TOP1_DROME - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: TOP1_DROME
• UniProt AC: P30189
• Protein Name: DNA topoisomerase 1
• Gene Name: Top1 {ECO:0000312|FlyBase:FBgn0004924}
• Organism: Drosophila melanogaster (Fruit fly).
• Sequence Length: 972
• Subcellular Localization: Nucleus . Cytoplasm . During early cell divisions of developing embryos, it is detected in the nucleus at interphase then diffusely dispersed in the cytoplasm at metaphase.
• 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 (By similarity). Introduces a single-strand break via transesterification at a target site in duplex DNA (By similarity). 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 (By similarity). The free DNA strand then undergoes passage around the unbroken strand thus removing DNA supercoils (By similarity). 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)..
• Protein Sequence: MSGDVAAENSIHIQNGGSCEVVQSNGVTTNGHGHHHHHHSSSSSSSKHKSSSKDKHRDREREHKSSNSSSSSKEHKSSSRDKDRHKSSSSSSKHRDKDKERDGSSNSHRSGSSSSHKDKDGSSSSKHKSSSGHHKRSSKDKERRDKDKDRGSSSSSRHKSSSSSRDKERSSSSHKSSSSSSSSKSKHSSSRHSSSSSSKDHPSYDGVFVKPEPVSQQLMHSGSVDAFQMQQLGSYEAAAAGTNFNGNGNVAGANYKNGYEESIVDIKKEEESFNNLSQASSCDYSMSQFRADEPPFVVKHEQSYAEEDSTMNYNDHDDDADEMNDDEEDVPLAMRKRKQEATDRPDGGMDNDDDDDIPLLARKKVKKEKIKKESKEKSKKRVKEEPSDDYGNVKPKKKKMKKEPEPAVSPGKRQKAKAKVEEEEVWRWWEEEKRADGVKWSTLEHKGPVFAPRYERVPRNVRFYYDGKPLELSEETEEAATFYAKMLNHDYCTKEVFNNNFFKDFRKSMTPREREIIKDFRKCNFQEMFNYFQAESEKRKAASKEEKLIKKNENEALMKEFGFCMIDGHKEKIGNFRLEPPGLFRGRGEHPKMGMIKRRIQASDVSINCGKDSKVPSPPPGSRWKEVRHDNTVTWLASWIENVQGQVKYIMLNPSSKLKGEKDHIKYETARRLDKVIDKIRATYRDEWKSKEMRVRQRAVALYFIDKLALRAGNEKDEDQADTVGCCSLRVEHVQLHKELNGKENVVVFDFPGKDSIRYYNEVEVEKRVFKNLELFMEHKKEGDDLFDRLNTQVLNEHLKELMEGLTAKVFRTYNASKTLQSQLDLLTDPSATVPEKLLAYNRANRAVAILCNHQRSVPKSHEKSMENLKEKIKAKREAIEKCESEYHSRDEKKGKQLERLRDQLKKLELQETDRDENKTIALGTSKLNYLDPRISVAWCKKHDVPIEKIFNKTQRTKFLWAVHMADENYRF

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
280	Phosphorylation	FNNLSQASSCDYSMS HCCHHHHHCCCCCHH	24.70	22817900
281	Phosphorylation	NNLSQASSCDYSMSQ CCHHHHHCCCCCHHH	17.64	22817900
303	Phosphorylation	FVVKHEQSYAEEDST EEEECCCCCCCCCCC	24.27	18327897
304	Phosphorylation	VVKHEQSYAEEDSTM EEECCCCCCCCCCCC	20.09	18327897
409	Phosphorylation	KEPEPAVSPGKRQKA CCCCCCCCCCHHHHH	30.00	19429919
617	Phosphorylation	GKDSKVPSPPPGSRW CCCCCCCCCCCCCCC	53.69	22668510

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of TOP1_DROME !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of TOP1_DROME !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of TOP1_DROME !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PPAN_DROME	ppan	physical	22036573
TOPRS_DROME	Topors	physical	14871887

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Phosphorylation

"Phosphoproteome analysis of Drosophila melanogaster embryos.";
Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
J. Proteome Res. 7:1675-1682(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-303 AND TYR-304, ANDMASS SPECTROMETRY.
PubMed: 18327897