dbPTM

RL4_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RL4_HUMAN
UniProt AC	P36578
Protein Name	60S ribosomal protein L4
Gene Name	RPL4
Organism	Homo sapiens (Human).
Sequence Length	427
Subcellular Localization
Protein Description
Protein Sequence	MACARPLISVYSEKGESSGKNVTLPAVFKAPIRPDIVNFVHTNLRKNNRQPYAVSELAGHQTSAESWGTGRAVARIPRVRGGGTHRSGQGAFGNMCRGGRMFAPTKTWRRWHRRVNTTQKRYAICSALAASALPALVMSKGHRIEEVPELPLVVEDKVEGYKKTKEAVLLLKKLKAWNDIKKVYASQRMRAGKGKMRNRRRIQRRGPCIIYNEDNGIIKAFRNIPGITLLNVSKLNILKLAPGGHVGRFCIWTESAFRKLDELYGTWRKAASLKSNYNLPMHKMINTDLSRILKSPEIQRALRAPRKKIHRRVLKKNPLKNLRIMLKLNPYAKTMRRNTILRQARNHKLRVDKAAAAAAALQAKSDEKAAVAGKKPVVGKKGKKAAVGVKKQKKPLVGKKAAATKKPAPEKKPAEKKPTTEEKKPAA

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MACARPLIS ------CCCCCCCEE	8.83	19413330
3	S-palmitoylation	-----MACARPLISV -----CCCCCCCEEE	2.97	29575903
9	Phosphorylation	ACARPLISVYSEKGE CCCCCCEEEEECCCC	23.76	23312004
11	Phosphorylation	ARPLISVYSEKGESS CCCCEEEEECCCCCC	12.34	28152594
12	Phosphorylation	RPLISVYSEKGESSG CCCEEEEECCCCCCC	30.58	28152594
14	Acetylation	LISVYSEKGESSGKN CEEEEECCCCCCCCC	63.14	19608861
14	Malonylation	LISVYSEKGESSGKN CEEEEECCCCCCCCC	63.14	26320211
14	Ubiquitination	LISVYSEKGESSGKN CEEEEECCCCCCCCC	63.14	27667366
17	Phosphorylation	VYSEKGESSGKNVTL EEECCCCCCCCCCCC	53.73	23312004
18	Phosphorylation	YSEKGESSGKNVTLP EECCCCCCCCCCCCC	49.86	23312004
20	2-Hydroxyisobutyrylation	EKGESSGKNVTLPAV CCCCCCCCCCCCCEE	50.63	-
20	Acetylation	EKGESSGKNVTLPAV CCCCCCCCCCCCCEE	50.63	26051181
20	Malonylation	EKGESSGKNVTLPAV CCCCCCCCCCCCCEE	50.63	30639696
20	Ubiquitination	EKGESSGKNVTLPAV CCCCCCCCCCCCCEE	50.63	21906983
23	Phosphorylation	ESSGKNVTLPAVFKA CCCCCCCCCCEEECC	36.10	21712546
29	Acetylation	VTLPAVFKAPIRPDI CCCCEEECCCCCHHH	46.80	23749302
29	Methylation	VTLPAVFKAPIRPDI CCCCEEECCCCCHHH	46.80	72592287
29	Ubiquitination	VTLPAVFKAPIRPDI CCCCEEECCCCCHHH	46.80	21963094
46	Ubiquitination	FVHTNLRKNNRQPYA HHHHHCCCCCCCCCC	62.84	-
52	Phosphorylation	RKNNRQPYAVSELAG CCCCCCCCCHHHHCC	15.99	28152594
55	Phosphorylation	NRQPYAVSELAGHQT CCCCCCHHHHCCCCC	20.79	28152594
62	Phosphorylation	SELAGHQTSAESWGT HHHCCCCCCHHHHCC	24.99	27080861
63	Phosphorylation	ELAGHQTSAESWGTG HHCCCCCCHHHHCCC	24.38	27080861
66	Phosphorylation	GHQTSAESWGTGRAV CCCCCHHHHCCCCCE	30.44	27080861
69	Phosphorylation	TSAESWGTGRAVARI CCHHHHCCCCCEEEC	19.75	-
71	Methylation	AESWGTGRAVARIPR HHHHCCCCCEEECCC	26.23	115492177
