dbPTM

RL3_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RL3_HUMAN
UniProt AC	P39023
Protein Name	60S ribosomal protein L3
Gene Name	RPL3
Organism	Homo sapiens (Human).
Sequence Length	403
Subcellular Localization	Nucleus, nucleolus . Cytoplasm .
Protein Description	The L3 protein is a component of the large subunit of cytoplasmic ribosomes..
Protein Sequence	MSHRKFSAPRHGSLGFLPRKRSSRHRGKVKSFPKDDPSKPVHLTAFLGYKAGMTHIVREVDRPGSKVNKKEVVEAVTIVETPPMVVVGIVGYVETPRGLRTFKTVFAEHISDECKRRFYKNWHKSKKKAFTKYCKKWQDEDGKKQLEKDFSSMKKYCQVIRVIAHTQMRLLPLRQKKAHLMEIQVNGGTVAEKLDWARERLEQQVPVNQVFGQDEMIDVIGVTKGKGYKGVTSRWHTKKLPRKTHRGLRKVACIGAWHPARVAFSVARAGQKGYHHRTEINKKIYKIGQGYLIKDGKLIKNNASTDYDLSDKSINPLGGFVHYGEVTNDFVMLKGCVVGTKKRVLTLRKSLLVQTKRRALEKIDLKFIDTTSKFGHGRFQTMEEKKAFMGPLKKDRIAKEEGA

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
7	Phosphorylation	-MSHRKFSAPRHGSL -CCCCCCCCCCCCCC	40.16	23927012
13	Phosphorylation	FSAPRHGSLGFLPRK CCCCCCCCCCCCCCC	21.13	25159151
19	Methylation	GSLGFLPRKRSSRHR CCCCCCCCCCCCCCC	49.52	115492017
34	Acetylation	GKVKSFPKDDPSKPV CCCCCCCCCCCCCCC	73.14	26051181
39	Acetylation	FPKDDPSKPVHLTAF CCCCCCCCCCEEEEE	57.35	26051181
39	Sumoylation	FPKDDPSKPVHLTAF CCCCCCCCCCEEEEE	57.35	28112733
39	Ubiquitination	FPKDDPSKPVHLTAF CCCCCCCCCCEEEEE	57.35	21890473
53	Sulfoxidation	FLGYKAGMTHIVREV EECHHHCCCEEEEEC	2.70	30846556
54	Phosphorylation	LGYKAGMTHIVREVD ECHHHCCCEEEEECC	13.92	20068231
65	Phosphorylation	REVDRPGSKVNKKEV EECCCCCCCCCHHHH	35.79	24719451
66	Ubiquitination	EVDRPGSKVNKKEVV ECCCCCCCCCHHHHE	56.60	-
103	2-Hydroxyisobutyrylation	PRGLRTFKTVFAEHI CCCCCHHHHHHHHHC	43.07	-
103	Acetylation	PRGLRTFKTVFAEHI CCCCCHHHHHHHHHC	43.07	25825284
114	Glutathionylation	AEHISDECKRRFYKN HHHCCHHHHHHHHHH	5.08	22555962
114	S-nitrosylation	AEHISDECKRRFYKN HHHCCHHHHHHHHHH	5.08	2212679
115	Acetylation	EHISDECKRRFYKNW HHCCHHHHHHHHHHH	44.56	25825284
115	Ubiquitination	EHISDECKRRFYKNW HHCCHHHHHHHHHHH	44.56	21906983
120	2-Hydroxyisobutyrylation	ECKRRFYKNWHKSKK HHHHHHHHHHHHHHH	51.34	-
120	Acetylation	ECKRRFYKNWHKSKK HHHHHHHHHHHHHHH	51.34	27452117
120	Ubiquitination	ECKRRFYKNWHKSKK HHHHHHHHHHHHHHH	51.34	21890473
125	Phosphorylation	FYKNWHKSKKKAFTK HHHHHHHHHHHHHHH	36.50	-
132	Acetylation	SKKKAFTKYCKKWQD HHHHHHHHHHHHHCC	42.04	25953088
132	Ubiquitination	SKKKAFTKYCKKWQD HHHHHHHHHHHHHCC	42.04	-
136	Acetylation	AFTKYCKKWQDEDGK HHHHHHHHHCCCHHH	46.67	26051181
136	Ubiquitination	AFTKYCKKWQDEDGK HHHHHHHHHCCCHHH	46.67	-
