dbPTM

TOP1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	TOP1_HUMAN
UniProt AC	P11387
Protein Name	DNA topoisomerase 1
Gene Name	TOP1
Organism	Homo sapiens (Human).
Sequence Length	765
Subcellular Localization	Nucleus, nucleolus . Nucleus, nucleoplasm . Diffuse nuclear localization with some enrichment in nucleoli. On CPT treatment, cleared from nucleoli into nucleoplasm. Sumoylated forms found in both nucleoplasm and nucleoli.
Protein Description	Releases the supercoiling and torsional tension of DNA introduced during the DNA replication and transcription by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(3'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 5'-OH DNA strand. The free DNA strand then rotates around the intact phosphodiester bond on the opposing strand, thus removing DNA supercoils. Finally, in the religation step, the DNA 5'-OH attacks the covalent intermediate to expel the active-site tyrosine and restore the DNA phosphodiester backbone (By similarity). Regulates the alternative splicing of tissue factor (F3) pre-mRNA in endothelial cells. Involved in the circadian transcription of the core circadian clock component ARNTL/BMAL1 by altering the chromatin structure around the ROR response elements (ROREs) on the ARNTL/BMAL1 promoter..
Protein Sequence	MSGDHLHNDSQIEADFRLNDSHKHKDKHKDREHRHKEHKKEKDREKSKHSNSEHKDSEKKHKEKEKTKHKDGSSEKHKDKHKDRDKEKRKEEKVRASGDAKIKKEKENGFSSPPQIKDEPEDDGYFVPPKEDIKPLKRPRDEDDADYKPKKIKTEDTKKEKKRKLEEEEDGKLKKPKNKDKDKKVPEPDNKKKKPKKEEEQKWKWWEEERYPEGIKWKFLEHKGPVFAPPYEPLPENVKFYYDGKVMKLSPKAEEVATFFAKMLDHEYTTKEIFRKNFFKDWRKEMTNEEKNIITNLSKCDFTQMSQYFKAQTEARKQMSKEEKLKIKEENEKLLKEYGFCIMDNHKERIANFKIEPPGLFRGRGNHPKMGMLKRRIMPEDIIINCSKDAKVPSPPPGHKWKEVRHDNKVTWLVSWTENIQGSIKYIMLNPSSRIKGEKDWQKYETARRLKKCVDKIRNQYREDWKSKEMKVRQRAVALYFIDKLALRAGNEKEEGETADTVGCCSLRVEHINLHPELDGQEYVVEFDFLGKDSIRYYNKVPVEKRVFKNLQLFMENKQPEDDLFDRLNTGILNKHLQDLMEGLTAKVFRTYNASITLQQQLKELTAPDENIPAKILSYNRANRAVAILCNHQRAPPKTFEKSMMNLQTKIDAKKEQLADARRDLKSAKADAKVMKDAKTKKVVESKKKAVQRLEEQLMKLEVQATDREENKQIALGTSKLNYLDPRITVAWCKKWGVPIEKIYNKTQREKFAWAIDMADEDYEF

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MSGDHLHND ------CCCCCCCCC	53.58	20068231
2	Phosphorylation	------MSGDHLHND ------CCCCCCCCC	53.58	23401153
10	Phosphorylation	GDHLHNDSQIEADFR CCCCCCCHHHHHHEE	38.07	29255136
21	Phosphorylation	ADFRLNDSHKHKDKH HHEECCCCCCCCCHH	33.10	20068231
57	Phosphorylation	SNSEHKDSEKKHKEK CCCCCCHHHHHHHHH	57.00	20068231
73	Phosphorylation	KTKHKDGSSEKHKDK HCCCCCCCCHHHHHH	45.52	20068231