80	Methylation	VARIPRVRGGGTHRS EEECCCCCCCCCCCC	39.04	82955055
86	Methylation	VRGGGTHRSGQGAFG CCCCCCCCCCCCCCC	42.17	83445847
87	Phosphorylation	RGGGTHRSGQGAFGN CCCCCCCCCCCCCCC	28.06	28450419
95	Sulfoxidation	GQGAFGNMCRGGRMF CCCCCCCCCCCCCCC	1.36	30846556
96	S-nitrosocysteine	QGAFGNMCRGGRMFA CCCCCCCCCCCCCCC	4.19	-
96	Glutathionylation	QGAFGNMCRGGRMFA CCCCCCCCCCCCCCC	4.19	22555962
96	S-nitrosylation	QGAFGNMCRGGRMFA CCCCCCCCCCCCCCC	4.19	22178444
97	Methylation	GAFGNMCRGGRMFAP CCCCCCCCCCCCCCC	39.57	16186617
100	Methylation	GNMCRGGRMFAPTKT CCCCCCCCCCCCHHH	21.62	26494253
106	Acetylation	GRMFAPTKTWRRWHR CCCCCCHHHHHHHHH	45.06	19608861
106	Ubiquitination	GRMFAPTKTWRRWHR CCCCCCHHHHHHHHH	45.06	23000965
107	Phosphorylation	RMFAPTKTWRRWHRR CCCCCHHHHHHHHHH	27.04	32645325
120	2-Hydroxyisobutyrylation	RRVNTTQKRYAICSA HHCCCHHHHHHHHHH	45.33	-
120	Ubiquitination	RRVNTTQKRYAICSA HHCCCHHHHHHHHHH	45.33	-
122	Phosphorylation	VNTTQKRYAICSALA CCCHHHHHHHHHHHH	13.83	21712546
125	Glutathionylation	TQKRYAICSALAASA HHHHHHHHHHHHHHH	1.16	22555962
126	Phosphorylation	QKRYAICSALAASAL HHHHHHHHHHHHHHH	21.87	20068231
131	Phosphorylation	ICSALAASALPALVM HHHHHHHHHHHHHHH	25.40	20068231
138	Sulfoxidation	SALPALVMSKGHRIE HHHHHHHHCCCCCCE	3.40	30846556
139	Phosphorylation	ALPALVMSKGHRIEE HHHHHHHCCCCCCEE	28.18	20068231
140	2-Hydroxyisobutyrylation	LPALVMSKGHRIEEV HHHHHHCCCCCCEEC	40.41	-
140	Acetylation	LPALVMSKGHRIEEV HHHHHHCCCCCCEEC	40.41	25953088
140	Ubiquitination	LPALVMSKGHRIEEV HHHHHHCCCCCCEEC	40.41	21906983
157	Acetylation	LPLVVEDKVEGYKKT CCEEEECCCCCCCHH	28.78	25953088
157	Ubiquitination	LPLVVEDKVEGYKKT CCEEEECCCCCCCHH	28.78	21963094
161	Phosphorylation	VEDKVEGYKKTKEAV EECCCCCCCHHHHHH	8.87	28152594
162	2-Hydroxyisobutyrylation	EDKVEGYKKTKEAVL ECCCCCCCHHHHHHH	65.90	-
162	Acetylation	EDKVEGYKKTKEAVL ECCCCCCCHHHHHHH	65.90	25953088
162	Ubiquitination	EDKVEGYKKTKEAVL ECCCCCCCHHHHHHH	65.90	23000965
163	Acetylation	DKVEGYKKTKEAVLL CCCCCCCHHHHHHHH	57.24	130547
163	Ubiquitination	DKVEGYKKTKEAVLL CCCCCCCHHHHHHHH	57.24	23000965
165	2-Hydroxyisobutyrylation	VEGYKKTKEAVLLLK CCCCCHHHHHHHHHH	53.18	-
165	Ubiquitination	VEGYKKTKEAVLLLK CCCCCHHHHHHHHHH	53.18	23000965
172	2-Hydroxyisobutyrylation	KEAVLLLKKLKAWND HHHHHHHHHHHHHHH	56.90	-
172	Acetylation	KEAVLLLKKLKAWND HHHHHHHHHHHHHHH	56.90	26051181
172	Succinylation	KEAVLLLKKLKAWND HHHHHHHHHHHHHHH	56.90	23954790