143	2-Hydroxyisobutyrylation	KWQDEDGKKQLEKDF HHCCCHHHHHHHHHH	50.06	-
143	Acetylation	KWQDEDGKKQLEKDF HHCCCHHHHHHHHHH	50.06	26051181
144	Acetylation	WQDEDGKKQLEKDFS HCCCHHHHHHHHHHH	66.69	26051181
148	2-Hydroxyisobutyrylation	DGKKQLEKDFSSMKK HHHHHHHHHHHHHHH	73.07	-
148	Acetylation	DGKKQLEKDFSSMKK HHHHHHHHHHHHHHH	73.07	23954790
148	Succinylation	DGKKQLEKDFSSMKK HHHHHHHHHHHHHHH	73.07	23954790
148	Ubiquitination	DGKKQLEKDFSSMKK HHHHHHHHHHHHHHH	73.07	-
154	2-Hydroxyisobutyrylation	EKDFSSMKKYCQVIR HHHHHHHHHHHHHHH	42.40	-
154	Acetylation	EKDFSSMKKYCQVIR HHHHHHHHHHHHHHH	42.40	25953088
155	2-Hydroxyisobutyrylation	KDFSSMKKYCQVIRV HHHHHHHHHHHHHHH	42.49	-
155	Acetylation	KDFSSMKKYCQVIRV HHHHHHHHHHHHHHH	42.49	25953088
155	Ubiquitination	KDFSSMKKYCQVIRV HHHHHHHHHHHHHHH	42.49	-
156	Phosphorylation	DFSSMKKYCQVIRVI HHHHHHHHHHHHHHH	5.21	28152594
157	Glutathionylation	FSSMKKYCQVIRVIA HHHHHHHHHHHHHHH	3.41	22555962
169	Methylation	VIAHTQMRLLPLRQK HHHHHHHHHHCHHHH	24.21	115492033
177	2-Hydroxyisobutyrylation	LLPLRQKKAHLMEIQ HHCHHHHCCCEEEEE	32.47	-
177	Acetylation	LLPLRQKKAHLMEIQ HHCHHHHCCCEEEEE	32.47	26051181
189	Phosphorylation	EIQVNGGTVAEKLDW EEEECCCHHHHHHHH	20.24	20068231
193	Acetylation	NGGTVAEKLDWARER CCCHHHHHHHHHHHH	41.85	26051181
193	Ubiquitination	NGGTVAEKLDWARER CCCHHHHHHHHHHHH	41.85	-
216	Sulfoxidation	QVFGQDEMIDVIGVT HHHCCCCEEEEEEEC	4.22	21406390
224	2-Hydroxyisobutyrylation	IDVIGVTKGKGYKGV EEEEEECCCCCCCCC	57.10	-
224	Sumoylation	IDVIGVTKGKGYKGV EEEEEECCCCCCCCC	57.10	28112733
224	Ubiquitination	IDVIGVTKGKGYKGV EEEEEECCCCCCCCC	57.10	21890473
226	Sumoylation	VIGVTKGKGYKGVTS EEEECCCCCCCCCCC	61.70	28112733
228	Phosphorylation	GVTKGKGYKGVTSRW EECCCCCCCCCCCCC	14.19	28509920
229	2-Hydroxyisobutyrylation	VTKGKGYKGVTSRWH ECCCCCCCCCCCCCC	56.42	-
229	Acetylation	VTKGKGYKGVTSRWH ECCCCCCCCCCCCCC	56.42	26210075
229	Ubiquitination	VTKGKGYKGVTSRWH ECCCCCCCCCCCCCC	56.42	-
232	Phosphorylation	GKGYKGVTSRWHTKK CCCCCCCCCCCCCCC	22.65	28509920
233	Phosphorylation	KGYKGVTSRWHTKKL CCCCCCCCCCCCCCC	30.85	28509920
250	Sumoylation	KTHRGLRKVACIGAW CCCCCCCCEEEEECC	38.95	-
250	Methylation	KTHRGLRKVACIGAW CCCCCCCCEEEEECC	38.95	23644510
250	Sumoylation	KTHRGLRKVACIGAW CCCCCCCCEEEEECC	38.95	-
250	Ubiquitination	KTHRGLRKVACIGAW CCCCCCCCEEEEECC	38.95	-
253	Glutathionylation	RGLRKVACIGAWHPA CCCCCEEEEECCCHH	3.10	22555962
253	S-palmitoylation	RGLRKVACIGAWHPA CCCCCEEEEECCCHH	3.10	26865113
