dbPTM

RS15_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RS15_HUMAN
UniProt AC	P62841
Protein Name	40S ribosomal protein S15
Gene Name	RPS15
Organism	Homo sapiens (Human).
Sequence Length	145
Subcellular Localization
Protein Description
Protein Sequence	MAEVEQKKKRTFRKFTYRGVDLDQLLDMSYEQLMQLYSARQRRRLNRGLRRKQHSLLKRLRKAKKEAPPMEKPEVVKTHLRDMIILPEMVGSMVGVYNGKTFNQVEIKPEMIGHYLGEFSITYKPVKHGRPGIGATHSSRFIPLK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAEVEQKKK ------CCCHHHHHH	29.55	22814378
7	Ubiquitination	-MAEVEQKKKRTFRK -CCCHHHHHHHHHHC	46.91	-
7	Malonylation	-MAEVEQKKKRTFRK -CCCHHHHHHHHHHC	46.91	26320211
9	Ubiquitination	AEVEQKKKRTFRKFT CCHHHHHHHHHHCHH	64.80	-
11	Phosphorylation	VEQKKKRTFRKFTYR HHHHHHHHHHCHHHC	36.35	-
17	Phosphorylation	RTFRKFTYRGVDLDQ HHHHCHHHCCCCHHH	14.43	24248375
28	Sulfoxidation	DLDQLLDMSYEQLMQ CHHHHHCCCHHHHHH	4.66	30846556
29	Phosphorylation	LDQLLDMSYEQLMQL HHHHHCCCHHHHHHH	25.78	20873877
30	Phosphorylation	DQLLDMSYEQLMQLY HHHHCCCHHHHHHHH	10.89	28464451
34	Sulfoxidation	DMSYEQLMQLYSARQ CCCHHHHHHHHHHHH	2.29	30846556
52	2-Hydroxyisobutyrylation	LNRGLRRKQHSLLKR HHHHHHHHHHHHHHH	46.02	-
55	Phosphorylation	GLRRKQHSLLKRLRK HHHHHHHHHHHHHHH	32.67	20068231
58	Acetylation	RKQHSLLKRLRKAKK HHHHHHHHHHHHHHH	55.47	25953088
58	Ubiquitination	RKQHSLLKRLRKAKK HHHHHHHHHHHHHHH	55.47	-
65	Acetylation	KRLRKAKKEAPPMEK HHHHHHHHHCCCCCC	65.06	26051181
65	2-Hydroxyisobutyrylation	KRLRKAKKEAPPMEK HHHHHHHHHCCCCCC	65.06	-
65	Ubiquitination	KRLRKAKKEAPPMEK HHHHHHHHHCCCCCC	65.06	21890473
70	Sulfoxidation	AKKEAPPMEKPEVVK HHHHCCCCCCCHHHH	11.42	21406390
72	Acetylation	KEAPPMEKPEVVKTH HHCCCCCCCHHHHHH	39.98	23236377
72	2-Hydroxyisobutyrylation	KEAPPMEKPEVVKTH HHCCCCCCCHHHHHH	39.98	-
72	Ubiquitination	KEAPPMEKPEVVKTH HHCCCCCCCHHHHHH	39.98	-
77	Acetylation	MEKPEVVKTHLRDMI CCCCHHHHHHHHHHH	35.09	25953088
77	Ubiquitination	MEKPEVVKTHLRDMI CCCCHHHHHHHHHHH	35.09	21890473
78	Phosphorylation	EKPEVVKTHLRDMII CCCHHHHHHHHHHHH	17.96	28674151
83	Sulfoxidation	VKTHLRDMIILPEMV HHHHHHHHHHCHHHH	1.33	28183972
89	Sulfoxidation	DMIILPEMVGSMVGV HHHHCHHHHCCEEEE	3.80	28183972
92	Phosphorylation	ILPEMVGSMVGVYNG HCHHHHCCEEEEECC	10.01	20068231
97	Phosphorylation	VGSMVGVYNGKTFNQ HCCEEEEECCEEECE	16.57	20068231
101	Phosphorylation	VGVYNGKTFNQVEIK EEEECCEEECEEEEC	29.26	20860994
108	Acetylation	TFNQVEIKPEMIGHY EECEEEECHHHHHHE	22.78	26051181
108	Sumoylation	TFNQVEIKPEMIGHY EECEEEECHHHHHHE	22.78	28112733
124	Ubiquitination	GEFSITYKPVKHGRP EEEEEEEEECCCCCC	34.38	-
136	Phosphorylation	GRPGIGATHSSRFIP CCCCCCCCCCCCCCC	19.65	21406692
138	Phosphorylation	PGIGATHSSRFIPLK CCCCCCCCCCCCCCC	20.89	20068231
139	Phosphorylation	GIGATHSSRFIPLK- CCCCCCCCCCCCCC-	24.49	21406692