74	Phosphorylation	TKHKDGSSEKHKDKH CCCCCCCCHHHHHHC	57.08	20068231
97	Phosphorylation	KEEKVRASGDAKIKK HHHHHHHCCCCCCHH	27.00	28176443
101	Sumoylation	VRASGDAKIKKEKEN HHHCCCCCCHHHHHC	60.85	28112733
103	Sumoylation	ASGDAKIKKEKENGF HCCCCCCHHHHHCCC	54.92	-
103	Sumoylation	ASGDAKIKKEKENGF HCCCCCCHHHHHCCC	54.92	-
111	Phosphorylation	KEKENGFSSPPQIKD HHHHCCCCCCCCCCC	43.25	30266825
112	Phosphorylation	EKENGFSSPPQIKDE HHHCCCCCCCCCCCC	38.04	30266825
117	Sumoylation	FSSPPQIKDEPEDDG CCCCCCCCCCCCCCC	51.28	-
117	Acetylation	FSSPPQIKDEPEDDG CCCCCCCCCCCCCCC	51.28	26051181
117	Sumoylation	FSSPPQIKDEPEDDG CCCCCCCCCCCCCCC	51.28	25114211
125	Phosphorylation	DEPEDDGYFVPPKED CCCCCCCCCCCCHHH	14.38	26657352
134	Sumoylation	VPPKEDIKPLKRPRD CCCHHHCCCCCCCCC	57.53	-
134	Acetylation	VPPKEDIKPLKRPRD CCCHHHCCCCCCCCC	57.53	22424773
134	Sumoylation	VPPKEDIKPLKRPRD CCCHHHCCCCCCCCC	57.53	28112733
137	Ubiquitination	KEDIKPLKRPRDEDD HHHCCCCCCCCCCCC	69.73	-
147	Phosphorylation	RDEDDADYKPKKIKT CCCCCCCCCCCCCCC	30.80	-
148	Sumoylation	DEDDADYKPKKIKTE CCCCCCCCCCCCCCC	51.40	-
148	Acetylation	DEDDADYKPKKIKTE CCCCCCCCCCCCCCC	51.40	23749302
148	Sumoylation	DEDDADYKPKKIKTE CCCCCCCCCCCCCCC	51.40	28112733
148	Ubiquitination	DEDDADYKPKKIKTE CCCCCCCCCCCCCCC	51.40	-
150	Acetylation	DDADYKPKKIKTEDT CCCCCCCCCCCCCCC	64.08	23749302
153	Sumoylation	DYKPKKIKTEDTKKE CCCCCCCCCCCCHHH	55.53	-
153	Sumoylation	DYKPKKIKTEDTKKE CCCCCCCCCCCCHHH	55.53	-
158	Sumoylation	KIKTEDTKKEKKRKL CCCCCCCHHHHHHHH	71.85	-
158	Sumoylation	KIKTEDTKKEKKRKL CCCCCCCHHHHHHHH	71.85	28112733
164	Sumoylation	TKKEKKRKLEEEEDG CHHHHHHHHHHHHCC	69.95	-
164	Acetylation	TKKEKKRKLEEEEDG CHHHHHHHHHHHHCC	69.95	21339330
164	Sumoylation	TKKEKKRKLEEEEDG CHHHHHHHHHHHHCC	69.95	28112733
172	Acetylation	LEEEEDGKLKKPKNK HHHHHCCCCCCCCCC	70.25	23749302
172	Sumoylation	LEEEEDGKLKKPKNK HHHHHCCCCCCCCCC	70.25	28112733
204	Sumoylation	KEEEQKWKWWEEERY HHHHHHHHHHHHHHC	49.84	28112733
204	Ubiquitination	KEEEQKWKWWEEERY HHHHHHHHHHHHHHC	49.84	-
211	Phosphorylation	KWWEEERYPEGIKWK HHHHHHHCCCCCCCE	14.65	26270265
218	Ubiquitination	YPEGIKWKFLEHKGP CCCCCCCEEHHCCCC	34.76	-
223	2-Hydroxyisobutyrylation	KWKFLEHKGPVFAPP CCEEHHCCCCCCCCC	56.38	-
223	Acetylation	KWKFLEHKGPVFAPP CCEEHHCCCCCCCCC	56.38	26051181
223	Ubiquitination	KWKFLEHKGPVFAPP CCEEHHCCCCCCCCC	56.38	21890473
231	Phosphorylation	GPVFAPPYEPLPENV CCCCCCCCCCCCCCC	29.17	28152594
239	Acetylation	EPLPENVKFYYDGKV CCCCCCCEEEECCEE	38.95	25953088
239	Ubiquitination	EPLPENVKFYYDGKV CCCCCCCEEEECCEE	38.95	21890473
242	Phosphorylation	PENVKFYYDGKVMKL CCCCEEEECCEEEEC	22.73	28064214
