CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-004329
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
 CG10223 
Created Date
 July 27, 2013 
Organism
 Drosophila melanogaster (Fruit fly) 
NCBI Taxa ID
 7227 
Lysine Modification
Position
Peptide
Type
References
333NKGGINIKPFQVRNHacetylation[1]
509YLTEDDLKTLRYGKVacetylation[1]
1061AMCDELLKRGYRPDPacetylation[1]
Reference
 [1] Proteome-wide mapping of the Drosophila acetylome demonstrates a high degree of conservation of lysine acetylation.
 Weinert BT, Wagner SA, Horn H, Henriksen P, Liu WR, Olsen JV, Jensen LJ, Choudhary C.
 Sci Signal. 2011 Jul 26;4(183):ra48. [PMID: 21791702] 
Functional Description
 Control of topological states of DNA by transient breakage and subsequent rejoining of DNA strands. Topoisomerase II makes double-strand breaks. 
Sequence Annotation
 DOMAIN 435 552 Toprim.
 NP_BIND 129 131 ATP (By similarity).
 NP_BIND 142 149 ATP (By similarity).
 NP_BIND 357 359 ATP (By similarity).
 REGION 323 325 Interaction with DNA (By similarity).
 ACT_SITE 785 785 O-(5'-phospho-DNA)-tyrosine intermediate
 METAL 441 441 Magnesium 1; catalytic (By similarity).
 METAL 521 521 Magnesium 1; catalytic (By similarity).
 METAL 521 521 Magnesium 2 (By similarity).
 METAL 523 523 Magnesium 2 (By similarity).
 BINDING 72 72 ATP (By similarity).
 BINDING 101 101 ATP (By similarity).
 MOD_RES 1284 1284 Phosphoserine.
 MOD_RES 1344 1344 Phosphoserine.
 MOD_RES 1352 1352 Phosphothreonine.
 MOD_RES 1374 1374 Phosphoserine.
 MOD_RES 1385 1385 Phosphoserine.
 MOD_RES 1392 1392 Phosphoserine.
 MOD_RES 1396 1396 Phosphoserine.  
Keyword
 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
 1447 AA 
Protein Sequence
MENGNKALSI EQMYQKKSQL EHILLRPDSY IGSVEFTKEL MWVYDNSQNR MVQKEISFVP 60
GLYKIFDEIL VNAADNKQRD KSMNTIKIDI DPERNMVSVW NNGQGIPVTM HKEQKMYVPT 120
MIFGHLLTSS NYNDDEKKVT GGRNGYGAKL CNIFSTSFTV ETATREYKKS FKQTWGNNMG 180
KASDVQIKDF NGTDYTRITF SPDLAKFKMD RLDEDIVALM SRRAYDVAAS SKGVSVFLNG 240
NKLGVRNFKD YIDLHIKNTD DDSGPPIKIV HEVANERWEV ACCPSDRGFQ QVSFVNSIAT 300
YKGGRHVDHV VDNLIKQLLE VLKKKNKGGI NIKPFQVRNH LWVFVNCLIE NPTFDSQTKE 360
NMTLQQKGFG SKCTLSEKFI NNMSKSGIVE SVLAWAKFKA QNDIAKTGGR KSSKIKGIPK 420
LEDANEAGGK NSIKCTLILT EGDSAKSLAV SGLGVIGRDL YGVFPLRGKL LNVREANFKQ 480
LSENAEINNL CKIIGLQYKK KYLTEDDLKT LRYGKVMIMT DQDQDGSHIK GLLINFIHTN 540
WPELLRLPFL EEFITPIVKA TKKNEELSFY SLPEFEEWKN DTANHHTYNI KYYKGLGTST 600
SKEAKEYFQD MDRHRILFKY DGSVDDESIV MAFSKKHIES RKVWLTNHMD EVKRRKELGL 660
PERYLYTKGT KSITYADFIN LELVLFSNAD NERSIPSLVD GLKPGQRKVM FTCFKRNDKR 720
EVKVAQLSGS VAEMSAYHHG EVSLQMTIVN LAQNFVGANN INLLEPRGQF GTRLSGGKDC 780
ASARYIFTIM SPLTRLIYHP LDDPLLDYQV DDGQKIEPLW YLPIIPMVLV NGAEGIGTGW 840
STKISNYNPR EIMKNLRKMI NGQEPSVMHP WYKNFLGRME YVSDGRYIQT GNIQILSGNR 900
LEISELPVGV WTQNYKENVL EPLSNGTEKV KGIISEYREY HTDTTVRFVI SFAPGEFERI 960
HAEEGGFYRV FKLTTTLSTN QMHAFDQNNC LRRFPTAIDI LKEYYKLRRE YYARRRDFLV 1020
GQLTAQADRL SDQARFILEK CEKKLVVENK QRKAMCDELL KRGYRPDPVK EWQRRIKMED 1080
AEQADEEDEE EEEAAPSVSS KAKKEKEVDP EKAFKKLTDV KKFDYLLGMS MWMLTEEKKN 1140
ELLKQRDTKL SELESLRKKT PEMLWLDDLD ALESKLNEVE EKERAEEQGI NLKTAKALKG 1200
QKSASAKGRK VKSMGGGAGA GDVFPDPDGE PVEFKITEEI IKKMAAAAKV AQAAKEPKKP 1260
KEPKEPKVKK EPKGKQIKAE PDASGDEVDE FDAMVEGGSK TSPKAKKAVV KKEPGEKKPR 1320
QKKENGGGLK QSKIDFSKAK AKKSDDDVEE VTPRAERPGR RQASKKIDYS SLFSDEEEDG 1380
GNVGSDDDGN ASDDDSPKRP AKRGREDESS GGAKKKAPPK KRRAVIESDD DDIEIDEDDD 1440
DDSDFNC 1447 
Gene Ontology
 GO:0008623; C:CHRAC; IDA:FlyBase.
 GO:0000795; C:synaptonemal complex; IBA:RefGenome.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0003918; F:DNA topoisomerase type II (ATP-hydrolyzing) activity; IDA:FlyBase.
 GO:0000400; F:four-way junction DNA binding; IDA:FlyBase.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0003729; F:mRNA binding; IDA:FlyBase.
 GO:0000182; F:rDNA binding; IDA:FlyBase.
 GO:0003696; F:satellite DNA binding; IDA:FlyBase.
 GO:0006342; P:chromatin silencing; IDA:FlyBase.
 GO:0006265; P:DNA topological change; IDA:FlyBase.
 GO:0006261; P:DNA-dependent DNA replication; IBA:RefGenome.
 GO:0051310; P:metaphase plate congression; IDA:FlyBase.
 GO:0007076; P:mitotic chromosome condensation; IMP:FlyBase.
 GO:0007095; P:mitotic G2 DNA damage checkpoint; IGI:FlyBase.
 GO:0006312; P:mitotic recombination; IBA:RefGenome.
 GO:0007052; P:mitotic spindle organization; IMP:FlyBase.
 GO:0000712; P:resolution of meiotic recombination intermediates; 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.