CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-003917
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 DNA topoisomerase 2-alpha 
Protein Synonyms/Alias
 DNA topoisomerase II, alpha isozyme 
Gene Name
 TOP2A 
Gene Synonyms/Alias
 TOP2 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
156SNYDDDEKKVTGGRNubiquitination[1]
225TFQPDLSKFKMQSLDubiquitination[1]
227QPDLSKFKMQSLDKDubiquitination[1]
555YEDEDSLKTLRYGKIubiquitination[1]
605EFITPIVKVSKNKQEubiquitination[1]
658KEYFADMKRHRIQFKubiquitination[1]
665KRHRIQFKYSGPEDDubiquitination[1]
681AISLAFSKKQIDDRKubiquitination[1]
702MEDRRQRKLLGLPEDubiquitination[1]
1222EQVGLPGKGGKAKGKubiquitination[1]
1285GVELEGLKQRLEKKQubiquitination[1]
Reference
 [1] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661] 
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 455 572 Toprim.
 NP_BIND 148 150 ATP.
 NP_BIND 161 168 ATP.
 NP_BIND 376 378 ATP.
 REGION 342 344 Interaction with DNA (Probable).
 REGION 990 999 Interaction with DNA.
 MOTIF 1018 1028 Nuclear export signal.
 ACT_SITE 805 805 O-(5'-phospho-DNA)-tyrosine intermediate
 METAL 461 461 Magnesium 1; catalytic (By similarity).
 METAL 541 541 Magnesium 1; catalytic (By similarity).
 METAL 541 541 Magnesium 2.
 METAL 543 543 Magnesium 2.
 BINDING 91 91 ATP.
 BINDING 120 120 ATP.
 MOD_RES 1 1 N-acetylmethionine.
 MOD_RES 4 4 Phosphoserine.
 MOD_RES 29 29 Phosphoserine (By similarity).
 MOD_RES 282 282 Phosphothreonine.
 MOD_RES 1106 1106 Phosphoserine; by CK1.
 MOD_RES 1205 1205 Phosphothreonine.
 MOD_RES 1213 1213 Phosphoserine.
 MOD_RES 1247 1247 Phosphoserine.
 MOD_RES 1295 1295 Phosphoserine.
 MOD_RES 1297 1297 Phosphoserine.
 MOD_RES 1299 1299 Phosphoserine.
 MOD_RES 1302 1302 Phosphoserine.
 MOD_RES 1332 1332 Phosphoserine.
 MOD_RES 1337 1337 Phosphoserine.
 MOD_RES 1343 1343 Phosphothreonine; by PLK3.
 MOD_RES 1351 1351 Phosphoserine.
 MOD_RES 1354 1354 Phosphoserine.
 MOD_RES 1374 1374 Phosphoserine.
 MOD_RES 1377 1377 Phosphoserine.
 MOD_RES 1387 1387 Phosphoserine.
 MOD_RES 1392 1392 Phosphoserine.
 MOD_RES 1393 1393 Phosphoserine.
 MOD_RES 1449 1449 Phosphoserine.
 MOD_RES 1469 1469 Phosphoserine; by CK2.
 MOD_RES 1470 1470 Phosphothreonine.
 MOD_RES 1471 1471 Phosphoserine.
 MOD_RES 1474 1474 Phosphoserine.
 MOD_RES 1476 1476 Phosphoserine.
 MOD_RES 1495 1495 Phosphoserine.
 MOD_RES 1504 1504 Phosphoserine.
 MOD_RES 1525 1525 Phosphoserine.  
Keyword
 3D-structure; Acetylation; Alternative splicing; ATP-binding; Complete proteome; Cytoplasm; Direct protein sequencing; DNA-binding; Isomerase; Magnesium; Metal-binding; Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Topoisomerase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1531 AA 
Protein Sequence
MEVSPLQPVN ENMQVNKIKK NEDAKKRLSV ERIYQKKTQL EHILLRPDTY IGSVELVTQQ 60
MWVYDEDVGI NYREVTFVPG LYKIFDEILV NAADNKQRDP KMSCIRVTID PENNLISIWN 120
NGKGIPVVEH KVEKMYVPAL IFGQLLTSSN YDDDEKKVTG GRNGYGAKLC NIFSTKFTVE 180
TASREYKKMF KQTWMDNMGR AGEMELKPFN GEDYTCITFQ PDLSKFKMQS LDKDIVALMV 240
RRAYDIAGST KDVKVFLNGN KLPVKGFRSY VDMYLKDKLD ETGNSLKVIH EQVNHRWEVC 300
LTMSEKGFQQ ISFVNSIATS KGGRHVDYVA DQIVTKLVDV VKKKNKGGVA VKAHQVKNHM 360
WIFVNALIEN PTFDSQTKEN MTLQPKSFGS TCQLSEKFIK AHLYSRFLID PFFPNMIPNM 420
