dbPTM

RL7A_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RL7A_HUMAN
UniProt AC	P62424
Protein Name	60S ribosomal protein L7a
Gene Name	RPL7A
Organism	Homo sapiens (Human).
Sequence Length	266
Subcellular Localization
Protein Description
Protein Sequence	MPKGKKAKGKKVAPAPAVVKKQEAKKVVNPLFEKRPKNFGIGQDIQPKRDLTRFVKWPRYIRLQRQRAILYKRLKVPPAINQFTQALDRQTATQLLKLAHKYRPETKQEKKQRLLARAEKKAAGKGDVPTKRPPVLRAGVNTVTTLVENKKAQLVVIAHDVDPIELVVFLPALCRKMGVPYCIIKGKARLGRLVHRKTCTTVAFTQVNSEDKGALAKLVEAIRTNYNDRYDEIRRHWGGNVLGPKSVARIAKLEKAKAKELATKLG

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
11	Malonylation	GKKAKGKKVAPAPAV CCCCCCCCCCCCCHH	52.91	26320211
11	Sumoylation	GKKAKGKKVAPAPAV CCCCCCCCCCCCCHH	52.91	28112733
11	Ubiquitination	GKKAKGKKVAPAPAV CCCCCCCCCCCCCHH	52.91	33845483
20	Sumoylation	APAPAVVKKQEAKKV CCCCHHCCHHHHHHH	41.98	-
20	2-Hydroxyisobutyrylation	APAPAVVKKQEAKKV CCCCHHCCHHHHHHH	41.98	-
20	Acetylation	APAPAVVKKQEAKKV CCCCHHCCHHHHHHH	41.98	25953088
20	Sumoylation	APAPAVVKKQEAKKV CCCCHHCCHHHHHHH	41.98	28112733
20	Ubiquitination	APAPAVVKKQEAKKV CCCCHHCCHHHHHHH	41.98	21906983
21	Sumoylation	PAPAVVKKQEAKKVV CCCHHCCHHHHHHHH	41.58	28112733
21	Ubiquitination	PAPAVVKKQEAKKVV CCCHHCCHHHHHHHH	41.58	33845483
25	Ubiquitination	VVKKQEAKKVVNPLF HCCHHHHHHHHCHHH	45.40	22817900
26	Acetylation	VKKQEAKKVVNPLFE CCHHHHHHHHCHHHH	59.47	26051181
26	Ubiquitination	VKKQEAKKVVNPLFE CCHHHHHHHHCHHHH	59.47	22817900
26	Ubiquitination	VKKQEAKKVVNPLFE CCHHHHHHHHCHHHH	59.47	21890473
34	2-Hydroxyisobutyrylation	VVNPLFEKRPKNFGI HHCHHHHHCCCCCCC	67.67	-
34	Acetylation	VVNPLFEKRPKNFGI HHCHHHHHCCCCCCC	67.67	19608861
34	Ubiquitination	VVNPLFEKRPKNFGI HHCHHHHHCCCCCCC	67.67	23000965
34	Ubiquitination	VVNPLFEKRPKNFGI HHCHHHHHCCCCCCC	67.67	21890473
37	Acetylation	PLFEKRPKNFGIGQD HHHHHCCCCCCCCCC	69.78	26051181
37	Ubiquitination	PLFEKRPKNFGIGQD HHHHHCCCCCCCCCC	69.78	23000965
37	Ubiquitination	PLFEKRPKNFGIGQD HHHHHCCCCCCCCCC	69.78	21890473
48	Sumoylation	IGQDIQPKRDLTRFV CCCCCCCCCCHHHHC	42.01	-
48	2-Hydroxyisobutyrylation	IGQDIQPKRDLTRFV CCCCCCCCCCHHHHC	42.01	-
48	Acetylation	IGQDIQPKRDLTRFV CCCCCCCCCCHHHHC	42.01	26051181
48	Succinylation	IGQDIQPKRDLTRFV CCCCCCCCCCHHHHC	42.01	23954790
48	Sumoylation	IGQDIQPKRDLTRFV CCCCCCCCCCHHHHC	42.01	28112733
48	Ubiquitination	IGQDIQPKRDLTRFV CCCCCCCCCCHHHHC	42.01	23000965
48	Ubiquitination	IGQDIQPKRDLTRFV CCCCCCCCCCHHHHC	42.01	21890473
56	Ubiquitination	RDLTRFVKWPRYIRL CCHHHHCCHHHHHHH	49.09	21890473
60	Phosphorylation	RFVKWPRYIRLQRQR HHCCHHHHHHHHHHH	6.06	22817900
71	Phosphorylation	QRQRAILYKRLKVPP HHHHHHHHHHCCCCH	6.48	-
72	Ubiquitination	RQRAILYKRLKVPPA HHHHHHHHHCCCCHH	48.05	23000965
75	Ubiquitination	AILYKRLKVPPAINQ HHHHHHCCCCHHHHH	57.64	23000965
