Search Results

Overview

Uniprot IDP11388
Protein NameDNA topoisomerase 2-alpha
Gene NameTOP2A
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
1011 DHVGCLKKYDTVLDI
1028 DFFELRLKYYGLRKE
1196 EQVGLPGKGGKAKGK
1199 GLPGKGGKAKGKKTQ
1203 KGGKAKGKKTQMAEV
1204 GGKAKGKKTQMAEVL
1276 EPGTKTKKQTTLAFK
1283 KQTTLAFKPIKKGKK
1287 LAFKPIKKGKKRNPW
1367 TSPKLSNKELKPQKS
1370 KLSNKELKPQKSVVS
1373 NKELKPQKSVVSDLE
1422 TVKKTAAKSQSSTST
1459 SQKPDPAKTKNRRKR
1484 NFEKIVSKAVTSKKS
1490 SKAVTSKKSKGESDD
1492 AVTSKKSKGESDDFH
17 NENMQVNKIKKNEDA
418 ILNWVKFKAQVQLNK
425 KAQVQLNKKCSAVKH
426 AQVQLNKKCSAVKHN
480 LGVVGRDKYGVFPLR
489 GVFPLRGKILNVREA
614 KWKVKYYKGLGTSTS

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 (PubMed:17567603, PubMed:18790802, PubMed:22013166, PubMed:22323612, PubMed:27754753). May play a role in regulating the period length of BMAL1 transcriptional oscillation (By similarity)

Protein Sequence

10 MEVSPLQPVN 20 ENMQVNKIKK 30 NEDAKKRLSV 40 ERIYQKKTQL 50 EHILLRPDTY 60 IGSVELVTQQ 70 MWVYDEDVGI 80 NYREVTFVPG 90 LYKIFDEILV 100 NAADNKQRDP 110 KMSCIRVTID 120 PENNLISIWN 130 NGKGIPVVEH 140 KVEKMYVPAL 150 IFGQLLTSSN 160 YDDDEKKVTG 170 GRNGYGAKLC 180 NIFSTKFTVE 190 TASREYKKMF 200 KQTWMDNMGR 210 AGEMELKPFN 220 GEDYTCITFQ 230 PDLSKFKMQS 240 LDKDIVALMV 250 RRAYDIAGST 260 KDVKVFLNGN 270 KLPVKGFRSY 280 VDMYLKDKLD 290 ETGNSLKVIH 300 EQVNHRWEVC 310 LTMSEKGFQQ 320 ISFVNSIATS 330 KGGRHVDYVA 340 DQIVTKLVDV 350 VKKKNKGGVA 360 VKAHQVKNHM 370 WIFVNALIEN 380 PTFDSQTKEN 390 MTLQPKSFGS 400 TCQLSEKFIK 410 AAIGCGIVES 420 ILNWVKFKAQ 430 VQLNKKCSAV 440 KHNRIKGIPK 450 LDDANDAGGR 460 NSTECTLILT 470 EGDSAKTLAV 480 SGLGVVGRDK 490 YGVFPLRGKI 500 LNVREASHKQ 510 IMENAEINNI 520 IKIVGLQYKK 530 NYEDEDSLKT 540 LRYGKIMIMT 550 DQDQDGSHIK 560 GLLINFIHHN 570 WPSLLRHRFL 580 EEFITPIVKV 590 SKNKQEMAFY 600 SLPEFEEWKS 610 STPNHKKWKV 620 KYYKGLGTST 630 SKEAKEYFAD 640 MKRHRIQFKY 650 SGPEDDAAIS 660 LAFSKKQIDD 670 RKEWLTNFME 680 DRRQRKLLGL 690 PEDYLYGQTT 700 TYLTYNDFIN 710 KELILFSNSD 720 NERSIPSMVD 730 GLKPGQRKVL 740 FTCFKRNDKR 750 EVKVAQLAGS 760 VAEMSSYHHG 770 EMSLMMTIIN 780 LAQNFVGSNN 790 LNLLQPIGQF 800 GTRLHGGKDS 810 ASPRYIFTML 820 SSLARLLFPP 830 KDDHTLKFLY 840 DDNQRVEPEW 850 YIPIIPMVLI 860 NGAEGIGTGW 870 SCKIPNFDVR 880 EIVNNIRRLM 890 DGEEPLPMLP 900 SYKNFKGTIE 910 ELAPNQYVIS 920 GEVAILNSTT 930 IEISELPVRT 940 WTQTYKEQVL 950 EPMLNGTEKT 960 PPLITDYREY 970 HTDTTVKFVV 980 KMTEEKLAEA 990 ERVGLHKVFK 1000 LQTSLTCNSM 1010 VLFDHVGCLK 1020 KYDTVLDILR 1030 DFFELRLKYY 1040 GLRKEWLLGM 1050 LGAESAKLNN 1060 QARFILEKID 1070 GKIIIENKPK 1080 KELIKVLIQR 1090 GYDSDPVKAW 1100 KEAQQKVPDE 1110 EENEESDNEK 1120 ETEKSDSVTD 1130 SGPTFNYLLD 1140 MPLWYLTKEK 1150 KDELCRLRNE 1160 KEQELDTLKR 1170 KSPSDLWKED 1180 LATFIEELEA 1190 VEAKEKQDEQ 1200 VGLPGKGGKA 1210 KGKKTQMAEV 1220 LPSPRGQRVI 1230 PRITIEMKAE 1240 AEKKNKKKIK 1250 NENTEGSPQE 1260 DGVELEGLKQ 1270 RLEKKQKREP 1280 GTKTKKQTTL 1290 AFKPIKKGKK 1300 RNPWSDSESD 1310 RSSDESNFDV 1320 PPRETEPRRA 1330 ATKTKFTMDL 1340 DSDEDFSDFD 1350 EKTDDEDFVP 1360 SDASPPKTKT 1370 SPKLSNKELK 1380 PQKSVVSDLE 1390 ADDVKGSVPL 1400 SSSPPATHFP 1410 DETEITNPVP 1420 KKNVTVKKTA 1430 AKSQSSTSTT 1440 GAKKRAAPKG 1450 TKRDPALNSG 1460 VSQKPDPAKT 1470 KNRRKRKPST 1480 SDDSDSNFEK 1490 IVSKAVTSKK 1500 SKGESDDFHM 1510 DFDSAVAPRA 1520 KSVRAKKPIK 1530 YLEESDEDDL F