172	Ubiquitination	KEAVLLLKKLKAWND HHHHHHHHHHHHHHH	56.90	21963094
173	Ubiquitination	EAVLLLKKLKAWNDI HHHHHHHHHHHHHHH	56.01	21963094
175	Acetylation	VLLLKKLKAWNDIKK HHHHHHHHHHHHHHH	61.30	26051181
175	Ubiquitination	VLLLKKLKAWNDIKK HHHHHHHHHHHHHHH	61.30	21963094
181	2-Hydroxyisobutyrylation	LKAWNDIKKVYASQR HHHHHHHHHHHHHHH	38.76	-
181	Acetylation	LKAWNDIKKVYASQR HHHHHHHHHHHHHHH	38.76	26051181
181	Succinylation	LKAWNDIKKVYASQR HHHHHHHHHHHHHHH	38.76	23954790
181	Ubiquitination	LKAWNDIKKVYASQR HHHHHHHHHHHHHHH	38.76	21963094
182	2-Hydroxyisobutyrylation	KAWNDIKKVYASQRM HHHHHHHHHHHHHHH	40.59	-
182	Ubiquitination	KAWNDIKKVYASQRM HHHHHHHHHHHHHHH	40.59	21963094
184	Nitration	WNDIKKVYASQRMRA HHHHHHHHHHHHHHC	14.93	-
184	Phosphorylation	WNDIKKVYASQRMRA HHHHHHHHHHHHHHC	14.93	-
186	Phosphorylation	DIKKVYASQRMRAGK HHHHHHHHHHHHCCC	10.71	-
188	Methylation	KKVYASQRMRAGKGK HHHHHHHHHHCCCCH	17.66	115492197
205	Methylation	NRRRIQRRGPCIIYN CCHHHHHHCCEEEEE	36.71	115492187
208	S-nitrosocysteine	RIQRRGPCIIYNEDN HHHHHCCEEEEECCC	3.09	-
208	Glutathionylation	RIQRRGPCIIYNEDN HHHHHCCEEEEECCC	3.09	22555962
208	S-nitrosylation	RIQRRGPCIIYNEDN HHHHHCCEEEEECCC	3.09	22178444
211	Phosphorylation	RRGPCIIYNEDNGII HHCCEEEEECCCCHH	7.81	30266825
219	2-Hydroxyisobutyrylation	NEDNGIIKAFRNIPG ECCCCHHHHHHCCCC	39.28	-
219	Acetylation	NEDNGIIKAFRNIPG ECCCCHHHHHHCCCC	39.28	26051181
219	Ubiquitination	NEDNGIIKAFRNIPG ECCCCHHHHHHCCCC	39.28	23000965
228	Phosphorylation	FRNIPGITLLNVSKL HHCCCCEEEEEHHHC	30.98	21712546
233	Phosphorylation	GITLLNVSKLNILKL CEEEEEHHHCCEEEC	30.28	28450419
234	Acetylation	ITLLNVSKLNILKLA EEEEEHHHCCEEECC	41.07	26051181
234	Ubiquitination	ITLLNVSKLNILKLA EEEEEHHHCCEEECC	41.07	23000965
239	2-Hydroxyisobutyrylation	VSKLNILKLAPGGHV HHHCCEEECCCCCCH	38.51	-
239	Acetylation	VSKLNILKLAPGGHV HHHCCEEECCCCCCH	38.51	25953088
239	Sumoylation	VSKLNILKLAPGGHV HHHCCEEECCCCCCH	38.51	28112733
239	Ubiquitination	VSKLNILKLAPGGHV HHHCCEEECCCCCCH	38.51	23000965
250	S-nitrosocysteine	GGHVGRFCIWTESAF CCCHHHEEEECHHHH	2.15	-
250	Glutathionylation	GGHVGRFCIWTESAF CCCHHHEEEECHHHH	2.15	22555962
250	S-nitrosylation	GGHVGRFCIWTESAF CCCHHHEEEECHHHH	2.15	22178444
250	S-palmitoylation	GGHVGRFCIWTESAF CCCHHHEEEECHHHH	2.15	29575903
253	Phosphorylation	VGRFCIWTESAFRKL HHHEEEECHHHHHHH	10.51	20068231
255	Phosphorylation	RFCIWTESAFRKLDE HEEEECHHHHHHHHH	25.90	20068231