245	2-Hydroxyisobutyrylation	VKFYYDGKVMKLSPK CEEEECCEEEECCCC	35.94	-
245	Acetylation	VKFYYDGKVMKLSPK CEEEECCEEEECCCC	35.94	25953088
245	Ubiquitination	VKFYYDGKVMKLSPK CEEEECCEEEECCCC	35.94	21890473
248	Acetylation	YYDGKVMKLSPKAEE EECCEEEECCCCHHH	49.12	25953088
252	2-Hydroxyisobutyrylation	KVMKLSPKAEEVATF EEEECCCCHHHHHHH	66.12	-
252	Acetylation	KVMKLSPKAEEVATF EEEECCCCHHHHHHH	66.12	26051181
252	Ubiquitination	KVMKLSPKAEEVATF EEEECCCCHHHHHHH	66.12	20639865
262	Acetylation	EVATFFAKMLDHEYT HHHHHHHHHHCCCCC	34.53	25825284
262	Ubiquitination	EVATFFAKMLDHEYT HHHHHHHHHHCCCCC	34.53	-
268	Phosphorylation	AKMLDHEYTTKEIFR HHHHCCCCCHHHHHH	19.11	15448168
271	2-Hydroxyisobutyrylation	LDHEYTTKEIFRKNF HCCCCCHHHHHHHHH	40.80	-
271	Acetylation	LDHEYTTKEIFRKNF HCCCCCHHHHHHHHH	40.80	26822725
280	2-Hydroxyisobutyrylation	IFRKNFFKDWRKEMT HHHHHHHHHHHHHCC	52.85	-
280	Acetylation	IFRKNFFKDWRKEMT HHHHHHHHHHHHHCC	52.85	19608861
280	Ubiquitination	IFRKNFFKDWRKEMT HHHHHHHHHHHHHCC	52.85	21890473
284	Acetylation	NFFKDWRKEMTNEEK HHHHHHHHHCCHHHH	47.81	26051181
291	Acetylation	KEMTNEEKNIITNLS HHCCHHHHHHHHHHH	47.47	23236377
295	Phosphorylation	NEEKNIITNLSKCDF HHHHHHHHHHHHCCH	26.72	-
298	Phosphorylation	KNIITNLSKCDFTQM HHHHHHHHHCCHHHH	33.05	20068231
299	Acetylation	NIITNLSKCDFTQMS HHHHHHHHCCHHHHH	40.78	25953088
303	Phosphorylation	NLSKCDFTQMSQYFK HHHHCCHHHHHHHHH	15.31	-
326	Ubiquitination	MSKEEKLKIKEENEK CCHHHHHHHHHHHHH	63.90	21890473
328	Sumoylation	KEEKLKIKEENEKLL HHHHHHHHHHHHHHH	58.34	-
333	2-Hydroxyisobutyrylation	KIKEENEKLLKEYGF HHHHHHHHHHHHHCE	71.36	-
336	Sumoylation	EENEKLLKEYGFCIM HHHHHHHHHHCEEEE	60.36	-
336	Acetylation	EENEKLLKEYGFCIM HHHHHHHHHHCEEEE	60.36	26051181
336	Sumoylation	EENEKLLKEYGFCIM HHHHHHHHHHCEEEE	60.36	28112733
347	2-Hydroxyisobutyrylation	FCIMDNHKERIANFK EEEECCCHHHHHCCE	55.75	-
347	Acetylation	FCIMDNHKERIANFK EEEECCCHHHHHCCE	55.75	25825284
347	Ubiquitination	FCIMDNHKERIANFK EEEECCCHHHHHCCE	55.75	-
354	Sumoylation	KERIANFKIEPPGLF HHHHHCCEECCCCCC	46.06	-
354	Acetylation	KERIANFKIEPPGLF HHHHHCCEECCCCCC	46.06	25953088
354	Sumoylation	KERIANFKIEPPGLF HHHHHCCEECCCCCC	46.06	-
354	Ubiquitination	KERIANFKIEPPGLF HHHHHCCEECCCCCC	46.06	21890473
369	Ubiquitination	RGRGNHPKMGMLKRR CCCCCCCCCCCHHCC	40.30	-
374	Methylation	HPKMGMLKRRIMPED CCCCCCHHCCCCCHH	30.64	-
378	Sulfoxidation	GMLKRRIMPEDIIIN CCHHCCCCCHHEEEE	2.56	21406390
386	Glutathionylation	PEDIIINCSKDAKVP CHHEEEECCCCCCCC	3.64	22555962
387	Phosphorylation	EDIIINCSKDAKVPS HHEEEECCCCCCCCC	29.14	25690035
