dbPTM

RS18_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RS18_HUMAN
UniProt AC	P62269
Protein Name	40S ribosomal protein S18
Gene Name	RPS18
Organism	Homo sapiens (Human).
Sequence Length	152
Subcellular Localization	Cytoplasm.
Protein Description	Located at the top of the head of the 40S subunit, it contacts several helices of the 18S rRNA..
Protein Sequence	MSLVIPEKFQHILRVLNTNIDGRRKIAFAITAIKGVGRRYAHVVLRKADIDLTKRAGELTEDEVERVITIMQNPRQYKIPDWFLNRQKDVKDGKYSQVLANGLDNKLREDLERLKKIRAHRGLRHFWGLRVRGQHTKTTGRRGRTVGVSKKK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MSLVIPEKF ------CCCCCHHHH	31.20	23401153
2	Acetylation	------MSLVIPEKF ------CCCCCHHHH	31.20	19413330
8	Acetylation	MSLVIPEKFQHILRV CCCCCHHHHHHHHHH	44.99	23954790
8	Ubiquitination	MSLVIPEKFQHILRV CCCCCHHHHHHHHHH	44.99	23000965
8	Ubiquitination	MSLVIPEKFQHILRV CCCCCHHHHHHHHHH	44.99	21890473
23	Methylation	LNTNIDGRRKIAFAI HCCCCCCHHHHHHHH	32.73	115492515
25	Ubiquitination	TNIDGRRKIAFAITA CCCCCHHHHHHHHHH	36.71	33845483
25	2-Hydroxyisobutyrylation	TNIDGRRKIAFAITA CCCCCHHHHHHHHHH	36.71	-
25	Acetylation	TNIDGRRKIAFAITA CCCCCHHHHHHHHHH	36.71	26051181
31	Phosphorylation	RKIAFAITAIKGVGR HHHHHHHHHHCCCCH	20.92	20068231
34	Acetylation	AFAITAIKGVGRRYA HHHHHHHCCCCHHHH	45.11	26051181
34	Ubiquitination	AFAITAIKGVGRRYA HHHHHHHCCCCHHHH	45.11	23000965
40	Phosphorylation	IKGVGRRYAHVVLRK HCCCCHHHHHHEEEC	10.33	28152594
46	Methylation	RYAHVVLRKADIDLT HHHHHEEECCCCCCH	22.10	115492525
47	2-Hydroxyisobutyrylation	YAHVVLRKADIDLTK HHHHEEECCCCCCHH	46.37	-
47	Ubiquitination	YAHVVLRKADIDLTK HHHHEEECCCCCCHH	46.37	21906983
54	Ubiquitination	KADIDLTKRAGELTE CCCCCCHHHCCCCCH	47.77	21906983
54	Acetylation	KADIDLTKRAGELTE CCCCCCHHHCCCCCH	47.77	27452117
54	2-Hydroxyisobutyrylation	KADIDLTKRAGELTE CCCCCCHHHCCCCCH	47.77	-
55	Methylation	ADIDLTKRAGELTED CCCCCHHHCCCCCHH	42.46	115492505
60	Phosphorylation	TKRAGELTEDEVERV HHHCCCCCHHHHHHH	36.77	29255136
71	Sulfoxidation	VERVITIMQNPRQYK HHHHHHHCCCCCHHC	2.06	21406390
78	2-Hydroxyisobutyrylation	MQNPRQYKIPDWFLN CCCCCHHCCCHHHHC	39.15	-
78	Acetylation	MQNPRQYKIPDWFLN CCCCCHHCCCHHHHC	39.15	19608861
78	Sumoylation	MQNPRQYKIPDWFLN CCCCCHHCCCHHHHC	39.15	-
78	Ubiquitination	MQNPRQYKIPDWFLN CCCCCHHCCCHHHHC	39.15	23000965
78	Ubiquitination	MQNPRQYKIPDWFLN CCCCCHHCCCHHHHC	39.15	21890473
88	Ubiquitination	DWFLNRQKDVKDGKY HHHHCCCCCCCCCCH	62.34	23000965
91	Ubiquitination	LNRQKDVKDGKYSQV HCCCCCCCCCCHHHH	71.54	23000965
91	Sumoylation	LNRQKDVKDGKYSQV HCCCCCCCCCCHHHH	71.54	28112733
94	Ubiquitination	QKDVKDGKYSQVLAN CCCCCCCCHHHHHHC	52.44	21890473
94	2-Hydroxyisobutyrylation	QKDVKDGKYSQVLAN CCCCCCCCHHHHHHC	52.44	-
94	Ubiquitination	QKDVKDGKYSQVLAN CCCCCCCCHHHHHHC	52.44	23000965
94	Sumoylation	QKDVKDGKYSQVLAN CCCCCCCCHHHHHHC	52.44	28112733
94	Sumoylation	QKDVKDGKYSQVLAN CCCCCCCCHHHHHHC	52.44	-
94	Acetylation	QKDVKDGKYSQVLAN CCCCCCCCHHHHHHC	52.44	19608861
