dbPTM

RL11_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RL11_HUMAN
UniProt AC	P62913
Protein Name	60S ribosomal protein L11
Gene Name	RPL11
Organism	Homo sapiens (Human).
Sequence Length	178
Subcellular Localization	Nucleus, nucleolus . Cytoplasm .
Protein Description	Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel. As part of the 5S RNP/5S ribonucleoprotein particle it is an essential component of the LSU, required for its formation and the maturation of rRNAs. [PubMed: 19061985]
Protein Sequence	MAQDQGEKENPMRELRIRKLCLNICVGESGDRLTRAAKVLEQLTGQTPVFSKARYTVRSFGIRRNEKIAVHCTVRGAKAEEILEKGLKVREYELRKNNFSDTGNFGFGIQEHIDLGIKYDPSIGIYGLDFYVVLGRPGFSIADKKRRTGCIGAKHRISKEEAMRWFQQKYDGIILPGK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAQDQGEKE ------CCCCCCCCC	22.96	12962325
7 (in isoform 2)	Ubiquitination	-	52.11	-
8	Acetylation	MAQDQGEKENPMREL CCCCCCCCCCHHHHH	70.39	23749302
8	Ubiquitination	MAQDQGEKENPMREL CCCCCCCCCCHHHHH	70.39	-
12	Sulfoxidation	QGEKENPMRELRIRK CCCCCCHHHHHHHHH	8.62	28183972
18 (in isoform 2)	Ubiquitination	-	21.33	21890473
19	Acetylation	MRELRIRKLCLNICV HHHHHHHHHHHHHHH	40.98	26051181
19	Ubiquitination	MRELRIRKLCLNICV HHHHHHHHHHHHHHH	40.98	21906983
19 (in isoform 1)	Ubiquitination	-	40.98	21890473
29	Phosphorylation	LNICVGESGDRLTRA HHHHHCCCCHHHHHH	39.81	29743597
34	Phosphorylation	GESGDRLTRAAKVLE CCCCHHHHHHHHHHH	21.11	28450419
37 (in isoform 2)	Ubiquitination	-	10.13	21890473
38	Sumoylation	DRLTRAAKVLEQLTG HHHHHHHHHHHHHHC	46.50	28112733
38 (in isoform 1)	Ubiquitination	-	46.50	21890473
38	2-Hydroxyisobutyrylation	DRLTRAAKVLEQLTG HHHHHHHHHHHHHHC	46.50	-
38	Ubiquitination	DRLTRAAKVLEQLTG HHHHHHHHHHHHHHC	46.50	21890473
38	Malonylation	DRLTRAAKVLEQLTG HHHHHHHHHHHHHHC	46.50	26320211
38	Acetylation	DRLTRAAKVLEQLTG HHHHHHHHHHHHHHC	46.50	26051181
38	Sumoylation	DRLTRAAKVLEQLTG HHHHHHHHHHHHHHC	46.50	-
44	Phosphorylation	AKVLEQLTGQTPVFS HHHHHHHHCCCCCCC	27.26	30266825
47	Phosphorylation	LEQLTGQTPVFSKAR HHHHHCCCCCCCCHH	23.82	30266825
51	Ubiquitination	TGQTPVFSKARYTVR HCCCCCCCCHHEEEH	26.16	19608861
51	Acetylation	TGQTPVFSKARYTVR HCCCCCCCCHHEEEH	26.16	19608861
51 (in isoform 2)	Ubiquitination	-	26.16	21890473
51	Phosphorylation	TGQTPVFSKARYTVR HCCCCCCCCHHEEEH	26.16	30266825
52	Malonylation	GQTPVFSKARYTVRS CCCCCCCCHHEEEHH	25.97	26320211
52	Sumoylation	GQTPVFSKARYTVRS CCCCCCCCHHEEEHH	25.97	28112733
52 (in isoform 1)	Ubiquitination	-	25.97	21890473
52	Acetylation	GQTPVFSKARYTVRS CCCCCCCCHHEEEHH	25.97	19608861
52	Ubiquitination	GQTPVFSKARYTVRS CCCCCCCCHHEEEHH	25.97	21890473
52	Sumoylation	GQTPVFSKARYTVRS CCCCCCCCHHEEEHH	25.97	-
67	Acetylation	FGIRRNEKIAVHCTV CCCCCCCEEEEEEEE	39.24	23749302
67	2-Hydroxyisobutyrylation	FGIRRNEKIAVHCTV CCCCCCCEEEEEEEE	39.24	-
67	Ubiquitination	FGIRRNEKIAVHCTV CCCCCCCEEEEEEEE	39.24	-
72	S-nitrosylation	NEKIAVHCTVRGAKA CCEEEEEEEECCHHH	2.78	19483679
72	S-nitrosocysteine	NEKIAVHCTVRGAKA CCEEEEEEEECCHHH	2.78	-
73	Phosphorylation	EKIAVHCTVRGAKAE CEEEEEEEECCHHHH	9.81	20068231
