dbPTM

RS12_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RS12_HUMAN
UniProt AC	P25398
Protein Name	40S ribosomal protein S12
Gene Name	RPS12
Organism	Homo sapiens (Human).
Sequence Length	132
Subcellular Localization	Cytoplasm.
Protein Description
Protein Sequence	MAEEGIAAGGVMDVNTALQEVLKTALIHDGLARGIREAAKALDKRQAHLCVLASNCDEPMYVKLVEALCAEHQINLIKVDDNKKLGEWVGLCKIDREGKPRKVVGCSCVVVKDYGKESQAKDVIEEYFKCKK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAEEGIAAG ------CCCCCCCCC	24.45	20068231
12	Sulfoxidation	GIAAGGVMDVNTALQ CCCCCCCCCHHHHHH	5.57	28465586
16	Phosphorylation	GGVMDVNTALQEVLK CCCCCHHHHHHHHHH	28.70	20068231
23	Ubiquitination	TALQEVLKTALIHDG HHHHHHHHHHHHHHH	36.61	33845483
24	Phosphorylation	ALQEVLKTALIHDGL HHHHHHHHHHHHHHH	23.64	20068231
33	Methylation	LIHDGLARGIREAAK HHHHHHHHHHHHHHH	46.22	115492431
40	Ubiquitination	RGIREAAKALDKRQA HHHHHHHHHHHHCHH	57.43	33845483
40	2-Hydroxyisobutyrylation	RGIREAAKALDKRQA HHHHHHHHHHHHCHH	57.43	-
44	Ubiquitination	EAAKALDKRQAHLCV HHHHHHHHCHHHEEH	47.46	24816145
50	Glutathionylation	DKRQAHLCVLASNCD HHCHHHEEHHCCCCC	1.37	22555962
60	Sulfoxidation	ASNCDEPMYVKLVEA CCCCCCCHHHHHHHH	5.89	30846556
61	Phosphorylation	SNCDEPMYVKLVEAL CCCCCCHHHHHHHHH	12.73	27642862
63	Ubiquitination	CDEPMYVKLVEALCA CCCCHHHHHHHHHHH	29.36	32015554
69	Glutathionylation	VKLVEALCAEHQINL HHHHHHHHHHCCCEE	5.56	22555962
78	Ubiquitination	EHQINLIKVDDNKKL HCCCEEEEECCCCCH	42.66	23000965
78	Acetylation	EHQINLIKVDDNKKL HCCCEEEEECCCCCH	42.66	25953088
78	2-Hydroxyisobutyrylation	EHQINLIKVDDNKKL HCCCEEEEECCCCCH	42.66	-
83	Ubiquitination	LIKVDDNKKLGEWVG EEEECCCCCHHCEEE	57.26	23000965
84	Ubiquitination	IKVDDNKKLGEWVGL EEECCCCCHHCEEEE	68.90	23000965
84	2-Hydroxyisobutyrylation	IKVDDNKKLGEWVGL EEECCCCCHHCEEEE	68.90	-
84	Acetylation	IKVDDNKKLGEWVGL EEECCCCCHHCEEEE	68.90	25953088
92	Glutathionylation	LGEWVGLCKIDREGK HHCEEEEEEECCCCC	2.74	22555962
93	Acetylation	GEWVGLCKIDREGKP HCEEEEEEECCCCCC	53.32	25953088
93	2-Hydroxyisobutyrylation	GEWVGLCKIDREGKP HCEEEEEEECCCCCC	53.32	-
93	Ubiquitination	GEWVGLCKIDREGKP HCEEEEEEECCCCCC	53.32	23000965
99	Acetylation	CKIDREGKPRKVVGC EEECCCCCCCCEEEE	36.58	23749302
99	Ubiquitination	CKIDREGKPRKVVGC EEECCCCCCCCEEEE	36.58	23000965
102	Ubiquitination	DREGKPRKVVGCSCV CCCCCCCCEEEEEEE	50.20	33845483
102	Acetylation	DREGKPRKVVGCSCV CCCCCCCCEEEEEEE	50.20	26051181
106	S-palmitoylation	KPRKVVGCSCVVVKD CCCCEEEEEEEEEEC	1.60	29575903
107	Phosphorylation	PRKVVGCSCVVVKDY CCCEEEEEEEEEECC	12.20	25690035
108	Glutathionylation	RKVVGCSCVVVKDYG CCEEEEEEEEEECCC	2.91	22555962
108	S-palmitoylation	RKVVGCSCVVVKDYG CCEEEEEEEEEECCC	2.91	29575903
112	Acetylation	GCSCVVVKDYGKESQ EEEEEEEECCCCHHH	33.35	25953088
112	Ubiquitination	GCSCVVVKDYGKESQ EEEEEEEECCCCHHH	33.35	21963094
112	Succinylation	GCSCVVVKDYGKESQ EEEEEEEECCCCHHH	33.35	23954790
112	2-Hydroxyisobutyrylation	GCSCVVVKDYGKESQ EEEEEEEECCCCHHH	33.35	-
116	Ubiquitination	VVVKDYGKESQAKDV EEEECCCCHHHHHHH	48.22	33845483
116	Succinylation	VVVKDYGKESQAKDV EEEECCCCHHHHHHH	48.22	23954790
116	Acetylation	VVVKDYGKESQAKDV EEEECCCCHHHHHHH	48.22	26051181
116	2-Hydroxyisobutyrylation	VVVKDYGKESQAKDV EEEECCCCHHHHHHH	48.22	-
121	Ubiquitination	YGKESQAKDVIEEYF CCCHHHHHHHHHHHH	44.91	29967540
121	Acetylation	YGKESQAKDVIEEYF CCCHHHHHHHHHHHH	44.91	26051181
121	2-Hydroxyisobutyrylation	YGKESQAKDVIEEYF CCCHHHHHHHHHHHH	44.91	-
121	Succinylation	YGKESQAKDVIEEYF CCCHHHHHHHHHHHH	44.91	23954790
