dbPTM

TOPRS_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	TOPRS_HUMAN
UniProt AC	Q9NS56
Protein Name	E3 ubiquitin-protein ligase Topors
Gene Name	TOPORS
Organism	Homo sapiens (Human).
Sequence Length	1045
Subcellular Localization	Nucleus. Nucleus, PML body. Localizes to discrete nuclear foci which partly overlap with PML nuclear bodies. Targeted to PML nuclear bodies upon DNA damage.
Protein Description	Functions as an E3 ubiquitin-protein ligase and as an E3 SUMO1-protein ligase. Probable tumor suppressor involved in cell growth, cell proliferation and apoptosis that regulates p53/TP53 stability through ubiquitin-dependent degradation. May regulate chromatin modification through sumoylation of several chromatin modification-associated proteins. May be involved in DNA damage-induced cell death through IKBKE sumoylation..
Protein Sequence	MGSQPPLGSPLSREEGEAPPPAPASEGRRRSRRVRLRGSCRHRPSFLGCRELAASAPARPAPASSEIMASAAKEFKMDNFSPKAGTSKLQQTVPADASPDSKCPICLDRFDNVSYLDRCLHKFCFRCVQEWSKNKAECPLCKQPFDSIFHSVRAEDDFKEYVLRPSYNGSFVTPDRRFRYRTTLTRERNASVYSPSGPVNRRTTTPPDSGVLFEGLGISTRPRDVEIPQFMRQIAVRRPTTADERSLRKIQEQDIINFRRTLYRAGARVRNIEDGGRYRDISAEFFRRNPACLHRLVPWLKRELTVLFGAHGSLVNIVQHIIMSNVTRYDLESQAFVSDLRPFLLNRTEHFIHEFISFARSPFNMAAFDQHANYDCPAPSYEEGSHSDSSVITISPDEAETQELDINVATVSQAPWDDETPGPSYSSSEQVHVTMSSLLNTSDSSDEELVTGGATSQIQGVQTNDDLNNDSDDSSDNCVIVGFVKPLAERTPELVELSSDSEDLGSYEKMETVKTQEQEQSYSSGDSDVSRCSSPHSVLGKDEQINKGHCDSSTRIKSKKEEKRSTSLSSPRNLNSSVRGDRVYSPYNHRHRKRGRSRSSDSRSQSRSGHDQKNHRKHHGKKRMKSKRSRSRESSRPRGRRDKKRSRTRDSSWSRRSQTLSLSSESTSRSRSRSSDHGKRRSRSRNRDRYYLRNNYGSRYKWEYTYYSRNKDRDGYESSYRRRTLSRAHYSRQSSSPEFRVQSFSERTNARKKNNHSERKYYYYERHRSRSLSSNRSRTASTGTDRVRNEKPGGKRKYKTRHLEGTNEVAQPSREFASKAKDSHYQKSSSKLDGNYKNESDTFSDSRSSDRETKHKRRKRKTRSLSVEIVYEGKATDTTKHHKKKKKKHKKKHKKHHGDNASRSPVVITIDSDSDKDSEVKEDTECDNSGPQDPLQNEFLAPSLEPFETKDVVTIEAEFGVLDKECDIATLSNNLNNANKTVDNIPPLAASVEQTLDVREESTFVSDLENQPSNIVSLQTEPSRQLPSPRTSLMSVCLGRDCDMS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
3	Phosphorylation	-----MGSQPPLGSP -----CCCCCCCCCC	51.91	22199227
8	Ubiquitination	MGSQPPLGSPLSREE CCCCCCCCCCCCCCC	32.75	23000965
9	Phosphorylation	GSQPPLGSPLSREEG CCCCCCCCCCCCCCC	30.28	29255136
11	Ubiquitination	QPPLGSPLSREEGEA CCCCCCCCCCCCCCC	8.91	23000965
