dbPTM

RS6_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RS6_HUMAN
UniProt AC	P62753
Protein Name	40S ribosomal protein S6
Gene Name	RPS6
Organism	Homo sapiens (Human).
Sequence Length	249
Subcellular Localization
Protein Description	May play an important role in controlling cell growth and proliferation through the selective translation of particular classes of mRNA..
Protein Sequence	MKLNISFPATGCQKLIEVDDERKLRTFYEKRMATEVAADALGEEWKGYVVRISGGNDKQGFPMKQGVLTHGRVRLLLSKGHSCYRPRRTGERKRKSVRGCIVDANLSVLNLVIVKKGEKDIPGLTDTTVPRRLGPKRASRIRKLFNLSKEDDVRQYVVRKPLNKEGKKPRTKAPKIQRLVTPRVLQHKRRRIALKKQRTKKNKEEAAEYAKLLAKRMKEAKEKRQEQIAKRRRLSSLRASTSKSESSQK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Methylation	------MKLNISFPA ------CCCEEEECC	50.68	115977441
6	Phosphorylation	--MKLNISFPATGCQ --CCCEEEECCCCCC	24.89	25159151
10	Phosphorylation	LNISFPATGCQKLIE CEEEECCCCCCEEEE	38.43	20068231
12	S-nitrosocysteine	ISFPATGCQKLIEVD EEECCCCCCEEEEEC	2.54	-
12	Glutathionylation	ISFPATGCQKLIEVD EEECCCCCCEEEEEC	2.54	22555962
12	S-nitrosylation	ISFPATGCQKLIEVD EEECCCCCCEEEEEC	2.54	19483679
14	Ubiquitination	FPATGCQKLIEVDDE ECCCCCCEEEEECCH	56.35	21890473
14	Acetylation	FPATGCQKLIEVDDE ECCCCCCEEEEECCH	56.35	23954790
14	2-Hydroxyisobutyrylation	FPATGCQKLIEVDDE ECCCCCCEEEEECCH	56.35	-
14	Sumoylation	FPATGCQKLIEVDDE ECCCCCCEEEEECCH	56.35	28112733
22	Methylation	LIEVDDERKLRTFYE EEEECCHHHHHHHHH	50.75	115493079
23	Ubiquitination	IEVDDERKLRTFYEK EEECCHHHHHHHHHH	40.03	-
28	Phosphorylation	ERKLRTFYEKRMATE HHHHHHHHHHHHHHH	21.67	-
30	Ubiquitination	KLRTFYEKRMATEVA HHHHHHHHHHHHHHH	35.77	-
30	Succinylation	KLRTFYEKRMATEVA HHHHHHHHHHHHHHH	35.77	23954790
30	Acetylation	KLRTFYEKRMATEVA HHHHHHHHHHHHHHH	35.77	26051181
32	Sulfoxidation	RTFYEKRMATEVAAD HHHHHHHHHHHHHHH	8.84	30846556
34	Phosphorylation	FYEKRMATEVAADAL HHHHHHHHHHHHHHH	22.96	29514088
46	Acetylation	DALGEEWKGYVVRIS HHHCCCCCEEEEEEE	43.58	26051181
46	Ubiquitination	DALGEEWKGYVVRIS HHHCCCCCEEEEEEE	43.58	-
53	Phosphorylation	KGYVVRISGGNDKQG CEEEEEEECCCCCCC	30.04	25159151
58	Acetylation	RISGGNDKQGFPMKQ EEECCCCCCCCCCCC	57.21	25953088
58	Ubiquitination	RISGGNDKQGFPMKQ EEECCCCCCCCCCCC	57.21	21890473
64	Ubiquitination	DKQGFPMKQGVLTHG CCCCCCCCCCEECHH	44.10	21890473
64	Acetylation	DKQGFPMKQGVLTHG CCCCCCCCCCEECHH	44.10	25953088
69	Phosphorylation	PMKQGVLTHGRVRLL CCCCCEECHHHHEEE	21.63	26437602
78	Phosphorylation	GRVRLLLSKGHSCYR HHHEEEECCCCCCCC	36.24	22817900
