RLA2_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: RLA2_MOUSE
• UniProt AC: P99027
• Protein Name: 60S acidic ribosomal protein P2
• Gene Name: Rplp2
• Organism: Mus musculus (Mouse).
• Sequence Length: 115
• Protein Description: Plays an important role in the elongation step of protein synthesis..
• Protein Sequence: MRYVASYLLAALGGNSSPSAKDIKKILDSVGIEADDDRLNKVISELNGKNIEDVIAQGVGKLASVPAGGAVAVSAAPGSAAPAAGSAPAAAEEKKDEKKEESEESDDDMGFGLFD

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
1	Acetylation	-------MRYVASYL -------CHHHHHHH	6.69	-
3	Phosphorylation	-----MRYVASYLLA -----CHHHHHHHHH	10.08	26239621
6	Phosphorylation	--MRYVASYLLAALG --CHHHHHHHHHHHC	13.28	24068923
7	Phosphorylation	-MRYVASYLLAALGG -CHHHHHHHHHHHCC	8.94	22817900
16	Phosphorylation	LAALGGNSSPSAKDI HHHHCCCCCCCHHHH	47.07	24925903
17	Phosphorylation	AALGGNSSPSAKDIK HHHCCCCCCCHHHHH	27.20	24925903
19	Phosphorylation	LGGNSSPSAKDIKKI HCCCCCCCHHHHHHH	50.31	24925903
21	Acetylation	GNSSPSAKDIKKILD CCCCCCHHHHHHHHH	65.41	23806337
21	Succinylation	GNSSPSAKDIKKILD CCCCCCHHHHHHHHH	65.41	-
21	Ubiquitination	GNSSPSAKDIKKILD CCCCCCHHHHHHHHH	65.41	-
21	Succinylation	GNSSPSAKDIKKILD CCCCCCHHHHHHHHH	65.41	23806337
21	Malonylation	GNSSPSAKDIKKILD CCCCCCHHHHHHHHH	65.41	26073543
24	Ubiquitination	SPSAKDIKKILDSVG CCCHHHHHHHHHHHC	43.84	-
24	Acetylation	SPSAKDIKKILDSVG CCCHHHHHHHHHHHC	43.84	23864654
25	Ubiquitination	PSAKDIKKILDSVGI CCHHHHHHHHHHHCC	49.16	-
25	Malonylation	PSAKDIKKILDSVGI CCHHHHHHHHHHHCC	49.16	26320211
41	Ubiquitination	ADDDRLNKVISELNG CCHHHHHHHHHHHCC	45.60	22790023
41	Acetylation	ADDDRLNKVISELNG CCHHHHHHHHHHHCC	45.60	23864654
44	Phosphorylation	DRLNKVISELNGKNI HHHHHHHHHHCCCCH	38.73	25338131
49	Ubiquitination	VISELNGKNIEDVIA HHHHHCCCCHHHHHH	54.39	22790023
49	Acetylation	VISELNGKNIEDVIA HHHHHCCCCHHHHHH	54.39	23201123
61	Ubiquitination	VIAQGVGKLASVPAG HHHHCCCHHHCCCCC	38.17	-
64	Phosphorylation	QGVGKLASVPAGGAV HCCCHHHCCCCCCEE	38.78	22942356
74	O-linked_Glycosylation	AGGAVAVSAAPGSAA CCCEEEEEECCCCCC	14.69	22517741
74	Phosphorylation	AGGAVAVSAAPGSAA CCCEEEEEECCCCCC	14.69	23984901
79	Phosphorylation	AVSAAPGSAAPAAGS EEEECCCCCCCCCCC	21.87	25521595
86	Phosphorylation	SAAPAAGSAPAAAEE CCCCCCCCCCHHHHH	26.76	26824392
94	Malonylation	APAAAEEKKDEKKEE CCHHHHHHHHHHHHH	57.96	26320211
98	Ubiquitination	AEEKKDEKKEESEES HHHHHHHHHHHCCCC	75.51	-
102	Phosphorylation	KDEKKEESEESDDDM HHHHHHHCCCCCCCC	47.99	24925903
105	Phosphorylation	KKEESEESDDDMGFG HHHHCCCCCCCCCCC	42.14	24925903

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of RLA2_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of RLA2_MOUSE !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of RLA2_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of RLA2_MOUSE !!

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Phosphorylation

"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-17; SER-102 AND SER-105,AND MASS SPECTROMETRY.
PubMed: 19131326

"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-102 AND SER-105, ANDMASS SPECTROMETRY.
PubMed: 19144319

"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-102 AND SER-105, ANDMASS SPECTROMETRY.
PubMed: 19367708

"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-102 AND SER-105, ANDMASS SPECTROMETRY.
PubMed: 18630941

"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-102 AND SER-105, ANDMASS SPECTROMETRY.
PubMed: 17242355

"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-102 AND SER-105, ANDMASS SPECTROMETRY.
PubMed: 17622165

"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-102 AND SER-105, ANDMASS SPECTROMETRY.
PubMed: 17203969

"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-102 AND SER-105, ANDMASS SPECTROMETRY.
PubMed: 14729942