dbPTM

RL7_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RL7_HUMAN
UniProt AC	P18124
Protein Name	60S ribosomal protein L7
Gene Name	RPL7
Organism	Homo sapiens (Human).
Sequence Length	248
Subcellular Localization
Protein Description	Component of the large ribosomal subunit. [PubMed: 12962325 Binds to G-rich structures in 28S rRNA and in mRNAs. Plays a regulatory role in the translation apparatus; inhibits cell-free translation of mRNAs.]
Protein Sequence	MEGVEEKKKEVPAVPETLKKKRRNFAELKIKRLRKKFAQKMLRKARRKLIYEKAKHYHKEYRQMYRTEIRMARMARKAGNFYVPAEPKLAFVIRIRGINGVSPKVRKVLQLLRLRQIFNGTFVKLNKASINMLRIVEPYIAWGYPNLKSVNELIYKRGYGKINKKRIALTDNALIARSLGKYGIICMEDLIHEIYTVGKRFKEANNFLWPFKLSSPRGGMKKKTTHFVEGGDAGNREDQINRLIRRMN

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MEGVEEKK -------CCCHHHHH	10.24	12962325
7	Ubiquitination	-MEGVEEKKKEVPAV -CCCHHHHHHCCCCC	56.49	33845483
8	Ubiquitination	MEGVEEKKKEVPAVP CCCHHHHHHCCCCCC	58.40	27667366
9	Ubiquitination	EGVEEKKKEVPAVPE CCHHHHHHCCCCCCH	75.02	32015554
13	Ubiquitination	EKKKEVPAVPETLKK HHHHCCCCCCHHHHH	34.37	27667366
15	Ubiquitination	KKEVPAVPETLKKKR HHCCCCCCHHHHHHH	30.84	22817900
17	Phosphorylation	EVPAVPETLKKKRRN CCCCCCHHHHHHHCC	37.50	30266825
19	Acetylation	PAVPETLKKKRRNFA CCCCHHHHHHHCCHH	64.76	23236377
19	Ubiquitination	PAVPETLKKKRRNFA CCCCHHHHHHHCCHH	64.76	27667366
19	Succinylation	PAVPETLKKKRRNFA CCCCHHHHHHHCCHH	64.76	23954790
20	Ubiquitination	AVPETLKKKRRNFAE CCCHHHHHHHCCHHH	55.41	33845483
21	Ubiquitination	VPETLKKKRRNFAEL CCHHHHHHHCCHHHH	55.81	23503661
29	Acetylation	RRNFAELKIKRLRKK HCCHHHHHHHHHHHH	37.37	23236377
29	Ubiquitination	RRNFAELKIKRLRKK HCCHHHHHHHHHHHH	37.37	23000965
31	Acetylation	NFAELKIKRLRKKFA CHHHHHHHHHHHHHH	43.74	-
31	Ubiquitination	NFAELKIKRLRKKFA CHHHHHHHHHHHHHH	43.74	23000965
35	Ubiquitination	LKIKRLRKKFAQKML HHHHHHHHHHHHHHH	57.76	23000965
36	Ubiquitination	KIKRLRKKFAQKMLR HHHHHHHHHHHHHHH	39.23	23000965
37	Ubiquitination	IKRLRKKFAQKMLRK HHHHHHHHHHHHHHH	11.05	23000965
40	Ubiquitination	LRKKFAQKMLRKARR HHHHHHHHHHHHHHH	36.15	23000965
40	Acetylation	LRKKFAQKMLRKARR HHHHHHHHHHHHHHH	36.15	25825284
44	Ubiquitination	FAQKMLRKARRKLIY HHHHHHHHHHHHHHH	42.14	23000965
48	Ubiquitination	MLRKARRKLIYEKAK HHHHHHHHHHHHHHH	33.41	23000965
48	Acetylation	MLRKARRKLIYEKAK HHHHHHHHHHHHHHH	33.41	26051181
51	Phosphorylation	KARRKLIYEKAKHYH HHHHHHHHHHHHHHH	23.09	28152594
53	Ubiquitination	RRKLIYEKAKHYHKE HHHHHHHHHHHHHHH	45.85	21906983
53	Acetylation	RRKLIYEKAKHYHKE HHHHHHHHHHHHHHH	45.85	26051181
55	Ubiquitination	KLIYEKAKHYHKEYR HHHHHHHHHHHHHHH	56.62	33845483
59	Acetylation	EKAKHYHKEYRQMYR HHHHHHHHHHHHHHH	49.64	26051181
59	Ubiquitination	EKAKHYHKEYRQMYR HHHHHHHHHHHHHHH	49.64	23503661
64	Ubiquitination	YHKEYRQMYRTEIRM HHHHHHHHHHHHHHH	1.48	23000965
67	Ubiquitination	EYRQMYRTEIRMARM HHHHHHHHHHHHHHH	20.48	23000965
77	Ubiquitination	RMARMARKAGNFYVP HHHHHHHHCCCEEEC	51.62	23000965
