dbPTM

NSUN2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	NSUN2_HUMAN
UniProt AC	Q08J23
Protein Name	tRNA (cytosine(34)-C(5))-methyltransferase
Gene Name	NSUN2
Organism	Homo sapiens (Human).
Sequence Length	767
Subcellular Localization	Nucleus, nucleolus. Cytoplasm, cytoskeleton, spindle. Concentrated in the nucleolus during interphase and translocates to the spindle during mitosis as an RNA-protein complex that includes 18S ribosomal RNA.
Protein Description	RNA methyltransferase that methylates tRNAs, and possibly RNA polymerase III transcripts. Methylates cytosine to 5-methylcytosine (m5C) at positions 34 and 48 of intron-containing tRNA(Leu)(CAA) precursors, and at positions 48, 49 and 50 of tRNA(Gly)(GCC) precursors. May act downstream of Myc to regulate epidermal cell growth and proliferation. Required for proper spindle assembly and chromosome segregation, independently of its methyltransferase activity..
Protein Sequence	MGRRSRGRRLQQQQRPEDAEDGAEGGGKRGEAGWEGGYPEIVKENKLFEHYYQELKIVPEGEWGQFMDALREPLPATLRITGYKSHAKEILHCLKNKYFKELEDLEVDGQKVEVPQPLSWYPEELAWHTNLSRKILRKSPHLEKFHQFLVSETESGNISRQEAVSMIPPLLLNVRPHHKILDMCAAPGSKTTQLIEMLHADMNVPFPEGFVIANDVDNKRCYLLVHQAKRLSSPCIMVVNHDASSIPRLQIDVDGRKEILFYDRILCDVPCSGDGTMRKNIDVWKKWTTLNSLQLHGLQLRIATRGAEQLAEGGRMVYSTCSLNPIEDEAVIASLLEKSEGALELADVSNELPGLKWMPGITQWKVMTKDGQWFTDWDAVPHSRHTQIRPTMFPPKDPEKLQAMHLERCLRILPHHQNTGGFFVAVLVKKSSMPWNKRQPKLQGKSAETRESTQLSPADLTEGKPTDPSKLESPSFTGTGDTEIAHATEDLENNGSKKDGVCGPPPSKKMKLFGFKEDPFVFIPEDDPLFPPIEKFYALDPSFPRMNLLTRTTEGKKRQLYMVSKELRNVLLNNSEKMKVINTGIKVWCRNNSGEEFDCAFRLAQEGIYTLYPFINSRIITVSMEDVKILLTQENPFFRKLSSETYSQAKDLAKGSIVLKYEPDSANPDALQCPIVLCGWRGKASIRTFVPKNERLHYLRMMGLEVLGEKKKEGVILTNESAASTGQPDNDVTEGQRAGEPNSPDAEEANSPDVTAGCDPAGVHPPR

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
21	Ubiquitination	QRPEDAEDGAEGGGK CCCCCCCCCCCCCCC	64.42	-
28	Acetylation	DGAEGGGKRGEAGWE CCCCCCCCCCCCCCC	61.58	26051181
28	Sumoylation	DGAEGGGKRGEAGWE CCCCCCCCCCCCCCC	61.58	-
28	Ubiquitination	DGAEGGGKRGEAGWE CCCCCCCCCCCCCCC	61.58	21906983
43	Ubiquitination	GGYPEIVKENKLFEH CCCHHHHHHCCCHHH	62.32	-
43	Sumoylation	GGYPEIVKENKLFEH CCCHHHHHHCCCHHH	62.32	-
43	Ubiquitination	GGYPEIVKENKLFEH CCCHHHHHHCCCHHH	62.32	23000965
46	Ubiquitination	PEIVKENKLFEHYYQ HHHHHHCCCHHHHHH	56.49	21890473
46	Ubiquitination	PEIVKENKLFEHYYQ HHHHHHCCCHHHHHH	56.49	21890473
46	Ubiquitination	PEIVKENKLFEHYYQ HHHHHHCCCHHHHHH	56.49	21890473
46	Sumoylation	PEIVKENKLFEHYYQ HHHHHHCCCHHHHHH	56.49	-
46	Acetylation	PEIVKENKLFEHYYQ HHHHHHCCCHHHHHH	56.49	25953088
46	Sumoylation	PEIVKENKLFEHYYQ HHHHHHCCCHHHHHH	56.49	28112733
46	Ubiquitination	PEIVKENKLFEHYYQ HHHHHHCCCHHHHHH	56.49	23000965
50	Ubiquitination	KENKLFEHYYQELKI HHCCCHHHHHHHCCC	21.18	-
51	Phosphorylation	ENKLFEHYYQELKIV HCCCHHHHHHHCCCC	10.31	28152594
