dbPTM

RS11_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RS11_HUMAN
UniProt AC	P62280
Protein Name	40S ribosomal protein S11
Gene Name	RPS11
Organism	Homo sapiens (Human).
Sequence Length	158
Subcellular Localization
Protein Description
Protein Sequence	MADIQTERAYQKQPTIFQNKKRVLLGETGKEKLPRYYKNIGLGFKTPKEAIEGTYIDKKCPFTGNVSIRGRILSGVVTKMKMQRTIVIRRDYLHYIRKYNRFEKRHKNMSVHLSPCFRDVQIGDIVTVGECRPLSKTVRFNVLKVTKAAGTKKQFQKF

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MADIQTERA ------CCCHHHHHH	23.71	22223895
6	Phosphorylation	--MADIQTERAYQKQ --CCCHHHHHHHHHC	27.98	28509920
10	Phosphorylation	DIQTERAYQKQPTIF CHHHHHHHHHCCCHH	23.59	28152594
12	Sumoylation	QTERAYQKQPTIFQN HHHHHHHHCCCHHHC	45.64	-
12	Ubiquitination	QTERAYQKQPTIFQN HHHHHHHHCCCHHHC	45.64	22817900
12	Sumoylation	QTERAYQKQPTIFQN HHHHHHHHCCCHHHC	45.64	-
12	Acetylation	QTERAYQKQPTIFQN HHHHHHHHCCCHHHC	45.64	25953088
12	2-Hydroxyisobutyrylation	QTERAYQKQPTIFQN HHHHHHHHCCCHHHC	45.64	-
15	Phosphorylation	RAYQKQPTIFQNKKR HHHHHCCCHHHCCCE	31.75	20068231
20	Ubiquitination	QPTIFQNKKRVLLGE CCCHHHCCCEEEECC	31.04	-
20	2-Hydroxyisobutyrylation	QPTIFQNKKRVLLGE CCCHHHCCCEEEECC	31.04	-
20	Succinylation	QPTIFQNKKRVLLGE CCCHHHCCCEEEECC	31.04	23954790
20	Acetylation	QPTIFQNKKRVLLGE CCCHHHCCCEEEECC	31.04	25953088
21	Ubiquitination	PTIFQNKKRVLLGET CCHHHCCCEEEECCC	56.12	24816145
21	Sumoylation	PTIFQNKKRVLLGET CCHHHCCCEEEECCC	56.12	-
21	Sumoylation	PTIFQNKKRVLLGET CCHHHCCCEEEECCC	56.12	-
22	Citrullination	TIFQNKKRVLLGETG CHHHCCCEEEECCCC	26.40	-
22	Citrullination	TIFQNKKRVLLGETG CHHHCCCEEEECCCC	26.40	-
28	Phosphorylation	KRVLLGETGKEKLPR CEEEECCCCHHHCCH	52.32	23312004
30	2-Hydroxyisobutyrylation	VLLGETGKEKLPRYY EEECCCCHHHCCHHH	60.12	-
30	Ubiquitination	VLLGETGKEKLPRYY EEECCCCHHHCCHHH	60.12	21906983
30	Sumoylation	VLLGETGKEKLPRYY EEECCCCHHHCCHHH	60.12	-
30	Sumoylation	VLLGETGKEKLPRYY EEECCCCHHHCCHHH	60.12	-
30	Acetylation	VLLGETGKEKLPRYY EEECCCCHHHCCHHH	60.12	23749302
32	Acetylation	LGETGKEKLPRYYKN ECCCCHHHCCHHHHH	68.24	25953088
32	Sumoylation	LGETGKEKLPRYYKN ECCCCHHHCCHHHHH	68.24	-
32	Ubiquitination	LGETGKEKLPRYYKN ECCCCHHHCCHHHHH	68.24	23000965
36	Phosphorylation	GKEKLPRYYKNIGLG CHHHCCHHHHHCCCC	19.49	28152594
37	Phosphorylation	KEKLPRYYKNIGLGF HHHCCHHHHHCCCCC	9.99	28152594
38	Sumoylation	EKLPRYYKNIGLGFK HHCCHHHHHCCCCCC	32.90	-
38	2-Hydroxyisobutyrylation	EKLPRYYKNIGLGFK HHCCHHHHHCCCCCC	32.90	-
38	Sumoylation	EKLPRYYKNIGLGFK HHCCHHHHHCCCCCC	32.90	-
