dbPTM

RL5_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RL5_HUMAN
UniProt AC	P46777
Protein Name	60S ribosomal protein L5
Gene Name	RPL5
Organism	Homo sapiens (Human).
Sequence Length	297
Subcellular Localization	Cytoplasm . Nucleus, nucleolus .
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: 12962325]
Protein Sequence	MGFVKVVKNKAYFKRYQVKFRRRREGKTDYYARKRLVIQDKNKYNTPKYRMIVRVTNRDIICQIAYARIEGDMIVCAAYAHELPKYGVKVGLTNYAAAYCTGLLLARRLLNRFGMDKIYEGQVEVTGDEYNVESIDGQPGAFTCYLDAGLARTTTGNKVFGALKGAVDGGLSIPHSTKRFPGYDSESKEFNAEVHRKHIMGQNVADYMRYLMEEDEDAYKKQFSQYIKNSVTPDMMEEMYKKAHAAIRENPVYEKKPKKEVKKKRWNRPKMSLAQKKDRVAQKKASFLRAQERAAES

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MGFVKVVKN ------CCCEEEECC	35.73	22814378
5	Methylation	---MGFVKVVKNKAY ---CCCEEEECCHHH	38.76	22635667
5	Acetylation	---MGFVKVVKNKAY ---CCCEEEECCHHH	38.76	19608861
5	Ubiquitination	---MGFVKVVKNKAY ---CCCEEEECCHHH	38.76	19608861
5	2-Hydroxyisobutyrylation	---MGFVKVVKNKAY ---CCCEEEECCHHH	38.76	-
5	Malonylation	---MGFVKVVKNKAY ---CCCEEEECCHHH	38.76	26320211
10	Ubiquitination	FVKVVKNKAYFKRYQ CEEEECCHHHHEEEE	38.45	-
10	Acetylation	FVKVVKNKAYFKRYQ CEEEECCHHHHEEEE	38.45	26051181
14	Ubiquitination	VKNKAYFKRYQVKFR ECCHHHHEEEEEEEH	37.20	-
19	Ubiquitination	YFKRYQVKFRRRREG HHEEEEEEEHHHCCC	20.02	21906983
19	Acetylation	YFKRYQVKFRRRREG HHEEEEEEEHHHCCC	20.02	26051181
27	Acetylation	FRRRREGKTDYYARK EHHHCCCCCCHHHEE	33.21	23749302
27	Ubiquitination	FRRRREGKTDYYARK EHHHCCCCCCHHHEE	33.21	21906983
30	Phosphorylation	RREGKTDYYARKRLV HCCCCCCHHHEEEEE	12.31	29449344
31	Phosphorylation	REGKTDYYARKRLVI CCCCCCHHHEEEEEE	11.62	29449344
41	Acetylation	KRLVIQDKNKYNTPK EEEEEECCCCCCCCC	38.68	21466224
41	Ubiquitination	KRLVIQDKNKYNTPK EEEEEECCCCCCCCC	38.68	-
41	2-Hydroxyisobutyrylation	KRLVIQDKNKYNTPK EEEEEECCCCCCCCC	38.68	-
43	Acetylation	LVIQDKNKYNTPKYR EEEECCCCCCCCCEE	45.69	21466224
43	Ubiquitination	LVIQDKNKYNTPKYR EEEECCCCCCCCCEE	45.69	-
44	Phosphorylation	VIQDKNKYNTPKYRM EEECCCCCCCCCEEE	33.39	27174698
46	Phosphorylation	QDKNKYNTPKYRMIV ECCCCCCCCCEEEEE	20.33	27174698
48	Acetylation	KNKYNTPKYRMIVRV CCCCCCCCEEEEEEE	43.37	19608861
48	Ubiquitination	KNKYNTPKYRMIVRV CCCCCCCCEEEEEEE	43.37	19608861
48	2-Hydroxyisobutyrylation	KNKYNTPKYRMIVRV CCCCCCCCEEEEEEE	43.37	-
49	Phosphorylation	NKYNTPKYRMIVRVT CCCCCCCEEEEEEEC	13.45	22817900
62	Glutathionylation	VTNRDIICQIAYARI ECCHHHEEEEEEEEE	2.15	22555962
62	S-palmitoylation	VTNRDIICQIAYARI ECCHHHEEEEEEEEE	2.15	29575903