12	Phosphorylation	PPLGSPLSREEGEAP CCCCCCCCCCCCCCC	40.82	29255136
16 (in isoform 2)	Phosphorylation	-	31.45	25056879
18	Ubiquitination	LSREEGEAPPPAPAS CCCCCCCCCCCCCCC	32.53	27667366
18 (in isoform 2)	Ubiquitination	-	32.53	21906983
23	Ubiquitination	GEAPPPAPASEGRRR CCCCCCCCCCCCCCC	41.93	21963094
23 (in isoform 2)	Ubiquitination	-	41.93	21906983
25	Phosphorylation	APPPAPASEGRRRSR CCCCCCCCCCCCCCC	39.25	28674419
28	Methylation	PAPASEGRRRSRRVR CCCCCCCCCCCCCEE	27.13	81120999
45	Phosphorylation	GSCRHRPSFLGCREL CCCCCCCCCCCHHHH	32.81	24247654
55	Phosphorylation	GCRELAASAPARPAP CHHHHHHCCCCCCCC	29.22	22210691
64	Phosphorylation	PARPAPASSEIMASA CCCCCCCCHHHHHHH	27.69	22210691
65	Phosphorylation	ARPAPASSEIMASAA CCCCCCCHHHHHHHH	32.99	22210691
70	Phosphorylation	ASSEIMASAAKEFKM CCHHHHHHHHHHHCC	16.04	22210691
73	Sumoylation	EIMASAAKEFKMDNF HHHHHHHHHHCCCCC	64.50	28112733
73	Ubiquitination	EIMASAAKEFKMDNF HHHHHHHHHHCCCCC	64.50	23000965
73 (in isoform 1)	Ubiquitination	-	64.50	21890473
76	Sumoylation	ASAAKEFKMDNFSPK HHHHHHHCCCCCCCC	46.57	-
76	Sumoylation	ASAAKEFKMDNFSPK HHHHHHHCCCCCCCC	46.57	28112733
76	Ubiquitination	ASAAKEFKMDNFSPK HHHHHHHCCCCCCCC	46.57	23000965
81	Phosphorylation	EFKMDNFSPKAGTSK HHCCCCCCCCCCCCC	31.57	21712546
83	Sumoylation	KMDNFSPKAGTSKLQ CCCCCCCCCCCCCCC	59.24	-
83	Sumoylation	KMDNFSPKAGTSKLQ CCCCCCCCCCCCCCC	59.24	28112733
83	Ubiquitination	KMDNFSPKAGTSKLQ CCCCCCCCCCCCCCC	59.24	27667366
83 (in isoform 1)	Ubiquitination	-	59.24	21890473
86	Phosphorylation	NFSPKAGTSKLQQTV CCCCCCCCCCCCEEC	27.78	30624053
88	Sumoylation	SPKAGTSKLQQTVPA CCCCCCCCCCEECCC	50.59	-
88	Sumoylation	SPKAGTSKLQQTVPA CCCCCCCCCCEECCC	50.59	28112733
88	Ubiquitination	SPKAGTSKLQQTVPA CCCCCCCCCCEECCC	50.59	21906983
88 (in isoform 1)	Ubiquitination	-	50.59	21890473
92	Phosphorylation	GTSKLQQTVPADASP CCCCCCEECCCCCCC	18.59	23403867
98	Phosphorylation	QTVPADASPDSKCPI EECCCCCCCCCCCCC	29.77	19664994
101	Phosphorylation	PADASPDSKCPICLD CCCCCCCCCCCCCCC	39.27	30266825
102	Ubiquitination	ADASPDSKCPICLDR CCCCCCCCCCCCCCC	51.95	-
114	Phosphorylation	LDRFDNVSYLDRCLH CCCCCCCHHHHHHHH	26.66	27542207
122	Ubiquitination	YLDRCLHKFCFRCVQ HHHHHHHHHHHHHHH	30.77	-
