dbPTM

RS16_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RS16_HUMAN
UniProt AC	P62249
Protein Name	40S ribosomal protein S16
Gene Name	RPS16
Organism	Homo sapiens (Human).
Sequence Length	146
Subcellular Localization
Protein Description
Protein Sequence	MPSKGPLQSVQVFGRKKTATAVAHCKRGNGLIKVNGRPLEMIEPRTLQYKLLEPVLLLGKERFAGVDIRVRVKGGGHVAQIYAIRQSISKALVAYYQKYVDEASKKEIKDILIQYDRTLLVADPRRCESKKFGGPGARARYQKSYR

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
3	Phosphorylation	-----MPSKGPLQSV -----CCCCCCCCEE	49.28	29632367
4	Methylation	----MPSKGPLQSVQ ----CCCCCCCCEEE	59.69	21671283
4	Sumoylation	----MPSKGPLQSVQ ----CCCCCCCCEEE	59.69	-
4	Ubiquitination	----MPSKGPLQSVQ ----CCCCCCCCEEE	59.69	21890473
4	Malonylation	----MPSKGPLQSVQ ----CCCCCCCCEEE	59.69	26320211
4	2-Hydroxyisobutyrylation	----MPSKGPLQSVQ ----CCCCCCCCEEE	59.69	-
4	Sumoylation	----MPSKGPLQSVQ ----CCCCCCCCEEE	59.69	-
9	Phosphorylation	PSKGPLQSVQVFGRK CCCCCCCEEEEECCC	23.38	30266825
15	Methylation	QSVQVFGRKKTATAV CEEEEECCCCCEEHH	26.32	115492463
20	Phosphorylation	FGRKKTATAVAHCKR ECCCCCEEHHHHCCC	27.22	24888630
25	S-palmitoylation	TATAVAHCKRGNGLI CEEHHHHCCCCCCEE	2.01	21044946
25	S-nitrosylation	TATAVAHCKRGNGLI CEEHHHHCCCCCCEE	2.01	2212679
26	Acetylation	ATAVAHCKRGNGLIK EEHHHHCCCCCCEEE	54.17	25953088
26	2-Hydroxyisobutyrylation	ATAVAHCKRGNGLIK EEHHHHCCCCCCEEE	54.17	-
26	Ubiquitination	ATAVAHCKRGNGLIK EEHHHHCCCCCCEEE	54.17	-
33	Ubiquitination	KRGNGLIKVNGRPLE CCCCCEEEECCEECC	34.39	21906983
33	Acetylation	KRGNGLIKVNGRPLE CCCCCEEEECCEECC	34.39	26051181
41	Sulfoxidation	VNGRPLEMIEPRTLQ ECCEECCCCCCCCHH	5.76	21406390
45	Methylation	PLEMIEPRTLQYKLL ECCCCCCCCHHHHHH	34.97	115492479
50	Ubiquitination	EPRTLQYKLLEPVLL CCCCHHHHHHHHHHH	33.37	21890473
50	Sumoylation	EPRTLQYKLLEPVLL CCCCHHHHHHHHHHH	33.37	-
50	Acetylation	EPRTLQYKLLEPVLL CCCCHHHHHHHHHHH	33.37	25825284
50	2-Hydroxyisobutyrylation	EPRTLQYKLLEPVLL CCCCHHHHHHHHHHH	33.37	-
50	Sumoylation	EPRTLQYKLLEPVLL CCCCHHHHHHHHHHH	33.37	-
60	2-Hydroxyisobutyrylation	EPVLLLGKERFAGVD HHHHHHCCCEECCCE	45.76	-
60	Ubiquitination	EPVLLLGKERFAGVD HHHHHHCCCEECCCE	45.76	21890473
60	Acetylation	EPVLLLGKERFAGVD HHHHHHCCCEECCCE	45.76	19608861
60	Succinylation	EPVLLLGKERFAGVD HHHHHHCCCEECCCE	45.76	23954790
62	Methylation	VLLLGKERFAGVDIR HHHHCCCEECCCEEE	30.15	115492447
69	Methylation	RFAGVDIRVRVKGGG EECCCEEEEEEECCC	13.01	115492455
73	Ubiquitination	VDIRVRVKGGGHVAQ CEEEEEEECCCCHHH	41.07	-
73	Sumoylation	VDIRVRVKGGGHVAQ CEEEEEEECCCCHHH	41.07	-
73	Sumoylation	VDIRVRVKGGGHVAQ CEEEEEEECCCCHHH	41.07	-
82	Phosphorylation	GGHVAQIYAIRQSIS CCCHHHHHHHHHHHH	5.49	20090780
