dbPTM

RS7_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RS7_HUMAN
UniProt AC	P62081
Protein Name	40S ribosomal protein S7
Gene Name	RPS7
Organism	Homo sapiens (Human).
Sequence Length	194
Subcellular Localization	Cytoplasm, cytoskeleton, microtubule organizing center, centrosome . Colocalizes with NEK6 in the centrosome.
Protein Description	Required for rRNA maturation..
Protein Sequence	MFSSSAKIVKPNGEKPDEFESGISQALLELEMNSDLKAQLRELNITAAKEIEVGGGRKAIIIFVPVPQLKSFQKIQVRLVRELEKKFSGKHVVFIAQRRILPKPTRKSRTKNKQKRPRSRTLTAVHDAILEDLVFPSEIVGKRIRVKLDGSRLIKVHLDKAQQNNVEHKVETFSGVYKKLTGKDVNFEFPEFQL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MFSSSAKI -------CCCCCCEE	7.11	25944712
3	Phosphorylation	-----MFSSSAKIVK -----CCCCCCEEEC	23.29	24719451
7	Ubiquitination	-MFSSSAKIVKPNGE -CCCCCCEEECCCCC	50.40	33845483
10	Ubiquitination	SSSAKIVKPNGEKPD CCCCEEECCCCCCCC	35.92	21906983
15	Ubiquitination	IVKPNGEKPDEFESG EECCCCCCCCHHHCC	60.20	21906983
15	Acetylation	IVKPNGEKPDEFESG EECCCCCCCCHHHCC	60.20	26051181
24	Phosphorylation	DEFESGISQALLELE CHHHCCHHHHHHHHH	16.96	17525332
32	Sulfoxidation	QALLELEMNSDLKAQ HHHHHHHCCCCHHHH	10.20	28465586
34	Phosphorylation	LLELEMNSDLKAQLR HHHHHCCCCHHHHHH	42.90	26270265
37	Ubiquitination	LEMNSDLKAQLRELN HHCCCCHHHHHHHCC	38.79	21906983
37	Acetylation	LEMNSDLKAQLRELN HHCCCCHHHHHHHCC	38.79	61235
37	Sumoylation	LEMNSDLKAQLRELN HHCCCCHHHHHHHCC	38.79	-
46	Phosphorylation	QLRELNITAAKEIEV HHHHCCCCEEEEEEE	21.35	20068231
49	Ubiquitination	ELNITAAKEIEVGGG HCCCCEEEEEEECCC	57.68	21890473
49	Ubiquitination	ELNITAAKEIEVGGG HCCCCEEEEEEECCC	57.68	21906983
58	Ubiquitination	IEVGGGRKAIIIFVP EEECCCCEEEEEEEE	47.41	33845483
58	Acetylation	IEVGGGRKAIIIFVP EEECCCCEEEEEEEE	47.41	26051181
70	Ubiquitination	FVPVPQLKSFQKIQV EEECCCCCCHHHHHH	43.93	23000965
70	Sumoylation	FVPVPQLKSFQKIQV EEECCCCCCHHHHHH	43.93	28112733
70	Acetylation	FVPVPQLKSFQKIQV EEECCCCCCHHHHHH	43.93	90379
70	2-Hydroxyisobutyrylation	FVPVPQLKSFQKIQV EEECCCCCCHHHHHH	43.93	-
70	Ubiquitination	FVPVPQLKSFQKIQV EEECCCCCCHHHHHH	43.93	21890473
74	2-Hydroxyisobutyrylation	PQLKSFQKIQVRLVR CCCCCHHHHHHHHHH	32.85	-
74	Ubiquitination	PQLKSFQKIQVRLVR CCCCCHHHHHHHHHH	32.85	23000965
74	Sumoylation	PQLKSFQKIQVRLVR CCCCCHHHHHHHHHH	32.85	28112733
74	Malonylation	PQLKSFQKIQVRLVR CCCCCHHHHHHHHHH	32.85	26320211
74	Ubiquitination	PQLKSFQKIQVRLVR CCCCCHHHHHHHHHH	32.85	21890473
74	Acetylation	PQLKSFQKIQVRLVR CCCCCHHHHHHHHHH	32.85	19608861
85	Neddylation	RLVRELEKKFSGKHV HHHHHHHHHCCCCEE	72.28	32015554
85	Ubiquitination	RLVRELEKKFSGKHV HHHHHHHHHCCCCEE	72.28	22817900
85	Sumoylation	RLVRELEKKFSGKHV HHHHHHHHHCCCCEE	72.28	-