265	Phosphorylation	HPARVAFSVARAGQK CHHHHHHHHHHCCCC	12.72	30266825
268	Methylation	RVAFSVARAGQKGYH HHHHHHHHCCCCCCC	36.78	115492025
272	2-Hydroxyisobutyrylation	SVARAGQKGYHHRTE HHHHCCCCCCCCCHH	61.59	-
283	Ubiquitination	HRTEINKKIYKIGQG CCHHHHHHHEEECCC	46.94	-
285	Phosphorylation	TEINKKIYKIGQGYL HHHHHHHEEECCCEE	12.87	29438985
286	Sumoylation	EINKKIYKIGQGYLI HHHHHHEEECCCEEE	43.78	-
286	Acetylation	EINKKIYKIGQGYLI HHHHHHEEECCCEEE	43.78	25953088
286	Sumoylation	EINKKIYKIGQGYLI HHHHHHEEECCCEEE	43.78	28112733
286	Ubiquitination	EINKKIYKIGQGYLI HHHHHHEEECCCEEE	43.78	21890473
291	Phosphorylation	IYKIGQGYLIKDGKL HEEECCCEEEECCCE	9.43	28152594
294	Sumoylation	IGQGYLIKDGKLIKN ECCCEEEECCCEECC	58.81	-
294	2-Hydroxyisobutyrylation	IGQGYLIKDGKLIKN ECCCEEEECCCEECC	58.81	-
294	Acetylation	IGQGYLIKDGKLIKN ECCCEEEECCCEECC	58.81	19608861
294	Malonylation	IGQGYLIKDGKLIKN ECCCEEEECCCEECC	58.81	26320211
294	Sumoylation	IGQGYLIKDGKLIKN ECCCEEEECCCEECC	58.81	19608861
294	Ubiquitination	IGQGYLIKDGKLIKN ECCCEEEECCCEECC	58.81	19608861
297	Acetylation	GYLIKDGKLIKNNAS CEEEECCCEECCCCC	58.11	26051181
297	Ubiquitination	GYLIKDGKLIKNNAS CEEEECCCEECCCCC	58.11	-
300	Sumoylation	IKDGKLIKNNASTDY EECCCEECCCCCCCC	55.36	-
300	2-Hydroxyisobutyrylation	IKDGKLIKNNASTDY EECCCEECCCCCCCC	55.36	-
300	Acetylation	IKDGKLIKNNASTDY EECCCEECCCCCCCC	55.36	26051181
300	Malonylation	IKDGKLIKNNASTDY EECCCEECCCCCCCC	55.36	26320211
300	Sumoylation	IKDGKLIKNNASTDY EECCCEECCCCCCCC	55.36	-
300	Ubiquitination	IKDGKLIKNNASTDY EECCCEECCCCCCCC	55.36	21890473
304	Phosphorylation	KLIKNNASTDYDLSD CEECCCCCCCCCCCC	24.76	25159151
305	Phosphorylation	LIKNNASTDYDLSDK EECCCCCCCCCCCCC	35.85	28152594
307	Phosphorylation	KNNASTDYDLSDKSI CCCCCCCCCCCCCCC	20.90	27273156
310	Phosphorylation	ASTDYDLSDKSINPL CCCCCCCCCCCCCCC	39.84	28796482
312	Acetylation	TDYDLSDKSINPLGG CCCCCCCCCCCCCCC	50.27	26051181
312	Sumoylation	TDYDLSDKSINPLGG CCCCCCCCCCCCCCC	50.27	-
312	Ubiquitination	TDYDLSDKSINPLGG CCCCCCCCCCCCCCC	50.27	21890473
323	Phosphorylation	PLGGFVHYGEVTNDF CCCCCCEEEECCCCE	15.07	27642862
332	Sulfoxidation	EVTNDFVMLKGCVVG ECCCCEEEEECCEEC	3.02	30846556
341	2-Hydroxyisobutyrylation	KGCVVGTKKRVLTLR ECCEECCCHHHHHHH	32.43	-
341	Acetylation	KGCVVGTKKRVLTLR ECCEECCCHHHHHHH	32.43	18585095
341	Ubiquitination	KGCVVGTKKRVLTLR ECCEECCCHHHHHHH	32.43	-
342	Acetylation	GCVVGTKKRVLTLRK CCEECCCHHHHHHHH	47.80	18585103
346	Phosphorylation	GTKKRVLTLRKSLLV CCCHHHHHHHHHHHH	22.97	26434776
