Phospho-TOP2A (Ser1213) Antibody - #AF8090
Product: | Phospho-TOP2A (Ser1213) Antibody |
Catalog: | AF8090 |
Description: | Rabbit polyclonal antibody to Phospho-TOP2A (Ser1213) |
Application: | WB IF/ICC |
Reactivity: | Human, Mouse |
Mol.Wt.: | 174kDa; 174kD(Calculated). |
Uniprot: | P11388 |
RRID: | AB_2840153 |
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Protocols
Product Info
*The optimal dilutions should be determined by the end user.
*Tips:
WB: For western blot detection of denatured protein samples. IHC: For immunohistochemical detection of paraffin sections (IHC-p) or frozen sections (IHC-f) of tissue samples. IF/ICC: For immunofluorescence detection of cell samples. ELISA(peptide): For ELISA detection of antigenic peptide.
Cite Format: Affinity Biosciences Cat# AF8090, RRID:AB_2840153.
Fold/Unfold
alpha isozyme; ATP hydrolyzing DNA topoisomerase II alfa; DNA gyrase; DNA topoisomerase (ATP hydrolyzing); DNA topoisomerase 2 alpha; DNA topoisomerase 2-alpha; DNA topoisomerase II 170 kD; DNA topoisomerase II alpha isozyme; DNA topoisomerase II; DNA Topoisomerase2; TOP 2A; TOP2; TOP2A; TOP2A_HUMAN; Topoisomerase DNA II alpha 170kDa; TP2A;
Immunogens
- P11388 TOP2A_HUMAN:
- Protein BLAST With
- NCBI/
- ExPASy/
- Uniprot
MEVSPLQPVNENMQVNKIKKNEDAKKRLSVERIYQKKTQLEHILLRPDTYIGSVELVTQQMWVYDEDVGINYREVTFVPGLYKIFDEILVNAADNKQRDPKMSCIRVTIDPENNLISIWNNGKGIPVVEHKVEKMYVPALIFGQLLTSSNYDDDEKKVTGGRNGYGAKLCNIFSTKFTVETASREYKKMFKQTWMDNMGRAGEMELKPFNGEDYTCITFQPDLSKFKMQSLDKDIVALMVRRAYDIAGSTKDVKVFLNGNKLPVKGFRSYVDMYLKDKLDETGNSLKVIHEQVNHRWEVCLTMSEKGFQQISFVNSIATSKGGRHVDYVADQIVTKLVDVVKKKNKGGVAVKAHQVKNHMWIFVNALIENPTFDSQTKENMTLQPKSFGSTCQLSEKFIKAAIGCGIVESILNWVKFKAQVQLNKKCSAVKHNRIKGIPKLDDANDAGGRNSTECTLILTEGDSAKTLAVSGLGVVGRDKYGVFPLRGKILNVREASHKQIMENAEINNIIKIVGLQYKKNYEDEDSLKTLRYGKIMIMTDQDQDGSHIKGLLINFIHHNWPSLLRHRFLEEFITPIVKVSKNKQEMAFYSLPEFEEWKSSTPNHKKWKVKYYKGLGTSTSKEAKEYFADMKRHRIQFKYSGPEDDAAISLAFSKKQIDDRKEWLTNFMEDRRQRKLLGLPEDYLYGQTTTYLTYNDFINKELILFSNSDNERSIPSMVDGLKPGQRKVLFTCFKRNDKREVKVAQLAGSVAEMSSYHHGEMSLMMTIINLAQNFVGSNNLNLLQPIGQFGTRLHGGKDSASPRYIFTMLSSLARLLFPPKDDHTLKFLYDDNQRVEPEWYIPIIPMVLINGAEGIGTGWSCKIPNFDVREIVNNIRRLMDGEEPLPMLPSYKNFKGTIEELAPNQYVISGEVAILNSTTIEISELPVRTWTQTYKEQVLEPMLNGTEKTPPLITDYREYHTDTTVKFVVKMTEEKLAEAERVGLHKVFKLQTSLTCNSMVLFDHVGCLKKYDTVLDILRDFFELRLKYYGLRKEWLLGMLGAESAKLNNQARFILEKIDGKIIIENKPKKELIKVLIQRGYDSDPVKAWKEAQQKVPDEEENEESDNEKETEKSDSVTDSGPTFNYLLDMPLWYLTKEKKDELCRLRNEKEQELDTLKRKSPSDLWKEDLATFIEELEAVEAKEKQDEQVGLPGKGGKAKGKKTQMAEVLPSPRGQRVIPRITIEMKAEAEKKNKKKIKNENTEGSPQEDGVELEGLKQRLEKKQKREPGTKTKKQTTLAFKPIKKGKKRNPWSDSESDRSSDESNFDVPPRETEPRRAATKTKFTMDLDSDEDFSDFDEKTDDEDFVPSDASPPKTKTSPKLSNKELKPQKSVVSDLEADDVKGSVPLSSSPPATHFPDETEITNPVPKKNVTVKKTAAKSQSSTSTTGAKKRAAPKGTKRDPALNSGVSQKPDPAKTKNRRKRKPSTSDDSDSNFEKIVSKAVTSKKSKGESDDFHMDFDSAVAPRAKSVRAKKPIKYLEESDEDDLF
PTMs - P11388 As Substrate
Site | PTM Type | Enzyme | Source |
---|---|---|---|
M1 | Acetylation | Uniprot | |
S4 | Phosphorylation | Uniprot | |
S29 | Phosphorylation | P05129 (PRKCG) , P05771 (PRKCB) | Uniprot |
Y82 | Phosphorylation | Uniprot | |
K96 | Ubiquitination | Uniprot | |
K101 | Ubiquitination | Uniprot | |
K123 | Ubiquitination | Uniprot | |
K131 | Sumoylation | Uniprot | |
K131 | Ubiquitination | Uniprot | |
Y151 | Phosphorylation | Uniprot | |
K156 | Ubiquitination | Uniprot | |
K157 | Ubiquitination | Uniprot | |
K168 | Ubiquitination | Uniprot | |
K191 | Ubiquitination | Uniprot | |
K225 | Ubiquitination | Uniprot | |
K227 | Sumoylation | Uniprot | |
K227 | Ubiquitination | Uniprot | |
S230 | Phosphorylation | Uniprot | |
K233 | Ubiquitination | Uniprot | |
S249 | Phosphorylation | Uniprot | |
T250 | Phosphorylation | Uniprot | |
K251 | Ubiquitination | Uniprot | |
K254 | Acetylation | Uniprot | |
K261 | Ubiquitination | Uniprot | |
K265 | Ubiquitination | Uniprot | |
K276 | Ubiquitination | Uniprot | |
K278 | Sumoylation | Uniprot | |
K278 | Ubiquitination | Uniprot | |
T282 | Phosphorylation | Uniprot | |
S285 | Phosphorylation | Uniprot | |
K287 | Ubiquitination | Uniprot | |
S312 | Phosphorylation | Uniprot | |
K321 | Ubiquitination | Uniprot | |
Y328 | Phosphorylation | Uniprot | |
K336 | Ubiquitination | Uniprot | |
K342 | Ubiquitination | Uniprot | |
K352 | Ubiquitination | Uniprot | |
K386 | Sumoylation | Uniprot | |
K386 | Ubiquitination | Uniprot | |
K397 | Acetylation | Uniprot | |
K397 | Ubiquitination | Uniprot | |
K418 | Ubiquitination | Uniprot | |
K425 | Ubiquitination | Uniprot | |
K431 | Ubiquitination | Uniprot | |
K440 | Sumoylation | Uniprot | |
K440 | Ubiquitination | Uniprot | |
S452 | Phosphorylation | Uniprot | |
C455 | S-Nitrosylation | Uniprot | |
S464 | Phosphorylation | Uniprot | |
K466 | Ubiquitination | Uniprot | |
S471 | Phosphorylation | Uniprot | |
K480 | Ubiquitination | Uniprot | |
K489 | Sumoylation | Uniprot | |
K489 | Ubiquitination | Uniprot | |
K499 | Ubiquitination | Uniprot | |
K512 | Ubiquitination | Uniprot | |
Y518 | Phosphorylation | Uniprot | |
K519 | Ubiquitination | Uniprot | |
K520 | Ubiquitination | Uniprot | |
Y522 | Phosphorylation | Uniprot | |
K529 | Ubiquitination | Uniprot | |
K535 | Ubiquitination | Uniprot | |
K579 | Ubiquitination | Uniprot | |
K584 | Ubiquitination | Uniprot | |
K599 | Sumoylation | Uniprot | |
K599 | Ubiquitination | Uniprot | |
Y612 | Phosphorylation | Uniprot | |
K614 | Ubiquitination | Uniprot | |
K622 | Ubiquitination | Uniprot | |
K625 | Sumoylation | Uniprot | |
K625 | Ubiquitination | Uniprot | |
K632 | Sumoylation | Uniprot | |
K632 | Ubiquitination | Uniprot | |
K639 | Methylation | Uniprot | |
K639 | Sumoylation | Uniprot | |
K639 | Ubiquitination | Uniprot | |
K655 | Ubiquitination | Uniprot | |
K656 | Ubiquitination | Uniprot | |
K662 | Sumoylation | Uniprot | |
K662 | Ubiquitination | Uniprot | |
R672 | Methylation | Uniprot | |
K676 | Sumoylation | Uniprot | |
K676 | Ubiquitination | Uniprot | |
S707 | Phosphorylation | Uniprot | |
S709 | Phosphorylation | Uniprot | |
S714 | Phosphorylation | Uniprot | |
S717 | Phosphorylation | Uniprot | |
K723 | Ubiquitination | Uniprot | |
K728 | Ubiquitination | Uniprot | |
K735 | Ubiquitination | Uniprot | |
Y805 | Phosphorylation | Uniprot | |
T825 | Phosphorylation | Uniprot | |
K827 | Ubiquitination | Uniprot | |
Y830 | Phosphorylation | Uniprot | |
K893 | Ubiquitination | Uniprot | |
T898 | Phosphorylation | Uniprot | |
K936 | Methylation | Uniprot | |
K936 | Ubiquitination | Uniprot | |
K949 | Ubiquitination | Uniprot | |
K967 | Ubiquitination | Uniprot | |
K971 | Acetylation | Uniprot | |
K971 | Ubiquitination | Uniprot | |
K976 | Ubiquitination | Uniprot | |
K987 | Ubiquitination | Uniprot | |
K1011 | Ubiquitination | Uniprot | |
R1026 | Methylation | Uniprot | |
K1028 | Ubiquitination | Uniprot | |
S1045 | Phosphorylation | Uniprot | |
K1047 | Ubiquitination | Uniprot | |
K1058 | Ubiquitination | Uniprot | |
K1062 | Ubiquitination | Uniprot | |
K1068 | Ubiquitination | Uniprot | |
K1070 | Ubiquitination | Uniprot | |
K1075 | Sumoylation | Uniprot | |
K1075 | Ubiquitination | Uniprot | |
K1088 | Ubiquitination | Uniprot | |
S1106 | Phosphorylation | Uniprot | |
T1112 | Phosphorylation | Uniprot | |
K1114 | Ubiquitination | Uniprot | |
T1119 | Phosphorylation | Uniprot | |
K1151 | Ubiquitination | Uniprot | |
T1157 | Phosphorylation | Uniprot | |
K1159 | Ubiquitination | Uniprot | |
S1162 | Phosphorylation | Uniprot | |
S1164 | Phosphorylation | Uniprot | |
K1184 | Ubiquitination | Uniprot | |
K1186 | Ubiquitination | Uniprot | |
K1196 | Acetylation | Uniprot | |
K1196 | Sumoylation | Uniprot | |
K1196 | Ubiquitination | Uniprot | |
K1199 | Acetylation | Uniprot | |
K1201 | Acetylation | Uniprot | |
K1204 | Sumoylation | Uniprot | |
K1204 | Ubiquitination | Uniprot | |
T1205 | Phosphorylation | Uniprot | |
S1213 | Phosphorylation | P28482 (MAPK1) , P27361 (MAPK3) , P06493 (CDK1) | Uniprot |
K1228 | Sumoylation | Uniprot | |
K1228 | Ubiquitination | Uniprot | |
K1233 | Acetylation | Uniprot | |
K1234 | Acetylation | Uniprot | |
K1237 | Acetylation | Uniprot | |
K1240 | Sumoylation | Uniprot | |
K1240 | Ubiquitination | Uniprot | |
T1244 | Phosphorylation | Uniprot | |
S1247 | Phosphorylation | P27361 (MAPK3) , P28482 (MAPK1) , P06493 (CDK1) | Uniprot |
K1259 | Ubiquitination | Uniprot | |
T1272 | Phosphorylation | Uniprot | |
T1274 | Phosphorylation | Uniprot | |
K1276 | Acetylation | Uniprot | |
K1276 | Ubiquitination | Uniprot | |
K1283 | Methylation | Uniprot | |
K1287 | Acetylation | Uniprot | |
K1289 | Acetylation | Uniprot | |
S1295 | Phosphorylation | Uniprot | |
S1297 | Phosphorylation | Uniprot | |
S1299 | Phosphorylation | Uniprot | |
S1302 | Phosphorylation | Uniprot | |
S1303 | Phosphorylation | Uniprot | |
S1306 | Phosphorylation | Uniprot | |
T1324 | Phosphorylation | Uniprot | |
T1327 | Phosphorylation | Uniprot | |
S1332 | Phosphorylation | Uniprot | |
S1337 | Phosphorylation | P53350 (PLK1) | Uniprot |
T1343 | Phosphorylation | P68400 (CSNK2A1) , P53350 (PLK1) , Q9H4B4 (PLK3) | Uniprot |
S1351 | Phosphorylation | Uniprot | |
S1354 | Phosphorylation | P27361 (MAPK3) , P28482 (MAPK1) , P06493 (CDK1) | Uniprot |
T1358 | Phosphorylation | Uniprot | |
T1360 | Phosphorylation | Uniprot | |
S1361 | Phosphorylation | P06493 (CDK1) , P28482 (MAPK1) , P27361 (MAPK3) , P49841 (GSK3B) | Uniprot |
S1365 | Phosphorylation | P68400 (CSNK2A1) | Uniprot |
K1367 | Acetylation | Uniprot | |
K1367 | Ubiquitination | Uniprot | |
S1374 | Phosphorylation | Uniprot | |
S1377 | Phosphorylation | P68400 (CSNK2A1) | Uniprot |
K1385 | Sumoylation | Uniprot | |
K1385 | Ubiquitination | Uniprot | |
S1387 | Phosphorylation | Uniprot | |
S1391 | Phosphorylation | Uniprot | |
S1392 | Phosphorylation | Uniprot | |
S1393 | Phosphorylation | P06493 (CDK1) , P28482 (MAPK1) , P27361 (MAPK3) | Uniprot |
T1397 | Phosphorylation | Uniprot | |
T1403 | Phosphorylation | Uniprot | |
T1406 | Phosphorylation | Uniprot | |
K1422 | Ubiquitination | Uniprot | |
S1426 | Phosphorylation | Uniprot | |
T1429 | Phosphorylation | Uniprot | |
T1430 | Phosphorylation | Uniprot | |
K1442 | Sumoylation | Uniprot | |
K1442 | Ubiquitination | Uniprot | |
R1443 | Methylation | Uniprot | |
S1449 | Phosphorylation | Uniprot | |
S1452 | Phosphorylation | Uniprot | |
K1454 | Acetylation | Uniprot | |
K1454 | Ubiquitination | Uniprot | |
K1459 | Ubiquitination | Uniprot | |
K1461 | Ubiquitination | Uniprot | |
K1467 | Acetylation | Uniprot | |
S1469 | Phosphorylation | P68400 (CSNK2A1) | Uniprot |
T1470 | Phosphorylation | Uniprot | |
S1471 | Phosphorylation | Uniprot | |
S1474 | Phosphorylation | Uniprot | |
S1476 | Phosphorylation | Uniprot | |
K1480 | Acetylation | Uniprot | |
K1484 | Ubiquitination | Uniprot | |
S1491 | Phosphorylation | Uniprot | |
K1492 | Sumoylation | Uniprot | |
K1492 | Ubiquitination | Uniprot | |
S1495 | Phosphorylation | Uniprot | |
S1504 | Phosphorylation | Uniprot | |
Y1521 | Phosphorylation | Uniprot | |
S1525 | Phosphorylation | P68400 (CSNK2A1) , P53350 (PLK1) , P53778 (MAPK12) | Uniprot |
Research Backgrounds
Control of topological states of DNA by transient breakage and subsequent rejoining of DNA strands. Topoisomerase II makes double-strand breaks. Essential during mitosis and meiosis for proper segregation of daughter chromosomes. May play a role in regulating the period length of ARNTL/BMAL1 transcriptional oscillation (By similarity).
Phosphorylation has no effect on catalytic activity. However, phosphorylation at Ser-1106 by CSNK1D/CK1 promotes DNA cleavable complex formation.
Cytoplasm. Nucleus>Nucleoplasm.
Note: Generally located in the nucleoplasm.
Homodimer. Interacts with COPS5. Interacts with RECQL5; this stimulates DNA decatenation. Interacts with SETMAR; stimulates the topoisomerase activity. Interacts with DHX9; this interaction occurs in a E2 enzyme UBE2I- and RNA-dependent manner, negatively regulates DHX9-mediated double-stranded DNA and RNA duplex helicase activity and stimulates TOP2A-mediated supercoiled DNA relaxation activity. Interacts with HNRNPU (via C-terminus); this interaction protects the topoisomerase TOP2A from degradation and positively regulates the relaxation of supercoiled DNA in a RNA-dependent manner (By similarity). Interacts with MCM3AP isoform GANP. Interacts with ERCC6.
The N-terminus has several structural domains; the ATPase domain (about residues 1-265), the transducer domain (about 266-428) and the toprim domain (455-572) (PubMed:25202966). Comparing different structures shows ATP hydrolysis induces domain shifts in the N-terminus that are probably part of the mechanism of DNA cleavage and rejoining (PubMed:25202966).
Belongs to the type II topoisomerase family.
Research Fields
· Human Diseases > Drug resistance: Antineoplastic > Platinum drug resistance.
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