259	2-Hydroxyisobutyrylation	WTESAFRKLDELYGT ECHHHHHHHHHHHHH	54.56	-
259	Acetylation	WTESAFRKLDELYGT ECHHHHHHHHHHHHH	54.56	26051181
259	Succinylation	WTESAFRKLDELYGT ECHHHHHHHHHHHHH	54.56	23954790
259	Ubiquitination	WTESAFRKLDELYGT ECHHHHHHHHHHHHH	54.56	23000965
264	Phosphorylation	FRKLDELYGTWRKAA HHHHHHHHHHHHHHH	15.51	27273156
266	Phosphorylation	KLDELYGTWRKAASL HHHHHHHHHHHHHHC	14.45	23403867
269	Ubiquitination	ELYGTWRKAASLKSN HHHHHHHHHHHCCCC	39.61	23000965
272	Phosphorylation	GTWRKAASLKSNYNL HHHHHHHHCCCCCCC	40.98	29214152
274	2-Hydroxyisobutyrylation	WRKAASLKSNYNLPM HHHHHHCCCCCCCCH	33.87	-
274	Acetylation	WRKAASLKSNYNLPM HHHHHHCCCCCCCCH	33.87	25825284
274	Methylation	WRKAASLKSNYNLPM HHHHHHCCCCCCCCH	33.87	30793583
274	Ubiquitination	WRKAASLKSNYNLPM HHHHHHCCCCCCCCH	33.87	23000965
275	Phosphorylation	RKAASLKSNYNLPMH HHHHHCCCCCCCCHH	50.25	28152594
277	Nitration	AASLKSNYNLPMHKM HHHCCCCCCCCHHHH	25.76	-
277	Phosphorylation	AASLKSNYNLPMHKM HHHCCCCCCCCHHHH	25.76	28152594
281	Sulfoxidation	KSNYNLPMHKMINTD CCCCCCCHHHHHCCC	5.52	30846556
283	2-Hydroxyisobutyrylation	NYNLPMHKMINTDLS CCCCCHHHHHCCCHH	34.91	-
283	Acetylation	NYNLPMHKMINTDLS CCCCCHHHHHCCCHH	34.91	26051181
283	Methylation	NYNLPMHKMINTDLS CCCCCHHHHHCCCHH	34.91	30793589
283	Ubiquitination	NYNLPMHKMINTDLS CCCCCHHHHHCCCHH	34.91	23000965
284	Sulfoxidation	YNLPMHKMINTDLSR CCCCHHHHHCCCHHH	1.41	21406390
287	Phosphorylation	PMHKMINTDLSRILK CHHHHHCCCHHHHHC	27.65	20860994
290	Phosphorylation	KMINTDLSRILKSPE HHHCCCHHHHHCCHH	21.78	27050516
294	2-Hydroxyisobutyrylation	TDLSRILKSPEIQRA CCHHHHHCCHHHHHH	62.69	-
294	Acetylation	TDLSRILKSPEIQRA CCHHHHHCCHHHHHH	62.69	26051181
294	Malonylation	TDLSRILKSPEIQRA CCHHHHHCCHHHHHH	62.69	30639696
294	Ubiquitination	TDLSRILKSPEIQRA CCHHHHHCCHHHHHH	62.69	23000965
295	Phosphorylation	DLSRILKSPEIQRAL CHHHHHCCHHHHHHH	25.07	29255136
300	Citrullination	LKSPEIQRALRAPRK HCCHHHHHHHHCCHH	41.05	-
300	Citrullination	LKSPEIQRALRAPRK HCCHHHHHHHHCCHH	41.05	-
315	Ubiquitination	KIHRRVLKKNPLKNL HHHHHHHHHCCCCCH	47.88	22817900
316	Ubiquitination	IHRRVLKKNPLKNLR HHHHHHHHCCCCCHH	60.69	21963094
320	2-Hydroxyisobutyrylation	VLKKNPLKNLRIMLK HHHHCCCCCHHHHHH	56.01	-
320	Ubiquitination	VLKKNPLKNLRIMLK HHHHCCCCCHHHHHH	56.01	27667366
327	2-Hydroxyisobutyrylation	KNLRIMLKLNPYAKT CCHHHHHHHCHHHHH	28.92	-
327	Acetylation	KNLRIMLKLNPYAKT CCHHHHHHHCHHHHH	28.92	25953088
327	Sumoylation	KNLRIMLKLNPYAKT CCHHHHHHHCHHHHH	28.92	28112733