52	Phosphorylation	NKLFEHYYQELKIVP CCCHHHHHHHCCCCC	9.45	28152594
77	Phosphorylation	LREPLPATLRITGYK HHCCCCCEEEEECCH	18.03	-
81	Phosphorylation	LPATLRITGYKSHAK CCCEEEEECCHHHHH	28.20	-
83	Phosphorylation	ATLRITGYKSHAKEI CEEEEECCHHHHHHH	10.73	-
84	Acetylation	TLRITGYKSHAKEIL EEEEECCHHHHHHHH	36.79	26210075
84	Ubiquitination	TLRITGYKSHAKEIL EEEEECCHHHHHHHH	36.79	29967540
85	Phosphorylation	LRITGYKSHAKEILH EEEECCHHHHHHHHH	21.86	-
88	Sumoylation	TGYKSHAKEILHCLK ECCHHHHHHHHHHHH	39.60	-
88	2-Hydroxyisobutyrylation	TGYKSHAKEILHCLK ECCHHHHHHHHHHHH	39.60	-
88	Sumoylation	TGYKSHAKEILHCLK ECCHHHHHHHHHHHH	39.60	-
88	Ubiquitination	TGYKSHAKEILHCLK ECCHHHHHHHHHHHH	39.60	29967540
93	S-nitrosocysteine	HAKEILHCLKNKYFK HHHHHHHHHHHHHHH	5.33	-
93	S-nitrosylation	HAKEILHCLKNKYFK HHHHHHHHHHHHHHH	5.33	19483679
94	Phosphorylation	AKEILHCLKNKYFKE HHHHHHHHHHHHHHH	4.82	24719451
95	2-Hydroxyisobutyrylation	KEILHCLKNKYFKEL HHHHHHHHHHHHHHH	57.71	-
95	Acetylation	KEILHCLKNKYFKEL HHHHHHHHHHHHHHH	57.71	25953088
95	Ubiquitination	KEILHCLKNKYFKEL HHHHHHHHHHHHHHH	57.71	21906983
97	Sumoylation	ILHCLKNKYFKELED HHHHHHHHHHHHHHH	50.94	-
97	Ubiquitination	ILHCLKNKYFKELED HHHHHHHHHHHHHHH	50.94	22817900
100	Sumoylation	CLKNKYFKELEDLEV HHHHHHHHHHHHCEE	59.30	-
100	Sumoylation	CLKNKYFKELEDLEV HHHHHHHHHHHHCEE	59.30	-
100	Ubiquitination	CLKNKYFKELEDLEV HHHHHHHHHHHHCEE	59.30	22817900
103	Ubiquitination	NKYFKELEDLEVDGQ HHHHHHHHHCEECCE	62.74	29967540
109	Ubiquitination	LEDLEVDGQKVEVPQ HHHCEECCEEEECCC	34.09	21890473
111	Sumoylation	DLEVDGQKVEVPQPL HCEECCEEEECCCCC	45.98	-
111	Sumoylation	DLEVDGQKVEVPQPL HCEECCEEEECCCCC	45.98	-
111	Ubiquitination	DLEVDGQKVEVPQPL HCEECCEEEECCCCC	45.98	21963094
120	Ubiquitination	EVPQPLSWYPEELAW ECCCCCCCCHHHHHH	22.00	-
129	Ubiquitination	PEELAWHTNLSRKIL HHHHHHCCHHHHHHH	27.44	-
129	Phosphorylation	PEELAWHTNLSRKIL HHHHHHCCHHHHHHH	27.44	24719451
133	Ubiquitination	AWHTNLSRKILRKSP HHCCHHHHHHHHHCH	32.95	-
138	Ubiquitination	LSRKILRKSPHLEKF HHHHHHHHCHHHHHH	65.96	29967540
139	Phosphorylation	SRKILRKSPHLEKFH HHHHHHHCHHHHHHH	15.89	29214152
144	Ubiquitination	RKSPHLEKFHQFLVS HHCHHHHHHHHHHHC	55.28	21890473
144	Ubiquitination	RKSPHLEKFHQFLVS HHCHHHHHHHHHHHC	55.28	21890473
144	Ubiquitination	RKSPHLEKFHQFLVS HHCHHHHHHHHHHHC	55.28	21890473
144	2-Hydroxyisobutyrylation	RKSPHLEKFHQFLVS HHCHHHHHHHHHHHC	55.28	-
144	Acetylation	RKSPHLEKFHQFLVS HHCHHHHHHHHHHHC	55.28	27452117
144	Ubiquitination	RKSPHLEKFHQFLVS HHCHHHHHHHHHHHC	55.28	22817900
151	Phosphorylation	KFHQFLVSETESGNI HHHHHHHCCCCCCCC	40.73	20873877
153	Phosphorylation	HQFLVSETESGNISR HHHHHCCCCCCCCCH	28.13	20873877
155	Phosphorylation	FLVSETESGNISRQE HHHCCCCCCCCCHHH	44.55	20873877
159	Phosphorylation	ETESGNISRQEAVSM CCCCCCCCHHHHHHC	31.73	20873877
165	Phosphorylation	ISRQEAVSMIPPLLL CCHHHHHHCCCCCHH	20.31	-