66	Phosphorylation	DIICQIAYARIEGDM HHEEEEEEEEECCCE	9.68	28152594
73	Sulfoxidation	YARIEGDMIVCAAYA EEEECCCEEEEEHHH	3.48	21406390
76	S-nitrosocysteine	IEGDMIVCAAYAHEL ECCCEEEEEHHHHCC	0.93	-
76	Glutathionylation	IEGDMIVCAAYAHEL ECCCEEEEEHHHHCC	0.93	22555962
76	S-nitrosylation	IEGDMIVCAAYAHEL ECCCEEEEEHHHHCC	0.93	22178444
85	Ubiquitination	AYAHELPKYGVKVGL HHHHCCCCCCCCCCC	68.23	-
85	2-Hydroxyisobutyrylation	AYAHELPKYGVKVGL HHHHCCCCCCCCCCC	68.23	-
85	Acetylation	AYAHELPKYGVKVGL HHHHCCCCCCCCCCC	68.23	26051181
89	Ubiquitination	ELPKYGVKVGLTNYA CCCCCCCCCCCCHHH	26.65	-
99	Phosphorylation	LTNYAAAYCTGLLLA CCHHHHHHHHHHHHH	5.94	28152594
100	S-nitrosocysteine	TNYAAAYCTGLLLAR CHHHHHHHHHHHHHH	1.77	-
100	Glutathionylation	TNYAAAYCTGLLLAR CHHHHHHHHHHHHHH	1.77	22555962
100	S-nitrosylation	TNYAAAYCTGLLLAR CHHHHHHHHHHHHHH	1.77	22178444
100	S-palmitoylation	TNYAAAYCTGLLLAR CHHHHHHHHHHHHHH	1.77	29575903
101	Phosphorylation	NYAAAYCTGLLLARR HHHHHHHHHHHHHHH	20.42	28152594
158	Ubiquitination	ARTTTGNKVFGALKG EECCCCCHHHHCCCC	40.04	-
158	2-Hydroxyisobutyrylation	ARTTTGNKVFGALKG EECCCCCHHHHCCCC	40.04	-
158	Acetylation	ARTTTGNKVFGALKG EECCCCCHHHHCCCC	40.04	26051181
164	Methylation	NKVFGALKGAVDGGL CHHHHCCCCHHCCCC	44.27	24129315
164	Sumoylation	NKVFGALKGAVDGGL CHHHHCCCCHHCCCC	44.27	-
164	Ubiquitination	NKVFGALKGAVDGGL CHHHHCCCCHHCCCC	44.27	21890473
164	Sumoylation	NKVFGALKGAVDGGL CHHHHCCCCHHCCCC	44.27	-
164	2-Hydroxyisobutyrylation	NKVFGALKGAVDGGL CHHHHCCCCHHCCCC	44.27	-
164	Acetylation	NKVFGALKGAVDGGL CHHHHCCCCHHCCCC	44.27	26051181
172	Phosphorylation	GAVDGGLSIPHSTKR CHHCCCCCCCCCCCC	37.03	25159151
176	Phosphorylation	GGLSIPHSTKRFPGY CCCCCCCCCCCCCCC	30.21	30266825
177	Phosphorylation	GLSIPHSTKRFPGYD CCCCCCCCCCCCCCC	24.17	30266825
178	Acetylation	LSIPHSTKRFPGYDS CCCCCCCCCCCCCCC	55.87	25953088
178	Ubiquitination	LSIPHSTKRFPGYDS CCCCCCCCCCCCCCC	55.87	21906983
178	2-Hydroxyisobutyrylation	LSIPHSTKRFPGYDS CCCCCCCCCCCCCCC	55.87	-
183	Phosphorylation	STKRFPGYDSESKEF CCCCCCCCCCCCCCC	19.28	30266825
185	Phosphorylation	KRFPGYDSESKEFNA CCCCCCCCCCCCCCH	34.97	30266825
187	Phosphorylation	FPGYDSESKEFNAEV CCCCCCCCCCCCHHH	41.24	30266825
188	Sumoylation	PGYDSESKEFNAEVH CCCCCCCCCCCHHHH	63.37	-
188	Ubiquitination	PGYDSESKEFNAEVH CCCCCCCCCCCHHHH	63.37	21906983
188	Sumoylation	PGYDSESKEFNAEVH CCCCCCCCCCCHHHH	63.37	-
188	Acetylation	PGYDSESKEFNAEVH CCCCCCCCCCCHHHH	63.37	26051181
197	Acetylation	FNAEVHRKHIMGQNV CCHHHHHHHHCCCCH	23.70	25825284
