dbPTM

RL10A_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RL10A_HUMAN
UniProt AC	P62906
Protein Name	60S ribosomal protein L10a
Gene Name	RPL10A
Organism	Homo sapiens (Human).
Sequence Length	217
Subcellular Localization
Protein Description	Component of the large ribosomal subunit..
Protein Sequence	MSSKVSRDTLYEAVREVLHGNQRKRRKFLETVELQISLKNYDPQKDKRFSGTVRLKSTPRPKFSVCVLGDQQHCDEAKAVDIPHMDIEALKKLNKNKKLVKKLAKKYDAFLASESLIKQIPRILGPGLNKAGKFPSLLTHNENMVAKVDEVKSTIKFQMKKVLCLAVAVGHVKMTDDELVYNIHLAVNFLVSLLKKNWQNVRALYIKSTMGKPQRLY

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MSSKVSRDT ------CCCCCCHHH	38.58	25072903
2	Acetylation	------MSSKVSRDT ------CCCCCCHHH	38.58	12962325
3	Phosphorylation	-----MSSKVSRDTL -----CCCCCCHHHH	35.46	25072903
4	Sumoylation	----MSSKVSRDTLY ----CCCCCCHHHHH	36.60	-
6	Phosphorylation	--MSSKVSRDTLYEA --CCCCCCHHHHHHH	28.33	28152594
9	Phosphorylation	SSKVSRDTLYEAVRE CCCCCHHHHHHHHHH	30.08	28152594
11	Phosphorylation	KVSRDTLYEAVREVL CCCHHHHHHHHHHHH	12.16	27273156
23	Methylation	EVLHGNQRKRRKFLE HHHHCCHHHHHHHHH	38.15	115491583
31	Phosphorylation	KRRKFLETVELQISL HHHHHHHHEEEEEEC	22.79	25690035
37	Phosphorylation	ETVELQISLKNYDPQ HHEEEEEECCCCCCC	21.96	25690035
45	2-Hydroxyisobutyrylation	LKNYDPQKDKRFSGT CCCCCCCCCCCCCEE	71.28	-
47	Acetylation	NYDPQKDKRFSGTVR CCCCCCCCCCCEEEE	63.48	25953088
50	Phosphorylation	PQKDKRFSGTVRLKS CCCCCCCCEEEEECC	37.27	29214152
52	Phosphorylation	KDKRFSGTVRLKSTP CCCCCCEEEEECCCC	10.97	21857030
56	Ubiquitination	FSGTVRLKSTPRPKF CCEEEEECCCCCCCE	41.54	-
62	Acetylation	LKSTPRPKFSVCVLG ECCCCCCCEEEEEEE	52.10	25825284
62	2-Hydroxyisobutyrylation	LKSTPRPKFSVCVLG ECCCCCCCEEEEEEE	52.10	-
62	Ubiquitination	LKSTPRPKFSVCVLG ECCCCCCCEEEEEEE	52.10	-
64	Phosphorylation	STPRPKFSVCVLGDQ CCCCCCEEEEEEECH	22.26	-
66	S-palmitoylation	PRPKFSVCVLGDQQH CCCCEEEEEEECHHH	1.71	21044946
74	S-palmitoylation	VLGDQQHCDEAKAVD EEECHHHCCCCHHCC	4.37	21044946
74	Glutathionylation	VLGDQQHCDEAKAVD EEECHHHCCCCHHCC	4.37	22555962
78	2-Hydroxyisobutyrylation	QQHCDEAKAVDIPHM HHHCCCCHHCCCCCC	47.06	-
78	Acetylation	QQHCDEAKAVDIPHM HHHCCCCHHCCCCCC	47.06	25953088
78	Ubiquitination	QQHCDEAKAVDIPHM HHHCCCCHHCCCCCC	47.06	-
85	Sulfoxidation	KAVDIPHMDIEALKK HHCCCCCCCHHHHHH	4.69	30846556
91	Acetylation	HMDIEALKKLNKNKK CCCHHHHHHHHHCHH	63.36	23954790
91	2-Hydroxyisobutyrylation	HMDIEALKKLNKNKK CCCHHHHHHHHHCHH	63.36	-
91	Ubiquitination	HMDIEALKKLNKNKK CCCHHHHHHHHHCHH	63.36	21890473
91	Malonylation	HMDIEALKKLNKNKK CCCHHHHHHHHHCHH	63.36	26320211
92	Ubiquitination	MDIEALKKLNKNKKL CCHHHHHHHHHCHHH	59.13	-
92	Acetylation	MDIEALKKLNKNKKL CCHHHHHHHHHCHHH	59.13	156251
106	Sumoylation	LVKKLAKKYDAFLAS HHHHHHHHHHHHHHC	42.63	-
106	Methylation	LVKKLAKKYDAFLAS HHHHHHHHHHHHHHC	42.63	23748837
106	Ubiquitination	LVKKLAKKYDAFLAS HHHHHHHHHHHHHHC	42.63	21890473
106	Sumoylation	LVKKLAKKYDAFLAS HHHHHHHHHHHHHHC	42.63	19608861
106	Acetylation	LVKKLAKKYDAFLAS HHHHHHHHHHHHHHC	42.63	19608861
106	Malonylation	LVKKLAKKYDAFLAS HHHHHHHHHHHHHHC	42.63	26320211
