dbPTM

RL22L_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RL22L_MOUSE
UniProt AC	Q9D7S7
Protein Name	60S ribosomal protein L22-like 1
Gene Name	Rpl22l1
Organism	Mus musculus (Mouse).
Sequence Length	122
Subcellular Localization
Protein Description
Protein Sequence	MAPQKDKKPKKSTWRFHLDLTHPVEDGIFDSGNFEQFLREKVKVNGKTGNLGNVVHIERLKNKITVVSEKQFSKRYLKYLTKKYLKKNNLRDWLRVVASDKETYELRYFQISQDEDGSESED

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
47	Ubiquitination	EKVKVNGKTGNLGNV HHHEECCCCCCCCCE	48.32	-
70	Acetylation	KITVVSEKQFSKRYL CEEEEEHHHHHHHHH	49.49	22826441
108	Phosphorylation	KETYELRYFQISQDE CCEEEEEEEEEECCC	16.68	25619855
112	Phosphorylation	ELRYFQISQDEDGSE EEEEEEEECCCCCCC	22.31	24925903
118	Phosphorylation	ISQDEDGSESED--- EECCCCCCCCCC---	50.72	24925903
120	Phosphorylation	QDEDGSESED----- CCCCCCCCCC-----	49.08	25521595

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 RL22L_MOUSE !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of RL22L_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 RL22L_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of RL22L_MOUSE !!

Drug and Disease Associations

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

Regulatory Network of RL22L_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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-118 AND SER-120, ANDMASS SPECTROMETRY.	19144319 [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-118 AND SER-120, 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-118 AND SER-120, ANDMASS SPECTROMETRY.	17622165 [Abstract]
"Phosphoproteomic analysis of the developing mouse brain."; Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.; Mol. Cell. Proteomics 3:1093-1101(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-118, AND MASSSPECTROMETRY.	15345747 [Abstract]