38	Acetylation	EKLPRYYKNIGLGFK HHCCHHHHHCCCCCC	32.90	19608861
38	Ubiquitination	EKLPRYYKNIGLGFK HHCCHHHHHCCCCCC	32.90	23000965
45	Sumoylation	KNIGLGFKTPKEAIE HHCCCCCCCHHHHHC	63.22	-
45	2-Hydroxyisobutyrylation	KNIGLGFKTPKEAIE HHCCCCCCCHHHHHC	63.22	-
45	Sumoylation	KNIGLGFKTPKEAIE HHCCCCCCCHHHHHC	63.22	-
45	Ubiquitination	KNIGLGFKTPKEAIE HHCCCCCCCHHHHHC	63.22	21906983
45	Acetylation	KNIGLGFKTPKEAIE HHCCCCCCCHHHHHC	63.22	19608861
45	Methylation	KNIGLGFKTPKEAIE HHCCCCCCCHHHHHC	63.22	68957
46	Phosphorylation	NIGLGFKTPKEAIEG HCCCCCCCHHHHHCC	37.01	28450419
48	Sumoylation	GLGFKTPKEAIEGTY CCCCCCHHHHHCCCC	66.08	-
48	Acetylation	GLGFKTPKEAIEGTY CCCCCCHHHHHCCCC	66.08	26051181
48	2-Hydroxyisobutyrylation	GLGFKTPKEAIEGTY CCCCCCHHHHHCCCC	66.08	-
48	Sumoylation	GLGFKTPKEAIEGTY CCCCCCHHHHHCCCC	66.08	-
48	Ubiquitination	GLGFKTPKEAIEGTY CCCCCCHHHHHCCCC	66.08	21906983
54	Phosphorylation	PKEAIEGTYIDKKCP HHHHHCCCCCCCCCC	12.43	28152594
55	Phosphorylation	KEAIEGTYIDKKCPF HHHHCCCCCCCCCCC	20.27	28152594
55	Nitration	KEAIEGTYIDKKCPF HHHHCCCCCCCCCCC	20.27	-
58	Ubiquitination	IEGTYIDKKCPFTGN HCCCCCCCCCCCCCC	46.87	21963094
58	Succinylation	IEGTYIDKKCPFTGN HCCCCCCCCCCCCCC	46.87	23954790
58	Acetylation	IEGTYIDKKCPFTGN HCCCCCCCCCCCCCC	46.87	25825284
58	2-Hydroxyisobutyrylation	IEGTYIDKKCPFTGN HCCCCCCCCCCCCCC	46.87	-
59	Acetylation	EGTYIDKKCPFTGNV CCCCCCCCCCCCCCE	43.31	26051181
59	Sumoylation	EGTYIDKKCPFTGNV CCCCCCCCCCCCCCE	43.31	-
59	Sumoylation	EGTYIDKKCPFTGNV CCCCCCCCCCCCCCE	43.31	-
59	Ubiquitination	EGTYIDKKCPFTGNV CCCCCCCCCCCCCCE	43.31	21890473
60	Glutathionylation	GTYIDKKCPFTGNVS CCCCCCCCCCCCCEE	4.06	22555962
60	S-nitrosylation	GTYIDKKCPFTGNVS CCCCCCCCCCCCCEE	4.06	22126794
60	S-palmitoylation	GTYIDKKCPFTGNVS CCCCCCCCCCCCCEE	4.06	21044946
63	Phosphorylation	IDKKCPFTGNVSIRG CCCCCCCCCCEEECC	17.00	30108239
67	Phosphorylation	CPFTGNVSIRGRILS CCCCCCEEECCEECC	15.57	28355574
69	Methylation	FTGNVSIRGRILSGV CCCCEEECCEECCCC	22.34	12018939
74	Phosphorylation	SIRGRILSGVVTKMK EECCEECCCCEECCE	27.46	28450419
78	Phosphorylation	RILSGVVTKMKMQRT EECCCCEECCEEEEE	24.02	21406692
79	Acetylation	ILSGVVTKMKMQRTI ECCCCEECCEEEEEE	25.55	25953088
79	Ubiquitination	ILSGVVTKMKMQRTI ECCCCEECCEEEEEE	25.55	21906983
81	Ubiquitination	SGVVTKMKMQRTIVI CCCEECCEEEEEEEE	33.18	22817900
90	Methylation	QRTIVIRRDYLHYIR EEEEEEEHHHHHHHH	26.29	115492411
92	Phosphorylation	TIVIRRDYLHYIRKY EEEEEHHHHHHHHHH	8.12	28152594
