dbPTM

RS3A_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RS3A_HUMAN
UniProt AC	P61247
Protein Name	40S ribosomal protein S3a {ECO:0000255\|HAMAP-Rule:MF_03122}
Gene Name	RPS3A {ECO:0000255\|HAMAP-Rule:MF_03122}
Organism	Homo sapiens (Human).
Sequence Length	264
Subcellular Localization	Cytoplasm . Nucleus . Localized in cytoplasmic mRNP granules containing untranslated mRNAs.
Protein Description	May play a role during erythropoiesis through regulation of transcription factor DDIT3..
Protein Sequence	MAVGKNKRLTKGGKKGAKKKVVDPFSKKDWYDVKAPAMFNIRNIGKTLVTRTQGTKIASDGLKGRVFEVSLADLQNDEVAFRKFKLITEDVQGKNCLTNFHGMDLTRDKMCSMVKKWQTMIEAHVDVKTTDGYLLRLFCVGFTKKRNNQIRKTSYAQHQQVRQIRKKMMEIMTREVQTNDLKEVVNKLIPDSIGKDIEKACQSIYPLHDVFVRKVKMLKKPKFELGKLMELHGEGSSSGKATGDETGAKVERADGYEPPVQESV

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
10	Phosphorylation	VGKNKRLTKGGKKGA CCCCCCCCCCCCCCC	31.51	-
19	Ubiquitination	GGKKGAKKKVVDPFS CCCCCCCCCCCCCCC	50.71	-
20	Ubiquitination	GKKGAKKKVVDPFSK CCCCCCCCCCCCCCC	46.94	-
26	Phosphorylation	KKVVDPFSKKDWYDV CCCCCCCCCCCCCCC	44.15	21815630
27	Methylation	KVVDPFSKKDWYDVK CCCCCCCCCCCCCCC	55.95	19608861
27	Acetylation	KVVDPFSKKDWYDVK CCCCCCCCCCCCCCC	55.95	19608861
27	Ubiquitination	KVVDPFSKKDWYDVK CCCCCCCCCCCCCCC	55.95	19608861
27	2-Hydroxyisobutyrylation	KVVDPFSKKDWYDVK CCCCCCCCCCCCCCC	55.95	-
27	Malonylation	KVVDPFSKKDWYDVK CCCCCCCCCCCCCCC	55.95	26320211
28	Ubiquitination	VVDPFSKKDWYDVKA CCCCCCCCCCCCCCC	52.90	-
28	2-Hydroxyisobutyrylation	VVDPFSKKDWYDVKA CCCCCCCCCCCCCCC	52.90	-
28	Acetylation	VVDPFSKKDWYDVKA CCCCCCCCCCCCCCC	52.90	26051181
31	Phosphorylation	PFSKKDWYDVKAPAM CCCCCCCCCCCCCEE	22.46	-
34	Acetylation	KKDWYDVKAPAMFNI CCCCCCCCCCEEEEE	45.84	19608861
34	Sumoylation	KKDWYDVKAPAMFNI CCCCCCCCCCEEEEE	45.84	-
34	Ubiquitination	KKDWYDVKAPAMFNI CCCCCCCCCCEEEEE	45.84	21890473
34	Sumoylation	KKDWYDVKAPAMFNI CCCCCCCCCCEEEEE	45.84	28112733
34	2-Hydroxyisobutyrylation	KKDWYDVKAPAMFNI CCCCCCCCCCEEEEE	45.84	-
38	Sulfoxidation	YDVKAPAMFNIRNIG CCCCCCEEEEEEECC	2.29	21406390
46	Acetylation	FNIRNIGKTLVTRTQ EEEEECCCEEEEECC	34.58	23749302
46	Ubiquitination	FNIRNIGKTLVTRTQ EEEEECCCEEEEECC	34.58	21906983
52	Phosphorylation	GKTLVTRTQGTKIAS CCEEEEECCCCEECC	23.22	27282143
55	Phosphorylation	LVTRTQGTKIASDGL EEEECCCCEECCCCC	14.95	28857561
56	Acetylation	VTRTQGTKIASDGLK EEECCCCEECCCCCC	43.00	25953088
56	Ubiquitination	VTRTQGTKIASDGLK EEECCCCEECCCCCC	43.00	-
56	Sumoylation	VTRTQGTKIASDGLK EEECCCCEECCCCCC	43.00	-