75	Methylation	IAVHCTVRGAKAEEI EEEEEEECCHHHHHH	22.62	115491639
77 (in isoform 2)	Ubiquitination	-	9.42	21890473
78	Sumoylation	HCTVRGAKAEEILEK EEEECCHHHHHHHHH	60.19	-
78	Sumoylation	HCTVRGAKAEEILEK EEEECCHHHHHHHHH	60.19	-
78	Ubiquitination	HCTVRGAKAEEILEK EEEECCHHHHHHHHH	60.19	21906983
78	2-Hydroxyisobutyrylation	HCTVRGAKAEEILEK EEEECCHHHHHHHHH	60.19	-
78	Acetylation	HCTVRGAKAEEILEK EEEECCHHHHHHHHH	60.19	26051181
78 (in isoform 1)	Ubiquitination	-	60.19	21890473
84	Acetylation	AKAEEILEKGLKVRE HHHHHHHHHCCEEEE	51.22	19608861
84 (in isoform 2)	Ubiquitination	-	51.22	21890473
84	Ubiquitination	AKAEEILEKGLKVRE HHHHHHHHHCCEEEE	51.22	19608861
85	Acetylation	KAEEILEKGLKVREY HHHHHHHHCCEEEEE	67.13	19608861
85 (in isoform 1)	Ubiquitination	-	67.13	21890473
85	Sumoylation	KAEEILEKGLKVREY HHHHHHHHCCEEEEE	67.13	19608861
85	Ubiquitination	KAEEILEKGLKVREY HHHHHHHHCCEEEEE	67.13	21890473
85	Malonylation	KAEEILEKGLKVREY HHHHHHHHCCEEEEE	67.13	26320211
85	2-Hydroxyisobutyrylation	KAEEILEKGLKVREY HHHHHHHHCCEEEEE	67.13	-
88	Ubiquitination	EILEKGLKVREYELR HHHHHCCEEEEEEHH	48.17	-
88	Sumoylation	EILEKGLKVREYELR HHHHHCCEEEEEEHH	48.17	-
92	Phosphorylation	KGLKVREYELRKNNF HCCEEEEEEHHHCCC	15.08	28152594
95	Methylation	KVREYELRKNNFSDT EEEEEEHHHCCCCCC	27.93	115491631
96	Ubiquitination	VREYELRKNNFSDTG EEEEEHHHCCCCCCC	69.72	-
119	Phosphorylation	HIDLGIKYDPSIGIY HHEECCEECCCCCEE	31.03	-
140	Phosphorylation	VLGRPGFSIADKKRR EECCCCCCHHCHHHC	23.84	24117733
143 (in isoform 2)	Ubiquitination	-	56.17	21890473
144 (in isoform 2)	Ubiquitination	-	38.87	21890473
144	2-Hydroxyisobutyrylation	PGFSIADKKRRTGCI CCCCHHCHHHCCCCC	38.87	-
144	Acetylation	PGFSIADKKRRTGCI CCCCHHCHHHCCCCC	38.87	25953088
144 (in isoform 1)	Ubiquitination	-	38.87	21890473
144	Ubiquitination	PGFSIADKKRRTGCI CCCCHHCHHHCCCCC	38.87	21890473
145	Ubiquitination	GFSIADKKRRTGCIG CCCHHCHHHCCCCCC	47.89	21890473
145 (in isoform 1)	Ubiquitination	-	47.89	21890473
150	S-nitrosocysteine	DKKRRTGCIGAKHRI CHHHCCCCCCCCCCC	2.28	-
150	S-nitrosylation	DKKRRTGCIGAKHRI CHHHCCCCCCCCCCC	2.28	19483679
150	S-palmitoylation	DKKRRTGCIGAKHRI CHHHCCCCCCCCCCC	2.28	21044946
153 (in isoform 2)	Ubiquitination	-	5.65	21890473
154	Acetylation	RTGCIGAKHRISKEE CCCCCCCCCCCCHHH	28.36	21466224
154	Ubiquitination	RTGCIGAKHRISKEE CCCCCCCCCCCCHHH	28.36	21906983
154	Sumoylation	RTGCIGAKHRISKEE CCCCCCCCCCCCHHH	28.36	28112733
154 (in isoform 1)	Ubiquitination	-	28.36	21890473
158 (in isoform 2)	Ubiquitination	-	33.69	21890473
158	Acetylation	IGAKHRISKEEAMRW CCCCCCCCHHHHHHH	33.69	19608861
158	Ubiquitination	IGAKHRISKEEAMRW CCCCCCCCHHHHHHH	33.69	19608861
159	Sumoylation	GAKHRISKEEAMRWF CCCCCCCHHHHHHHH	58.14	19608861
159	Ubiquitination	GAKHRISKEEAMRWF CCCCCCCHHHHHHHH	58.14	19608861
159	Sumoylation	GAKHRISKEEAMRWF CCCCCCCHHHHHHHH	58.14	-
159	2-Hydroxyisobutyrylation	GAKHRISKEEAMRWF CCCCCCCHHHHHHHH	58.14	-
159	Acetylation	GAKHRISKEEAMRWF CCCCCCCHHHHHHHH	58.14	23749302
159 (in isoform 1)	Ubiquitination	-	58.14	21890473
