dbPTM

RS19_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RS19_HUMAN
UniProt AC	P39019
Protein Name	40S ribosomal protein S19
Gene Name	RPS19
Organism	Homo sapiens (Human).
Sequence Length	145
Subcellular Localization	Nucleus . Located more specifically in the nucleoli.
Protein Description	Required for pre-rRNA processing and maturation of 40S ribosomal subunits..
Protein Sequence	MPGVTVKDVNQQEFVRALAAFLKKSGKLKVPEWVDTVKLAKHKELAPYDENWFYTRAASTARHLYLRGGAGVGSMTKIYGGRQRNGVMPSHFSRGSKSVARRVLQALEGLKMVEKDQDGGRKLTPQGQRDLDRIAGQVAAANKKH

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
7	Ubiquitination	-MPGVTVKDVNQQEF -CCCCCCCCCCHHHH	46.74	-
7	Succinylation	-MPGVTVKDVNQQEF -CCCCCCCCCCHHHH	46.74	23954790
23	Succinylation	RALAAFLKKSGKLKV HHHHHHHHHHCCCCC	38.14	23954790
23	Ubiquitination	RALAAFLKKSGKLKV HHHHHHHHHHCCCCC	38.14	-
23	2-Hydroxyisobutyrylation	RALAAFLKKSGKLKV HHHHHHHHHHCCCCC	38.14	-
23	Malonylation	RALAAFLKKSGKLKV HHHHHHHHHHCCCCC	38.14	26320211
23	Acetylation	RALAAFLKKSGKLKV HHHHHHHHHHCCCCC	38.14	19608861
27	Acetylation	AFLKKSGKLKVPEWV HHHHHHCCCCCCHHH	52.83	26051181
29	Acetylation	LKKSGKLKVPEWVDT HHHHCCCCCCHHHHH	60.26	26051181
29	Malonylation	LKKSGKLKVPEWVDT HHHHCCCCCCHHHHH	60.26	26320211
29	Ubiquitination	LKKSGKLKVPEWVDT HHHHCCCCCCHHHHH	60.26	21890473
29	2-Hydroxyisobutyrylation	LKKSGKLKVPEWVDT HHHHCCCCCCHHHHH	60.26	-
38	Acetylation	PEWVDTVKLAKHKEL CHHHHHHHHHHCCCC	44.83	26051181
38	Ubiquitination	PEWVDTVKLAKHKEL CHHHHHHHHHHCCCC	44.83	21906983
38	2-Hydroxyisobutyrylation	PEWVDTVKLAKHKEL CHHHHHHHHHHCCCC	44.83	-
43	Acetylation	TVKLAKHKELAPYDE HHHHHHCCCCCCCCC	54.43	26822725
43	2-Hydroxyisobutyrylation	TVKLAKHKELAPYDE HHHHHHCCCCCCCCC	54.43	-
43	Ubiquitination	TVKLAKHKELAPYDE HHHHHHCCCCCCCCC	54.43	21906983
48	Phosphorylation	KHKELAPYDENWFYT HCCCCCCCCCCCCHH	30.22	28152594
54	Phosphorylation	PYDENWFYTRAASTA CCCCCCCHHHHHHHC	6.22	20860994
55	Phosphorylation	YDENWFYTRAASTAR CCCCCCHHHHHHHCC	12.35	20860994
56	Methylation	DENWFYTRAASTARH CCCCCHHHHHHHCCH	19.44	115492543
59	Phosphorylation	WFYTRAASTARHLYL CCHHHHHHHCCHHHH	22.93	19200342
60	Phosphorylation	FYTRAASTARHLYLR CHHHHHHHCCHHHHC	24.00	22210691
65	Phosphorylation	ASTARHLYLRGGAGV HHHCCHHHHCCCCCC	6.55	22210691
67	Methylation	TARHLYLRGGAGVGS HCCHHHHCCCCCCCC	28.13	24129315
74	Phosphorylation	RGGAGVGSMTKIYGG CCCCCCCCCCEEECC	22.37	20068231
75	Sulfoxidation	GGAGVGSMTKIYGGR CCCCCCCCCEEECCC	3.49	30846556
76	Phosphorylation	GAGVGSMTKIYGGRQ CCCCCCCCEEECCCC	18.91	28985074
77	Acetylation	AGVGSMTKIYGGRQR CCCCCCCEEECCCCC	25.86	19608861
77	Ubiquitination	AGVGSMTKIYGGRQR CCCCCCCEEECCCCC	25.86	21906983
77	2-Hydroxyisobutyrylation	AGVGSMTKIYGGRQR CCCCCCCEEECCCCC	25.86	-
88	Sulfoxidation	GRQRNGVMPSHFSRG CCCCCCCCCCCCCCC	2.74	21406390
90	Phosphorylation	QRNGVMPSHFSRGSK CCCCCCCCCCCCCCH	21.04	26434776
93	Phosphorylation	GVMPSHFSRGSKSVA CCCCCCCCCCCHHHH	30.24	26434776
94	Methylation	VMPSHFSRGSKSVAR CCCCCCCCCCHHHHH	53.08	115492551
96	Phosphorylation	PSHFSRGSKSVARRV CCCCCCCCHHHHHHH	22.20	26434776
98	Phosphorylation	HFSRGSKSVARRVLQ CCCCCCHHHHHHHHH	23.78	29514088
111	Acetylation	LQALEGLKMVEKDQD HHHHHHHCCEEECCC	52.32	19608861
111	2-Hydroxyisobutyrylation	LQALEGLKMVEKDQD HHHHHHHCCEEECCC	52.32	-
111	Ubiquitination	LQALEGLKMVEKDQD HHHHHHHCCEEECCC	52.32	21906983
112	Sulfoxidation	QALEGLKMVEKDQDG HHHHHHCCEEECCCC	5.90	28183972
115	Acetylation	EGLKMVEKDQDGGRK HHHCCEEECCCCCCE	49.64	25825284
122	2-Hydroxyisobutyrylation	KDQDGGRKLTPQGQR ECCCCCCEECCCCHH	61.05	-
122	Ubiquitination	KDQDGGRKLTPQGQR ECCCCCCEECCCCHH	61.05	-
133	Methylation	QGQRDLDRIAGQVAA CCHHHHHHHHHHHHH	28.14	115492535
143	2-Hydroxyisobutyrylation	GQVAAANKKH----- HHHHHHHCCC-----	47.71	-
143	Ubiquitination	GQVAAANKKH----- HHHHHHHCCC-----	47.71	-
143	Succinylation	GQVAAANKKH----- HHHHHHHCCC-----	47.71	-
143	Succinylation	GQVAAANKKH----- HHHHHHHCCC-----	47.71	-
143	Acetylation	GQVAAANKKH----- HHHHHHHCCC-----	47.71	25953088
144	Acetylation	QVAAANKKH------ HHHHHHCCC------	55.12	25953088