79	Ubiquitination	RVRLLLSKGHSCYRP HHEEEECCCCCCCCC	61.69	-
79	Acetylation	RVRLLLSKGHSCYRP HHEEEECCCCCCCCC	61.69	23749302
82	Phosphorylation	LLLSKGHSCYRPRRT EEECCCCCCCCCCCC	22.85	28152594
84	Phosphorylation	LSKGHSCYRPRRTGE ECCCCCCCCCCCCCC	27.02	28152594
107	Phosphorylation	CIVDANLSVLNLVIV EEECCCCEEEEEEEE	25.11	28122231
116	Malonylation	LNLVIVKKGEKDIPG EEEEEEECCCCCCCC	62.50	26320211
116	Acetylation	LNLVIVKKGEKDIPG EEEEEEECCCCCCCC	62.50	23236377
116	Ubiquitination	LNLVIVKKGEKDIPG EEEEEEECCCCCCCC	62.50	21890473
119	Acetylation	VIVKKGEKDIPGLTD EEEECCCCCCCCCCC	70.40	25953088
119	Ubiquitination	VIVKKGEKDIPGLTD EEEECCCCCCCCCCC	70.40	-
119	2-Hydroxyisobutyrylation	VIVKKGEKDIPGLTD EEEECCCCCCCCCCC	70.40	-
127	Phosphorylation	DIPGLTDTTVPRRLG CCCCCCCCCCCCCCC	25.18	23186163
128	Phosphorylation	IPGLTDTTVPRRLGP CCCCCCCCCCCCCCH	31.18	21815630
137	Hydroxylation	PRRLGPKRASRIRKL CCCCCHHHHHHHHHH	40.71	29563586
143	Ubiquitination	KRASRIRKLFNLSKE HHHHHHHHHHCCCCC	55.87	21890473
143	Acetylation	KRASRIRKLFNLSKE HHHHHHHHHHCCCCC	55.87	26051181
148	Phosphorylation	IRKLFNLSKEDDVRQ HHHHHCCCCCCCHHH	34.79	30266825
149	Ubiquitination	RKLFNLSKEDDVRQY HHHHCCCCCCCHHHH	69.22	21890473
149	Acetylation	RKLFNLSKEDDVRQY HHHHCCCCCCCHHHH	69.22	23236377
149	2-Hydroxyisobutyrylation	RKLFNLSKEDDVRQY HHHHCCCCCCCHHHH	69.22	-
154	Methylation	LSKEDDVRQYVVRKP CCCCCCHHHHHHCCC	29.16	115493069
156	Phosphorylation	KEDDVRQYVVRKPLN CCCCHHHHHHCCCCC	7.14	23312004
160	Ubiquitination	VRQYVVRKPLNKEGK HHHHHHCCCCCCCCC	42.10	-
164	2-Hydroxyisobutyrylation	VVRKPLNKEGKKPRT HHCCCCCCCCCCCCC	75.44	-
181	Phosphorylation	PKIQRLVTPRVLQHK CHHHHHCCHHHHHHH	15.23	23312004
188	Ubiquitination	TPRVLQHKRRRIALK CHHHHHHHHHHHHHH	34.34	-
195	Acetylation	KRRRIALKKQRTKKN HHHHHHHHHHHCCCC	37.53	26051181
203	Ubiquitination	KQRTKKNKEEAAEYA HHHCCCCHHHHHHHH	66.85	21890473
203	Acetylation	KQRTKKNKEEAAEYA HHHCCCCHHHHHHHH	66.85	26051181
209	Phosphorylation	NKEEAAEYAKLLAKR CHHHHHHHHHHHHHH	12.33	28152594
211	Malonylation	EEAAEYAKLLAKRMK HHHHHHHHHHHHHHH	43.03	26320211
211	Acetylation	EEAAEYAKLLAKRMK HHHHHHHHHHHHHHH	43.03	19608861
211	Ubiquitination	EEAAEYAKLLAKRMK HHHHHHHHHHHHHHH	43.03	21890473
218	Acetylation	KLLAKRMKEAKEKRQ HHHHHHHHHHHHHHH	59.56	11921179
230	Acetylation	KRQEQIAKRRRLSSL HHHHHHHHHHHHHHH	48.33	25953088
235	Phosphorylation	IAKRRRLSSLRASTS HHHHHHHHHHHHHCC	26.05	22039466
