dbPTM

RS3_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RS3_MOUSE
UniProt AC	P62908
Protein Name	40S ribosomal protein S3
Gene Name	Rps3
Organism	Mus musculus (Mouse).
Sequence Length	243
Subcellular Localization	Cytoplasm . Nucleus . Nucleus, nucleolus . Mitochondrion inner membrane Peripheral membrane protein . Cytoplasm, cytoskeleton, spindle . In normal cells, located mainly in the cytoplasm with small amounts in the nucleus but translocates to the nucl
Protein Description	Involved in translation as a component of the 40S small ribosomal subunit (By similarity). Has endonuclease activity and plays a role in repair of damaged DNA. [PubMed: 7775413 Cleaves phosphodiester bonds of DNAs containing altered bases with broad specificity and cleaves supercoiled DNA more efficiently than relaxed DNA (By similarity Displays high binding affinity for 7,8-dihydro-8-oxoguanine (8-oxoG), a common DNA lesion caused by reactive oxygen species (ROS) (By similarity Has also been shown to bind with similar affinity to intact and damaged DNA (By similarity Stimulates the N-glycosylase activity of the base excision protein OGG1 (By similarity Enhances the uracil excision activity of UNG1 (By similarity Also stimulates the cleavage of the phosphodiester backbone by APEX1 (By similarity When located in the mitochondrion, reduces cellular ROS levels and mitochondrial DNA damage (By similarity Has also been shown to negatively regulate DNA repair in cells exposed to hydrogen peroxide (By similarity Plays a role in regulating transcription as part of the NF-kappa-B p65-p50 complex where it binds to the RELA/p65 subunit, enhances binding of the complex to DNA and promotes transcription of target genes (By similarity Represses its own translation by binding to its cognate mRNA (By similarity Binds to and protects TP53/p53 from MDM2-mediated ubiquitination (By similarity Involved in spindle formation and chromosome movement during mitosis by regulating microtubule polymerization (By similarity Involved in induction of apoptosis through its role in activation of CASP8]
Protein Sequence	MAVQISKKRKFVADGIFKAELNEFLTRELAEDGYSGVEVRVTPTRTEIIILATRTQNVLGEKGRRIRELTAVVQKRFGFPEGSVELYAEKVATRGLCAIAQAESLRYKLLGGLAVRRACYGVLRFIMESGAKGCEVVVSGKLRGQRAKSMKFVDGLMIHSGDPVNYYVDTAVRHVLLRQGVLGIKVKIMLPWDPSGKIGPKKPLPDHVSIVEPKDEILPTTPISEQKGGKPEPPAMPQPVPTA