75	Ubiquitination	AILYKRLKVPPAINQ HHHHHHCCCCHHHHH	57.64	21890473
84	Phosphorylation	PPAINQFTQALDRQT CHHHHHHHHHHHHHH	11.81	21955146
89	Methylation	QFTQALDRQTATQLL HHHHHHHHHHHHHHH	36.28	115492295
97	Acetylation	QTATQLLKLAHKYRP HHHHHHHHHHHHHCC	52.82	19608861
97	Malonylation	QTATQLLKLAHKYRP HHHHHHHHHHHHHCC	52.82	26320211
97	Sumoylation	QTATQLLKLAHKYRP HHHHHHHHHHHHHCC	52.82	28112733
97	Ubiquitination	QTATQLLKLAHKYRP HHHHHHHHHHHHHCC	52.82	23000965
97	Ubiquitination	QTATQLLKLAHKYRP HHHHHHHHHHHHHCC	52.82	21890473
101	2-Hydroxyisobutyrylation	QLLKLAHKYRPETKQ HHHHHHHHHCCCCHH	37.03	-
101	Acetylation	QLLKLAHKYRPETKQ HHHHHHHHHCCCCHH	37.03	25825284
101	Methylation	QLLKLAHKYRPETKQ HHHHHHHHHCCCCHH	37.03	23748837
101	Ubiquitination	QLLKLAHKYRPETKQ HHHHHHHHHCCCCHH	37.03	23000965
106	Phosphorylation	AHKYRPETKQEKKQR HHHHCCCCHHHHHHH	40.48	-
107	2-Hydroxyisobutyrylation	HKYRPETKQEKKQRL HHHCCCCHHHHHHHH	55.59	-
107	Ubiquitination	HKYRPETKQEKKQRL HHHCCCCHHHHHHHH	55.59	24816145
120	Ubiquitination	RLLARAEKKAAGKGD HHHHHHHHHHCCCCC	46.88	22817900
121	Ubiquitination	LLARAEKKAAGKGDV HHHHHHHHHCCCCCC	34.67	29967540
125	2-Hydroxyisobutyrylation	AEKKAAGKGDVPTKR HHHHHCCCCCCCCCC	47.41	-
125	Succinylation	AEKKAAGKGDVPTKR HHHHHCCCCCCCCCC	47.41	23954790
125	Sumoylation	AEKKAAGKGDVPTKR HHHHHCCCCCCCCCC	47.41	28112733
125	Ubiquitination	AEKKAAGKGDVPTKR HHHHHCCCCCCCCCC	47.41	23000965
131	2-Hydroxyisobutyrylation	GKGDVPTKRPPVLRA CCCCCCCCCCCCCCC	57.76	-
131	Acetylation	GKGDVPTKRPPVLRA CCCCCCCCCCCCCCC	57.76	25953088
131	Malonylation	GKGDVPTKRPPVLRA CCCCCCCCCCCCCCC	57.76	26320211
131	Ubiquitination	GKGDVPTKRPPVLRA CCCCCCCCCCCCCCC	57.76	23000965
131	Ubiquitination	GKGDVPTKRPPVLRA CCCCCCCCCCCCCCC	57.76	21890473
150	2-Hydroxyisobutyrylation	VTTLVENKKAQLVVI EHHHHCCCCEEEEEE	35.66	-
150	Acetylation	VTTLVENKKAQLVVI EHHHHCCCCEEEEEE	35.66	25953088
150	Malonylation	VTTLVENKKAQLVVI EHHHHCCCCEEEEEE	35.66	26320211
150	Ubiquitination	VTTLVENKKAQLVVI EHHHHCCCCEEEEEE	35.66	21963094
151	Acetylation	TTLVENKKAQLVVIA HHHHCCCCEEEEEEE	53.61	21466224
151	Ubiquitination	TTLVENKKAQLVVIA HHHHCCCCEEEEEEE	53.61	22817900
176	Sumoylation	FLPALCRKMGVPYCI HHHHHHHHHCCCEEE	38.72	-
176	2-Hydroxyisobutyrylation	FLPALCRKMGVPYCI HHHHHHHHHCCCEEE	38.72	-
176	Acetylation	FLPALCRKMGVPYCI HHHHHHHHHCCCEEE	38.72	26051181
176	Malonylation	FLPALCRKMGVPYCI HHHHHHHHHCCCEEE	38.72	26320211
176	Sumoylation	FLPALCRKMGVPYCI HHHHHHHHHCCCEEE	38.72	-
176	Ubiquitination	FLPALCRKMGVPYCI HHHHHHHHHCCCEEE	38.72	23000965
181	Phosphorylation	CRKMGVPYCIIKGKA HHHHCCCEEEEECCC	8.22	28152594
185	Acetylation	GVPYCIIKGKARLGR CCCEEEEECCCHHHH	34.15	25953088