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
59	S	Phosphorylation	Kinase	PRKACA	P17612	GPS
59	S	Phosphorylation	Kinase	CAMK1	Q14012	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of RS19_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 RS19_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
A4_HUMAN	APP	physical	21832049
RS23_HUMAN	RPS23	physical	22939629
RS26_HUMAN	RPS26	physical	22939629
RS28_HUMAN	RPS28	physical	22939629
RS2_HUMAN	RPS2	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
RS3A_HUMAN	RPS3A	physical	22939629
RS24_HUMAN	RPS24	physical	22939629
RSSA_HUMAN	RPSA	physical	22939629
RS25_HUMAN	RPS25	physical	22939629
RS9_HUMAN	RPS9	physical	22939629
RS7_HUMAN	RPS7	physical	22939629
RS20_HUMAN	RPS20	physical	22939629
RS27A_HUMAN	RPS27A	physical	22939629
RS21_HUMAN	RPS21	physical	22939629
STT3B_HUMAN	STT3B	physical	22939629
UBL4A_HUMAN	UBL4A	physical	22939629
STX7_HUMAN	STX7	physical	22939629
THIK_HUMAN	ACAA1	physical	22939629
TBL2_HUMAN	TBL2	physical	22939629
SUGP1_HUMAN	SUGP1	physical	22939629
RT28_HUMAN	MRPS28	physical	22939629
TXD11_HUMAN	TXNDC11	physical	21988832
EIF3E_HUMAN	EIF3E	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
RS17_HUMAN	RPS17	physical	22863883
RS18_HUMAN	RPS18	physical	22863883
RS24_HUMAN	RPS24	physical	22863883
RS25_HUMAN	RPS25	physical	22863883
RS2_HUMAN	RPS2	physical	22863883
RS3A_HUMAN	RPS3A	physical	22863883
RS3_HUMAN	RPS3	physical	22863883
RS6_HUMAN	RPS6	physical	22863883
RS8_HUMAN	RPS8	physical	22863883
PAIRB_HUMAN	SERBP1	physical	22863883
TSR1_HUMAN	TSR1	physical	22863883
PYM1_HUMAN	WIBG	physical	22863883
ASCC2_HUMAN	ASCC2	physical	26344197
IMA5_HUMAN	KPNA1	physical	26344197
PRP4_HUMAN	PRPF4	physical	26344197
RL10_HUMAN	RPL10	physical	26344197
RL10A_HUMAN	RPL10A	physical	26344197
RL12_HUMAN	RPL12	physical	26344197
RL13_HUMAN	RPL13	physical	26344197
RL13A_HUMAN	RPL13A	physical	26344197
RL14_HUMAN	RPL14	physical	26344197
RL18_HUMAN	RPL18	physical	26344197
RL19_HUMAN	RPL19	physical	26344197
RL22_HUMAN	RPL22	physical	26344197
RL23_HUMAN	RPL23	physical	26344197
RL27_HUMAN	RPL27	physical	26344197
RL27A_HUMAN	RPL27A	physical	26344197
RL30_HUMAN	RPL30	physical	26344197
RL31_HUMAN	RPL31	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
RL5_HUMAN	RPL5	physical	26344197
RL7_HUMAN	RPL7	physical	26344197
RL7A_HUMAN	RPL7A	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
RS15_HUMAN	RPS15	physical	26344197
RS23_HUMAN	RPS23	physical	26344197
RS25_HUMAN	RPS25	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
RL40_HUMAN	UBA52	physical	26344197

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
105650	Diamond-Blackfan anemia 1 (DBA1)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of RS19_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-23; LYS-77 AND LYS-111, ANDMASS SPECTROMETRY.	19608861 [Abstract]