RIOX2_HUMAN - dbPTM
RIOX2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RIOX2_HUMAN
UniProt AC Q8IUF8
Protein Name Ribosomal oxygenase 2 {ECO:0000312|HGNC:HGNC:19441}
Gene Name RIOX2 {ECO:0000312|HGNC:HGNC:19441}
Organism Homo sapiens (Human).
Sequence Length 465
Subcellular Localization Nucleus . Nucleus, nucleolus .
Protein Description Oxygenase that can act as both a histone lysine demethylase and a ribosomal histidine hydroxylase. Is involved in the demethylation of trimethylated 'Lys-9' on histone H3 (H3K9me3), leading to an increase in ribosomal RNA expression. Also catalyzes the hydroxylation of 60S ribosomal protein L27a on 'His-39'. May play an important role in cell growth and survival. May be involved in ribosome biogenesis, most likely during the assembly process of pre-ribosomal particles..
Protein Sequence MPKKAKPTGSGKEEGPAPCKQMKLEAAGGPSALNFDSPSSLFESLISPIKTETFFKEFWEQKPLLIQRDDPALATYYGSLFKLTDLKSLCSRGMYYGRDVNVCRCVNGKKKVLNKDGKAHFLQLRKDFDQKRATIQFHQPQRFKDELWRIQEKLECYFGSLVGSNVYITPAGSQGLPPHYDDVEVFILQLEGEKHWRLYHPTVPLAREYSVEAEERIGRPVHEFMLKPGDLLYFPRGTIHQADTPAGLAHSTHVTISTYQNNSWGDFLLDTISGLVFDTAKEDVELRTGIPRQLLLQVESTTVATRRLSGFLRTLADRLEGTKELLSSDMKKDFIMHRLPPYSAGDGAELSTPGGKLPRLDSVVRLQFKDHIVLTVLPDQDQSDEAQEKMVYIYHSLKNSRETHMMGNEEETEFHGLRFPLSHLDALKQIWNSPAISVKDLKLTTDEEKESLVLSLWTECLIQVV
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
8PhosphorylationMPKKAKPTGSGKEEG
CCCCCCCCCCCCCCC
25002506
10PhosphorylationKKAKPTGSGKEEGPA
CCCCCCCCCCCCCCC
25002506
12AcetylationAKPTGSGKEEGPAPC
CCCCCCCCCCCCCCH
23749302
20AcetylationEEGPAPCKQMKLEAA
CCCCCCHHHCEEEEC
23749302
39PhosphorylationALNFDSPSSLFESLI
CCCCCCHHHHHHHHH
27251275
40PhosphorylationLNFDSPSSLFESLIS
CCCCCHHHHHHHHHC
27251275
44PhosphorylationSPSSLFESLISPIKT
CHHHHHHHHHCCCCC
26434776
47PhosphorylationSLFESLISPIKTETF
HHHHHHHCCCCCHHH
29496963
50SumoylationESLISPIKTETFFKE
HHHHCCCCCHHHHHH
-
51PhosphorylationSLISPIKTETFFKEF
HHHCCCCCHHHHHHH
26434776
53PhosphorylationISPIKTETFFKEFWE
HCCCCCHHHHHHHHH
26434776
56UbiquitinationIKTETFFKEFWEQKP
CCCHHHHHHHHHHCC
-
62UbiquitinationFKEFWEQKPLLIQRD
HHHHHHHCCEEEECC
-
76PhosphorylationDDPALATYYGSLFKL
CCHHHHHHHHHHHHH
22817900
77PhosphorylationDPALATYYGSLFKLT
CHHHHHHHHHHHHHH
22817900
77 (in isoform 3)Ubiquitination-21906983
79PhosphorylationALATYYGSLFKLTDL
HHHHHHHHHHHHHCH
24719451
82UbiquitinationTYYGSLFKLTDLKSL
HHHHHHHHHHCHHHH
-
82MethylationTYYGSLFKLTDLKSL
HHHHHHHHHHCHHHH
115973029
87UbiquitinationLFKLTDLKSLCSRGM
HHHHHCHHHHHHCCC
-
87MethylationLFKLTDLKSLCSRGM
HHHHHCHHHHHHCCC
30785459
87AcetylationLFKLTDLKSLCSRGM
HHHHHCHHHHHHCCC
25953088
95PhosphorylationSLCSRGMYYGRDVNV
HHHHCCCCCCCCCCE
22817900