133	Ubiquitination	RCVQEWSKNKAECPL HHHHHHHCCCCCCCC	64.64	-
135	Ubiquitination	VQEWSKNKAECPLCK HHHHHCCCCCCCCCC	49.66	-
151	Phosphorylation	PFDSIFHSVRAEDDF CCHHHHHHHCCCCCH	11.53	23663014
159	Sumoylation	VRAEDDFKEYVLRPS HCCCCCHHHHCCCCC	55.95	28112733
161	Phosphorylation	AEDDFKEYVLRPSYN CCCCHHHHCCCCCCC	12.84	29083192
166	Phosphorylation	KEYVLRPSYNGSFVT HHHCCCCCCCCCCCC	25.46	29083192
167	Phosphorylation	EYVLRPSYNGSFVTP HHCCCCCCCCCCCCC	26.65	29083192
170	Phosphorylation	LRPSYNGSFVTPDRR CCCCCCCCCCCCCCC	16.95	29083192
173	Phosphorylation	SYNGSFVTPDRRFRY CCCCCCCCCCCCEEE	19.91	22617229
180	Phosphorylation	TPDRRFRYRTTLTRE CCCCCEEEEEEECCC	15.03	22817900
183	Phosphorylation	RRFRYRTTLTRERNA CCEEEEEEECCCCCC	19.68	22817900
184	Ubiquitination	RFRYRTTLTRERNAS CEEEEEEECCCCCCE	4.14	23000965
184 (in isoform 2)	Ubiquitination	-	4.14	21906983
191	Phosphorylation	LTRERNASVYSPSGP ECCCCCCEECCCCCC	25.74	28450419
193	Phosphorylation	RERNASVYSPSGPVN CCCCCEECCCCCCCC	16.62	23663014
194	Phosphorylation	ERNASVYSPSGPVNR CCCCEECCCCCCCCC	15.50	23401153
196	Phosphorylation	NASVYSPSGPVNRRT CCEECCCCCCCCCCC	50.19	23927012
203	Phosphorylation	SGPVNRRTTTPPDSG CCCCCCCCCCCCCCC	31.61	30266825
204	Phosphorylation	GPVNRRTTTPPDSGV CCCCCCCCCCCCCCC	35.18	30266825
205	Phosphorylation	PVNRRTTTPPDSGVL CCCCCCCCCCCCCCC	32.01	30266825
209	Phosphorylation	RTTTPPDSGVLFEGL CCCCCCCCCCCEECC	36.25	30266825
219	Phosphorylation	LFEGLGISTRPRDVE CEECCCCCCCCCCCC	19.30	26074081
220	Phosphorylation	FEGLGISTRPRDVEI EECCCCCCCCCCCCH	42.65	26074081
249	Sumoylation	ADERSLRKIQEQDII CCHHHHHHHHHHHHH	54.77	-
249	Sumoylation	ADERSLRKIQEQDII CCHHHHHHHHHHHHH	54.77	28112733
249	Ubiquitination	ADERSLRKIQEQDII CCHHHHHHHHHHHHH	54.77	23000965
249 (in isoform 1)	Ubiquitination	-	54.77	21890473
263	Phosphorylation	INFRRTLYRAGARVR HHHHHHHHHCCCCEE	9.60	-
482	Ubiquitination	SDNCVIVGFVKPLAE CCCEEEEEEEHHHHH	15.54	33845483
491	Phosphorylation	VKPLAERTPELVELS EHHHHHCCHHHHHCC	16.78	20363803
498	Phosphorylation	TPELVELSSDSEDLG CHHHHHCCCCCCCCC	20.70	20363803
499	Phosphorylation	PELVELSSDSEDLGS HHHHHCCCCCCCCCC	58.75	25159151
501	Phosphorylation	LVELSSDSEDLGSYE HHHCCCCCCCCCCHH	34.65	20363803
505	Phosphorylation	SSDSEDLGSYEKMET CCCCCCCCCHHHHHC	40.27	33259812