349	2-Hydroxyisobutyrylation	KRVLTLRKSLLVQTK HHHHHHHHHHHHHHH	48.87	-
349	Acetylation	KRVLTLRKSLLVQTK HHHHHHHHHHHHHHH	48.87	27178108
349	Ubiquitination	KRVLTLRKSLLVQTK HHHHHHHHHHHHHHH	48.87	21890473
350	Phosphorylation	RVLTLRKSLLVQTKR HHHHHHHHHHHHHHH	22.09	30266825
355	Phosphorylation	RKSLLVQTKRRALEK HHHHHHHHHHHHHHH	21.02	26434776
356	2-Hydroxyisobutyrylation	KSLLVQTKRRALEKI HHHHHHHHHHHHHHC	23.85	-
356	Acetylation	KSLLVQTKRRALEKI HHHHHHHHHHHHHHC	23.85	25953088
356	Succinylation	KSLLVQTKRRALEKI HHHHHHHHHHHHHHC	23.85	23954790
356	Ubiquitination	KSLLVQTKRRALEKI HHHHHHHHHHHHHHC	23.85	-
362	2-Hydroxyisobutyrylation	TKRRALEKIDLKFID HHHHHHHHCCEEEEE	42.23	-
362	Acetylation	TKRRALEKIDLKFID HHHHHHHHCCEEEEE	42.23	25953088
362	Succinylation	TKRRALEKIDLKFID HHHHHHHHCCEEEEE	42.23	23954790
362	Ubiquitination	TKRRALEKIDLKFID HHHHHHHHCCEEEEE	42.23	21890473
366	Sumoylation	ALEKIDLKFIDTTSK HHHHCCEEEEECCCC	36.20	-
366	2-Hydroxyisobutyrylation	ALEKIDLKFIDTTSK HHHHCCEEEEECCCC	36.20	-
366	Acetylation	ALEKIDLKFIDTTSK HHHHCCEEEEECCCC	36.20	19608861
366	Succinylation	ALEKIDLKFIDTTSK HHHHCCEEEEECCCC	36.20	23954790
366	Sumoylation	ALEKIDLKFIDTTSK HHHHCCEEEEECCCC	36.20	28112733
366	Ubiquitination	ALEKIDLKFIDTTSK HHHHCCEEEEECCCC	36.20	21890473
370	Phosphorylation	IDLKFIDTTSKFGHG CCEEEEECCCCCCCC	28.31	29514088
371	Phosphorylation	DLKFIDTTSKFGHGR CEEEEECCCCCCCCC	26.60	29514088
372	Phosphorylation	LKFIDTTSKFGHGRF EEEEECCCCCCCCCC	28.25	29514088
373	Sumoylation	KFIDTTSKFGHGRFQ EEEECCCCCCCCCCC	53.96	-
373	2-Hydroxyisobutyrylation	KFIDTTSKFGHGRFQ EEEECCCCCCCCCCC	53.96	-
373	Acetylation	KFIDTTSKFGHGRFQ EEEECCCCCCCCCCC	53.96	23954790
373	Methylation	KFIDTTSKFGHGRFQ EEEECCCCCCCCCCC	53.96	68777
373	Sumoylation	KFIDTTSKFGHGRFQ EEEECCCCCCCCCCC	53.96	19608861
373	Ubiquitination	KFIDTTSKFGHGRFQ EEEECCCCCCCCCCC	53.96	21890473
381	Phosphorylation	FGHGRFQTMEEKKAF CCCCCCCCHHHHHHH	24.68	20068231
382	Sulfoxidation	GHGRFQTMEEKKAFM CCCCCCCHHHHHHHC	4.32	21406390
385	2-Hydroxyisobutyrylation	RFQTMEEKKAFMGPL CCCCHHHHHHHCCCC	35.77	-
385	Acetylation	RFQTMEEKKAFMGPL CCCCHHHHHHHCCCC	35.77	26051181
385	Ubiquitination	RFQTMEEKKAFMGPL CCCCHHHHHHHCCCC	35.77	21906983
386	Sumoylation	FQTMEEKKAFMGPLK CCCHHHHHHHCCCCH	50.57	-
386	2-Hydroxyisobutyrylation	FQTMEEKKAFMGPLK CCCHHHHHHHCCCCH	50.57	-
386	Acetylation	FQTMEEKKAFMGPLK CCCHHHHHHHCCCCH	50.57	26051181
386	Sumoylation	FQTMEEKKAFMGPLK CCCHHHHHHHCCCCH	50.57	28112733