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAVQISKKR ------CCCCCCCCC	11.26	-
6	Phosphorylation	--MAVQISKKRKFVA --CCCCCCCCCCCCC	18.29	-
10	Ubiquitination	VQISKKRKFVADGIF CCCCCCCCCCCCCCH	53.74	-
10	Acetylation	VQISKKRKFVADGIF CCCCCCCCCCCCCCH	53.74	22826441
18	Ubiquitination	FVADGIFKAELNEFL CCCCCCHHHHHHHHH	38.74	-
18	Acetylation	FVADGIFKAELNEFL CCCCCCHHHHHHHHH	38.74	22826441
35	Phosphorylation	ELAEDGYSGVEVRVT HHHHCCCCCEEEEEC	41.72	28066266
42	Phosphorylation	SGVEVRVTPTRTEII CCEEEEECCCCCEEE	14.37	-
62	Acetylation	TQNVLGEKGRRIREL CCCCCCCHHHHHHHH	56.79	23806337
62	Ubiquitination	TQNVLGEKGRRIREL CCCCCCCHHHHHHHH	56.79	-
62	Malonylation	TQNVLGEKGRRIREL CCCCCCCHHHHHHHH	56.79	26320211
64	Asymmetric dimethylarginine	NVLGEKGRRIRELTA CCCCCHHHHHHHHHH	41.75	-
64	Methylation	NVLGEKGRRIRELTA CCCCCHHHHHHHHHH	41.75	-
65	Methylation	VLGEKGRRIRELTAV CCCCHHHHHHHHHHH	40.77	-
65	Asymmetric dimethylarginine	VLGEKGRRIRELTAV CCCCHHHHHHHHHHH	40.77	-
67	Methylation	GEKGRRIRELTAVVQ CCHHHHHHHHHHHHH	30.94	-
67	Asymmetric dimethylarginine	GEKGRRIRELTAVVQ CCHHHHHHHHHHHHH	30.94	-
70	Phosphorylation	GRRIRELTAVVQKRF HHHHHHHHHHHHHHH	16.80	18779572
75	Acetylation	ELTAVVQKRFGFPEG HHHHHHHHHHCCCCC	37.78	22826441
75	Ubiquitination	ELTAVVQKRFGFPEG HHHHHHHHHHCCCCC	37.78	22790023
87	Phosphorylation	PEGSVELYAEKVATR CCCCCHHHHHHHHHH	10.14	25367039
90	Malonylation	SVELYAEKVATRGLC CCHHHHHHHHHHHHH	29.06	26073543
90	Ubiquitination	SVELYAEKVATRGLC CCHHHHHHHHHHHHH	29.06	-
90	Acetylation	SVELYAEKVATRGLC CCHHHHHHHHHHHHH	29.06	23236377
97	S-palmitoylation	KVATRGLCAIAQAES HHHHHHHHHHHCHHH	2.61	28526873
97	Glutathionylation	KVATRGLCAIAQAES HHHHHHHHHHHCHHH	2.61	24333276
97	S-nitrosylation	KVATRGLCAIAQAES HHHHHHHHHHHCHHH	2.61	24926564
97	S-nitrosocysteine	KVATRGLCAIAQAES HHHHHHHHHHHCHHH	2.61	-
104	Phosphorylation	CAIAQAESLRYKLLG HHHHCHHHHHHHHHH	22.59	26745281
107	Phosphorylation	AQAESLRYKLLGGLA HCHHHHHHHHHHHHH	15.98	23984901
108	Ubiquitination	QAESLRYKLLGGLAV CHHHHHHHHHHHHHH	30.70	-
108	Malonylation	QAESLRYKLLGGLAV CHHHHHHHHHHHHHH	30.70	26320211
108	Acetylation	QAESLRYKLLGGLAV CHHHHHHHHHHHHHH	30.70	23806337
119	Glutathionylation	GLAVRRACYGVLRFI HHHHHHHHHHHHHHH	2.63	24333276
119	S-nitrosylation	GLAVRRACYGVLRFI HHHHHHHHHHHHHHH	2.63	21278135
119	S-palmitoylation	GLAVRRACYGVLRFI HHHHHHHHHHHHHHH	2.63	26165157
119	S-nitrosocysteine	GLAVRRACYGVLRFI HHHHHHHHHHHHHHH	2.63	-
120	Phosphorylation	LAVRRACYGVLRFIM HHHHHHHHHHHHHHH	14.86	25367039
132	Succinylation	FIMESGAKGCEVVVS HHHHCCCCCCEEEEC	68.56	23806337
132	Succinylation	FIMESGAKGCEVVVS HHHHCCCCCCEEEEC	68.56	-
132	Acetylation	FIMESGAKGCEVVVS HHHHCCCCCCEEEEC	68.56	23806337
132	Malonylation	FIMESGAKGCEVVVS HHHHCCCCCCEEEEC	68.56	26320211
134	Glutathionylation	MESGAKGCEVVVSGK HHCCCCCCEEEECCC	3.37	24333276
134	S-nitrosocysteine	MESGAKGCEVVVSGK HHCCCCCCEEEECCC	3.37	-
134	S-nitrosylation	MESGAKGCEVVVSGK HHCCCCCCEEEECCC	3.37	24926564
139	Phosphorylation	KGCEVVVSGKLRGQR CCCEEEECCCCCCCC	20.71	25293948
141	Acetylation	CEVVVSGKLRGQRAK CEEEECCCCCCCCCC	27.75	22826441
141	Ubiquitination	CEVVVSGKLRGQRAK CEEEECCCCCCCCCC	27.75	-
166	Phosphorylation	HSGDPVNYYVDTAVR ECCCCCHHHHHHHHH	12.71	-
187	Acetylation	GVLGIKVKIMLPWDP CCCEEEEEEEECCCC	19.86	22826441
197	Malonylation	LPWDPSGKIGPKKPL ECCCCCCCCCCCCCC	49.15	26320211
197	Acetylation	LPWDPSGKIGPKKPL ECCCCCCCCCCCCCC	49.15	23201123
197	Ubiquitination	LPWDPSGKIGPKKPL ECCCCCCCCCCCCCC	49.15	-
201	Malonylation	PSGKIGPKKPLPDHV CCCCCCCCCCCCCCE	62.91	26320211
201	Phosphoglycerylation	PSGKIGPKKPLPDHV CCCCCCCCCCCCCCE	62.91	-
201	Ubiquitination	PSGKIGPKKPLPDHV CCCCCCCCCCCCCCE	62.91	-
202	Malonylation	SGKIGPKKPLPDHVS CCCCCCCCCCCCCEE	55.72	26320211
202	Ubiquitination	SGKIGPKKPLPDHVS CCCCCCCCCCCCCEE	55.72	-
209	Phosphorylation	KPLPDHVSIVEPKDE CCCCCCEEECCCCCC	19.93	24925903
214	Acetylation	HVSIVEPKDEILPTT CEEECCCCCCCCCCC	55.26	23954790
214	Ubiquitination	HVSIVEPKDEILPTT CEEECCCCCCCCCCC	55.26	22790023
220	Phosphorylation	PKDEILPTTPISEQK CCCCCCCCCCCCCCC	41.58	24925903
221	Phosphorylation	KDEILPTTPISEQKG CCCCCCCCCCCCCCC	19.38	27087446
224	Phosphorylation	ILPTTPISEQKGGKP CCCCCCCCCCCCCCC	34.87	24925903
227	Ubiquitination	TTPISEQKGGKPEPP CCCCCCCCCCCCCCC	66.63	-
230	Malonylation	ISEQKGGKPEPPAMP CCCCCCCCCCCCCCC	55.68	26320211
230	Ubiquitination	ISEQKGGKPEPPAMP CCCCCCCCCCCCCCC	55.68	-
242	Phosphorylation	AMPQPVPTA------ CCCCCCCCC------	45.28	23684622

