dbPTM

RIOK1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RIOK1_HUMAN
UniProt AC	Q9BRS2
Protein Name	Serine/threonine-protein kinase RIO1
Gene Name	RIOK1 {ECO:0000312\|HGNC:HGNC:18656}
Organism	Homo sapiens (Human).
Sequence Length	568
Subcellular Localization	Cytoplasm, cytosol .
Protein Description	Involved in the final steps of cytoplasmic maturation of the 40S ribosomal subunit. Involved in processing of 18S-E pre-rRNA to the mature 18S rRNA. Required for the recycling of NOB1 and PNO1 from the late 40S precursor. [PubMed: 22072790 The association with the very late 40S subunit intermediate may involve a translation-like checkpoint point cycle preceeding the binding to the 60S ribosomal subunit (By similarity Despite the protein kinase domain is proposed to act predominantly as an ATPase (By similarity The catalytic activity regulates its dynamic association with the 40S subunit (By similarity In addition to its role in ribosomal biogenesis acts as an adapter protein by recruiting NCL/nucleolin the to PRMT5 complex for its symmetrical methylation]
Protein Sequence	MDYRRLLMSRVVPGQFDDADSSDSENRDLKTVKEKDDILFEDLQDNVNENGEGEIEDEEEEGYDDDDDDWDWDEGVGKLAKGYVWNGGSNPQANRQTSDSSSAKMSTPADKVLRKFENKINLDKLNVTDSVINKVTEKSRQKEADMYRIKDKADRATVEQVLDPRTRMILFKMLTRGIITEINGCISTGKEANVYHASTANGESRAIKIYKTSILVFKDRDKYVSGEFRFRHGYCKGNPRKMVKTWAEKEMRNLIRLNTAEIPCPEPIMLRSHVLVMSFIGKDDMPAPLLKNVQLSESKARELYLQVIQYMRRMYQDARLVHADLSEFNMLYHGGGVYIIDVSQSVEHDHPHALEFLRKDCANVNDFFMRHSVAVMTVRELFEFVTDPSITHENMDAYLSKAMEIASQRTKEERSSQDHVDEEVFKRAYIPRTLNEVKNYERDMDIIMKLKEEDMAMNAQQDNILYQTVTGLKKDLSGVQKVPALLENQVEERTCSDSEDIGSSECSDTDSEEQGDHARPKKHTTDPDIDKKERKKMVKEAQREKRKNKIPKHVKKRKEKTAKTKKGK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
21	Phosphorylation	GQFDDADSSDSENRD CCCCCCCCCCCCCCC	37.45	29255136
22	Phosphorylation	QFDDADSSDSENRDL CCCCCCCCCCCCCCH	45.78	19664994
24	Phosphorylation	DDADSSDSENRDLKT CCCCCCCCCCCCHHH	38.42	29255136
30	Ubiquitination	DSENRDLKTVKEKDD CCCCCCHHHHHHHCC	56.41	32015554
31	Phosphorylation	SENRDLKTVKEKDDI CCCCCHHHHHHHCCC	44.07	28111955
38	Ubiquitination	TVKEKDDILFEDLQD HHHHHCCCCHHHHHH	7.33	24816145
78	Ubiquitination	DWDEGVGKLAKGYVW CCCCCCHHHCCEEEC	42.75	22817900
81	Ubiquitination	EGVGKLAKGYVWNGG CCCHHHCCEEECCCC	62.30	21890473
81	Ubiquitination	EGVGKLAKGYVWNGG CCCHHHCCEEECCCC	62.30	21890473
83	Phosphorylation	VGKLAKGYVWNGGSN CHHHCCEEECCCCCC	11.11	-
89	Phosphorylation	GYVWNGGSNPQANRQ EEECCCCCCCCCCCC	46.89	25159151
90	Ubiquitination	YVWNGGSNPQANRQT EECCCCCCCCCCCCC	35.66	22817900
93	Ubiquitination	NGGSNPQANRQTSDS CCCCCCCCCCCCCCC	17.90	21890473
95	Methylation	GSNPQANRQTSDSSS CCCCCCCCCCCCCCC	44.14	115491277
97	Phosphorylation	NPQANRQTSDSSSAK CCCCCCCCCCCCCCC	31.12	20363803