86	Ubiquitination	LVRELEKKFSGKHVV HHHHHHHHCCCCEEE	35.07	22817900
86	Sumoylation	LVRELEKKFSGKHVV HHHHHHHHCCCCEEE	35.07	-
88	Phosphorylation	RELEKKFSGKHVVFI HHHHHHCCCCEEEEE	56.67	24719451
90	Malonylation	LEKKFSGKHVVFIAQ HHHHCCCCEEEEEEE	31.84	26320211
90	Acetylation	LEKKFSGKHVVFIAQ HHHHCCCCEEEEEEE	31.84	25953088
90	Sumoylation	LEKKFSGKHVVFIAQ HHHHCCCCEEEEEEE	31.84	-
90	Ubiquitination	LEKKFSGKHVVFIAQ HHHHCCCCEEEEEEE	31.84	22817900
103	Ubiquitination	AQRRILPKPTRKSRT EECCCCCCCCCCCCC	56.42	24816145
108	Phosphorylation	LPKPTRKSRTKNKQK CCCCCCCCCCCCCCC	41.72	28258704
113	Ubiquitination	RKSRTKNKQKRPRSR CCCCCCCCCCCCCHH	59.77	24816145
119	Phosphorylation	NKQKRPRSRTLTAVH CCCCCCCHHCHHHHH	32.09	25159151
121	Phosphorylation	QKRPRSRTLTAVHDA CCCCCHHCHHHHHHH	29.70	27273156
123	Phosphorylation	RPRSRTLTAVHDAIL CCCHHCHHHHHHHHH	26.48	27273156
137	Phosphorylation	LEDLVFPSEIVGKRI HHHCCCCHHHCCCEE	28.61	28450419
142	Ubiquitination	FPSEIVGKRIRVKLD CCHHHCCCEEEEEEC	33.48	21963094
142	Acetylation	FPSEIVGKRIRVKLD CCHHHCCCEEEEEEC	33.48	25953088
142	2-Hydroxyisobutyrylation	FPSEIVGKRIRVKLD CCHHHCCCEEEEEEC	33.48	-
147	Ubiquitination	VGKRIRVKLDGSRLI CCCEEEEEECCCEEE	30.89	27667366
147	Acetylation	VGKRIRVKLDGSRLI CCCEEEEEECCCEEE	30.89	25953088
151	Phosphorylation	IRVKLDGSRLIKVHL EEEEECCCEEEEEEH	24.47	29514088
155	2-Hydroxyisobutyrylation	LDGSRLIKVHLDKAQ ECCCEEEEEEHHHHH	28.35	-
155	Ubiquitination	LDGSRLIKVHLDKAQ ECCCEEEEEEHHHHH	28.35	21890473
155	Ubiquitination	LDGSRLIKVHLDKAQ ECCCEEEEEEHHHHH	28.35	23000965
155	Acetylation	LDGSRLIKVHLDKAQ ECCCEEEEEEHHHHH	28.35	25825284
160	2-Hydroxyisobutyrylation	LIKVHLDKAQQNNVE EEEEEHHHHHHCCCC	55.22	-
160	Ubiquitination	LIKVHLDKAQQNNVE EEEEEHHHHHHCCCC	55.22	23000965
160	Acetylation	LIKVHLDKAQQNNVE EEEEEHHHHHHCCCC	55.22	23236377
169	Sumoylation	QQNNVEHKVETFSGV HHCCCCHHHHEEHHH	28.41	-
169	2-Hydroxyisobutyrylation	QQNNVEHKVETFSGV HHCCCCHHHHEEHHH	28.41	-
169	Ubiquitination	QQNNVEHKVETFSGV HHCCCCHHHHEEHHH	28.41	21963094
169	Acetylation	QQNNVEHKVETFSGV HHCCCCHHHHEEHHH	28.41	19608861
172	Phosphorylation	NVEHKVETFSGVYKK CCCHHHHEEHHHHHH	26.53	28152594
174	Phosphorylation	EHKVETFSGVYKKLT CHHHHEEHHHHHHHH	34.47	28152594
177	Phosphorylation	VETFSGVYKKLTGKD HHEEHHHHHHHHCCC	13.11	28152594
177	Nitration	VETFSGVYKKLTGKD HHEEHHHHHHHHCCC	13.11	-
178	Ubiquitination	ETFSGVYKKLTGKDV HEEHHHHHHHHCCCC	38.61	21906983
178	2-Hydroxyisobutyrylation	ETFSGVYKKLTGKDV HEEHHHHHHHHCCCC	38.61	-
178	Acetylation	ETFSGVYKKLTGKDV HEEHHHHHHHHCCCC	38.61	25953088
178	Methylation	ETFSGVYKKLTGKDV HEEHHHHHHHHCCCC	38.61	24470459
179	Ubiquitination	TFSGVYKKLTGKDVN EEHHHHHHHHCCCCC	33.33	22817900
