dbPTM

RS9_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RS9_HUMAN
UniProt AC	P46781
Protein Name	40S ribosomal protein S9
Gene Name	RPS9
Organism	Homo sapiens (Human).
Sequence Length	194
Subcellular Localization	Cytoplasm . Localized in cytoplasmic mRNP granules containing untranslated mRNAs.
Protein Description
Protein Sequence	MPVARSWVCRKTYVTPRRPFEKSRLDQELKLIGEYGLRNKREVWRVKFTLAKIRKAARELLTLDEKDPRRLFEGNALLRRLVRIGVLDEGKMKLDYILGLKIEDFLERRLQTQVFKLGLAKSIHHARVLIRQRHIRVRKQVVNIPSFIVRLDSQKHIDFSLRSPYGGGRPGRVKRKNAKKGQGGAGAGDDEEED

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
5	Methylation	---MPVARSWVCRKT ---CCCCCEEEECCC	31.14	115492823
11	Methylation	ARSWVCRKTYVTPRR CCEEEECCCCCCCCC	38.80	116252333
11	Ubiquitination	ARSWVCRKTYVTPRR CCEEEECCCCCCCCC	38.80	21890473
11	2-Hydroxyisobutyrylation	ARSWVCRKTYVTPRR CCEEEECCCCCCCCC	38.80	-
12	Phosphorylation	RSWVCRKTYVTPRRP CEEEECCCCCCCCCC	12.13	28152594
13	Phosphorylation	SWVCRKTYVTPRRPF EEEECCCCCCCCCCC	12.83	28152594
15	Phosphorylation	VCRKTYVTPRRPFEK EECCCCCCCCCCCCH	10.72	21815630
22	Acetylation	TPRRPFEKSRLDQEL CCCCCCCHHCHHHHH	41.05	26051181
22	Ubiquitination	TPRRPFEKSRLDQEL CCCCCCCHHCHHHHH	41.05	-
23	Phosphorylation	PRRPFEKSRLDQELK CCCCCCHHCHHHHHH	30.77	26437602
30	Ubiquitination	SRLDQELKLIGEYGL HCHHHHHHHHHHHCC	36.99	21906983
30	Acetylation	SRLDQELKLIGEYGL HCHHHHHHHHHHHCC	36.99	25953088
30	Ubiquitination	SRLDQELKLIGEYGL HCHHHHHHHHHHHCC	36.99	21890473
30	2-Hydroxyisobutyrylation	SRLDQELKLIGEYGL HCHHHHHHHHHHHCC	36.99	-
35	Phosphorylation	ELKLIGEYGLRNKRE HHHHHHHHCCCCHHH	19.08	28152594
38	Methylation	LIGEYGLRNKREVWR HHHHHCCCCHHHHHH	42.11	115492815
47	Acetylation	KREVWRVKFTLAKIR HHHHHHHHHHHHHHH	24.86	25953088
47	2-Hydroxyisobutyrylation	KREVWRVKFTLAKIR HHHHHHHHHHHHHHH	24.86	-
47	Ubiquitination	KREVWRVKFTLAKIR HHHHHHHHHHHHHHH	24.86	-
52	Acetylation	RVKFTLAKIRKAARE HHHHHHHHHHHHHHH	46.27	26051181
52	Ubiquitination	RVKFTLAKIRKAARE HHHHHHHHHHHHHHH	46.27	21906983
52	Ubiquitination	RVKFTLAKIRKAARE HHHHHHHHHHHHHHH	46.27	21890473
55	Ubiquitination	FTLAKIRKAARELLT HHHHHHHHHHHHHCC	50.28	-
66	Succinylation	ELLTLDEKDPRRLFE HHCCCCCCCHHHHHC	73.10	27452117
66	Acetylation	ELLTLDEKDPRRLFE HHCCCCCCCHHHHHC	73.10	23236377
66	Ubiquitination	ELLTLDEKDPRRLFE HHCCCCCCCHHHHHC	73.10	-
79	Methylation	FEGNALLRRLVRIGV HCHHHHHHHHHHCCC	30.64	115492807
91	Ubiquitination	IGVLDEGKMKLDYIL CCCCCCCCCCHHHHH	30.71	21906983
