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Protein Page:
RPS3 (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitylation
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
RPS3 a component of the 40S ribosomal subunit of eukaryotes. Identified in a mRNP granule complex, at least composed of ACTB, ACTN4, DHX9, ERG, HNRNPA1, HNRNPA2B1, HNRNPAB, HNRNPD, HNRNPL, HNRNPR, HNRNPU, HSPA1, HSPA8, IGF2BP1, ILF2, ILF3, NCBP1, NCL, PABPC1, PABPC4, PABPN1, RPLP0, RPS3, RPS3A, RPS4X, RPS8, RPS9, SYNCRIP, TROVE2, YBX1 and untranslated mRNAs. Identified in a HCV IRES-mediated translation complex, at least composed of EIF3C, IGF2BP1, RPS3 and HCV RNA-replicon. Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Overexpressed in colorectal cancer. Note: This description may include information from UniProtKB.
Protein type: Translation; EC 4.2.99.18; Ribosomal; RNA-binding; Apoptosis
Chromosomal Location of Human Ortholog: 11q13.3-q13.5
Cellular Component: cytoplasm; cytosol; focal adhesion; membrane; mitochondrial inner membrane; mitochondrial matrix; nucleolus; nucleoplasm; nucleus; plasma membrane; polysome; ribonucleoprotein complex; ribosome
Molecular Function: damaged DNA binding; DNA binding; DNA N-glycosylase activity; DNA-(apurinic or apyrimidinic site) lyase activity; endodeoxyribonuclease activity; enzyme binding; Hsp70 protein binding; Hsp90 protein binding; iron-sulfur cluster binding; kinase binding; microtubule binding; mRNA binding; NF-kappaB binding; oxidized purine base lesion DNA N-glycosylase activity; oxidized purine DNA binding; oxidized pyrimidine DNA binding; protein binding; protein kinase A binding; protein kinase binding; RNA binding; structural constituent of ribosome; SUMO binding; transcription factor binding; tubulin binding
Biological Process: activation of NF-kappaB transcription factor; cell division; chromosome segregation; DNA damage response, detection of DNA damage; DNA repair; mitosis; mRNA catabolic process, nonsense-mediated decay; negative regulation of DNA repair; negative regulation of protein ubiquitination; negative regulation of translation; positive regulation of DNA repair; positive regulation of endodeoxyribonuclease activity; positive regulation of JNK activity; positive regulation of microtubule polymerization; regulation of apoptosis; response to DNA damage stimulus; response to oxidative stress; rRNA processing; spindle assembly; SRP-dependent cotranslational protein targeting to membrane; transcription, DNA-dependent; translation; translational initiation; viral transcription
Reference #:  P23396 (UniProtKB)
Alt. Names/Synonyms: 40S ribosomal protein S3; FLJ26283; FLJ27450; IMR-90 ribosomal protein S3; MGC87870; ribosomal protein S3; RPS3; RS3
Gene Symbols: RPS3
Molecular weight: 26,688 Da
Basal Isoelectric point: 9.68  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

RPS3

Protein Structure Not Found.
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Sites Implicated In
apoptosis, altered: T70‑p
translation, altered: S6‑p, T221‑p
activity, induced: S6‑p, T70‑p, T221‑p
intracellular localization: S6‑p, T42‑p, R64‑m2, R65‑m2, R67‑m2, T70‑p, S209‑p, T221‑p
molecular association, regulation: T70‑p

Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 LTP 

LTP: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 HTP 

HTP: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
2 0 S6‑p __MAVQIskkRkFVA
0 2 K7‑ub _MAVQIskkRkFVAD
0 1 K8‑ub MAVQIskkRkFVADG
0 1 K10 VQIskkRKFVADGIF
0 30 K10‑ub VQIskkRkFVADGIF
0 38 K18‑ub FVADGIFkAELNEFL
1 0 K18‑sm FVADGIFkAELNEFL
0 2 S35‑p ELAEDGYsGVEVRVt
2 0 T42‑p sGVEVRVtPTRtEII
0 2 T46‑p VRVtPTRtEIIILAT
0 4 K62‑ac TQNVLGEkGrrIrEL
0 79 K62‑ub TQNVLGEkGrrIrEL
0 1 K62‑sc TQNVLGEkGrrIrEL
1 0 R64‑m2 NVLGEkGrrIrELtA
1 0 R65‑m2 VLGEkGrrIrELtAV
1 0 R67‑m2 GEkGrrIrELtAVVQ
2 1 T70‑p GrrIrELtAVVQkRF
0 2 K75‑ac ELtAVVQkRFGFPEG
0 28 K75‑ub ELtAVVQkRFGFPEG
0 2 S83‑p RFGFPEGsVELyAEk
0 4 Y87‑p PEGsVELyAEkVATR
0 1 K90 sVELyAEKVATRGLC
0 85 K90‑ub sVELyAEkVATRGLC
0 1 K90‑sc sVELyAEkVATRGLC
0 7 S104‑p CAIAQAEsLRykLLG
0 14 Y107‑p AQAEsLRykLLGGLA
0 2 K108‑ac QAEsLRykLLGGLAV
0 29 K108‑ub QAEsLRykLLGGLAV
0 49 Y120‑p LAVRRACyGVLRFIM
0 5 K132‑ub FIMESGAkGCEVVVs
0 1 S139‑p kGCEVVVsGkLRGQR
0 71 K141‑ub CEVVVsGkLRGQRAK
0 5 K151‑ub GQRAKSMkFVDGLMI
0 20 Y166‑p HSGDPVNyyVDTAVR
0 2 Y167‑p SGDPVNyyVDTAVRH
0 1 K185‑ub RQGVLGIkVkIMLPW
0 3 K187‑ub GVLGIkVkIMLPWDP
0 2 K197‑ac LPWDPTGkIGPkkPL
0 51 K197‑ub LPWDPTGkIGPkkPL
0 41 K201‑ub PTGkIGPkkPLPDHV
0 28 K202‑ub TGkIGPkkPLPDHVs
1 6 S209‑p kPLPDHVsIVEPkDE
0 2 K214‑ac HVsIVEPkDEILPtt
0 144 K214‑ub HVsIVEPkDEILPtt
1 0 K214‑sm HVsIVEPkDEILPtt
1 52 T220‑p PkDEILPttPIsEQk
5 176 T221‑p kDEILPttPIsEQkG
1 18 S224‑p ILPttPIsEQkGGkP
0 2 K227‑ub ttPIsEQkGGkPEPP
1 0 K230‑sm IsEQkGGkPEPPAMP
1 80 K230‑ub IsEQkGGkPEPPAMP
0 14 T242‑p AMPQPVPtA______
  mouse