56	2-Hydroxyisobutyrylation	VTRTQGTKIASDGLK EEECCCCEECCCCCC	43.00	-
56	Malonylation	VTRTQGTKIASDGLK EEECCCCEECCCCCC	43.00	26320211
59	Phosphorylation	TQGTKIASDGLKGRV CCCCEECCCCCCCCE	35.37	26270265
63	Ubiquitination	KIASDGLKGRVFEVS EECCCCCCCCEEEEE	50.64	-
63	2-Hydroxyisobutyrylation	KIASDGLKGRVFEVS EECCCCCCCCEEEEE	50.64	-
63	Succinylation	KIASDGLKGRVFEVS EECCCCCCCCEEEEE	50.64	23954790
83	Ubiquitination	NDEVAFRKFKLITED CCHHHHHHCCEECCC	40.16	-
85	Acetylation	EVAFRKFKLITEDVQ HHHHHHCCEECCCCC	41.85	25953088
85	Ubiquitination	EVAFRKFKLITEDVQ HHHHHHCCEECCCCC	41.85	-
85	2-Hydroxyisobutyrylation	EVAFRKFKLITEDVQ HHHHHHCCEECCCCC	41.85	-
88	Phosphorylation	FRKFKLITEDVQGKN HHHCCEECCCCCCCC	36.25	-
94	Acetylation	ITEDVQGKNCLTNFH ECCCCCCCCCCCCCC	27.65	25953088
94	Ubiquitination	ITEDVQGKNCLTNFH ECCCCCCCCCCCCCC	27.65	21890473
94	2-Hydroxyisobutyrylation	ITEDVQGKNCLTNFH ECCCCCCCCCCCCCC	27.65	-
96	Glutathionylation	EDVQGKNCLTNFHGM CCCCCCCCCCCCCCC	5.89	22555962
103	Sulfoxidation	CLTNFHGMDLTRDKM CCCCCCCCCCCHHHH	2.61	30846556
109	Acetylation	GMDLTRDKMCSMVKK CCCCCHHHHHHHHHH	38.22	23749302
109	Ubiquitination	GMDLTRDKMCSMVKK CCCCCHHHHHHHHHH	38.22	-
109	2-Hydroxyisobutyrylation	GMDLTRDKMCSMVKK CCCCCHHHHHHHHHH	38.22	-
112	Phosphorylation	LTRDKMCSMVKKWQT CCHHHHHHHHHHHHH	24.10	23401153
115	2-Hydroxyisobutyrylation	DKMCSMVKKWQTMIE HHHHHHHHHHHHHHH	39.39	-
115	Acetylation	DKMCSMVKKWQTMIE HHHHHHHHHHHHHHH	39.39	25953088
116	Acetylation	KMCSMVKKWQTMIEA HHHHHHHHHHHHHHH	32.88	26051181
130	Phosphorylation	AHVDVKTTDGYLLRL HCCCEECCCCCHHHH	23.01	28152594
133	Phosphorylation	DVKTTDGYLLRLFCV CEECCCCCHHHHHHE	12.84	28152594
139	S-nitrosocysteine	GYLLRLFCVGFTKKR CCHHHHHHEEEECCC	3.28	-
139	Glutathionylation	GYLLRLFCVGFTKKR CCHHHHHHEEEECCC	3.28	22555962
139	S-nitrosylation	GYLLRLFCVGFTKKR CCHHHHHHEEEECCC	3.28	19483679
139	S-palmitoylation	GYLLRLFCVGFTKKR CCHHHHHHEEEECCC	3.28	29575903
144	Methylation	LFCVGFTKKRNNQIR HHHEEEECCCCCCCC	47.69	19608861
144	Acetylation	LFCVGFTKKRNNQIR HHHEEEECCCCCCCC	47.69	23749302
144	Ubiquitination	LFCVGFTKKRNNQIR HHHEEEECCCCCCCC	47.69	-
144	2-Hydroxyisobutyrylation	LFCVGFTKKRNNQIR HHHEEEECCCCCCCC	47.69	-
144	Malonylation	LFCVGFTKKRNNQIR HHHEEEECCCCCCCC	47.69	26320211
145	Ubiquitination	FCVGFTKKRNNQIRK HHEEEECCCCCCCCC	58.25	-
152	Ubiquitination	KRNNQIRKTSYAQHQ CCCCCCCCCHHHHHH	43.37	21906983
152	2-Hydroxyisobutyrylation	KRNNQIRKTSYAQHQ CCCCCCCCCHHHHHH	43.37	-
153	Phosphorylation	RNNQIRKTSYAQHQQ CCCCCCCCHHHHHHH	19.68	28152594