388	Acetylation	DIIINCSKDAKVPSP HEEEECCCCCCCCCC	65.00	25953088
391	Sumoylation	INCSKDAKVPSPPPG EECCCCCCCCCCCCC	65.89	-
391	Sumoylation	INCSKDAKVPSPPPG EECCCCCCCCCCCCC	65.89	-
391	Ubiquitination	INCSKDAKVPSPPPG EECCCCCCCCCCCCC	65.89	-
394	Phosphorylation	SKDAKVPSPPPGHKW CCCCCCCCCCCCCCC	53.69	30266825
400	Ubiquitination	PSPPPGHKWKEVRHD CCCCCCCCCEEEEEC	66.91	21906983
423	Phosphorylation	WTENIQGSIKYIMLN EECCCCCEEEEEEEC	10.26	-
426	Phosphorylation	NIQGSIKYIMLNPSS CCCCEEEEEEECHHH	7.01	20068231
428	Sulfoxidation	QGSIKYIMLNPSSRI CCEEEEEEECHHHHC	2.41	21406390
432	Phosphorylation	KYIMLNPSSRIKGEK EEEEECHHHHCCCCC	31.04	20068231
433	Phosphorylation	YIMLNPSSRIKGEKD EEEECHHHHCCCCCH	39.00	23312004
436	Sumoylation	LNPSSRIKGEKDWQK ECHHHHCCCCCHHHH	60.96	-
436	Acetylation	LNPSSRIKGEKDWQK ECHHHHCCCCCHHHH	60.96	26051181
436	Sumoylation	LNPSSRIKGEKDWQK ECHHHHCCCCCHHHH	60.96	-
439	2-Hydroxyisobutyrylation	SSRIKGEKDWQKYET HHHCCCCCHHHHHHH	73.30	-
443	Acetylation	KGEKDWQKYETARRL CCCCHHHHHHHHHHH	40.58	25825284
444	Phosphorylation	GEKDWQKYETARRLK CCCHHHHHHHHHHHH	11.92	28152594
446	Phosphorylation	KDWQKYETARRLKKC CHHHHHHHHHHHHHH	23.52	28152594
456	Acetylation	RLKKCVDKIRNQYRE HHHHHHHHHHHHHHH	24.14	25953088
456	Ubiquitination	RLKKCVDKIRNQYRE HHHHHHHHHHHHHHH	24.14	-
466	Methylation	NQYREDWKSKEMKVR HHHHHHHHCCHHHHH	65.06	-
471	Methylation	DWKSKEMKVRQRAVA HHHCCHHHHHHHHHH	35.04	-
480	Phosphorylation	RQRAVALYFIDKLAL HHHHHHHHHHHHHHH	6.69	28152594
484	Acetylation	VALYFIDKLALRAGN HHHHHHHHHHHHCCC	30.73	26051181
484	Ubiquitination	VALYFIDKLALRAGN HHHHHHHHHHHHCCC	30.73	-
493	Acetylation	ALRAGNEKEEGETAD HHHCCCCCCCCCCCC	66.13	25953088
493	Ubiquitination	ALRAGNEKEEGETAD HHHCCCCCCCCCCCC	66.13	-
506	Phosphorylation	ADTVGCCSLRVEHIN CCCCCEEEEEEEEEE	24.24	28112733
534	Phosphorylation	FDFLGKDSIRYYNKV EEECCCCCCEEECCC	16.67	29759185
537	Phosphorylation	LGKDSIRYYNKVPVE CCCCCCEEECCCCHH	15.10	29759185
538	Phosphorylation	GKDSIRYYNKVPVEK CCCCCEEECCCCHHH	9.92	28152594
540	2-Hydroxyisobutyrylation	DSIRYYNKVPVEKRV CCCEEECCCCHHHHH	31.62	-
540	Acetylation	DSIRYYNKVPVEKRV CCCEEECCCCHHHHH	31.62	26051181
545	Acetylation	YNKVPVEKRVFKNLQ ECCCCHHHHHHHHHH	54.84	23749302
545	Ubiquitination	YNKVPVEKRVFKNLQ ECCCCHHHHHHHHHH	54.84	-
549	Acetylation	PVEKRVFKNLQLFME CHHHHHHHHHHHHHH	54.62	25953088
549	Sumoylation	PVEKRVFKNLQLFME CHHHHHHHHHHHHHH	54.62	28112733
549	Ubiquitination	PVEKRVFKNLQLFME CHHHHHHHHHHHHHH	54.62	21890473
555	Sulfoxidation	FKNLQLFMENKQPED HHHHHHHHHCCCCCC	8.25	21406390
558	Ubiquitination	LQLFMENKQPEDDLF HHHHHHCCCCCCHHH	54.66	21890473
