dbPTM

HNRPR_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	HNRPR_HUMAN
UniProt AC	O43390
Protein Name	Heterogeneous nuclear ribonucleoprotein R
Gene Name	HNRNPR
Organism	Homo sapiens (Human).
Sequence Length	633
Subcellular Localization	Nucleus . Microsome . Nucleus, nucleoplasm . Cytoplasm . Localized in cytoplasmic mRNP granules containing untranslated mRNAs. The tyrosine phosphorylated form bound to RNA is found in microsomes (By similarity).
Protein Description	Component of ribonucleosomes, which are complexes of at least 20 other different heterogenious nuclear ribonucleoproteins (hnRNP). hnRNP play an important role in processing of precursor mRNA in the nucleus..
Protein Sequence	MANQVNGNAVQLKEEEEPMDTSSVTHTEHYKTLIEAGLPQKVAERLDEIFQTGLVAYVDLDERAIDALREFNEEGALSVLQQFKESDLSHVQNKSAFLCGVMKTYRQREKQGSKVQESTKGPDEAKIKALLERTGYTLDVTTGQRKYGGPPPDSVYSGVQPGIGTEVFVGKIPRDLYEDELVPLFEKAGPIWDLRLMMDPLSGQNRGYAFITFCGKEAAQEAVKLCDSYEIRPGKHLGVCISVANNRLFVGSIPKNKTKENILEEFSKVTEGLVDVILYHQPDDKKKNRGFCFLEYEDHKSAAQARRRLMSGKVKVWGNVVTVEWADPVEEPDPEVMAKVKVLFVRNLATTVTEEILEKSFSEFGKLERVKKLKDYAFVHFEDRGAAVKAMDEMNGKEIEGEEIEIVLAKPPDKKRKERQAARQASRSTAYEDYYYHPPPRMPPPIRGRGRGGGRGGYGYPPDYYGYEDYYDDYYGYDYHDYRGGYEDPYYGYDDGYAVRGRGGGRGGRGAPPPPRGRGAPPPRGRAGYSQRGAPLGPPRGSRGGRGGPAQQQRGRGSRGSRGNRGGNVGGKRKADGYNQPDSKRRQTNNQQNWGSQPIAQQPLQQGGDYSGNYGYNNDNQEFYQDTYGQQWK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MANQVNGNA ------CCCCCCCCC	18.37	22223895
13	Sumoylation	NGNAVQLKEEEEPMD CCCCEECCCCCCCCC	46.09	-
13	Sumoylation	NGNAVQLKEEEEPMD CCCCEECCCCCCCCC	46.09	28112733
21	Phosphorylation	EEEEPMDTSSVTHTE CCCCCCCCCCCCHHH	19.36	23401153
22	Phosphorylation	EEEPMDTSSVTHTEH CCCCCCCCCCCHHHH	20.67	30266825
22 (in isoform 2)	Phosphorylation	-	20.67	27251275
23	Phosphorylation	EEPMDTSSVTHTEHY CCCCCCCCCCHHHHH	32.88	30266825
25	Phosphorylation	PMDTSSVTHTEHYKT CCCCCCCCHHHHHHH	25.65	30266825
27	Phosphorylation	DTSSVTHTEHYKTLI CCCCCCHHHHHHHHH	18.32	30266825
30	Phosphorylation	SVTHTEHYKTLIEAG CCCHHHHHHHHHHCC	10.23	20873877
31	Ubiquitination	VTHTEHYKTLIEAGL CCHHHHHHHHHHCCC	38.47	-
32	Phosphorylation	THTEHYKTLIEAGLP CHHHHHHHHHHCCCC	26.29	25159151
41	Acetylation	IEAGLPQKVAERLDE HHCCCCHHHHHHHHH	41.28	27452117
41	Ubiquitination	IEAGLPQKVAERLDE HHCCCCHHHHHHHHH	41.28	21890473
41 (in isoform 1)	Ubiquitination	-	41.28	21890473
41 (in isoform 2)	Ubiquitination	-	41.28	21890473
41	Ubiquitination	IEAGLPQKVAERLDE HHCCCCHHHHHHHHH	41.28	21890473
