TOP2_DROME - dbPTM
TOP2_DROME - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TOP2_DROME
UniProt AC P15348
Protein Name DNA topoisomerase 2 {ECO:0000305}
Gene Name Top2 {ECO:0000303|PubMed:25340780, ECO:0000312|FlyBase:FBgn0284220}
Organism Drosophila melanogaster (Fruit fly).
Sequence Length 1447
Subcellular Localization Nucleus . Chromosome . Cytoplasm . Nuclear at interphase, becoming diffusely dispersed in the cytoplasm at later cell cycle stages (PubMed:10885744, PubMed:10751154). However in early developing embryos, some may remain associated with condensed chro
Protein Description Control of topological states of DNA by transient breakage and subsequent rejoining of DNA strands. [PubMed: 6308011]
Protein Sequence MENGNKALSIEQMYQKKSQLEHILLRPDSYIGSVEFTKELMWVYDNSQNRMVQKEISFVPGLYKIFDEILVNAADNKQRDKSMNTIKIDIDPERNMVSVWNNGQGIPVTMHKEQKMYVPTMIFGHLLTSSNYNDDEKKVTGGRNGYGAKLCNIFSTSFTVETATREYKKSFKQTWGNNMGKASDVQIKDFNGTDYTRITFSPDLAKFKMDRLDEDIVALMSRRAYDVAASSKGVSVFLNGNKLGVRNFKDYIDLHIKNTDDDSGPPIKIVHEVANERWEVACCPSDRGFQQVSFVNSIATYKGGRHVDHVVDNLIKQLLEVLKKKNKGGINIKPFQVRNHLWVFVNCLIENPTFDSQTKENMTLQQKGFGSKCTLSEKFINNMSKSGIVESVLAWAKFKAQNDIAKTGGRKSSKIKGIPKLEDANEAGGKNSIKCTLILTEGDSAKSLAVSGLGVIGRDLYGVFPLRGKLLNVREANFKQLSENAEINNLCKIIGLQYKKKYLTEDDLKTLRYGKVMIMTDQDQDGSHIKGLLINFIHTNWPELLRLPFLEEFITPIVKATKKNEELSFYSLPEFEEWKNDTANHHTYNIKYYKGLGTSTSKEAKEYFQDMDRHRILFKYDGSVDDESIVMAFSKKHIESRKVWLTNHMDEVKRRKELGLPERYLYTKGTKSITYADFINLELVLFSNADNERSIPSLVDGLKPGQRKVMFTCFKRNDKREVKVAQLSGSVAEMSAYHHGEVSLQMTIVNLAQNFVGANNINLLEPRGQFGTRLSGGKDCASARYIFTIMSPLTRLIYHPLDDPLLDYQVDDGQKIEPLWYLPIIPMVLVNGAEGIGTGWSTKISNYNPREIMKNLRKMINGQEPSVMHPWYKNFLGRMEYVSDGRYIQTGNIQILSGNRLEISELPVGVWTQNYKENVLEPLSNGTEKVKGIISEYREYHTDTTVRFVISFAPGEFERIHAEEGGFYRVFKLTTTLSTNQMHAFDQNNCLRRFPTAIDILKEYYKLRREYYARRRDFLVGQLTAQADRLSDQARFILEKCEKKLVVENKQRKAMCDELLKRGYRPDPVKEWQRRIKMEDAEQADEEDEEEEEAAPSVSSKAKKEKEVDPEKAFKKLTDVKKFDYLLGMSMWMLTEEKKNELLKQRDTKLSELESLRKKTPEMLWLDDLDALESKLNEVEEKERAEEQGINLKTAKALKGQKSASAKGRKVKSMGGGAGAGDVFPDPDGEPVEFKITEEIIKKMAAAAKVAQAAKEPKKPKEPKEPKVKKEPKGKQIKAEPDASGDEVDEFDAMVEGGSKTSPKAKKAVVKKEPGEKKPRQKKENGGGLKQSKIDFSKAKAKKSDDDVEEVTPRAERPGRRQASKKIDYSSLFSDEEEDGGNVGSDDDGNASDDDSPKRPAKRGREDESSGGAKKKAPPKKRRAVIESDDDDIEIDEDDDDDSDFNC
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 Orthologous
Protein Cluster
263PhosphorylationIKNTDDDSGPPIKIV
EECCCCCCCCCCEEE
61.2627626673
333AcetylationNKGGINIKPFQVRNH
