RS2_MOUSE - dbPTM
RS2_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RS2_MOUSE
UniProt AC P25444
Protein Name 40S ribosomal protein S2
Gene Name Rps2
Organism Mus musculus (Mouse).
Sequence Length 293
Subcellular Localization
Protein Description
Protein Sequence MADDAGAAGGPGGPGGPGLGGRGGFRGGFGSGLRGRGRGRGRGRGRGRGARGGKAEDKEWIPVTKLGRLVKDMKIKSLEEIYLFSLPIKESEIIDFFLGASLKDEVLKIMPVQKQTRAGQRTRFKAFVAIGDYNGHVGLGVKCSKEVATAIRGAIILAKLSIVPVRRGYWGNKIGKPHTVPCKVTGRCGSVLVRLIPAPRGTGIVSAPVPKKLLMMAGIDDCYTSARGCTATLGNFAKATFDAISKTYSYLTPDLWKETVFTKSPYQEFTDHLVKTHTRVSVQRTQAPAVATT
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 Orthologous
Protein Cluster
2Acetylation------MADDAGAAG
------CCCCCCCCC		24.32-
22MethylationGGPGLGGRGGFRGGF
CCCCCCCCCCCCCCC		40.0230989259
26MethylationLGGRGGFRGGFGSGL
CCCCCCCCCCCCCCC		47.8324383459
34MethylationGGFGSGLRGRGRGRG
CCCCCCCCCCCCCCC		35.975149751
36MethylationFGSGLRGRGRGRGRG
CCCCCCCCCCCCCCC		25.795149743
38MethylationSGLRGRGRGRGRGRG
CCCCCCCCCCCCCCC		30.215149739
40MethylationLRGRGRGRGRGRGRG
CCCCCCCCCCCCCCC		30.215149749
42MethylationGRGRGRGRGRGRGRG
CCCCCCCCCCCCCCC		30.215149753
44MethylationGRGRGRGRGRGRGAR
CCCCCCCCCCCCCCC		30.215149745
46MethylationGRGRGRGRGRGARGG
CCCCCCCCCCCCCCC		30.215149741
48MethylationGRGRGRGRGARGGKA
CCCCCCCCCCCCCCC		33.955149747
58SuccinylationRGGKAEDKEWIPVTK
CCCCCCCCCCEEHHH		46.5923806337
58UbiquitinationRGGKAEDKEWIPVTK
CCCCCCCCCCEEHHH		46.59-
58MalonylationRGGKAEDKEWIPVTK
CCCCCCCCCCEEHHH		46.5926320211
58AcetylationRGGKAEDKEWIPVTK
CCCCCCCCCCEEHHH		46.5923864654
65AcetylationKEWIPVTKLGRLVKD
CCCEEHHHHHHHHHC		49.5322826441
65UbiquitinationKEWIPVTKLGRLVKD
CCCEEHHHHHHHHHC		49.53-
76AcetylationLVKDMKIKSLEEIYL
HHHCCCCCCHHEEEE		43.3922826441
76UbiquitinationLVKDMKIKSLEEIYL
HHHCCCCCCHHEEEE		43.39-
77PhosphorylationVKDMKIKSLEEIYLF
HHCCCCCCHHEEEEE		44.4826824392
82PhosphorylationIKSLEEIYLFSLPIK
CCCHHEEEEEECCCC		12.6526239621
85PhosphorylationLEEIYLFSLPIKESE
HHEEEEEECCCCHHH		30.5526643407
108SuccinylationSLKDEVLKIMPVQKQ
CCCHHHHHHCCCCCC		41.9823954790
108AcetylationSLKDEVLKIMPVQKQ
CCCHHHHHHCCCCCC		41.9822826441
114UbiquitinationLKIMPVQKQTRAGQR
HHHCCCCCCCCCCCC		54.60-
114AcetylationLKIMPVQKQTRAGQR
HHHCCCCCCCCCCCC		54.6022826441
116PhosphorylationIMPVQKQTRAGQRTR
HCCCCCCCCCCCCCE		29.53-
133PhosphorylationAFVAIGDYNGHVGLG
EEEEEECCCCCEEEC		20.1726745281
173AcetylationRRGYWGNKIGKPHTV
CCCCCCCCCCCCCEE		49.2322826441
176UbiquitinationYWGNKIGKPHTVPCK
CCCCCCCCCCEECCE		36.78-
182GlutathionylationGKPHTVPCKVTGRCG
CCCCEECCEEECCCC		4.8724333276
182S-nitrosylationGKPHTVPCKVTGRCG
CCCCEECCEEECCCC		4.8721278135
182S-nitrosocysteineGKPHTVPCKVTGRCG
CCCCEECCEEECCCC		4.87-
188GlutathionylationPCKVTGRCGSVLVRL
