RIOK3_HUMAN - dbPTM
RIOK3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RIOK3_HUMAN
UniProt AC O14730
Protein Name Serine/threonine-protein kinase RIO3
Gene Name RIOK3
Organism Homo sapiens (Human).
Sequence Length 519
Subcellular Localization Cytoplasm .
Protein Description Involved in regulation of type I interferon (IFN)-dependent immune response which plays a critical role in the innate immune response against DNA and RNA viruses. May act as an adapter protein essential for the recruitment of TBK1 to IRF3. [PubMed: 24807708 Phosphorylates IFIH1 on 'Ser-828' interfering with IFIH1 filament assembly on long dsRNA and resulting in attenuated IFIH1-signaling]
Protein Sequence MDLVGVASPEPGTAAAWGPSKCPWAIPQNTISCSLADVMSEQLAKELQLEEEAAVFPEVAVAEGPFITGENIDTSSDLMLAQMLQMEYDREYDAQLRREEKKFNGDSKVSISFENYRKVHPYEDSDSSEDEVDWQDTRDDPYRPAKPVPTPKKGFIGKGKDITTKHDEVVCGRKNTARMENFAPEFQVGDGIGMDLKLSNHVFNALKQHAYSEERRSARLHEKKEHSTAEKAVDPKTRLLMYKMVNSGMLETITGCISTGKESVVFHAYGGSMEDEKEDSKVIPTECAIKVFKTTLNEFKNRDKYIKDDFRFKDRFSKLNPRKIIRMWAEKEMHNLARMQRAGIPCPTVVLLKKHILVMSFIGHDQVPAPKLKEVKLNSEEMKEAYYQTLHLMRQLYHECTLVHADLSEYNMLWHAGKVWLIDVSQSVEPTHPHGLEFLFRDCRNVSQFFQKGGVKEALSERELFNAVSGLNITADNEADFLAEIEALEKMNEDHVQKNGRKAASFLKDDGDPPLLYDE
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
8PhosphorylationMDLVGVASPEPGTAA
CCCCCCCCCCCCCCC		27.6523401153
13PhosphorylationVASPEPGTAAAWGPS
CCCCCCCCCCCCCCC		24.6822199227
20PhosphorylationTAAAWGPSKCPWAIP
CCCCCCCCCCCCCCC		42.8422199227
21UbiquitinationAAAWGPSKCPWAIPQ
CCCCCCCCCCCCCCC		47.66-
101UbiquitinationAQLRREEKKFNGDSK
HHHHHHHHHHCCCCC		58.89-
102UbiquitinationQLRREEKKFNGDSKV
HHHHHHHHHCCCCCE		47.55-
107PhosphorylationEKKFNGDSKVSISFE
HHHHCCCCCEEEEEE		36.0329759185
108UbiquitinationKKFNGDSKVSISFEN
HHHCCCCCEEEEEEC		44.7521890473
108 (in isoform 2)Ubiquitination-44.7521890473
108 (in isoform 1)Ubiquitination-44.7521890473
110PhosphorylationFNGDSKVSISFENYR
HCCCCCEEEEEECCE		19.0922210691
112PhosphorylationGDSKVSISFENYRKV
CCCCEEEEEECCEEE		20.9925159151
116PhosphorylationVSISFENYRKVHPYE
EEEEEECCEEECCCC		12.4725159151
122PhosphorylationNYRKVHPYEDSDSSE
CCEEECCCCCCCCCC		19.9323927012
125PhosphorylationKVHPYEDSDSSEDEV
EECCCCCCCCCCCCC		27.7023927012
127PhosphorylationHPYEDSDSSEDEVDW
CCCCCCCCCCCCCCC		39.3123927012
128PhosphorylationPYEDSDSSEDEVDWQ
CCCCCCCCCCCCCCC		54.8023927012
142PhosphorylationQDTRDDPYRPAKPVP
CCCCCCCCCCCCCCC		35.9028064214
146 (in isoform 1)Ubiquitination-49.5921890473
146 (in isoform 2)Ubiquitination-49.5921890473
146UbiquitinationDDPYRPAKPVPTPKK
CCCCCCCCCCCCCCC		49.5921906983
150PhosphorylationRPAKPVPTPKKGFIG
CCCCCCCCCCCCCCC		48.2330576142
152UbiquitinationAKPVPTPKKGFIGKG
CCCCCCCCCCCCCCC		68.92-
158UbiquitinationPKKGFIGKGKDITTK
CCCCCCCCCCCCCCC		58.95-
160UbiquitinationKGFIGKGKDITTKHD
CCCCCCCCCCCCCCC		49.82-
165UbiquitinationKGKDITTKHDEVVCG
CCCCCCCCCCEEECC		40.17-