52	Phosphorylation	RLDEIFQTGLVAYVD HHHHHHHHCCEEEEE	23.02	28450419
57	Phosphorylation	FQTGLVAYVDLDERA HHHCCEEEEECCHHH	6.24	28450419
69	Methylation	ERAIDALREFNEEGA HHHHHHHHHHCHHHH	48.45	115479377
78	Phosphorylation	FNEEGALSVLQQFKE HCHHHHHHHHHHHHH	21.90	21712546
84	2-Hydroxyisobutyrylation	LSVLQQFKESDLSHV HHHHHHHHHHCCHHH	52.55	-
84	Acetylation	LSVLQQFKESDLSHV HHHHHHHHHHCCHHH	52.55	25825284
84	Ubiquitination	LSVLQQFKESDLSHV HHHHHHHHHHCCHHH	52.55	-
94	2-Hydroxyisobutyrylation	DLSHVQNKSAFLCGV CCHHHCCHHHHHHHH	26.52	-
94	Acetylation	DLSHVQNKSAFLCGV CCHHHCCHHHHHHHH	26.52	26051181
94	Ubiquitination	DLSHVQNKSAFLCGV CCHHHCCHHHHHHHH	26.52	-
95	Phosphorylation	LSHVQNKSAFLCGVM CHHHCCHHHHHHHHH	31.63	21712546
99	Glutathionylation	QNKSAFLCGVMKTYR CCHHHHHHHHHHHHH	2.89	22555962
103	2-Hydroxyisobutyrylation	AFLCGVMKTYRQREK HHHHHHHHHHHHHHH	39.74	-
103	Acetylation	AFLCGVMKTYRQREK HHHHHHHHHHHHHHH	39.74	23954790
103	Malonylation	AFLCGVMKTYRQREK HHHHHHHHHHHHHHH	39.74	26320211
103	Ubiquitination	AFLCGVMKTYRQREK HHHHHHHHHHHHHHH	39.74	-
113	Phosphorylation	RQREKQGSKVQESTK HHHHHHCCCCHHHCC	27.45	30108239
114	Acetylation	QREKQGSKVQESTKG HHHHHCCCCHHHCCC	55.55	26051181
114	Ubiquitination	QREKQGSKVQESTKG HHHHHCCCCHHHCCC	55.55	-
118	Phosphorylation	QGSKVQESTKGPDEA HCCCCHHHCCCCCHH	20.51	30108239
119	Phosphorylation	GSKVQESTKGPDEAK CCCCHHHCCCCCHHH	38.99	30108239
126	Trimethylation	TKGPDEAKIKALLER CCCCCHHHHHHHHHH	42.57	-
126	2-Hydroxyisobutyrylation	TKGPDEAKIKALLER CCCCCHHHHHHHHHH	42.57	-
126	Acetylation	TKGPDEAKIKALLER CCCCCHHHHHHHHHH	42.57	23749302
126	Methylation	TKGPDEAKIKALLER CCCCCHHHHHHHHHH	42.57	-
126	Ubiquitination	TKGPDEAKIKALLER CCCCCHHHHHHHHHH	42.57	-
128	Trimethylation	GPDEAKIKALLERTG CCCHHHHHHHHHHHC	32.07	-
128	Methylation	GPDEAKIKALLERTG CCCHHHHHHHHHHHC	32.07	-
134	Phosphorylation	IKALLERTGYTLDVT HHHHHHHHCCEEEEC	25.76	21406692
136	Phosphorylation	ALLERTGYTLDVTTG HHHHHHCCEEEECCC	11.97	21406692
137	Phosphorylation	LLERTGYTLDVTTGQ HHHHHCCEEEECCCC	20.16	21406692
141	Phosphorylation	TGYTLDVTTGQRKYG HCCEEEECCCCCCCC	25.52	21406692
142	Phosphorylation	GYTLDVTTGQRKYGG CCEEEECCCCCCCCC	31.03	21406692
146	Acetylation	DVTTGQRKYGGPPPD EECCCCCCCCCCCCC	40.12	26051181
146	Ubiquitination	DVTTGQRKYGGPPPD EECCCCCCCCCCCCC	40.12	-
147	Phosphorylation	VTTGQRKYGGPPPDS ECCCCCCCCCCCCCC	29.51	28152594
156	Phosphorylation	GPPPDSVYSGVQPGI CCCCCCHHCCCCCCC	12.03	-
171	Acetylation	GTEVFVGKIPRDLYE CCEEEEECCCCHHHC	44.21	25953088