154	Phosphorylation	NNQIRKTSYAQHQQV CCCCCCCHHHHHHHH	22.85	28152594
155	Phosphorylation	NQIRKTSYAQHQQVR CCCCCCHHHHHHHHH	18.60	28152594
155	Nitration	NQIRKTSYAQHQQVR CCCCCCHHHHHHHHH	18.60	-
155	ADP-ribosylation	NQIRKTSYAQHQQVR CCCCCCHHHHHHHHH	18.60	29954836
166	Ubiquitination	QQVRQIRKKMMEIMT HHHHHHHHHHHHHHH	46.80	-
166	Acetylation	QQVRQIRKKMMEIMT HHHHHHHHHHHHHHH	46.80	25953088
167	Ubiquitination	QVRQIRKKMMEIMTR HHHHHHHHHHHHHHH	33.36	21890473
167	2-Hydroxyisobutyrylation	QVRQIRKKMMEIMTR HHHHHHHHHHHHHHH	33.36	-
168	Sulfoxidation	VRQIRKKMMEIMTRE HHHHHHHHHHHHHHH	3.06	28183972
169	Sulfoxidation	RQIRKKMMEIMTREV HHHHHHHHHHHHHHH	4.30	28183972
173	Phosphorylation	KKMMEIMTREVQTND HHHHHHHHHHHCCCC	29.37	20860994
182	Acetylation	EVQTNDLKEVVNKLI HHCCCCHHHHHHHHC	51.86	25825284
182	Ubiquitination	EVQTNDLKEVVNKLI HHCCCCHHHHHHHHC	51.86	21890473
182	2-Hydroxyisobutyrylation	EVQTNDLKEVVNKLI HHCCCCHHHHHHHHC	51.86	-
187	Ubiquitination	DLKEVVNKLIPDSIG CHHHHHHHHCCHHHC	35.86	21890473
187	Acetylation	DLKEVVNKLIPDSIG CHHHHHHHHCCHHHC	35.86	25953088
187	Succinylation	DLKEVVNKLIPDSIG CHHHHHHHHCCHHHC	35.86	23954790
195	Acetylation	LIPDSIGKDIEKACQ HCCHHHCHHHHHHHH	54.59	23749302
195	Ubiquitination	LIPDSIGKDIEKACQ HCCHHHCHHHHHHHH	54.59	-
195	2-Hydroxyisobutyrylation	LIPDSIGKDIEKACQ HCCHHHCHHHHHHHH	54.59	-
195	Succinylation	LIPDSIGKDIEKACQ HCCHHHCHHHHHHHH	54.59	23954790
199	Ubiquitination	SIGKDIEKACQSIYP HHCHHHHHHHHHHCC	55.59	-
199	2-Hydroxyisobutyrylation	SIGKDIEKACQSIYP HHCHHHHHHHHHHCC	55.59	-
199	Acetylation	SIGKDIEKACQSIYP HHCHHHHHHHHHHCC	55.59	25953088
201	S-nitrosocysteine	GKDIEKACQSIYPLH CHHHHHHHHHHCCHH	4.89	-
201	Glutathionylation	GKDIEKACQSIYPLH CHHHHHHHHHHCCHH	4.89	22555962
201	S-nitrosylation	GKDIEKACQSIYPLH CHHHHHHHHHHCCHH	4.89	22178444
201	S-palmitoylation	GKDIEKACQSIYPLH CHHHHHHHHHHCCHH	4.89	29575903
203	Phosphorylation	DIEKACQSIYPLHDV HHHHHHHHHCCHHHH	24.79	28152594
205	Phosphorylation	EKACQSIYPLHDVFV HHHHHHHCCHHHHHH	12.65	28152594
220	Ubiquitination	RKVKMLKKPKFELGK HHHHCCCCCCCHHHH	49.86	-
222	Acetylation	VKMLKKPKFELGKLM HHCCCCCCCHHHHHE	61.42	25953088
227	Ubiquitination	KPKFELGKLMELHGE CCCCHHHHHEEECCC	58.23	21890473
227	2-Hydroxyisobutyrylation	KPKFELGKLMELHGE CCCCHHHHHEEECCC	58.23	-
227	Acetylation	KPKFELGKLMELHGE CCCCHHHHHEEECCC	58.23	23236377
229	Sulfoxidation	KFELGKLMELHGEGS CCHHHHHEEECCCCC	6.16	30846556
236	Phosphorylation	MELHGEGSSSGKATG EEECCCCCCCCCCCC	19.61	29255136
237	Phosphorylation	ELHGEGSSSGKATGD EECCCCCCCCCCCCC	54.70	29255136
