dbPTM

RS13_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RS13_HUMAN
UniProt AC	P62277
Protein Name	40S ribosomal protein S13
Gene Name	RPS13
Organism	Homo sapiens (Human).
Sequence Length	151
Subcellular Localization
Protein Description
Protein Sequence	MGRMHAPGKGLSQSALPYRRSVPTWLKLTSDDVKEQIYKLAKKGLTPSQIGVILRDSHGVAQVRFVTGNKILRILKSKGLAPDLPEDLYHLIKKAVAVRKHLERNRKDKDAKFRLILIESRIHRLARYYKTKRVLPPNWKYESSTASALVA

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
9	2-Hydroxyisobutyrylation	GRMHAPGKGLSQSAL CCCCCCCCCCCCCCC	56.47	-
9	Ubiquitination	GRMHAPGKGLSQSAL CCCCCCCCCCCCCCC	56.47	23000965
9	Acetylation	GRMHAPGKGLSQSAL CCCCCCCCCCCCCCC	56.47	26051181
12	Phosphorylation	HAPGKGLSQSALPYR CCCCCCCCCCCCCCC	30.66	21712546
14	Phosphorylation	PGKGLSQSALPYRRS CCCCCCCCCCCCCCC	28.53	30108239
18	Phosphorylation	LSQSALPYRRSVPTW CCCCCCCCCCCCCCE	21.36	28152594
21	Phosphorylation	SALPYRRSVPTWLKL CCCCCCCCCCCEEEC	24.37	20068231
24	Phosphorylation	PYRRSVPTWLKLTSD CCCCCCCCEEECCCH	41.07	20068231
27	Succinylation	RSVPTWLKLTSDDVK CCCCCEEECCCHHHH	41.08	-
27	Succinylation	RSVPTWLKLTSDDVK CCCCCEEECCCHHHH	41.08	21890473
27	Ubiquitination	RSVPTWLKLTSDDVK CCCCCEEECCCHHHH	41.08	27667366
27	2-Hydroxyisobutyrylation	RSVPTWLKLTSDDVK CCCCCEEECCCHHHH	41.08	-
27	Acetylation	RSVPTWLKLTSDDVK CCCCCEEECCCHHHH	41.08	19608861
29	Phosphorylation	VPTWLKLTSDDVKEQ CCCEEECCCHHHHHH	28.64	19691289
30	Phosphorylation	PTWLKLTSDDVKEQI CCEEECCCHHHHHHH	42.10	19691289
34	Ubiquitination	KLTSDDVKEQIYKLA ECCCHHHHHHHHHHH	51.39	23000965
34	Succinylation	KLTSDDVKEQIYKLA ECCCHHHHHHHHHHH	51.39	-
34	Succinylation	KLTSDDVKEQIYKLA ECCCHHHHHHHHHHH	51.39	23954790
34	Acetylation	KLTSDDVKEQIYKLA ECCCHHHHHHHHHHH	51.39	25825284
38	Phosphorylation	DDVKEQIYKLAKKGL HHHHHHHHHHHHCCC	10.31	27155012
39	Acetylation	DVKEQIYKLAKKGLT HHHHHHHHHHHCCCC	43.53	23749302
39	Ubiquitination	DVKEQIYKLAKKGLT HHHHHHHHHHHCCCC	43.53	23000965
39	Malonylation	DVKEQIYKLAKKGLT HHHHHHHHHHHCCCC	43.53	26320211
42	Ubiquitination	EQIYKLAKKGLTPSQ HHHHHHHHCCCCHHH	58.78	23000965
43	Sumoylation	QIYKLAKKGLTPSQI HHHHHHHCCCCHHHH	54.25	28112733
43	Malonylation	QIYKLAKKGLTPSQI HHHHHHHCCCCHHHH	54.25	26320211
43	Ubiquitination	QIYKLAKKGLTPSQI HHHHHHHCCCCHHHH	54.25	23000965
43	Acetylation	QIYKLAKKGLTPSQI HHHHHHHCCCCHHHH	54.25	26051181
46	Phosphorylation	KLAKKGLTPSQIGVI HHHHCCCCHHHHEEE	29.57	-
48	Phosphorylation	AKKGLTPSQIGVILR HHCCCCHHHHEEEEE	29.24	28450419
57	Phosphorylation	IGVILRDSHGVAQVR HEEEEECCCCEEEEE	18.73	20860994
70	Ubiquitination	VRFVTGNKILRILKS EEEEEHHHHHHHHHH	44.45	23000965
70	2-Hydroxyisobutyrylation	VRFVTGNKILRILKS EEEEEHHHHHHHHHH	44.45	-
76	Ubiquitination	NKILRILKSKGLAPD HHHHHHHHHCCCCCC	47.99	23000965
78	Ubiquitination	ILRILKSKGLAPDLP HHHHHHHCCCCCCCC	57.25	23000965
78	2-Hydroxyisobutyrylation	ILRILKSKGLAPDLP HHHHHHHCCCCCCCC	57.25	-
78	Acetylation	ILRILKSKGLAPDLP HHHHHHHCCCCCCCC	57.25	26051181
89	Phosphorylation	PDLPEDLYHLIKKAV CCCCHHHHHHHHHHH	13.60	-
93	2-Hydroxyisobutyrylation	EDLYHLIKKAVAVRK HHHHHHHHHHHHHHH	40.83	-
