TOP2A
entrez
7153
canonical
uniprot
P11388
canonical
ensembl
ENSG00000131747
resolver
ensp
ENSP00000411532
resolver
ensp
ENSP00000729830
resolver
genesymbol
TOP2A
resolver
genesymbol_syn
TOP2
resolver
hgnc
HGNC:11989
resolver
uniprot
B2RTS1
resolver
uniprot
Q71UN1
resolver
uniprot
Q71UQ5
resolver
uniprot
Q9HB24
resolver
uniprot
Q9HB25
resolver
uniprot
Q9HB26
resolver
uniprot
Q9UP44
resolver
uniprot
Q9UQP9
resolver
uniprot_entry
TOP2A_HUMAN
resolver
uniprot_sec
B2RTS1
resolver
uniprot_sec
Q71UN1
resolver
uniprot_sec
Q71UQ5
resolver
uniprot_sec
Q9HB24
resolver
uniprot_sec
Q9HB25
resolver
uniprot_sec
Q9HB26
resolver
uniprot_sec
Q9UP44
resolver
uniprot_sec
Q9UQP9
resolver
activity_regulation
ACTIVITY REGULATION: Specifically inhibited by the intercalating agent amsacrine.
uniprot
proteins
amino_acid_sequence
MEVSPLQPVNENMQVNKIKKNEDAKKRLSVERIYQKKTQLEHILLRPDTYIGSVELVTQQMWVYDEDVGINYREVTFVPGLYKIFDEILVNAADNKQRDPKMSCIRVTIDPENNLISIWNNGKGIPVVEHKVEKMYVPALIFGQLLTSSNYDDDEKKVTGGRNGYGAKLCNIFSTKFTVETASREYKKMFKQTWMDNMGRAGEMELKPFNGEDYTCITFQPDLSKFKMQSLDKDIVALMVRRAYDIAGSTKDVKVFLNGNKLPVKGFRSYVDMYLKDKLDETGNSLKVIHEQVNHRWEVCLTMSEKGFQQISFVNSIATSKGGRHVDYVADQIVTKLVDVVKKKNKGGVAVKAHQVKNHMWIFVNALIENPTFDSQTKENMTLQPKSFGSTCQLSEKFIKAAIGCGIVESILNWVKFKAQVQLNKKCSAVKHNRIKGIPKLDDANDAGGRNSTECTLILTEGDSAKTLAVSGLGVVGRDKYGVFPLRGKILNVREASHKQIMENAEINNIIKIVGLQYKKNYEDEDSLKTLRYGKIMIMTDQDQDGSHIKGLLINFIHHNWPSLLRHRFLEEFITPIVKVSKNKQEMAFYSLPEFEEWKSSTPNHKKWKVKYYKGLGTSTSKEAKEYFADMKRHRIQFKYSGPEDDAAISLAFSKKQIDDRKEWLTNFMEDRRQRKLLGLPEDYLYGQTTTYLTYNDFINKELILFSNSDNERSIPSMVDGLKPGQRKVLFTCFKRNDKREVKVAQLAGSVAEMSSYHHGEMSLMMTIINLAQNFVGSNNLNLLQPIGQFGTRLHGGKDSASPRYIFTMLSSLARLLFPPKDDHTLKFLYDDNQRVEPEWYIPIIPMVLINGAEGIGTGWSCKIPNFDVREIVNNIRRLMDGEEPLPMLPSYKNFKGTIEELAPNQYVISGEVAILNSTTIEISELPVRTWTQTYKEQVLEPMLNGTEKTPPLITDYREYHTDTTVKFVVKMTEEKLAEAERVGLHKVFKLQTSLTCNSMVLFDHVGCLKKYDTVLDILRDFFELRLKYYGLRKEWLLGMLGAESAKLNNQARFILEKIDGKIIIENKPKKELIKVLIQRGYDSDPVKAWKEAQQKVPDEEENEESDNEKETEKSDSVTDSGPTFNYLLDMPLWYLTKEKKDELCRLRNEKEQELDTLKRKSPSDLWKEDLATFIEELEAVEAKEKQDEQVGLPGKGGKAKGKKTQMAEVLPSPRGQRVIPRITIEMKAEAEKKNKKKIKNENTEGSPQEDGVELEGLKQRLEKKQKREPGTKTKKQTTLAFKPIKKGKKRNPWSDSESDRSSDESNFDVPPRETEPRRAATKTKFTMDLDSDEDFSDFDEKTDDEDFVPSDASPPKTKTSPKLSNKELKPQKSVVSDLEADDVKGSVPLSSSPPATHFPDETEITNPVPKKNVTVKKTAAKSQSSTSTTGAKKRAAPKGTKRDPALNSGVSQKPDPAKTKNRRKRKPSTSDDSDSNFEKIVSKAVTSKKSKGESDDFHMDFDSAVAPRAKSVRAKKPIKYLEESDEDDLF
uniprot
proteins
ec_number
5.6.2.2
uniprot
proteins
function
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). {ECO:0000250|UniProtKB:Q01320, ECO:0000269|PubMed:17567603, ECO:0000269|PubMed:18790802, ECO:0000269|PubMed:22013166, ECO:0000269|PubMed:22323612, ECO:0000269|PubMed:27754753}.