185	Ubiquitination	GVPYCIIKGKARLGR CCCEEEEECCCHHHH	34.15	21963094
187	Ubiquitination	PYCIIKGKARLGRLV CEEEEECCCHHHHHC	25.90	-
197	2-Hydroxyisobutyrylation	LGRLVHRKTCTTVAF HHHHCCCCCCEEEEE	32.83	-
197	Ubiquitination	LGRLVHRKTCTTVAF HHHHCCCCCCEEEEE	32.83	33845483
198	Phosphorylation	GRLVHRKTCTTVAFT HHHCCCCCCEEEEEE	18.29	21601212
199	S-palmitoylation	RLVHRKTCTTVAFTQ HHCCCCCCEEEEEEE	3.17	21044946
200	Phosphorylation	LVHRKTCTTVAFTQV HCCCCCCEEEEEEEC	29.54	23312004
201	Phosphorylation	VHRKTCTTVAFTQVN CCCCCCEEEEEEECC	16.39	23312004
205	Phosphorylation	TCTTVAFTQVNSEDK CCEEEEEEECCCCCH	23.13	23312004
209	Phosphorylation	VAFTQVNSEDKGALA EEEEECCCCCHHHHH	48.60	28985074
212	2-Hydroxyisobutyrylation	TQVNSEDKGALAKLV EECCCCCHHHHHHHH	41.87	-
212	Acetylation	TQVNSEDKGALAKLV EECCCCCHHHHHHHH	41.87	23954790
212	Malonylation	TQVNSEDKGALAKLV EECCCCCHHHHHHHH	41.87	26320211
212	Ubiquitination	TQVNSEDKGALAKLV EECCCCCHHHHHHHH	41.87	23000965
217	Acetylation	EDKGALAKLVEAIRT CCHHHHHHHHHHHHH	54.65	19608861
217	Ubiquitination	EDKGALAKLVEAIRT CCHHHHHHHHHHHHH	54.65	23000965
217	Ubiquitination	EDKGALAKLVEAIRT CCHHHHHHHHHHHHH	54.65	21890473
223	Methylation	AKLVEAIRTNYNDRY HHHHHHHHHCCHHHH	24.78	115492263
224	Phosphorylation	KLVEAIRTNYNDRYD HHHHHHHHCCHHHHH	35.62	28152594
226	Phosphorylation	VEAIRTNYNDRYDEI HHHHHHCCHHHHHHH	20.16	28152594
229	Methylation	IRTNYNDRYDEIRRH HHHCCHHHHHHHHHH	36.84	115492279
230	Phosphorylation	RTNYNDRYDEIRRHW HHCCHHHHHHHHHHC	22.31	28152594
234	Methylation	NDRYDEIRRHWGGNV HHHHHHHHHHCCCCC	23.51	115492287
235	Methylation	DRYDEIRRHWGGNVL HHHHHHHHHCCCCCC	35.26	115492271
245	2-Hydroxyisobutyrylation	GGNVLGPKSVARIAK CCCCCCHHHHHHHHH	56.62	-
245	Acetylation	GGNVLGPKSVARIAK CCCCCCHHHHHHHHH	56.62	26210075
245	Sumoylation	GGNVLGPKSVARIAK CCCCCCHHHHHHHHH	56.62	28112733
245	Ubiquitination	GGNVLGPKSVARIAK CCCCCCHHHHHHHHH	56.62	23000965
245	Ubiquitination	GGNVLGPKSVARIAK CCCCCCHHHHHHHHH	56.62	21890473
252	Sumoylation	KSVARIAKLEKAKAK HHHHHHHHHHHHHHH	55.60	-
252	Sumoylation	KSVARIAKLEKAKAK HHHHHHHHHHHHHHH	55.60	-
252	Ubiquitination	KSVARIAKLEKAKAK HHHHHHHHHHHHHHH	55.60	27667366
255	Ubiquitination	ARIAKLEKAKAKELA HHHHHHHHHHHHHHH	66.67	22817900
257	Ubiquitination	IAKLEKAKAKELATK HHHHHHHHHHHHHHH	71.68	22817900
259	Ubiquitination	KLEKAKAKELATKLG HHHHHHHHHHHHHHC	53.18	21906983
264	Sumoylation	KAKELATKLG----- HHHHHHHHHC-----	45.67	-
264	Sumoylation	KAKELATKLG----- HHHHHHHHHC-----	45.67	-
264	Ubiquitination	KAKELATKLG----- HHHHHHHHHC-----	45.67	21906983

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
106	T	Phosphorylation	Kinase	AKT1	P31749	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of RL7A_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 RL7A_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RL7_HUMAN	RPL7	physical	22939629