82	Phosphorylation	ARKAGNFYVPAEPKL HHHCCCEEECCCCCE	14.99	28152594
84	Ubiquitination	KAGNFYVPAEPKLAF HCCCEEECCCCCEEE	21.37	23000965
87	Ubiquitination	NFYVPAEPKLAFVIR CEEECCCCCEEEEEE	38.78	23000965
88	Ubiquitination	FYVPAEPKLAFVIRI EEECCCCCEEEEEEE	43.91	23000965
88	Acetylation	FYVPAEPKLAFVIRI EEECCCCCEEEEEEE	43.91	26051181
96	Methylation	LAFVIRIRGINGVSP EEEEEEECCCCCCCH	30.04	115492247
102	Phosphorylation	IRGINGVSPKVRKVL ECCCCCCCHHHHHHH	22.02	28985074
104	Ubiquitination	GINGVSPKVRKVLQL CCCCCCHHHHHHHHH	47.36	23000965
107	Ubiquitination	GVSPKVRKVLQLLRL CCCHHHHHHHHHHHH	50.73	23000965
108	Ubiquitination	VSPKVRKVLQLLRLR CCHHHHHHHHHHHHH	2.63	21963094
116	Ubiquitination	LQLLRLRQIFNGTFV HHHHHHHHHHCCCEE	49.57	23000965
121	Ubiquitination	LRQIFNGTFVKLNKA HHHHHCCCEEECCHH	26.76	23000965
124	Acetylation	IFNGTFVKLNKASIN HHCCCEEECCHHHCC	42.00	19608861
124	Ubiquitination	IFNGTFVKLNKASIN HHCCCEEECCHHHCC	42.00	23000965
124	Methylation	IFNGTFVKLNKASIN HHCCCEEECCHHHCC	42.00	22647069
127	Succinylation	GTFVKLNKASINMLR CCEEECCHHHCCCHH	54.68	21890473
127	Acetylation	GTFVKLNKASINMLR CCEEECCHHHCCCHH	54.68	25953088
127	Succinylation	GTFVKLNKASINMLR CCEEECCHHHCCCHH	54.68	-
127	Ubiquitination	GTFVKLNKASINMLR CCEEECCHHHCCCHH	54.68	23000965
129	Phosphorylation	FVKLNKASINMLRIV EEECCHHHCCCHHHC	18.99	27251275
132	Sulfoxidation	LNKASINMLRIVEPY CCHHHCCCHHHCCCH	2.25	21406390
134	Methylation	KASINMLRIVEPYIA HHHCCCHHHCCCHHH	21.82	115492239
139	Phosphorylation	MLRIVEPYIAWGYPN CHHHCCCHHHCCCCC	6.97	28152594
141	Ubiquitination	RIVEPYIAWGYPNLK HHCCCHHHCCCCCHH	6.44	21963094
144	Phosphorylation	EPYIAWGYPNLKSVN CCHHHCCCCCHHHHH	4.35	28152594
148	Ubiquitination	AWGYPNLKSVNELIY HCCCCCHHHHHHHHH	60.02	21906983
148	Methylation	AWGYPNLKSVNELIY HCCCCCHHHHHHHHH	60.02	30793667
149	Phosphorylation	WGYPNLKSVNELIYK CCCCCHHHHHHHHHH	33.08	21712546
155	Phosphorylation	KSVNELIYKRGYGKI HHHHHHHHHCCCCCC	13.78	28152594
156	Ubiquitination	SVNELIYKRGYGKIN HHHHHHHHCCCCCCC	32.14	23000965
156	Acetylation	SVNELIYKRGYGKIN HHHHHHHHCCCCCCC	32.14	26051181
156	Methylation	SVNELIYKRGYGKIN HHHHHHHHCCCCCCC	32.14	66702645
159	Ubiquitination	ELIYKRGYGKINKKR HHHHHCCCCCCCHHH	21.19	21963094
159	Phosphorylation	ELIYKRGYGKINKKR HHHHHCCCCCCCHHH	21.19	20068231
161	Ubiquitination	IYKRGYGKINKKRIA HHHCCCCCCCHHHEE	34.32	23000965
161	Acetylation	IYKRGYGKINKKRIA HHHCCCCCCCHHHEE	34.32	19608861
162	Ubiquitination	YKRGYGKINKKRIAL HHCCCCCCCHHHEEE	8.74	21963094
164	Ubiquitination	RGYGKINKKRIALTD CCCCCCCHHHEEECC	47.07	24816145
170	Phosphorylation	NKKRIALTDNALIAR CHHHEEECCCHHHHH	20.41	21712546
172	Ubiquitination	KRIALTDNALIARSL HHEEECCCHHHHHHH	31.26	21890473
181	Ubiquitination	LIARSLGKYGIICME HHHHHHHHCEEEEHH	45.67	21963094
182	Phosphorylation	IARSLGKYGIICMED HHHHHHHCEEEEHHH	16.26	26126808
182	Ubiquitination	IARSLGKYGIICMED HHHHHHHCEEEEHHH	16.26	22505724
