dbPTM

RS23_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RS23_HUMAN
UniProt AC	P62266
Protein Name	40S ribosomal protein S23
Gene Name	RPS23
Organism	Homo sapiens (Human).
Sequence Length	143
Subcellular Localization	Cytoplasm, cytosol . Cytoplasm . Rough endoplasmic reticulum . Detected on cytosolic polysomes (PubMed:25957688). Detected in ribosomes that are associated with the rough endoplasmic reticulum (By similarity).
Protein Description	Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. [PubMed: 28257692]
Protein Sequence	MGKCRGLRTARKLRSHRRDQKWHDKQYKKAHLGTALKANPFGGASHAKGIVLEKVGVEAKQPNSAIRKCVRVQLIKNGKKITAFVPNDGCLNFIEENDEVLVAGFGRKGHAVGDIPGVRFKVVKVANVSLLALYKGKKERPRS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
21	2-Hydroxyisobutyrylation	RSHRRDQKWHDKQYK HHCCCCCCCCHHHHH	51.27	-
25	Ubiquitination	RDQKWHDKQYKKAHL CCCCCCHHHHHHHHH	42.51	-
25	Acetylation	RDQKWHDKQYKKAHL CCCCCCHHHHHHHHH	42.51	27452117
25	2-Hydroxyisobutyrylation	RDQKWHDKQYKKAHL CCCCCCHHHHHHHHH	42.51	-
29	Sumoylation	WHDKQYKKAHLGTAL CCHHHHHHHHHHHHH	35.78	-
29	2-Hydroxyisobutyrylation	WHDKQYKKAHLGTAL CCHHHHHHHHHHHHH	35.78	-
29	Sumoylation	WHDKQYKKAHLGTAL CCHHHHHHHHHHHHH	35.78	-
29	Ubiquitination	WHDKQYKKAHLGTAL CCHHHHHHHHHHHHH	35.78	-
34	Phosphorylation	YKKAHLGTALKANPF HHHHHHHHHHHCCCC	34.87	20068231
37	Acetylation	AHLGTALKANPFGGA HHHHHHHHCCCCCCC	43.59	25953088
37	Sumoylation	AHLGTALKANPFGGA HHHHHHHHCCCCCCC	43.59	-
37	Ubiquitination	AHLGTALKANPFGGA HHHHHHHHCCCCCCC	43.59	21890473
37	Sumoylation	AHLGTALKANPFGGA HHHHHHHHCCCCCCC	43.59	28112733
48	Acetylation	FGGASHAKGIVLEKV CCCCCCCCCEEEEEE	43.69	26051181
48	2-Hydroxyisobutyrylation	FGGASHAKGIVLEKV CCCCCCCCCEEEEEE	43.69	-
48	Ubiquitination	FGGASHAKGIVLEKV CCCCCCCCCEEEEEE	43.69	21890473
48	Sumoylation	FGGASHAKGIVLEKV CCCCCCCCCEEEEEE	43.69	-
48	Sumoylation	FGGASHAKGIVLEKV CCCCCCCCCEEEEEE	43.69	-
54	Ubiquitination	AKGIVLEKVGVEAKQ CCCEEEEEECCCCCC	39.88	21890473
54	Acetylation	AKGIVLEKVGVEAKQ CCCEEEEEECCCCCC	39.88	26051181
54	Succinylation	AKGIVLEKVGVEAKQ CCCEEEEEECCCCCC	39.88	21890473
54	2-Hydroxyisobutyrylation	AKGIVLEKVGVEAKQ CCCEEEEEECCCCCC	39.88	-
54	Sumoylation	AKGIVLEKVGVEAKQ CCCEEEEEECCCCCC	39.88	-
54	Succinylation	AKGIVLEKVGVEAKQ CCCEEEEEECCCCCC	39.88	-
60	Ubiquitination	EKVGVEAKQPNSAIR EEECCCCCCCCHHHH	53.43	-
62	Hydroxylation	VGVEAKQPNSAIRKC ECCCCCCCCHHHHHH	35.72	24550462
76	2-Hydroxyisobutyrylation	CVRVQLIKNGKKITA HHEEEEEECCCEEEE	69.14	-
76	Ubiquitination	CVRVQLIKNGKKITA HHEEEEEECCCEEEE	69.14	-
76	Acetylation	CVRVQLIKNGKKITA HHEEEEEECCCEEEE	69.14	25953088
80	Ubiquitination	QLIKNGKKITAFVPN EEEECCCEEEEEECC	46.84	-
108	Ubiquitination	LVAGFGRKGHAVGDI EEEECCCCCCCCCCC	56.26	-
129	Phosphorylation	VVKVANVSLLALYKG EEEEECHHHHHHHCC	19.92	28450419
134	Phosphorylation	NVSLLALYKGKKERP CHHHHHHHCCCCCCC	16.46	21552520
135	Ubiquitination	VSLLALYKGKKERPR HHHHHHHCCCCCCCC	66.17	21890473
135	Acetylation	VSLLALYKGKKERPR HHHHHHHCCCCCCCC	66.17	19608861
138	Ubiquitination	LALYKGKKERPRS-- HHHHCCCCCCCCC--	68.57	-

