dbPTM

RS3A_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RS3A_MOUSE
UniProt AC	P97351
Protein Name	40S ribosomal protein S3a {ECO:0000255\|HAMAP-Rule:MF_03122}
Gene Name	Rps3a
Organism	Mus musculus (Mouse).
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	MAVGKNKRLTKGGKKGAKKKVVDPFSKKDWYDVKAPAMFNIRNIGKTLVTRTQGTKIASDGLKGRVFEVSLADLQNDEVAFRKFKLITEDVQGKNCLTNFHGMDLTRDKMCSMVKKWQTMIEAHVDVKTTDGYLLRLFCVGFTKKRNNQIRKTSYAQHQQVRQIRKKMMEIMTREVQTNDLKEVVNKLIPDSIGKDIEKACQSIYPLHDVFVRKVKMLKKPKFELGKLMELHGEGGSSGKAAGDETGAKVERADGYEPPVQESV

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
20	Malonylation	GKKGAKKKVVDPFSK CCCCCCCCCCCCCCC	46.94	26320211
20	Acetylation	GKKGAKKKVVDPFSK CCCCCCCCCCCCCCC	46.94	22826441
27	Malonylation	KVVDPFSKKDWYDVK CCCCCCCCCCCCCCC	55.95	26320211
27	Succinylation	KVVDPFSKKDWYDVK CCCCCCCCCCCCCCC	55.95	23954790
27	Acetylation	KVVDPFSKKDWYDVK CCCCCCCCCCCCCCC	55.95	23864654
34	Acetylation	KKDWYDVKAPAMFNI CCCCCCCCCCEEEEE	45.84	22826441
34	Succinylation	KKDWYDVKAPAMFNI CCCCCCCCCCEEEEE	45.84	23954790
34	Ubiquitination	KKDWYDVKAPAMFNI CCCCCCCCCCEEEEE	45.84	-
46	Succinylation	FNIRNIGKTLVTRTQ EEEEECCCEEEEECC	34.58	23806337
46	Acetylation	FNIRNIGKTLVTRTQ EEEEECCCEEEEECC	34.58	23806337
46	Ubiquitination	FNIRNIGKTLVTRTQ EEEEECCCEEEEECC	34.58	-
47	Phosphorylation	NIRNIGKTLVTRTQG EEEECCCEEEEECCC	22.65	22817900
56	Ubiquitination	VTRTQGTKIASDGLK EEECCCCEECCCCCC	43.00	-
56	Malonylation	VTRTQGTKIASDGLK EEECCCCEECCCCCC	43.00	26320211
56	Succinylation	VTRTQGTKIASDGLK EEECCCCEECCCCCC	43.00	23806337
56	Acetylation	VTRTQGTKIASDGLK EEECCCCEECCCCCC	43.00	23806337
63	Acetylation	KIASDGLKGRVFEVS EECCCCCCCCEEEEE	50.64	23806337
63	Succinylation	KIASDGLKGRVFEVS EECCCCCCCCEEEEE	50.64	23806337
85	Acetylation	EVAFRKFKLITEDVQ HHHHHHCCEECCCCC	41.85	22826441
94	Ubiquitination	ITEDVQGKNCLTNFH ECCCCCCCCCCCCCC	27.65	-
94	Malonylation	ITEDVQGKNCLTNFH ECCCCCCCCCCCCCC	27.65	26320211
94	Acetylation	ITEDVQGKNCLTNFH ECCCCCCCCCCCCCC	27.65	23864654
96	Glutathionylation	EDVQGKNCLTNFHGM CCCCCCCCCCCCCCC	5.89	24333276
96	S-nitrosylation	EDVQGKNCLTNFHGM CCCCCCCCCCCCCCC	5.89	24926564
96	S-palmitoylation	EDVQGKNCLTNFHGM CCCCCCCCCCCCCCC	5.89	28526873
96	S-nitrosocysteine	EDVQGKNCLTNFHGM CCCCCCCCCCCCCCC	5.89	-
109	Ubiquitination	GMDLTRDKMCSMVKK CCCCCHHHHHHHHHH	38.22	-
109	Acetylation	GMDLTRDKMCSMVKK CCCCCHHHHHHHHHH	38.22	23806337
111	Glutathionylation	DLTRDKMCSMVKKWQ CCCHHHHHHHHHHHH	2.67	24333276
111	S-nitrosocysteine	DLTRDKMCSMVKKWQ CCCHHHHHHHHHHHH	2.67	-
111	S-nitrosylation	DLTRDKMCSMVKKWQ CCCHHHHHHHHHHHH	2.67	20925432
115	Acetylation	DKMCSMVKKWQTMIE HHHHHHHHHHHHHHH	39.39	2373251
139	Glutathionylation	GYLLRLFCVGFTKKR CCHHHHHHEEEECCC	3.28	24333276
139	S-nitrosylation	GYLLRLFCVGFTKKR CCHHHHHHEEEECCC	3.28	21278135
139	S-palmitoylation	GYLLRLFCVGFTKKR CCHHHHHHEEEECCC	3.28	28526873
139	S-nitrosocysteine	GYLLRLFCVGFTKKR CCHHHHHHEEEECCC	3.28	-
144	Malonylation	LFCVGFTKKRNNQIR HHHEEEECCCCCCCC	47.69	26320211
144	Acetylation	LFCVGFTKKRNNQIR HHHEEEECCCCCCCC	47.69	23864654
144	Ubiquitination	LFCVGFTKKRNNQIR HHHEEEECCCCCCCC	47.69	-
152	Ubiquitination	KRNNQIRKTSYAQHQ CCCCCCCCCHHHHHH	43.37	-
