TOP2A_MOUSE - dbPTM
TOP2A_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TOP2A_MOUSE
UniProt AC Q01320
Protein Name DNA topoisomerase 2-alpha
Gene Name Top2a
Organism Mus musculus (Mouse).
Sequence Length 1528
Subcellular Localization Nucleus.
Protein Description Control of topological states of DNA by transient breakage and subsequent rejoining of DNA strands. Topoisomerase II makes double-strand breaks. Essential during mitosis and meiosis for proper segregation of daughter chromosomes. May play a role in regulating the period length of ARNTL/BMAL1 transcriptional oscillation. [PubMed: 24321095]
Protein Sequence MELSPLQPVNENMLMNKKKNEDGKKRLSIERIYQKKTQLEHILLRPDTYIGSVELVTQQMWVYDEDVGINYREVTFVPGLYKIFDEILVNAADNKQRDPKMSCIRVTIDPENNVISIWNNGKGIPVVEHKVEKIYVPALIFGQLLTSSNYDDDEKKVTGGRNGYGAKLCNIFSTKFTVETASREYKKMFKQTWMDNMGRAGDMELKPFSGEDYTCITFQPDLSKFKMQSLDKDIVALMVRRAYDIAGSTKDVKVFLNGNSLPVKGFRSYVDLYLKDKVDETGNSLKVIHEQVNPRWEVCLTMSERGFQQISFVNSIATSKGGRHVDYVADQIVSKLVDVVKKKNKGGVAVKAHQVKNHMWIFVNALIENPTFDSQTKENMTLQAKSFGSTCQLSEKFIKAAIGCGIVESILNWVKFKAQIQLNKKCSAVKHTKIKGIPKLDDANDAGSRNSTECTLILTEGDSAKTLAVSGLGVVGRDKYGVFPLRGKILNVREASHKQIMENAEINNIIKIVGLQYKKNYEDEDSLKTLRYGKIMIMTDQDQDGSHIKGLLINFIHHNWPSLLRHRFLEEFITPIVKVSKNKQEIAFYSLPEFEEWKSSTPNHKKWKVKYYKGLGTSTSKEAKEYFADMKRHRIQFKYSGPEDDAAISLAFSKKQVDDRKEWLTNFMEDRRQRKLLGLPEDYLYGQSTSYLTYNDFINKELILFSNSDNERSIPSMVDGLKPGQRKVLFTCFKRNDKREVKVAQLAGSVAEMSSYHHGEMSLMMTIINLAQNFVGSNNLNLLQPIGQFGTRLHGGKDSASPRYIFTMLSPLARLLFPPKDDHTLRFLYDDNQRVEPEWYIPIIPMVLINGAEGIGTGWSCKIPNFDVREVVNNIRRLLDGEEPLPMLPSYKNFKGTIEELASNQYVINGEVAILDSTTIEISELPIRTWTQTYKEQVLEPMLNGTEKTPSLITDYREYHTDTTVKFVIKMTEEKLAEAERVGLHKVFKLQSSLTCNSMVLFDHVGCLKKYDTVLDILRDFFELRLKYYGLRKEWLLGMLGAESSKLNNQARFILEKIDGKIVIENKPKKELIKVLIQRGYDSDPVKAWKEAQQKVPDEEENEESDTETSTSDSAAEAGPTFNYLLDMPLWYLTKEKKDELCKQRNEKEQELNTLKQKSPSDLWKEDLAVFIEELEVVEAKEKQDEQVGLPGKAGKAKGKKAQMCADVLPSPRGKRVIPQVTVEMKAEAEKKIRKKIKSENVEGTPAEDGAEPGSLRQRIEKKQKKEPGAKKQTTLPFKPVKKGRKKNPWSDSESDVSSNESNVDVPPRQKEQRSAAAKAKFTVDLDSDEDFSGLDEKDEDEDFLPLDATPPKAKIPPKNTKKALKTQGSSMSVVDLESDVKDSVPASPGVPAADFPAETEQSKPSKKTVGVKKTATKSQSSVSTAGTKKRAAPKGTKSDSALSARVSEKPAPAKAKNSRKRKPSSSDSSDSDFERAISKGATSKKAKGEEQDFPVDLEDTIAPRAKSDRARKPIKYLEESDDDDDLF
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
1Acetylation-------MELSPLQP
-------CCCCCCCC
48.18-
4Phosphorylation----MELSPLQPVNE
