RLA0_MOUSE - dbPTM
RLA0_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RLA0_MOUSE
UniProt AC P14869
Protein Name 60S acidic ribosomal protein P0
Gene Name Rplp0
Organism Mus musculus (Mouse).
Sequence Length 317
Subcellular Localization Nucleus . Cytoplasm . Localized in cytoplasmic mRNP granules containing untranslated mRNAs.
Protein Description Ribosomal protein P0 is the functional equivalent of E.coli protein L10..
Protein Sequence MPREDRATWKSNYFLKIIQLLDDYPKCFIVGADNVGSKQMQQIRMSLRGKAVVLMGKNTMMRKAIRGHLENNPALEKLLPHIRGNVGFVFTKEDLTEIRDMLLANKVPAAARAGAIAPCEVTVPAQNTGLGPEKTSFFQALGITTKISRGTIEILSDVQLIKTGDKVGASEATLLNMLNISPFSFGLIIQQVFDNGSIYNPEVLDITEQALHSRFLEGVRNVASVCLQIGYPTVASVPHSIINGYKRVLALSVETEYTFPLTEKVKAFLADPSAFAAAAPAAAATTAAPAAAAAPAKAEAKEESEESDEDMGFGLFD
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
8PhosphorylationMPREDRATWKSNYFL
CCHHHHHHHHHHHHH		34.0325338131
10AcetylationREDRATWKSNYFLKI
HHHHHHHHHHHHHHH		25.1922826441
10UbiquitinationREDRATWKSNYFLKI
HHHHHHHHHHHHHHH		25.1922790023
16UbiquitinationWKSNYFLKIIQLLDD
HHHHHHHHHHHHHHC		28.06-
24PhosphorylationIIQLLDDYPKCFIVG
HHHHHHCCCCEEEEC		12.3126824392
26UbiquitinationQLLDDYPKCFIVGAD
HHHHCCCCEEEECCC		35.2322790023
27S-nitrosylationLLDDYPKCFIVGADN
HHHCCCCEEEECCCC		2.1324926564
27S-palmitoylationLLDDYPKCFIVGADN
HHHCCCCEEEECCCC		2.1328526873
27S-nitrosocysteineLLDDYPKCFIVGADN
HHHCCCCEEEECCCC		2.13-
38UbiquitinationGADNVGSKQMQQIRM
CCCCCCCHHHHHHHH		43.8122790023
50UbiquitinationIRMSLRGKAVVLMGK
HHHHHHCCEEEEECC		31.41-
57AcetylationKAVVLMGKNTMMRKA
CEEEEECCCHHHHHH		34.9722826441
59PhosphorylationVVLMGKNTMMRKAIR
EEEECCCHHHHHHHH		18.81-
77UbiquitinationENNPALEKLLPHIRG
HCCHHHHHHHHHHCC		57.0622790023
77AcetylationENNPALEKLLPHIRG
HCCHHHHHHHHHHCC		57.0623864654
92UbiquitinationNVGFVFTKEDLTEIR
CEEEEEEHHHHHHHH		37.45-
106UbiquitinationRDMLLANKVPAAARA
HHHHHHCCCCHHHHC		43.9422790023
119S-palmitoylationRAGAIAPCEVTVPAQ
HCCCCCCEEEEECCC		4.9228526873
119S-nitrosylationRAGAIAPCEVTVPAQ
HCCCCCCEEEEECCC		4.9218335467
119S-nitrosocysteineRAGAIAPCEVTVPAQ
HCCCCCCEEEEECCC		4.92-
119GlutathionylationRAGAIAPCEVTVPAQ
HCCCCCCEEEEECCC		4.9224333276
128PhosphorylationVTVPAQNTGLGPEKT
EEECCCCCCCCCCCC		23.0029514104
144PhosphorylationFFQALGITTKISRGT
HHHHHCCEEEECCCE		21.9022006019
145PhosphorylationFQALGITTKISRGTI
HHHHCCEEEECCCEE		25.1822006019
162UbiquitinationLSDVQLIKTGDKVGA
CCCCEEEECCCCCCC		55.8622790023
246AcetylationHSIINGYKRVLALSV
HHHHCCCCEEEEEEE		37.11129377
264UbiquitinationYTFPLTEKVKAFLAD
EEEECCHHHHHHHCC		43.7422790023
266UbiquitinationFPLTEKVKAFLADPS
EECCHHHHHHHCCHH		44.4822790023
273PhosphorylationKAFLADPSAFAAAAP
HHHHCCHHHHHHHHH		36.2424068923
285PhosphorylationAAPAAAATTAAPAAA
HHHHHHHHCHHHHHH		16.5524759943
286PhosphorylationAPAAAATTAAPAAAA
HHHHHHHCHHHHHHH		18.9824068923
297MalonylationAAAAAPAKAEAKEES
HHHHCCHHHHHHHHH		45.7826320211
304PhosphorylationKAEAKEESEESDEDM
HHHHHHHHHHCCCCC		47.9924925903
307PhosphorylationAKEESEESDEDMGFG
HHHHHHHCCCCCCCC		42.1024925903
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 RLA0_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RLA0_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 RLA0_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of RLA0_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RLA0_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large scale localization of protein phosphorylation by use ofelectron capture dissociation mass spectrometry.";
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
Mol. Cell. Proteomics 8:904-912(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-304 AND SER-307, ANDMASS SPECTROMETRY.
"Specific phosphopeptide enrichment with immobilized titanium ionaffinity chromatography adsorbent for phosphoproteome analysis.";
Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
J. Proteome Res. 7:3957-3967(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-304 AND SER-307, ANDMASS SPECTROMETRY.
"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-304, 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-304 AND SER-307, ANDMASS SPECTROMETRY.
"Identification of phosphoproteins and their phosphorylation sites inthe WEHI-231 B lymphoma cell line.";
Shu H., Chen S., Bi Q., Mumby M., Brekken D.L.;
Mol. Cell. Proteomics 3:279-286(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-304 AND SER-307, ANDMASS SPECTROMETRY.
"Quantitative time-resolved phosphoproteomic analysis of mast cellsignaling.";
Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,Kawakami T., Salomon A.R.;
J. Immunol. 179:5864-5876(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-24, AND MASSSPECTROMETRY.

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