238	Phosphorylation	LHGEGSSSGKATGDE ECCCCCCCCCCCCCC	46.11	29255136
240	Ubiquitination	GEGSSSGKATGDETG CCCCCCCCCCCCCCC	44.73	21906983
240	2-Hydroxyisobutyrylation	GEGSSSGKATGDETG CCCCCCCCCCCCCCC	44.73	-
240	Acetylation	GEGSSSGKATGDETG CCCCCCCCCCCCCCC	44.73	26051181
242	Phosphorylation	GSSSGKATGDETGAK CCCCCCCCCCCCCCC	48.96	29255136
246	Phosphorylation	GKATGDETGAKVERA CCCCCCCCCCCCEEC	47.37	29255136
249	Acetylation	TGDETGAKVERADGY CCCCCCCCCEECCCC	46.07	19608861
249	Sumoylation	TGDETGAKVERADGY CCCCCCCCCEECCCC	46.07	-
249	Ubiquitination	TGDETGAKVERADGY CCCCCCCCCEECCCC	46.07	2190698
249	Sumoylation	TGDETGAKVERADGY CCCCCCCCCEECCCC	46.07	28112733
256	Phosphorylation	KVERADGYEPPVQES CCEECCCCCCCCCCC	26.30	21945579
263	Phosphorylation	YEPPVQESV------ CCCCCCCCC------	18.94	25159151

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
10	T	Phosphorylation	Kinase	AKT1	P31749	PSP
88	T	Phosphorylation	Kinase	AKT1	P31749	PSP
112	S	Phosphorylation	Kinase	AKT1	P31749	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of RS3A_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 RS3A_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
EDEM2_HUMAN	EDEM2	physical	16169070
SAP18_HUMAN	SAP18	physical	16169070
SODM_HUMAN	SOD2	physical	16169070
HS90A_HUMAN	HSP90AA1	physical	16169070
DDIT3_HUMAN	DDIT3	physical	10713066
PARP1_HUMAN	PARP1	physical	11790116
RS3_HUMAN	RPS3	physical	22939629
RS6_HUMAN	RPS6	physical	22939629
RSSA_HUMAN	RPSA	physical	22939629
RS4X_HUMAN	RPS4X	physical	22939629
RS9_HUMAN	RPS9	physical	22939629
RS5_HUMAN	RPS5	physical	22939629
RS8_HUMAN	RPS8	physical	22939629
VHL_HUMAN	VHL	physical	23612971
EIF3A_HUMAN	EIF3A	physical	22863883
EIFCL_HUMAN	EIF3CL	physical	22863883
EIF3E_HUMAN	EIF3E	physical	22863883
RSSA_HUMAN	RPSA	physical	22863883
LARP1_HUMAN	LARP1	physical	22863883
RS10_HUMAN	RPS10	physical	22863883
RS12_HUMAN	RPS12	physical	22863883
RS13_HUMAN	RPS13	physical	22863883
RS14_HUMAN	RPS14	physical	22863883
RS15A_HUMAN	RPS15A	physical	22863883
RS16_HUMAN	RPS16	physical	22863883
RS17_HUMAN	RPS17	physical	22863883
RS21_HUMAN	RPS21	physical	22863883
RS24_HUMAN	RPS24	physical	22863883
RS26_HUMAN	RPS26	physical	22863883
RS27_HUMAN	RPS27	physical	22863883
RS28_HUMAN	RPS28	physical	22863883
RS4X_HUMAN	RPS4X	physical	22863883
RS5_HUMAN	RPS5	physical	22863883
RS6_HUMAN	RPS6	physical	22863883
RS7_HUMAN	RPS7	physical	22863883
RS8_HUMAN	RPS8	physical	22863883
RS9_HUMAN	RPS9	physical	22863883
