dbPTM

RS5_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RS5_HUMAN
UniProt AC	P46782
Protein Name	40S ribosomal protein S5
Gene Name	RPS5
Organism	Homo sapiens (Human).
Sequence Length	204
Subcellular Localization
Protein Description
Protein Sequence	MTEWETAAPAVAETPDIKLFGKWSTDDVQINDISLQDYIAVKEKYAKYLPHSAGRYAAKRFRKAQCPIVERLTNSMMMHGRNNGKKLMTVRIVKHAFEIIHLLTGENPLQVLVNAIINSGPREDSTRIGRAGTVRRQAVDVSPLRRVNQAIWLLCTGAREAAFRNIKTIAECLADELINAAKGSSNSYAIKKKDELERVAKSNR

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MTEWETAA -------CCCCCCCC	7.46	22223895
2	Acetylation	------MTEWETAAP ------CCCCCCCCC	50.21	19413330
2	Phosphorylation	------MTEWETAAP ------CCCCCCCCC	50.21	21406692
6	Phosphorylation	--MTEWETAAPAVAE --CCCCCCCCCCCCC	29.23	20873877
14	Phosphorylation	AAPAVAETPDIKLFG CCCCCCCCCCEEEEC	19.27	28355574
18	2-Hydroxyisobutyrylation	VAETPDIKLFGKWST CCCCCCEEEECCCCC	45.18	-
18	Acetylation	VAETPDIKLFGKWST CCCCCCEEEECCCCC	45.18	27452117
18	Sumoylation	VAETPDIKLFGKWST CCCCCCEEEECCCCC	45.18	-
18	Ubiquitination	VAETPDIKLFGKWST CCCCCCEEEECCCCC	45.18	21890473
22	Ubiquitination	PDIKLFGKWSTDDVQ CCEEEECCCCCCCCE	30.54	21890473
22	Sumoylation	PDIKLFGKWSTDDVQ CCEEEECCCCCCCCE	30.54	-
25	Phosphorylation	KLFGKWSTDDVQIND EEECCCCCCCCEECC	34.79	18452278
38	Phosphorylation	NDISLQDYIAVKEKY CCCCHHHHHHHHHHH	4.28	-
42	Sumoylation	LQDYIAVKEKYAKYL HHHHHHHHHHHHHHC	39.19	-
42	Acetylation	LQDYIAVKEKYAKYL HHHHHHHHHHHHHHC	39.19	26051181
42	Ubiquitination	LQDYIAVKEKYAKYL HHHHHHHHHHHHHHC	39.19	21890473
44	Ubiquitination	DYIAVKEKYAKYLPH HHHHHHHHHHHHCCC	44.80	-
45	Phosphorylation	YIAVKEKYAKYLPHS HHHHHHHHHHHCCCH	14.93	-
47	Ubiquitination	AVKEKYAKYLPHSAG HHHHHHHHHCCCHHH	44.20	21906983
47	Acetylation	AVKEKYAKYLPHSAG HHHHHHHHHCCCHHH	44.20	19608861
47	Sumoylation	AVKEKYAKYLPHSAG HHHHHHHHHCCCHHH	44.20	28112733
48	Phosphorylation	VKEKYAKYLPHSAGR HHHHHHHHCCCHHHH	19.79	30266825
52	Phosphorylation	YAKYLPHSAGRYAAK HHHHCCCHHHHHHHH	30.40	30266825
55	Methylation	YLPHSAGRYAAKRFR HCCCHHHHHHHHHHH	20.03	83108447
56	Phosphorylation	LPHSAGRYAAKRFRK CCCHHHHHHHHHHHH	15.25	-
63	Ubiquitination	YAAKRFRKAQCPIVE HHHHHHHHCCCCHHH	39.85	-
66	Glutathionylation	KRFRKAQCPIVERLT HHHHHCCCCHHHHHH	2.72	22555962
66	S-palmitoylation	KRFRKAQCPIVERLT HHHHHCCCCHHHHHH	2.72	21044946
73	Phosphorylation	CPIVERLTNSMMMHG CCHHHHHHHHHHHCC	31.31	28450419
75	Phosphorylation	IVERLTNSMMMHGRN HHHHHHHHHHHCCCC	11.65	28450419
76	Sulfoxidation	VERLTNSMMMHGRNN HHHHHHHHHHCCCCC	2.76	30846556
77	Sulfoxidation	ERLTNSMMMHGRNNG HHHHHHHHHCCCCCC	1.47	30846556