171	Sumoylation	GTEVFVGKIPRDLYE CCEEEEECCCCHHHC	44.21	28112733
171	Ubiquitination	GTEVFVGKIPRDLYE CCEEEEECCCCHHHC	44.21	-
171 (in isoform 2)	Ubiquitination	-	44.21	-
177	Phosphorylation	GKIPRDLYEDELVPL ECCCCHHHCCCCHHH	26.14	21712546
187	Ubiquitination	ELVPLFEKAGPIWDL CCHHHHHHHCCCEEE	51.84	21906983
187 (in isoform 2)	Ubiquitination	-	51.84	-
195	Methylation	AGPIWDLRLMMDPLS HCCCEEEEEEECCCC	20.33	-
197	Sulfoxidation	PIWDLRLMMDPLSGQ CCEEEEEEECCCCCC	2.01	28465586
198	Sulfoxidation	IWDLRLMMDPLSGQN CEEEEEEECCCCCCC	5.93	28465586
208	Phosphorylation	LSGQNRGYAFITFCG CCCCCCCEEEEEECC	8.63	20090780
212	Phosphorylation	NRGYAFITFCGKEAA CCCEEEEEECCHHHH	13.35	29083192
214	S-palmitoylation	GYAFITFCGKEAAQE CEEEEEECCHHHHHH	5.95	29575903
216	Acetylation	AFITFCGKEAAQEAV EEEEECCHHHHHHHH	45.41	26051181
217	Ubiquitination	FITFCGKEAAQEAVK EEEECCHHHHHHHHH	34.22	21890473
224	2-Hydroxyisobutyrylation	EAAQEAVKLCDSYEI HHHHHHHHHHHCCCC	50.90	-
224	Acetylation	EAAQEAVKLCDSYEI HHHHHHHHHHHCCCC	50.90	25953088
224	Ubiquitination	EAAQEAVKLCDSYEI HHHHHHHHHHHCCCC	50.90	-
226	Glutathionylation	AQEAVKLCDSYEIRP HHHHHHHHHCCCCCC	2.43	22555962
228	Phosphorylation	EAVKLCDSYEIRPGK HHHHHHHCCCCCCCC	24.54	28152594
229	Phosphorylation	AVKLCDSYEIRPGKH HHHHHHCCCCCCCCC	11.34	20090780
235	Acetylation	SYEIRPGKHLGVCIS CCCCCCCCCEEEEEE	38.04	25953088
235	Methylation	SYEIRPGKHLGVCIS CCCCCCCCCEEEEEE	38.04	23644510
252	Phosphorylation	NNRLFVGSIPKNKTK CCEEEECCCCCCCCH	30.34	30266825
252 (in isoform 2)	Phosphorylation	-	30.34	24719451
255	Ubiquitination	LFVGSIPKNKTKENI EEECCCCCCCCHHHH	70.21	21890473
255 (in isoform 1)	Ubiquitination	-	70.21	21890473
255 (in isoform 2)	Ubiquitination	-	70.21	21890473
257	Ubiquitination	VGSIPKNKTKENILE ECCCCCCCCHHHHHH	68.08	-
258	O-linked_Glycosylation	GSIPKNKTKENILEE CCCCCCCCHHHHHHH	53.65	32119511
259	2-Hydroxyisobutyrylation	SIPKNKTKENILEEF CCCCCCCHHHHHHHH	50.83	-
259	Acetylation	SIPKNKTKENILEEF CCCCCCCHHHHHHHH	50.83	26051181
259	Methylation	SIPKNKTKENILEEF CCCCCCCHHHHHHHH	50.83	-
259	Ubiquitination	SIPKNKTKENILEEF CCCCCCCHHHHHHHH	50.83	-
279	Phosphorylation	GLVDVILYHQPDDKK HHHHEEEEECCCCCC	6.31	-
285	2-Hydroxyisobutyrylation	LYHQPDDKKKNRGFC EEECCCCCCCCCCEE	73.38	-
285	Acetylation	LYHQPDDKKKNRGFC EEECCCCCCCCCCEE	73.38	25953088
286	Acetylation	YHQPDDKKKNRGFCF EECCCCCCCCCCEEE	63.37	25953088
289	Methylation	PDDKKKNRGFCFLEY CCCCCCCCCEEEEEE	48.74	-
292	S-nitrosocysteine	KKKNRGFCFLEYEDH CCCCCCEEEEEECCH	4.19	-