102 (in isoform 3)Ubiquitination-21906983
118UbiquitinationKVLNKDGKAHFLQLR
EEECCCCCEEEEEEH
-
144UbiquitinationFHQPQRFKDELWRIQ
ECCCHHHHHHHHHHH
-
185 (in isoform 3)Ubiquitination-21906983
188 (in isoform 3)Ubiquitination-21906983
210PhosphorylationVPLAREYSVEAEERI
CCCCCCCCHHHHHHH
24719451
238 (in isoform 2)Phosphorylation-22210691
244 (in isoform 2)Phosphorylation-22210691
257 (in isoform 2)Phosphorylation-22210691
299 (in isoform 4)Phosphorylation-25690035
300 (in isoform 4)Phosphorylation-25690035
300PhosphorylationQLLLQVESTTVATRR
HHEEEEEECHHHHHH
26434776
301 (in isoform 4)Phosphorylation-25690035
301PhosphorylationLLLQVESTTVATRRL
HEEEEEECHHHHHHH
26434776
302PhosphorylationLLQVESTTVATRRLS
EEEEEECHHHHHHHH
26434776
309PhosphorylationTVATRRLSGFLRTLA
HHHHHHHHHHHHHHH
19502796
318MethylationFLRTLADRLEGTKEL
HHHHHHHHHHHHHHH
115483291
323UbiquitinationADRLEGTKELLSSDM
HHHHHHHHHHHCCHH
-
327O-linked_GlycosylationEGTKELLSSDMKKDF
HHHHHHHCCHHCHHC
30379171
327PhosphorylationEGTKELLSSDMKKDF
HHHHHHHCCHHCHHC
20068231
328PhosphorylationGTKELLSSDMKKDFI
HHHHHHCCHHCHHCH
20068231
331UbiquitinationELLSSDMKKDFIMHR
HHHCCHHCHHCHHHC
21906983
331 (in isoform 1)Ubiquitination-21906983
332UbiquitinationLLSSDMKKDFIMHRL
HHCCHHCHHCHHHCC
-
332AcetylationLLSSDMKKDFIMHRL
HHCCHHCHHCHHHCC
24889819
342PhosphorylationIMHRLPPYSAGDGAE
HHHCCCCCCCCCCCC
20068231
343PhosphorylationMHRLPPYSAGDGAEL
HHCCCCCCCCCCCCC
20068231
351PhosphorylationAGDGAELSTPGGKLP
CCCCCCCCCCCCCCC
20068231
352PhosphorylationGDGAELSTPGGKLPR
CCCCCCCCCCCCCCC
20068231
356 (in isoform 1)Ubiquitination-21906983
356UbiquitinationELSTPGGKLPRLDSV
CCCCCCCCCCCCCCE
21906983
356AcetylationELSTPGGKLPRLDSV
CCCCCCCCCCCCCCE
23749302
369UbiquitinationSVVRLQFKDHIVLTV
CEEEEEECCEEEEEE
-
428UbiquitinationLSHLDALKQIWNSPA
HHHHHHHHHHHCCCC
-
439 (in isoform 1)Ubiquitination-21906983
439UbiquitinationNSPAISVKDLKLTTD
CCCCCCHHHCCCCCC
21906983
442 (in isoform 1)Ubiquitination-21906983
442UbiquitinationAISVKDLKLTTDEEK
CCCHHHCCCCCCHHH
2190698

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 RIOX2_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RIOX2_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 RIOX2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RIOX2_HUMANMINAphysical
16189514
A4_HUMANAPPphysical
21832049
NAA16_HUMANNAA16physical
22939629
TXNL1_HUMANTXNL1physical
22939629
RIOX2_HUMANMINAphysical
25416956
EXOC7_HUMANEXOC7physical
26344197

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RIOX2_HUMAN

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Related Literatures of Post-Translational Modification

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