153	Phosphorylation	RNNQIRKTSYAQHQQ CCCCCCCCHHHHHHH	19.68	28507225
154	Phosphorylation	NNQIRKTSYAQHQQV CCCCCCCHHHHHHHH	22.85	27149854
155	ADP-ribosylation	NQIRKTSYAQHQQVR CCCCCCHHHHHHHHH	18.60	-
167	Ubiquitination	QVRQIRKKMMEIMTR HHHHHHHHHHHHHHH	33.36	-
167	Acetylation	QVRQIRKKMMEIMTR HHHHHHHHHHHHHHH	33.36	23806337
167	Succinylation	QVRQIRKKMMEIMTR HHHHHHHHHHHHHHH	33.36	23806337
173	Phosphorylation	KKMMEIMTREVQTND HHHHHHHHHHHCCCC	29.37	26643407
178	Phosphorylation	IMTREVQTNDLKEVV HHHHHHCCCCHHHHH	35.56	26643407
182	Acetylation	EVQTNDLKEVVNKLI HHCCCCHHHHHHHHC	51.86	23864654
182	Succinylation	EVQTNDLKEVVNKLI HHCCCCHHHHHHHHC	51.86	23954790
182	Ubiquitination	EVQTNDLKEVVNKLI HHCCCCHHHHHHHHC	51.86	-
187	Acetylation	DLKEVVNKLIPDSIG CHHHHHHHHCCHHHC	35.86	23806337
187	Succinylation	DLKEVVNKLIPDSIG CHHHHHHHHCCHHHC	35.86	23806337
195	Acetylation	LIPDSIGKDIEKACQ HCCHHHCHHHHHHHH	54.59	23864654
195	Malonylation	LIPDSIGKDIEKACQ HCCHHHCHHHHHHHH	54.59	26320211
199	Acetylation	SIGKDIEKACQSIYP HHCHHHHHHHHHHCC	55.59	22826441
201	S-nitrosocysteine	GKDIEKACQSIYPLH CHHHHHHHHHHCCHH	4.89	-
201	S-palmitoylation	GKDIEKACQSIYPLH CHHHHHHHHHHCCHH	4.89	28526873
201	S-nitrosylation	GKDIEKACQSIYPLH CHHHHHHHHHHCCHH	4.89	24926564
201	Glutathionylation	GKDIEKACQSIYPLH CHHHHHHHHHHCCHH	4.89	24333276
205	Phosphorylation	EKACQSIYPLHDVFV HHHHHHHCCHHHHHH	12.65	29514104
227	Ubiquitination	KPKFELGKLMELHGE CCCCCHHHHEECCCC	58.23	-
237	Phosphorylation	ELHGEGGSSGKAAGD ECCCCCCCCCCCCCC	46.93	25521595
238	Phosphorylation	LHGEGGSSGKAAGDE CCCCCCCCCCCCCCC	47.81	25521595
240	Ubiquitination	GEGGSSGKAAGDETG CCCCCCCCCCCCCCC	36.69	-
240	Malonylation	GEGGSSGKAAGDETG CCCCCCCCCCCCCCC	36.69	26320211
246	Phosphorylation	GKAAGDETGAKVERA CCCCCCCCCCCCEEC	47.37	21183079
249	Ubiquitination	AGDETGAKVERADGY CCCCCCCCCEECCCC	46.07	-
249	Acetylation	AGDETGAKVERADGY CCCCCCCCCEECCCC	46.07	23864654
256	Phosphorylation	KVERADGYEPPVQES CCEECCCCCCCCCCC	26.30	25619855
263	Phosphorylation	YEPPVQESV------ CCCCCCCCC------	18.94	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
Oops, there are no upstream regulatory protein records of RS3A_MOUSE !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of RS3A_MOUSE !!

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_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of RS3A_MOUSE !!

Drug and Disease Associations

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

Regulatory Network of RS3A_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Protein phosphorylation and expression profiling by Yin-yangmultidimensional liquid chromatography (Yin-yang MDLC) massspectrometry."; Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.; J. Proteome Res. 6:250-262(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263, AND MASSSPECTROMETRY.	17203969 [Abstract]
"Quantitative time-resolved phosphoproteomic analysis of mast cellsignaling."; Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,Kawakami T., Salomon A.R.; J. Immunol. 179:5864-5876(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-256, AND MASSSPECTROMETRY.	17947660 [Abstract]