ID TOP2A_MOUSE Reviewed; 1528 AA.
AC Q01320; E9PX08;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 2.
DT 27-MAR-2024, entry version 216.
DE RecName: Full=DNA topoisomerase 2-alpha;
DE EC=5.6.2.2 {ECO:0000255|PROSITE-ProRule:PRU00995, ECO:0000269|PubMed:1331984};
DE AltName: Full=DNA topoisomerase II, alpha isozyme;
GN Name=Top2a; Synonyms=Top-2, Top2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, AND FUNCTION.
RX PubMed=1331984; DOI=10.1093/nar/20.20.5297;
RA Adachi N., Miyaike M., Ikeda H., Kikuchi A.;
RT "Characterization of cDNA encoding the mouse DNA topoisomerase II that can
RT complement the budding yeast top2 mutation.";
RL Nucleic Acids Res. 20:5297-5303(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1254-1528.
RC TISSUE=Lymphoma;
RX PubMed=8261398;
RA McPherson J., Brown G.A., Goldenberg G.J.;
RT "Characterization of a DNA topoisomerase IIalpha gene rearrangement in
RT adriamycin-resistant P388 leukemia: expression of a fusion messenger RNA
RT transcript encoding topoisomerase IIalpha and the retinoic acid receptor
RT alpha locus.";
RL Cancer Res. 53:5885-5889(1993).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1211; THR-1245; THR-1323;
RP SER-1328; SER-1333; THR-1350; SER-1373; SER-1388 AND SER-1521, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver, Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1418 AND LYS-1438, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [6]
RP FUNCTION.
RX PubMed=24321095; DOI=10.1016/j.bbrc.2013.11.116;
RA Ogawa Y., Kawano Y., Yamazaki Y., Onishi Y.;
RT "Shikonin shortens the circadian period: possible involvement of Top2
RT inhibition.";
RL Biochem. Biophys. Res. Commun. 443:339-343(2014).
RN [7]
RP INTERACTION WITH GCNA.
RX PubMed=31839538; DOI=10.1016/j.devcel.2019.11.006;
RA Dokshin G.A., Davis G.M., Sawle A.D., Eldridge M.D., Nicholls P.K.,
RA Gourley T.E., Romer K.A., Molesworth L.W., Tatnell H.R., Ozturk A.R.,
RA de Rooij D.G., Hannon G.J., Page D.C., Mello C.C., Carmell M.A.;
RT "GCNA Interacts with Spartan and Topoisomerase II to Regulate Genome
RT Stability.";
RL Dev. Cell 52:53-68(2020).
CC -!- FUNCTION: Key decatenating enzyme that alters DNA topology by binding
CC to two double-stranded DNA molecules, generating a double-stranded
CC break in one of the strands, passing the intact strand through the
CC broken strand, and religating the broken strand (PubMed:1331984). May
CC play a role in regulating the period length of BMAL1 transcriptional
CC oscillation (PubMed:24321095). {ECO:0000269|PubMed:1331984,
CC ECO:0000269|PubMed:24321095}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP-dependent breakage, passage and rejoining of double-
CC stranded DNA.; EC=5.6.2.2; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU00995, ECO:0000269|PubMed:1331984};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00995};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00995};
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00995};
CC Note=Binds two Mg(2+) per subunit. The magnesium ions form salt bridges
CC with both the protein and the DNA. Can also accept other divalent metal
CC cations, such as Mn(2+) or Ca(2+). {ECO:0000255|PROSITE-
CC ProRule:PRU00995};
CC -!- SUBUNIT: Homodimer (By similarity). Interacts with COPS5 (By
CC similarity). Interacts with RECQL5; this stimulates DNA decatenation
CC (By similarity). Interacts with SETMAR; stimulates the topoisomerase
CC activity (By similarity). Interacts with DHX9; this interaction occurs
CC in a E2 enzyme UBE2I- and RNA-dependent manner, negatively regulates
CC DHX9-mediated double-stranded DNA and RNA duplex helicase activity and
CC stimulates TOP2A-mediated supercoiled DNA relaxation activity (By
CC similarity). Interacts with HNRNPU (via C-terminus); this interaction
CC protects the topoisomerase TOP2A from degradation and positively
CC regulates the relaxation of supercoiled DNA in a RNA-dependent manner
CC (By similarity). Interacts with MCM3AP (By similarity). Interacts with
CC ERCC6 (By similarity). Interacts with PLSCR1 (By similarity). Interacts
CC with GCNA; this interaction allows the resolution of topoisomerase II
CC (TOP2A) DNA-protein cross-links (PubMed:31839538). Interacts with
CC POL1RA/RPA1 (via dock II) and UBTF in the context of Pol I complex; may
CC assist Pol I transcription initiation by releasing supercoils occurring
CC during DNA unwinding. {ECO:0000250|UniProtKB:P11388,
CC ECO:0000250|UniProtKB:P41516, ECO:0000269|PubMed:31839538}.
