CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-002392
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 DNA topoisomerase 2 
Protein Synonyms/Alias
 DNA topoisomerase II 
Gene Name
 TOP2 
Gene Synonyms/Alias
 TOR3; YNL088W; N2244 
Created Date
 July 27, 2013 
Organism
 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 
NCBI Taxa ID
 559292 
Lysine Modification
Position
Peptide
Type
References
11EPVSASDKYQKISQLacetylation[1]
1220ARKGKKIKLEDKNFEsumoylation[2, 3, 4]
1246SKAPTKIKKEKTPSVsumoylation[2, 3, 4]
1277SSSIFDIKKEDKDEGsumoylation[2, 3, 4]
1302KISTIFDKMGSTSATacetylation[1]
Reference
 [1] Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae.
 Henriksen P, Wagner SA, Weinert BT, Sharma S, Bacinskaja G, Rehman M, Juffer AH, Walther TC, Lisby M, Choudhary C.
 Mol Cell Proteomics. 2012 Nov;11(11):1510-22. [PMID: 22865919]
 [2] The SUMO-1 isopeptidase Smt4 is linked to centromeric cohesion through SUMO-1 modification of DNA topoisomerase II.
 Bachant J, Alcasabas A, Blat Y, Kleckner N, Elledge SJ.
 Mol Cell. 2002 Jun;9(6):1169-82. [PMID: 12086615]
 [3] SIZ1/SIZ2 control of chromosome transmission fidelity is mediated by the sumoylation of topoisomerase II.
 Takahashi Y, Yong-Gonzalez V, Kikuchi Y, Strunnikov A.
 Genetics. 2006 Feb;172(2):783-94. [PMID: 16204216]
 [4] Top2 SUMO conjugation in yeast cell lysates.
 Baldwin M, Bachant J.
 Methods Mol Biol. 2009;582:209-19. [PMID: 19763952] 
Functional Description
 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. 
Sequence Annotation
 DOMAIN 443 557 Toprim.
 NP_BIND 127 129 ATP.
 NP_BIND 140 147 ATP.
 NP_BIND 365 367 ATP.
 REGION 333 336 Interaction with DNA.
 REGION 965 974 Interaction with DNA.
 ACT_SITE 782 782 O-(5'-phospho-DNA)-tyrosine intermediate.
 METAL 449 449 Magnesium 1; catalytic.
 METAL 526 526 Magnesium 1; catalytic.
 METAL 526 526 Magnesium 2.
 METAL 528 528 Magnesium 2.
 BINDING 70 70 ATP.
 BINDING 99 99 ATP.
 MOD_RES 1086 1086 Phosphothreonine; by CK2.
 MOD_RES 1087 1087 Phosphoserine; by CK2.
 MOD_RES 1252 1252 Phosphoserine.
 MOD_RES 1258 1258 Phosphothreonine; by CK2.
 MOD_RES 1266 1266 Phosphoserine; by CK2.
 MOD_RES 1269 1269 Phosphoserine; by CK2.
 MOD_RES 1272 1272 Phosphoserine; by CK2.
 MOD_RES 1353 1353 Phosphoserine; by CK2.
 MOD_RES 1356 1356 Phosphoserine; by CK2.
 MOD_RES 1408 1408 Phosphoserine; by CK2.
 MOD_RES 1423 1423 Phosphoserine; by CK2.  
Keyword
 3D-structure; ATP-binding; Complete proteome; DNA-binding; Isomerase; Magnesium; Metal-binding; Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome; Topoisomerase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1428 AA 
Protein Sequence
MSTEPVSASD KYQKISQLEH ILKRPDTYIG SVETQEQLQW IYDEETDCMI EKNVTIVPGL 60
FKIFDEILVN AADNKVRDPS MKRIDVNIHA EEHTIEVKND GKGIPIEIHN KENIYIPEMI 120
FGHLLTSSNY DDDEKKVTGG RNGYGAKLCN IFSTEFILET ADLNVGQKYV QKWENNMSIC 180
HPPKITSYKK GPSYTKVTFK PDLTRFGMKE LDNDILGVMR RRVYDINGSV RDINVYLNGK 240
SLKIRNFKNY VELYLKSLEK KRQLDNGEDG AAKSDIPTIL YERINNRWEV AFAVSDISFQ 300
QISFVNSIAT TMGGTHVNYI TDQIVKKISE ILKKKKKKSV KSFQIKNNMF IFINCLIENP 360
AFTSQTKEQL TTRVKDFGSR CEIPLEYINK IMKTDLATRM FEIADANEEN ALKKSDGTRK 420
SRITNYPKLE DANKAGTKEG YKCTLVLTEG DSALSLAVAG LAVVGRDYYG CYPLRGKMLN 480
VREASADQIL KNAEIQAIKK IMGLQHRKKY EDTKSLRYGH LMIMTDQDHD GSHIKGLIIN 540
FLESSFPGLL DIQGFLLEFI TPIIKVSITK PTKNTIAFYN MPDYEKWREE ESHKFTWKQK 600
YYKGLGTSLA QEVREYFSNL DRHLKIFHSL QGNDKDYIDL AFSKKKADDR KEWLRQYEPG 660
TVLDPTLKEI PISDFINKEL ILFSLADNIR SIPNVLDGFK PGQRKVLYGC FKKNLKSELK 720
VAQLAPYVSE CTAYHHGEQS LAQTIIGLAQ NFVGSNNIYL LLPNGAFGTR ATGGKDAAAA 780
RYIYTELNKL TRKIFHPADD PLYKYIQEDE KTVEPEWYLP ILPMILVNGA EGIGTGWSTY 840
IPPFNPLEII KNIRHLMNDE ELEQMHPWFR GWTGTIEEIE PLRYRMYGRI EQIGDNVLEI 900
TELPARTWTS TIKEYLLLGL SGNDKIKPWI KDMEEQHDDN IKFIITLSPE EMAKTRKIGF 960
YERFKLISPI SLMNMVAFDP HGKIKKYNSV NEILSEFYYV RLEYYQKRKD HMSERLQWEV 1020
EKYSFQVKFI KMIIEKELTV TNKPRNAIIQ ELENLGFPRF NKEGKPYYGS PNDEIAEQIN 1080
DVKGATSDEE DEESSHEDTE NVINGPEELY GTYEYLLGMR IWSLTKERYQ KLLKQKQEKE 1140
TELENLLKLS AKDIWNTDLK AFEVGYQEFL QRDAEARGGN VPNKGSKTKG KGKRKLVDDE 1200
DYDPSKKNKK STARKGKKIK LEDKNFERIL LEQKLVTKSK APTKIKKEKT PSVSETKTEE 1260
EENAPSSTSS SSIFDIKKED KDEGELSKIS NKFKKISTIF DKMGSTSATS KENTPEQDDV 1320
ATKKNQTTAK KTAVKPKLAK KPVRKQQKVV ELSGESDLEI LDSYTDREDS NKDEDDAIPQ 1380
RSRRQRSSRA ASVPKKSYVE TLELSDDSFI EDDEEENQGS DVSFNEED 1428 
Gene Ontology
 GO:0097047; C:DNA replication termination region; IPI:SGD.
 GO:0009330; C:DNA topoisomerase complex (ATP-hydrolyzing); IBA:RefGenome.
 GO:0005739; C:mitochondrion; IDA:SGD.
 GO:0000795; C:synaptonemal complex; IDA:SGD.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0003918; F:DNA topoisomerase type II (ATP-hydrolyzing) activity; IDA:SGD.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0006333; P:chromatin assembly or disassembly; IMP:SGD.
 GO:0031055; P:chromatin remodeling at centromere; IMP:SGD.
 GO:0006271; P:DNA strand elongation involved in DNA replication; IMP:SGD.
 GO:0006265; P:DNA topological change; IDA:SGD.
 GO:0044774; P:mitotic DNA integrity checkpoint; IMP:SGD.
 GO:0000019; P:regulation of mitotic recombination; IMP:SGD.
 GO:0097046; P:replication fork progression beyond termination site; IMP:SGD.
 GO:0000712; P:resolution of meiotic recombination intermediates; IBA:RefGenome.
 GO:0000819; P:sister chromatid segregation; IBA:RefGenome. 
Interpro
 IPR024946; Arg_repress_C-like.
 IPR003594; HATPase_ATP-bd.
 IPR020568; Ribosomal_S5_D2-typ_fold.
 IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
 IPR001241; Topo_IIA.
 IPR002205; Topo_IIA_A/C.
 IPR013758; Topo_IIA_A/C_ab.
 IPR013757; Topo_IIA_A_a.
 IPR013506; Topo_IIA_bsu_dom2.
 IPR013759; Topo_IIA_cen_dom.
 IPR013760; Topo_IIA_like_dom.
 IPR018522; TopoIIA_CS.
 IPR006171; Toprim_domain. 
Pfam
 PF00204; DNA_gyraseB
 PF00521; DNA_topoisoIV
 PF02518; HATPase_c
 PF01751; Toprim 
SMART
 SM00387; HATPase_c
 SM00433; TOP2c
 SM00434; TOP4c 
PROSITE
 PS00177; TOPOISOMERASE_II
 PS50880; TOPRIM 
PRINTS
 PR00418; TPI2FAMILY.