292	Glutathionylation	KKKNRGFCFLEYEDH CCCCCCEEEEEECCH	4.19	22555962
292	S-nitrosylation	KKKNRGFCFLEYEDH CCCCCCEEEEEECCH	4.19	22178444
292	S-palmitoylation	KKKNRGFCFLEYEDH CCCCCCEEEEEECCH	4.19	29575903
296	Phosphorylation	RGFCFLEYEDHKSAA CCEEEEEECCHHHHH	28.89	28152594
300	2-Hydroxyisobutyrylation	FLEYEDHKSAAQARR EEEECCHHHHHHHHH	54.86	-
300	Acetylation	FLEYEDHKSAAQARR EEEECCHHHHHHHHH	54.86	23749302
300	Malonylation	FLEYEDHKSAAQARR EEEECCHHHHHHHHH	54.86	26320211
300	Ubiquitination	FLEYEDHKSAAQARR EEEECCHHHHHHHHH	54.86	-
303	Ubiquitination	YEDHKSAAQARRRLM ECCHHHHHHHHHHHH	15.62	21890473
311	Phosphorylation	QARRRLMSGKVKVWG HHHHHHHHCCCEEEC	39.80	24719451
313	2-Hydroxyisobutyrylation	RRRLMSGKVKVWGNV HHHHHHCCCEEECCE	31.41	-
313	Ubiquitination	RRRLMSGKVKVWGNV HHHHHHCCCEEECCE	31.41	-
314 (in isoform 2)	Phosphorylation	-	7.44	24719451
328	Ubiquitination	VTVEWADPVEEPDPE EEEEECCCCCCCCHH	27.89	21890473
341	2-Hydroxyisobutyrylation	PEVMAKVKVLFVRNL HHHHHHEEEEEECCC	32.30	-
341	Acetylation	PEVMAKVKVLFVRNL HHHHHHEEEEEECCC	32.30	25825284
341	Ubiquitination	PEVMAKVKVLFVRNL HHHHHHEEEEEECCC	32.30	21890473
341 (in isoform 1)	Ubiquitination	-	32.30	21890473
344 (in isoform 2)	Ubiquitination	-	5.63	21890473
350	Phosphorylation	LFVRNLATTVTEEIL EEECCCCHHCCHHHH	25.60	21712546
351	Phosphorylation	FVRNLATTVTEEILE EECCCCHHCCHHHHH	21.59	21712546
359	Sumoylation	VTEEILEKSFSEFGK CCHHHHHHHHHHCCC	54.04	28112733
359	Ubiquitination	VTEEILEKSFSEFGK CCHHHHHHHHHHCCC	54.04	21906983
360	Phosphorylation	TEEILEKSFSEFGKL CHHHHHHHHHHCCCH	25.32	21815630
362	Phosphorylation	EILEKSFSEFGKLER HHHHHHHHHCCCHHH	38.82	22199227
362 (in isoform 2)	Ubiquitination	-	38.82	-
363 (in isoform 2)	Phosphorylation	-	57.31	27251275
366	Sumoylation	KSFSEFGKLERVKKL HHHHHCCCHHHHHHH	53.12	-
366	Acetylation	KSFSEFGKLERVKKL HHHHHCCCHHHHHHH	53.12	19608861
366	Methylation	KSFSEFGKLERVKKL HHHHHCCCHHHHHHH	53.12	68337
366	Sumoylation	KSFSEFGKLERVKKL HHHHHCCCHHHHHHH	53.12	-
366	Ubiquitination	KSFSEFGKLERVKKL HHHHHCCCHHHHHHH	53.12	21890473
366 (in isoform 1)	Ubiquitination	-	53.12	21890473
369	Acetylation	SEFGKLERVKKLKDY HHCCCHHHHHHHCCE	56.86	19608861
369	Ubiquitination	SEFGKLERVKKLKDY HHCCCHHHHHHHCCE	56.86	19608861
369 (in isoform 2)	Ubiquitination	-	56.86	21890473
374	2-Hydroxyisobutyrylation	LERVKKLKDYAFVHF HHHHHHHCCEEEEEE	58.53	-
374	Acetylation	LERVKKLKDYAFVHF HHHHHHHCCEEEEEE	58.53	26051181
374	Ubiquitination	LERVKKLKDYAFVHF HHHHHHHCCEEEEEE	58.53	-