CC -!- INTERACTION:
CC Q01320; Q3TKT4: Smarca4; NbExp=3; IntAct=EBI-642809, EBI-1210244;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P11388}.
CC Nucleus, nucleoplasm {ECO:0000250|UniProtKB:P11388}. Nucleus
CC {ECO:0000250|UniProtKB:P11388}. Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:P11388}.
CC -!- PTM: Phosphorylation has no effect on catalytic activity (By
CC similarity). However, phosphorylation at Ser-1105 by CSNK1D/CK1
CC promotes DNA cleavable complex formation (By similarity).
CC {ECO:0000250|UniProtKB:P11388}.
CC -!- MISCELLANEOUS: Eukaryotic topoisomerase I and II can relax both
CC negative and positive supercoils, whereas prokaryotic enzymes relax
CC only negative supercoils.
CC -!- SIMILARITY: Belongs to the type II topoisomerase family. {ECO:0000305}.
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DR EMBL; D12513; BAA02076.1; -; mRNA.
DR EMBL; AL591067; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; U01915; AAC52135.1; -; mRNA.
DR CCDS; CCDS25370.1; -.
DR PIR; JS0703; JS0703.
DR RefSeq; NP_035753.2; NM_011623.2.
DR RefSeq; XP_006533216.1; XM_006533153.2.
DR AlphaFoldDB; Q01320; -.
DR SMR; Q01320; -.
DR BioGRID; 204276; 28.
DR CORUM; Q01320; -.
DR DIP; DIP-40621N; -.
DR IntAct; Q01320; 22.
DR MINT; Q01320; -.
DR STRING; 10090.ENSMUSP00000068896; -.
DR ChEMBL; CHEMBL3586; -.
DR GlyGen; Q01320; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q01320; -.
DR PhosphoSitePlus; Q01320; -.
DR SwissPalm; Q01320; -.
DR EPD; Q01320; -.
DR jPOST; Q01320; -.
DR MaxQB; Q01320; -.
DR PaxDb; 10090-ENSMUSP00000068896; -.
DR PeptideAtlas; Q01320; -.
DR ProteomicsDB; 260721; -.
DR Pumba; Q01320; -.
DR Antibodypedia; 1583; 1693 antibodies from 45 providers.
DR DNASU; 21973; -.
DR Ensembl; ENSMUST00000068031.8; ENSMUSP00000068896.8; ENSMUSG00000020914.18.
DR GeneID; 21973; -.
DR KEGG; mmu:21973; -.
DR UCSC; uc007lid.1; mouse.
DR AGR; MGI:98790; -.
DR CTD; 7153; -.
DR MGI; MGI:98790; Top2a.
DR VEuPathDB; HostDB:ENSMUSG00000020914; -.
DR eggNOG; KOG0355; Eukaryota.
DR GeneTree; ENSGT00940000157539; -.
DR HOGENOM; CLU_001935_1_0_1; -.
DR InParanoid; Q01320; -.
DR OMA; NESMDYN; -.
DR OrthoDB; 1944951at2759; -.
DR PhylomeDB; Q01320; -.
DR TreeFam; TF105282; -.
DR BRENDA; 5.99.1.3; 3474.
DR Reactome; R-MMU-4615885; SUMOylation of DNA replication proteins.
DR BioGRID-ORCS; 21973; 28 hits in 79 CRISPR screens.