----CCCCCCCCCCH
27.1926824392
28PhosphorylationEDGKKRLSIERIYQK
CCCCCHHCHHHHHCC
26.8322942356
130UbiquitinationGIPVVEHKVEKIYVP
CCCEEEECCEECCCC
38.2927667366
130AcetylationGIPVVEHKVEKIYVP
CCCEEEECCEECCCC
38.2922826441
155UbiquitinationSNYDDDEKKVTGGRN
CCCCCCCCCCCCCCC
60.58-
156UbiquitinationNYDDDEKKVTGGRNG
CCCCCCCCCCCCCCC
42.87-
229PhosphorylationLSKFKMQSLDKDIVA
HHHHCCCCCCHHHHH
34.7322817900
281PhosphorylationLKDKVDETGNSLKVI
EHHCCCCCCCCEEEE
36.88-
327PhosphorylationKGGRHVDYVADQIVS
CCCCCHHHHHHHHHH
9.1028066266
391S-nitrosocysteineAKSFGSTCQLSEKFI
EHHCCCHHHCCHHHH
4.03-
391S-nitrosylationAKSFGSTCQLSEKFI
EHHCCCHHHCCHHHH
4.0320925432
394PhosphorylationFGSTCQLSEKFIKAA
CCCHHHCCHHHHHHH
16.92-
404S-nitrosocysteineFIKAAIGCGIVESIL
HHHHHHHCCHHHHHH
2.48-
404S-nitrosylationFIKAAIGCGIVESIL
HHHHHHHCCHHHHHH
2.4820925432
409PhosphorylationIGCGIVESILNWVKF
HHCCHHHHHHHHHHH
22.8322817900
448PhosphorylationDDANDAGSRNSTECT
CCCCCCCCCCCCEEE
29.9727841257
459PhosphorylationTECTLILTEGDSAKT
CEEEEEEECCCCCCE
30.8122802335
463PhosphorylationLILTEGDSAKTLAVS
EEEECCCCCCEEEEE
42.3922802335
479AcetylationLGVVGRDKYGVFPLR
EECCCCCCCCCCCCC
42.4123806337
528AcetylationYEDEDSLKTLRYGKI
CCCHHHHHHEEECEE
49.8422826441
580PhosphorylationITPIVKVSKNKQEIA
CHHHEEECCCCCEEE
25.4523737553
601PhosphorylationFEEWKSSTPNHKKWK
HHHHHCCCCCCCCEE
34.8919367708
610AcetylationNHKKWKVKYYKGLGT
CCCCEEEEEECCCCC
38.856571715
621AcetylationGLGTSTSKEAKEYFA
CCCCCCCHHHHHHHH
62.886571661
621UbiquitinationGLGTSTSKEAKEYFA
CCCCCCCHHHHHHHH
62.88-
706PhosphorylationNKELILFSNSDNERS
CCEEEEEECCCCCCC
31.7928066266
708PhosphorylationELILFSNSDNERSIP
EEEEEECCCCCCCCC
40.3828066266
797UbiquitinationGTRLHGGKDSASPRY
CCCCCCCCCCCCHHH
53.77-
996S-nitrosocysteineKLQSSLTCNSMVLFD
HHCCCCCCCCEEEEC
4.27-
996S-nitrosylationKLQSSLTCNSMVLFD
HHCCCCCCCCEEEEC
4.2720925432
1033AcetylationLKYYGLRKEWLLGML
HHHHCCCHHHHHHHH
59.2822826441
1105PhosphorylationDEEENEESDTETSTS
CHHHCCCCCCCCCCC
43.5921149613
1107PhosphorylationEENEESDTETSTSDS
HHCCCCCCCCCCCHH
50.9021149613
1109PhosphorylationNEESDTETSTSDSAA
CCCCCCCCCCCHHHH
39.1221149613
1110PhosphorylationEESDTETSTSDSAAE
CCCCCCCCCCHHHHH
21.4921149613
1111PhosphorylationESDTETSTSDSAAEA
CCCCCCCCCHHHHHH
43.9325159016
1112PhosphorylationSDTETSTSDSAAEAG
CCCCCCCCHHHHHHC
29.3622345495
1114PhosphorylationTETSTSDSAAEAGPT