327	Ubiquitination	KNLRIMLKLNPYAKT CCHHHHHHHCHHHHH	28.92	23000965
331	Phosphorylation	IMLKLNPYAKTMRRN HHHHHCHHHHHHHHH	21.47	20068231
333	2-Hydroxyisobutyrylation	LKLNPYAKTMRRNTI HHHCHHHHHHHHHHH	36.69	-
333	Acetylation	LKLNPYAKTMRRNTI HHHCHHHHHHHHHHH	36.69	19608861
333	Ubiquitination	LKLNPYAKTMRRNTI HHHCHHHHHHHHHHH	36.69	23000965
334	Phosphorylation	KLNPYAKTMRRNTIL HHCHHHHHHHHHHHH	14.03	20068231
339	Phosphorylation	AKTMRRNTILRQARN HHHHHHHHHHHHHHH	21.41	25884760
348	Ubiquitination	LRQARNHKLRVDKAA HHHHHHCCCCHHHHH	41.35	23000965
353	2-Hydroxyisobutyrylation	NHKLRVDKAAAAAAA HCCCCHHHHHHHHHH	36.75	-
353	Acetylation	NHKLRVDKAAAAAAA HCCCCHHHHHHHHHH	36.75	25953088
353	Ubiquitination	NHKLRVDKAAAAAAA HCCCCHHHHHHHHHH	36.75	23000965
364	2-Hydroxyisobutyrylation	AAAALQAKSDEKAAV HHHHHHHCCHHHHHH	45.54	-
364	Acetylation	AAAALQAKSDEKAAV HHHHHHHCCHHHHHH	45.54	23236377
364	Malonylation	AAAALQAKSDEKAAV HHHHHHHCCHHHHHH	45.54	26320211
364	Sumoylation	AAAALQAKSDEKAAV HHHHHHHCCHHHHHH	45.54	25114211
364	Ubiquitination	AAAALQAKSDEKAAV HHHHHHHCCHHHHHH	45.54	23000965
365	Phosphorylation	AAALQAKSDEKAAVA HHHHHHCCHHHHHHC	54.76	25159151
368	2-Hydroxyisobutyrylation	LQAKSDEKAAVAGKK HHHCCHHHHHHCCCC	46.79	-
368	Acetylation	LQAKSDEKAAVAGKK HHHCCHHHHHHCCCC	46.79	23749302
368	Ubiquitination	LQAKSDEKAAVAGKK HHHCCHHHHHHCCCC	46.79	23000965
374	Acetylation	EKAAVAGKKPVVGKK HHHHHCCCCCCCCCC	44.13	25953088
374	Ubiquitination	EKAAVAGKKPVVGKK HHHHHCCCCCCCCCC	44.13	21963094
375	Ubiquitination	KAAVAGKKPVVGKKG HHHHCCCCCCCCCCC	41.97	22817900
380	2-Hydroxyisobutyrylation	GKKPVVGKKGKKAAV CCCCCCCCCCCCCCC	46.90	-
380	Ubiquitination	GKKPVVGKKGKKAAV CCCCCCCCCCCCCCC	46.90	25015289
384	2-Hydroxyisobutyrylation	VVGKKGKKAAVGVKK CCCCCCCCCCCCCCC	50.69	-
384	Ubiquitination	VVGKKGKKAAVGVKK CCCCCCCCCCCCCCC	50.69	33845483
390	Ubiquitination	KKAAVGVKKQKKPLV CCCCCCCCCCCCCCC	43.49	33845483
394	Ubiquitination	VGVKKQKKPLVGKKA CCCCCCCCCCCCCCC	40.88	27667366
399	2-Hydroxyisobutyrylation	QKKPLVGKKAAATKK CCCCCCCCCCCCCCC	31.59	-
399	Acetylation	QKKPLVGKKAAATKK CCCCCCCCCCCCCCC	31.59	25953088
400	Acetylation	KKPLVGKKAAATKKP CCCCCCCCCCCCCCC	37.01	26051181
405	Acetylation	GKKAAATKKPAPEKK CCCCCCCCCCCCCCC	52.62	26051181
405	Ubiquitination	GKKAAATKKPAPEKK CCCCCCCCCCCCCCC	52.62	29967540
411	2-Hydroxyisobutyrylation	TKKPAPEKKPAEKKP CCCCCCCCCCCCCCC	64.10	-
411	Acetylation	TKKPAPEKKPAEKKP CCCCCCCCCCCCCCC	64.10	26210075
