TOP2B_MOUSE - dbPTM
TOP2B_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TOP2B_MOUSE
UniProt AC Q64511
Protein Name DNA topoisomerase 2-beta
Gene Name Top2b
Organism Mus musculus (Mouse).
Sequence Length 1612
Subcellular Localization Nucleus, nucleolus.
Protein Description Control of topological states of DNA by transient breakage and subsequent rejoining of DNA strands. Topoisomerase II makes double-strand breaks..
Protein Sequence MAKSSLAGSDGALTWVNNATKKEELETANKNDSTKKLSVERVYQKKTQLEHILLRPDTYIGSVEPLTQLMWVYDEDVGMNCREVTFVPGLYKIFDEILVNAADNKQRDKNMTCIKVSIDPESNIISIWNNGKGIPVVEHKVEKVYVPALIFGQLLTSSNYDDDEKKVTGGRNGYGAKLCNIFSTKFTVETACKEYKHSFKQTWMNNMMKTSEAKIKHFDGEDYTCITFQPDLSKFKMEKLDKDIVALMTRRAYDLAGSCKGVKVMFNGKKLPVNGFRSYVDLYVKDKLDETGVALKVIHELANERWDVCLTLSEKGFQQISFVNSIATTKGGRHVDYVVDQVVSKLIEVVKKKNKAGVSVKPFQVKNHIWVFINCLIENPTFDSQTKENMTLQPKSFGSKCQLSEKFFKAASNCGIVESILNWVKFKAQTQLNKKCSSVKYSKIKGIPKLDDANDAGGKHSLECTLILTEGDSAKSLAVSGLGVIGRDRYGVFPLRGKILNVREASHKQIMENAEINNIIKIVGLQYKKSYDDAESLKTLRYGKIMIMTDQDQDGSHIKGLLINFIHHNWPSLLKHGFLEEFITPIVKASKNKQELSFYSIPEFDEWKKHIENQKAWKIKYYKGLGTSTAKEAKEYFADMERHRILFRYAGPEDDAAITLAFSKKKIDDRKEWLTNFMEDRRQRRLHGLPEQFLYGTATKHLTYNDFINKELILFSNSDNERSIPSLVDGFKPGQRKVLFTCFKRNDKREVKVAQLAGSVAEMSAYHHGEQALMMTIVNLAQNFVGSNNINLLQPIGQFGTRLHGGKDAASPRYIFTMLSSLARLLFPAVDDNLLKFLYDDNQRVEPEWYIPIIPMVLINGAEGIGTGWACKLPNYDAREIVNNVRRMLEGLDPHPMLPNYKNFKGTIQELGQNQYAVSGEIFVVDRNTVEITELPVRTWTQVYKEQVLEPMLNGTDKTPALISDYKEYHTDTTVKFVVKMTEEKLAQAEAAGLHKVFKLQTTLTCNSMVLFDHMGCLKKYETVQDILKEFFDLRLSYYGLRKEWLVGMLGAESTKLNNQARFILEKIQGKITIENRSKKDLIQMLVQRGYESDPVKAWKEAQEKAAEEEDSQNQHDDSSSDSGTPSGPDFNYILNMSLWSLTKEKVEELIKQRDTKGREVNDLKRKSPSDLWKEDLAAFVEELDKVEAQEREDILAGMSGKAIKGKVGKPKVKKLQLEETMPSPYGRRIVPEITAMKADASRKLLKKKKGDPDTTVVKVEFDEEFSGTPAEGTGEETLTPSAPVNKGPKPKREKKEPGTRVRKTPTSTGKTNAKKVKKRNPWSDDESKSESDLEEAEPVVIPRDSLLRRAAAERPKYTFDFSEEEDDDAAAADDSNDLEELKVKASPITNDGEDEFVPSDGLDKDEYAFSSGKSKATPEKSSNDKKSQDFGNLFSFPSYSQKSEDDSAKFDSNEEDTASVFAPSFGLKQTDKLPSKTVAAKKGKPPSDTAPKAKRAPKQKKIVETINSDSDSEFGIPKKTTTPKGKGRGAKKRKASGSENEGDYNPGRKPSKTASKKPKKTSFDQDSDVDIFPSDFTSEPPALPRTGRARKEVKYFAESDEEEDVDFAMFN
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
2Acetylation------MAKSSLAGS
------CCCCCCCCC
31.5723806337
3Acetylation-----MAKSSLAGSD
-----CCCCCCCCCC
53.0623806337
4Phosphorylation----MAKSSLAGSDG
----CCCCCCCCCCC
37.3326643407
5Phosphorylation---MAKSSLAGSDGA
---CCCCCCCCCCCC
22.8726643407
9PhosphorylationAKSSLAGSDGALTWV
CCCCCCCCCCCHHHC
27.5426643407
14PhosphorylationAGSDGALTWVNNATK
CCCCCCHHHCCCCCC
27.1722802335
20PhosphorylationLTWVNNATKKEELET
HHHCCCCCCHHHHHH
