LOCUS       NP_035753               1528 aa            linear   ROD 27-APR-2025
DEFINITION  DNA topoisomerase 2-alpha [Mus musculus].
ACCESSION   NP_035753
VERSION     NP_035753.2
DBSOURCE    REFSEQ: accession NM_011623.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 1528)
  AUTHORS   Zhang,K., Zheng,X., Sun,Y., Feng,X., Wu,X., Liu,W., Gao,C., Yan,Y.,
            Tian,W. and Wang,Y.
  TITLE     TOP2A modulates signaling via the AKT/mTOR pathway to promote
            ovarian cancer cell proliferation
  JOURNAL   Cancer Biol Ther 25 (1), 2325126 (2024)
   PUBMED   38445610
  REMARK    GeneRIF: TOP2A modulates signaling via the AKT/mTOR pathway to
            promote ovarian cancer cell proliferation.
REFERENCE   2  (residues 1 to 1528)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   3  (residues 1 to 1528)
  AUTHORS   Yao,X., Wang,C., Yu,W., Sun,L., Lv,Z., Xie,X., Tian,S., Yan,L.,
            Li,L. and Liu,J.
  TITLE     BCAS2 regulates oocyte meiotic prophase I by participating in mRNA
            alternative splicing
  JOURNAL   FASEB J 38 (1), e23361 (2024)
   PUBMED   38085152
REFERENCE   4  (residues 1 to 1528)
  AUTHORS   Zhang,W., Zhang,R., Wu,L., Zhu,C., Zhang,C., Xu,C., Zhao,S.,
            Liu,X., Guo,T., Lu,Y., Gao,Z., Yu,X., Li,L., Chen,Z.J., Qin,Y. and
            Jiao,X.
  TITLE     NLRP14 deficiency causes female infertility with oocyte maturation
            defects and early embryonic arrest by impairing cytoplasmic UHRF1
            abundance
  JOURNAL   Cell Rep 42 (12), 113531 (2023)
   PUBMED   38060382
REFERENCE   5  (residues 1 to 1528)
  AUTHORS   Sun,B., Reynolds,K., Saha,S.K., Zhang,S., McMahon,M. and Zhou,C.J.
  TITLE     Ezh2-dependent methylation in oral epithelia promotes secondary
            palatogenesis
  JOURNAL   Birth Defects Res 115 (19), 1851-1865 (2023)
   PUBMED   37435868
REFERENCE   6  (residues 1 to 1528)
  AUTHORS   Baloch,Z., Cohen,S., Fresa,K. and Coffman,F.D.
  TITLE     Modulation of topoisomerase activities by tumor necrosis factor
  JOURNAL   Cell Immunol 160 (1), 98-103 (1995)
   PUBMED   7842491
REFERENCE   7  (residues 1 to 1528)
  AUTHORS   Adachi,N., Miyaike,M., Ikeda,H. and Kikuchi,A.
  TITLE     Characterization of cDNA encoding the mouse DNA topoisomerase II
            that can complement the budding yeast top2 mutation
  JOURNAL   Nucleic Acids Res 20 (20), 5297-5303 (1992)
   PUBMED   1331984
REFERENCE   8  (residues 1 to 1528)
  AUTHORS   Capranico,G., Tinelli,S., Austin,C.A., Fisher,M.L. and Zunino,F.
  TITLE     Different patterns of gene expression of topoisomerase II isoforms
            in differentiated tissues during murine development
  JOURNAL   Biochim Biophys Acta 1132 (1), 43-48 (1992)
   PUBMED   1380833
REFERENCE   9  (residues 1 to 1528)
  AUTHORS   Ura,K. and Hirose,S.
  TITLE     Possible role of DNA topoisomerase II on transcription of the
            homeobox gene Hox-2.1 in F9 embryonal carcinoma cells
  JOURNAL   Nucleic Acids Res 19 (22), 6087-6092 (1991)
   PUBMED   1683482
REFERENCE   10 (residues 1 to 1528)
  AUTHORS   Deffie,A.M., Bosman,D.J. and Goldenberg,G.J.
  TITLE     Evidence for a mutant allele of the gene for DNA topoisomerase II
            in adriamycin-resistant P388 murine leukemia cells
  JOURNAL   Cancer Res 49 (24 Pt 1), 6879-6882 (1989)
   PUBMED   2555055
  REMARK    Erratum:[Cancer Res 1990 Jan 15;50(2):449]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL591067.35.