179	Ubiquitination	LNVRPHHKILDMCAA HCCCCCCCHHHCCCC	41.76	29967540
183	Sulfoxidation	PHHKILDMCAAPGSK CCCCHHHCCCCCCCH	1.18	21406390
184	Glutathionylation	HHKILDMCAAPGSKT CCCHHHCCCCCCCHH	2.66	22555962
189	Phosphorylation	DMCAAPGSKTTQLIE HCCCCCCCHHHHHHH	26.27	21712546
194	Ubiquitination	PGSKTTQLIEMLHAD CCCHHHHHHHHHHCC	3.17	29967540
197	Phosphorylation	KTTQLIEMLHADMNV HHHHHHHHHHCCCCC	2.35	24719451
201	Ubiquitination	LIEMLHADMNVPFPE HHHHHHCCCCCCCCC	20.59	-
222	Ubiquitination	DVDNKRCYLLVHQAK CCCCCEEEHHHHHHH	13.70	24816145
228	Acetylation	CYLLVHQAKRLSSPC EEHHHHHHHCCCCCE	5.53	-
229	Acetylation	YLLVHQAKRLSSPCI EHHHHHHHCCCCCEE	47.50	25953088
229	Ubiquitination	YLLVHQAKRLSSPCI EHHHHHHHCCCCCEE	47.50	29967540
232	Phosphorylation	VHQAKRLSSPCIMVV HHHHHCCCCCEEEEE	35.95	24719451
233	Phosphorylation	HQAKRLSSPCIMVVN HHHHCCCCCEEEEEC	28.51	30108239
244	Phosphorylation	MVVNHDASSIPRLQI EEECCCHHHCCCEEE	34.55	20068231
244	Ubiquitination	MVVNHDASSIPRLQI EEECCCHHHCCCEEE	34.55	29967540
245	Phosphorylation	VVNHDASSIPRLQID EECCCHHHCCCEEEC	38.03	20068231
250	Ubiquitination	ASSIPRLQIDVDGRK HHHCCCEEECCCCCE	30.99	22817900
251	Ubiquitination	SSIPRLQIDVDGRKE HHCCCEEECCCCCEE	7.07	21963094
256	Methylation	LQIDVDGRKEILFYD EEECCCCCEEEEEEE	29.04	115485655
257	Acetylation	QIDVDGRKEILFYDR EECCCCCEEEEEEEE	55.42	26822725
257	Ubiquitination	QIDVDGRKEILFYDR EECCCCCEEEEEEEE	55.42	24816145
273	Ubiquitination	LCDVPCSGDGTMRKN EEECCCCCCCHHHCC	44.05	-
275	Ubiquitination	DVPCSGDGTMRKNID ECCCCCCCHHHCCHH	25.57	-
277	Sulfoxidation	PCSGDGTMRKNIDVW CCCCCCHHHCCHHHH	7.60	21406390
279	Sumoylation	SGDGTMRKNIDVWKK CCCCHHHCCHHHHHH	47.64	-
279	Malonylation	SGDGTMRKNIDVWKK CCCCHHHCCHHHHHH	47.64	26320211
279	Sumoylation	SGDGTMRKNIDVWKK CCCCHHHCCHHHHHH	47.64	-
279	Ubiquitination	SGDGTMRKNIDVWKK CCCCHHHCCHHHHHH	47.64	29967540
285	Acetylation	RKNIDVWKKWTTLNS HCCHHHHHHHEECHH	37.98	25953088
285	Ubiquitination	RKNIDVWKKWTTLNS HCCHHHHHHHEECHH	37.98	22817900
286	Sumoylation	KNIDVWKKWTTLNSL CCHHHHHHHEECHHH	33.78	-
286	Sumoylation	KNIDVWKKWTTLNSL CCHHHHHHHEECHHH	33.78	-
286	Ubiquitination	KNIDVWKKWTTLNSL CCHHHHHHHEECHHH	33.78	21963094
321	Glutathionylation	GRMVYSTCSLNPIED CEEEEEECCCCCCCC	3.42	22555962
321	Ubiquitination	GRMVYSTCSLNPIED CEEEEEECCCCCCCC	3.42	21963094
329	Ubiquitination	SLNPIEDEAVIASLL CCCCCCCHHHHHHHH	31.85	-
330	Ubiquitination	LNPIEDEAVIASLLE CCCCCCHHHHHHHHH	15.44	21890473
334	Phosphorylation	EDEAVIASLLEKSEG CCHHHHHHHHHHCCC	23.51	24719451
334	Ubiquitination	EDEAVIASLLEKSEG CCHHHHHHHHHHCCC	23.51	21963094
339	Phosphorylation	IASLLEKSEGALELA HHHHHHHCCCCHHHH	31.71	21712546
341	Ubiquitination	SLLEKSEGALELADV HHHHHCCCCHHHHHH	42.42	-
343	Ubiquitination	LEKSEGALELADVSN HHHCCCCHHHHHHHC	9.01	-
349	Phosphorylation	ALELADVSNELPGLK CHHHHHHHCCCCCCC	25.74	21712546
350	Acetylation	LELADVSNELPGLKW HHHHHHHCCCCCCCC	55.46	-