RS3A_HUMAN	RPS3A	physical	22939629
RS3_HUMAN	RPS3	physical	22939629
RS9_HUMAN	RPS9	physical	22939629
RLA0_HUMAN	RPLP0	physical	22939629
RL8_HUMAN	RPL8	physical	22939629
RL9_HUMAN	RPL9	physical	22939629
RS13_HUMAN	RPS13	physical	22939629
RS15A_HUMAN	RPS15A	physical	22939629
RS16_HUMAN	RPS16	physical	22939629
RS19_HUMAN	RPS19	physical	22939629
RS20_HUMAN	RPS20	physical	22939629
RS23_HUMAN	RPS23	physical	22939629
RS25_HUMAN	RPS25	physical	22939629
RS26_HUMAN	RPS26	physical	22939629
RS28_HUMAN	RPS28	physical	22939629
RS2_HUMAN	RPS2	physical	22939629
RS4X_HUMAN	RPS4X	physical	22939629
RS5_HUMAN	RPS5	physical	22939629
RS8_HUMAN	RPS8	physical	22939629
RSSA_HUMAN	RPSA	physical	22939629
RS6_HUMAN	RPS6	physical	22939629
RS24_HUMAN	RPS24	physical	22939629
RS12_HUMAN	RPS12	physical	22939629
RS11_HUMAN	RPS11	physical	22939629
RS14_HUMAN	RPS14	physical	22939629
RLA1_HUMAN	RPLP1	physical	22939629
RS27A_HUMAN	RPS27A	physical	22939629
RS21_HUMAN	RPS21	physical	22939629
RS27L_HUMAN	RPS27L	physical	22939629
RM12_HUMAN	MRPL12	physical	22939629
SOCS3_HUMAN	SOCS3	physical	21988832
AIMP1_HUMAN	AIMP1	physical	22863883
SYDC_HUMAN	DARS	physical	22863883
MCA3_HUMAN	EEF1E1	physical	22863883
SYQ_HUMAN	QARS	physical	22863883
RL13_HUMAN	RPL13	physical	22863883
RL21_HUMAN	RPL21	physical	22863883
RL23A_HUMAN	RPL23A	physical	22863883
RL26_HUMAN	RPL26	physical	22863883
RL36_HUMAN	RPL36	physical	22863883
RLA0_HUMAN	RPLP0	physical	22863883
DDX18_HUMAN	DDX18	physical	26344197
EF1A1_HUMAN	EEF1A1	physical	26344197
PESC_HUMAN	PES1	physical	26344197
RL10_HUMAN	RPL10	physical	26344197
RL10A_HUMAN	RPL10A	physical	26344197
RL10L_HUMAN	RPL10L	physical	26344197
RL14_HUMAN	RPL14	physical	26344197
RL15_HUMAN	RPL15	physical	26344197
RL26_HUMAN	RPL26	physical	26344197
RL26L_HUMAN	RPL26L1	physical	26344197
RL27A_HUMAN	RPL27A	physical	26344197
RL3_HUMAN	RPL3	physical	26344197
RL30_HUMAN	RPL30	physical	26344197
RL31_HUMAN	RPL31	physical	26344197
RL35_HUMAN	RPL35	physical	26344197
RL35A_HUMAN	RPL35A	physical	26344197
RL37A_HUMAN	RPL37A	physical	26344197
RL3L_HUMAN	RPL3L	physical	26344197
RL8_HUMAN	RPL8	physical	26344197
RL9_HUMAN	RPL9	physical	26344197
RLA2_HUMAN	RPLP2	physical	26344197
RS15_HUMAN	RPS15	physical	26344197
RS18_HUMAN	RPS18	physical	26344197
RS3A_HUMAN	RPS3A	physical	26344197
RS4X_HUMAN	RPS4X	physical	26344197
RS6_HUMAN	RPS6	physical	26344197
RS7_HUMAN	RPS7	physical	26344197
RSSA_HUMAN	RPSA	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 RL7A_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-34; LYS-97 AND LYS-217, ANDMASS SPECTROMETRY.	19608861 [Abstract]