197	Sumoylation	FNAEVHRKHIMGQNV CCHHHHHHHHCCCCH	23.70	-
197	Ubiquitination	FNAEVHRKHIMGQNV CCHHHHHHHHCCCCH	23.70	21906983
197	Sumoylation	FNAEVHRKHIMGQNV CCHHHHHHHHCCCCH	23.70	-
197	2-Hydroxyisobutyrylation	FNAEVHRKHIMGQNV CCHHHHHHHHCCCCH	23.70	-
200	Sulfoxidation	EVHRKHIMGQNVADY HHHHHHHCCCCHHHH	4.52	28183972
207	Phosphorylation	MGQNVADYMRYLMEE CCCCHHHHHHHHHHC	3.61	21945579
208	Sulfoxidation	GQNVADYMRYLMEED CCCHHHHHHHHHHCC	2.03	28183972
209	Methylation	QNVADYMRYLMEEDE CCHHHHHHHHHHCCH	18.40	115492215
210	Phosphorylation	NVADYMRYLMEEDED CHHHHHHHHHHCCHH	8.22	29496907
212	Sulfoxidation	ADYMRYLMEEDEDAY HHHHHHHHHCCHHHH	3.82	30846556
219	Phosphorylation	MEEDEDAYKKQFSQY HHCCHHHHHHHHHHH	30.92	29496907
220	Acetylation	EEDEDAYKKQFSQYI HCCHHHHHHHHHHHH	41.65	23954790
220	Ubiquitination	EEDEDAYKKQFSQYI HCCHHHHHHHHHHHH	41.65	-
220	Sumoylation	EEDEDAYKKQFSQYI HCCHHHHHHHHHHHH	41.65	25114211
220	2-Hydroxyisobutyrylation	EEDEDAYKKQFSQYI HCCHHHHHHHHHHHH	41.65	-
220	Succinylation	EEDEDAYKKQFSQYI HCCHHHHHHHHHHHH	41.65	23954790
221	Acetylation	EDEDAYKKQFSQYIK CCHHHHHHHHHHHHH	43.85	26051181
221	Sumoylation	EDEDAYKKQFSQYIK CCHHHHHHHHHHHHH	43.85	-
221	Ubiquitination	EDEDAYKKQFSQYIK CCHHHHHHHHHHHHH	43.85	21906983
221	Sumoylation	EDEDAYKKQFSQYIK CCHHHHHHHHHHHHH	43.85	-
221	2-Hydroxyisobutyrylation	EDEDAYKKQFSQYIK CCHHHHHHHHHHHHH	43.85	-
224	Phosphorylation	DAYKKQFSQYIKNSV HHHHHHHHHHHHHCC	21.41	28152594
226	Phosphorylation	YKKQFSQYIKNSVTP HHHHHHHHHHHCCCH	16.80	28152594
228	Methylation	KQFSQYIKNSVTPDM HHHHHHHHHCCCHHH	37.93	66704083
228	Ubiquitination	KQFSQYIKNSVTPDM HHHHHHHHHCCCHHH	37.93	21906983
230	Phosphorylation	FSQYIKNSVTPDMME HHHHHHHCCCHHHHH	23.51	20068231
232	Phosphorylation	QYIKNSVTPDMMEEM HHHHHCCCHHHHHHH	17.25	25159151
240	Phosphorylation	PDMMEEMYKKAHAAI HHHHHHHHHHHHHHH	16.77	20068231
241	Acetylation	DMMEEMYKKAHAAIR HHHHHHHHHHHHHHH	42.02	23236377
241	Succinylation	DMMEEMYKKAHAAIR HHHHHHHHHHHHHHH	42.02	23954790
242	Acetylation	MMEEMYKKAHAAIRE HHHHHHHHHHHHHHH	28.10	24471099
242	Ubiquitination	MMEEMYKKAHAAIRE HHHHHHHHHHHHHHH	28.10	-
242	2-Hydroxyisobutyrylation	MMEEMYKKAHAAIRE HHHHHHHHHHHHHHH	28.10	-
248	Methylation	KKAHAAIRENPVYEK HHHHHHHHHCCCCCC	32.67	115492207
253	Phosphorylation	AIRENPVYEKKPKKE HHHHCCCCCCCCHHH	24.24	29496907
255	Ubiquitination	RENPVYEKKPKKEVK HHCCCCCCCCHHHHH	57.60	-
255	2-Hydroxyisobutyrylation	RENPVYEKKPKKEVK HHCCCCCCCCHHHHH	57.60	-
255	Acetylation	RENPVYEKKPKKEVK HHCCCCCCCCHHHHH	57.60	26051181