159	Succinylation	GAKHRISKEEAMRWF CCCCCCCHHHHHHHH	58.14	23954790
164	Methylation	ISKEEAMRWFQQKYD CCHHHHHHHHHHHCC	37.80	115491623
168 (in isoform 2)	Ubiquitination	-	36.48	21890473
169 (in isoform 1)	Ubiquitination	-	34.23	21890473
169	Acetylation	AMRWFQQKYDGIILP HHHHHHHHCCCEEEC	34.23	25825284
169	2-Hydroxyisobutyrylation	AMRWFQQKYDGIILP HHHHHHHHCCCEEEC	34.23	-
169	Sumoylation	AMRWFQQKYDGIILP HHHHHHHHCCCEEEC	34.23	-
169	Sumoylation	AMRWFQQKYDGIILP HHHHHHHHCCCEEEC	34.23	-
169	Ubiquitination	AMRWFQQKYDGIILP HHHHHHHHCCCEEEC	34.23	21890473
170	Phosphorylation	MRWFQQKYDGIILPG HHHHHHHCCCEEECC	18.31	28152594
178	Sumoylation	DGIILPGK------- CCEEECCC-------	56.05	-
178	Ubiquitination	DGIILPGK------- CCEEECCC-------	56.05	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
47	T	Phosphorylation	Kinase	CDK2	P24941	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of RL11_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 RL11_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PML_HUMAN	PML	physical	15195100
CDN2A_HUMAN	CDKN2A	physical	14612427
ARF_HUMAN	CDKN2A	physical	14612427
P53_HUMAN	TP53	physical	14612427
MDM2_HUMAN	MDM2	physical	14612427
MDM2_HUMAN	MDM2	physical	16803902
MDM2_HUMAN	MDM2	physical	15308643
RL5_HUMAN	RPL5	physical	15308643
RL23_HUMAN	RPL23	physical	15308643
P53_HUMAN	TP53	physical	15308643
MYC_HUMAN	MYC	physical	17599065
MDM2_HUMAN	MDM2	physical	21804542
MDM2_HUMAN	MDM2	physical	20554519
RL5_HUMAN	RPL5	physical	18560357
MDM2_HUMAN	MDM2	physical	18560357
MDM2_HUMAN	MDM2	physical	21903592
MDM2_HUMAN	MDM2	physical	12842086
RL23_HUMAN	RPL23	physical	22939629
RL5_HUMAN	RPL5	physical	22939629
RL12_HUMAN	RPL12	physical	22939629
RL13_HUMAN	RPL13	physical	22939629
RL14_HUMAN	RPL14	physical	22939629
RL15_HUMAN	RPL15	physical	22939629
RL18A_HUMAN	RPL18A	physical	22939629
RL18_HUMAN	RPL18	physical	22939629
RL19_HUMAN	RPL19	physical	22939629
RL21_HUMAN	RPL21	physical	22939629
RL23A_HUMAN	RPL23A	physical	22939629
RL24_HUMAN	RPL24	physical	22939629
RL27A_HUMAN	RPL27A	physical	22939629
RL31_HUMAN	RPL31	physical	22939629
RL37A_HUMAN	RPL37A	physical	22939629
RL6_HUMAN	RPL6	physical	22939629
RL7A_HUMAN	RPL7A	physical	22939629
RL7_HUMAN	RPL7	physical	22939629
RL9_HUMAN	RPL9	physical	22939629
RS11_HUMAN	RPS11	physical	22939629
RS12_HUMAN	RPS12	physical	22939629
RS13_HUMAN	RPS13	physical	22939629
RS14_HUMAN	RPS14	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
RS3_HUMAN	RPS3	physical	22939629
RS4X_HUMAN	RPS4X	physical	22939629
RS6_HUMAN	RPS6	physical	22939629
RS8_HUMAN	RPS8	physical	22939629
RSSA_HUMAN	RPSA	physical	22939629
RL30_HUMAN	RPL30	physical	22939629
RS3A_HUMAN	RPS3A	physical	22939629
RS5_HUMAN	RPS5	physical	22939629
RS19_HUMAN	RPS19	physical	22939629
RL4_HUMAN	RPL4	physical	22939629
RS7_HUMAN	RPS7	physical	22939629
RL22_HUMAN	RPL22	physical	22939629
RS26_HUMAN	RPS26	physical	22939629
RLA1_HUMAN	RPLP1	physical	22939629
RL36_HUMAN	RPL36	physical	22939629
RL8_HUMAN	RPL8	physical	22939629