567	Methylation	PEDDLFDRLNTGILN CCCHHHHHHHHHHHH	23.62	115918725
570	Phosphorylation	DLFDRLNTGILNKHL HHHHHHHHHHHHHHH	30.14	-
575	Acetylation	LNTGILNKHLQDLME HHHHHHHHHHHHHHH	42.10	25825284
575	Ubiquitination	LNTGILNKHLQDLME HHHHHHHHHHHHHHH	42.10	-
581	Sulfoxidation	NKHLQDLMEGLTAKV HHHHHHHHHHHHHHH	5.30	28183972
587	2-Hydroxyisobutyrylation	LMEGLTAKVFRTYNA HHHHHHHHHHHHHCC	36.35	-
587	Acetylation	LMEGLTAKVFRTYNA HHHHHHHHHHHHHCC	36.35	26051181
587	Ubiquitination	LMEGLTAKVFRTYNA HHHHHHHHHHHHHCC	36.35	21890473
591	Phosphorylation	LTAKVFRTYNASITL HHHHHHHHHCCEEEH	15.06	28152594
592	Phosphorylation	TAKVFRTYNASITLQ HHHHHHHHCCEEEHH	12.41	28152594
603	Ubiquitination	ITLQQQLKELTAPDE EEHHHHHHHCCCCCC	46.47	21906983
615	Acetylation	PDENIPAKILSYNRA CCCCCCHHHHCCCCC	38.53	25953088
615	Ubiquitination	PDENIPAKILSYNRA CCCCCCHHHHCCCCC	38.53	21906983
642	Acetylation	APPKTFEKSMMNLQT CCCCCHHHHHHHHHH	39.19	25825284
642	Sumoylation	APPKTFEKSMMNLQT CCCCCHHHHHHHHHH	39.19	28112733
642	Ubiquitination	APPKTFEKSMMNLQT CCCCCHHHHHHHHHH	39.19	21890473
643	Phosphorylation	PPKTFEKSMMNLQTK CCCCHHHHHHHHHHH	18.96	28387310
649	Phosphorylation	KSMMNLQTKIDAKKE HHHHHHHHHHHHHHH	32.88	-
650	Acetylation	SMMNLQTKIDAKKEQ HHHHHHHHHHHHHHH	26.15	25953088
655	2-Hydroxyisobutyrylation	QTKIDAKKEQLADAR HHHHHHHHHHHHHHH	53.03	-
666	Ubiquitination	ADARRDLKSAKADAK HHHHHHHHHHHHHHH	53.29	-
673	Acetylation	KSAKADAKVMKDAKT HHHHHHHHHHCCHHC	43.33	25953088
686	Phosphorylation	KTKKVVESKKKAVQR HCHHHHHHHHHHHHH	37.86	24702127
688	Ubiquitination	KKVVESKKKAVQRLE HHHHHHHHHHHHHHH	56.07	-
689	Ubiquitination	KVVESKKKAVQRLEE HHHHHHHHHHHHHHH	58.49	-
699	Sulfoxidation	QRLEEQLMKLEVQAT HHHHHHHHHHHCCCC	4.68	21406390
700	Sumoylation	RLEEQLMKLEVQATD HHHHHHHHHHCCCCC	50.52	28112733
706	Phosphorylation	MKLEVQATDREENKQ HHHHCCCCCHHHHCE	20.64	-
712	Acetylation	ATDREENKQIALGTS CCCHHHHCEEEEECC	46.49	26051181
712	Sumoylation	ATDREENKQIALGTS CCCHHHHCEEEEECC	46.49	28112733
712	Ubiquitination	ATDREENKQIALGTS CCCHHHHCEEEEECC	46.49	21890473
720	Acetylation	QIALGTSKLNYLDPR EEEEECCCCCCCCCC	40.36	25953088
720	Ubiquitination	QIALGTSKLNYLDPR EEEEECCCCCCCCCC	40.36	-
723	Phosphorylation	LGTSKLNYLDPRITV EECCCCCCCCCCCCH	23.95	28152594
733	Glutathionylation	PRITVAWCKKWGVPI CCCCHHHHHHHCCCH	2.04	22555962
734	2-Hydroxyisobutyrylation	RITVAWCKKWGVPIE CCCHHHHHHHCCCHH	40.64	-
735	Acetylation	ITVAWCKKWGVPIEK CCHHHHHHHCCCHHH	46.15	25953088
742	Acetylation	KWGVPIEKIYNKTQR HHCCCHHHHCCHHHH	51.73	26051181
742	Ubiquitination	KWGVPIEKIYNKTQR HHCCCHHHHCCHHHH	51.73	2190698

