV CCHHCHHHHHCCCCC | 24043423 | ||
480 | Ubiquitination | RRTAFMEKVRVLVAR HHHHHHHHHHHHHHH | - | ||
480 | Methylation | RRTAFMEKVRVLVAR HHHHHHHHHHHHHHH | - | ||
503 | Ubiquitination | AVADQRAKDFIHDSL HHCCHHHHHHHHHCC | - | ||
522 | Phosphorylation | TDRERALSVYGLPIR CCHHHHHHHHCCCCE | 20068231 | ||
524 | Phosphorylation | RERALSVYGLPIRWE HHHHHHHHCCCCEEE | 27642862 | ||
629 | Ubiquitination | LATTLYDKGLLLTKM HHHHHHHCCCHHHCC | 29967540 | ||
635 | Ubiquitination | DKGLLLTKMPLALN- HCCCHHHCCCCCCC- | - |
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 RIOX1_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of RIOX1_HUMAN !! |
* 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 RIOX1_HUMAN !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
MYC_HUMAN | MYC | physical | 17308053 | |
TRRAP_HUMAN | TRRAP | physical | 17308053 | |
KAT5_HUMAN | KAT5 | physical | 17308053 |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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