94	Malonylation	QKDVKDGKYSQVLAN CCCCCCCCHHHHHHC	52.44	26320211
95	Phosphorylation	KDVKDGKYSQVLANG CCCCCCCHHHHHHCC	15.18	28152594
96	Phosphorylation	DVKDGKYSQVLANGL CCCCCCHHHHHHCCC	19.80	28152594
106	Ubiquitination	LANGLDNKLREDLER HHCCCCHHHHHHHHH	48.89	21906983
106	Sumoylation	LANGLDNKLREDLER HHCCCCHHHHHHHHH	48.89	28112733
106	Sumoylation	LANGLDNKLREDLER HHCCCCHHHHHHHHH	48.89	-
106	Acetylation	LANGLDNKLREDLER HHCCCCHHHHHHHHH	48.89	19608861
106	Ubiquitination	LANGLDNKLREDLER HHCCCCHHHHHHHHH	48.89	21890473
106	2-Hydroxyisobutyrylation	LANGLDNKLREDLER HHCCCCHHHHHHHHH	48.89	-
113	Methylation	KLREDLERLKKIRAH HHHHHHHHHHHHHHH	60.13	115492495
149	Phosphorylation	RGRTVGVSKKK---- CCCEEEECCCC----	32.59	23312004
150	Acetylation	GRTVGVSKKK----- CCEEEECCCC-----	63.27	25953088
150	2-Hydroxyisobutyrylation	GRTVGVSKKK----- CCEEEECCCC-----	63.27	-
152	Ubiquitination	TVGVSKKK------- EEEECCCC-------	70.12	24816145

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 RS18_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of RS18_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 RS18_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
A4_HUMAN	APP	physical	21832049
VPP3_HUMAN	TCIRG1	physical	22939629
VATD_HUMAN	ATP6V1D	physical	22939629
RT09_HUMAN	MRPS9	physical	22939629
VPP1_HUMAN	ATP6V0A1	physical	22939629
EIF3A_HUMAN	EIF3A	physical	22863883
EIF3E_HUMAN	EIF3E	physical	22863883
RSSA_HUMAN	RPSA	physical	22863883
LARP1_HUMAN	LARP1	physical	22863883
RS10_HUMAN	RPS10	physical	22863883
RS12_HUMAN	RPS12	physical	22863883
RS13_HUMAN	RPS13	physical	22863883
RS14_HUMAN	RPS14	physical	22863883
RS15A_HUMAN	RPS15A	physical	22863883
RS16_HUMAN	RPS16	physical	22863883
RS21_HUMAN	RPS21	physical	22863883
RS25_HUMAN	RPS25	physical	22863883
RS26_HUMAN	RPS26	physical	22863883
RS27_HUMAN	RPS27	physical	22863883
RS28_HUMAN	RPS28	physical	22863883
RS3A_HUMAN	RPS3A	physical	22863883
RS3_HUMAN	RPS3	physical	22863883
RS4X_HUMAN	RPS4X	physical	22863883
RS5_HUMAN	RPS5	physical	22863883
RS6_HUMAN	RPS6	physical	22863883
RS7_HUMAN	RPS7	physical	22863883
RS8_HUMAN	RPS8	physical	22863883
RS9_HUMAN	RPS9	physical	22863883
TSR1_HUMAN	TSR1	physical	22863883
PYM1_HUMAN	WIBG	physical	22863883
RM24_HUMAN	MRPL24	physical	26344197
RT10_HUMAN	MRPS10	physical	26344197
RL10A_HUMAN	RPL10A	physical	26344197
RL26_HUMAN	RPL26	physical	26344197
RL26L_HUMAN	RPL26L1	physical	26344197
RL3_HUMAN	RPL3	physical	26344197
RL31_HUMAN	RPL31	physical	26344197
RL35_HUMAN	RPL35	physical	26344197
RL3L_HUMAN	RPL3L	physical	26344197
RS11_HUMAN	RPS11	physical	26344197
RS26_HUMAN	RPS26	physical	26344197
RS6_HUMAN	RPS6	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 RS18_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"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-8; LYS-78; LYS-94 ANDLYS-106, AND MASS SPECTROMETRY.	19608861 [Abstract]