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
10	S	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
10	S	Phosphorylation	Kinase	PRKDC	P78527	GPS
21	S	Phosphorylation	Kinase	PRKCA	P17252	GPS
112	S	Phosphorylation	Kinase	CDK1	P06493	PSP
268	Y	Phosphorylation	Kinase	ABL1	P00519	PhosphoELM
268	Y	Phosphorylation	Kinase	ABL-FAMILY	-	GPS
394	S	Phosphorylation	Kinase	CDK1	P06493	PSP
506	S	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
506	S	Phosphorylation	Kinase	CK2	-	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
117	K	Sumoylation	12149243
Lys-117 is the main site of sumoylation.
506	S	Phosphorylation	23185622
Phosphorylation at Ser-506 by CK2 increases binding to supercoiled DNA and sensitivity to camptothecin.

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 TOP1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SRSF1_HUMAN	SRSF1	physical	9611241
SRSF1_HUMAN	SRSF1	physical	12270705
SRS11_HUMAN	SRSF11	physical	9756848
SFPQ_HUMAN	SFPQ	physical	9756848
NUCL_HUMAN	NCL	physical	8567649
UBC9_HUMAN	UBE2I	physical	10759568
NPM_HUMAN	NPM1	physical	15848144
FBRL_HUMAN	FBL	physical	15848144
H12_HUMAN	HIST1H1C	physical	15848144
H1X_HUMAN	H1FX	physical	15848144
ROA1_HUMAN	HNRNPA1	physical	15848144
ROA2_HUMAN	HNRNPA2B1	physical	15848144
ROA3_HUMAN	HNRNPA3	physical	15848144
HNRPC_HUMAN	HNRNPC	physical	15848144
HNRPK_HUMAN	HNRNPK	physical	15848144
HNRPL_HUMAN	HNRNPL	physical	15848144
HNRPR_HUMAN	HNRNPR	physical	15848144
ELAV1_HUMAN	ELAVL1	physical	15848144
KI67_HUMAN	MKI67	physical	15848144
NAT10_HUMAN	NAT10	physical	15848144
DHX9_HUMAN	DHX9	physical	15848144
NUCL_HUMAN	NCL	physical	15848144
NOP2_HUMAN	NOP2	physical	15848144
NONO_HUMAN	NONO	physical	15848144
PARP1_HUMAN	PARP1	physical	15848144
SFPQ_HUMAN	SFPQ	physical	15848144
DDX21_HUMAN	DDX21	physical	15848144
DDX17_HUMAN	DDX17	physical	15848144
SRSF1_HUMAN	SRSF1	physical	15848144
SF3B3_HUMAN	SF3B3	physical	15848144
SF3B1_HUMAN	SF3B1	physical	15848144
TCOF_HUMAN	TCOF1	physical	15848144
RU2A_HUMAN	SNRPA1	physical	15848144
DDX23_HUMAN	DDX23	physical	15848144
U5S1_HUMAN	EFTUD2	physical	15848144
U520_HUMAN	SNRNP200	physical	15848144
PRP8_HUMAN	PRPF8	physical	15848144
BTBD1_HUMAN	BTBD1	physical	21092135
BTBD2_HUMAN	BTBD2	physical	21092135
DDB2_HUMAN	DDB2	physical	12549820
ERCC8_HUMAN	ERCC8	physical	12549820
ATM_HUMAN	ATM	physical	12549820
IRF4_HUMAN	IRF4	physical	12549820
BARD1_HUMAN	BARD1	physical	12549820
ELK3_HUMAN	ELK3	physical	12549820
TRBP2_HUMAN	TARBP2	physical	12549820