506	Phosphorylation	SDSEDLGSYEKMETV CCCCCCCCHHHHHCC	37.10	21406692
507	Phosphorylation	DSEDLGSYEKMETVK CCCCCCCHHHHHCCC	20.12	21406692
520	Phosphorylation	VKTQEQEQSYSSGDS CCCHHHHHHHCCCCC	47.57	32645325
533	Phosphorylation	DSDVSRCSSPHSVLG CCCHHHCCCCCCCCC	45.88	-
534	Phosphorylation	SDVSRCSSPHSVLGK CCHHHCCCCCCCCCC	30.20	25159151
537	Phosphorylation	SRCSSPHSVLGKDEQ HHCCCCCCCCCCCCC	23.56	-
547	Sumoylation	GKDEQINKGHCDSST CCCCCCCCCCCCCCH	52.22	-
547	Sumoylation	GKDEQINKGHCDSST CCCCCCCCCCCCCCH	52.22	-
547	Ubiquitination	GKDEQINKGHCDSST CCCCCCCCCCCCCCH	52.22	33845483
557	Acetylation	CDSSTRIKSKKEEKR CCCCHHHCCCHHHHC	53.59	19827721
559	Acetylation	SSTRIKSKKEEKRST CCHHHCCCHHHHCCC	60.24	19827729
560	Sumoylation	STRIKSKKEEKRSTS CHHHCCCHHHHCCCC	77.52	-
560	Acetylation	STRIKSKKEEKRSTS CHHHCCCHHHHCCCC	77.52	19827367
560	Sumoylation	STRIKSKKEEKRSTS CHHHCCCHHHHCCCC	77.52	28112733
565	Phosphorylation	SKKEEKRSTSLSSPR CCHHHHCCCCCCCCC	33.16	30266825
566	Phosphorylation	KKEEKRSTSLSSPRN CHHHHCCCCCCCCCC	37.41	30266825
567	Phosphorylation	KEEKRSTSLSSPRNL HHHHCCCCCCCCCCC	27.74	30266825
569	Phosphorylation	EKRSTSLSSPRNLNS HHCCCCCCCCCCCCC	37.76	30266825
570	Phosphorylation	KRSTSLSSPRNLNSS HCCCCCCCCCCCCCC	32.92	27794612
572	Dimethylation	STSLSSPRNLNSSVR CCCCCCCCCCCCCCC	63.32	-
572	Methylation	STSLSSPRNLNSSVR CCCCCCCCCCCCCCC	63.32	24380047
576	Phosphorylation	SSPRNLNSSVRGDRV CCCCCCCCCCCCCCC	33.12	29978859
577	Phosphorylation	SPRNLNSSVRGDRVY CCCCCCCCCCCCCCC	18.11	20068231
579	Dimethylation	RNLNSSVRGDRVYSP CCCCCCCCCCCCCCC	43.15	-
579	Methylation	RNLNSSVRGDRVYSP CCCCCCCCCCCCCCC	43.15	24380055
582	Dimethylation	NSSVRGDRVYSPYNH CCCCCCCCCCCCCCC	31.90	-
582	Methylation	NSSVRGDRVYSPYNH CCCCCCCCCCCCCCC	31.90	24380063
584	Phosphorylation	SVRGDRVYSPYNHRH CCCCCCCCCCCCCCC	12.57	28176443
585	Phosphorylation	VRGDRVYSPYNHRHR CCCCCCCCCCCCCCC	20.32	25159151
587	Phosphorylation	GDRVYSPYNHRHRKR CCCCCCCCCCCCCCC	20.05	23403867
597	Phosphorylation	RHRKRGRSRSSDSRS CCCCCCCCCCCCCCH	39.06	23403867
599	Phosphorylation	RKRGRSRSSDSRSQS CCCCCCCCCCCCHHC	39.48	23403867
600	Phosphorylation	KRGRSRSSDSRSQSR CCCCCCCCCCCHHCC	38.20	23403867
602	Phosphorylation	GRSRSSDSRSQSRSG CCCCCCCCCHHCCCC	35.46	23403867