uniprot
proteins
mass_dalton
174385
uniprot
proteins
mutagenesis
MUTAGEN 342..344; /note="KKK->AAA: Reduced enzyme activity; abolishes stimulation of ATPase activity upon DNA binding."; /evidence="ECO:0000269|PubMed:23022727"; MUTAGEN 342..344; /note="KKK->EEE: Strongly reduced enzyme activity; abolishes stimulation of ATPase activity upon DNA binding."; /evidence="ECO:0000269|PubMed:23022727"; MUTAGEN 461; /note="E->A,C: Impairs bending of target DNA. Strongly reduced DNA cleavage."; /evidence="ECO:0000269|PubMed:19697956, ECO:0000269|PubMed:22323612"; MUTAGEN 541; /note="D->A,C: Impairs bending of target DNA. Strongly reduced DNA cleavage."; /evidence="ECO:0000269|PubMed:19697956, ECO:0000269|PubMed:22323612"; MUTAGEN 543; /note="D->A,C: Impairs bending of target DNA. Strongly reduced DNA cleavage."; /evidence="ECO:0000269|PubMed:19697956, ECO:0000269|PubMed:22323612"; MUTAGEN 545; /note="D->A,C: Strongly reduced DNA cleavage."; /evidence="ECO:0000269|PubMed:19697956"; MUTAGEN 1469; /note="S->A: Abolishes binding to the antibody MPM2."; /evidence="ECO:0000269|PubMed:10942766
uniprot
proteins
post_translational_modification
PTM: Phosphorylation has no effect on catalytic activity. However, phosphorylation at Ser-1106 by CSNK1D/CK1 promotes DNA cleavable complex formation. {ECO:0000269|PubMed:10942766, ECO:0000269|PubMed:18062778, ECO:0000269|PubMed:19043076, ECO:0000269|Ref.11}.; PTM: (Microbial infection) Deubiquitinated by Epstein-Barr virus BPLF1; leading to stabilized SUMOylated TOP2A trapped in cleavage complexes, which halts the DNA damage response to TOP2A-induced double-strand DNA breaks. {ECO:0000269|PubMed:34543352}.; PTM: SUMOylated. {ECO:0000269|PubMed:34543352}.; PTM: Ubiquitinated in a FBXO28-dependent manner; leading to TOP2A proteasomal degradation. {ECO:0000269|PubMed:27754753}.
uniprot
proteins
protein_family
Type II topoisomerase family
uniprot
proteins
pubmed
10095062
uniprot
proteins
pubmed
10942766
uniprot
proteins
pubmed
12711669
uniprot
proteins
pubmed
12821127
uniprot
proteins
pubmed
15126503
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16100112
uniprot
proteins
pubmed
1651812
uniprot
proteins
pubmed
1652758
uniprot
proteins
pubmed
16625196
uniprot
proteins
pubmed
16964243
uniprot
proteins
pubmed
17081983
uniprot
proteins
pubmed
17567603
uniprot
proteins
pubmed
17924679
uniprot
proteins
pubmed
18062778
uniprot
proteins
pubmed
18220336
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
18691976
uniprot
proteins
pubmed
18790802
uniprot
proteins
pubmed
19043076
uniprot
proteins
pubmed
19222228
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
19697956
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20457750
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
22013166
uniprot
proteins
pubmed
22323612
uniprot
proteins
pubmed
22814378
uniprot
proteins
pubmed
22841979
uniprot
proteins
pubmed
23022727
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23213405
uniprot
proteins
pubmed
23652018
uniprot
proteins
pubmed
25114211
uniprot
proteins
pubmed
25202966
uniprot
proteins
pubmed
25218447
uniprot
proteins
pubmed
25755297
uniprot
proteins
pubmed
25772364
uniprot
proteins
pubmed
26030138
uniprot
proteins
pubmed
27754753
uniprot
proteins
pubmed
28112733
uniprot
proteins
pubmed
2845399
uniprot
proteins
pubmed
34543352
uniprot
proteins
pubmed
36271492
uniprot
proteins
pubmed
8299728
uniprot
proteins
pubmed
8393377
uniprot
proteins
pubmed
9155056
uniprot
proteins
pubmed
9795238
uniprot
proteins
sequence_length
1531
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9155056}. Nucleus, nucleoplasm {ECO:0000269|PubMed:8299728}. Nucleus {ECO:0000269|PubMed:17567603, ECO:0000269|PubMed:22013166, ECO:0000269|PubMed:8299728, ECO:0000269|PubMed:9155056}. Nucleus, nucleolus {ECO:0000269|PubMed:9155056}.
uniprot
proteins