KMT2A_HUMAN	KMT2A	physical	12549820
IRF8_HUMAN	IRF8	physical	12549820
IRF9_HUMAN	IRF9	physical	12549820
SNW1_HUMAN	SNW1	physical	12549820
SF3B1_HUMAN	SF3B1	physical	12549820
PRP1_HUMAN	PRB1	physical	12549820
RU17_HUMAN	SNRNP70	physical	12549820
U2AF2_HUMAN	U2AF2	physical	12549820
LSM4_HUMAN	LSM4	physical	12549820
GEMI4_HUMAN	GEMIN4	physical	12549820
CDK8_HUMAN	CDK8	physical	12549820
BUB3_HUMAN	BUB3	physical	12549820
RBL1_HUMAN	RBL1	physical	12549820
RBL2_HUMAN	RBL2	physical	12549820
GRWD1_HUMAN	GRWD1	physical	12549820
SYMPK_HUMAN	SYMPK	physical	12549820
JAK1_HUMAN	JAK1	physical	12549820
DNLI4_HUMAN	LIG4	physical	12549820
2ABB_HUMAN	PPP2R2B	physical	12549820
TRI32_HUMAN	TRIM32	physical	12549820
RECO_HUMAN	RCVRN	physical	12549820
PYGM_HUMAN	PYGM	physical	12549820
APAF_HUMAN	APAF1	physical	12549820
CKAP5_HUMAN	CKAP5	physical	12549820
TBD_HUMAN	TUBD1	physical	12549820
PDE10_HUMAN	PDE10A	physical	12549820
A4_HUMAN	APP	physical	21832049
UTP20_HUMAN	UTP20	physical	22939629
TPR_HUMAN	TPR	physical	22939629
NKX31_HUMAN	NKX3-1	physical	17234752
IL7RA_HUMAN	IL7R	physical	23151878
PARP1_HUMAN	PARP1	physical	15247263
P53_HUMAN	TP53	physical	18697815
RBM25_HUMAN	RBM25	physical	26344197
TSC1_HUMAN	TSC1	genetic	28319113
CHK1_HUMAN	CHEK1	genetic	27453043
BRCA2_HUMAN	BRCA2	genetic	27453043
WEE1_HUMAN	WEE1	genetic	27453043
PALB2_HUMAN	PALB2	genetic	27453043
RAD17_HUMAN	RAD17	genetic	27453043
L2GL1_HUMAN	LLGL1	genetic	27453043
MSH2_HUMAN	MSH2	genetic	27453043
NF1_HUMAN	NF1	genetic	27453043
RS11_HUMAN	RPS11	genetic	27453043
CDC73_HUMAN	CDC73	genetic	27453043
CDC6_HUMAN	CDC6	genetic	27453043
M3K4_HUMAN	MAP3K4	genetic	27453043
TITIN_HUMAN	TTN	genetic	27453043
FUMH_HUMAN	FH	genetic	27453043

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
DB00762	Irinotecan
DB04967	Lucanthone
DB05630	Sodium stibogluconate
DB01030	Topotecan

Regulatory Network of TOP1_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-280, AND MASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-112, AND MASSSPECTROMETRY.	19413330 [Abstract]
Sumoylation
Reference	PubMed
"Sumoylation of topoisomerase I is involved in its partitioningbetween nucleoli and nucleoplasm and its clearing from nucleoli inresponse to camptothecin."; Rallabhandi P., Hashimoto K., Mo Y.-Y., Beck W.T., Moitra P.K.,D'Arpa P.; J. Biol. Chem. 277:40020-40026(2002). Cited for: SUMOYLATION AT LYS-117, SUBCELLULAR LOCATION, AND MUTAGENESIS OFLYS-103; LYS-117; LYS-153 AND TYR-723.	12149243 [Abstract]

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