107	Phosphorylation	VKKLAKKYDAFLASE HHHHHHHHHHHHHCH	16.28	28152594
113	Phosphorylation	KYDAFLASESLIKQI HHHHHHHCHHHHHHH	29.84	28450419
115	Phosphorylation	DAFLASESLIKQIPR HHHHHCHHHHHHHHH	32.66	28450419
118	Sumoylation	LASESLIKQIPRILG HHCHHHHHHHHHHHC	47.68	19608861
118	Ubiquitination	LASESLIKQIPRILG HHCHHHHHHHHHHHC	47.68	21890473
118	2-Hydroxyisobutyrylation	LASESLIKQIPRILG HHCHHHHHHHHHHHC	47.68	-
118	Acetylation	LASESLIKQIPRILG HHCHHHHHHHHHHHC	47.68	19608861
130	Ubiquitination	ILGPGLNKAGKFPSL HHCCCCCCCCCCHHH	64.66	21890473
130	Malonylation	ILGPGLNKAGKFPSL HHCCCCCCCCCCHHH	64.66	26320211
130	Acetylation	ILGPGLNKAGKFPSL HHCCCCCCCCCCHHH	64.66	25953088
133	Ubiquitination	PGLNKAGKFPSLLTH CCCCCCCCCHHHHCC	59.99	21890473
133	Acetylation	PGLNKAGKFPSLLTH CCCCCCCCCHHHHCC	59.99	23749302
136	Phosphorylation	NKAGKFPSLLTHNEN CCCCCCHHHHCCCCC	38.86	30108239
139	Phosphorylation	GKFPSLLTHNENMVA CCCHHHHCCCCCCEE	28.13	30108239
144	Sulfoxidation	LLTHNENMVAKVDEV HHCCCCCCEEEHHHH	2.24	30846556
147	Ubiquitination	HNENMVAKVDEVKST CCCCCEEEHHHHHHH	38.52	-
147	Acetylation	HNENMVAKVDEVKST CCCCCEEEHHHHHHH	38.52	26051181
147	2-Hydroxyisobutyrylation	HNENMVAKVDEVKST CCCCCEEEHHHHHHH	38.52	-
152	2-Hydroxyisobutyrylation	VAKVDEVKSTIKFQM EEEHHHHHHHHHHHH	39.57	-
152	Ubiquitination	VAKVDEVKSTIKFQM EEEHHHHHHHHHHHH	39.57	-
152	Succinylation	VAKVDEVKSTIKFQM EEEHHHHHHHHHHHH	39.57	23954790
152	Acetylation	VAKVDEVKSTIKFQM EEEHHHHHHHHHHHH	39.57	25953088
156	Ubiquitination	DEVKSTIKFQMKKVL HHHHHHHHHHHHHHH	29.63	-
156	Acetylation	DEVKSTIKFQMKKVL HHHHHHHHHHHHHHH	29.63	26051181
161	Sumoylation	TIKFQMKKVLCLAVA HHHHHHHHHHHHHHH	34.79	28112733
161	Acetylation	TIKFQMKKVLCLAVA HHHHHHHHHHHHHHH	34.79	26051181
164	S-palmitoylation	FQMKKVLCLAVAVGH HHHHHHHHHHHHHCC	2.28	29575903
174	Sulfoxidation	VAVGHVKMTDDELVY HHHCCCCCCCCHHHH	4.90	28183972
192	Phosphorylation	LAVNFLVSLLKKNWQ HHHHHHHHHHHHCCC	30.08	24719451
196	Acetylation	FLVSLLKKNWQNVRA HHHHHHHHCCCHHHH	64.49	26051181
196	Ubiquitination	FLVSLLKKNWQNVRA HHHHHHHHCCCHHHH	64.49	-
207	2-Hydroxyisobutyrylation	NVRALYIKSTMGKPQ HHHHHHHCCCCCCCC	26.73	-
207	Acetylation	NVRALYIKSTMGKPQ HHHHHHHCCCCCCCC	26.73	26051181
207	Ubiquitination	NVRALYIKSTMGKPQ HHHHHHHCCCCCCCC	26.73	-
212	Ubiquitination	YIKSTMGKPQRLY-- HHCCCCCCCCCCC--	27.44	21890473
215	Methylation	STMGKPQRLY----- CCCCCCCCCC-----	44.47	115491591
217	Phosphorylation	MGKPQRLY------- CCCCCCCC-------	20.78	28102081

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 RL10A_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of RL10A_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 RL10A_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RL21_HUMAN	RPL21	physical	22939629
RL6_HUMAN	RPL6	physical	22939629
RL7A_HUMAN	RPL7A	physical	22939629
RS3A_HUMAN	RPS3A	physical	22939629
RS3_HUMAN	RPS3	physical	22939629
RS9_HUMAN	RPS9	physical	22939629
RL4_HUMAN	RPL4	physical	22939629
RL7_HUMAN	RPL7	physical	22939629
RLA0_HUMAN	RPLP0	physical	22939629
RL11_HUMAN	RPL11	physical	22939629
RL12_HUMAN	RPL12	physical	22939629