91	Sumoylation	IGVLDEGKMKLDYIL CCCCCCCCCCHHHHH	30.71	-
91	Sumoylation	IGVLDEGKMKLDYIL CCCCCCCCCCHHHHH	30.71	-
91	2-Hydroxyisobutyrylation	IGVLDEGKMKLDYIL CCCCCCCCCCHHHHH	30.71	-
91	Acetylation	IGVLDEGKMKLDYIL CCCCCCCCCCHHHHH	30.71	23236377
92	Sulfoxidation	GVLDEGKMKLDYILG CCCCCCCCCHHHHHC	8.40	28183972
93	Ubiquitination	VLDEGKMKLDYILGL CCCCCCCCHHHHHCC	41.51	21890473
93	Sumoylation	VLDEGKMKLDYILGL CCCCCCCCHHHHHCC	41.51	-
93	Acetylation	VLDEGKMKLDYILGL CCCCCCCCHHHHHCC	41.51	23236377
93	Sumoylation	VLDEGKMKLDYILGL CCCCCCCCHHHHHCC	41.51	28112733
93	Ubiquitination	VLDEGKMKLDYILGL CCCCCCCCHHHHHCC	41.51	21890473
93	Succinylation	VLDEGKMKLDYILGL CCCCCCCCHHHHHCC	41.51	23954790
96	Phosphorylation	EGKMKLDYILGLKIE CCCCCHHHHHCCCHH	14.42	25884760
101	Ubiquitination	LDYILGLKIEDFLER HHHHHCCCHHHHHHH	42.10	21906983
108	Methylation	KIEDFLERRLQTQVF CHHHHHHHHHHHHHH	46.91	115492799
116	Ubiquitination	RLQTQVFKLGLAKSI HHHHHHHHHHHHHHH	42.67	21890473
116	Ubiquitination	RLQTQVFKLGLAKSI HHHHHHHHHHHHHHH	42.67	21890473
116	Succinylation	RLQTQVFKLGLAKSI HHHHHHHHHHHHHHH	42.67	23954790
116	2-Hydroxyisobutyrylation	RLQTQVFKLGLAKSI HHHHHHHHHHHHHHH	42.67	-
116	Acetylation	RLQTQVFKLGLAKSI HHHHHHHHHHHHHHH	42.67	26051181
121	2-Hydroxyisobutyrylation	VFKLGLAKSIHHARV HHHHHHHHHHHHHHH	55.79	-
121	Acetylation	VFKLGLAKSIHHARV HHHHHHHHHHHHHHH	55.79	25953088
121	Ubiquitination	VFKLGLAKSIHHARV HHHHHHHHHHHHHHH	55.79	21906983
139	Sumoylation	QRHIRVRKQVVNIPS HHHHHHHHHHEECCE	44.58	28112733
139	Ubiquitination	QRHIRVRKQVVNIPS HHHHHHHHHHEECCE	44.58	21890473
139	Ubiquitination	QRHIRVRKQVVNIPS HHHHHHHHHHEECCE	44.58	21890473
139	Malonylation	QRHIRVRKQVVNIPS HHHHHHHHHHEECCE	44.58	26320211
139	2-Hydroxyisobutyrylation	QRHIRVRKQVVNIPS HHHHHHHHHHEECCE	44.58	-
146	Phosphorylation	KQVVNIPSFIVRLDS HHHEECCEEEEEECC	24.65	22199227
153	Phosphorylation	SFIVRLDSQKHIDFS EEEEEECCCCCEEEE	45.80	23401153
155	Ubiquitination	IVRLDSQKHIDFSLR EEEECCCCCEEEEEC	46.62	21890473
155	Ubiquitination	IVRLDSQKHIDFSLR EEEECCCCCEEEEEC	46.62	21890473
155	Acetylation	IVRLDSQKHIDFSLR EEEECCCCCEEEEEC	46.62	19608861
155	2-Hydroxyisobutyrylation	IVRLDSQKHIDFSLR EEEECCCCCEEEEEC	46.62	-
155	Malonylation	IVRLDSQKHIDFSLR EEEECCCCCEEEEEC	46.62	26320211
160	Phosphorylation	SQKHIDFSLRSPYGG CCCCEEEEECCCCCC	21.08	25867546
162	Methylation	KHIDFSLRSPYGGGR CCEEEEECCCCCCCC	34.09	115492791
163	Phosphorylation	HIDFSLRSPYGGGRP CEEEEECCCCCCCCC	27.97	23401153