44.7822802335
21AcetylationTWVNNATKKEELETA
HHCCCCCCHHHHHHC
56.6422826441
263MalonylationAGSCKGVKVMFNGKK
HCCCCEEEEEECCEE
36.3326320211
414S-nitrosylationFFKAASNCGIVESIL
HHHHHHCCCHHHHHH
3.4920925432
414S-nitrosocysteineFFKAASNCGIVESIL
HHHHHHCCCHHHHHH
3.49-
419PhosphorylationSNCGIVESILNWVKF
HCCCHHHHHHHHHHH
22.8317203969
529MalonylationIVGLQYKKSYDDAES
HHCEEECCCCCCHHH
49.6826320211
538AcetylationYDDAESLKTLRYGKI
CCCHHHHHHCCCCEE
55.5922826441
627PhosphorylationKYYKGLGTSTAKEAK
EEECCCCCCCHHHHH
28.1317203969
716PhosphorylationNKELILFSNSDNERS
CCEEEEEECCCCCCC
31.7928066266
718PhosphorylationELILFSNSDNERSIP
EEEEEECCCCCCCCC
40.3828066266
764PhosphorylationAGSVAEMSAYHHGEQ
HHHHHHHHHCHHHHH
19.7222802335
766PhosphorylationSVAEMSAYHHGEQAL
HHHHHHHCHHHHHHH
6.2422802335
776PhosphorylationGEQALMMTIVNLAQN
HHHHHHHHHHHHHHH
14.0622802335
787PhosphorylationLAQNFVGSNNINLLQ
HHHHCCCCCCCCEEE
22.7722802335
969PhosphorylationLISDYKEYHTDTTVK
HHHCHHHHCCCCEEE
13.0828576409
1039PhosphorylationFDLRLSYYGLRKEWL
HHHHHHHHHCCHHHH
13.3029109428
1120PhosphorylationQNQHDDSSSDSGTPS
CCCCCCCCCCCCCCC
45.2029899451
1121PhosphorylationNQHDDSSSDSGTPSG
CCCCCCCCCCCCCCC
39.4829899451
1123PhosphorylationHDDSSSDSGTPSGPD
CCCCCCCCCCCCCCC
46.6529899451
1125PhosphorylationDSSSDSGTPSGPDFN
CCCCCCCCCCCCCHH
20.4529899451
1127PhosphorylationSSDSGTPSGPDFNYI
CCCCCCCCCCCHHHH
63.9027600695
1133PhosphorylationPSGPDFNYILNMSLW
CCCCCHHHHHHHHHH
13.5327600695
1168PhosphorylationVNDLKRKSPSDLWKE
HHHHHHCCHHHHHHH
33.4028066266
1170PhosphorylationDLKRKSPSDLWKEDL
HHHHCCHHHHHHHHH
53.0428066266
1200PhosphorylationEDILAGMSGKAIKGK
HHHHHHCCCCHHCCC
35.9028066266
1202AcetylationILAGMSGKAIKGKVG
HHHHCCCCHHCCCCC
39.3623806337
1221PhosphorylationKKLQLEETMPSPYGR
CEEECEECCCCCCCC
25.6326643407
1224PhosphorylationQLEETMPSPYGRRIV
ECEECCCCCCCCCCH
21.6726745281
1226PhosphorylationEETMPSPYGRRIVPE
EECCCCCCCCCCHHH
27.8326745281
1267PhosphorylationVEFDEEFSGTPAEGT
EEECCCCCCCCCCCC
45.0725619855
1269PhosphorylationFDEEFSGTPAEGTGE
ECCCCCCCCCCCCCC
20.3725619855
1274PhosphorylationSGTPAEGTGEETLTP
CCCCCCCCCCCCCCC
32.6925293948
1278PhosphorylationAEGTGEETLTPSAPV
CCCCCCCCCCCCCCC
31.4625293948
1280PhosphorylationGTGEETLTPSAPVNK
CCCCCCCCCCCCCCC
23.7126824392
1282PhosphorylationGEETLTPSAPVNKGP
CCCCCCCCCCCCCCC
39.7125293948
1300PhosphorylationREKKEPGTRVRKTPT
CCCCCCCCCCCCCCC
36.3820531401
1304AcetylationEPGTRVRKTPTSTGK
CCCCCCCCCCCCCCC
56.8719852639
1305PhosphorylationPGTRVRKTPTSTGKT
CCCCCCCCCCCCCCC
22.6421183079
1308PhosphorylationRVRKTPTSTGKTNAK
CCCCCCCCCCCCCCC
36.0421183079
1311AcetylationKTPTSTGKTNAKKVK
CCCCCCCCCCCCHHH
38.4023806337
1315AcetylationSTGKTNAKKVKKRNP
CCCCCCCCHHHHCCC
61.2319852651
1316AcetylationTGKTNAKKVKKRNPW
CCCCCCCHHHHCCCC
57.8019852663
1324PhosphorylationVKKRNPWSDDESKSE
HHHCCCCCCCCCCCH
36.1225521595
1328PhosphorylationNPWSDDESKSESDLE
CCCCCCCCCCHHHHH
48.7725521595
1330PhosphorylationWSDDESKSESDLEEA
CCCCCCCCHHHHHHC
52.1721082442
1332PhosphorylationDDESKSESDLEEAEP
CCCCCCHHHHHHCCC
55.3725521595
1346PhosphorylationPVVIPRDSLLRRAAA
CEEECHHHHHHHHHH
30.50-
1358PhosphorylationAAAERPKYTFDFSEE
HHHHCCCEEECCCHH
18.4724925903
1359PhosphorylationAAERPKYTFDFSEEE
HHHCCCEEECCCHHC
23.8924925903
1363PhosphorylationPKYTFDFSEEEDDDA
CCEEECCCHHCCCCH
46.0424925903
1376PhosphorylationDAAAADDSNDLEELK
CHHCCCCCCCHHHHC
32.5624925903
1387PhosphorylationEELKVKASPITNDGE
HHHCCCEECCCCCCC
15.8927087446
1390PhosphorylationKVKASPITNDGEDEF
CCCEECCCCCCCCCC
30.5525521595
1400PhosphorylationGEDEFVPSDGLDKDE
CCCCCCCCCCCCCCH
38.7227087446
1408PhosphorylationDGLDKDEYAFSSGKS
CCCCCCHHHHCCCCC
24.0721082442
1411PhosphorylationDKDEYAFSSGKSKAT
CCCHHHHCCCCCCCC
29.9723375375
1412PhosphorylationKDEYAFSSGKSKATP
CCHHHHCCCCCCCCC
43.7321082442
1422PhosphorylationSKATPEKSSNDKKSQ
CCCCCCCCCCCCCCC
32.4826745281
1423PhosphorylationKATPEKSSNDKKSQD
CCCCCCCCCCCCCCC
61.1826745281
1428PhosphorylationKSSNDKKSQDFGNLF
CCCCCCCCCCCHHCC
40.5028833060
1436PhosphorylationQDFGNLFSFPSYSQK
CCCHHCCCCCCCCCC
39.1428833060
1439PhosphorylationGNLFSFPSYSQKSED
HHCCCCCCCCCCCCC
35.0921082442
1440PhosphorylationNLFSFPSYSQKSEDD
HCCCCCCCCCCCCCC
18.5028833060
1441PhosphorylationLFSFPSYSQKSEDDS
CCCCCCCCCCCCCCC
35.1528833060
1444PhosphorylationFPSYSQKSEDDSAKF
CCCCCCCCCCCCCCC
38.3227087446
1448PhosphorylationSQKSEDDSAKFDSNE
CCCCCCCCCCCCCCH
45.7622942356
1453PhosphorylationDDSAKFDSNEEDTAS
CCCCCCCCCHHHHHH
49.6427087446
1458PhosphorylationFDSNEEDTASVFAPS
CCCCHHHHHHHCCHH
24.9017203969
1460PhosphorylationSNEEDTASVFAPSFG
CCHHHHHHHCCHHHC
21.6227087446
1465PhosphorylationTASVFAPSFGLKQTD
HHHHCCHHHCCCCCC
28.6325619855
1506PhosphorylationKQKKIVETINSDSDS
CHHHHEEECCCCCCC
17.9824925903
1509PhosphorylationKIVETINSDSDSEFG
HHEEECCCCCCCCCC
34.3427087446
1511PhosphorylationVETINSDSDSEFGIP
EEECCCCCCCCCCCC
42.7427087446
1513PhosphorylationTINSDSDSEFGIPKK
ECCCCCCCCCCCCCC
38.4824925903
1521PhosphorylationEFGIPKKTTTPKGKG
CCCCCCCCCCCCCCC
41.8724759943
1522PhosphorylationFGIPKKTTTPKGKGR
CCCCCCCCCCCCCCC
50.4024759943
1523PhosphorylationGIPKKTTTPKGKGRG
CCCCCCCCCCCCCCC
28.3825367039
1535AcetylationGRGAKKRKASGSENE
CCCCCCCCCCCCCCC
56.647627767
1537PhosphorylationGAKKRKASGSENEGD
CCCCCCCCCCCCCCC