            
            On Jul 26, 2007 this sequence version replaced NP_035753.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: D12513.1, SRR9219380.46551.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN00849374,
                                           SAMN00849375 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1528
                     /organism="Mus musculus"
                     /db_xref="taxon:10090"
                     /chromosome="11"
                     /map="11 62.91 cM"
     Protein         1..1528
                     /product="DNA topoisomerase 2-alpha"
                     /EC_number="5.6.2.2"
                     /note="DNA topoisomerase II, alpha isozyme; DNA
                     Topoisomerase II alpha"
                     /calculated_mol_wt=172660
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:P11388; propagated from
                     UniProtKB/Swiss-Prot (Q01320.2)"
     Site            4
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P11388; propagated from
                     UniProtKB/Swiss-Prot (Q01320.2)"
     Region          24..1441
                     /region_name="PTZ00108"
                     /note="DNA topoisomerase 2-like protein; Provisional"
                     /db_xref="CDD:240271"
     Site            281
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P11388; propagated from
                     UniProtKB/Swiss-Prot (Q01320.2)"
     Region          341..343
                     /region_name="Interaction with DNA.
                     /evidence=ECO:0000250|UniProtKB:P11388"
                     /note="propagated from UniProtKB/Swiss-Prot (Q01320.2)"
     Site            488
                     /site_type="other"
                     /note="Interaction with DNA.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00995; propagated
                     from UniProtKB/Swiss-Prot (Q01320.2)"
     Site            491
                     /site_type="other"
                     /note="Interaction with DNA.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00995; propagated
                     from UniProtKB/Swiss-Prot (Q01320.2)"
     Site            660
                     /site_type="other"
                     /note="Interaction with DNA.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00995; propagated
                     from UniProtKB/Swiss-Prot (Q01320.2)"
     Site            661
                     /site_type="other"
                     /note="Interaction with DNA.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00995; propagated
                     from UniProtKB/Swiss-Prot (Q01320.2)"
     Site            722
                     /site_type="other"
                     /note="Interaction with DNA.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00995; propagated
                     from UniProtKB/Swiss-Prot (Q01320.2)"
     Site            756
                     /site_type="other"
                     /note="Interaction with DNA.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00995; propagated
                     from UniProtKB/Swiss-Prot (Q01320.2)"
     Site            762
                     /site_type="other"
                     /note="Interaction with DNA.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00995; propagated
                     from UniProtKB/Swiss-Prot (Q01320.2)"
     Site            803
                     /site_type="other"
                     /note="Transition state stabilizer.
                     /evidence=ECO:0000250|UniProtKB:P06786; propagated from
                     UniProtKB/Swiss-Prot (Q01320.2)"
     Site            855
                     /site_type="other"
                     /note="Important for DNA bending, intercalates between
                     base pairs of target DNA.
                     /evidence=ECO:0000250|UniProtKB:P06786; propagated from
                     UniProtKB/Swiss-Prot (Q01320.2)"
     Site            930
                     /site_type="other"
                     /note="Interaction with DNA.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00995; propagated
                     from UniProtKB/Swiss-Prot (Q01320.2)"
     Region          989..998
                     /region_name="Interaction with DNA.
                     /evidence=ECO:0000250|UniProtKB:P11388"
                     /note="propagated from UniProtKB/Swiss-Prot (Q01320.2)"
     Region          1090..1118
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q01320.2)"
     Site            1105
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CK1.
                     /evidence=ECO:0000250|UniProtKB:P11388; propagated from
                     UniProtKB/Swiss-Prot (Q01320.2)"
     Region          1183..1211
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q01320.2)"
     Site            1211
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q01320.2)"
     Region          1229..1528
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q01320.2)"
     Site            1245
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q01320.2)"
     Site            1291
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P11388; propagated from
                     UniProtKB/Swiss-Prot (Q01320.2)"
     Site            1293
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P11388; propagated from
                     UniProtKB/Swiss-Prot (Q01320.2)"
     Site            1295
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P11388; propagated from
                     UniProtKB/Swiss-Prot (Q01320.2)"
     Site            1298
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P11388; propagated from
                     UniProtKB/Swiss-Prot (Q01320.2)"
     Site            1323
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q01320.2)"
     Site            1328
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q01320.2)"
     Site            1333
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q01320.2)"
     Site            1350
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q01320.2)"
     Site            1370
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P11388; propagated from
                     UniProtKB/Swiss-Prot (Q01320.2)"
     Site            1373
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q01320.2)"
     Site            1384
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P11388; propagated from
                     UniProtKB/Swiss-Prot (Q01320.2)"
     Site            1388
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q01320.2)"
     Site            1418
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:23806337; propagated from
                     UniProtKB/Swiss-Prot (Q01320.2)"
     Region          1429..1435
                     /region_name="Interaction with PLSCR1.