604	Phosphorylation	SRSSDSRSQSRSGHD CCCCCCCHHCCCCCC	36.14	27251275
606	Phosphorylation	SSDSRSQSRSGHDQK CCCCCHHCCCCCCHH	29.66	27251275
608	Phosphorylation	DSRSQSRSGHDQKNH CCCHHCCCCCCHHHH	45.81	24719451
631	Phosphorylation	MKSKRSRSRESSRPR HHHHHHHHCCCCCCC	41.46	28509920
634	Phosphorylation	KRSRSRESSRPRGRR HHHHHCCCCCCCCHH	30.45	28509920
635	Phosphorylation	RSRSRESSRPRGRRD HHHHCCCCCCCCHHH	41.36	28509920
646	Ubiquitination	GRRDKKRSRTRDSSW CHHHHHHHHCCCCHH	47.05	23000965
657	Phosphorylation	DSSWSRRSQTLSLSS CCHHHHHHCEEECCC	26.80	24719451
659	Phosphorylation	SWSRRSQTLSLSSES HHHHHHCEEECCCCC	21.40	30576142
664	Phosphorylation	SQTLSLSSESTSRSR HCEEECCCCCCCCCC	40.64	30576142
666	Phosphorylation	TLSLSSESTSRSRSR EEECCCCCCCCCCCC	33.36	30576142
679	Acetylation	SRSSDHGKRRSRSRN CCCCCCCCCCCCCCC	41.01	19825047
695	Ubiquitination	DRYYLRNNYGSRYKW HHEEECCCCCCCCEE	35.79	27667366
700	Phosphorylation	RNNYGSRYKWEYTYY CCCCCCCCEEEEEEE	23.34	30576142
701	Sumoylation	NNYGSRYKWEYTYYS CCCCCCCEEEEEEEE	32.22	-
701	Sumoylation	NNYGSRYKWEYTYYS CCCCCCCEEEEEEEE	32.22	-
706	Phosphorylation	RYKWEYTYYSRNKDR CCEEEEEEEECCCCC	9.88	30576142
707	Phosphorylation	YKWEYTYYSRNKDRD CEEEEEEEECCCCCC	8.05	30576142
708	Phosphorylation	KWEYTYYSRNKDRDG EEEEEEEECCCCCCC	20.97	21815630
711	Sumoylation	YTYYSRNKDRDGYES EEEEECCCCCCCCCC	53.69	-
711	Sumoylation	YTYYSRNKDRDGYES EEEEECCCCCCCCCC	53.69	-
711	Ubiquitination	YTYYSRNKDRDGYES EEEEECCCCCCCCCC	53.69	23000965
716	Phosphorylation	RNKDRDGYESSYRRR CCCCCCCCCCHHHHH	19.54	29116813
718	Phosphorylation	KDRDGYESSYRRRTL CCCCCCCCHHHHHHH	24.96	29116813
719	Phosphorylation	DRDGYESSYRRRTLS CCCCCCCHHHHHHHH	15.66	29083192
720	Phosphorylation	RDGYESSYRRRTLSR CCCCCCHHHHHHHHH	19.88	29116813
724	Phosphorylation	ESSYRRRTLSRAHYS CCHHHHHHHHHHHHC	27.55	29978859
726	Phosphorylation	SYRRRTLSRAHYSRQ HHHHHHHHHHHHCCC	27.15	29978859
726	Ubiquitination	SYRRRTLSRAHYSRQ HHHHHHHHHHHHCCC	27.15	29967540
730	Phosphorylation	RTLSRAHYSRQSSSP HHHHHHHHCCCCCCC	12.45	29978859
731	Phosphorylation	TLSRAHYSRQSSSPE HHHHHHHCCCCCCCC	17.61	28450419
734	Phosphorylation	RAHYSRQSSSPEFRV HHHHCCCCCCCCHHH	31.50	22617229
734	Ubiquitination	RAHYSRQSSSPEFRV HHHHCCCCCCCCHHH	31.50	29967540
735	Phosphorylation	AHYSRQSSSPEFRVQ HHHCCCCCCCCHHHH	41.39	22617229
