dbPTM

RS6_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RS6_MOUSE
UniProt AC	P62754
Protein Name	40S ribosomal protein S6
Gene Name	Rps6
Organism	Mus musculus (Mouse).
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	Acetylation	------MKLNISFPA ------CCCEEEECC	50.68	22826441
6	Phosphorylation	--MKLNISFPATGCQ --CCCEEEECCCCCC	24.89	29514104
12	S-nitrosocysteine	ISFPATGCQKLIEVD EEECCCCCCEEEEEC	2.54	-
12	S-palmitoylation	ISFPATGCQKLIEVD EEECCCCCCEEEEEC	2.54	28526873
12	S-nitrosylation	ISFPATGCQKLIEVD EEECCCCCCEEEEEC	2.54	22178444
12	Glutathionylation	ISFPATGCQKLIEVD EEECCCCCCEEEEEC	2.54	24333276
14	Ubiquitination	FPATGCQKLIEVDDE ECCCCCCEEEEECCH	56.35	-
14	Acetylation	FPATGCQKLIEVDDE ECCCCCCEEEEECCH	56.35	22826441
30	Acetylation	KLRTFYEKRMATEVA HHHHHHHHHHHHHHH	35.77	22826441
46	Acetylation	DALGEEWKGYVVRIS HHHCCCCCEEEEEEE	43.58	23954790
46	Succinylation	DALGEEWKGYVVRIS HHHCCCCCEEEEEEE	43.58	23954790
53	Phosphorylation	KGYVVRISGGNDKQG CEEEEEEECCCCCCC	30.04	29514104
58	Acetylation	RISGGNDKQGFPMKQ EEECCCCCCCCCCCC	57.21	22826441
58	Ubiquitination	RISGGNDKQGFPMKQ EEECCCCCCCCCCCC	57.21	-
64	Malonylation	DKQGFPMKQGVLTHG CCCCCCCCCCEECHH	44.10	26320211
69	Phosphorylation	PMKQGVLTHGRVRLL CCCCCEECHHHHEEE	21.63	24899341
82	Phosphorylation	LLLSKGHSCYRPRRT EEECCCCCCCCCCCC	22.85	29514104
83	Glutathionylation	LLSKGHSCYRPRRTG EECCCCCCCCCCCCC	2.50	24333276
83	S-nitrosylation	LLSKGHSCYRPRRTG EECCCCCCCCCCCCC	2.50	21278135
83	S-nitrosocysteine	LLSKGHSCYRPRRTG EECCCCCCCCCCCCC	2.50	-
96	Phosphorylation	TGERKRKSVRGCIVD CCCCCCCCCCCEEEC	22.53	26643407
116	Succinylation	LNLVIVKKGEKDIPG EEEEEEECCCCCCCC	62.50	23954790
116	Ubiquitination	LNLVIVKKGEKDIPG EEEEEEECCCCCCCC	62.50	-
119	Acetylation	VIVKKGEKDIPGLTD EEEECCCCCCCCCCC	70.40	23864654
119	Ubiquitination	VIVKKGEKDIPGLTD EEEECCCCCCCCCCC	70.40	-
125	Phosphorylation	EKDIPGLTDTTVPRR CCCCCCCCCCCCCCC	36.90	23984901
127	Phosphorylation	DIPGLTDTTVPRRLG CCCCCCCCCCCCCCC	25.18	23984901
128	Phosphorylation	IPGLTDTTVPRRLGP CCCCCCCCCCCCCCH	31.18	21454597
137	Hydroxylation	PRRLGPKRASRIRKL CCCCCHHHHHHHHHH	40.71	-
143	Ubiquitination	KRASRIRKLFNLSKE HHHHHHHHHHCCCCC	55.87	-
143	Acetylation	KRASRIRKLFNLSKE HHHHHHHHHHCCCCC	55.87	23806337
148	Phosphorylation	IRKLFNLSKEDDVRQ HHHHHCCCCCCCHHH	34.79	26824392
149	Succinylation	RKLFNLSKEDDVRQY HHHHCCCCCCCHHHH	69.22	23954790
149	Ubiquitination	RKLFNLSKEDDVRQY HHHHCCCCCCCHHHH	69.22	-
149	Acetylation	RKLFNLSKEDDVRQY HHHHCCCCCCCHHHH	69.22	23806337
156	Phosphorylation	KEDDVRQYVVRKPLN CCCCHHHHHHCCCCC	7.14	29514104
181	Phosphorylation	PKIQRLVTPRVLQHK CHHHHHCCHHHHHHH	15.23	27149854
203	Succinylation	KQRTKKNKEEAAEYA HHHCCCCHHHHHHHH	66.85	23954790
203	Acetylation	KQRTKKNKEEAAEYA HHHCCCCHHHHHHHH	66.85	23864654
203	Malonylation	KQRTKKNKEEAAEYA HHHCCCCHHHHHHHH	66.85	26320211
203	Ubiquitination	KQRTKKNKEEAAEYA HHHCCCCHHHHHHHH	66.85	-
209	Phosphorylation	NKEEAAEYAKLLAKR CHHHHHHHHHHHHHH	12.33	25367039
211	Malonylation	EEAAEYAKLLAKRMK HHHHHHHHHHHHHHH	43.03	26320211
211	Ubiquitination	EEAAEYAKLLAKRMK HHHHHHHHHHHHHHH	43.03	-
211	Acetylation	EEAAEYAKLLAKRMK HHHHHHHHHHHHHHH	43.03	23806337
235	Phosphorylation	IAKRRRLSSLRASTS HHHHHHHHHHHHHCC	26.05	27087446
236	Phosphorylation	AKRRRLSSLRASTSK HHHHHHHHHHHHCCC	26.85	18388127
240	Phosphorylation	RLSSLRASTSKSESS HHHHHHHHCCCCHHC	27.12	18388127
241	Phosphorylation	LSSLRASTSKSESSQ HHHHHHHCCCCHHCC	38.91	27742792
242	Phosphorylation	SSLRASTSKSESSQK HHHHHHCCCCHHCCC	31.52	27742792
244	Phosphorylation	LRASTSKSESSQK-- HHHHCCCCHHCCC--	42.34	27087446
246	Phosphorylation	ASTSKSESSQK---- HHCCCCHHCCC----	45.20	22942356
247	Phosphorylation	STSKSESSQK----- HCCCCHHCCC-----	37.63	27087446