Gene Ontology

Classification GO ID Description
Cellular Component GO:0000775 chromosome, centromeric region
Cellular Component GO:0000793 condensed chromosome
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0009330 DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) complex
Cellular Component GO:0005730 nucleolus
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Cellular Component GO:0032991 protein-containing complex
Cellular Component GO:1990904 ribonucleoprotein complex
Molecular Function GO:0005524 ATP binding
Molecular Function GO:0008094 ATP-dependent activity, acting on DNA
Molecular Function GO:0003682 chromatin binding
Molecular Function GO:0003677 DNA binding
Molecular Function GO:0008301 DNA binding, bending
Molecular Function GO:0003918 DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity
Molecular Function GO:0000287 magnesium ion binding
Molecular Function GO:0046982 protein heterodimerization activity
Molecular Function GO:0042803 protein homodimerization activity
Molecular Function GO:0005080 protein kinase C binding
Molecular Function GO:0003723 RNA binding
Molecular Function GO:0043130 ubiquitin binding
Biological Process GO:0030263 apoptotic chromosome condensation
Biological Process GO:0006325 chromatin organization
Biological Process GO:0007059 chromosome segregation
Biological Process GO:0006974 DNA damage response
Biological Process GO:0006265 DNA topological change
Biological Process GO:0007143 female meiotic nuclear division
Biological Process GO:0043065 positive regulation of apoptotic process
Biological Process GO:0045870 positive regulation of single stranded viral RNA replication via double stranded DNA intermediate
Biological Process GO:0042752 regulation of circadian rhythm
Biological Process GO:0000712 resolution of meiotic recombination intermediates
Biological Process GO:0048511 rhythmic process
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] Cheng Z, Huang H, Li M, Chen Y. Proteomic analysis identifies PFKP lactylation in SW480 colon cancer cells.. iScience 27(1):108645. 2024 Jan 19. PMID: 38155775.

[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] 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.

[6] 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.