78	Sulfoxidation	RLTNSMMMHGRNNGK HHHHHHHHCCCCCCC	1.96	30846556
86	Ubiquitination	HGRNNGKKLMTVRIV CCCCCCCEEEHHHHH	44.91	-
133	Phosphorylation	TRIGRAGTVRRQAVD CCCCCCCCHHCCCCC	15.17	26853621
136	Methylation	GRAGTVRRQAVDVSP CCCCCHHCCCCCCHH	25.19	115492751
142	Phosphorylation	RRQAVDVSPLRRVNQ HCCCCCCHHHHHHHH	17.47	30266825
145	Methylation	AVDVSPLRRVNQAIW CCCCHHHHHHHHHHH	43.83	115492759
155	S-nitrosocysteine	NQAIWLLCTGAREAA HHHHHHHHHHHHHHH	2.86	-
155	Glutathionylation	NQAIWLLCTGAREAA HHHHHHHHHHHHHHH	2.86	22555962
155	S-nitrosylation	NQAIWLLCTGAREAA HHHHHHHHHHHHHHH	2.86	22178444
167	Acetylation	EAAFRNIKTIAECLA HHHHHHHHHHHHHHH	37.11	26051181
167	Ubiquitination	EAAFRNIKTIAECLA HHHHHHHHHHHHHHH	37.11	21890473
168	Phosphorylation	AAFRNIKTIAECLAD HHHHHHHHHHHHHHH	22.94	26846344
172	S-nitrosocysteine	NIKTIAECLADELIN HHHHHHHHHHHHHHH	2.54	-
172	S-palmitoylation	NIKTIAECLADELIN HHHHHHHHHHHHHHH	2.54	29575903
172	S-nitrosylation	NIKTIAECLADELIN HHHHHHHHHHHHHHH	2.54	18335467
172	Glutathionylation	NIKTIAECLADELIN HHHHHHHHHHHHHHH	2.54	22555962
182	Ubiquitination	DELINAAKGSSNSYA HHHHHHHCCCCCCCC	57.84	21906983
182	Sumoylation	DELINAAKGSSNSYA HHHHHHHCCCCCCCC	57.84	19608861
182	2-Hydroxyisobutyrylation	DELINAAKGSSNSYA HHHHHHHCCCCCCCC	57.84	-
182	Acetylation	DELINAAKGSSNSYA HHHHHHHCCCCCCCC	57.84	26051181
184	Phosphorylation	LINAAKGSSNSYAIK HHHHHCCCCCCCCCC	26.16	20068231
185	Phosphorylation	INAAKGSSNSYAIKK HHHHCCCCCCCCCCC	38.16	20068231
187	Phosphorylation	AAKGSSNSYAIKKKD HHCCCCCCCCCCCHH	20.21	28152594
188	Phosphorylation	AKGSSNSYAIKKKDE HCCCCCCCCCCCHHH	19.32	28152594
191	2-Hydroxyisobutyrylation	SSNSYAIKKKDELER CCCCCCCCCHHHHHH	45.67	-
191	Sumoylation	SSNSYAIKKKDELER CCCCCCCCCHHHHHH	45.67	-
191	Acetylation	SSNSYAIKKKDELER CCCCCCCCCHHHHHH	45.67	25953088
191	Succinylation	SSNSYAIKKKDELER CCCCCCCCCHHHHHH	45.67	23954790
191	Ubiquitination	SSNSYAIKKKDELER CCCCCCCCCHHHHHH	45.67	-
191	Sumoylation	SSNSYAIKKKDELER CCCCCCCCCHHHHHH	45.67	-
192	Ubiquitination	SNSYAIKKKDELERV CCCCCCCCHHHHHHH	60.38	-
201	Sumoylation	DELERVAKSNR---- HHHHHHHHHCC----	45.46	-

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 RS5_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of RS5_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 RS5_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RS6_HUMAN	RPS6	physical	22939629
RS8_HUMAN	RPS8	physical	22939629
RSSA_HUMAN	RPSA	physical	22939629
RS7_HUMAN	RPS7	physical	22939629
RU2A_HUMAN	SNRPA1	physical	22939629
VATB2_HUMAN	ATP6V1B2	physical	22939629
EIFCL_HUMAN	EIF3CL	physical	22863883
RACK1_HUMAN	GNB2L1	physical	22863883