350	Ubiquitination	LELADVSNELPGLKW HHHHHHHCCCCCCCC	55.46	-
356	Ubiquitination	SNELPGLKWMPGITQ HCCCCCCCCCCCCCE	47.57	21906983
361	Ubiquitination	GLKWMPGITQWKVMT CCCCCCCCCEEEEEE	1.82	29967540
365	Ubiquitination	MPGITQWKVMTKDGQ CCCCCEEEEEECCCC	16.59	21890473
365	Ubiquitination	MPGITQWKVMTKDGQ CCCCCEEEEEECCCC	16.59	21890473
365	Ubiquitination	MPGITQWKVMTKDGQ CCCCCEEEEEECCCC	16.59	21890473
365	Ubiquitination	MPGITQWKVMTKDGQ CCCCCEEEEEECCCC	16.59	22817900
369	Sumoylation	TQWKVMTKDGQWFTD CEEEEEECCCCEECC	41.59	-
369	Acetylation	TQWKVMTKDGQWFTD CEEEEEECCCCEECC	41.59	26051181
369	Sumoylation	TQWKVMTKDGQWFTD CEEEEEECCCCEECC	41.59	-
369	Ubiquitination	TQWKVMTKDGQWFTD CEEEEEECCCCEECC	41.59	21963094
383	Phosphorylation	DWDAVPHSRHTQIRP CCCCCCCCCCCCCCC	21.49	20873877
392	Ubiquitination	HTQIRPTMFPPKDPE CCCCCCCCCCCCCHH	5.42	-
396	Ubiquitination	RPTMFPPKDPEKLQA CCCCCCCCCHHHHHH	82.95	29967540
402	Ubiquitination	PKDPEKLQAMHLERC CCCHHHHHHHHHHHH	47.94	32015554
404	Ubiquitination	DPEKLQAMHLERCLR CHHHHHHHHHHHHHH	2.09	-
406	Ubiquitination	EKLQAMHLERCLRIL HHHHHHHHHHHHHHC	2.59	24816145
410	Ubiquitination	AMHLERCLRILPHHQ HHHHHHHHHHCCCCC	4.83	33845483
414	Ubiquitination	ERCLRILPHHQNTGG HHHHHHCCCCCCCCC	22.12	-
417	Phosphorylation	LRILPHHQNTGGFFV HHHCCCCCCCCCEEE	46.26	32142685
418	Ubiquitination	RILPHHQNTGGFFVA HHCCCCCCCCCEEEE	36.01	-
421	Phosphorylation	PHHQNTGGFFVAVLV CCCCCCCCEEEEEEE	15.69	24719451
424	Ubiquitination	QNTGGFFVAVLVKKS CCCCCEEEEEEEECC	3.17	-
429	Ubiquitination	FFVAVLVKKSSMPWN EEEEEEEECCCCCCC	42.66	29967540
437	Sumoylation	KSSMPWNKRQPKLQG CCCCCCCCCCCCCCC	48.84	-
437	Sumoylation	KSSMPWNKRQPKLQG CCCCCCCCCCCCCCC	48.84	-
437	Ubiquitination	KSSMPWNKRQPKLQG CCCCCCCCCCCCCCC	48.84	32015554
441	Ubiquitination	PWNKRQPKLQGKSAE CCCCCCCCCCCCCCC	45.14	24816145
445	Sumoylation	RQPKLQGKSAETRES CCCCCCCCCCCCCCC	33.27	-
445	Sumoylation	RQPKLQGKSAETRES CCCCCCCCCCCCCCC	33.27	-
445	Ubiquitination	RQPKLQGKSAETRES CCCCCCCCCCCCCCC	33.27	33845483
446	Phosphorylation	QPKLQGKSAETREST CCCCCCCCCCCCCCC	37.86	26074081
449	Phosphorylation	LQGKSAETRESTQLS CCCCCCCCCCCCCCC	39.18	29514088
452	Phosphorylation	KSAETRESTQLSPAD CCCCCCCCCCCCHHH	20.40	29255136
453	Phosphorylation	SAETRESTQLSPADL CCCCCCCCCCCHHHC	28.86	29255136
456	Ubiquitination	TRESTQLSPADLTEG CCCCCCCCHHHCCCC	14.28	-
456	Phosphorylation	TRESTQLSPADLTEG CCCCCCCCHHHCCCC	14.28	19664994
461	Phosphorylation	QLSPADLTEGKPTDP CCCHHHCCCCCCCCH	43.15	30278072
462	Ubiquitination	LSPADLTEGKPTDPS CCHHHCCCCCCCCHH	72.94	32015554
464	Sumoylation	PADLTEGKPTDPSKL HHHCCCCCCCCHHHC	38.21	-
464	Acetylation	PADLTEGKPTDPSKL HHHCCCCCCCCHHHC	38.21	23236377
464	Sumoylation	PADLTEGKPTDPSKL HHHCCCCCCCCHHHC	38.21	28112733
464	Ubiquitination	PADLTEGKPTDPSKL HHHCCCCCCCCHHHC	38.21	29967540
466	Phosphorylation	DLTEGKPTDPSKLES HCCCCCCCCHHHCCC	65.12	23927012