386	Ubiquitination	FQTMEEKKAFMGPLK CCCHHHHHHHCCCCH	50.57	21890473
393	Sumoylation	KAFMGPLKKDRIAKE HHHCCCCHHHHHHHH	56.62	-
393	2-Hydroxyisobutyrylation	KAFMGPLKKDRIAKE HHHCCCCHHHHHHHH	56.62	-
393	Acetylation	KAFMGPLKKDRIAKE HHHCCCCHHHHHHHH	56.62	25953088
393	Succinylation	KAFMGPLKKDRIAKE HHHCCCCHHHHHHHH	56.62	23954790
393	Sumoylation	KAFMGPLKKDRIAKE HHHCCCCHHHHHHHH	56.62	28112733
393	Ubiquitination	KAFMGPLKKDRIAKE HHHCCCCHHHHHHHH	56.62	-
394	"N6,N6-dimethyllysine"	AFMGPLKKDRIAKEE HHCCCCHHHHHHHHC	60.98	-
394	Methylation	AFMGPLKKDRIAKEE HHCCCCHHHHHHHHC	60.98	-
399	"N6,N6-dimethyllysine"	LKKDRIAKEEGA--- CHHHHHHHHCCC---	54.66	-
399	Methylation	LKKDRIAKEEGA--- CHHHHHHHHCCC---	54.66	-
399	Succinylation	LKKDRIAKEEGA--- CHHHHHHHHCCC---	54.66	23954790
399	Sumoylation	LKKDRIAKEEGA--- CHHHHHHHHCCC---	54.66	28112733

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 RL3_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of RL3_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 RL3_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RL4_HUMAN	RPL4	physical	22939629
RL5_HUMAN	RPL5	physical	22939629
RL7_HUMAN	RPL7	physical	22939629
RL8_HUMAN	RPL8	physical	22939629
RL9_HUMAN	RPL9	physical	22939629
RS16_HUMAN	RPS16	physical	22939629
RS23_HUMAN	RPS23	physical	22939629
RS26_HUMAN	RPS26	physical	22939629
RS2_HUMAN	RPS2	physical	22939629
RS3A_HUMAN	RPS3A	physical	22939629
RS3_HUMAN	RPS3	physical	22939629
RS4X_HUMAN	RPS4X	physical	22939629
RS8_HUMAN	RPS8	physical	22939629
RSSA_HUMAN	RPSA	physical	22939629
RL6_HUMAN	RPL6	physical	22939629
RS15_HUMAN	RPS15	physical	22939629
RL7A_HUMAN	RPL7A	physical	22939629
RS6_HUMAN	RPS6	physical	22939629
RS20_HUMAN	RPS20	physical	22939629
RS13_HUMAN	RPS13	physical	22939629
RS7_HUMAN	RPS7	physical	22939629
RLA0_HUMAN	RPLP0	physical	22939629
RS15A_HUMAN	RPS15A	physical	22939629
RS24_HUMAN	RPS24	physical	22939629
STXB3_HUMAN	STXBP3	physical	21988832
SIK1_HUMAN	SIK1	physical	21988832
SYDC_HUMAN	DARS	physical	22863883
TBCD4_HUMAN	TBC1D4	physical	22863883
EF1A1_HUMAN	EEF1A1	physical	26344197
NUCL_HUMAN	NCL	physical	26344197
RNPS1_HUMAN	RNPS1	physical	26344197
RL10_HUMAN	RPL10	physical	26344197
RL10A_HUMAN	RPL10A	physical	26344197
RL10L_HUMAN	RPL10L	physical	26344197
RL12_HUMAN	RPL12	physical	26344197
RL13_HUMAN	RPL13	physical	26344197
RL13A_HUMAN	RPL13A	physical	26344197
RL14_HUMAN	RPL14	physical	26344197
