dbPTM

RLA1_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RLA1_MOUSE
UniProt AC	P47955
Protein Name	60S acidic ribosomal protein P1
Gene Name	Rplp1
Organism	Mus musculus (Mouse).
Sequence Length	114
Subcellular Localization
Protein Description	Plays an important role in the elongation step of protein synthesis..
Protein Sequence	MASVSELACIYSALILHDDEVTVTEDKINALIKAAGVSVEPFWPGLFAKALANVNIGSLICNVGAGGPAPAAGAAPAGGAAPSTAAAPAEEKKVEAKKEESEESEDDMGFGLFD

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MASVSELAC ------CCCHHHHHH	20.74	-
3	Phosphorylation	-----MASVSELACI -----CCCHHHHHHH	25.52	26643407
5	Phosphorylation	---MASVSELACIYS ---CCCHHHHHHHHH	25.13	26643407
12	Phosphorylation	SELACIYSALILHDD HHHHHHHHHHHCCCC	9.18	30387612
22	Phosphorylation	ILHDDEVTVTEDKIN HCCCCCCCCCHHHHH	21.47	30352176
38	Phosphorylation	LIKAAGVSVEPFWPG HHHHHCCCCCCCCHH	21.61	26745281
58	Phosphorylation	LANVNIGSLICNVGA HHCCCCCCEEECCCC	15.68	23140645
61	S-nitrosocysteine	VNIGSLICNVGAGGP CCCCCEEECCCCCCC	4.02	-
61	Glutathionylation	VNIGSLICNVGAGGP CCCCCEEECCCCCCC	4.02	24333276
61	S-nitrosylation	VNIGSLICNVGAGGP CCCCCEEECCCCCCC	4.02	22178444
61	S-palmitoylation	VNIGSLICNVGAGGP CCCCCEEECCCCCCC	4.02	28526873
83	Phosphorylation	PAGGAAPSTAAAPAE CCCCCCCCCCCCCHH	26.42	23649490
84	Phosphorylation	AGGAAPSTAAAPAEE CCCCCCCCCCCCHHH	21.18	23140645
101	Phosphorylation	VEAKKEESEESEDDM HHHHHHHCCCCCCCC	47.99	24925903
104	Phosphorylation	KKEESEESEDDMGFG HHHHCCCCCCCCCCC	42.12	24925903

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 RLA1_MOUSE !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of RLA1_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 RLA1_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of RLA1_MOUSE !!

Drug and Disease Associations

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

Regulatory Network of RLA1_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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-101 AND SER-104, ANDMASS SPECTROMETRY.	19131326 [Abstract]
"The phagosomal proteome in interferon-gamma-activated macrophages."; Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,Thibault P.; Immunity 30:143-154(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-101 AND SER-104, ANDMASS SPECTROMETRY.	19144319 [Abstract]
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry."; Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.; J. Proteome Res. 7:5314-5326(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-101 AND SER-104, ANDMASS SPECTROMETRY.	19367708 [Abstract]
"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-101 AND SER-104, ANDMASS SPECTROMETRY.	18630941 [Abstract]
"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-101 AND SER-104, ANDMASS SPECTROMETRY.	17242355 [Abstract]
"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-101 AND SER-104, ANDMASS SPECTROMETRY.	17622165 [Abstract]
"Protein phosphorylation and expression profiling by Yin-yangmultidimensional liquid chromatography (Yin-yang MDLC) massspectrometry."; Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.; J. Proteome Res. 6:250-262(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-101 AND SER-104, ANDMASS SPECTROMETRY.	17203969 [Abstract]
"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-101 AND SER-104, ANDMASS SPECTROMETRY.	14729942 [Abstract]