RIOX1_HUMAN - dbPTM
RIOX1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
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
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
1Acetylation-------MDGLQASA
-------CCCCCCCC
22814378
26PhosphorylationRRKPQPHSGSVLALP
CCCCCCCCCCCCCHH
21712546
28PhosphorylationKPQPHSGSVLALPLR
CCCCCCCCCCCHHCC
28555341
48PhosphorylationKQLRSVVSRMAALRT
HHHHHHHHHHHHHHH
-
55PhosphorylationSRMAALRTQTLPSEN
HHHHHHHHCCCCCCC
-
60PhosphorylationLRTQTLPSENSEESR
HHHCCCCCCCCHHHH
28348404
63PhosphorylationQTLPSENSEESRVES
CCCCCCCCHHHHCCC
21815630
66PhosphorylationPSENSEESRVESTAD
CCCCCHHHHCCCCHH
21815630
70PhosphorylationSEESRVESTADDLGD
CHHHHCCCCHHHHHH
-
97PhosphorylationDAARREPYGHLGPAE
HHHHCCCCCCCCHHH
29255136
109PhosphorylationPAELLEASPAARSLQ
HHHHHHHCHHHHHCC
30266825
114PhosphorylationEASPAARSLQTPSAR
HHCHHHHHCCCCCCC
24114839
117PhosphorylationPAARSLQTPSARLVP
HHHHHCCCCCCCCCC
24114839
119PhosphorylationARSLQTPSARLVPAS
HHHCCCCCCCCCCCC
24114839
126PhosphorylationSARLVPASAPPARLV
CCCCCCCCCCCCCEE
24114839
197PhosphorylationAELNRIPSSRRRAAR
HHHCCCCCHHHHHHH
20860994
198PhosphorylationELNRIPSSRRRAARL
HHCCCCCHHHHHHHH
20860994
236PhosphorylationLVRRQDHTYYQGLFS
EEECCCCCCEECCCC
24043423
237PhosphorylationVRRQDHTYYQGLFST
EECCCCCCEECCCCH
24043423
238PhosphorylationRRQDHTYYQGLFSTA
ECCCCCCEECCCCHH
24043423
243PhosphorylationTYYQGLFSTADLDSM
CCEECCCCHHCHHHH
24043423
244PhosphorylationYYQGLFSTADLDSML
CEECCCCHHCHHHHH
24043423
249PhosphorylationFSTADLDSMLRNEEV
CCHHCHHHHHCCCCC
24043423
480UbiquitinationRRTAFMEKVRVLVAR
HHHHHHHHHHHHHHH
-
480MethylationRRTAFMEKVRVLVAR
HHHHHHHHHHHHHHH
-
503UbiquitinationAVADQRAKDFIHDSL
HHCCHHHHHHHHHCC
-
522PhosphorylationTDRERALSVYGLPIR
CCHHHHHHHHCCCCE
20068231
524PhosphorylationRERALSVYGLPIRWE
HHHHHHHHCCCCEEE
27642862
629UbiquitinationLATTLYDKGLLLTKM
HHHHHHHCCCHHHCC
29967540
635UbiquitinationDKGLLLTKMPLALN-
HCCCHHHCCCCCCC-
-

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

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RIOX1_HUMAN !!

Disease-associated PTM Sites based on SAP

* 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 !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MYC_HUMANMYCphysical
17308053
TRRAP_HUMANTRRAPphysical
17308053
KAT5_HUMANKAT5physical
17308053

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RIOX1_HUMAN

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Related Literatures of Post-Translational Modification

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