Search Results

Overview

Uniprot IDQ02880
Protein NameDNA topoisomerase 2-beta
Gene NameTOP2B
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
1214 VLAGMSGKAIKGKVG
1217 GMSGKAIKGKVGKPK
1227 VGKPKVKKLQLEETM
1262 KKLLKKKKGDLDTAA
1429 TFSPGKSKATPEKSL
1434 KSKATPEKSLHDKKS
1486 FGLKQTDKVPSKTVA
1490 QTDKVPSKTVAAKKG
1548 GRGAKKRKASGSENE
367 EVVKKKNKAGVSVKP
439 ILNWVKFKAQTQLNK
471 DANDAGGKHSLECTL
635 AWKIKYYKGLGTSTA

Function

Key decatenating enzyme that alters DNA topology by binding to two double-stranded DNA molecules, generating a double-stranded break in one of the strands, passing the intact strand through the broken strand, and religating the broken strand. Plays a role in B-cell differentiation

Protein Sequence

10 MAKSGGCGAG 20 AGVGGGNGAL 30 TWVTLFDQNN 40 AAKKEESETA 50 NKNDSSKKLS 60 VERVYQKKTQ 70 LEHILLRPDT 80 YIGSVEPLTQ 90 FMWVYDEDVG 100 MNCREVTFVP 110 GLYKIFDEIL 120 VNAADNKQRD 130 KNMTCIKVSI 140 DPESNIISIW 150 NNGKGIPVVE 160 HKVEKVYVPA 170 LIFGQLLTSS 180 NYDDDEKKVT 190 GGRNGYGAKL 200 CNIFSTKFTV 210 ETACKEYKHS 220 FKQTWMNNMM 230 KTSEAKIKHF 240 DGEDYTCITF 250 QPDLSKFKME 260 KLDKDIVALM 270 TRRAYDLAGS 280 CRGVKVMFNG 290 KKLPVNGFRS 300 YVDLYVKDKL 310 DETGVALKVI 320 HELANERWDV 330 CLTLSEKGFQ 340 QISFVNSIAT 350 TKGGRHVDYV 360 VDQVVGKLIE 370 VVKKKNKAGV 380 SVKPFQVKNH 390 IWVFINCLIE 400 NPTFDSQTKE 410 NMTLQPKSFG 420 SKCQLSEKFF 430 KAASNCGIVE 440 SILNWVKFKA 450 QTQLNKKCSS 460 VKYSKIKGIP 470 KLDDANDAGG 480 KHSLECTLIL 490 TEGDSAKSLA 500 VSGLGVIGRD 510 RYGVFPLRGK 520 ILNVREASHK 530 QIMENAEINN 540 IIKIVGLQYK 550 KSYDDAESLK 560 TLRYGKIMIM 570 TDQDQDGSHI 580 KGLLINFIHH 590 NWPSLLKHGF 600 LEEFITPIVK 610 ASKNKQELSF 620 YSIPEFDEWK 630 KHIENQKAWK 640 IKYYKGLGTS 650 TAKEAKEYFA 660 DMERHRILFR 670 YAGPEDDAAI 680 TLAFSKKKID 690 DRKEWLTNFM 700 EDRRQRRLHG 710 LPEQFLYGTA 720 TKHLTYNDFI 730 NKELILFSNS 740 DNERSIPSLV 750 DGFKPGQRKV 760 LFTCFKRNDK 770 REVKVAQLAG 780 SVAEMSAYHH 790 GEQALMMTIV 800 NLAQNFVGSN 810 NINLLQPIGQ 820 FGTRLHGGKD 830 AASPRYIFTM 840 LSTLARLLFP 850 AVDDNLLKFL 860 YDDNQRVEPE 870 WYIPIIPMVL 880 INGAEGIGTG 890 WACKLPNYDA 900 REIVNNVRRM 910 LDGLDPHPML 920 PNYKNFKGTI 930 QELGQNQYAV 940 SGEIFVVDRN 950 TVEITELPVR 960 TWTQVYKEQV 970 LEPMLNGTDK 980 TPALISDYKE 990 YHTDTTVKFV 1000 VKMTEEKLAQ 1010 AEAAGLHKVF 1020 KLQTTLTCNS 1030 MVLFDHMGCL 1040 KKYETVQDIL 1050 KEFFDLRLSY 1060 YGLRKEWLVG 1070 MLGAESTKLN 1080 NQARFILEKI 1090 QGKITIENRS 1100 KKDLIQMLVQ 1110 RGYESDPVKA 1120 WKEAQEKAAE 1130 EDETQNQHDD 1140 SSSDSGTPSG 1150 PDFNYILNMS 1160 LWSLTKEKVE 1170 ELIKQRDAKG 1180 REVNDLKRKS 1190 PSDLWKEDLA 1200 AFVEELDKVE 1210 SQEREDVLAG 1220 MSGKAIKGKV 1230 GKPKVKKLQL 1240 EETMPSPYGR 1250 RIIPEITAMK 1260 ADASKKLLKK 1270 KKGDLDTAAV 1280 KVEFDEEFSG 1290 APVEGAGEEA 1300 LTPSVPINKG 1310 PKPKREKKEP 1320 GTRVRKTPTS 1330 SGKPSAKKVK 1340 KRNPWSDDES 1350 KSESDLEETE 1360 PVVIPRDSLL 1370 RRAAAERPKY 1380 TFDFSEEEDD 1390 DADDDDDDNN 1400 DLEELKVKAS 1410 PITNDGEDEF 1420 VPSDGLDKDE 1430 YTFSPGKSKA 1440 TPEKSLHDKK 1450 SQDFGNLFSF 1460 PSYSQKSEDD 1470 SAKFDSNEED 1480 SASVFSPSFG 1490 LKQTDKVPSK 1500 TVAAKKGKPS 1510 SDTVPKPKRA 1520 PKQKKVVEAV 1530 NSDSDSEFGI 1540 PKKTTTPKGK 1550 GRGAKKRKAS 1560 GSENEGDYNP 1570 GRKTSKTTSK 1580 KPKKTSFDQD 1590 SDVDIFPSDF 1600 PTEPPSLPRT 1610 GRARKEVKYF 1620 AESDEEEDDV DFAMFN