411	Ubiquitination	TKKPAPEKKPAEKKP CCCCCCCCCCCCCCC	64.10	29967540
412	Acetylation	KKPAPEKKPAEKKPT CCCCCCCCCCCCCCC	48.04	90309
412	Ubiquitination	KKPAPEKKPAEKKPT CCCCCCCCCCCCCCC	48.04	29967540
416	Ubiquitination	PEKKPAEKKPTTEEK CCCCCCCCCCCCCCC	67.18	29967540
419	Phosphorylation	KPAEKKPTTEEKKPA CCCCCCCCCCCCCCC	56.57	20068231
420	Phosphorylation	PAEKKPTTEEKKPAA CCCCCCCCCCCCCCC	51.15	20068231
423	2-Hydroxyisobutyrylation	KKPTTEEKKPAA--- CCCCCCCCCCCC---	58.80	-

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 RL4_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of RL4_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 RL4_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
MYB_HUMAN	MYB	physical	20604807
RL6_HUMAN	RPL6	physical	22939629
RL8_HUMAN	RPL8	physical	22939629
RS11_HUMAN	RPS11	physical	22939629
RS13_HUMAN	RPS13	physical	22939629
RS3_HUMAN	RPS3	physical	22939629
RL7_HUMAN	RPL7	physical	22939629
RS3A_HUMAN	RPS3A	physical	22939629
RL7A_HUMAN	RPL7A	physical	22939629
RLA0_HUMAN	RPLP0	physical	22939629
RS9_HUMAN	RPS9	physical	22939629
RL5_HUMAN	RPL5	physical	22939629
RL9_HUMAN	RPL9	physical	22939629
RS14_HUMAN	RPS14	physical	22939629
RS15A_HUMAN	RPS15A	physical	22939629
RS16_HUMAN	RPS16	physical	22939629
RS20_HUMAN	RPS20	physical	22939629
RS26_HUMAN	RPS26	physical	22939629
RS2_HUMAN	RPS2	physical	22939629
RS6_HUMAN	RPS6	physical	22939629
RS8_HUMAN	RPS8	physical	22939629
RSSA_HUMAN	RPSA	physical	22939629
RS23_HUMAN	RPS23	physical	22939629
RS5_HUMAN	RPS5	physical	22939629
RS4X_HUMAN	RPS4X	physical	22939629
RLA1_HUMAN	RPLP1	physical	22939629
RS24_HUMAN	RPS24	physical	22939629
RS7_HUMAN	RPS7	physical	22939629
RS17_HUMAN	RPS17	physical	22939629
RS25_HUMAN	RPS25	physical	22939629
RS19_HUMAN	RPS19	physical	22939629
RS28_HUMAN	RPS28	physical	22939629
RS12_HUMAN	RPS12	physical	22939629
RS27A_HUMAN	RPS27A	physical	22939629
RS21_HUMAN	RPS21	physical	22939629
RS27L_HUMAN	RPS27L	physical	22939629
SND1_HUMAN	SND1	physical	22939629
TEBP_HUMAN	PTGES3	physical	22939629
TBA1C_HUMAN	TUBA1C	physical	22939629
SYTC_HUMAN	TARS	physical	22939629
SRBS1_HUMAN	SORBS1	physical	21988832
HD_HUMAN	HTT	physical	23275563
IF6_HUMAN	EIF6	physical	26344197
SPB1_HUMAN	FTSJ3	physical	26344197
NOG1_HUMAN	GTPBP4	physical	26344197
NIP7_HUMAN	NIP7	physical	26344197
PESC_HUMAN	PES1	physical	26344197
RNPS1_HUMAN	RNPS1	physical	26344197