376	Phosphorylation	RVKKLKDYAFVHFED HHHHHCCEEEEEECC	10.60	28152594
379 (in isoform 2)	Phosphorylation	-	3.73	27642862
384	Methylation	AFVHFEDRGAAVKAM EEEEECCCCHHHHHH	29.47	115479383
389	2-Hydroxyisobutyrylation	EDRGAAVKAMDEMNG CCCCHHHHHHHHHCC	33.01	-
389	Acetylation	EDRGAAVKAMDEMNG CCCCHHHHHHHHHCC	33.01	19608861
389	Ubiquitination	EDRGAAVKAMDEMNG CCCCHHHHHHHHHCC	33.01	2190698
392	Acetylation	GAAVKAMDEMNGKEI CHHHHHHHHHCCEEE	57.78	19608861
392	Ubiquitination	GAAVKAMDEMNGKEI CHHHHHHHHHCCEEE	57.78	19608861
397	Acetylation	AMDEMNGKEIEGEEI HHHHHCCEEECCEEE	50.98	19608861
400	Acetylation	EMNGKEIEGEEIEIV HHCCEEECCEEEEEE	62.74	19608861
410	Ubiquitination	EIEIVLAKPPDKKRK EEEEEEECCCCHHHH	53.58	-
414	2-Hydroxyisobutyrylation	VLAKPPDKKRKERQA EEECCCCHHHHHHHH	61.32	-
426	Phosphorylation	RQAARQASRSTAYED HHHHHHHHHHHHHHH	20.58	28450419
428	Phosphorylation	AARQASRSTAYEDYY HHHHHHHHHHHHHCC	18.20	21945579
429	Phosphorylation	ARQASRSTAYEDYYY HHHHHHHHHHHHCCC	31.95	21945579
431	Phosphorylation	QASRSTAYEDYYYHP HHHHHHHHHHCCCCC	14.93	21945579
431 (in isoform 2)	Phosphorylation	-	14.93	24719451
434	Phosphorylation	RSTAYEDYYYHPPPR HHHHHHHCCCCCCCC	8.25	21945579
434 (in isoform 2)	Phosphorylation	-	8.25	27642862
435	Phosphorylation	STAYEDYYYHPPPRM HHHHHHCCCCCCCCC	13.97	21945579
436	Phosphorylation	TAYEDYYYHPPPRMP HHHHHCCCCCCCCCC	11.13	21945579
437 (in isoform 2)	Phosphorylation	-	16.57	27642862
438 (in isoform 2)	Phosphorylation	-	25.19	27642862
439 (in isoform 2)	Phosphorylation	-	18.80	27642862
441	Methylation	YYYHPPPRMPPPIRG CCCCCCCCCCCCCCC	56.89	58857897
483	Methylation	GYDYHDYRGGYEDPY CCCCCCCCCCCCCCC	37.81	-
491	Phosphorylation	GGYEDPYYGYDDGYA CCCCCCCCCCCCCCE	18.01	28152594
493	Phosphorylation	YEDPYYGYDDGYAVR CCCCCCCCCCCCEEC	8.50	28152594
497	Phosphorylation	YYGYDDGYAVRGRGG CCCCCCCCEECCCCC	14.66	28152594
500	Methylation	YDDGYAVRGRGGGRG CCCCCEECCCCCCCC	22.40	24383367
502	Methylation	DGYAVRGRGGGRGGR CCCEECCCCCCCCCC	29.98	24395437
506	Methylation	VRGRGGGRGGRGAPP ECCCCCCCCCCCCCC	47.90	115479389
509	Methylation	RGGGRGGRGAPPPPR CCCCCCCCCCCCCCC	40.71	115479395
529	Phosphorylation	PPRGRAGYSQRGAPL CCCCCCCCCCCCCCC	10.72	28152594
530	Phosphorylation	PRGRAGYSQRGAPLG CCCCCCCCCCCCCCC	16.69	28152594
532	Methylation	GRAGYSQRGAPLGPP CCCCCCCCCCCCCCC	36.98	24383375
542	Phosphorylation	PLGPPRGSRGGRGGP CCCCCCCCCCCCCCH	29.09	22468782
573	Methylation	GGNVGGKRKADGYNQ CCCCCCCCCCCCCCC	42.54	-