RLA0_HUMAN	RPLP0	physical	22939629
RL3_HUMAN	RPL3	physical	22939629
RS9_HUMAN	RPS9	physical	22939629
RL35_HUMAN	RPL35	physical	22939629
RS10_HUMAN	RPS10	physical	22939629
RL38_HUMAN	RPL38	physical	22939629
RL17_HUMAN	RPL17	physical	22939629
RS21_HUMAN	RPS21	physical	22939629
RS27A_HUMAN	RPS27A	physical	22939629
RS27L_HUMAN	RPS27L	physical	22939629
RM12_HUMAN	MRPL12	physical	22939629
RRS1_HUMAN	RRS1	physical	22939629
MDM2_HUMAN	MDM2	physical	23169665
RL5_HUMAN	RPL5	physical	23169665
P53_HUMAN	TP53	physical	23169665
STAT3_HUMAN	STAT3	physical	21988832
PML_HUMAN	PML	physical	23169665
K1C40_HUMAN	KRT40	physical	25416956
KR107_HUMAN	KRTAP10-7	physical	25416956
MDM2_HUMAN	MDM2	physical	23507139
BRX1_HUMAN	BRIX1	physical	26344197
UBIM_HUMAN	FAU	physical	26344197
RM24_HUMAN	MRPL24	physical	26344197
RT10_HUMAN	MRPS10	physical	26344197
RT07_HUMAN	MRPS7	physical	26344197
NOP2_HUMAN	NOP2	physical	26344197
PK1IP_HUMAN	PAK1IP1	physical	26344197
RL10A_HUMAN	RPL10A	physical	26344197
RL12_HUMAN	RPL12	physical	26344197
RL13_HUMAN	RPL13	physical	26344197
RL17_HUMAN	RPL17	physical	26344197
RL18_HUMAN	RPL18	physical	26344197
RL23A_HUMAN	RPL23A	physical	26344197
RL27A_HUMAN	RPL27A	physical	26344197
RL3_HUMAN	RPL3	physical	26344197
RL30_HUMAN	RPL30	physical	26344197
RL31_HUMAN	RPL31	physical	26344197
RL32_HUMAN	RPL32	physical	26344197
RL35A_HUMAN	RPL35A	physical	26344197
RL37A_HUMAN	RPL37A	physical	26344197
RL38_HUMAN	RPL38	physical	26344197
RL3L_HUMAN	RPL3L	physical	26344197
RL6_HUMAN	RPL6	physical	26344197
RL7_HUMAN	RPL7	physical	26344197
RL7A_HUMAN	RPL7A	physical	26344197
RL9_HUMAN	RPL9	physical	26344197
RLA1_HUMAN	RPLP1	physical	26344197
RS14_HUMAN	RPS14	physical	26344197
RS16_HUMAN	RPS16	physical	26344197
RS18_HUMAN	RPS18	physical	26344197
RS19_HUMAN	RPS19	physical	26344197
RS23_HUMAN	RPS23	physical	26344197
RS25_HUMAN	RPS25	physical	26344197
RS26_HUMAN	RPS26	physical	26344197
RS27_HUMAN	RPS27	physical	26344197
RS3_HUMAN	RPS3	physical	26344197
RS3A_HUMAN	RPS3A	physical	26344197
RS4X_HUMAN	RPS4X	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
P73_HUMAN	TP73	physical	25301064
GRWD1_HUMAN	GRWD1	physical	27856536
MDM2_HUMAN	MDM2	physical	27856536

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
612562	Diamond-Blackfan anemia 7 (DBA7)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of RL11_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 ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT THR-47, 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 ACETYLATION AT ALA-2.	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-52; LYS-85 AND LYS-159, ANDMASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
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 ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT THR-47, AND MASS SPECTROMETRY.	19413330 [Abstract]
"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 THR-44 AND THR-47, AND MASSSPECTROMETRY.	18691976 [Abstract]