45.9827087446
1539PhosphorylationKKRKASGSENEGDYN
CCCCCCCCCCCCCCC
34.4527087446
1545PhosphorylationGSENEGDYNPGRKPS
CCCCCCCCCCCCCCC
33.8328833060
1552PhosphorylationYNPGRKPSKTASKKP
CCCCCCCCCCCCCCC
45.7526745281
1553AcetylationNPGRKPSKTASKKPK
CCCCCCCCCCCCCCC
57.5519855909
1557AcetylationKPSKTASKKPKKTSF
CCCCCCCCCCCCCCC
71.3019855921
1558AcetylationPSKTASKKPKKTSFD
CCCCCCCCCCCCCCC
60.6219855933
1562PhosphorylationASKKPKKTSFDQDSD
CCCCCCCCCCCCCCC
40.5327087446
1563PhosphorylationSKKPKKTSFDQDSDV
CCCCCCCCCCCCCCC
35.3925521595
1568PhosphorylationKTSFDQDSDVDIFPS
CCCCCCCCCCCCCCC
33.6227087446
1575PhosphorylationSDVDIFPSDFTSEPP
CCCCCCCCCCCCCCC
34.3124925903
1578PhosphorylationDIFPSDFTSEPPALP
CCCCCCCCCCCCCCC
36.8525619855
1579PhosphorylationIFPSDFTSEPPALPR
CCCCCCCCCCCCCCC
48.3625619855
1596PhosphorylationRARKEVKYFAESDEE
CCHHHCEEHHCCCCC
17.1325619855
1600PhosphorylationEVKYFAESDEEEDVD
HCEEHHCCCCCCCCC
47.0624925903

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 TOP2B_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TOP2B_MOUSE !!

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 TOP2B_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ZN451_HUMANZNF451physical
20360068
TOP2A_HUMANTOP2Aphysical
20360068
ITPR1_HUMANITPR1physical
20360068
TOP2B_HUMANTOP2Bphysical
20360068

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TOP2B_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large scale localization of protein phosphorylation by use ofelectron capture dissociation mass spectrometry.";
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
Mol. Cell. Proteomics 8:904-912(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1453; SER-1509 ANDSER-1511, AND MASS SPECTROMETRY.
"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-1509, 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-1324; SER-1328;SER-1330; SER-1332; SER-1387; SER-1509; SER-1511; SER-1537 ANDSER-1539, AND MASS SPECTROMETRY.
"Large-scale phosphorylation analysis of mouse liver.";
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1387; SER-1453;SER-1509; SER-1511; SER-1513; SER-1537 AND SER-1539, AND MASSSPECTROMETRY.
"Protein phosphorylation and expression profiling by Yin-yangmultidimensional liquid chromatography (Yin-yang MDLC) massspectrometry.";
Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
J. Proteome Res. 6:250-262(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-419; THR-627; SER-1387;SER-1400; SER-1453 AND THR-1458, AND MASS SPECTROMETRY.

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