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 RS23_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
62	P	Hydroxylation		24550462
Hydroxylation at Pro-62 affects translation termination efficiency.

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 RS23_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RS25_HUMAN	RPS25	physical	22939629
RS28_HUMAN	RPS28	physical	22939629
RS3A_HUMAN	RPS3A	physical	22939629
RS3_HUMAN	RPS3	physical	22939629
RS4X_HUMAN	RPS4X	physical	22939629
RS5_HUMAN	RPS5	physical	22939629
RS6_HUMAN	RPS6	physical	22939629
RS7_HUMAN	RPS7	physical	22939629
RS8_HUMAN	RPS8	physical	22939629
RSSA_HUMAN	RPSA	physical	22939629
RS2_HUMAN	RPS2	physical	22939629
RS24_HUMAN	RPS24	physical	22939629
RS26_HUMAN	RPS26	physical	22939629
RS9_HUMAN	RPS9	physical	22939629
RS27A_HUMAN	RPS27A	physical	22939629
UBIM_HUMAN	FAU	physical	22939629
RS29_HUMAN	RPS29	physical	22939629
RS27L_HUMAN	RPS27L	physical	22939629
VASN_HUMAN	VASN	physical	22939629
SAM50_HUMAN	SAMM50	physical	22939629
RT11_HUMAN	MRPS11	physical	22939629
EIF3A_HUMAN	EIF3A	physical	22863883
EIFCL_HUMAN	EIF3CL	physical	22863883
EIF3E_HUMAN	EIF3E	physical	22863883
UBIM_HUMAN	FAU	physical	22863883
RSSA_HUMAN	RPSA	physical	22863883
PNO1_HUMAN	PNO1	physical	22863883
RS11_HUMAN	RPS11	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
RS18_HUMAN	RPS18	physical	22863883
RS19_HUMAN	RPS19	physical	22863883
RS24_HUMAN	RPS24	physical	22863883
RS25_HUMAN	RPS25	physical	22863883
RS27_HUMAN	RPS27	physical	22863883
RS2_HUMAN	RPS2	physical	22863883
RS3A_HUMAN	RPS3A	physical	22863883
RS3_HUMAN	RPS3	physical	22863883
RS4X_HUMAN	RPS4X	physical	22863883
RS6_HUMAN	RPS6	physical	22863883
RS7_HUMAN	RPS7	physical	22863883
RS8_HUMAN	RPS8	physical	22863883
RS9_HUMAN	RPS9	physical	22863883
PAIRB_HUMAN	SERBP1	physical	22863883
TSR1_HUMAN	TSR1	physical	22863883
PYM1_HUMAN	WIBG	physical	22863883
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
RL28_HUMAN	RPL28	physical	26344197
RL30_HUMAN	RPL30	physical	26344197
RL31_HUMAN	RPL31	physical	26344197
RL37A_HUMAN	RPL37A	physical	26344197
RL5_HUMAN	RPL5	physical	26344197
RL7_HUMAN	RPL7	physical	26344197
RL7A_HUMAN	RPL7A	physical	26344197
RL9_HUMAN	RPL9	physical	26344197
RLA1_HUMAN	RPLP1	physical	26344197
RS15_HUMAN	RPS15	physical	26344197
RS16_HUMAN	RPS16	physical	26344197
RS17_HUMAN	RPS17	physical	26344197
RS18_HUMAN	RPS18	physical	26344197
RS26_HUMAN	RPS26	physical	26344197
RS27_HUMAN	RPS27	physical	26344197
RS4X_HUMAN	RPS4X	physical	26344197
RS5_HUMAN	RPS5	physical	26344197
RS6_HUMAN	RPS6	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 RS23_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-135, AND MASS SPECTROMETRY.	19608861 [Abstract]

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