RL10A_HUMAN	RPL10A	physical	26344197
RL11_HUMAN	RPL11	physical	26344197
RL12_HUMAN	RPL12	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
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
RL3_HUMAN	RPL3	physical	26344197
RL30_HUMAN	RPL30	physical	26344197
RL35A_HUMAN	RPL35A	physical	26344197
RL37A_HUMAN	RPL37A	physical	26344197
RL3L_HUMAN	RPL3L	physical	26344197
RL7_HUMAN	RPL7	physical	26344197
RL7A_HUMAN	RPL7A	physical	26344197
RL8_HUMAN	RPL8	physical	26344197
RL9_HUMAN	RPL9	physical	26344197
RLA2_HUMAN	RPLP2	physical	26344197
RS11_HUMAN	RPS11	physical	26344197
RS14_HUMAN	RPS14	physical	26344197
RS15_HUMAN	RPS15	physical	26344197
RS15A_HUMAN	RPS15A	physical	26344197
RS16_HUMAN	RPS16	physical	26344197
RS18_HUMAN	RPS18	physical	26344197
RS19_HUMAN	RPS19	physical	26344197
RS2_HUMAN	RPS2	physical	26344197
RS23_HUMAN	RPS23	physical	26344197
RS25_HUMAN	RPS25	physical	26344197
RS26_HUMAN	RPS26	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
RS8_HUMAN	RPS8	physical	26344197
MDM2_HUMAN	MDM2	physical	26908445
P53_HUMAN	TP53	physical	26908445
RL5_HUMAN	RPL5	physical	26908445
RL11_HUMAN	RPL11	physical	26908445

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 RL4_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, AND MASS SPECTROMETRY.	19413330 [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-14; LYS-106 AND LYS-333, ANDMASS 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-295, 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-295 AND SER-365, ANDMASS SPECTROMETRY.	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-295 AND SER-365, ANDMASS SPECTROMETRY.	18691976 [Abstract]
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column."; Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.; Anal. Sci. 24:161-166(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-295, AND MASSSPECTROMETRY.	18187866 [Abstract]
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis."; Wang B., Malik R., Nigg E.A., Korner R.; Anal. Chem. 80:9526-9533(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-295 AND SER-365, ANDMASS SPECTROMETRY.	19007248 [Abstract]
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."; Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.; J. Proteome Res. 6:4150-4162(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-295, AND MASSSPECTROMETRY.	17924679 [Abstract]