179	Acetylation	TFSGVYKKLTGKDVN EEHHHHHHHHCCCCC	33.33	23954790
183	Ubiquitination	VYKKLTGKDVNFEFP HHHHHHCCCCCCCCC	53.95	21906983
183	Sumoylation	VYKKLTGKDVNFEFP HHHHHHCCCCCCCCC	53.95	-
183	Acetylation	VYKKLTGKDVNFEFP HHHHHHCCCCCCCCC	53.95	26051181
183	2-Hydroxyisobutyrylation	VYKKLTGKDVNFEFP HHHHHHCCCCCCCCC	53.95	-
183	Ubiquitination	VYKKLTGKDVNFEFP HHHHHHCCCCCCCCC	53.95	21890473

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 RS7_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of RS7_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 RS7_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
MDM2_HUMAN	MDM2	physical	21561866
MDM2_HUMAN	MDM2	physical	19683495
P53_HUMAN	TP53	physical	19683495
MDM2_HUMAN	MDM2	physical	17310983
RS8_HUMAN	RPS8	physical	22939629
RSSA_HUMAN	RPSA	physical	22939629
RS9_HUMAN	RPS9	physical	22939629
U2AF1_HUMAN	U2AF1	physical	22939629
SMD1_HUMAN	SNRPD1	physical	22939629
DX39B_HUMAN	DDX39B	physical	22939629
GA45A_HUMAN	GADD45A	physical	23563151
MDM2_HUMAN	MDM2	physical	23563151
PNO1_HUMAN	PNO1	physical	22863883
PRS6B_HUMAN	PSMC4	physical	22863883
RS12_HUMAN	RPS12	physical	22863883
RS13_HUMAN	RPS13	physical	22863883
RS14_HUMAN	RPS14	physical	22863883
RS15A_HUMAN	RPS15A	physical	22863883
RS19_HUMAN	RPS19	physical	22863883
RS20_HUMAN	RPS20	physical	22863883
RS26_HUMAN	RPS26	physical	22863883
RS27L_HUMAN	RPS27L	physical	22863883
RS27_HUMAN	RPS27	physical	22863883
RS28_HUMAN	RPS28	physical	22863883
RS5_HUMAN	RPS5	physical	22863883
RS6_HUMAN	RPS6	physical	22863883
RS8_HUMAN	RPS8	physical	22863883
TSR1_HUMAN	TSR1	physical	22863883
PYM1_HUMAN	WIBG	physical	22863883
ZBT14_HUMAN	ZBTB14	physical	25416956
DDX23_HUMAN	DDX23	physical	26344197
NOL6_HUMAN	NOL6	physical	26344197
RL10A_HUMAN	RPL10A	physical	26344197
RL12_HUMAN	RPL12	physical	26344197
RL14_HUMAN	RPL14	physical	26344197
RL23A_HUMAN	RPL23A	physical	26344197
RL37A_HUMAN	RPL37A	physical	26344197
RL4_HUMAN	RPL4	physical	26344197
RS18_HUMAN	RPS18	physical	26344197
RS23_HUMAN	RPS23	physical	26344197
RS26_HUMAN	RPS26	physical	26344197
RL40_HUMAN	UBA52	physical	26344197
RL36L_HUMAN	RPL36AL	physical	28514442
MDM2_HUMAN	MDM2	physical	28514442
TRI26_HUMAN	TRIM26	physical	28514442
RL26L_HUMAN	RPL26L1	physical	28514442
RL5_HUMAN	RPL5	physical	28514442
RS15A_HUMAN	RPS15A	physical	28514442

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
612563	Diamond-Blackfan anemia 8 (DBA8)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of RS7_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-74 AND LYS-169, AND MASSSPECTROMETRY.	19608861 [Abstract]