SND1_HUMAN	SND1	physical	22863883
TSR1_HUMAN	TSR1	physical	22863883
ABCE1_HUMAN	ABCE1	physical	26344197
EF1A1_HUMAN	EEF1A1	physical	26344197
RACK1_HUMAN	GNB2L1	physical	26344197
HNRPU_HUMAN	HNRNPU	physical	26344197
RL10_HUMAN	RPL10	physical	26344197
RL10A_HUMAN	RPL10A	physical	26344197
RL12_HUMAN	RPL12	physical	26344197
RL13_HUMAN	RPL13	physical	26344197
RL13A_HUMAN	RPL13A	physical	26344197
RL14_HUMAN	RPL14	physical	26344197
RL15_HUMAN	RPL15	physical	26344197
RL17_HUMAN	RPL17	physical	26344197
RL18_HUMAN	RPL18	physical	26344197
RL27_HUMAN	RPL27	physical	26344197
RL27A_HUMAN	RPL27A	physical	26344197
RL28_HUMAN	RPL28	physical	26344197
RL30_HUMAN	RPL30	physical	26344197
RL32_HUMAN	RPL32	physical	26344197
RL37A_HUMAN	RPL37A	physical	26344197
RL38_HUMAN	RPL38	physical	26344197
RL6_HUMAN	RPL6	physical	26344197
RL9_HUMAN	RPL9	physical	26344197
RLA2_HUMAN	RPLP2	physical	26344197
RS14_HUMAN	RPS14	physical	26344197
RS15_HUMAN	RPS15	physical	26344197
RS16_HUMAN	RPS16	physical	26344197
RS18_HUMAN	RPS18	physical	26344197
RS19_HUMAN	RPS19	physical	26344197
RS23_HUMAN	RPS23	physical	26344197
RS25_HUMAN	RPS25	physical	26344197
RS26_HUMAN	RPS26	physical	26344197
RS27_HUMAN	RPS27	physical	26344197
RS4X_HUMAN	RPS4X	physical	26344197
RS5_HUMAN	RPS5	physical	26344197
RS6_HUMAN	RPS6	physical	26344197
RS7_HUMAN	RPS7	physical	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 RS3A_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-34 AND LYS-249, AND MASSSPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"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-263, 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-263, AND MASSSPECTROMETRY.	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-263, AND MASSSPECTROMETRY.	18691976 [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-263, AND MASSSPECTROMETRY.	19007248 [Abstract]
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization."; Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; Nat. Biotechnol. 24:1285-1292(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263, AND MASSSPECTROMETRY.	16964243 [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-263, AND MASSSPECTROMETRY.	17081983 [Abstract]
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells."; Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.; Nat. Biotechnol. 23:94-101(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-256, AND MASSSPECTROMETRY.	15592455 [Abstract]