 
S6 __MAVQISKKRkFVA
K7 _MAVQISKKRkFVAD
K8 MAVQISKKRkFVADG
K10 VQISKKRKFVADGIF
K10‑ub VQISKKRkFVADGIF
K18‑ub FVADGIFkAELNEFL
K18 FVADGIFKAELNEFL
S35 ELAEDGYSGVEVRVT
T42 SGVEVRVTPTRTEII
T46 VRVTPTRTEIIILAT
K62‑ac TQNVLGEkGRRIREL
K62‑ub TQNVLGEkGRRIREL
K62 TQNVLGEKGRRIREL
R64 NVLGEkGRRIRELtA
R65 VLGEkGRRIRELtAV
R67 GEkGRRIRELtAVVQ
T70‑p GRRIRELtAVVQkRF
K75 ELtAVVQKRFGFPEG
K75‑ub ELtAVVQkRFGFPEG
S83 RFGFPEGSVELYAEk
Y87 PEGSVELYAEkVATR
K90 SVELYAEKVATRGLC
K90‑ub SVELYAEkVATRGLC
K90 SVELYAEKVATRGLC
S104‑p CAIAQAEsLRYkLLG
Y107 AQAEsLRYkLLGGLA
K108 QAEsLRYKLLGGLAV
K108‑ub QAEsLRYkLLGGLAV
Y120‑p LAVRRACyGVLRFIM
K132 FIMESGAKGCEVVVS
S139 KGCEVVVSGkLRGQR
K141‑ub CEVVVSGkLRGQRAK
K151 GQRAKSMKFVDGLMI
Y166‑p HSGDPVNyYVDTAVR
Y167 SGDPVNyYVDTAVRH
K185 RQGVLGIKVKIMLPW
K187 GVLGIKVKIMLPWDP
K197 LPWDPSGKIGPkkPL
K197‑ub LPWDPSGkIGPkkPL
K201‑ub PSGkIGPkkPLPDHV
K202‑ub SGkIGPkkPLPDHVs
S209‑p kPLPDHVsIVEPkDE
K214‑ac HVsIVEPkDEILPtt
K214‑ub HVsIVEPkDEILPtt
K214 HVsIVEPKDEILPtt
T220‑p PkDEILPttPIsEQk
T221‑p kDEILPttPIsEQkG
S224‑p ILPttPIsEQkGGkP
K227‑ub ttPIsEQkGGkPEPP
K230 IsEQkGGKPEPPAMP
K230‑ub IsEQkGGkPEPPAMP
T242‑p AMPQPVPtA______
  rat

 
S6 __MAVQISKKRkFVA
K7 _MAVQISKKRkFVAD
K8 MAVQISKKRkFVADG
K10‑ac VQISKKRkFVADGIF
K10 VQISKKRKFVADGIF
K18 FVADGIFKAELNEFL
K18 FVADGIFKAELNEFL
S35 ELAEDGYSGVEVRVT
T42 SGVEVRVTPTRTEII
T46 VRVTPTRTEIIILAT
K62‑ac TQNVLGEkGRRIREL
K62 TQNVLGEKGRRIREL
K62 TQNVLGEKGRRIREL
R64 NVLGEkGRRIRELTA
R65 VLGEkGRRIRELTAV
R67 GEkGRRIRELTAVVQ
T70 GRRIRELTAVVQkRF
K75‑ac ELTAVVQkRFGFPEG
K75 ELTAVVQKRFGFPEG
S83 RFGFPEGSVELYAEk
Y87 PEGSVELYAEkVATR
K90‑ac SVELYAEkVATRGLC
K90 SVELYAEKVATRGLC
K90 SVELYAEKVATRGLC
S104 CAIAQAESLRYkLLG
Y107 AQAESLRYkLLGGLA
K108‑ac QAESLRYkLLGGLAV
K108 QAESLRYKLLGGLAV
Y120 LAVRRACYGVLRFIM
K132 FIMESGAKGCEVVVS
S139 KGCEVVVSGKLRGQR
K141 CEVVVSGKLRGQRAK
K151 GQRAKSMKFVDGLMI
Y166 HSGDPVNYYVDTAVR
Y167 SGDPVNYYVDTAVRH
K185 RQGVLGIKVKIMLPW
K187 GVLGIKVKIMLPWDP
K197‑ac LPWDPSGkIGPKKPL
K197 LPWDPSGKIGPKKPL
K201 PSGkIGPKKPLPDHV
K202 SGkIGPKKPLPDHVS
S209 KPLPDHVSIVEPkDE
K214‑ac HVSIVEPkDEILPtt
K214‑ub HVSIVEPkDEILPtt
K214 HVSIVEPKDEILPtt
T220‑p PkDEILPttPISEQK
T221‑p kDEILPttPISEQKG
S224 ILPttPISEQKGGKP
K227 ttPISEQKGGKPEPP
K230 ISEQKGGKPEPPAMP
K230 ISEQKGGKPEPPAMP
T242 AMPQPVPTA______
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