236	Phosphorylation	AKRRRLSSLRASTSK HHHHHHHHHHHHCCC	26.85	22039466
240	Phosphorylation	RLSSLRASTSKSESS HHHHHHHHCCCCHHC	27.12	22322096
241	Phosphorylation	LSSLRASTSKSESSQ HHHHHHHCCCCHHCC	38.91	22322096
242	Phosphorylation	SSLRASTSKSESSQK HHHHHHCCCCHHCCC	31.52	22322096
243	Sumoylation	SLRASTSKSESSQK- HHHHHCCCCHHCCC-	59.33	-
244	Phosphorylation	LRASTSKSESSQK-- HHHHCCCCHHCCC--	42.34	22322096
246	Phosphorylation	ASTSKSESSQK---- HHCCCCHHCCC----	45.20	22322096
247	Phosphorylation	STSKSESSQK----- HCCCCHHCCC-----	37.63	21418524

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
235	S	Phosphorylation	Kinase	RSK2	P51812	PSP
235	S	Phosphorylation	Kinase	MTOR	P42345	PSP
235	S	Phosphorylation	Kinase	PASK	Q96RG2	Uniprot
235	S	Phosphorylation	Kinase	P70-SUBFAMILY	-	GPS
235	S	Phosphorylation	Kinase	RPS6KB1	P23443	GPS
235	S	Phosphorylation	Kinase	RSK-SUBFAMILY	-	GPS
235	S	Phosphorylation	Kinase	P70S6K_GROUP	-	PhosphoELM
235	S	Phosphorylation	Kinase	P90RSK	Q15418	PSP
235	S	Phosphorylation	Kinase	RSK_GROUP	-	PhosphoELM
235	S	Phosphorylation	Kinase	PRKCD	Q05655	GPS
235	S	Phosphorylation	Kinase	DAPK1	P53355	Uniprot
236	S	Phosphorylation	Kinase	RSK_GROUP	-	PhosphoELM
236	S	Phosphorylation	Kinase	RSK-SUBFAMILY	-	GPS
236	S	Phosphorylation	Kinase	P70-SUBFAMILY	-	GPS
236	S	Phosphorylation	Kinase	P70S6K_GROUP	-	PhosphoELM
236	S	Phosphorylation	Kinase	PASK	Q96RG2	Uniprot
236	S	Phosphorylation	Kinase	AKT1	P31749	PSP
236	S	Phosphorylation	Kinase	MTOR	P42345	PSP
236	S	Phosphorylation	Kinase	RPS6KB1	P23443	GPS
236	S	Phosphorylation	Kinase	RSK2	P51812	PSP
236	S	Phosphorylation	Kinase	P90RSK	Q15418	PSP
236	S	Phosphorylation	Kinase	PRKCD	Q05655	GPS
236	S	Phosphorylation	Kinase	DAPK1	P53355	Uniprot
240	S	Phosphorylation	Kinase	P70S6K	P67999	PSP
240	S	Phosphorylation	Kinase	RPS6KB1	P23443	GPS
244	S	Phosphorylation	Kinase	P70S6K	P67999	PSP
244	S	Phosphorylation	Kinase	RPS6KB1	P23443	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
137	R	Hydroxylation	29563586
Specifically hydroxylated (with R stereochemistry) at C-3 of Arg-137 by KDM8.
235	S	Phosphorylation	17360704
Phosphorylated at Ser-235 and Ser-236 by RPS6KA1 and RPS6KA3; phosphorylation at these sites facilitates the assembly of the pre-initiation complex.
236	S	Phosphorylation	17360704
Phosphorylated at Ser-235 and Ser-236 by RPS6KA1 and RPS6KA3; phosphorylation at these sites facilitates the assembly of the pre-initiation complex.