CCEEECCCCCEEEEE		5.1524333276
188S-nitrosylationPCKVTGRCGSVLVRL
CCEEECCCCCEEEEE		5.1524926564
190PhosphorylationKVTGRCGSVLVRLIP
EEECCCCCEEEEEEE		18.86-
211MalonylationIVSAPVPKKLLMMAG
CCCCCCCHHHHHHCC		57.1826320211
211AcetylationIVSAPVPKKLLMMAG
CCCCCCCHHHHHHCC		57.187630859
212AcetylationVSAPVPKKLLMMAGI
CCCCCCHHHHHHCCC		40.5622826441
222S-palmitoylationMMAGIDDCYTSARGC
HHCCCCHHHHHHCCC		3.3728526873
222GlutathionylationMMAGIDDCYTSARGC
HHCCCCHHHHHHCCC		3.3724333276
223PhosphorylationMAGIDDCYTSARGCT
HCCCCHHHHHHCCCC		15.66-
229GlutathionylationCYTSARGCTATLGNF
HHHHHCCCCCCHHHH		1.6324333276
229S-nitrosocysteineCYTSARGCTATLGNF
HHHHHCCCCCCHHHH		1.63-
229S-nitrosylationCYTSARGCTATLGNF
HHHHHCCCCCCHHHH		1.6322178444
229S-palmitoylationCYTSARGCTATLGNF
HHHHHCCCCCCHHHH		1.6328526873
250PhosphorylationAISKTYSYLTPDLWK
HHHHHHHHCCHHHHH		12.2723984901
252PhosphorylationSKTYSYLTPDLWKET
HHHHHHCCHHHHHHC		13.4126745281
257UbiquitinationYLTPDLWKETVFTKS
HCCHHHHHHCCCCCC		51.29-
257SuccinylationYLTPDLWKETVFTKS
HCCHHHHHHCCCCCC		51.2923954790
257AcetylationYLTPDLWKETVFTKS
HCCHHHHHHCCCCCC		51.2922826441
259PhosphorylationTPDLWKETVFTKSPY
CHHHHHHCCCCCCHH		19.7225159016
262PhosphorylationLWKETVFTKSPYQEF
HHHHCCCCCCHHHHH		26.6928507225
263UbiquitinationWKETVFTKSPYQEFT
HHHCCCCCCHHHHHH		37.66-
263AcetylationWKETVFTKSPYQEFT
HHHCCCCCCHHHHHH		37.6622826441
264PhosphorylationKETVFTKSPYQEFTD
HHCCCCCCHHHHHHH		26.2825521595
266PhosphorylationTVFTKSPYQEFTDHL
CCCCCCHHHHHHHHH		27.9727742792
270PhosphorylationKSPYQEFTDHLVKTH
CCHHHHHHHHHHHHC		23.0425159016
275MalonylationEFTDHLVKTHTRVSV
HHHHHHHHHCCCCEE		40.7326320211
275AcetylationEFTDHLVKTHTRVSV
HHHHHHHHHCCCCEE		40.7322826441
275UbiquitinationEFTDHLVKTHTRVSV
HHHHHHHHHCCCCEE		40.73-
276PhosphorylationFTDHLVKTHTRVSVQ
HHHHHHHHCCCCEEE		22.4725159016
278PhosphorylationDHLVKTHTRVSVQRT
HHHHHHCCCCEEECC		37.6923375375
281PhosphorylationVKTHTRVSVQRTQAP
HHHCCCCEEECCCCC		14.8326824392
285PhosphorylationTRVSVQRTQAPAVAT
CCCEEECCCCCCCCC		16.4023375375
292PhosphorylationTQAPAVATT------
CCCCCCCCC------		26.8330635358
293PhosphorylationQAPAVATT-------
CCCCCCCC-------		27.2025521595
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 RS2_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RS2_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 RS2_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NGLY1_MOUSENgly1physical
11562482
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RS2_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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.
"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.

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