RIOK2_HUMAN - dbPTM
RIOK2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RIOK2_HUMAN
UniProt AC Q9BVS4
Protein Name Serine/threonine-protein kinase RIO2
Gene Name RIOK2 {ECO:0000312|HGNC:HGNC:18999}
Organism Homo sapiens (Human).
Sequence Length 552
Subcellular Localization Cytoplasm . Exported out of the nucleus via its NES in a XPO1-dependent manner.
Protein Description Serine/threonine-protein kinase involved in the final steps of cytoplasmic maturation of the 40S ribosomal subunit. Involved in export of the 40S pre-ribosome particles (pre-40S) from the nucleus to the cytoplasm. Its kinase activity is required for the release of NOB1, PNO1 and LTV1 from the late pre-40S and the processing of 18S-E pre-rRNA to the mature 18S rRNA. [PubMed: 19564402 Regulates the timing of the metaphase-anaphase transition during mitotic progression, and its phosphorylation, most likely by PLK1, regulates this function]
Protein Sequence MGKVNVAKLRYMSRDDFRVLTAVEMGMKNHEIVPGSLIASIASLKHGGCNKVLRELVKHKLIAWERTKTVQGYRLTNAGYDYLALKTLSSRQVVESVGNQMGVGKESDIYIVANEEGQQFALKLHRLGRTSFRNLKNKRDYHKHRHNVSWLYLSRLSAMKEFAYMKALYERKFPVPKPIDYNRHAVVMELINGYPLCQIHHVEDPASVYDEAMELIVKLANHGLIHGDFNEFNLILDESDHITMIDFPQMVSTSHPNAEWYFDRDVKCIKDFFMKRFSYESELFPTFKDIRREDTLDVEVSASGYTKEMQADDELLHPLGPDDKNIETKEGSEFSFSDGEVAEKAEVYGSENESERNCLEESEGCYCRSSGDPEQIKEDSLSEESADARSFEMTEFNQALEEIKGQVVENNSVTEFSEEKNRTENYNRQDGQRVQGGVPAGSDEYEDECPHLIALSSLNREFRPFRDEENVGAMNQYRTRTLSITSSGSAVSCSTIPPELVKQKVKRQLTKQQKSAVRRRLQKGEANIFTKQRRENMQNIKSSLEAASFWGE
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
3Ubiquitination-----MGKVNVAKLR
-----CCCCCHHHCE		29.3624816145
8UbiquitinationMGKVNVAKLRYMSRD
CCCCCHHHCEECCHH		29.2529967540
21PhosphorylationRDDFRVLTAVEMGMK
HHHHHHHHHHHHCCC		26.29-
36PhosphorylationNHEIVPGSLIASIAS
CCCCCCHHHHHHHHH		15.5520873877
40PhosphorylationVPGSLIASIASLKHG
CCHHHHHHHHHCCCC		16.2220873877
43PhosphorylationSLIASIASLKHGGCN
HHHHHHHHCCCCCHH		35.9620873877
45UbiquitinationIASIASLKHGGCNKV
HHHHHHCCCCCHHHH		37.3932015554
51UbiquitinationLKHGGCNKVLRELVK
CCCCCHHHHHHHHHH		46.8829967540
68UbiquitinationLIAWERTKTVQGYRL
CCEEECCCCCCCEEE		53.5824816145
86UbiquitinationGYDYLALKTLSSRQV
CCCEEEEECCCCHHH		41.6421963094
101UbiquitinationVESVGNQMGVGKESD
HHHHHHCCCCCCCCC		5.6421963094
130PhosphorylationKLHRLGRTSFRNLKN
HHHHCCCHHHHHCCC		30.34-
131PhosphorylationLHRLGRTSFRNLKNK
HHHCCCHHHHHCCCC		22.35-
141PhosphorylationNLKNKRDYHKHRHNV
HCCCCCHHHHHHCCC		19.4626074081
149PhosphorylationHKHRHNVSWLYLSRL
HHHHCCCHHHHHHHH		19.3828152594
152PhosphorylationRHNVSWLYLSRLSAM
HCCCHHHHHHHHHHH		9.0728152594
154PhosphorylationNVSWLYLSRLSAMKE
CCHHHHHHHHHHHHH		20.0228152594
157PhosphorylationWLYLSRLSAMKEFAY
HHHHHHHHHHHHHHH		25.8028270605
160UbiquitinationLSRLSAMKEFAYMKA
HHHHHHHHHHHHHHH		49.77-