95	Phosphorylation	IRRDYLHYIRKYNRF EEHHHHHHHHHHCCH	10.38	28152594
97	Methylation	RDYLHYIRKYNRFEK HHHHHHHHHHCCHHH	28.39	115492421
99	Phosphorylation	YLHYIRKYNRFEKRH HHHHHHHHCCHHHHH	11.17	28152594
104	Ubiquitination	RKYNRFEKRHKNMSV HHHCCHHHHHCCCEE	58.03	24816145
107	Ubiquitination	NRFEKRHKNMSVHLS CCHHHHHCCCEEEEC	59.38	22505724
107	2-Hydroxyisobutyrylation	NRFEKRHKNMSVHLS CCHHHHHCCCEEEEC	59.38	-
110	Phosphorylation	EKRHKNMSVHLSPCF HHHHCCCEEEECCCC	18.77	25159151
114	Phosphorylation	KNMSVHLSPCFRDVQ CCCEEEECCCCCCCC	12.54	25159151
116	Glutathionylation	MSVHLSPCFRDVQIG CEEEECCCCCCCCCC	3.82	22555962
131	S-nitrosylation	DIVTVGECRPLSKTV CEEEEEECEECCCEE	4.46	22178444
131	Glutathionylation	DIVTVGECRPLSKTV CEEEEEECEECCCEE	4.46	22555962
131	S-nitrosocysteine	DIVTVGECRPLSKTV CEEEEEECEECCCEE	4.46	-
131	S-palmitoylation	DIVTVGECRPLSKTV CEEEEEECEECCCEE	4.46	29575903
135	Phosphorylation	VGECRPLSKTVRFNV EEECEECCCEEEEEE	29.03	22210691
136	Ubiquitination	GECRPLSKTVRFNVL EECEECCCEEEEEEE	59.74	21906983
136	Acetylation	GECRPLSKTVRFNVL EECEECCCEEEEEEE	59.74	25953088
136	2-Hydroxyisobutyrylation	GECRPLSKTVRFNVL EECEECCCEEEEEEE	59.74	-
137	Phosphorylation	ECRPLSKTVRFNVLK ECEECCCEEEEEEEE	17.34	22210691
144	Ubiquitination	TVRFNVLKVTKAAGT EEEEEEEEEEECCCC	43.50	21963094
144	2-Hydroxyisobutyrylation	TVRFNVLKVTKAAGT EEEEEEEEEEECCCC	43.50	-
144	Acetylation	TVRFNVLKVTKAAGT EEEEEEEEEEECCCC	43.50	25953088
147	Ubiquitination	FNVLKVTKAAGTKKQ EEEEEEEECCCCHHH	38.95	22817900
153	Ubiquitination	TKAAGTKKQFQKF-- EECCCCHHHHCCC--	57.07	-

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
28	T	Phosphorylation	Kinase	LRRK2	Q5S007	PSP
46	T	Phosphorylation	Kinase	LRRK2	Q5S007	PSP
54	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 RS11_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 RS11_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
A4_HUMAN	APP	physical	21832049
RS13_HUMAN	RPS13	physical	22939629
RS12_HUMAN	RPS12	physical	22939629
RS14_HUMAN	RPS14	physical	22939629
RS15A_HUMAN	RPS15A	physical	22939629
RS19_HUMAN	RPS19	physical	22939629
RS23_HUMAN	RPS23	physical	22939629
RS26_HUMAN	RPS26	physical	22939629
RS3A_HUMAN	RPS3A	physical	22939629
RS3_HUMAN	RPS3	physical	22939629
RS4X_HUMAN	RPS4X	physical	22939629
RS5_HUMAN	RPS5	physical	22939629
RS8_HUMAN	RPS8	physical	22939629
RS16_HUMAN	RPS16	physical	22939629
RS2_HUMAN	RPS2	physical	22939629
RS7_HUMAN	RPS7	physical	22939629
RS24_HUMAN	RPS24	physical	22939629
RS6_HUMAN	RPS6	physical	22939629