                     /evidence=ECO:0000250|UniProtKB:P11388"
                     /note="propagated from UniProtKB/Swiss-Prot (Q01320.2)"
     Region          1431..1518
                     /region_name="DTHCT"
                     /note="DTHCT (NUC029) region; pfam08070"
                     /db_xref="CDD:462355"
     Site            1438
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:23806337; propagated from
                     UniProtKB/Swiss-Prot (Q01320.2)"
     Site            1465
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P11388; propagated from
                     UniProtKB/Swiss-Prot (Q01320.2)"
     Site            1467
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P11388; propagated from
                     UniProtKB/Swiss-Prot (Q01320.2)"
     Site            1470
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P11388; propagated from
                     UniProtKB/Swiss-Prot (Q01320.2)"
     Site            1472
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P11388; propagated from
                     UniProtKB/Swiss-Prot (Q01320.2)"
     Site            1521
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q01320.2)"
     CDS             1..1528
                     /gene="Top2a"
                     /gene_synonym="Top-2"
                     /coded_by="NM_011623.2:124..4710"
                     /db_xref="CCDS:CCDS25370.1"
                     /db_xref="GeneID:21973"
                     /db_xref="MGI:MGI:98790"
ORIGIN      
        1 melsplqpvn enmlmnkkkn edgkkrlsie riyqkktqle hillrpdtyi gsvelvtqqm
       61 wvydedvgin yrevtfvpgl ykifdeilvn aadnkqrdpk mscirvtidp ennvisiwnn
      121 gkgipvvehk vekiyvpali fgqlltssny dddekkvtgg rngygaklcn ifstkftvet
      181 asreykkmfk qtwmdnmgra gdmelkpfsg edytcitfqp dlskfkmqsl dkdivalmvr
      241 raydiagstk dvkvflngns lpvkgfrsyv dlylkdkvde tgnslkvihe qvnprwevcl
      301 tmsergfqqi sfvnsiatsk ggrhvdyvad qivsklvdvv kkknkggvav kahqvknhmw
      361 ifvnalienp tfdsqtkenm tlqaksfgst cqlsekfika aigcgivesi lnwvkfkaqi
      421 qlnkkcsavk htkikgipkl ddandagsrn stectlilte gdsaktlavs glgvvgrdky
      481 gvfplrgkil nvreashkqi menaeinnii kivglqykkn yededslktl rygkimimtd
      541 qdqdgshikg llinfihhnw psllrhrfle efitpivkvs knkqeiafys lpefeewkss
      601 tpnhkkwkvk yykglgtsts keakeyfadm krhriqfkys gpeddaaisl afskkqvddr
      661 kewltnfmed rrqrkllglp edylygqsts yltyndfink elilfsnsdn ersipsmvdg
      721 lkpgqrkvlf tcfkrndkre vkvaqlagsv aemssyhhge mslmmtiinl aqnfvgsnnl
      781 nllqpigqfg trlhggkdsa spryiftmls plarllfppk ddhtlrflyd dnqrvepewy
      841 ipiipmvlin gaegigtgws ckipnfdvre vvnnirrlld geeplpmlps yknfkgtiee
      901 lasnqyving evaildstti eiselpirtw tqtykeqvle pmlngtektp slitdyreyh
      961 tdttvkfvik mteeklaeae rvglhkvfkl qssltcnsmv lfdhvgclkk ydtvldilrd
     1021 ffelrlkyyg lrkewllgml gaessklnnq arfilekidg kivienkpkk elikvliqrg
     1081 ydsdpvkawk eaqqkvpdee eneesdtets tsdsaaeagp tfnylldmpl wyltkekkde
     1141 lckqrnekeq elntlkqksp sdlwkedlav fieelevvea kekqdeqvgl pgkagkakgk
     1201 kaqmcadvlp sprgkrvipq vtvemkaeae kkirkkikse nvegtpaedg aepgslrqri
     1261 ekkqkkepga kkqttlpfkp vkkgrkknpw sdsesdvssn esnvdvpprq keqrsaaaka
     1321 kftvdldsde dfsgldekde dedflpldat ppkakippkn tkkalktqgs smsvvdlesd
     1381 vkdsvpaspg vpaadfpaet eqskpskktv gvkktatksq ssvstagtkk raapkgtksd
     1441 salsarvsek papakaknsr krkpsssdss dsdferaisk gatskkakge eqdfpvdled
     1501 tiapraksdr arkpikylee sdddddlf
//