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
6	S	Phosphorylation	Kinase	PRKCD	P28867	Uniprot
42	T	Phosphorylation	Kinase	MAPK	-	Uniprot
70	T	Phosphorylation	Kinase	AKT1	P31749	PSP
70	T	Phosphorylation	Kinase	PKB	P31750	Uniprot
209	S	Phosphorylation	Kinase	IKKB	O88351	Uniprot
221	T	Phosphorylation	Kinase	MAPK1	P63085	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
18	K	Sumoylation	-
Sumoylation occurs at one or more of the three consensus sites, Lys-18, Lys-214 and Lys-230.
209	S	Phosphorylation	-
Phosphorylated on Ser-209 by IKKB in response to activation of the NF-kappa-B p65-p50 complex which enhances the association of RPS3 with importin-alpha and mediates the nuclear translocation of RPS3.
214	K	Sumoylation	-
Sumoylation occurs at one or more of the three consensus sites, Lys-18, Lys-214 and Lys-230.
214	K	ubiquitylation	-
Monoubiquitinated at Lys-214 by ZNF598 when a ribosome has stalled during translation of poly(A) sequences, leading to preclude synthesis of a long poly-lysine tail and initiate the ribosome quality control (RQC) pathway to degrade the potentially detrimental aberrant nascent polypeptide.
221	T	Phosphorylation	17242355
Phosphorylation at Thr-221 by CDK1 occurs mainly in G2/M phase.
230	K	Sumoylation	-
Sumoylation occurs at one or more of the three consensus sites, Lys-18, Lys-214 and Lys-230.

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 RS3_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
NPM_MOUSE	Npm1	physical	18809582

Drug and Disease Associations

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

Regulatory Network of RS3_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Qualitative and quantitative analyses of protein phosphorylation innaive and stimulated mouse synaptosomal preparations."; Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,Gerrits B., Panse C., Schlapbach R., Mansuy I.M.; Mol. Cell. Proteomics 6:283-293(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-221, AND MASSSPECTROMETRY.	17114649 [Abstract]
"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 THR-221, AND MASSSPECTROMETRY.	17203969 [Abstract]

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