256	Ubiquitination	ENPVYEKKPKKEVKK HCCCCCCCCHHHHHH	50.56	-
256	Acetylation	ENPVYEKKPKKEVKK HCCCCCCCCHHHHHH	50.56	25953088
258	Ubiquitination	PVYEKKPKKEVKKKR CCCCCCCHHHHHHHH	71.14	-
270	Ubiquitination	KKRWNRPKMSLAQKK HHHCCCCCCCHHHHH	37.57	21906983
270	Acetylation	KKRWNRPKMSLAQKK HHHCCCCCCCHHHHH	37.57	25953088
272	Phosphorylation	RWNRPKMSLAQKKDR HCCCCCCCHHHHHHH	27.04	21406692
276	Acetylation	PKMSLAQKKDRVAQK CCCCHHHHHHHHHHH	51.54	25953088
276	Ubiquitination	PKMSLAQKKDRVAQK CCCCHHHHHHHHHHH	51.54	-
276	2-Hydroxyisobutyrylation	PKMSLAQKKDRVAQK CCCCHHHHHHHHHHH	51.54	-
283	Methylation	KKDRVAQKKASFLRA HHHHHHHHHHHHHHH	40.34	116252325
284	Ubiquitination	KDRVAQKKASFLRAQ HHHHHHHHHHHHHHH	36.86	-
286	Phosphorylation	RVAQKKASFLRAQER HHHHHHHHHHHHHHH	33.42	23927012
297	Phosphorylation	AQERAAES------- HHHHHHHC-------	40.57	25056879

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 RL5_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of RL5_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 RL5_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PDCD4_HUMAN	PDCD4	physical	12054647
MDM2_HUMAN	MDM2	physical	15308643
RL11_HUMAN	RPL11	physical	15308643
RL23_HUMAN	RPL23	physical	15308643
P53_HUMAN	TP53	physical	15308643
MDM2_HUMAN	MDM2	physical	17116689
RL11_HUMAN	RPL11	physical	17116689
RL23_HUMAN	RPL23	physical	17116689
MDM2_HUMAN	MDM2	physical	18560357
MDM2_HUMAN	MDM2	physical	17242401
RL11_HUMAN	RPL11	physical	17242401
RL7_HUMAN	RPL7	physical	22939629
RS23_HUMAN	RPS23	physical	22939629
RS3A_HUMAN	RPS3A	physical	22939629
RS4X_HUMAN	RPS4X	physical	22939629
RS6_HUMAN	RPS6	physical	22939629
RSSA_HUMAN	RPSA	physical	22939629
RLA0_HUMAN	RPLP0	physical	22939629
RL6_HUMAN	RPL6	physical	22939629
RL7A_HUMAN	RPL7A	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
RS19_HUMAN	RPS19	physical	22939629
RS28_HUMAN	RPS28	physical	22939629
RS2_HUMAN	RPS2	physical	22939629
RS3_HUMAN	RPS3	physical	22939629
RS5_HUMAN	RPS5	physical	22939629
RS7_HUMAN	RPS7	physical	22939629
RS8_HUMAN	RPS8	physical	22939629
RLA2_HUMAN	RPLP2	physical	22939629
RS24_HUMAN	RPS24	physical	22939629
RS12_HUMAN	RPS12	physical	22939629
RS17_HUMAN	RPS17	physical	22939629
RS20_HUMAN	RPS20	physical	22939629
RS14_HUMAN	RPS14	physical	22939629
RS26_HUMAN	RPS26	physical	22939629
RS25_HUMAN	RPS25	physical	22939629
RS9_HUMAN	RPS9	physical	22939629
RS10_HUMAN	RPS10	physical	22939629
RS21_HUMAN	RPS21	physical	22939629
RS27A_HUMAN	RPS27A	physical	22939629
UBIM_HUMAN	FAU	physical	22939629