RSSA_HUMAN	RPSA	physical	22863883
LARP1_HUMAN	LARP1	physical	22863883
CND1_HUMAN	NCAPD2	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
RS19_HUMAN	RPS19	physical	22863883
RS20_HUMAN	RPS20	physical	22863883
RS23_HUMAN	RPS23	physical	22863883
RS24_HUMAN	RPS24	physical	22863883
RS25_HUMAN	RPS25	physical	22863883
RS27_HUMAN	RPS27	physical	22863883
RS28_HUMAN	RPS28	physical	22863883
RS29_HUMAN	RPS29	physical	22863883
RS2_HUMAN	RPS2	physical	22863883
RS6_HUMAN	RPS6	physical	22863883
RS8_HUMAN	RPS8	physical	22863883
TSR1_HUMAN	TSR1	physical	22863883
PYM1_HUMAN	WIBG	physical	22863883
CALX_HUMAN	CANX	physical	26344197
CLGN_HUMAN	CLGN	physical	26344197
EF1A1_HUMAN	EEF1A1	physical	26344197
FBRL_HUMAN	FBL	physical	26344197
RRF2M_HUMAN	GFM2	physical	26344197
GNL3_HUMAN	GNL3	physical	26344197
HBS1L_HUMAN	HBS1L	physical	26344197
HNRPK_HUMAN	HNRNPK	physical	26344197
KRR1_HUMAN	KRR1	physical	26344197
RM11_HUMAN	MRPL11	physical	26344197
RM22_HUMAN	MRPL22	physical	26344197
RM24_HUMAN	MRPL24	physical	26344197
RT10_HUMAN	MRPS10	physical	26344197
MSH2_HUMAN	MSH2	physical	26344197
NAT10_HUMAN	NAT10	physical	26344197
NOL6_HUMAN	NOL6	physical	26344197
RPA1_HUMAN	POLR1A	physical	26344197
RL10A_HUMAN	RPL10A	physical	26344197
RL11_HUMAN	RPL11	physical	26344197
RL12_HUMAN	RPL12	physical	26344197
RL13A_HUMAN	RPL13A	physical	26344197
RL22_HUMAN	RPL22	physical	26344197
RL23A_HUMAN	RPL23A	physical	26344197
RL24_HUMAN	RPL24	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
RL37A_HUMAN	RPL37A	physical	26344197
RL38_HUMAN	RPL38	physical	26344197
RL7A_HUMAN	RPL7A	physical	26344197
RL8_HUMAN	RPL8	physical	26344197
RL9_HUMAN	RPL9	physical	26344197
RLA1_HUMAN	RPLP1	physical	26344197
RS10_HUMAN	RPS10	physical	26344197
RS12_HUMAN	RPS12	physical	26344197
RS15_HUMAN	RPS15	physical	26344197
RS16_HUMAN	RPS16	physical	26344197
RS18_HUMAN	RPS18	physical	26344197
RS19_HUMAN	RPS19	physical	26344197
RS25_HUMAN	RPS25	physical	26344197
RS26_HUMAN	RPS26	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
RRP7A_HUMAN	RRP7A	physical	26344197
S61A1_HUMAN	SEC61A1	physical	26344197
TXTP_HUMAN	SLC25A1	physical	26344197
EFTU_HUMAN	TUFM	physical	26344197
RL40_HUMAN	UBA52	physical	26344197
WDR36_HUMAN	WDR36	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 RS5_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 MET-1, AND MASS SPECTROMETRY.	19413330 [Abstract]
"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-47, 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-142, AND MASSSPECTROMETRY.	18691976 [Abstract]