RS21_HUMAN	RPS21	physical	22939629
RS27A_HUMAN	RPS27A	physical	22939629
RS27L_HUMAN	RPS27L	physical	22939629
VTNC_HUMAN	VTN	physical	22939629
EIFCL_HUMAN	EIF3CL	physical	22863883
RS12_HUMAN	RPS12	physical	22863883
RS24_HUMAN	RPS24	physical	22863883
RS2_HUMAN	RPS2	physical	22863883
RS3_HUMAN	RPS3	physical	22863883
RS4X_HUMAN	RPS4X	physical	22863883
RS7_HUMAN	RPS7	physical	22863883
RS9_HUMAN	RPS9	physical	22863883
EF1A1_HUMAN	EEF1A1	physical	26344197
KRR1_HUMAN	KRR1	physical	26344197
RM18_HUMAN	MRPL18	physical	26344197
RM24_HUMAN	MRPL24	physical	26344197
NOC4L_HUMAN	NOC4L	physical	26344197
RL10_HUMAN	RPL10	physical	26344197
RL10A_HUMAN	RPL10A	physical	26344197
RL11_HUMAN	RPL11	physical	26344197
RL12_HUMAN	RPL12	physical	26344197
RL13_HUMAN	RPL13	physical	26344197
RL13A_HUMAN	RPL13A	physical	26344197
RL14_HUMAN	RPL14	physical	26344197
RL15_HUMAN	RPL15	physical	26344197
RL17_HUMAN	RPL17	physical	26344197
RL18_HUMAN	RPL18	physical	26344197
RL23A_HUMAN	RPL23A	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
RL35_HUMAN	RPL35	physical	26344197
RL35A_HUMAN	RPL35A	physical	26344197
RL37_HUMAN	RPL37	physical	26344197
RL37A_HUMAN	RPL37A	physical	26344197
RL38_HUMAN	RPL38	physical	26344197
RL5_HUMAN	RPL5	physical	26344197
RL6_HUMAN	RPL6	physical	26344197
RL7_HUMAN	RPL7	physical	26344197
RL7A_HUMAN	RPL7A	physical	26344197
RL9_HUMAN	RPL9	physical	26344197
RLA2_HUMAN	RPLP2	physical	26344197
RS14_HUMAN	RPS14	physical	26344197
RS17_HUMAN	RPS17	physical	26344197
RS23_HUMAN	RPS23	physical	26344197
RS26_HUMAN	RPS26	physical	26344197
RS27_HUMAN	RPS27	physical	26344197
RS3A_HUMAN	RPS3A	physical	26344197
RS4X_HUMAN	RPS4X	physical	26344197
RS5_HUMAN	RPS5	physical	26344197
RS7_HUMAN	RPS7	physical	26344197
RS8_HUMAN	RPS8	physical	26344197
RS9_HUMAN	RPS9	physical	26344197
RSSA_HUMAN	RPSA	physical	26344197
RL1D1_HUMAN	RSL1D1	physical	26344197
PSMG3_HUMAN	PSMG3	physical	28514442
MDM2_HUMAN	MDM2	physical	28514442
EF1A2_HUMAN	EEF1A2	physical	28514442
RL26L_HUMAN	RPL26L1	physical	28514442
NAT10_HUMAN	NAT10	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.

Regulatory Network of RS11_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]
"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-38 AND LYS-45, AND MASSSPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"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 TYR-10; TYR-36; TYR-37 ANDTYR-55, AND MASS SPECTROMETRY.	19369195 [Abstract]