574	Ubiquitination	GNVGGKRKADGYNQP CCCCCCCCCCCCCCC	55.08	-
578	Phosphorylation	GKRKADGYNQPDSKR CCCCCCCCCCCCHHH	15.92	28102081
583	Phosphorylation	DGYNQPDSKRRQTNN CCCCCCCHHHCCCCC	34.44	21815630
584	Acetylation	GYNQPDSKRRQTNNQ CCCCCCHHHCCCCCC	60.01	25953088
584	Ubiquitination	GYNQPDSKRRQTNNQ CCCCCCHHHCCCCCC	60.01	-
586 (in isoform 2)	Phosphorylation	-	51.95	27251275
588	Phosphorylation	PDSKRRQTNNQQNWG CCHHHCCCCCCCCCC	34.03	26074081
596	Phosphorylation	NNQQNWGSQPIAQQP CCCCCCCCCCCCCCC	25.13	26074081
610	Phosphorylation	PLQQGGDYSGNYGYN CHHCCCCCCCCCCCC	23.04	28348404
611	Phosphorylation	LQQGGDYSGNYGYNN HHCCCCCCCCCCCCC	25.88	28348404
614	Phosphorylation	GGDYSGNYGYNNDNQ CCCCCCCCCCCCCCH	25.22	28348404
616	Phosphorylation	DYSGNYGYNNDNQEF CCCCCCCCCCCCHHH	10.63	28348404
624	Phosphorylation	NNDNQEFYQDTYGQQ CCCCHHHHHHCCCCC	12.53	28348404
627	Phosphorylation	NQEFYQDTYGQQWK- CHHHHHHCCCCCCC-	17.64	-
628	Phosphorylation	QEFYQDTYGQQWK-- HHHHHHCCCCCCC--	22.64	-

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 HNRPR_HUMAN !!

Functions of PTM Sites

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RL26_HUMAN	RPL26	physical	16169070
ANM1_HUMAN	PRMT1	physical	16169070
SMN_HUMAN	SMN1	physical	11574476
ROA1_HUMAN	HNRNPA1	physical	22939629
SRSF1_HUMAN	SRSF1	physical	22939629
U520_HUMAN	SNRNP200	physical	22939629
U5S1_HUMAN	EFTUD2	physical	22939629
SF3B3_HUMAN	SF3B3	physical	22939629
SF3B1_HUMAN	SF3B1	physical	22939629
SF3A1_HUMAN	SF3A1	physical	22939629
SF3A3_HUMAN	SF3A3	physical	22939629
SRSF5_HUMAN	SRSF5	physical	22939629
SFPQ_HUMAN	SFPQ	physical	22939629
U2AF2_HUMAN	U2AF2	physical	22939629
RU17_HUMAN	SNRNP70	physical	22939629
PABP1_HUMAN	PABPC1	physical	22939629
NPM_HUMAN	NPM1	physical	22939629
TADBP_HUMAN	TARDBP	physical	22939629
ROA0_HUMAN	HNRNPA0	physical	22939629
SNUT1_HUMAN	SART1	physical	22939629
RALY_HUMAN	RALY	physical	22939629
IF4A3_HUMAN	EIF4A3	physical	22939629
ILF3_HUMAN	ILF3	physical	22939629
ILF2_HUMAN	ILF2	physical	22939629
PR40A_HUMAN	PRPF40A	physical	22939629
KHDR1_HUMAN	KHDRBS1	physical	22939629
RM42_HUMAN	MRPL42	physical	22939629
TOP2B_HUMAN	TOP2B	physical	22939629
VTNC_HUMAN	VTN	physical	22939629
MYO1C_HUMAN	MYO1C	physical	22939629
RM04_HUMAN	MRPL4	physical	22939629
RM14_HUMAN	MRPL14	physical	22939629
MPV17_HUMAN	MPV17	physical	22939629
TF3C1_HUMAN	GTF3C1	physical	22939629
LMO7_HUMAN	LMO7	physical	22939629
RM23_HUMAN	MRPL23	physical	22939629