469	Phosphorylation	EGKPTDPSKLESPSF CCCCCCHHHCCCCCC	53.32	23927012
470	Sumoylation	GKPTDPSKLESPSFT CCCCCHHHCCCCCCC	62.76	28112733
473	Phosphorylation	TDPSKLESPSFTGTG CCHHHCCCCCCCCCC	35.96	29255136
473	Ubiquitination	TDPSKLESPSFTGTG CCHHHCCCCCCCCCC	35.96	22817900
474	Ubiquitination	DPSKLESPSFTGTGD CHHHCCCCCCCCCCC	24.88	22817900
475	Ubiquitination	PSKLESPSFTGTGDT HHHCCCCCCCCCCCC	44.73	-
475	Phosphorylation	PSKLESPSFTGTGDT HHHCCCCCCCCCCCC	44.73	29255136
476	Ubiquitination	SKLESPSFTGTGDTE HHCCCCCCCCCCCCH	9.19	-
476	Ubiquitination	SKLESPSFTGTGDTE HHCCCCCCCCCCCCH	9.19	21890473
477	Phosphorylation	KLESPSFTGTGDTEI HCCCCCCCCCCCCHH	37.87	29255136
479	Phosphorylation	ESPSFTGTGDTEIAH CCCCCCCCCCCHHHC	28.91	28464451
481	Ubiquitination	PSFTGTGDTEIAHAT CCCCCCCCCHHHCCH	40.79	22817900
482	Phosphorylation	SFTGTGDTEIAHATE CCCCCCCCHHHCCHH	30.54	28464451
488	Phosphorylation	DTEIAHATEDLENNG CCHHHCCHHHHHHCC	21.84	29632367
496	Phosphorylation	EDLENNGSKKDGVCG HHHHHCCCCCCCCCC	38.36	24144214
497	Acetylation	DLENNGSKKDGVCGP HHHHCCCCCCCCCCC	57.17	26051181
497	Ubiquitination	DLENNGSKKDGVCGP HHHHCCCCCCCCCCC	57.17	32015554
500	Ubiquitination	NNGSKKDGVCGPPPS HCCCCCCCCCCCCCC	26.04	29967540
508	Acetylation	VCGPPPSKKMKLFGF CCCCCCCCCCEECCC	63.76	25953088
508	Ubiquitination	VCGPPPSKKMKLFGF CCCCCCCCCCEECCC	63.76	22817900
509	Ubiquitination	CGPPPSKKMKLFGFK CCCCCCCCCEECCCC	45.68	22817900
511	Ubiquitination	PPPSKKMKLFGFKED CCCCCCCEECCCCCC	49.93	21890473
511	Ubiquitination	PPPSKKMKLFGFKED CCCCCCCEECCCCCC	49.93	21890473
511	Ubiquitination	PPPSKKMKLFGFKED CCCCCCCEECCCCCC	49.93	21890473
511	Sumoylation	PPPSKKMKLFGFKED CCCCCCCEECCCCCC	49.93	-
511	Sumoylation	PPPSKKMKLFGFKED CCCCCCCEECCCCCC	49.93	28112733
511	Ubiquitination	PPPSKKMKLFGFKED CCCCCCCEECCCCCC	49.93	22817900
516	Sumoylation	KMKLFGFKEDPFVFI CCEECCCCCCCEEEC	62.68	-
516	Sumoylation	KMKLFGFKEDPFVFI CCEECCCCCCCEEEC	62.68	28112733
516	Ubiquitination	KMKLFGFKEDPFVFI CCEECCCCCCCEEEC	62.68	22817900
535	Ubiquitination	PLFPPIEKFYALDPS CCCCCHHHHEECCCC	44.38	29967540
537	Phosphorylation	FPPIEKFYALDPSFP CCCHHHHEECCCCCC	19.81	28796482
542	Ubiquitination	KFYALDPSFPRMNLL HHEECCCCCCCCCCE	47.77	21963094
544	Ubiquitination	YALDPSFPRMNLLTR EECCCCCCCCCCEEE	38.66	22817900
550	Phosphorylation	FPRMNLLTRTTEGKK CCCCCCEEECCCCCH	29.18	27251275
552	Phosphorylation	RMNLLTRTTEGKKRQ CCCCEEECCCCCHHH	24.78	27251275
557	Sumoylation	TRTTEGKKRQLYMVS EECCCCCHHHHHHHC	57.12	-
557	Sumoylation	TRTTEGKKRQLYMVS EECCCCCHHHHHHHC	57.12	-
561	Phosphorylation	EGKKRQLYMVSKELR CCCHHHHHHHCHHHH	6.27	-
564	Phosphorylation	KRQLYMVSKELRNVL HHHHHHHCHHHHHHH	12.13	-
565	Ubiquitination	RQLYMVSKELRNVLL HHHHHHCHHHHHHHC	49.73	-
568	Methylation	YMVSKELRNVLLNNS HHHCHHHHHHHCCCH	32.10	115485647
575	Phosphorylation	RNVLLNNSEKMKVIN HHHHCCCHHHEEEEE	37.20	27067055