736	Phosphorylation	HYSRQSSSPEFRVQS HHCCCCCCCCHHHHH	33.42	22617229
743	Phosphorylation	SPEFRVQSFSERTNA CCCHHHHHHHHHHCC	28.08	21406692
745	Phosphorylation	EFRVQSFSERTNARK CHHHHHHHHHHCCHH	31.26	21406692
754	Ubiquitination	RTNARKKNNHSERKY HHCCHHHCCCHHHHH	55.25	22505724
756	Ubiquitination	NARKKNNHSERKYYY CCHHHCCCHHHHHHH	40.19	29967540
760	Ubiquitination	KNNHSERKYYYYERH HCCCHHHHHHHHHHH	33.29	27667366
762	Ubiquitination	NHSERKYYYYERHRS CCHHHHHHHHHHHHC	11.56	23000965
766	Ubiquitination	RKYYYYERHRSRSLS HHHHHHHHHHCCCCC	17.88	23000965
771	Phosphorylation	YERHRSRSLSSNRSR HHHHHCCCCCCCCCC	33.57	26546556
772	Ubiquitination	ERHRSRSLSSNRSRT HHHHCCCCCCCCCCC	6.73	23000965
779	Phosphorylation	LSSNRSRTASTGTDR CCCCCCCCCCCCCHH	26.63	28102081
781	Phosphorylation	SNRSRTASTGTDRVR CCCCCCCCCCCHHHH	27.10	28102081
782	Phosphorylation	NRSRTASTGTDRVRN CCCCCCCCCCHHHHC	41.45	28102081
784	Phosphorylation	SRTASTGTDRVRNEK CCCCCCCCHHHHCCC	22.26	28102081
791	Ubiquitination	TDRVRNEKPGGKRKY CHHHHCCCCCCCCCE	53.14	29967540
799	Ubiquitination	PGGKRKYKTRHLEGT CCCCCCEECHHCCCC	41.96	29967540
813	Phosphorylation	TNEVAQPSREFASKA CCCCCCCCHHHHHHH	32.15	28555341
819	Sumoylation	PSREFASKAKDSHYQ CCHHHHHHHCHHHCC	56.90	28112733
819	Ubiquitination	PSREFASKAKDSHYQ CCHHHHHHHCHHHCC	56.90	22505724
821	Ubiquitination	REFASKAKDSHYQKS HHHHHHHCHHHCCCC	64.60	29967540
827	Ubiquitination	AKDSHYQKSSSKLDG HCHHHCCCCCCCCCC	45.18	23000965
831	Ubiquitination	HYQKSSSKLDGNYKN HCCCCCCCCCCCCCC	53.17	23000965
836	Phosphorylation	SSKLDGNYKNESDTF CCCCCCCCCCCCCCC	22.26	26074081
837	Sumoylation	SKLDGNYKNESDTFS CCCCCCCCCCCCCCC	59.23	28112733
837	Ubiquitination	SKLDGNYKNESDTFS CCCCCCCCCCCCCCC	59.23	23000965
840	Phosphorylation	DGNYKNESDTFSDSR CCCCCCCCCCCCCCC	51.88	30108239
842	Phosphorylation	NYKNESDTFSDSRSS CCCCCCCCCCCCCCC	34.03	29255136
844	Phosphorylation	KNESDTFSDSRSSDR CCCCCCCCCCCCCCH	36.45	29255136
846	Phosphorylation	ESDTFSDSRSSDRET CCCCCCCCCCCCHHH	32.63	29255136
848	Phosphorylation	DTFSDSRSSDRETKH CCCCCCCCCCHHHHH	40.31	30108239
849	Phosphorylation	TFSDSRSSDRETKHK CCCCCCCCCHHHHHH	39.31	30108239
853	Phosphorylation	SRSSDRETKHKRRKR CCCCCHHHHHHHHCH	39.07	30108239
862	Phosphorylation	HKRRKRKTRSLSVEI HHHHCHHCCCCEEEE	29.53	25219547