CCCCCCCCCEEECCE
34.9821791702
333AcetylationNKGGINIKPFQVRNH
CCCCCCCCCEEECCE
34.98-
509AcetylationYLTEDDLKTLRYGKV
CCCHHHHHHCCCCCE
53.13-
509AcetylationYLTEDDLKTLRYGKV
CCCHHHHHHCCCCCE
53.1321791702
1061AcetylationAMCDELLKRGYRPDP
HHHHHHHHCCCCCCH
57.30-
1061AcetylationAMCDELLKRGYRPDP
HHHHHHHHCCCCCCH
57.3021791702
1064PhosphorylationDELLKRGYRPDPVKE
HHHHHCCCCCCHHHH
24.0122817900
1213PhosphorylationAKGRKVKSMGGGAGA
CCCCCCEECCCCCCC
26.1619429919
1284PhosphorylationIKAEPDASGDEVDEF
CCCCCCCCCCCCCCC
54.9121082442
1299PhosphorylationDAMVEGGSKTSPKAK
HHHCCCCCCCCHHHH
43.5519429919
1301PhosphorylationMVEGGSKTSPKAKKA
HCCCCCCCCHHHHHH
52.5422668510
1302PhosphorylationVEGGSKTSPKAKKAV
CCCCCCCCHHHHHHH
28.3019429919
1344PhosphorylationSKAKAKKSDDDVEEV
HHHHCCCCCCCHHHC
45.6319429919
1352PhosphorylationDDDVEEVTPRAERPG
CCCHHHCCCCCCCCC
15.4419429919
1369PhosphorylationQASKKIDYSSLFSDE
CCCCCCCHHHHCCCC
12.0219429919
1370PhosphorylationASKKIDYSSLFSDEE
CCCCCCHHHHCCCCC
19.4719429919
1371PhosphorylationSKKIDYSSLFSDEEE
CCCCCHHHHCCCCCC
27.4919429919
1374PhosphorylationIDYSSLFSDEEEDGG
CCHHHHCCCCCCCCC
49.7819429919
1385PhosphorylationEDGGNVGSDDDGNAS
CCCCCCCCCCCCCCC
33.3219429919
1392PhosphorylationSDDDGNASDDDSPKR
CCCCCCCCCCCCCCC
45.6419429919
1396PhosphorylationGNASDDDSPKRPAKR
CCCCCCCCCCCCHHC
39.0419429919
1409PhosphorylationKRGREDESSGGAKKK
HCCCCCCCCCCCCCC
46.7530478224
1410PhosphorylationRGREDESSGGAKKKA
CCCCCCCCCCCCCCC
38.9230478224
1428PhosphorylationKRRAVIESDDDDIEI
HCCEEEECCCCCCCC
34.9021082442
1443PhosphorylationDEDDDDDSDFNC---
CCCCCCCCCCCC---
51.6121082442

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 TOP2_DROME !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TOP2_DROME !!

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 TOP2_DROME !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MOF_DROMEmofgenetic
25340516
ATR_DROMEmei-41genetic
25340516
ATM_DROMEtefugenetic
25340516
PHP_DROMEph-pphysical
11172718
MSL1_DROMEmsl-1physical
25694028
TOP2_DROMETop2physical
11447119
MLE_DROMEmlephysical
25694028
ISWI_DROMEIswiphysical
9252192
MMD4_DROMEmod(mdg4)physical
21304601

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TOP2_DROME

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-1284; SER-1344;THR-1352; SER-1374; SER-1385; SER-1392 AND SER-1396, AND MASSSPECTROMETRY.

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