98	Phosphorylation	PQANRQTSDSSSAKM CCCCCCCCCCCCCCC	27.44	20363803
100	Phosphorylation	ANRQTSDSSSAKMST CCCCCCCCCCCCCCC	26.42	20363803
101	Phosphorylation	NRQTSDSSSAKMSTP CCCCCCCCCCCCCCH	39.03	20363803
102	Phosphorylation	RQTSDSSSAKMSTPA CCCCCCCCCCCCCHH	35.54	-
104	Ubiquitination	TSDSSSAKMSTPADK CCCCCCCCCCCHHHH	35.02	24816145
106	Phosphorylation	DSSSAKMSTPADKVL CCCCCCCCCHHHHHH	30.45	24719451
107	Phosphorylation	SSSAKMSTPADKVLR CCCCCCCCHHHHHHH	20.99	28985074
111	Acetylation	KMSTPADKVLRKFEN CCCCHHHHHHHHHHH	45.32	25953088
116	Ubiquitination	ADKVLRKFENKINLD HHHHHHHHHHCCCHH	11.48	24816145
124	Ubiquitination	ENKINLDKLNVTDSV HHCCCHHHCCCCHHH	45.16	29967540
128	Phosphorylation	NLDKLNVTDSVINKV CHHHCCCCHHHHHHH	22.83	28555341
130	Phosphorylation	DKLNVTDSVINKVTE HHCCCCHHHHHHHCH	18.61	24961811
134	Ubiquitination	VTDSVINKVTEKSRQ CCHHHHHHHCHHHHH	39.13	32015554
142	Ubiquitination	VTEKSRQKEADMYRI HCHHHHHHHCHHHHC	54.48	24816145
154	Ubiquitination	YRIKDKADRATVEQV HHCCCHHHHHHHHHH	46.63	24816145
166	Phosphorylation	EQVLDPRTRMILFKM HHHCCHHHHHHHHHH	29.94	22210691
175	Phosphorylation	MILFKMLTRGIITEI HHHHHHHHHHHHHEE	24.29	22210691
180	Phosphorylation	MLTRGIITEINGCIS HHHHHHHHEECCCCC	28.97	28122231
187	Phosphorylation	TEINGCISTGKEANV HEECCCCCCCCCEEE	34.87	28122231
188	Phosphorylation	EINGCISTGKEANVY EECCCCCCCCCEEEE	32.15	28122231
195	Phosphorylation	TGKEANVYHASTANG CCCCEEEEEEECCCC	7.47	25072903
198	Phosphorylation	EANVYHASTANGESR CEEEEEEECCCCCCC	18.10	25072903
199	Phosphorylation	ANVYHASTANGESRA EEEEEEECCCCCCCE	25.56	25072903
204	Phosphorylation	ASTANGESRAIKIYK EECCCCCCCEEEEEE	28.54	25072903
218	Ubiquitination	KTSILVFKDRDKYVS EEEEEEECCCCCCCC	44.36	-
223	Phosphorylation	VFKDRDKYVSGEFRF EECCCCCCCCCEEEE	12.25	27642862
225	Phosphorylation	KDRDKYVSGEFRFRH CCCCCCCCCEEEECC	29.52	23186163
245	Phosphorylation	NPRKMVKTWAEKEMR CHHHHHHHHHHHHHH	20.63	29666759
291	Ubiquitination	DMPAPLLKNVQLSES CCCHHHHHHHCCCHH	63.86	24816145
295	Ubiquitination	PLLKNVQLSESKARE HHHHHHCCCHHHHHH	5.51	24816145
299	Ubiquitination	NVQLSESKARELYLQ HHCCCHHHHHHHHHH	47.62	-
327	Ubiquitination	LVHADLSEFNMLYHG HHCCCHHHCCCEEEC	48.62	24816145
334	Ubiquitination	EFNMLYHGGGVYIID HCCCEEECCEEEEEE	22.46	32015554
369	Sulfoxidation	ANVNDFFMRHSVAVM CCCHHHHHHHHHHHH	3.68	21406390
410	Phosphorylation	MEIASQRTKEERSSQ HHHHHHHCHHHHHCC	34.86	23312004
411	Methylation	EIASQRTKEERSSQD HHHHHHCHHHHHCCC	60.82	-
415	Phosphorylation	QRTKEERSSQDHVDE HHCHHHHHCCCCCCH	35.31	30108239
416	Phosphorylation	RTKEERSSQDHVDEE HCHHHHHCCCCCCHH	45.94	30108239
426	Ubiquitination	HVDEEVFKRAYIPRT CCCHHHHHHHHCCCC	41.09	29967540
426	Methylation	HVDEEVFKRAYIPRT CCCHHHHHHHHCCCC	41.09	115976697
