RL22L_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: RL22L_HUMAN
• UniProt AC: Q6P5R6
• Protein Name: 60S ribosomal protein L22-like 1
• Gene Name: RPL22L1
• Organism: Homo sapiens (Human).
• Sequence Length: 122
• Protein Sequence: MAPQKDRKPKRSTWRFNLDLTHPVEDGIFDSGNFEQFLREKVKVNGKTGNLGNVVHIERFKNKITVVSEKQFSKRYLKYLTKKYLKKNNLRDWLRVVASDKETYELRYFQISQDEDESESED

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
47	Ubiquitination	EKVKVNGKTGNLGNV HHHEECCCCCCCCCE	48.32	21906983
65	Phosphorylation	ERFKNKITVVSEKQF EEECCCEEEEEHHHH	19.23	21406692
68	Phosphorylation	KNKITVVSEKQFSKR CCCEEEEEHHHHHHH	34.44	21406692
70	Acetylation	KITVVSEKQFSKRYL CEEEEEHHHHHHHHH	49.49	23236377
70	Ubiquitination	KITVVSEKQFSKRYL CEEEEEHHHHHHHHH	49.49	-
74	Acetylation	VSEKQFSKRYLKYLT EEHHHHHHHHHHHHH	46.48	7976705
78	Acetylation	QFSKRYLKYLTKKYL HHHHHHHHHHHHHHH	29.31	24588809
78	Ubiquitination	QFSKRYLKYLTKKYL HHHHHHHHHHHHHHH	29.31	21890473
99	Phosphorylation	DWLRVVASDKETYEL HHHHHHHCCCCEEEE	37.29	26074081
101	Acetylation	LRVVASDKETYELRY HHHHHCCCCEEEEEE	49.84	26051181
101	Ubiquitination	LRVVASDKETYELRY HHHHHCCCCEEEEEE	49.84	2190698
103	Phosphorylation	VVASDKETYELRYFQ HHHCCCCEEEEEEEE	28.21	26074081
104	Phosphorylation	VASDKETYELRYFQI HHCCCCEEEEEEEEE	17.66	28152594
108	Phosphorylation	KETYELRYFQISQDE CCEEEEEEEEEECCC	16.68	23403867
112	Phosphorylation	ELRYFQISQDEDESE EEEEEEEECCCCCCC	22.31	28176443
118	Phosphorylation	ISQDEDESESED--- EECCCCCCCCCC---	59.76	25159151
120	Phosphorylation	QDEDESESED----- CCCCCCCCCC-----	57.24	30266825

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

Oops, there are no upstream regulatory protein records of RL22L_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of RL22L_HUMAN !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of RL22L_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
FP100_HUMAN	C17orf70	physical	26186194
T3HPD_HUMAN	L3HYPDH	physical	26186194
VMAC_HUMAN	VMAC	physical	26186194
MDM2_HUMAN	MDM2	physical	26186194
CC85B_HUMAN	CCDC85B	physical	26186194
VMAC_HUMAN	VMAC	physical	28514442
FP100_HUMAN	C17orf70	physical	28514442
CC85B_HUMAN	CCDC85B	physical	28514442
T3HPD_HUMAN	L3HYPDH	physical	28514442

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Phosphorylation

"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-118, AND MASSSPECTROMETRY.
PubMed: 19690332

"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-118 AND SER-120, ANDMASS SPECTROMETRY.
PubMed: 19369195

"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-118, AND MASSSPECTROMETRY.
PubMed: 19413330

"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-118 AND SER-120, ANDMASS SPECTROMETRY.
PubMed: 18669648

"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry.";
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-120, AND MASSSPECTROMETRY.
PubMed: 17287340