864	Phosphorylation	RRKRKTRSLSVEIVY HHCHHCCCCEEEEEE	30.17	25159151
866	Phosphorylation	KRKTRSLSVEIVYEG CHHCCCCEEEEEECC	20.96	25159151
871	Phosphorylation	SLSVEIVYEGKATDT CCEEEEEECCCCCCC	25.32	28176443
902	Phosphorylation	KHHGDNASRSPVVIT HHCCCCCCCCCEEEE	39.27	21406692
904	Phosphorylation	HGDNASRSPVVITID CCCCCCCCCEEEEEC	21.39	28985074
909	Phosphorylation	SRSPVVITIDSDSDK CCCCEEEEECCCCCC	13.71	20363803
912	Phosphorylation	PVVITIDSDSDKDSE CEEEEECCCCCCCCC	34.85	25159151
914	Phosphorylation	VITIDSDSDKDSEVK EEEECCCCCCCCCCC	50.98	25159151
918	Phosphorylation	DSDSDKDSEVKEDTE CCCCCCCCCCCCCCC	50.45	21406692
943	Phosphorylation	QNEFLAPSLEPFETK CCCCCCCCCCCCCCC	39.49	26074081
949	Phosphorylation	PSLEPFETKDVVTIE CCCCCCCCCCEEEEE	32.68	26074081
1013	Phosphorylation	SDLENQPSNIVSLQT CCCCCCCCCEEEEEC	29.44	26074081
1017	Phosphorylation	NQPSNIVSLQTEPSR CCCCCEEEEECCCCC	15.80	26074081
1020	Phosphorylation	SNIVSLQTEPSRQLP CCEEEEECCCCCCCC	55.97	26074081
1023	Phosphorylation	VSLQTEPSRQLPSPR EEEECCCCCCCCCCC	26.82	26074081
1028	Phosphorylation	EPSRQLPSPRTSLMS CCCCCCCCCCHHHHH	35.29	23403867
1031	Phosphorylation	RQLPSPRTSLMSVCL CCCCCCCHHHHHHHH	29.60	26074081
1032	Phosphorylation	QLPSPRTSLMSVCLG CCCCCCHHHHHHHHC	24.29	26074081
1035	Phosphorylation	SPRTSLMSVCLGRDC CCCHHHHHHHHCCCC	18.25	28555341

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
718	S	Phosphorylation	Kinase	PLK1	P53350	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
98	S	Phosphorylation	19053840
Phosphorylation at Ser-98 regulates the E3 ubiquitin-protein ligase activity but not the SUMO1-protein ligase activity.
98	S	ubiquitylation	19053840
Phosphorylation at Ser-98 regulates the E3 ubiquitin-protein ligase activity but not the SUMO1-protein ligase activity.
718	S	Phosphorylation	19473992
Phosphorylation at Ser-718 increases the E3 ubiquitin-protein ligase activity versus the SUMO1-protein ligase activity resulting in increased p53/TP53 ubiquitination and degradation.
718	S	ubiquitylation	19473992
Phosphorylation at Ser-718 increases the E3 ubiquitin-protein ligase activity versus the SUMO1-protein ligase activity resulting in increased p53/TP53 ubiquitination and degradation.