428	Ubiquitination	DEEVFKRAYIPRTLN CHHHHHHHHCCCCHH	13.75	24816145
432	Ubiquitination	FKRAYIPRTLNEVKN HHHHHCCCCHHHHHC	42.14	24816145
438	Ubiquitination	PRTLNEVKNYERDMD CCCHHHHHCHHHHHH	47.86	32015554
440	Phosphorylation	TLNEVKNYERDMDII CHHHHHCHHHHHHHH	13.46	-
451	Ubiquitination	MDIIMKLKEEDMAMN HHHHHHHCHHHHHHH	54.24	29967540
464	Ubiquitination	MNAQQDNILYQTVTG HHHHHHCHHHHHHHC	5.22	24816145
466	Phosphorylation	AQQDNILYQTVTGLK HHHHCHHHHHHHCCH	9.80	21945579
468	Phosphorylation	QDNILYQTVTGLKKD HHCHHHHHHHCCHHC	13.38	21945579
470	Phosphorylation	NILYQTVTGLKKDLS CHHHHHHHCCHHCCC	39.94	29978859
473	Ubiquitination	YQTVTGLKKDLSGVQ HHHHHCCHHCCCCCC	45.65	29967540
474	Ubiquitination	QTVTGLKKDLSGVQK HHHHCCHHCCCCCCC	69.79	29967540
481	Ubiquitination	KDLSGVQKVPALLEN HCCCCCCCHHHHHHH	48.02	29967540
494	Phosphorylation	ENQVEERTCSDSEDI HHHCCCCCCCCCCCC	21.46	-
503	Phosphorylation	SDSEDIGSSECSDTD CCCCCCCCCCCCCCC	24.25	24461736
504	Phosphorylation	DSEDIGSSECSDTDS CCCCCCCCCCCCCCC	37.09	24461736
507	Phosphorylation	DIGSSECSDTDSEEQ CCCCCCCCCCCCCCC	39.22	24461736
509	Phosphorylation	GSSECSDTDSEEQGD CCCCCCCCCCCCCCC	25.73	24461736
511	Phosphorylation	SECSDTDSEEQGDHA CCCCCCCCCCCCCCC	45.16	24461736
525	Phosphorylation	ARPKKHTTDPDIDKK CCCCCCCCCCCCCHH	45.30	28985074
532	Ubiquitination	TDPDIDKKERKKMVK CCCCCCHHHHHHHHH	60.03	24816145
536	Ubiquitination	IDKKERKKMVKEAQR CCHHHHHHHHHHHHH	55.96	24816145
539	Ubiquitination	KERKKMVKEAQREKR HHHHHHHHHHHHHHH	43.78	29967540
544	Ubiquitination	MVKEAQREKRKNKIP HHHHHHHHHHHCCCC	45.17	24816145
548	Ubiquitination	AQREKRKNKIPKHVK HHHHHHHCCCCHHHH	52.07	24816145
568	Ubiquitination	TAKTKKGK------- HCCCCCCC-------	67.08	24816145
580	Ubiquitination	------------------- -------------------		24816145

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
410	T	Phosphorylation	Kinase	CSNK2A1	P68400	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of RIOK1_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 RIOK1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
A4_HUMAN	APP	physical	21832049
ANM5_HUMAN	PRMT5	physical	25852190
MEP50_HUMAN	WDR77	physical	25852190
U520_HUMAN	SNRNP200	physical	27173435
SMU1_HUMAN	SMU1	physical	27173435
U5S1_HUMAN	EFTUD2	physical	27173435

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 RIOK1_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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-21 AND SER-22, AND MASSSPECTROMETRY.	19690332 [Abstract]
"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-21 AND SER-22, AND MASSSPECTROMETRY.	19413330 [Abstract]
"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-21; SER-22 AND SER-24,AND MASS SPECTROMETRY.	18669648 [Abstract]