DR ChiTaRS; Top2a; mouse.
DR PRO; PR:Q01320; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q01320; Protein.
DR Bgee; ENSMUSG00000020914; Expressed in undifferentiated genital tubercle and 227 other cell types or tissues.
DR Genevisible; Q01320; MM.
DR GO; GO:0005814; C:centriole; IEA:Ensembl.
DR GO; GO:0000775; C:chromosome, centromeric region; IDA:MGI.
DR GO; GO:0000793; C:condensed chromosome; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0009330; C:DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) complex; ISO:MGI.
DR GO; GO:0001673; C:male germ cell nucleus; IDA:MGI.
DR GO; GO:0000228; C:nuclear chromosome; IEA:Ensembl.
DR GO; GO:0005730; C:nucleolus; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:1990904; C:ribonucleoprotein complex; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; ISO:MGI.
DR GO; GO:0008094; F:ATP-dependent activity, acting on DNA; ISO:MGI.
DR GO; GO:0003682; F:chromatin binding; ISO:MGI.
DR GO; GO:0003677; F:DNA binding; ISO:MGI.
DR GO; GO:0008301; F:DNA binding, bending; ISS:UniProtKB.
DR GO; GO:0003916; F:DNA topoisomerase activity; ISO:MGI.
DR GO; GO:0003918; F:DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity; IDA:MGI.
DR GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR GO; GO:0046982; F:protein heterodimerization activity; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0005080; F:protein kinase C binding; ISO:MGI.
DR GO; GO:0043565; F:sequence-specific DNA binding; ISO:MGI.
DR GO; GO:0043130; F:ubiquitin binding; ISO:MGI.
DR GO; GO:0030263; P:apoptotic chromosome condensation; ISO:MGI.
DR GO; GO:0030261; P:chromosome condensation; IMP:MGI.
DR GO; GO:0007059; P:chromosome segregation; IDA:MGI.
DR GO; GO:0006974; P:DNA damage response; ISO:MGI.
DR GO; GO:0006266; P:DNA ligation; ISO:MGI.
DR GO; GO:0006265; P:DNA topological change; IDA:MGI.
DR GO; GO:0040016; P:embryonic cleavage; IMP:MGI.
DR GO; GO:0051309; P:female meiosis chromosome separation; TAS:MGI.
DR GO; GO:0007143; P:female meiotic nuclear division; IMP:MGI.
DR GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IMP:MGI.
DR GO; GO:1905463; P:negative regulation of DNA duplex unwinding; ISS:UniProtKB.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISO:MGI.
DR GO; GO:0045870; P:positive regulation of single stranded viral RNA replication via double stranded DNA intermediate; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:MGI.
DR GO; GO:0042752; P:regulation of circadian rhythm; IMP:UniProtKB.
DR GO; GO:0000712; P:resolution of meiotic recombination intermediates; IBA:GO_Central.
DR GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
DR GO; GO:0000819; P:sister chromatid segregation; IBA:GO_Central.
DR CDD; cd16930; HATPase_TopII-like; 1.
DR CDD; cd00187; TOP4c; 1.
DR CDD; cd03481; TopoIIA_Trans_ScTopoIIA; 1.
DR CDD; cd03365; TOPRIM_TopoIIA; 1.
DR Gene3D; 3.30.1360.40; -; 1.
DR Gene3D; 3.30.1490.30; -; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.40.50.670; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.90.199.10; Topoisomerase II, domain 5; 1.
DR Gene3D; 1.10.268.10; Topoisomerase, domain 3; 1.
DR InterPro; IPR012542; DTHCT.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR InterPro; IPR001241; Topo_IIA.
DR InterPro; IPR013760; Topo_IIA-like_dom_sf.
DR InterPro; IPR013758; Topo_IIA_A/C_ab.
DR InterPro; IPR013757; Topo_IIA_A_a_sf.
DR InterPro; IPR013759; Topo_IIA_B_C.
DR InterPro; IPR013506; Topo_IIA_bsu_dom2.
DR InterPro; IPR002205; Topo_IIA_dom_A.
DR InterPro; IPR001154; TopoII_euk.
DR InterPro; IPR018522; TopoIIA_CS.