577	Sumoylation	VLLNNSEKMKVINTG HHCCCHHHEEEEECC	43.79	-
577	Acetylation	VLLNNSEKMKVINTG HHCCCHHHEEEEECC	43.79	25953088
577	Sumoylation	VLLNNSEKMKVINTG HHCCCHHHEEEEECC	43.79	-
577	Ubiquitination	VLLNNSEKMKVINTG HHCCCHHHEEEEECC	43.79	21906983
579	Sumoylation	LNNSEKMKVINTGIK CCCHHHEEEEECCCE	51.54	-
579	2-Hydroxyisobutyrylation	LNNSEKMKVINTGIK CCCHHHEEEEECCCE	51.54	-
579	Sumoylation	LNNSEKMKVINTGIK CCCHHHEEEEECCCE	51.54	-
579	Ubiquitination	LNNSEKMKVINTGIK CCCHHHEEEEECCCE	51.54	21906983
583	Phosphorylation	EKMKVINTGIKVWCR HHEEEEECCCEEEEE	29.20	20068231
586	N6-malonyllysine	KVINTGIKVWCRNNS EEEECCCEEEEECCC	30.90	-
586	Acetylation	KVINTGIKVWCRNNS EEEECCCEEEEECCC	30.90	23954790
586	Malonylation	KVINTGIKVWCRNNS EEEECCCEEEEECCC	30.90	26320211
586	Succinylation	KVINTGIKVWCRNNS EEEECCCEEEEECCC	30.90	27452117
586	Sumoylation	KVINTGIKVWCRNNS EEEECCCEEEEECCC	30.90	28112733
586	Ubiquitination	KVINTGIKVWCRNNS EEEECCCEEEEECCC	30.90	-
593	Phosphorylation	KVWCRNNSGEEFDCA EEEEECCCCCCCHHH	51.64	22167270
593	Ubiquitination	KVWCRNNSGEEFDCA EEEEECCCCCCCHHH	51.64	22817900
605	Ubiquitination	DCAFRLAQEGIYTLY HHHHHHHHCCHHHHH	54.78	27667366
609	Phosphorylation	RLAQEGIYTLYPFIN HHHHCCHHHHHHHHC	11.10	27259358
615	Ubiquitination	IYTLYPFINSRIITV HHHHHHHHCCEEEEE	3.85	23000965
617	Phosphorylation	TLYPFINSRIITVSM HHHHHHCCEEEEEEH	21.75	21712546
619	Ubiquitination	YPFINSRIITVSMED HHHHCCEEEEEEHHH	2.88	23000965
621	Phosphorylation	FINSRIITVSMEDVK HHCCEEEEEEHHHHE	12.26	-
623	Phosphorylation	NSRIITVSMEDVKIL CCEEEEEEHHHHEEE	14.06	21712546
624	Sulfoxidation	SRIITVSMEDVKILL CEEEEEEHHHHEEEE	4.42	21406390
625	Ubiquitination	RIITVSMEDVKILLT EEEEEEHHHHEEEEC	52.74	21963094
628	Ubiquitination	TVSMEDVKILLTQEN EEEHHHHEEEECCCC	39.70	22817900
640	Sumoylation	QENPFFRKLSSETYS CCCHHHHHHCCCCHH	47.79	-
640	Sumoylation	QENPFFRKLSSETYS CCCHHHHHHCCCCHH	47.79	25218447
640	Ubiquitination	QENPFFRKLSSETYS CCCHHHHHHCCCCHH	47.79	21906983
642	Phosphorylation	NPFFRKLSSETYSQA CHHHHHHCCCCHHHH	29.21	28796482
643	Phosphorylation	PFFRKLSSETYSQAK HHHHHHCCCCHHHHH	44.38	28796482
645	Phosphorylation	FRKLSSETYSQAKDL HHHHCCCCHHHHHHH	30.35	28796482
646	Nitration	RKLSSETYSQAKDLA HHHCCCCHHHHHHHH	8.50	-
646	Phosphorylation	RKLSSETYSQAKDLA HHHCCCCHHHHHHHH	8.50	28796482
647	Phosphorylation	KLSSETYSQAKDLAK HHCCCCHHHHHHHHC	30.95	28796482
650	Ubiquitination	SETYSQAKDLAKGSI CCCHHHHHHHHCCCE	45.71	21890473
650	Ubiquitination	SETYSQAKDLAKGSI CCCHHHHHHHHCCCE	45.71	21890473
650	Ubiquitination	SETYSQAKDLAKGSI CCCHHHHHHHHCCCE	45.71	21890473
650	Sumoylation	SETYSQAKDLAKGSI CCCHHHHHHHHCCCE	45.71	-
650	Acetylation	SETYSQAKDLAKGSI CCCHHHHHHHHCCCE	45.71	26051181
650	Sumoylation	SETYSQAKDLAKGSI CCCHHHHHHHHCCCE	45.71	-
650	Ubiquitination	SETYSQAKDLAKGSI CCCHHHHHHHHCCCE	45.71	23000965