197UbiquitinationDGIGMDLKLSNHVFN
CCCCCCHHHHHHHHH		45.68-
207 (in isoform 1)Ubiquitination-37.3121890473
207UbiquitinationNHVFNALKQHAYSEE
HHHHHHHHHHCCCHH		37.3121890473
207 (in isoform 2)Ubiquitination-37.3121890473
212PhosphorylationALKQHAYSEERRSAR
HHHHHCCCHHHHHHH		33.4928348404
217PhosphorylationAYSEERRSARLHEKK
CCCHHHHHHHHHHHH		24.7827282143
231UbiquitinationKEHSTAEKAVDPKTR
HCCCCHHHHCCHHHH		51.77-
236UbiquitinationAEKAVDPKTRLLMYK
HHHHCCHHHHHHHHH		41.64-
247PhosphorylationLMYKMVNSGMLETIT
HHHHHHHCCCHHHHH		17.7323532336
281UbiquitinationEDEKEDSKVIPTECA
CCCCCCCCCCCHHHH		57.41-
290 (in isoform 2)Ubiquitination-24.0821890473
290UbiquitinationIPTECAIKVFKTTLN
CCHHHHHHHHHHHHH		24.0821890473
290 (in isoform 1)Ubiquitination-24.0821890473
293UbiquitinationECAIKVFKTTLNEFK
HHHHHHHHHHHHHHH		43.52-
294PhosphorylationCAIKVFKTTLNEFKN
HHHHHHHHHHHHHHC		25.6730622161
295PhosphorylationAIKVFKTTLNEFKNR
HHHHHHHHHHHHHCC		28.3330622161
300 (in isoform 2)Ubiquitination-44.9121890473
300 (in isoform 1)Ubiquitination-44.9121890473
300UbiquitinationKTTLNEFKNRDKYIK
HHHHHHHHCCCCCCC		44.9121890473
304UbiquitinationNEFKNRDKYIKDDFR
HHHHCCCCCCCCCCC		45.71-
307UbiquitinationKNRDKYIKDDFRFKD
HCCCCCCCCCCCCHH		48.43-
318 (in isoform 2)Ubiquitination-49.9621890473
318 (in isoform 1)Ubiquitination-49.9621890473
318UbiquitinationRFKDRFSKLNPRKII
CCHHHHHHCCHHHHH		49.9621890473
348PhosphorylationRAGIPCPTVVLLKKH
HCCCCCCHHHHCCCC		29.9323403867
376UbiquitinationAPKLKEVKLNSEEMK
CCCCCEECCCHHHHH		42.94-
452 (in isoform 1)Ubiquitination-53.1021890473
452UbiquitinationNVSQFFQKGGVKEAL
CHHHHHHCCCHHHHH		53.1021890473
456 (in isoform 1)Ubiquitination-40.3121890473
456UbiquitinationFFQKGGVKEALSERE
HHHCCCHHHHHCHHH		40.3121890473
502UbiquitinationHVQKNGRKAASFLKD
HHHHHCHHHHHHHCC		50.10-
505PhosphorylationKNGRKAASFLKDDGD
HHCHHHHHHHCCCCC		35.6530576142
505 (in isoform 2)Ubiquitination-35.6521890473
508 (in isoform 1)Ubiquitination-52.3321890473
508UbiquitinationRKAASFLKDDGDPPL
HHHHHHHCCCCCCCC		52.332190698
517PhosphorylationDGDPPLLYDE-----
CCCCCCCCCC-----		26.2118083107
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
-KUbiquitinationE3 ubiquitin ligaseSMURF1Q9HCE7
PMID:20804422
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RIOK3_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 RIOK3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RUVB2_HUMANRUVBL2physical
17353931
SSRD_HUMANSSR4physical
17353931
FBRL_HUMANFBLphysical
17353931
PSB1_HUMANPSMB1physical
17353931
PRS6B_HUMANPSMC4physical
17353931
MAGA6_HUMANMAGEA6physical
17353931
SPT6H_HUMANSUPT6Hphysical
26496610
ZMAT3_HUMANZMAT3physical
26496610
OSBL5_HUMANOSBPL5physical
26496610
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RIOK3_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-122; SER-127 ANDSER-128, AND MASS SPECTROMETRY.

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