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
136	T	Phosphorylation	Kinase	LRRK2	Q5S007	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of RS15_HUMAN !!

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 RS15_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RS18_HUMAN	RPS18	physical	22939629
RS7_HUMAN	RPS7	physical	22939629
RSSA_HUMAN	RPSA	physical	22939629
RS2_HUMAN	RPS2	physical	22939629
RS19_HUMAN	RPS19	physical	22939629
RS16_HUMAN	RPS16	physical	22939629
RS17_HUMAN	RPS17	physical	22939629
RS23_HUMAN	RPS23	physical	22939629
RS6_HUMAN	RPS6	physical	22939629
RS3A_HUMAN	RPS3A	physical	22939629
RS26_HUMAN	RPS26	physical	22939629
RS24_HUMAN	RPS24	physical	22939629
RS25_HUMAN	RPS25	physical	22939629
RS3_HUMAN	RPS3	physical	22939629
RS28_HUMAN	RPS28	physical	22939629
RS29_HUMAN	RPS29	physical	22939629
STT3B_HUMAN	STT3B	physical	22939629
VATD_HUMAN	ATP6V1D	physical	22939629
VPP2_HUMAN	ATP6V0A2	physical	22939629
VPP1_HUMAN	ATP6V0A1	physical	22939629
VPP3_HUMAN	TCIRG1	physical	22939629
MDM2_HUMAN	MDM2	physical	23874713
MDM4_HUMAN	MDM4	physical	23874713
SERC3_HUMAN	SERINC3	physical	21988832
RS10_HUMAN	RPS10	physical	22863883
RS17_HUMAN	RPS17	physical	22863883
RS19_HUMAN	RPS19	physical	22863883
RS25_HUMAN	RPS25	physical	22863883
RS29_HUMAN	RPS29	physical	22863883
RS2_HUMAN	RPS2	physical	22863883
RS9_HUMAN	RPS9	physical	22863883
G2E3_HUMAN	G2E3	physical	25416956
RM14_HUMAN	MRPL14	physical	26344197
RNPS1_HUMAN	RNPS1	physical	26344197
RL11_HUMAN	RPL11	physical	26344197
RL15_HUMAN	RPL15	physical	26344197
RL18A_HUMAN	RPL18A	physical	26344197
RL27_HUMAN	RPL27	physical	26344197
RL27A_HUMAN	RPL27A	physical	26344197
RL28_HUMAN	RPL28	physical	26344197
RL30_HUMAN	RPL30	physical	26344197
RL31_HUMAN	RPL31	physical	26344197
RL32_HUMAN	RPL32	physical	26344197
RL35A_HUMAN	RPL35A	physical	26344197
RL36_HUMAN	RPL36	physical	26344197
RL36L_HUMAN	RPL36AL	physical	26344197
RL37_HUMAN	RPL37	physical	26344197
RL37A_HUMAN	RPL37A	physical	26344197
RL5_HUMAN	RPL5	physical	26344197
RL7_HUMAN	RPL7	physical	26344197
RS11_HUMAN	RPS11	physical	26344197
RS16_HUMAN	RPS16	physical	26344197
RS18_HUMAN	RPS18	physical	26344197
RS25_HUMAN	RPS25	physical	26344197
RS27_HUMAN	RPS27	physical	26344197
RS6_HUMAN	RPS6	physical	26344197
RS7_HUMAN	RPS7	physical	26344197
RS8_HUMAN	RPS8	physical	26344197
RS9_HUMAN	RPS9	physical	26344197
S61A1_HUMAN	SEC61A1	physical	26344197

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.

Regulatory Network of RS15_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.	19413330 [Abstract]