RS23_HUMAN	RPS23	physical	22939629
RAD50_HUMAN	RAD50	physical	22939629
NDUV1_HUMAN	NDUFV1	physical	22939629
MTX2_HUMAN	MTX2	physical	22939629
TIM10_HUMAN	TIMM10	physical	22939629
TOM22_HUMAN	TOMM22	physical	22939629
PRR3_HUMAN	PRR3	physical	22939629
NPL4_HUMAN	NPLOC4	physical	22939629
SPTN1_HUMAN	SPTAN1	physical	22939629
SPG7_HUMAN	SPG7	physical	22939629
LBR_HUMAN	LBR	physical	22939629
RT09_HUMAN	MRPS9	physical	22939629
MIRO2_HUMAN	RHOT2	physical	22939629
SND1_HUMAN	SND1	physical	22939629
SMCA5_HUMAN	SMARCA5	physical	22939629
K2013_HUMAN	KIAA2013	physical	22939629
RBM14_HUMAN	RBM14	physical	22939629
SLIRP_HUMAN	SLIRP	physical	22939629
RL31_HUMAN	RPL31	physical	22939629
PTSS2_HUMAN	PTDSS2	physical	22939629
MIC60_HUMAN	IMMT	physical	22939629
RT28_HUMAN	MRPS28	physical	22939629
RT16_HUMAN	MRPS16	physical	22939629
LGMN_HUMAN	LGMN	physical	22939629
RM40_HUMAN	MRPL40	physical	22939629
PEX3_HUMAN	PEX3	physical	22939629
NICA_HUMAN	NCSTN	physical	22939629
MBB1A_HUMAN	MYBBP1A	physical	22939629
RT21_HUMAN	MRPS21	physical	22939629
MOGS_HUMAN	MOGS	physical	22939629
T179B_HUMAN	TMEM179B	physical	22939629
K1C18_HUMAN	KRT18	physical	22939629
RT26_HUMAN	MRPS26	physical	22939629
IL7RA_HUMAN	IL7R	physical	23151878
BRCC3_HUMAN	BRCC3	physical	22863883
CD2AP_HUMAN	CD2AP	physical	22863883
EH1L1_HUMAN	EHBP1L1	physical	22863883
GAPD1_HUMAN	GAPVD1	physical	22863883
LARP7_HUMAN	LARP7	physical	22863883
MAP4_HUMAN	MAP4	physical	22863883
MTA2_HUMAN	MTA2	physical	22863883
RPB1_HUMAN	POLR2A	physical	22863883
PP4R1_HUMAN	PPP4R1	physical	22863883
RABE2_HUMAN	RABEP2	physical	22863883
WDHD1_HUMAN	WDHD1	physical	22863883
KHDR2_HUMAN	KHDRBS2	physical	25416956
DDX3X_HUMAN	DDX3X	physical	26344197
DDX5_HUMAN	DDX5	physical	26344197
MO4L1_HUMAN	MORF4L1	physical	26344197
MO4L2_HUMAN	MORF4L2	physical	26344197
NAA15_HUMAN	NAA15	physical	26344197
NH2L1_HUMAN	NHP2L1	physical	26344197
PRP8_HUMAN	PRPF8	physical	26344197
RL7_HUMAN	RPL7	physical	26344197
PAIRB_HUMAN	SERBP1	physical	26344197
SF3B3_HUMAN	SF3B3	physical	26344197
TRM6_HUMAN	TRMT6	physical	26344197
ZFR_HUMAN	ZFR	physical	28514442
RU17_HUMAN	SNRNP70	physical	28514442
RT05_HUMAN	MRPS5	physical	28514442
RT31_HUMAN	MRPS31	physical	28514442

Drug and Disease Associations

Kegg Disease
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of HNRPR_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-103; LYS-366; LYS-389 ANDLYS-397, AND MASS SPECTROMETRY.	19608861 [Abstract]