93	Ubiquitination	EDLYHLIKKAVAVRK HHHHHHHHHHHHHHH	40.83	21906983
93	Acetylation	EDLYHLIKKAVAVRK HHHHHHHHHHHHHHH	40.83	26051181
94	Ubiquitination	DLYHLIKKAVAVRKH HHHHHHHHHHHHHHH	40.89	22817900
107	Ubiquitination	KHLERNRKDKDAKFR HHHHHCCCCCCCCHH	73.08	24816145
109	Ubiquitination	LERNRKDKDAKFRLI HHHCCCCCCCCHHHH	63.72	24816145
112	2-Hydroxyisobutyrylation	NRKDKDAKFRLILIE CCCCCCCCHHHHHHH	40.94	-
120	Phosphorylation	FRLILIESRIHRLAR HHHHHHHHHHHHHHH	29.55	21712546
128	Phosphorylation	RIHRLARYYKTKRVL HHHHHHHHHCCCCCC	12.05	22817900
129	Phosphorylation	IHRLARYYKTKRVLP HHHHHHHHCCCCCCC	13.46	17081983
141	Phosphorylation	VLPPNWKYESSTASA CCCCCCCCCCCCCHH	16.80	28152594
143	Phosphorylation	PPNWKYESSTASALV CCCCCCCCCCCHHHC	29.87	28152594
144	Phosphorylation	PNWKYESSTASALVA CCCCCCCCCCHHHCC	18.95	28152594
145	Phosphorylation	NWKYESSTASALVA- CCCCCCCCCHHHCC-	33.63	28152594
147	Phosphorylation	KYESSTASALVA--- CCCCCCCHHHCC---	23.40	28152594

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 RS13_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of RS13_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 RS13_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PDCD4_HUMAN	PDCD4	physical	12054647
RS14_HUMAN	RPS14	physical	22939629
RS15A_HUMAN	RPS15A	physical	22939629
RS16_HUMAN	RPS16	physical	22939629
RS19_HUMAN	RPS19	physical	22939629
RS23_HUMAN	RPS23	physical	22939629
RS24_HUMAN	RPS24	physical	22939629
RS26_HUMAN	RPS26	physical	22939629
RS2_HUMAN	RPS2	physical	22939629
RS3A_HUMAN	RPS3A	physical	22939629
RS4X_HUMAN	RPS4X	physical	22939629
RS5_HUMAN	RPS5	physical	22939629
RS7_HUMAN	RPS7	physical	22939629
RS8_HUMAN	RPS8	physical	22939629
RS6_HUMAN	RPS6	physical	22939629
RS15_HUMAN	RPS15	physical	22939629
RS3_HUMAN	RPS3	physical	22939629
RS25_HUMAN	RPS25	physical	22939629
RSSA_HUMAN	RPSA	physical	22939629
RS28_HUMAN	RPS28	physical	22939629
RS9_HUMAN	RPS9	physical	22939629
RS20_HUMAN	RPS20	physical	22939629
RS17_HUMAN	RPS17	physical	22939629
RS21_HUMAN	RPS21	physical	22939629
RS27A_HUMAN	RPS27A	physical	22939629
UBIM_HUMAN	FAU	physical	22939629
U2AF1_HUMAN	U2AF1	physical	22939629
RS27L_HUMAN	RPS27L	physical	22939629
DC1I2_HUMAN	DYNC1I2	physical	22863883
RSSA_HUMAN	RPSA	physical	22863883
LARP1_HUMAN	LARP1	physical	22863883
PNO1_HUMAN	PNO1	physical	22863883
PRS4_HUMAN	PSMC1	physical	22863883
PRS8_HUMAN	PSMC5	physical	22863883
PSMD3_HUMAN	PSMD3	physical	22863883
PSMD7_HUMAN	PSMD7	physical	22863883
RANB9_HUMAN	RANBP9	physical	22863883
RS10_HUMAN	RPS10	physical	22863883
RS12_HUMAN	RPS12	physical	22863883
RS14_HUMAN	RPS14	physical	22863883
RS15A_HUMAN	RPS15A	physical	22863883
RS26_HUMAN	RPS26	physical	22863883
RS3_HUMAN	RPS3	physical	22863883
RS6_HUMAN	RPS6	physical	22863883
RS8_HUMAN	RPS8	physical	22863883
TSR1_HUMAN	TSR1	physical	22863883
PYM1_HUMAN	WIBG	physical	22863883
BRX1_HUMAN	BRIX1	physical	26344197
DIM1_HUMAN	DIMT1	physical	26344197
EF1A1_HUMAN	EEF1A1	physical	26344197
EIF2A_HUMAN	EIF2A	physical	26344197
EIF3I_HUMAN	EIF3I	physical	26344197
