Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  40S ribosomal protein S2  

UniProtKB / Swiss-Prot ID :  RS2_MOUSE

Gene Name (Synonyms) : 
Rps2, Llrep3, Rps4  

Species :  Mus musculus (Mouse). 

Subcellular Localization :   

Protein Function :   

Protein Sequence MADDAGAAGGPGGPGGPGLGGRGGFRGGFGSGLRGRGRGRGRGRGRGRGARGGKAEDKEWIPVTKLGRLV...
Predicted Secondary Structure CCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCEEHHHHHHHH...
Protein Variant -
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
345-methylarginineGSGLRGRGR
CCCCCCCCC
35.97Phosphositeplus
Link-
365-methylarginineGLRGRGRGR
CCCCCCCCC
25.79Phosphositeplus
Link-
385-methylarginineRGRGRGRGR
CCCCCCCCC
30.21Phosphositeplus
Link-
405-methylarginineRGRGRGRGR
CCCCCCCCC
30.21Phosphositeplus
Link-
425-methylarginineRGRGRGRGR
CCCCCCCCC
30.21Phosphositeplus
Link-
445-methylarginineRGRGRGRGR
CCCCCCCCC
30.21Phosphositeplus
Link-
465-methylarginineRGRGRGRGA
CCCCCCCCC
30.21Phosphositeplus
Link-
485-methylarginineRGRGRGARG
CCCCCCCCC
33.95Phosphositeplus
Link-
77PhosphoserineMKIKSLEEI
CCCCCHHHH
44.48Phosphositeplus
Link-
77Phosphoserine.MKIKSLEEI
CCCCCHHHH
44.48UniProtKB
Link-
82PhosphotyrosineLEEIYLFSL
HHHHHHCCC
12.65Phosphositeplus
Link-
82Phosphotyrosine.LEEIYLFSL
HHHHHHCCC
12.65UniProtKB
Link-
85PhosphoserineIYLFSLPIK
HHHCCCCCC
30.55Phosphositeplus
Link-
85Phosphoserine.IYLFSLPIK
HHHCCCCCC
30.55UniProtKB
Link-
133PhosphotyrosineAIGDYNGHV
EEECCCCEE
20.17Phosphositeplus
Link-
133Phosphotyrosine.AIGDYNGHV
EEECCCCEE
20.17UniProtKB
Link-
182S-nitrosocysteineHTVPCKVTG
CEEEEEEEE
4.87dbSNO
Link-
211N6-acetyllysineAPVPKKLLM
CCHHHHHHH
57.18Phosphositeplus
Link-
229S-nitrosocysteineSARGCTATL
EECCCCCCH
1.63dbSNO
Link-
257N6-acetyllysinePDLWKETVF
HHHHHHCCC
51.29Phosphositeplus
Link-
264PhosphoserineVFTKSPYQE
CCCCCHHHH
26.28PhosphoELM
Link-
264PhosphoserineVFTKSPYQE
CCCCCHHHH
26.28Phosphositeplus
Link-
264Phosphoserine.VFTKSPYQE
CCCCCHHHH
26.28UniProtKB
Link-
281PhosphoserineHTRVSVQRT
CCCEEEEEE
14.83Phosphositeplus
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
There are no Protein-Protein Interactions.
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Disease Reference
Drug Reference
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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A differential phosphoproteomic analysis of retinoic acid-treated P19cells.";
Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.;
J. Proteome Res. 6:3174-3186(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-77; TYR-82 AND SER-85,AND MASS SPECTROMETRY.
"Large-scale identification and evolution indexing of tyrosinephosphorylation sites from murine brain.";
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
J. Proteome Res. 7:311-318(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-133, AND MASSSPECTROMETRY.
"Large-scale phosphorylation analysis of mouse liver.";
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-264, AND MASSSPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures