Top2a
entrez
21973
canonical
uniprot
Q01320
canonical
ensembl
ENSMUSG00000020914
resolver
ensp
ENSMUSP00000068896
resolver
ensp
ENSMUSP00000162815
resolver
ensp
ENSMUSP00000162816
resolver
enst
ENSMUST00000068031
resolver
genesymbol
Top2a
resolver
genesymbol_syn
Top-2
resolver
genesymbol_syn
Top2
resolver
uniprot
E9PX08
resolver
uniprot_entry
TOP2A_MOUSE
resolver
uniprot_sec
E9PX08
resolver
amino_acid_sequence
MELSPLQPVNENMLMNKKKNEDGKKRLSIERIYQKKTQLEHILLRPDTYIGSVELVTQQMWVYDEDVGINYREVTFVPGLYKIFDEILVNAADNKQRDPKMSCIRVTIDPENNVISIWNNGKGIPVVEHKVEKIYVPALIFGQLLTSSNYDDDEKKVTGGRNGYGAKLCNIFSTKFTVETASREYKKMFKQTWMDNMGRAGDMELKPFSGEDYTCITFQPDLSKFKMQSLDKDIVALMVRRAYDIAGSTKDVKVFLNGNSLPVKGFRSYVDLYLKDKVDETGNSLKVIHEQVNPRWEVCLTMSERGFQQISFVNSIATSKGGRHVDYVADQIVSKLVDVVKKKNKGGVAVKAHQVKNHMWIFVNALIENPTFDSQTKENMTLQAKSFGSTCQLSEKFIKAAIGCGIVESILNWVKFKAQIQLNKKCSAVKHTKIKGIPKLDDANDAGSRNSTECTLILTEGDSAKTLAVSGLGVVGRDKYGVFPLRGKILNVREASHKQIMENAEINNIIKIVGLQYKKNYEDEDSLKTLRYGKIMIMTDQDQDGSHIKGLLINFIHHNWPSLLRHRFLEEFITPIVKVSKNKQEIAFYSLPEFEEWKSSTPNHKKWKVKYYKGLGTSTSKEAKEYFADMKRHRIQFKYSGPEDDAAISLAFSKKQVDDRKEWLTNFMEDRRQRKLLGLPEDYLYGQSTSYLTYNDFINKELILFSNSDNERSIPSMVDGLKPGQRKVLFTCFKRNDKREVKVAQLAGSVAEMSSYHHGEMSLMMTIINLAQNFVGSNNLNLLQPIGQFGTRLHGGKDSASPRYIFTMLSPLARLLFPPKDDHTLRFLYDDNQRVEPEWYIPIIPMVLINGAEGIGTGWSCKIPNFDVREVVNNIRRLLDGEEPLPMLPSYKNFKGTIEELASNQYVINGEVAILDSTTIEISELPIRTWTQTYKEQVLEPMLNGTEKTPSLITDYREYHTDTTVKFVIKMTEEKLAEAERVGLHKVFKLQSSLTCNSMVLFDHVGCLKKYDTVLDILRDFFELRLKYYGLRKEWLLGMLGAESSKLNNQARFILEKIDGKIVIENKPKKELIKVLIQRGYDSDPVKAWKEAQQKVPDEEENEESDTETSTSDSAAEAGPTFNYLLDMPLWYLTKEKKDELCKQRNEKEQELNTLKQKSPSDLWKEDLAVFIEELEVVEAKEKQDEQVGLPGKAGKAKGKKAQMCADVLPSPRGKRVIPQVTVEMKAEAEKKIRKKIKSENVEGTPAEDGAEPGSLRQRIEKKQKKEPGAKKQTTLPFKPVKKGRKKNPWSDSESDVSSNESNVDVPPRQKEQRSAAAKAKFTVDLDSDEDFSGLDEKDEDEDFLPLDATPPKAKIPPKNTKKALKTQGSSMSVVDLESDVKDSVPASPGVPAADFPAETEQSKPSKKTVGVKKTATKSQSSVSTAGTKKRAAPKGTKSDSALSARVSEKPAPAKAKNSRKRKPSSSDSSDSDFERAISKGATSKKAKGEEQDFPVDLEDTIAPRAKSDRARKPIKYLEESDDDDDLF
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:1331984). May play a role in regulating the period length of BMAL1 transcriptional oscillation (PubMed:24321095). {ECO:0000269|PubMed:1331984, ECO:0000269|PubMed:24321095}.
uniprot
proteins
mass_dalton
172790
uniprot
proteins
post_translational_modification
PTM: Phosphorylation has no effect on catalytic activity (By similarity). However, phosphorylation at Ser-1105 by CSNK1D/CK1 promotes DNA cleavable complex formation (By similarity). {ECO:0000250|UniProtKB:P11388}.; PTM: Ubiquitinated in a FBXO28-dependent manner; leading to TOP2A proteasomal degradation. {ECO:0000250|UniProtKB:P11388}.
uniprot
proteins
protein_family
Type II topoisomerase family
uniprot
proteins
pubmed
1331984
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
23806337
uniprot
proteins
pubmed
24321095
uniprot
proteins
pubmed
31839538
uniprot
proteins
pubmed
8261398
uniprot
proteins
sequence_length
1528
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P11388}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:P11388}. Nucleus {ECO:0000250|UniProtKB:P11388}. Nucleus, nucleolus {ECO:0000250|UniProtKB:P11388}.
uniprot
proteins