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 RS6_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RSSA_HUMAN	RPSA	physical	22939629
RS7_HUMAN	RPS7	physical	22939629
RS8_HUMAN	RPS8	physical	22939629
RS9_HUMAN	RPS9	physical	22939629
VASN_HUMAN	VASN	physical	22939629
VHL_HUMAN	VHL	physical	23612971
EIFCL_HUMAN	EIF3CL	physical	22863883
HNRPU_HUMAN	HNRNPU	physical	22863883
TSR1_HUMAN	TSR1	physical	22863883
IF2P_HUMAN	EIF5B	physical	26344197
RL10_HUMAN	RPL10	physical	26344197
RL10A_HUMAN	RPL10A	physical	26344197
RL12_HUMAN	RPL12	physical	26344197
RL15_HUMAN	RPL15	physical	26344197
RL27A_HUMAN	RPL27A	physical	26344197
RL35_HUMAN	RPL35	physical	26344197
RL37A_HUMAN	RPL37A	physical	26344197
RL3L_HUMAN	RPL3L	physical	26344197
RL9_HUMAN	RPL9	physical	26344197
RLA1_HUMAN	RPLP1	physical	26344197
RLA2_HUMAN	RPLP2	physical	26344197
RS10_HUMAN	RPS10	physical	26344197
RS11_HUMAN	RPS11	physical	26344197
RS3_HUMAN	RPS3	physical	26344197
RS7_HUMAN	RPS7	physical	26344197
RS9_HUMAN	RPS9	physical	26344197
RSSA_HUMAN	RPSA	physical	26344197
RS23_HUMAN	RPS23	physical	27022092
RL4_HUMAN	RPL4	physical	27022092
RLA0_HUMAN	RPLP0	physical	27022092
G3BP1_HUMAN	G3BP1	physical	27022092
G3BP2_HUMAN	G3BP2	physical	27022092
CAPR1_HUMAN	CAPRIN1	physical	27022092
UBP10_HUMAN	USP10	physical	27022092
RL7A_HUMAN	RPL7A	physical	27022092
EIF3B_HUMAN	EIF3B	physical	27022092

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 RS6_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-30 AND LYS-211, AND MASSSPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"Substrate preference and phosphatidylinositol monophosphateinhibition of the catalytic domain of the Per-Arnt-Sim domain kinasePASKIN."; Schlafli P., Troger J., Eckhardt K., Borter E., Spielmann P.,Wenger R.H.; FEBS J. 278:1757-1768(2011). Cited for: PHOSPHORYLATION AT SER-235 AND SER-236, AND MUTAGENESIS OF235-SER-SER-236.	21418524 [Abstract]
"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-235 AND SER-240, ANDMASS SPECTROMETRY.	19369195 [Abstract]
"Peptide combinatorial libraries identify TSC2 as a death-associatedprotein kinase (DAPK) death domain-binding protein and reveal astimulatory role for DAPK in mTORC1 signaling."; Stevens C., Lin Y., Harrison B., Burch L., Ridgway R.A., Sansom O.,Hupp T.; J. Biol. Chem. 284:334-344(2009). Cited for: PHOSPHORYLATION AT SER-235 AND SER-236 BY DAPK1.	18974095 [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-148; SER-235; SER-236;SER-240; SER-244 AND SER-247, AND MASS SPECTROMETRY.	18669648 [Abstract]
"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-240, AND MASSSPECTROMETRY.	18691976 [Abstract]
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column."; Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.; Anal. Sci. 24:161-166(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-236, AND MASSSPECTROMETRY.	18187866 [Abstract]
"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-240, AND MASSSPECTROMETRY.	19007248 [Abstract]
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry."; Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.; Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-78; SER-235; SER-236;SER-240 AND SER-244, AND MASS SPECTROMETRY.	17287340 [Abstract]
"RAS/ERK signaling promotes site-specific ribosomal protein S6phosphorylation via RSK and stimulates cap-dependent translation."; Roux P.P., Shahbazian D., Vu H., Holz M.K., Cohen M.S., Taunton J.,Sonenberg N., Blenis J.; J. Biol. Chem. 282:14056-14064(2007). Cited for: PHOSPHORYLATION AT SER-235 AND SER-236.	17360704 [Abstract]
"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-235; SER-236 ANDSER-240, AND MASS SPECTROMETRY.	17081983 [Abstract]
"Global phosphoproteome of HT-29 human colon adenocarcinoma cells."; Kim J.-E., Tannenbaum S.R., White F.M.; J. Proteome Res. 4:1339-1346(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-235 AND SER-236, ANDMASS SPECTROMETRY.	16083285 [Abstract]

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