RS17_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: RS17_HUMAN
• UniProt AC: P08708
• Protein Name: 40S ribosomal protein S17 {ECO:0000305}
• Gene Name: RPS17 {ECO:0000312|HGNC:HGNC:10397}
• Organism: Homo sapiens (Human).
• Sequence Length: 135
• Protein Sequence: MGRVRTKTVKKAARVIIEKYYTRLGNDFHTNKRVCEEIAIIPSKKLRNKIAGYVTHLMKRIQRGPVRGISIKLQEEERERRDNYVPEVSALDQEIIEVDPDTKEMLKLLDFGSLSNLQVTQPTVGMNFKTPRGPV

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
11	Ubiquitination	VRTKTVKKAARVIIE CCHHHHHHHHHHHHH	42.83	24816145
19	Succinylation	AARVIIEKYYTRLGN HHHHHHHHHHHHHCC	32.90	-
19	Ubiquitination	AARVIIEKYYTRLGN HHHHHHHHHHHHHCC	32.90	23000965
19	Acetylation	AARVIIEKYYTRLGN HHHHHHHHHHHHHCC	32.90	23954790
19	Succinylation	AARVIIEKYYTRLGN HHHHHHHHHHHHHCC	32.90	27452117
19	Ubiquitination	AARVIIEKYYTRLGN HHHHHHHHHHHHHCC	32.90	21906983
20	Phosphorylation	ARVIIEKYYTRLGND HHHHHHHHHHHHCCC	9.40	23882029
21	Phosphorylation	RVIIEKYYTRLGNDF HHHHHHHHHHHCCCC	9.10	22817900
22	Phosphorylation	VIIEKYYTRLGNDFH HHHHHHHHHHCCCCC	19.14	28851738
23	Methylation	IIEKYYTRLGNDFHT HHHHHHHHHCCCCCC	25.20	115492487
32	Acetylation	GNDFHTNKRVCEEIA CCCCCCCCCHHHEEE	47.57	25953088
32	Ubiquitination	GNDFHTNKRVCEEIA CCCCCCCCCHHHEEE	47.57	21963094
32	Ubiquitination	GNDFHTNKRVCEEIA CCCCCCCCCHHHEEE	47.57	-
35	S-palmitoylation	FHTNKRVCEEIAIIP CCCCCCHHHEEEEEC	4.51	26865113
35	S-nitrosylation	FHTNKRVCEEIAIIP CCCCCCHHHEEEEEC	4.51	2212679
35	Glutathionylation	FHTNKRVCEEIAIIP CCCCCCHHHEEEEEC	4.51	22555962
43	Phosphorylation	EEIAIIPSKKLRNKI HEEEEECCHHHHHHH	31.82	22210691
44	Ubiquitination	EIAIIPSKKLRNKIA EEEEECCHHHHHHHH	50.93	23000965
44	Acetylation	EIAIIPSKKLRNKIA EEEEECCHHHHHHHH	50.93	25953088
44	Ubiquitination	EIAIIPSKKLRNKIA EEEEECCHHHHHHHH	50.93	2190698
45	Ubiquitination	IAIIPSKKLRNKIAG EEEECCHHHHHHHHH	57.95	23000965
49	Acetylation	PSKKLRNKIAGYVTH CCHHHHHHHHHHHHH	27.74	25825284
49	Ubiquitination	PSKKLRNKIAGYVTH CCHHHHHHHHHHHHH	27.74	23000965
49	Ubiquitination	PSKKLRNKIAGYVTH CCHHHHHHHHHHHHH	27.74	21906983
53	Phosphorylation	LRNKIAGYVTHLMKR HHHHHHHHHHHHHHH	7.98	27273156
55	Phosphorylation	NKIAGYVTHLMKRIQ HHHHHHHHHHHHHHH	10.78	28152594
58	Sulfoxidation	AGYVTHLMKRIQRGP HHHHHHHHHHHHCCC	1.81	30846556
59	Acetylation	GYVTHLMKRIQRGPV HHHHHHHHHHHCCCC	53.35	26051181
59	Ubiquitination	GYVTHLMKRIQRGPV HHHHHHHHHHHCCCC	53.35	-
59	Ubiquitination	GYVTHLMKRIQRGPV HHHHHHHHHHHCCCC	53.35	23000965
70	Phosphorylation	RGPVRGISIKLQEEE CCCCCCEEEECCHHH	19.25	28450419
72	Ubiquitination	PVRGISIKLQEEERE CCCCEEEECCHHHHH	37.01	23000965
72	Ubiquitination	PVRGISIKLQEEERE CCCCEEEECCHHHHH	37.01	-
72	Acetylation	PVRGISIKLQEEERE CCCCEEEECCHHHHH	37.01	25953088
84	Phosphorylation	ERERRDNYVPEVSAL HHHHHHCCCCCHHHH	22.98	29523821
89	Phosphorylation	DNYVPEVSALDQEII HCCCCCHHHHCHHHE	22.81	29523821
102	Phosphorylation	IIEVDPDTKEMLKLL HEEECCCHHHHHHHH	34.00	21712546
103	Neddylation	IEVDPDTKEMLKLLD EEECCCHHHHHHHHH	48.81	32015554
103	Acetylation	IEVDPDTKEMLKLLD EEECCCHHHHHHHHH	48.81	66696585
103	Sumoylation	IEVDPDTKEMLKLLD EEECCCHHHHHHHHH	48.81	25114211
103	Ubiquitination	IEVDPDTKEMLKLLD EEECCCHHHHHHHHH	48.81	23000965
103	Ubiquitination	IEVDPDTKEMLKLLD EEECCCHHHHHHHHH	48.81	21906983
105	Sulfoxidation	VDPDTKEMLKLLDFG ECCCHHHHHHHHHHH	4.22	30846556
107	Neddylation	PDTKEMLKLLDFGSL CCHHHHHHHHHHHCC	45.77	32015554
107	Ubiquitination	PDTKEMLKLLDFGSL CCHHHHHHHHHHHCC	45.77	-
107	Ubiquitination	PDTKEMLKLLDFGSL CCHHHHHHHHHHHCC	45.77	23000965
113	Phosphorylation	LKLLDFGSLSNLQVT HHHHHHHCCCCCEEC	28.72	18669648
113	Phosphorylation	LKLLDFGSLSNLQVT HHHHHHHCCCCCEEC	28.72	29255136
115	Phosphorylation	LLDFGSLSNLQVTQP HHHHHCCCCCEECCC	36.87	29255136
120	Phosphorylation	SLSNLQVTQPTVGMN CCCCCEECCCCCCCC	18.83	28176443
123	Phosphorylation	NLQVTQPTVGMNFKT CCEECCCCCCCCCCC	21.63	28176443
126	Sulfoxidation	VTQPTVGMNFKTPRG ECCCCCCCCCCCCCC	4.66	28465586
129	Acetylation	PTVGMNFKTPRGPV- CCCCCCCCCCCCCC-	53.25	26051181
129	Methylation	PTVGMNFKTPRGPV- CCCCCCCCCCCCCC-	53.25	24469415
129	Ubiquitination	PTVGMNFKTPRGPV- CCCCCCCCCCCCCC-	53.25	23000965
129	Ubiquitination	PTVGMNFKTPRGPV- CCCCCCCCCCCCCC-	53.25	-
130	Phosphorylation	TVGMNFKTPRGPV-- CCCCCCCCCCCCC--	17.68	25159151
130	Phosphorylation	TVGMNFKTPRGPV-- CCCCCCCCCCCCC--	17.68	18669648