183	Ubiquitination	ARSLGKYGIICMEDL HHHHHHCEEEEHHHH	13.28	21963094
195	Phosphorylation	EDLIHEIYTVGKRFK HHHHHHHHHHHHHHH	7.74	19060867
196	Phosphorylation	DLIHEIYTVGKRFKE HHHHHHHHHHHHHHH	28.57	26126808
199	Acetylation	HEIYTVGKRFKEANN HHHHHHHHHHHHHHC	50.77	26051181
199	Ubiquitination	HEIYTVGKRFKEANN HHHHHHHHHHHHHHC	50.77	21906983
202	Acetylation	YTVGKRFKEANNFLW HHHHHHHHHHHCCCC	61.01	26051181
202	Methylation	YTVGKRFKEANNFLW HHHHHHHHHHHCCCC	61.01	42367625
202	Ubiquitination	YTVGKRFKEANNFLW HHHHHHHHHHHCCCC	61.01	21963094
212	Ubiquitination	NNFLWPFKLSSPRGG HCCCCCEECCCCCCC	43.30	21963094
212	Acetylation	NNFLWPFKLSSPRGG HCCCCCEECCCCCCC	43.30	26051181
214	Phosphorylation	FLWPFKLSSPRGGMK CCCCEECCCCCCCCC	38.60	28450419
215	Phosphorylation	LWPFKLSSPRGGMKK CCCEECCCCCCCCCC	29.11	28450419
217	Methylation	PFKLSSPRGGMKKKT CEECCCCCCCCCCCE	57.13	115492255
221	Ubiquitination	SSPRGGMKKKTTHFV CCCCCCCCCCEEEEE	55.16	24816145
222	Ubiquitination	SPRGGMKKKTTHFVE CCCCCCCCCEEEEEC	46.60	22505724
223	Ubiquitination	PRGGMKKKTTHFVEG CCCCCCCCEEEEECC	53.81	21906983
224	Phosphorylation	RGGMKKKTTHFVEGG CCCCCCCEEEEECCC	34.09	23312004
225	Phosphorylation	GGMKKKTTHFVEGGD CCCCCCEEEEECCCC	23.38	23312004

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 RL7_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of RL7_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 RL7_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ZNF7_HUMAN	ZNF7	physical	9268371
RS3A_HUMAN	RPS3A	physical	22939629
RS4X_HUMAN	RPS4X	physical	22939629
RS6_HUMAN	RPS6	physical	22939629
RSSA_HUMAN	RPSA	physical	22939629
RS3_HUMAN	RPS3	physical	22939629
RLA0_HUMAN	RPLP0	physical	22939629
RL9_HUMAN	RPL9	physical	22939629
RS13_HUMAN	RPS13	physical	22939629
RS14_HUMAN	RPS14	physical	22939629
RS15A_HUMAN	RPS15A	physical	22939629
RS15_HUMAN	RPS15	physical	22939629
RS16_HUMAN	RPS16	physical	22939629
RS19_HUMAN	RPS19	physical	22939629
RS23_HUMAN	RPS23	physical	22939629
RS26_HUMAN	RPS26	physical	22939629
RS2_HUMAN	RPS2	physical	22939629
RS7_HUMAN	RPS7	physical	22939629
RS8_HUMAN	RPS8	physical	22939629
RS24_HUMAN	RPS24	physical	22939629
RL8_HUMAN	RPL8	physical	22939629
RS11_HUMAN	RPS11	physical	22939629
RS5_HUMAN	RPS5	physical	22939629
RS20_HUMAN	RPS20	physical	22939629
RS12_HUMAN	RPS12	physical	22939629
RS28_HUMAN	RPS28	physical	22939629
RS25_HUMAN	RPS25	physical	22939629
RS21_HUMAN	RPS21	physical	22939629
RS29_HUMAN	RPS29	physical	22939629
RS27L_HUMAN	RPS27L	physical	22939629
RRS1_HUMAN	RRS1	physical	22939629
TMX1_HUMAN	TMX1	physical	22939629
IPO5_HUMAN	IPO5	physical	20828572
RAN_HUMAN	RAN	physical	20828572
IL7RA_HUMAN	IL7R	physical	23151878
ABCE1_HUMAN	ABCE1	physical	26344197
BRX1_HUMAN	BRIX1	physical	26344197
CAPR1_HUMAN	CAPRIN1	physical	26344197
DDX24_HUMAN	DDX24	physical	26344197
EF1A1_HUMAN	EEF1A1	physical	26344197
EIF3C_HUMAN	EIF3C	physical	26344197