RL13_HUMAN	RPL13	physical	22939629
RL14_HUMAN	RPL14	physical	22939629
RL15_HUMAN	RPL15	physical	22939629
RL17_HUMAN	RPL17	physical	22939629
RL18A_HUMAN	RPL18A	physical	22939629
RL18_HUMAN	RPL18	physical	22939629
RL19_HUMAN	RPL19	physical	22939629
RL23_HUMAN	RPL23	physical	22939629
RL24_HUMAN	RPL24	physical	22939629
RL30_HUMAN	RPL30	physical	22939629
RL31_HUMAN	RPL31	physical	22939629
RL37A_HUMAN	RPL37A	physical	22939629
RL3_HUMAN	RPL3	physical	22939629
RL5_HUMAN	RPL5	physical	22939629
RL8_HUMAN	RPL8	physical	22939629
RL9_HUMAN	RPL9	physical	22939629
RS11_HUMAN	RPS11	physical	22939629
RS13_HUMAN	RPS13	physical	22939629
RS15A_HUMAN	RPS15A	physical	22939629
RS16_HUMAN	RPS16	physical	22939629
RS20_HUMAN	RPS20	physical	22939629
RS23_HUMAN	RPS23	physical	22939629
RS24_HUMAN	RPS24	physical	22939629
RS25_HUMAN	RPS25	physical	22939629
RS28_HUMAN	RPS28	physical	22939629
RS2_HUMAN	RPS2	physical	22939629
RS4X_HUMAN	RPS4X	physical	22939629
RS5_HUMAN	RPS5	physical	22939629
RS6_HUMAN	RPS6	physical	22939629
RS8_HUMAN	RPS8	physical	22939629
RSSA_HUMAN	RPSA	physical	22939629
RL23A_HUMAN	RPL23A	physical	22939629
RS26_HUMAN	RPS26	physical	22939629
RS12_HUMAN	RPS12	physical	22939629
RS19_HUMAN	RPS19	physical	22939629
RL22_HUMAN	RPL22	physical	22939629
RL32_HUMAN	RPL32	physical	22939629
RS21_HUMAN	RPS21	physical	22939629
RS27A_HUMAN	RPS27A	physical	22939629
RL29_HUMAN	RPL29	physical	22939629
RS27L_HUMAN	RPS27L	physical	22939629
RL10L_HUMAN	RPL10L	physical	22939629
S10AA_HUMAN	S100A10	physical	22939629
SRPRA_HUMAN	SRPR	physical	21988832
RGS17_HUMAN	RGS17	physical	25416956
DDX27_HUMAN	DDX27	physical	26186194
H2B2F_HUMAN	HIST2H2BF	physical	26186194
RL26L_HUMAN	RPL26L1	physical	26186194
NPA1P_HUMAN	URB1	physical	26186194
NOL8_HUMAN	NOL8	physical	26186194
NPM_HUMAN	NPM1	physical	26186194
NOG1_HUMAN	GTPBP4	physical	26186194
WDR89_HUMAN	WDR89	physical	26186194
RL36L_HUMAN	RPL36AL	physical	26186194
NOP2_HUMAN	NOP2	physical	26186194
UIF_HUMAN	FYTTD1	physical	26186194
MDM2_HUMAN	MDM2	physical	26186194
GZF1_HUMAN	GZF1	physical	26186194
ZCHC7_HUMAN	ZCCHC7	physical	26186194
RS8_HUMAN	RPS8	physical	26344197
H2B2F_HUMAN	HIST2H2BF	physical	28514442
WDR89_HUMAN	WDR89	physical	28514442
NOL8_HUMAN	NOL8	physical	28514442
SART3_HUMAN	SART3	physical	28514442
RL30_HUMAN	RPL30	physical	28514442
RL36L_HUMAN	RPL36AL	physical	28514442
ZCHC7_HUMAN	ZCCHC7	physical	28514442
ZCCHV_HUMAN	ZC3HAV1	physical	28514442
RBM34_HUMAN	RBM34	physical	28514442
H14_HUMAN	HIST1H1E	physical	28514442
MDM2_HUMAN	MDM2	physical	28514442
NOP53_HUMAN	GLTSCR2	physical	28514442
RL18A_HUMAN	RPL18A	physical	28514442
NPM_HUMAN	NPM1	physical	28514442
RL26L_HUMAN	RPL26L1	physical	28514442
PUM3_HUMAN	KIAA0020	physical	28514442
RBM4B_HUMAN	RBM4B	physical	28514442
UIF_HUMAN	FYTTD1	physical	28514442
RRP8_HUMAN	RRP8	physical	28514442

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 RL10A_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-106 AND LYS-118, AND MASSSPECTROMETRY.	19608861 [Abstract]