654	Ubiquitination	SQAKDLAKGSIVLKY HHHHHHHCCCEEEEE	61.56	21890473
654	Ubiquitination	SQAKDLAKGSIVLKY HHHHHHHCCCEEEEE	61.56	21890473
654	Ubiquitination	SQAKDLAKGSIVLKY HHHHHHHCCCEEEEE	61.56	21890473
654	Sumoylation	SQAKDLAKGSIVLKY HHHHHHHCCCEEEEE	61.56	-
654	2-Hydroxyisobutyrylation	SQAKDLAKGSIVLKY HHHHHHHCCCEEEEE	61.56	-
654	Sumoylation	SQAKDLAKGSIVLKY HHHHHHHCCCEEEEE	61.56	28112733
654	Ubiquitination	SQAKDLAKGSIVLKY HHHHHHHCCCEEEEE	61.56	23000965
657	Ubiquitination	KDLAKGSIVLKYEPD HHHHCCCEEEEECCC	6.00	21890473
660	Sumoylation	AKGSIVLKYEPDSAN HCCCEEEEECCCCCC	36.35	-
660	Sumoylation	AKGSIVLKYEPDSAN HCCCEEEEECCCCCC	36.35	28112733
660	Ubiquitination	AKGSIVLKYEPDSAN HCCCEEEEECCCCCC	36.35	21963094
665	Phosphorylation	VLKYEPDSANPDALQ EEEECCCCCCCCHHC	40.43	21601212
675	Ubiquitination	PDALQCPIVLCGWRG CCHHCCCEEEECCCC	4.93	22817900
676	Ubiquitination	DALQCPIVLCGWRGK CHHCCCEEEECCCCC	1.87	21963094
677	Ubiquitination	ALQCPIVLCGWRGKA HHCCCEEEECCCCCE	2.01	21963094
690	Phosphorylation	KASIRTFVPKNERLH CEEEEEECCCCHHHH	6.97	24719451
692	Ubiquitination	SIRTFVPKNERLHYL EEEEECCCCHHHHHH	67.16	21890473
692	Ubiquitination	SIRTFVPKNERLHYL EEEEECCCCHHHHHH	67.16	21890473
692	Ubiquitination	SIRTFVPKNERLHYL EEEEECCCCHHHHHH	67.16	21890473
692	Sumoylation	SIRTFVPKNERLHYL EEEEECCCCHHHHHH	67.16	-
692	Sumoylation	SIRTFVPKNERLHYL EEEEECCCCHHHHHH	67.16	-
692	Ubiquitination	SIRTFVPKNERLHYL EEEEECCCCHHHHHH	67.16	22817900
701	Sulfoxidation	ERLHYLRMMGLEVLG HHHHHHHHCCCEECC	2.00	28183972
702	Sulfoxidation	RLHYLRMMGLEVLGE HHHHHHHCCCEECCC	4.47	28183972
708	Phosphorylation	MMGLEVLGEKKKEGV HCCCEECCCCCCCEE	50.26	24719451
710	2-Hydroxyisobutyrylation	GLEVLGEKKKEGVIL CCEECCCCCCCEEEE	68.31	-
710	Ubiquitination	GLEVLGEKKKEGVIL CCEECCCCCCCEEEE	68.31	22817900
711	Ubiquitination	LEVLGEKKKEGVILT CEECCCCCCCEEEEE	52.32	21963094
712	Ubiquitination	EVLGEKKKEGVILTN EECCCCCCCEEEEEC	71.42	21963094
716	Phosphorylation	EKKKEGVILTNESAA CCCCCEEEEECCCHH	6.04	24719451
718	Phosphorylation	KKEGVILTNESAAST CCCEEEEECCCHHCC	26.30	20873877
721	Phosphorylation	GVILTNESAASTGQP EEEEECCCHHCCCCC	31.07	20873877
724	Phosphorylation	LTNESAASTGQPDND EECCCHHCCCCCCCC	32.55	25159151
725	Phosphorylation	TNESAASTGQPDNDV ECCCHHCCCCCCCCC	34.80	26657352
733	Phosphorylation	GQPDNDVTEGQRAGE CCCCCCCCCCCCCCC	36.94	20873877
743	Phosphorylation	QRAGEPNSPDAEEAN CCCCCCCCCCHHHHC	34.57	19664994
751	Phosphorylation	PDAEEANSPDVTAGC CCHHHHCCCCCCCCC	29.53	19664994
755	Phosphorylation	EANSPDVTAGCDPAG HHCCCCCCCCCCCCC	25.39	23927012

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
139	S	Phosphorylation	Kinase	AURB	Q96GD4	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
139	S	Phosphorylation		17215513
Phosphorylated at Ser-139 by AURKB during mitosis, leading to abolish methyltransferase activity and the interaction with NPM1.