FBRL_HUMAN	FBL	physical	26344197
IMP3_HUMAN	IMP3	physical	26344197
NUMA1_HUMAN	NUMA1	physical	26344197
RL10_HUMAN	RPL10	physical	26344197
RL10A_HUMAN	RPL10A	physical	26344197
RL10L_HUMAN	RPL10L	physical	26344197
RL11_HUMAN	RPL11	physical	26344197
RL12_HUMAN	RPL12	physical	26344197
RL13_HUMAN	RPL13	physical	26344197
RL13A_HUMAN	RPL13A	physical	26344197
RL14_HUMAN	RPL14	physical	26344197
RL15_HUMAN	RPL15	physical	26344197
RL17_HUMAN	RPL17	physical	26344197
RL22_HUMAN	RPL22	physical	26344197
RL23A_HUMAN	RPL23A	physical	26344197
RL24_HUMAN	RPL24	physical	26344197
RL26_HUMAN	RPL26	physical	26344197
RL26L_HUMAN	RPL26L1	physical	26344197
RL27_HUMAN	RPL27	physical	26344197
RL27A_HUMAN	RPL27A	physical	26344197
RL30_HUMAN	RPL30	physical	26344197
RL34_HUMAN	RPL34	physical	26344197
RL35_HUMAN	RPL35	physical	26344197
RL35A_HUMAN	RPL35A	physical	26344197
RL36_HUMAN	RPL36	physical	26344197
RL37_HUMAN	RPL37	physical	26344197
RL37A_HUMAN	RPL37A	physical	26344197
RL38_HUMAN	RPL38	physical	26344197
RL4_HUMAN	RPL4	physical	26344197
RL5_HUMAN	RPL5	physical	26344197
RL6_HUMAN	RPL6	physical	26344197
RL7_HUMAN	RPL7	physical	26344197
RL7A_HUMAN	RPL7A	physical	26344197
RL8_HUMAN	RPL8	physical	26344197
RL9_HUMAN	RPL9	physical	26344197
RLA0_HUMAN	RPLP0	physical	26344197
RLA1_HUMAN	RPLP1	physical	26344197
RLA2_HUMAN	RPLP2	physical	26344197
RS10_HUMAN	RPS10	physical	26344197
RS11_HUMAN	RPS11	physical	26344197
RS12_HUMAN	RPS12	physical	26344197
RS14_HUMAN	RPS14	physical	26344197
RS15_HUMAN	RPS15	physical	26344197
RS18_HUMAN	RPS18	physical	26344197
RS2_HUMAN	RPS2	physical	26344197
RS23_HUMAN	RPS23	physical	26344197
RS25_HUMAN	RPS25	physical	26344197
RS26_HUMAN	RPS26	physical	26344197
RS27_HUMAN	RPS27	physical	26344197
RS29_HUMAN	RPS29	physical	26344197
RS3_HUMAN	RPS3	physical	26344197
RS3A_HUMAN	RPS3A	physical	26344197
RS4X_HUMAN	RPS4X	physical	26344197
RS5_HUMAN	RPS5	physical	26344197
RS6_HUMAN	RPS6	physical	26344197
RS7_HUMAN	RPS7	physical	26344197
RS8_HUMAN	RPS8	physical	26344197
RS9_HUMAN	RPS9	physical	26344197
RSSA_HUMAN	RPSA	physical	26344197
SRRM2_HUMAN	SRRM2	physical	26344197
PR38A_HUMAN	PRPF38A	physical	27173435

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 RS13_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-27 AND LYS-39, AND MASSSPECTROMETRY.	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-12, AND MASSSPECTROMETRY.	18691976 [Abstract]
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column."; Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.; Anal. Sci. 24:161-166(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30, AND MASSSPECTROMETRY.	18187866 [Abstract]
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-128 AND TYR-129, ANDMASS SPECTROMETRY.	17081983 [Abstract]
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells."; Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.; Nat. Biotechnol. 23:94-101(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-38, AND MASSSPECTROMETRY.	15592455 [Abstract]