CCCCCCHHHHHHCCC
29.1922802335
1121PhosphorylationSAAEAGPTFNYLLDM
HHHHHCCCHHHHHHC
24.4822345495
1124PhosphorylationEAGPTFNYLLDMPLW
HHCCCHHHHHHCCHH
12.4022345495
1132PhosphorylationLLDMPLWYLTKEKKD
HHHCCHHHHCHHHHH
16.5122345495
1134PhosphorylationDMPLWYLTKEKKDEL
HCCHHHHCHHHHHHH
22.8222345495
1159PhosphorylationLNTLKQKSPSDLWKE
HHHHHHCCHHHHHHH
27.4328066266
1161PhosphorylationTLKQKSPSDLWKEDL
HHHHCCHHHHHHHHH
53.0428066266
1204OxidationAKGKKAQMCADVLPS
CCCCCCCCHHHCCCC
2.1317242355
1211PhosphorylationMCADVLPSPRGKRVI
CHHHCCCCCCCCCCC
24.0627087446
1238SumoylationKKIRKKIKSENVEGT
HHHHHHHHHCCCCCC
61.6728289178
1239PhosphorylationKIRKKIKSENVEGTP
HHHHHHHHCCCCCCC
37.5725619855
1245PhosphorylationKSENVEGTPAEDGAE
HHCCCCCCCCCCCCC
13.0626824392
1255PhosphorylationEDGAEPGSLRQRIEK
CCCCCCCHHHHHHHH
30.9725619855
1291PhosphorylationGRKKNPWSDSESDVS
CCCCCCCCCCCCCCC
32.3025159016
1293PhosphorylationKKNPWSDSESDVSSN
CCCCCCCCCCCCCCC
33.2225159016
1295PhosphorylationNPWSDSESDVSSNES
CCCCCCCCCCCCCCC
47.4625159016
1298PhosphorylationSDSESDVSSNESNVD
CCCCCCCCCCCCCCC
32.2225159016
1299PhosphorylationDSESDVSSNESNVDV
CCCCCCCCCCCCCCC
44.4525159016
1302PhosphorylationSDVSSNESNVDVPPR
CCCCCCCCCCCCCHH
46.5325159016
1311AcetylationVDVPPRQKEQRSAAA
CCCCHHHHHHHHHHH
58.0323864654
1319AcetylationEQRSAAAKAKFTVDL
HHHHHHHHCCEEEEC
47.5923864654
1323PhosphorylationAAAKAKFTVDLDSDE
HHHHCCEEEECCCCC
16.6521082442
1328PhosphorylationKFTVDLDSDEDFSGL
CEEEECCCCCCCCCC
50.6321082442
1333PhosphorylationLDSDEDFSGLDEKDE
CCCCCCCCCCCCCCC
51.2521082442
1350PhosphorylationDFLPLDATPPKAKIP
CCCCCCCCCCCCCCC
39.5325521595
1367PhosphorylationNTKKALKTQGSSMSV
CHHHHHHHCCCCCEE
38.7321149613
1370PhosphorylationKALKTQGSSMSVVDL
HHHHHCCCCCEEEEC
17.0421082442
1371PhosphorylationALKTQGSSMSVVDLE
HHHHCCCCCEEEECC
23.1522942356
1373PhosphorylationKTQGSSMSVVDLESD
HHCCCCCEEEECCCH
22.4221082442
1379PhosphorylationMSVVDLESDVKDSVP
CEEEECCCHHCCCCC
55.8125159016
1384PhosphorylationLESDVKDSVPASPGV
CCCHHCCCCCCCCCC
25.0422942356
1388PhosphorylationVKDSVPASPGVPAAD
HCCCCCCCCCCCHHH
19.0027087446
1400PhosphorylationAADFPAETEQSKPSK
HHHCCCCCCCCCCCC
41.2425619855
1403PhosphorylationFPAETEQSKPSKKTV
CCCCCCCCCCCCCEE
40.0625619855
1406PhosphorylationETEQSKPSKKTVGVK
CCCCCCCCCCEECEE
50.9925619855
1418AcetylationGVKKTATKSQSSVST
CEEECCCCCCCCCCC
43.9923806337