165	Phosphorylation	DFSLRSPYGGGRPGR EEEECCCCCCCCCCC	29.64	28152594
180	Ubiquitination	VKRKNAKKGQGGAGA CCCCCCCCCCCCCCC	54.80	21906983

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 RS9_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of RS9_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 RS9_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
A4_HUMAN	APP	physical	21832049
RSSA_HUMAN	RPSA	physical	22939629
STAT3_HUMAN	STAT3	physical	21988832
RSSA_HUMAN	RPSA	physical	22863883
LARP1_HUMAN	LARP1	physical	22863883
PNO1_HUMAN	PNO1	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
RS17_HUMAN	RPS17	physical	22863883
RS19_HUMAN	RPS19	physical	22863883
RS20_HUMAN	RPS20	physical	22863883
RS21_HUMAN	RPS21	physical	22863883
RS24_HUMAN	RPS24	physical	22863883
RS25_HUMAN	RPS25	physical	22863883
RS26_HUMAN	RPS26	physical	22863883
RS27_HUMAN	RPS27	physical	22863883
RS28_HUMAN	RPS28	physical	22863883
RS2_HUMAN	RPS2	physical	22863883
RS5_HUMAN	RPS5	physical	22863883
RS6_HUMAN	RPS6	physical	22863883
RS7_HUMAN	RPS7	physical	22863883
RS8_HUMAN	RPS8	physical	22863883
TSR1_HUMAN	TSR1	physical	22863883
RNPS1_HUMAN	RNPS1	physical	26344197
RL10A_HUMAN	RPL10A	physical	26344197
RL12_HUMAN	RPL12	physical	26344197
RL13A_HUMAN	RPL13A	physical	26344197
RL14_HUMAN	RPL14	physical	26344197
RL15_HUMAN	RPL15	physical	26344197
RL17_HUMAN	RPL17	physical	26344197
RL23A_HUMAN	RPL23A	physical	26344197
RL27A_HUMAN	RPL27A	physical	26344197
RL32_HUMAN	RPL32	physical	26344197
RL35_HUMAN	RPL35	physical	26344197
RL35A_HUMAN	RPL35A	physical	26344197
RL37A_HUMAN	RPL37A	physical	26344197
RL38_HUMAN	RPL38	physical	26344197
RL4_HUMAN	RPL4	physical	26344197
RL6_HUMAN	RPL6	physical	26344197
RL7_HUMAN	RPL7	physical	26344197
RL7A_HUMAN	RPL7A	physical	26344197
RLA2_HUMAN	RPLP2	physical	26344197
RS10_HUMAN	RPS10	physical	26344197
RS18_HUMAN	RPS18	physical	26344197
RS20_HUMAN	RPS20	physical	26344197
RS23_HUMAN	RPS23	physical	26344197
RS26_HUMAN	RPS26	physical	26344197
RS27_HUMAN	RPS27	physical	26344197
RS29_HUMAN	RPS29	physical	26344197
RS3A_HUMAN	RPS3A	physical	26344197
RS4X_HUMAN	RPS4X	physical	26344197
RS7_HUMAN	RPS7	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 RS9_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-155, AND MASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-153 AND SER-163, ANDMASS SPECTROMETRY.	18691976 [Abstract]