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 TOPRS_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
UBC9_HUMAN	UBE2I	physical	14516784
SUMO1_HUMAN	SUMO1	physical	14516784
TOP1_HUMAN	TOP1	physical	10352183
P53_HUMAN	TP53	physical	11842245
UB2D1_HUMAN	UBE2D1	physical	19053840
P53_HUMAN	TP53	physical	15247280
P53_HUMAN	TP53	physical	17803295
GTF2I_HUMAN	GTF2I	physical	17803295
NONO_HUMAN	NONO	physical	17803295
SFPQ_HUMAN	SFPQ	physical	17803295
SIN3A_HUMAN	SIN3A	physical	17803295
PARP1_HUMAN	PARP1	physical	17803295
SAFB2_HUMAN	SAFB2	physical	17803295
DDB2_HUMAN	DDB2	physical	17803295
RBBP7_HUMAN	RBBP7	physical	17803295
TIF1B_HUMAN	TRIM28	physical	17803295
RBBP4_HUMAN	RBBP4	physical	17803295
SMRC2_HUMAN	SMARCC2	physical	17803295
DHX15_HUMAN	DHX15	physical	17803295
HNRPL_HUMAN	HNRNPL	physical	17803295
RAGP1_HUMAN	RANGAP1	physical	17803295
REN3A_HUMAN	UPF3A	physical	17803295
HNRPM_HUMAN	HNRNPM	physical	17803295
ROA1_HUMAN	HNRNPA1	physical	17803295
SF3B1_HUMAN	SF3B1	physical	17803295
EF1A1_HUMAN	EEF1A1	physical	17803295
S10A9_HUMAN	S100A9	physical	17803295
NKX31_HUMAN	NKX3-1	physical	18077445
TOP1_HUMAN	TOP1	physical	20805487
TOP1_HUMAN	TOP1	physical	17976381
IKKE_HUMAN	IKBKE	physical	20188669
PML_HUMAN	PML	physical	20188669
P53_HUMAN	TP53	physical	17290218
H2AX_HUMAN	H2AFX	physical	22972498
PLK1_HUMAN	PLK1	physical	22972498
UB2D1_HUMAN	UBE2D1	physical	18077445
UB2D1_HUMAN	UBE2D1	physical	15247280
UB2D3_HUMAN	UBE2D3	physical	15247280
UB2E1_HUMAN	UBE2E1	physical	15247280
PLK1_HUMAN	PLK1	physical	19473992
UBC_HUMAN	UBC	physical	15247280
P53_HUMAN	TP53	physical	16122737
UBC9_HUMAN	UBE2I	physical	16122737
PRS4_HUMAN	PSMC1	physical	26872363

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
609923	Retinitis pigmentosa 31 (RP31)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of TOPRS_HUMAN

Related Literatures of Post-Translational Modification

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-98; SER-864 AND SER-866,AND MASS SPECTROMETRY.	19690332 [Abstract]
"Plk1-mediated phosphorylation of Topors regulates p53 stability."; Yang X., Li H., Zhou Z., Wang W.H., Deng A., Andrisani O., Liu X.; J. Biol. Chem. 284:18588-18592(2009). Cited for: FUNCTION, INTERACTION WITH PLK1, PHOSPHORYLATION AT SER-718 BY PLK1,MUTAGENESIS OF SER-718, AND SUBCELLULAR LOCATION.	19473992 [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-98, AND MASSSPECTROMETRY.	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-98, 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-98, AND MASSSPECTROMETRY.	18691976 [Abstract]
"Identification of phosphorylation sites of TOPORS and a role forserine 98 in the regulation of ubiquitin but not SUMO E3 ligaseactivity."; Park H.J., Zheng H., Kulkarni D., Kerrigan J., Pungaliya P.,Saleem A., Rubin E.H.; Biochemistry 47:13887-13896(2008). Cited for: PHOSPHORYLATION AT SER-98; SER-499; SER-585 AND SER-866, MASSSPECTROMETRY, AND MUTAGENESIS OF SER-98.	19053840 [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-194, AND MASSSPECTROMETRY.	19007248 [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-902; SER-912 ANDSER-914, AND MASS SPECTROMETRY.	17081983 [Abstract]
"Large-scale characterization of HeLa cell nuclear phosphoproteins."; Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-98, AND MASSSPECTROMETRY.	15302935 [Abstract]

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