RS3_RAT - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: RS3_RAT
• UniProt AC: P62909
• Protein Name: 40S ribosomal protein S3
• Gene Name: Rps3
• Organism: Rattus norvegicus (Rat).
• 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. 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 (By similarity Induces neuronal apoptosis by interacting with the E2F1 transcription factor and acting synergistically with it to up-regulate pro-apoptotic proteins BCL2L11/BIM and HRK/Dp5 (By similarity Interacts with TRADD following exposure to UV radiation and induces apoptosis by caspase-dependent JNK activation (By similarity]
• Protein Sequence: MAVQISKKRKFVADGIFKAELNEFLTRELAEDGYSGVEVRVTPTRTEIIILATRTQNVLGEKGRRIRELTAVVQKRFGFPEGSVELYAEKVATRGLCAIAQAESLRYKLLGGLAVRRACYGVLRFIMESGAKGCEVVVSGKLRGQRAKSMKFVDGLMIHSGDPVNYYVDTAVRHVLLRQGVLGIKVKIMLPWDPSGKIGPKKPLPDHVSIVEPKDEILPTTPISEQKGGKPEPPAMPQPVPTA

Overview of Protein Modification Sites with Functional and Structural Information

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	Succinylation	VQISKKRKFVADGIF CCCCCCCCCCCCCCH	53.74	26843850
10	Acetylation	VQISKKRKFVADGIF CCCCCCCCCCCCCCH	53.74	22902405
34	Phosphorylation	RELAEDGYSGVEVRV HHHHHCCCCCEEEEE	17.99	23984901
35	Phosphorylation	ELAEDGYSGVEVRVT HHHHCCCCCEEEEEC	41.72	23984901
42	Phosphorylation	SGVEVRVTPTRTEII CCEEEEECCCCCEEE	14.37	-
62	Acetylation	TQNVLGEKGRRIREL CCCCCCCHHHHHHHH	56.79	22902405
64	Asymmetric dimethylarginine	NVLGEKGRRIRELTA CCCCCHHHHHHHHHH	41.75	-
64	Methylation	NVLGEKGRRIRELTA CCCCCHHHHHHHHHH	41.75	-
65	Asymmetric dimethylarginine	VLGEKGRRIRELTAV CCCCHHHHHHHHHHH	40.77	-
65	Methylation	VLGEKGRRIRELTAV CCCCHHHHHHHHHHH	40.77	-
67	Methylation	GEKGRRIRELTAVVQ CCHHHHHHHHHHHHH	30.94	-
67	Asymmetric dimethylarginine	GEKGRRIRELTAVVQ CCHHHHHHHHHHHHH	30.94	-
70	Phosphorylation	GRRIRELTAVVQKRF HHHHHHHHHHHHHHH	16.80	-
75	Acetylation	ELTAVVQKRFGFPEG HHHHHHHHHHCCCCC	37.78	25786129
83	Phosphorylation	RFGFPEGSVELYAEK HHCCCCCCCHHHHHH	15.68	23984901
87	Phosphorylation	PEGSVELYAEKVATR CCCCCHHHHHHHHHH	10.14	23984901
90	Acetylation	SVELYAEKVATRGLC CCHHHHHHHHHHHHH	29.06	22902405
104	Phosphorylation	CAIAQAESLRYKLLG HHHHCHHHHHHHHHH	22.59	23984901
108	Acetylation	QAESLRYKLLGGLAV CHHHHHHHHHHHHHH	30.70	72602743
132	Succinylation	FIMESGAKGCEVVVS HHHHCCCCCCEEEEC	68.56	-
132	Succinylation	FIMESGAKGCEVVVS HHHHCCCCCCEEEEC	68.56	-
197	Acetylation	LPWDPSGKIGPKKPL ECCCCCCCCCCCCCC	49.15	22902405
209	Phosphorylation	KPLPDHVSIVEPKDE CCCCCCEEECCCCCC	19.93	25575281
214	Ubiquitination	HVSIVEPKDEILPTT CEEECCCCCCCCCCC	55.26	-
214	Acetylation	HVSIVEPKDEILPTT CEEECCCCCCCCCCC	55.26	22902405
220	Phosphorylation	PKDEILPTTPISEQK CCCCCCCCCCCCCCC	41.58	23991683
221	Phosphorylation	KDEILPTTPISEQKG CCCCCCCCCCCCCCC	19.38	23991683
224	Phosphorylation	ILPTTPISEQKGGKP CCCCCCCCCCCCCCC	34.87	27097102
242	Phosphorylation	AMPQPVPTA------ CCCCCCCCC------	45.28	23991683

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	P09215	Uniprot
42	T	Phosphorylation	Kinase	MAPK	-	Uniprot
70	T	Phosphorylation	Kinase	PKB	P47196	Uniprot
209	S	Phosphorylation	Kinase	IKKB	Q9QY78	Uniprot
221	T	Phosphorylation	Kinase	CDK1	P39951	Uniprot
221	T	Phosphorylation	Kinase	PRKCD	P09215	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	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	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.

Oops, there are no SNP-PTM records of RS3_RAT !!

Protein-Protein Interaction

Oops, there are no PPI records of RS3_RAT !!

Drug and Disease Associations

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