87	Phosphorylation	QIYAIRQSISKALVA HHHHHHHHHHHHHHH	20.98	30622161
89	Phosphorylation	YAIRQSISKALVAYY HHHHHHHHHHHHHHH	19.68	30622161
90	Acetylation	AIRQSISKALVAYYQ HHHHHHHHHHHHHHH	44.03	25953088
90	Ubiquitination	AIRQSISKALVAYYQ HHHHHHHHHHHHHHH	44.03	21890473
90	2-Hydroxyisobutyrylation	AIRQSISKALVAYYQ HHHHHHHHHHHHHHH	44.03	-
95	Phosphorylation	ISKALVAYYQKYVDE HHHHHHHHHHHHCHH	10.03	28152594
96	Phosphorylation	SKALVAYYQKYVDEA HHHHHHHHHHHCHHH	6.70	28152594
98	Acetylation	ALVAYYQKYVDEASK HHHHHHHHHCHHHHH	30.99	21466224
98	Ubiquitination	ALVAYYQKYVDEASK HHHHHHHHHCHHHHH	30.99	21890473
98	2-Hydroxyisobutyrylation	ALVAYYQKYVDEASK HHHHHHHHHCHHHHH	30.99	-
104	O-linked_Glycosylation	QKYVDEASKKEIKDI HHHCHHHHHHHHHHH	42.06	22121020
105	2-Hydroxyisobutyrylation	KYVDEASKKEIKDIL HHCHHHHHHHHHHHH	62.57	-
105	Acetylation	KYVDEASKKEIKDIL HHCHHHHHHHHHHHH	62.57	25953088
105	Sumoylation	KYVDEASKKEIKDIL HHCHHHHHHHHHHHH	62.57	-
105	Sumoylation	KYVDEASKKEIKDIL HHCHHHHHHHHHHHH	62.57	-
105	Ubiquitination	KYVDEASKKEIKDIL HHCHHHHHHHHHHHH	62.57	-
106	Ubiquitination	YVDEASKKEIKDILI HCHHHHHHHHHHHHH	63.28	-
109	Ubiquitination	EASKKEIKDILIQYD HHHHHHHHHHHHHCC	39.55	21890473
109	Succinylation	EASKKEIKDILIQYD HHHHHHHHHHHHHCC	39.55	27452117
109	Acetylation	EASKKEIKDILIQYD HHHHHHHHHHHHHCC	39.55	26822725
109	Sumoylation	EASKKEIKDILIQYD HHHHHHHHHHHHHCC	39.55	-
109	Sumoylation	EASKKEIKDILIQYD HHHHHHHHHHHHHCC	39.55	-
109	2-Hydroxyisobutyrylation	EASKKEIKDILIQYD HHHHHHHHHHHHHCC	39.55	-
115	Nitration	IKDILIQYDRTLLVA HHHHHHHCCCEEEEE	10.61	-
115	Phosphorylation	IKDILIQYDRTLLVA HHHHHHHCCCEEEEE	10.61	28152594
117	Methylation	DILIQYDRTLLVADP HHHHHCCCEEEEECH	23.49	26494265
125	Methylation	TLLVADPRRCESKKF EEEEECHHHCCCCCC	57.33	115492471
129	Phosphorylation	ADPRRCESKKFGGPG ECHHHCCCCCCCCCC	44.78	-
131	2-Hydroxyisobutyrylation	PRRCESKKFGGPGAR HHHCCCCCCCCCCHH	59.53	-
131	Ubiquitination	PRRCESKKFGGPGAR HHHCCCCCCCCCCHH	59.53	-
131	Acetylation	PRRCESKKFGGPGAR HHHCCCCCCCCCCHH	59.53	25953088
143	Sumoylation	GARARYQKSYR---- CHHHHHHHHCC----	40.29	-
143	Sumoylation	GARARYQKSYR---- CHHHHHHHHCC----	40.29	-

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 RS16_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of RS16_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 RS16_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
A4_HUMAN	APP	physical	21832049
RS25_HUMAN	RPS25	physical	22939629
RS19_HUMAN	RPS19	physical	22939629
RS23_HUMAN	RPS23	physical	22939629
RS26_HUMAN	RPS26	physical	22939629
RS28_HUMAN	RPS28	physical	22939629