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005829 cytosol
Cellular Component GO:0005730 nucleolus
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Cellular Component GO:1990904 ribonucleoprotein complex
Molecular Function GO:0005524 ATP binding
Molecular Function GO:0003682 chromatin binding
Molecular Function GO:0003677 DNA binding
Molecular Function GO:0003918 DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity
Molecular Function GO:0046872 metal ion binding
Molecular Function GO:0043021 ribonucleoprotein complex binding
Biological Process GO:0030183 B cell differentiation
Biological Process GO:0071318 cellular response to ATP
Biological Process GO:0070301 cellular response to hydrogen peroxide
Biological Process GO:0090398 cellular senescence
Biological Process GO:0006265 DNA topological change
Biological Process GO:2001034 positive regulation of double-strand break repair via nonhomologous end joining
Biological Process GO:0045870 positive regulation of single stranded viral RNA replication via double stranded DNA intermediate
Biological Process GO:0000712 resolution of meiotic recombination intermediates
Biological Process GO:0000819 sister chromatid segregation

Reference

[1] Yang D, Yin J, Shan L, Yi X, Zhang W et al.. Identification of lysine-lactylated substrates in gastric cancer cells.. iScience 25(7):104630. 2022 Jul 15. PMID: 35800753.

[2] Hong H, Chen X, Wang H, Gu X, Yuan Y et al.. Global profiling of protein lysine lactylation and potential target modified protein analysis in hepatocellular carcinoma.. Proteomics 23(9):e2200432. 2023 May. PMID: 36625413.

[3] He C, Zhang J, Bai X, Lu C, Zhang K. Lysine lactylation-based insight to understanding the characterization of cervical cancer.. Biochim Biophys Acta Mol Basis Dis 1870(7):167356. 2024 Oct. PMID: 39025375.

[4] Bao Q, Wan N, He Z, Cao J, Yuan W et al.. Subcellular Proteomic Mapping of Lysine Lactylation.. J Am Soc Mass Spectrom 35(12):3221-3232. 2024 Dec 4. PMID: 39569522.

[5] Guo X, Ren X, Yan C, Huang H. Quantitative Proteomics Reveals the Role of Lysine Lactylation in Lenalidomide-Resistance in Multiple Myeloma Cells.. ACS Chem Biol 20(7):1728-1738. 2025 Jul 18. PMID: 40590393.

[6] He J, Lai T, Zhou Z, Yang H, Lei Z et al.. Multiomics profiling reveals the involvement of protein lactylation in nonhomologous end joining pathway conferring radioresistance in lung adenocarcinoma cell.. Sci Rep 15(1):24651. 2025 Jul 9. PMID: 40634431.

[7] Wu Q, Li Z, Gong T, Zheng X, Zhou X et al.. Porphyromonas gingivalis infection induces lysine lactylation reprogramming in human umbilical vein endothelial cells.. Front Cell Infect Microbiol 16:1706727. 2026. PMID: 41696360.