DR InterPro; IPR031660; TOPRIM_C.
DR InterPro; IPR006171; TOPRIM_domain.
DR InterPro; IPR034157; TOPRIM_TopoII.
DR PANTHER; PTHR10169:SF61; DNA TOPOISOMERASE 2-ALPHA; 1.
DR PANTHER; PTHR10169; DNA TOPOISOMERASE/GYRASE; 1.
DR Pfam; PF00204; DNA_gyraseB; 1.
DR Pfam; PF00521; DNA_topoisoIV; 1.
DR Pfam; PF08070; DTHCT; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF01751; Toprim; 1.
DR Pfam; PF16898; TOPRIM_C; 1.
DR PRINTS; PR01158; TOPISMRASEII.
DR PRINTS; PR00418; TPI2FAMILY.
DR SMART; SM00433; TOP2c; 1.
DR SMART; SM00434; TOP4c; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR SUPFAM; SSF56719; Type II DNA topoisomerase; 1.
DR PROSITE; PS52040; TOPO_IIA; 1.
DR PROSITE; PS00177; TOPOISOMERASE_II; 1.
DR PROSITE; PS50880; TOPRIM; 1.
PE 1: Evidence at protein level;
KW Acetylation; ATP-binding; Biological rhythms; Cytoplasm; DNA-binding;
KW Isomerase; Isopeptide bond; Magnesium; Metal-binding; Nucleotide-binding;
KW Nucleus; Phosphoprotein; Reference proteome; Topoisomerase;
KW Ubl conjugation.
FT CHAIN 1..1528
FT /note="DNA topoisomerase 2-alpha"
FT /id="PRO_0000145364"
FT DOMAIN 454..571
FT /note="Toprim"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT DOMAIN 714..1168
FT /note="Topo IIA-type catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01384"
FT REGION 341..343
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT REGION 989..998
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT REGION 1090..1118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1183..1211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1229..1528
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1429..1435
FT /note="Interaction with PLSCR1"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT COMPBIAS 1229..1245
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1254..1272
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1312..1328
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1329..1344
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1363..1377
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1403..1428
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1461..1520
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 804
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01384"
FT BINDING 90
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT BINDING 119
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT BINDING 147..149
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT BINDING 160..167
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT BINDING 375..377
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT BINDING 460
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT BINDING 540
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT BINDING 540
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT BINDING 542
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 488
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 491
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 660
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 661
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 722
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 756
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 762
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 803
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P06786"
FT SITE 855
FT /note="Important for DNA bending; intercalates between base
FT pairs of target DNA"
FT /evidence="ECO:0000250|UniProtKB:P06786"
FT SITE 930
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT MOD_RES 4
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT MOD_RES 281
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT MOD_RES 1105
FT /note="Phosphoserine; by CK1"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT MOD_RES 1211
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1245
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1291
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT MOD_RES 1293
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT MOD_RES 1295
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT MOD_RES 1298
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT MOD_RES 1323
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1328
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1333
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1350
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1370
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT MOD_RES 1373
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1384
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT MOD_RES 1388
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1418
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 1438
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 1465
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT MOD_RES 1467
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT MOD_RES 1470