RS2_HUMAN	RPS2	physical	22939629
RS3A_HUMAN	RPS3A	physical	22939629
RS3_HUMAN	RPS3	physical	22939629
RS4X_HUMAN	RPS4X	physical	22939629
RS5_HUMAN	RPS5	physical	22939629
RS6_HUMAN	RPS6	physical	22939629
RS8_HUMAN	RPS8	physical	22939629
RSSA_HUMAN	RPSA	physical	22939629
RS17_HUMAN	RPS17	physical	22939629
RS24_HUMAN	RPS24	physical	22939629
RS20_HUMAN	RPS20	physical	22939629
RS9_HUMAN	RPS9	physical	22939629
RS7_HUMAN	RPS7	physical	22939629
RS21_HUMAN	RPS21	physical	22939629
RS27A_HUMAN	RPS27A	physical	22939629
UBIM_HUMAN	FAU	physical	22939629
RS29_HUMAN	RPS29	physical	22939629
RS27L_HUMAN	RPS27L	physical	22939629
THIOM_HUMAN	TXN2	physical	22939629
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
RS25_HUMAN	RPS25	physical	22863883
RS27_HUMAN	RPS27	physical	22863883
RS3_HUMAN	RPS3	physical	22863883
RS5_HUMAN	RPS5	physical	22863883
RS6_HUMAN	RPS6	physical	22863883
RS7_HUMAN	RPS7	physical	22863883
RS8_HUMAN	RPS8	physical	22863883
SND1_HUMAN	SND1	physical	22863883
TSR1_HUMAN	TSR1	physical	22863883
VA0D1_HUMAN	ATP6V0D1	physical	26344197
UBIM_HUMAN	FAU	physical	26344197
RL10A_HUMAN	RPL10A	physical	26344197
RL12_HUMAN	RPL12	physical	26344197
RL13_HUMAN	RPL13	physical	26344197
RL13A_HUMAN	RPL13A	physical	26344197
RL18_HUMAN	RPL18	physical	26344197
RL18A_HUMAN	RPL18A	physical	26344197
RL21_HUMAN	RPL21	physical	26344197
RL23_HUMAN	RPL23	physical	26344197
RL24_HUMAN	RPL24	physical	26344197
RL27_HUMAN	RPL27	physical	26344197
RL27A_HUMAN	RPL27A	physical	26344197
RL28_HUMAN	RPL28	physical	26344197
RL30_HUMAN	RPL30	physical	26344197
RL34_HUMAN	RPL34	physical	26344197
RL35_HUMAN	RPL35	physical	26344197
RL35A_HUMAN	RPL35A	physical	26344197
RL36_HUMAN	RPL36	physical	26344197
RL37A_HUMAN	RPL37A	physical	26344197
RL38_HUMAN	RPL38	physical	26344197
RL3L_HUMAN	RPL3L	physical	26344197
RL7A_HUMAN	RPL7A	physical	26344197
RLA2_HUMAN	RPLP2	physical	26344197
RS10_HUMAN	RPS10	physical	26344197
RS11_HUMAN	RPS11	physical	26344197
RS12_HUMAN	RPS12	physical	26344197
RS13_HUMAN	RPS13	physical	26344197
RS14_HUMAN	RPS14	physical	26344197
RS15A_HUMAN	RPS15A	physical	26344197
RS17_HUMAN	RPS17	physical	26344197
RS18_HUMAN	RPS18	physical	26344197
RS19_HUMAN	RPS19	physical	26344197
RS27_HUMAN	RPS27	physical	26344197
RS3_HUMAN	RPS3	physical	26344197
RS4X_HUMAN	RPS4X	physical	26344197
RS6_HUMAN	RPS6	physical	26344197
RS7_HUMAN	RPS7	physical	26344197
RS9_HUMAN	RPS9	physical	26344197
RSSA_HUMAN	RPSA	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 RS16_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-60, AND MASS SPECTROMETRY.	19608861 [Abstract]