RACK1_HUMAN	GNB2L1	physical	26344197
GNL1_HUMAN	GNL1	physical	26344197
GNL3_HUMAN	GNL3	physical	26344197
PABP1_HUMAN	PABPC1	physical	26344197
PABP4_HUMAN	PABPC4	physical	26344197
RNPS1_HUMAN	RNPS1	physical	26344197
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
RL23_HUMAN	RPL23	physical	26344197
RL23A_HUMAN	RPL23A	physical	26344197
RL27A_HUMAN	RPL27A	physical	26344197
RL28_HUMAN	RPL28	physical	26344197
RL3_HUMAN	RPL3	physical	26344197
RL30_HUMAN	RPL30	physical	26344197
RL35_HUMAN	RPL35	physical	26344197
RL35A_HUMAN	RPL35A	physical	26344197
RL37A_HUMAN	RPL37A	physical	26344197
RL3L_HUMAN	RPL3L	physical	26344197
RL5_HUMAN	RPL5	physical	26344197
RL7A_HUMAN	RPL7A	physical	26344197
RL8_HUMAN	RPL8	physical	26344197
RL9_HUMAN	RPL9	physical	26344197
RLA1_HUMAN	RPLP1	physical	26344197
RS16_HUMAN	RPS16	physical	26344197
RS18_HUMAN	RPS18	physical	26344197
RS20_HUMAN	RPS20	physical	26344197
RS25_HUMAN	RPS25	physical	26344197
RS27_HUMAN	RPS27	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
RSSA_HUMAN	RPSA	physical	26344197
TBB4B_HUMAN	TUBB4B	physical	26344197
WDR12_HUMAN	WDR12	physical	26344197
CBX2_HUMAN	CBX2	physical	28514442
SRS12_HUMAN	SRSF12	physical	28514442
BMI1_HUMAN	BMI1	physical	28514442
RL26L_HUMAN	RPL26L1	physical	28514442
PHC2_HUMAN	PHC2	physical	28514442
ZN689_HUMAN	ZNF689	physical	28514442
TSYL2_HUMAN	TSPYL2	physical	28514442
RL36L_HUMAN	RPL36AL	physical	28514442
NOC4L_HUMAN	NOC4L	physical	28514442
DCAF1_HUMAN	VPRBP	physical	28514442
GZF1_HUMAN	GZF1	physical	28514442
RRP12_HUMAN	RRP12	physical	28514442
ZBT11_HUMAN	ZBTB11	physical	28514442
NGRN_HUMAN	NGRN	physical	28514442
RBM19_HUMAN	RBM19	physical	28514442
ZBT24_HUMAN	ZBTB24	physical	28514442
KRR1_HUMAN	KRR1	physical	28514442
ZN771_HUMAN	ZNF771	physical	28514442
UTP23_HUMAN	UTP23	physical	28514442
ZCCHV_HUMAN	ZC3HAV1	physical	28514442
ZN668_HUMAN	ZNF668	physical	28514442
ZN184_HUMAN	ZNF184	physical	28514442
RM13_HUMAN	MRPL13	physical	28514442
RM27_HUMAN	MRPL27	physical	28514442
POP1_HUMAN	POP1	physical	28514442
RL26_HUMAN	RPL26	physical	28514442
RALY_HUMAN	RALY	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 RL7_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]
"Characterization and analysis of posttranslational modifications ofthe human large cytoplasmic ribosomal subunit proteins by massspectrometry and Edman sequencing."; Odintsova T.I., Muller E.C., Ivanov A.V., Egorov T.A., Bienert R.,Vladimirov S.N., Kostka S., Otto A., Wittmann-Liebold B.,Karpova G.G.; J. Protein Chem. 22:249-258(2003). Cited for: MASS SPECTROMETRY, AND PROBABLE ACETYLATION AT MET-1.	12962325 [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-29; LYS-31; LYS-124 ANDLYS-161, AND MASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"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-139 AND TYR-195, ANDMASS SPECTROMETRY.	15592455 [Abstract]