RL15_HUMAN	RPL15	physical	26344197
RL17_HUMAN	RPL17	physical	26344197
RL18_HUMAN	RPL18	physical	26344197
RL18A_HUMAN	RPL18A	physical	26344197
RL19_HUMAN	RPL19	physical	26344197
RL21_HUMAN	RPL21	physical	26344197
RL23A_HUMAN	RPL23A	physical	26344197
RL24_HUMAN	RPL24	physical	26344197
RL26_HUMAN	RPL26	physical	26344197
RL26L_HUMAN	RPL26L1	physical	26344197
RL27A_HUMAN	RPL27A	physical	26344197
RL28_HUMAN	RPL28	physical	26344197
RL30_HUMAN	RPL30	physical	26344197
RL32_HUMAN	RPL32	physical	26344197
RL34_HUMAN	RPL34	physical	26344197
RL35_HUMAN	RPL35	physical	26344197
RL35A_HUMAN	RPL35A	physical	26344197
RL36L_HUMAN	RPL36AL	physical	26344197
RL37A_HUMAN	RPL37A	physical	26344197
RL38_HUMAN	RPL38	physical	26344197
RL5_HUMAN	RPL5	physical	26344197
RL6_HUMAN	RPL6	physical	26344197
RL9_HUMAN	RPL9	physical	26344197
RLA1_HUMAN	RPLP1	physical	26344197
RLA2_HUMAN	RPLP2	physical	26344197
RS11_HUMAN	RPS11	physical	26344197
RS12_HUMAN	RPS12	physical	26344197
RS13_HUMAN	RPS13	physical	26344197
RS14_HUMAN	RPS14	physical	26344197
RS15_HUMAN	RPS15	physical	26344197
RS15A_HUMAN	RPS15A	physical	26344197
RS16_HUMAN	RPS16	physical	26344197
RS19_HUMAN	RPS19	physical	26344197
RS20_HUMAN	RPS20	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
RS5_HUMAN	RPS5	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
RRP12_HUMAN	RRP12	physical	26344197
S61A1_HUMAN	SEC61A1	physical	26344197
EAA2_HUMAN	SLC1A2	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
DB04865	Homoharringtonine

Regulatory Network of RL3_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-294; LYS-366 AND LYS-373,AND MASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"Large-scale proteomics analysis of the human kinome."; Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.; Mol. Cell. Proteomics 8:1751-1764(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13, AND MASSSPECTROMETRY.	19369195 [Abstract]
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13, AND MASSSPECTROMETRY.	18669648 [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 SER-7, AND MASSSPECTROMETRY.	18691976 [Abstract]
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer."; Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.; Cell 131:1190-1203(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-307, AND MASSSPECTROMETRY.	18083107 [Abstract]
"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-307, AND MASSSPECTROMETRY.	15592455 [Abstract]