1419PhosphorylationVKKTATKSQSSVSTA
EEECCCCCCCCCCCC
30.8227841257
1421PhosphorylationKTATKSQSSVSTAGT
ECCCCCCCCCCCCCC
39.5427149854
1422PhosphorylationTATKSQSSVSTAGTK
CCCCCCCCCCCCCCC
16.6727841257
1424PhosphorylationTKSQSSVSTAGTKKR
CCCCCCCCCCCCCCC
17.9425890499
1437PhosphorylationKRAAPKGTKSDSALS
CCCCCCCCCCCCHHH
33.2428066266
1438AcetylationRAAPKGTKSDSALSA
CCCCCCCCCCCHHHH
62.0223806337
1439PhosphorylationAAPKGTKSDSALSAR
CCCCCCCCCCHHHHH
36.3122817900
1441PhosphorylationPKGTKSDSALSARVS
CCCCCCCCHHHHHHC
37.8928066266
1444PhosphorylationTKSDSALSARVSEKP
CCCCCHHHHHHCCCC
17.4726239621
1448PhosphorylationSALSARVSEKPAPAK
CHHHHHHCCCCCCCC
34.0626239621
1450AcetylationLSARVSEKPAPAKAK
HHHHHCCCCCCCCCC
38.6923806337
1465PhosphorylationNSRKRKPSSSDSSDS
CCCCCCCCCCCCCHH
45.5723375375
1466PhosphorylationSRKRKPSSSDSSDSD
CCCCCCCCCCCCHHH
46.8421149613
1467PhosphorylationRKRKPSSSDSSDSDF
CCCCCCCCCCCHHHH
45.9421149613
1469PhosphorylationRKPSSSDSSDSDFER
CCCCCCCCCHHHHHH
37.6821149613
1470PhosphorylationKPSSSDSSDSDFERA
CCCCCCCCHHHHHHH
46.2321149613
1472PhosphorylationSSSDSSDSDFERAIS
CCCCCCHHHHHHHHH
46.2627149854
1501PhosphorylationFPVDLEDTIAPRAKS
CCCCHHHCCCCCCCC
15.0625619855
1517PhosphorylationRARKPIKYLEESDDD
CCCCCCCCCCCCCCC
21.7725619855
1521PhosphorylationPIKYLEESDDDDDLF
CCCCCCCCCCCCCCC
36.6427087446

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
1105SPhosphorylationKinaseCK1-Uniprot

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
1105SPhosphorylation

-

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 TOP2A_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of TOP2A_MOUSE !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TOP2A_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,Thibault P.;
Immunity 30:143-154(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28, AND MASSSPECTROMETRY.
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1333, AND MASSSPECTROMETRY.
"A differential phosphoproteomic analysis of retinoic acid-treated P19cells.";
Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.;
J. Proteome Res. 6:3174-3186(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1367; SER-1370;SER-1371; SER-1373; SER-1379; SER-1465; SER-1466; SER-1467; SER-1469;SER-1470 AND SER-1472, AND MASS SPECTROMETRY.

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