181PhosphorylationPVPKPIDYNRHAVVM
CCCCCCCCCCHHHHH		18.15-
190UbiquitinationRHAVVMELINGYPLC
CHHHHHHHHCCCCCE		1.6722817900
239O-linked_GlycosylationFNLILDESDHITMID
HCEEEECCCCEEEEE		33.8730379171
270UbiquitinationDRDVKCIKDFFMKRF
CCCCHHHHHHHHHHC		58.9329967540
275UbiquitinationCIKDFFMKRFSYESE
HHHHHHHHHCCCHHH		45.17-
288UbiquitinationSELFPTFKDIRREDT
HHCCCCHHHCCCCCC		55.5121906983
324UbiquitinationHPLGPDDKNIETKEG
CCCCCCCCCCCCCCC		68.1724816145
328PhosphorylationPDDKNIETKEGSEFS
CCCCCCCCCCCCEEC		30.5128450419
332PhosphorylationNIETKEGSEFSFSDG
CCCCCCCCEECCCCC		36.2422322096
335PhosphorylationTKEGSEFSFSDGEVA
CCCCCEECCCCCHHH		21.5722322096
337PhosphorylationEGSEFSFSDGEVAEK
CCCEECCCCCHHHHH		43.4319664994
344UbiquitinationSDGEVAEKAEVYGSE
CCCHHHHHEEECCCC		39.8624816145
348PhosphorylationVAEKAEVYGSENESE
HHHHEEECCCCCHHH		13.3622167270
350PhosphorylationEKAEVYGSENESERN
HHEEECCCCCHHHHH		21.4023401153
354PhosphorylationVYGSENESERNCLEE
ECCCCCHHHHHHCHH		54.1322167270
362PhosphorylationERNCLEESEGCYCRS
HHHHCHHHCCCEECC		29.8825159151
366PhosphorylationLEESEGCYCRSSGDP
CHHHCCCEECCCCCH		11.1822322096
369PhosphorylationSEGCYCRSSGDPEQI
HCCCEECCCCCHHHH		34.8023927012
370PhosphorylationEGCYCRSSGDPEQIK
CCCEECCCCCHHHHC		28.0623927012
377UbiquitinationSGDPEQIKEDSLSEE
CCCHHHHCCCCCCHH		55.9822817900
380PhosphorylationPEQIKEDSLSEESAD
HHHHCCCCCCHHHHH		34.5829255136
382PhosphorylationQIKEDSLSEESADAR
HHCCCCCCHHHHHHH		43.1829255136
385PhosphorylationEDSLSEESADARSFE
CCCCCHHHHHHHHHH		27.6529255136
390PhosphorylationEESADARSFEMTEFN
HHHHHHHHHHHHHHH		27.5525159151
394PhosphorylationDARSFEMTEFNQALE
HHHHHHHHHHHHHHH		30.1729116813
412PhosphorylationGQVVENNSVTEFSEE
CCEECCCCCCCCCHH		41.8323401153
414PhosphorylationVVENNSVTEFSEEKN
EECCCCCCCCCHHHC		31.0028450419
417PhosphorylationNNSVTEFSEEKNRTE
CCCCCCCCHHHCCCC		38.3225159151
420UbiquitinationVTEFSEEKNRTENYN
CCCCCHHHCCCCCCC		47.9129967540
426PhosphorylationEKNRTENYNRQDGQR
HHCCCCCCCCCCCCE		12.8926074081
442PhosphorylationQGGVPAGSDEYEDEC
CCCCCCCCCCCCCCC		29.4025159151
445PhosphorylationVPAGSDEYEDECPHL
CCCCCCCCCCCCCHH		33.4021712546
456PhosphorylationCPHLIALSSLNREFR
CCHHHHHHHCCCCCC		24.6125159151
457PhosphorylationPHLIALSSLNREFRP
CHHHHHHHCCCCCCC		30.4325159151
481PhosphorylationMNQYRTRTLSITSSG
CCCEEEEEEEEECCC		25.0130108239
483PhosphorylationQYRTRTLSITSSGSA
CEEEEEEEEECCCCC		24.1719369195
485PhosphorylationRTRTLSITSSGSAVS
EEEEEEEECCCCCCC		17.2925159151
486PhosphorylationTRTLSITSSGSAVSC
EEEEEEECCCCCCCC		30.9125159151
487PhosphorylationRTLSITSSGSAVSCS
EEEEEECCCCCCCCC		28.2825159151
489PhosphorylationLSITSSGSAVSCSTI
EEEECCCCCCCCCCC		27.6925159151
492PhosphorylationTSSGSAVSCSTIPPE
ECCCCCCCCCCCCHH		11.3217081983
494PhosphorylationSGSAVSCSTIPPELV
CCCCCCCCCCCHHHH		23.1230108239