127	Phosphorylation	AKDVIEEYFKCKK-- HHHHHHHHHCCCC--	8.78	28152594
129	Succinylation	DVIEEYFKCKK---- HHHHHHHCCCC----	44.22	23954790
129	Ubiquitination	DVIEEYFKCKK---- HHHHHHHCCCC----	44.22	23000965
129	Succinylation	DVIEEYFKCKK---- HHHHHHHCCCC----	44.22	-
129	Acetylation	DVIEEYFKCKK---- HHHHHHHCCCC----	44.22	23954790
129	Methylation	DVIEEYFKCKK---- HHHHHHHCCCC----	44.22	66728369
129	2-Hydroxyisobutyrylation	DVIEEYFKCKK---- HHHHHHHCCCC----	44.22	-
129	Neddylation	DVIEEYFKCKK---- HHHHHHHCCCC----	44.22	32015554
131	Ubiquitination	IEEYFKCKK------ HHHHHCCCC------	63.21	23000965
132	Ubiquitination	EEYFKCKK------- HHHHCCCC-------	75.05	23000965

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 RS12_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of RS12_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 RS12_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
A4_HUMAN	APP	physical	21832049
RS15A_HUMAN	RPS15A	physical	22939629
RS16_HUMAN	RPS16	physical	22939629
RS23_HUMAN	RPS23	physical	22939629
RS2_HUMAN	RPS2	physical	22939629
RS4X_HUMAN	RPS4X	physical	22939629
RS6_HUMAN	RPS6	physical	22939629
RS19_HUMAN	RPS19	physical	22939629
RS26_HUMAN	RPS26	physical	22939629
RS8_HUMAN	RPS8	physical	22939629
RS13_HUMAN	RPS13	physical	22939629
RS28_HUMAN	RPS28	physical	22939629
RS5_HUMAN	RPS5	physical	22939629
RS3_HUMAN	RPS3	physical	22939629
RS3A_HUMAN	RPS3A	physical	22939629
RS24_HUMAN	RPS24	physical	22939629
RS21_HUMAN	RPS21	physical	22939629
RS27A_HUMAN	RPS27A	physical	22939629
VAMP2_HUMAN	VAMP2	physical	22939629
RS27L_HUMAN	RPS27L	physical	22939629
EIF3A_HUMAN	EIF3A	physical	22863883
EIF3E_HUMAN	EIF3E	physical	22863883
RSSA_HUMAN	RPSA	physical	22863883
LARP1_HUMAN	LARP1	physical	22863883
PNO1_HUMAN	PNO1	physical	22863883
PRS10_HUMAN	PSMC6	physical	22863883
PSMD1_HUMAN	PSMD1	physical	22863883
PSMD4_HUMAN	PSMD4	physical	22863883
PSMD8_HUMAN	PSMD8	physical	22863883
RANB9_HUMAN	RANBP9	physical	22863883
RS14_HUMAN	RPS14	physical	22863883
RS15A_HUMAN	RPS15A	physical	22863883
RS27_HUMAN	RPS27	physical	22863883
RS2_HUMAN	RPS2	physical	22863883
RS4X_HUMAN	RPS4X	physical	22863883
RS6_HUMAN	RPS6	physical	22863883
RS8_HUMAN	RPS8	physical	22863883
TSR1_HUMAN	TSR1	physical	22863883
PYM1_HUMAN	WIBG	physical	22863883
UBIM_HUMAN	FAU	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
RL21_HUMAN	RPL21	physical	26344197
RL22_HUMAN	RPL22	physical	26344197
RL23_HUMAN	RPL23	physical	26344197
RL24_HUMAN	RPL24	physical	26344197
RL27_HUMAN	RPL27	physical	26344197
RL27A_HUMAN	RPL27A	physical	26344197
RL30_HUMAN	RPL30	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
RL4_HUMAN	RPL4	physical	26344197
RL5_HUMAN	RPL5	physical	26344197
RL7_HUMAN	RPL7	physical	26344197
RL7A_HUMAN	RPL7A	physical	26344197
RL9_HUMAN	RPL9	physical	26344197
RS10_HUMAN	RPS10	physical	26344197
RS11_HUMAN	RPS11	physical	26344197
RS14_HUMAN	RPS14	physical	26344197
RS15A_HUMAN	RPS15A	physical	26344197
RS18_HUMAN	RPS18	physical	26344197
RS2_HUMAN	RPS2	physical	26344197
RS23_HUMAN	RPS23	physical	26344197
RS25_HUMAN	RPS25	physical	26344197
RS26_HUMAN	RPS26	physical	26344197
RS3_HUMAN	RPS3	physical	26344197
RS3A_HUMAN	RPS3A	physical	26344197
RS4X_HUMAN	RPS4X	physical	26344197
RS6_HUMAN	RPS6	physical	26344197
RS7_HUMAN	RPS7	physical	26344197
RS8_HUMAN	RPS8	physical	26344197
RS9_HUMAN	RPS9	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 RS12_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]