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 NSUN2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
NPM_HUMAN	NPM1	physical	17215513
NUCL_HUMAN	NCL	physical	17215513
RS27A_HUMAN	RPS27A	physical	22939629
PFD5_HUMAN	PFDN5	physical	22939629
UBA1_HUMAN	UBA1	physical	22939629
SYAC_HUMAN	AARS	physical	22939629
WDR74_HUMAN	WDR74	physical	22939629
FUBP1_HUMAN	FUBP1	physical	22863883
SYHC_HUMAN	HARS	physical	22863883
KBP_HUMAN	KIAA1279	physical	22863883
NRDC_HUMAN	NRD1	physical	22863883
PFD1_HUMAN	PFDN1	physical	22863883
RAGP1_HUMAN	RANGAP1	physical	22863883
RADI_HUMAN	RDX	physical	22863883
RFA1_HUMAN	RPA1	physical	22863883
SH3G1_HUMAN	SH3GL1	physical	22863883
THG1_HUMAN	THG1L	physical	22863883
UBXN7_HUMAN	UBXN7	physical	22863883
UGGG1_HUMAN	UGGT1	physical	22863883
KC1E_HUMAN	CSNK1E	physical	26344197
DDX49_HUMAN	DDX49	physical	26344197
PNO1_HUMAN	PNO1	physical	26344197
YES_HUMAN	YES1	physical	26344197
UBE3A_HUMAN	UBE3A	physical	28514442
MPP6_HUMAN	MPP6	physical	28514442
MTA70_HUMAN	METTL3	physical	28514442
ERCC3_HUMAN	ERCC3	physical	28514442
LIN7C_HUMAN	LIN7C	physical	28514442
TBA4A_HUMAN	TUBA4A	physical	28514442
LIN7A_HUMAN	LIN7A	physical	28514442
CNDP2_HUMAN	CNDP2	physical	28514442

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
611091	Mental retardation, autosomal recessive 5 (MRT5)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of NSUN2_HUMAN

Related Literatures of Post-Translational Modification

Malonylation
Reference	PubMed
"The first identification of lysine malonylation substrates and itsregulatory enzyme."; Peng C., Lu Z., Xie Z., Cheng Z., Chen Y., Tan M., Luo H., Zhang Y.,He W., Yang K., Zwaans B.M., Tishkoff D., Ho L., Lombard D., He T.C.,Dai J., Verdin E., Ye Y., Zhao Y.; Mol. Cell. Proteomics 10:M111.012658.01-M111.012658.12(2011). Cited for: MALONYLATION AT LYS-586.	21908771 [Abstract]
N6-malonyllysine
Reference	PubMed
"The first identification of lysine malonylation substrates and itsregulatory enzyme."; Peng C., Lu Z., Xie Z., Cheng Z., Chen Y., Tan M., Luo H., Zhang Y.,He W., Yang K., Zwaans B.M., Tishkoff D., Ho L., Lombard D., He T.C.,Dai J., Verdin E., Ye Y., Zhao Y.; Mol. Cell. Proteomics 10:M111.012658.01-M111.012658.12(2011). Cited for: MALONYLATION AT LYS-586.	21908771 [Abstract]
Phosphorylation
Reference	PubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-593; SER-743 ANDSER-751, AND MASS SPECTROMETRY.	19690332 [Abstract]
"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-456; SER-743 ANDSER-751, AND MASS SPECTROMETRY.	19413330 [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-456; SER-473; SER-593;SER-743 AND SER-751, AND MASS SPECTROMETRY.	18669648 [Abstract]
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis."; Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III; J. Proteome Res. 7:1346-1351(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-743 AND SER-751, ANDMASS SPECTROMETRY.	18220336 [Abstract]
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization."; Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; Nat. Biotechnol. 24:1285-1292(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-743 AND SER-751, ANDMASS SPECTROMETRY.	16964243 [Abstract]
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-456; SER-743 ANDSER-751, AND MASS SPECTROMETRY.	17081983 [Abstract]
"Aurora-B regulates RNA methyltransferase NSUN2."; Sakita-Suto S., Kanda A., Suzuki F., Sato S., Takata T., Tatsuka M.; Mol. Biol. Cell 18:1107-1117(2007). Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE,SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-139, INTERACTION WITHNPM1 AND NCL, AND MUTAGENESIS OF SER-139.	17215513 [Abstract]
"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 THR-461, AND MASSSPECTROMETRY.	17287340 [Abstract]

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