TBA1A_HUMAN	TUBA1A	physical	22939629
RRP12_HUMAN	RRP12	physical	22939629
SSRG_HUMAN	SSR3	physical	22939629
RRS1_HUMAN	RRS1	physical	22939629
RS27L_HUMAN	RPS27L	physical	22939629
TBA1B_HUMAN	TUBA1B	physical	22939629
VASN_HUMAN	VASN	physical	22939629
SPB1_HUMAN	FTSJ3	physical	22939629
MDM2_HUMAN	MDM2	physical	23169665
RL5_HUMAN	RPL5	physical	23169665
RL11_HUMAN	RPL11	physical	23169665
P53_HUMAN	TP53	physical	23169665
PML_HUMAN	PML	physical	23169665
VA0D1_HUMAN	ATP6V0D1	physical	26344197
DDX24_HUMAN	DDX24	physical	26344197
EF1A1_HUMAN	EEF1A1	physical	26344197
IF6_HUMAN	EIF6	physical	26344197
RACK1_HUMAN	GNB2L1	physical	26344197
NSA2_HUMAN	NSA2	physical	26344197
PABP1_HUMAN	PABPC1	physical	26344197
PABP4_HUMAN	PABPC4	physical	26344197
PWP1_HUMAN	PWP1	physical	26344197
RL10A_HUMAN	RPL10A	physical	26344197
RL11_HUMAN	RPL11	physical	26344197
RL12_HUMAN	RPL12	physical	26344197
RL13_HUMAN	RPL13	physical	26344197
RL14_HUMAN	RPL14	physical	26344197
RL15_HUMAN	RPL15	physical	26344197
RL17_HUMAN	RPL17	physical	26344197
RL27_HUMAN	RPL27	physical	26344197
RL27A_HUMAN	RPL27A	physical	26344197
RL28_HUMAN	RPL28	physical	26344197
RL30_HUMAN	RPL30	physical	26344197
RL31_HUMAN	RPL31	physical	26344197
RL35_HUMAN	RPL35	physical	26344197
RL36_HUMAN	RPL36	physical	26344197
RL37A_HUMAN	RPL37A	physical	26344197
RL38_HUMAN	RPL38	physical	26344197
RL3L_HUMAN	RPL3L	physical	26344197
RL4_HUMAN	RPL4	physical	26344197
RL6_HUMAN	RPL6	physical	26344197
RL7A_HUMAN	RPL7A	physical	26344197
RL9_HUMAN	RPL9	physical	26344197
RLA1_HUMAN	RPLP1	physical	26344197
RS10_HUMAN	RPS10	physical	26344197
RS15A_HUMAN	RPS15A	physical	26344197
RS16_HUMAN	RPS16	physical	26344197
RS17_HUMAN	RPS17	physical	26344197
RS18_HUMAN	RPS18	physical	26344197
RS25_HUMAN	RPS25	physical	26344197
RS27_HUMAN	RPS27	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
RS9_HUMAN	RPS9	physical	26344197
RSSA_HUMAN	RPSA	physical	26344197
S61A1_HUMAN	SEC61A1	physical	26344197
XRN1_HUMAN	XRN1	physical	26344197
P73_HUMAN	TP73	physical	25301064

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
612561	Diamond-Blackfan anemia 6 (DBA6)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of RL5_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-5 AND LYS-48, AND MASSSPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry."; Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.; Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-286, AND MASSSPECTROMETRY.	17287340 [Abstract]