dbPTM

RLA2_RAT - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RLA2_RAT
UniProt AC	P02401
Protein Name	60S acidic ribosomal protein P2
Gene Name	Rplp2
Organism	Rattus norvegicus (Rat).
Sequence Length	115
Subcellular Localization
Protein Description	Plays an important role in the elongation step of protein synthesis..
Protein Sequence	MRYVASYLLAALGGNSNPSAKDIKKILDSVGIEADDERLNKVISELNGKNIEDVIAQGVGKLASVPAGGAVAVSAAPGSAAPAAGSAPAAAEEKKDEKKEESEESDDDMGFGLFD

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MRYVASYL -------CHHHHHHH	6.69	-
6	Phosphorylation	--MRYVASYLLAALG --CHHHHHHHHHHHC	13.28	23984901
7	Phosphorylation	-MRYVASYLLAALGG -CHHHHHHHHHHHCC	8.94	23984901
16	Phosphorylation	LAALGGNSNPSAKDI HHHHCCCCCCCHHHH	54.08	27097102
19	Phosphorylation	LGGNSNPSAKDIKKI HCCCCCCCHHHHHHH	52.80	27097102
21	Acetylation	GNSNPSAKDIKKILD CCCCCCHHHHHHHHH	65.41	25786129
21	Succinylation	GNSNPSAKDIKKILD CCCCCCHHHHHHHHH	65.41	-
21	Succinylation	GNSNPSAKDIKKILD CCCCCCHHHHHHHHH	65.41	-
25	Acetylation	PSAKDIKKILDSVGI CCHHHHHHHHHHHCC	49.16	22902405
41	Acetylation	ADDERLNKVISELNG CCHHHHHHHHHHHCC	45.60	22902405
49	Acetylation	VISELNGKNIEDVIA HHHHHCCCCHHHHHH	54.39	22902405
61	Acetylation	VIAQGVGKLASVPAG HHHHCCCHHHCCCCC	38.17	22902405
64	Phosphorylation	QGVGKLASVPAGGAV HCCCHHHCCCCCCEE	38.78	23984901
74	Phosphorylation	AGGAVAVSAAPGSAA CCCEEEEEECCCCCC	14.69	23984901
79	Phosphorylation	AVSAAPGSAAPAAGS EEEECCCCCCCCCCC	21.87	29779826
86	Phosphorylation	SAAPAAGSAPAAAEE CCCCCCCCCCHHHHH	26.76	27097102
94	Acetylation	APAAAEEKKDEKKEE CCHHHHHHHHHHHHH	57.96	22902405
102	Phosphorylation	KDEKKEESEESDDDM HHHHHHHCCCCCCCC	47.99	19700791
105	Phosphorylation	KKEESEESDDDMGFG HHHHCCCCCCCCCCC	42.14	19700791

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
102	S	Phosphorylation	Kinase	GRK2	P25098	PSP
105	S	Phosphorylation	Kinase	GRK2	P25098	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of RLA2_RAT !!

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 RLA2_RAT !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of RLA2_RAT !!

Drug and Disease Associations

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

Regulatory Network of RLA2_RAT

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Quantitative phosphoproteomics of vasopressin-sensitive renal cells:regulation of aquaporin-2 phosphorylation at two sites."; Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.; Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102 AND SER-105, ANDMASS SPECTROMETRY.	16641100 [Abstract]
"Phosphoproteomic analysis of rat liver by high capacity IMAC and LC-MS/MS."; Moser K., White F.M.; J. Proteome Res. 5:98-104(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102 AND SER-105, ANDMASS SPECTROMETRY.	16396499 [Abstract]