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT MOD_RES 1472
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT MOD_RES 1521
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CROSSLNK 17
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 155
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 156
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 351
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 385
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 396
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 415
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 417
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 424
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 439
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 465
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 479
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 528
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 583
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 598
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 613
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 621
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 624
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 631
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 638
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 654
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 661
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 675
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 1074
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 1193
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 1201
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 1226
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 1238
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 1238
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 1272
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 1279
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 1282
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 1359
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 1363
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 1382
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 1418
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 1438
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 1450
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 1455
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 1480
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 1488
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CONFLICT 184
FT /note="E -> A (in Ref. 1; BAA02076)"
FT /evidence="ECO:0000305"
FT CONFLICT 260
FT /note="S -> M (in Ref. 1; BAA02076)"
FT /evidence="ECO:0000305"
FT CONFLICT 640
FT /note="S -> P (in Ref. 1; BAA02076)"
FT /evidence="ECO:0000305"
FT CONFLICT 841
FT /note="I -> N (in Ref. 1; BAA02076)"
FT /evidence="ECO:0000305"
FT CONFLICT 844..845
FT /note="IP -> NT (in Ref. 1; BAA02076)"
FT /evidence="ECO:0000305"
FT CONFLICT 1316
FT /note="A -> R (in Ref. 1; BAA02076 and 3; AAC52135)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1528 AA; 172790 MW; 63CBF8F649D103C7 CRC64;
MELSPLQPVN ENMLMNKKKN EDGKKRLSIE RIYQKKTQLE HILLRPDTYI GSVELVTQQM
WVYDEDVGIN YREVTFVPGL YKIFDEILVN AADNKQRDPK MSCIRVTIDP ENNVISIWNN
GKGIPVVEHK VEKIYVPALI FGQLLTSSNY DDDEKKVTGG RNGYGAKLCN IFSTKFTVET
ASREYKKMFK QTWMDNMGRA GDMELKPFSG EDYTCITFQP DLSKFKMQSL DKDIVALMVR
RAYDIAGSTK DVKVFLNGNS LPVKGFRSYV DLYLKDKVDE TGNSLKVIHE QVNPRWEVCL
TMSERGFQQI SFVNSIATSK GGRHVDYVAD QIVSKLVDVV KKKNKGGVAV KAHQVKNHMW
IFVNALIENP TFDSQTKENM TLQAKSFGST CQLSEKFIKA AIGCGIVESI LNWVKFKAQI
QLNKKCSAVK HTKIKGIPKL DDANDAGSRN STECTLILTE GDSAKTLAVS GLGVVGRDKY
GVFPLRGKIL NVREASHKQI MENAEINNII KIVGLQYKKN YEDEDSLKTL RYGKIMIMTD
QDQDGSHIKG LLINFIHHNW PSLLRHRFLE EFITPIVKVS KNKQEIAFYS LPEFEEWKSS
TPNHKKWKVK YYKGLGTSTS KEAKEYFADM KRHRIQFKYS GPEDDAAISL AFSKKQVDDR
KEWLTNFMED RRQRKLLGLP EDYLYGQSTS YLTYNDFINK ELILFSNSDN ERSIPSMVDG
LKPGQRKVLF TCFKRNDKRE VKVAQLAGSV AEMSSYHHGE MSLMMTIINL AQNFVGSNNL
NLLQPIGQFG TRLHGGKDSA SPRYIFTMLS PLARLLFPPK DDHTLRFLYD DNQRVEPEWY
IPIIPMVLIN GAEGIGTGWS CKIPNFDVRE VVNNIRRLLD GEEPLPMLPS YKNFKGTIEE
LASNQYVING EVAILDSTTI EISELPIRTW TQTYKEQVLE PMLNGTEKTP SLITDYREYH
TDTTVKFVIK MTEEKLAEAE RVGLHKVFKL QSSLTCNSMV LFDHVGCLKK YDTVLDILRD
FFELRLKYYG LRKEWLLGML GAESSKLNNQ ARFILEKIDG KIVIENKPKK ELIKVLIQRG
YDSDPVKAWK EAQQKVPDEE ENEESDTETS TSDSAAEAGP TFNYLLDMPL WYLTKEKKDE
LCKQRNEKEQ ELNTLKQKSP SDLWKEDLAV FIEELEVVEA KEKQDEQVGL PGKAGKAKGK
KAQMCADVLP SPRGKRVIPQ VTVEMKAEAE KKIRKKIKSE NVEGTPAEDG AEPGSLRQRI
EKKQKKEPGA KKQTTLPFKP VKKGRKKNPW SDSESDVSSN ESNVDVPPRQ KEQRSAAAKA
KFTVDLDSDE DFSGLDEKDE DEDFLPLDAT PPKAKIPPKN TKKALKTQGS SMSVVDLESD
VKDSVPASPG VPAADFPAET EQSKPSKKTV GVKKTATKSQ SSVSTAGTKK RAAPKGTKSD
SALSARVSEK PAPAKAKNSR KRKPSSSDSS DSDFERAISK GATSKKAKGE EQDFPVDLED
TIAPRAKSDR ARKPIKYLEE SDDDDDLF
//
