P41516
uniprot
P41516
canonical
amino_acid_sequence
MELSPLQPVNENMLLNKKKNEDGKKRLSVERIYQKKTQLEHILLRPDTYIGSVELVTQQMWVYDEDVGINYREVTFVPGLYKIFDEILVNAADNKQRDPKMSCIRVTMMRNNLISIWNNGKGIPVVEHKVEKMYVPALIFGQLLTSSNYDDDEKKVTGGRNGYGAKLCNIFSTKFTVETASREYKKMFKQTWMDNMGRAGDMELKPFSGEDYTCITFQPDLSKFKMQSLDKDIVALMVRRAYDIAGSTKDVKVFLNGNRLPVKGFRSYVDMYLKDKVDETGNALKVVHEQVNPRWEVCLTMSEKGFQQISFVNSIATSKGGRHVDYVADQIVSKLVDVVKKKNKGGVAVKADQVKNHMWIFGNAVIENPTFDSQTKENMTLQAKSFGSTCQLSEKFIKAAIGCGIVESILNWVKFKAQIQLNKKCSAVKHNRIKGIPKLDDANDAGSRNSAECTLILTEGDSAKTLAVSGLGVVGRDKYGVFPLRGKILNVREASHKQIMENAEINNIIKIVGLQYKKNYEDEDSLKTLRYGKIMIMTDQDQDGSHIKGLLINFIHHNWPSLLRHRFLEEFITPIVKVSKNKQEIAFYSLPEFEEWKSTNPNHKKWKVKYYKGLGTSTSKEAKEYFANMKRHRIQFKYSGPEDDAAISLAFSKKQVDDRKEWLTNFMEDRRQRKLLGLPEDYLYGQTTMYLTYNDFINKELILFSNSDNERSIPSMVDGLKPGQRKVLFTCFKRNDKREVKVAQLAGSVAEMSSYHHGEMSLMMTIINLAQNFVGSNNLNLLQPIGQFGTRLHGGKDSASPRYIFTMLSPLARLLFPSKDDHTLRFLYDDNQRVEPEWYIPIIPMVLINGAEGIGTGWSCKIPNFDVREVVNNIRRLLDGEEPLPMLPSYKNYKGTIEELASNQYVINGEVAILNSTTIEITELPIRTWTQTYKEQVLEPMLNGTEKTPPLITDYREYHTDTTVKFVIKMTEEKLAEAERVGLHKVFKLQTSLTCNSMVLFDHVGCLKKYDTVLDILRDFFELRLKYYGLRKEWLLGMLGAESSKLNNQARFILEKIDGKIVIENKPKKELIKVLIQRGYDSDPVKAWKEAQQKVPEEEENEENEESESESTSPAAESGPTFNYLLDMPLWYLTKEKKDELCKQRDEKEQELNTLKKKTPSDLWKEDLAAFVEELEVVEAKEKQDEQVGLPGKGVKAKGKKAQISEVLPSPVGKRVIPQVTMEMRAEAEKKIRRKIKSENVEGTPAEDGAEPGLRQRLEKRQKREPGTRAKKQTTLPFKPIKKAQKQNPWSDSESDMSSNESNFDVPPREKEPRIAATKAKFTADLDSDDDFSGLDEKDEDEDFFPLDDTPPKTKMPPKNTKKALKPQKSSTSVDLESDGKDSVPASPGASAADVPAETEPSKPSSKQTVGVKRTITKGQSLTSTAGTKKRAVPKETKSDSALNAHVSKKPAPAKAKNSRKRMPSSSDSSDSEFEKAISKGATSKKLKGEERDFHVDLDDTVAPRAKSGRARKPIKYLEESDDDLF
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 (By similarity). May play a role in regulating the period length of BMAL1 transcriptional oscillation (By similarity). {ECO:0000250|UniProtKB:P11388, ECO:0000250|UniProtKB:Q01320}.
uniprot
proteins
mass_dalton
173221
uniprot
proteins
post_translational_modification
PTM: Phosphorylation has no effect on catalytic activity. {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
20554522
uniprot
proteins
pubmed
22673903
uniprot
proteins
pubmed
8390253
uniprot
proteins
sequence_length
1526
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