495PhosphorylationGSAVSCSTIPPELVK
CCCCCCCCCCHHHHH		41.6630108239
510PhosphorylationQKVKRQLTKQQKSAV
HHHHHHCHHHHHHHH		20.61-
511UbiquitinationKVKRQLTKQQKSAVR
HHHHHCHHHHHHHHH		60.3624816145
523UbiquitinationAVRRRLQKGEANIFT
HHHHHHHHHCCCHHH		64.4129967540
531UbiquitinationGEANIFTKQRRENMQ
HCCCHHHHHHHHHHH		30.9324816145
531MethylationGEANIFTKQRRENMQ
HCCCHHHHHHHHHHH		30.93115976705
542PhosphorylationENMQNIKSSLEAASF
HHHHHHHHHHHHHHH		36.0425627689
543PhosphorylationNMQNIKSSLEAASFW
HHHHHHHHHHHHHHH		25.8125159151
548PhosphorylationKSSLEAASFWGE---
HHHHHHHHHHCC---		28.6914702039
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
335SPhosphorylationKinasePLK1P53350
PSP
380SPhosphorylationKinasePLK1P53350
PSP
548SPhosphorylationKinasePLK1P53350
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
335SPhosphorylation

18691976
380SPhosphorylation

18669648
548SPhosphorylation

21880710
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 RIOK2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
TSR1_HUMANTSR1physical
22939629
SMAD3_HUMANSMAD3physical
21988832
FCL_HUMANTSTA3physical
21988832
RPR1A_HUMANRPRD1Aphysical
21988832
VP26A_HUMANVPS26Aphysical
23455922
PARP1_HUMANPARP1physical
23455922
EIF3B_HUMANEIF3Bphysical
23455922
EWS_HUMANEWSR1physical
23455922
ACACA_HUMANACACAphysical
23455922
G3BP1_HUMANG3BP1physical
23455922
EIF3A_HUMANEIF3Aphysical
23455922
HP1B3_HUMANHP1BP3physical
23455922
BEND3_HUMANBEND3physical
23455922
RT27_HUMANMRPS27physical
23455922
VPS35_HUMANVPS35physical
23455922
HECD1_HUMANHECTD1physical
23455922
EIF3L_HUMANEIF3Lphysical
23455922
TSR1_HUMANTSR1physical
26344197
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 RIOK2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-332; SER-335; SER-337;SER-380; SER-382; SER-385 AND SER-390, AND MASS SPECTROMETRY.
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-332; SER-335; SER-337;SER-350; SER-362; SER-369; SER-380; SER-382; SER-385; SER-390;SER-442; TYR-445; THR-481; SER-483; SER-486; SER-487 AND SER-489, ANDMASS SPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-332 AND SER-337, ANDMASS SPECTROMETRY.
"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 SER-332; SER-335; SER-337;SER-350; SER-380; SER-382; SER-385 AND SER-442, AND MASS SPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-332; SER-335; SER-337;SER-350; SER-380; SER-382; SER-385; SER-390; SER-417 AND SER-442, ANDMASS SPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-442, AND MASSSPECTROMETRY.
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-350, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-332; SER-335; SER-337;SER-380; SER-382; SER-385 AND SER-390, AND MASS SPECTROMETRY.

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