IFSFSKAAIG CGIVESILNW VKFKAQVQLN KKCSAVKHNR IKGIPKLDDA NDAGGRNSTE 480
CTLILTEGDS AKTLAVSGLG VVGRDKYGVF PLRGKILNVR EASHKQIMEN AEINNIIKIV 540
GLQYKKNYED EDSLKTLRYG KIMIMTDQDQ DGSHIKGLLI NFIHHNWPSL LRHRFLEEFI 600
TPIVKVSKNK QEMAFYSLPE FEEWKSSTPN HKKWKVKYYK GLGTSTSKEA KEYFADMKRH 660
RIQFKYSGPE DDAAISLAFS KKQIDDRKEW LTNFMEDRRQ RKLLGLPEDY LYGQTTTYLT 720
YNDFINKELI LFSNSDNERS IPSMVDGLKP GQRKVLFTCF KRNDKREVKV AQLAGSVAEM 780
SSYHHGEMSL MMTIINLAQN FVGSNNLNLL QPIGQFGTRL HGGKDSASPR YIFTMLSSLA 840
RLLFPPKDDH TLKFLYDDNQ RVEPEWYIPI IPMVLINGAE GIGTGWSCKI PNFDVREIVN 900
NIRRLMDGEE PLPMLPSYKN FKGTIEELAP NQYVISGEVA ILNSTTIEIS ELPVRTWTQT 960
YKEQVLEPML NGTEKTPPLI TDYREYHTDT TVKFVVKMTE EKLAEAERVG LHKVFKLQTS 1020
LTCNSMVLFD HVGCLKKYDT VLDILRDFFE LRLKYYGLRK EWLLGMLGAE SAKLNNQARF 1080
ILEKIDGKII IENKPKKELI KVLIQRGYDS DPVKAWKEAQ QKVPDEEENE ESDNEKETEK 1140
SDSVTDSGPT FNYLLDMPLW YLTKEKKDEL CRLRNEKEQE LDTLKRKSPS DLWKEDLATF 1200
IEELEAVEAK EKQDEQVGLP GKGGKAKGKK TQMAEVLPSP RGQRVIPRIT IEMKAEAEKK 1260
NKKKIKNENT EGSPQEDGVE LEGLKQRLEK KQKREPGTKT KKQTTLAFKP IKKGKKRNPW 1320
SDSESDRSSD ESNFDVPPRE TEPRRAATKT KFTMDLDSDE DFSDFDEKTD DEDFVPSDAS 1380
PPKTKTSPKL SNKELKPQKS VVSDLEADDV KGSVPLSSSP PATHFPDETE ITNPVPKKNV 1440
TVKKTAAKSQ SSTSTTGAKK RAAPKGTKRD PALNSGVSQK PDPAKTKNRR KRKPSTSDDS 1500
DSNFEKIVSK AVTSKKSKGE SDDFHMDFDS AVAPRAKSVR AKKPIKYLEE SDEDDLF 1557 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0009330; C:DNA topoisomerase complex (ATP-hydrolyzing); IDA:UniProtKB.
 GO:0005730; C:nucleolus; IDA:UniProtKB.
 GO:0005654; C:nucleoplasm; IDA:UniProtKB.
 GO:0000795; C:synaptonemal complex; IBA:RefGenome.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0003682; F:chromatin binding; IDA:UniProtKB.
 GO:0008301; F:DNA binding, bending; IDA:UniProtKB.
 GO:0003918; F:DNA topoisomerase type II (ATP-hydrolyzing) activity; IDA:UniProtKB.
 GO:0008144; F:drug binding; IDA:UniProtKB.
 GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
 GO:0043130; F:ubiquitin binding; IMP:UniProtKB.
 GO:0030263; P:apoptotic chromosome condensation; IDA:UniProtKB.
 GO:0006266; P:DNA ligation; IDA:UniProtKB.
 GO:0006281; P:DNA repair; NAS:UniProtKB.
 GO:0006265; P:DNA topological change; IDA:UniProtKB.
 GO:0006261; P:DNA-dependent DNA replication; IBA:RefGenome.
 GO:0040016; P:embryonic cleavage; IEA:Compara.
 GO:0000278; P:mitotic cell cycle; TAS:Reactome.
 GO:0006312; P:mitotic recombination; IBA:RefGenome.
 GO:0048015; P:phosphatidylinositol-mediated signaling; NAS:UniProtKB.
 GO:0043065; P:positive regulation of apoptotic process; IDA:UniProtKB.
 GO:0045870; P:positive regulation of retroviral genome replication; IMP:UniProtKB.
 GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IEA:Compara.
 GO:0000712; P:resolution of meiotic recombination intermediates; IBA:RefGenome.
 GO:0000819; P:sister chromatid segregation; IBA:RefGenome. 
Interpro
 IPR024946; Arg_repress_C-like.
 IPR012542; DTHCT.
 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
 PF08070; DTHCT
 PF02518; HATPase_c
 PF01751; Toprim 
SMART
 SM00387; HATPase_c
 SM00433; TOP2c
 SM00434; TOP4c 
PROSITE
 PS00177; TOPOISOMERASE_II
 PS50880; TOPRIM 
PRINTS
 PR00418; TPI2FAMILY.