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	DAPK1	Q80YE7	Uniprot
235	S	Phosphorylation	Kinase	RPS6KA1	P18653	Uniprot
235	S	Phosphorylation	Kinase	RPS6KA3	P18654	Uniprot
235	S	Phosphorylation	Kinase	RPS6KB1	Q8BSK8	GPS
235	S	Phosphorylation	Kinase	RPS6KB2	Q9Z1M4	GPS
235	S	Phosphorylation	Kinase	PASK	Q8CEE6	Uniprot
236	S	Phosphorylation	Kinase	AKT1	P31750	PSP
236	S	Phosphorylation	Kinase	DAPK1	Q80YE7	Uniprot
236	S	Phosphorylation	Kinase	RPS6KA1	P18653	Uniprot
236	S	Phosphorylation	Kinase	RPS6KA3	P18654	Uniprot
236	S	Phosphorylation	Kinase	RPS6KB1	Q8BSK8	GPS
236	S	Phosphorylation	Kinase	RPS6KB2	Q9Z1M4	GPS
236	S	Phosphorylation	Kinase	PASK	Q8CEE6	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
137	R	Hydroxylation	-
Specifically hydroxylated (with R stereochemistry) at C-3 of Arg-137 by KDM8.
235	S	Phosphorylation	1939282
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	1939282
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_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of RS6_MOUSE !!

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of RS6_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Large-scale phosphorylation analysis of mouse liver."; Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-235; SER-236; SER-244;SER-246 AND SER-247, AND MASS SPECTROMETRY.	17242355 [Abstract]
"Identification of 40 S ribosomal protein S6 phosphorylation sites inSwiss mouse 3T3 fibroblasts stimulated with serum."; Bandi H.R., Ferrari S., Krieg J., Meyer H.E., Thomas G.; J. Biol. Chem. 268:4530-4533(1993). Cited for: PARTIAL PROTEIN SEQUENCE, AND PHOSPHORYLATION AT SER-235; SER-240;SER-244 AND SER-247.	8440735 [Abstract]
"Mitogen-activated 70K S6 kinase. Identification of in vitro 40 Sribosomal S6 phosphorylation sites."; Ferrari S., Bandi H.R., Hofsteenge J., Bussian B.M., Thomas G.; J. Biol. Chem. 266:22770-22775(1991). Cited for: PARTIAL PROTEIN SEQUENCE, AND PHOSPHORYLATION AT SER-235; SER-236;SER-240 AND SER-244.	1939282 [Abstract]

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