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

Oops, there are no upstream regulatory protein records of RS17_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of RS17_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 RS17_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RS24_HUMAN	RPS24	physical	22939629
RSSA_HUMAN	RPSA	physical	22939629
RS23_HUMAN	RPS23	physical	22939629
RS2_HUMAN	RPS2	physical	22939629
RS26_HUMAN	RPS26	physical	22939629
RS28_HUMAN	RPS28	physical	22939629
RS9_HUMAN	RPS9	physical	22939629
RS8_HUMAN	RPS8	physical	22939629
RS7_HUMAN	RPS7	physical	22939629
RS3A_HUMAN	RPS3A	physical	22939629
RS25_HUMAN	RPS25	physical	22939629
RS3_HUMAN	RPS3	physical	22939629
RS4X_HUMAN	RPS4X	physical	22939629
RS6_HUMAN	RPS6	physical	22939629
RS21_HUMAN	RPS21	physical	22939629
UBIM_HUMAN	FAU	physical	22939629
RS29_HUMAN	RPS29	physical	22939629
RS11_HUMAN	RPS11	physical	22863883
RS3_HUMAN	RPS3	physical	22863883
RL23A_HUMAN	RPL23A	physical	26344197
RL4_HUMAN	RPL4	physical	26344197
RLA0_HUMAN	RPLP0	physical	26344197

Drug and Disease Associations

• Kegg Disease
• There are no disease associations of PTM sites.
• OMIM Disease
• 612527: Diamond-Blackfan anemia 4 (DBA4)
• 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

Acetylation

"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-19, AND MASS SPECTROMETRY.
PubMed: 19608861

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-113, 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-113, AND MASSSPECTROMETRY.
PubMed: 19369195

"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-113 AND THR-130, ANDMASS SPECTROMETRY.
PubMed: 18669648