UniProt Accession

 TOP2B_HUMAN; Q02880; Q13600; Q9UMG8; Q9UQP8 

Genbank Protein ID

 X68060; X71911; Z15111; Z15115; M27504; AJ011721; AJ011722; AJ011723; AJ011724; AJ011725; AJ011726; AJ011727; AJ011728; AJ011729; AJ011730; AJ011731; AJ011732; X53662; U54831 

Genbank Nucleotide ID

 CAA48197.1; CAA78815.1; CAA78821.1; AAA61210.1; CAA09753.1; CAA09753.1; CAA09753.1; CAA09753.1; CAA09753.1; CAA09753.1; CAA09753.1; CAA09753.1; CAA09753.1; CAA09753.1; CAA09753.1; CAA09753.1; CAA37706.1; AAB01982.1 

Protein Name

 DNA topoisomerase 2-beta 

Protein Synonyms/Alias

 DNA topoisomerase II, beta isozyme 

Gene Name

 TOP2B 

Gene Synonyms/Alias

  

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
42	EESETANKNDSSKKL	ubiquitination	[1]
117	LVNAADNKQRDKNMT	ubiquitination	[1, 2]
144	ISIWNNGKGIPVVEH	ubiquitination	[1]
152	GIPVVEHKVEKVYVP	ubiquitination	[1]
177	SNYDDDEKKVTGGRN	ubiquitination	[1]
254	FKMEKLDKDIVALMT	ubiquitination	[3, 4, 5]
299	VDLYVKDKLDETGVA	ubiquitination	[1]
308	DETGVALKVIHELAN	ubiquitination	[1]
342	VNSIATTKGGRHVDY	ubiquitination	[3, 5]
365	LIEVVKKKNKAGVSV	acetylation	[6]
367	EVVKKKNKAGVSVKP	acetylation	[6]
367	EVVKKKNKAGVSVKP	ubiquitination	[1]
373	NKAGVSVKPFQVKNH	acetylation	[6]
373	NKAGVSVKPFQVKNH	ubiquitination	[4]
407	ENMTLQPKSFGSKCQ	ubiquitination	[3, 4, 5]
412	QPKSFGSKCQLSEKF	ubiquitination	[2, 4]
510	GVFPLRGKILNVREA	ubiquitination	[3, 4]
520	NVREASHKQIMENAE	ubiquitination	[1, 2, 3, 4]
540	KIVGLQYKKSYDDAE	ubiquitination	[2]
541	IVGLQYKKSYDDAES	ubiquitination	[1, 3, 5]
550	YDDAESLKTLRYGKI	ubiquitination	[1, 3, 4, 5]
556	LKTLRYGKIMIMTDQ	ubiquitination	[1, 3, 4, 5]
600	EFITPIVKASKNKQE	ubiquitination	[1]
605	IVKASKNKQELSFYS	ubiquitination	[1, 2]
620	IPEFDEWKKHIENQK	ubiquitination	[1]
627	KKHIENQKAWKIKYY	ubiquitination	[1]
635	AWKIKYYKGLGTSTA	ubiquitination	[1]
643	GLGTSTAKEAKEYFA	ubiquitination	[1]
646	TSTAKEAKEYFADME	ubiquitination	[1]
676	AITLAFSKKKIDDRK	ubiquitination	[1, 2]
683	KKKIDDRKEWLTNFM	ubiquitination	[1, 3]
712	FLYGTATKHLTYNDF	ubiquitination	[1]
744	PSLVDGFKPGQRKVL	ubiquitination	[3, 5]
749	GFKPGQRKVLFTCFK	ubiquitination	[4]
970	PMLNGTDKTPALISD	ubiquitination	[1]
979	PALISDYKEYHTDTT	ubiquitination	[1]
988	YHTDTTVKFVVKMTE	ubiquitination	[3]
1008	AEAAGLHKVFKLQTT	ubiquitination	[3, 5]
1068	MLGAESTKLNNQARF	ubiquitination	[1]
1214	VLAGMSGKAIKGKVG	ubiquitination	[1]
1227	VGKPKVKKLQLEETM	ubiquitination	[1]
1250	IPEITAMKADASKKL	ubiquitination	[1]
1262	KKLLKKKKGDLDTAA	ubiquitination	[1]
1299	TPSVPINKGPKPKRE	ubiquitination	[1]
1302	VPINKGPKPKREKKE	ubiquitination	[1]
1323	KTPTSSGKPSAKKVK	ubiquitination	[1]
1440	EKSLHDKKSQDFGNL	ubiquitination	[4]
1574	TTSKKPKKTSFDQDS	ubiquitination	[1]

Reference

 [1] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [2] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [3] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [4] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [5] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [6] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861] 

Functional Description

 Control of topological states of DNA by transient breakage and subsequent rejoining of DNA strands. Topoisomerase II makes double-strand breaks. Indirectly involved in vitamin D- coupled transcription regulation via its association with the WINAC complex, a chromatin-remodeling complex recruited by vitamin D receptor (VDR), which is required for the ligand-bound VDR- mediated transrepression of the CYP27B1 gene. 

Sequence Annotation

 DOMAIN 476 593 Toprim.
 NP_BIND 169 171 ATP (By similarity).
 NP_BIND 182 189 ATP (By similarity).
 NP_BIND 397 399 ATP (By similarity).
 REGION 363 365 Interaction with DNA (By similarity).
 REGION 1011 1020 Interaction with DNA.
 MOTIF 1034 1044 Nuclear export signal.
 ACT_SITE 826 826 O-(5'-phospho-DNA)-tyrosine intermediate.
 METAL 482 482 Magnesium 1; catalytic (By similarity).
 METAL 562 562 Magnesium 1; catalytic (By similarity).
 METAL 562 562 Magnesium 2.
 METAL 564 564 Magnesium 2.
 BINDING 112 112 ATP (By similarity).
 BINDING 141 141 ATP (By similarity).
 MOD_RES 431 431 Phosphoserine (By similarity).
 MOD_RES 639 639 Phosphothreonine (By similarity).
 MOD_RES 1236 1236 Phosphoserine.
 MOD_RES 1292 1292 Phosphothreonine.
 MOD_RES 1336 1336 Phosphoserine.
 MOD_RES 1340 1340 Phosphoserine.
 MOD_RES 1342 1342 Phosphoserine.
 MOD_RES 1344 1344 Phosphoserine.
 MOD_RES 1358 1358 Phosphoserine.
 MOD_RES 1375 1375 Phosphoserine.
 MOD_RES 1400 1400 Phosphoserine.
 MOD_RES 1403 1403 Phosphothreonine.
 MOD_RES 1413 1413 Phosphoserine.
 MOD_RES 1421 1421 Phosphotyrosine.
 MOD_RES 1424 1424 Phosphoserine.
 MOD_RES 1441 1441 Phosphoserine.
 MOD_RES 1452 1452 Phosphoserine.
 MOD_RES 1454 1454 Phosphoserine.
 MOD_RES 1461 1461 Phosphoserine.
 MOD_RES 1466 1466 Phosphoserine.
 MOD_RES 1473 1473 Phosphoserine.
 MOD_RES 1476 1476 Phosphoserine.
 MOD_RES 1522 1522 Phosphoserine.
 MOD_RES 1524 1524 Phosphoserine.
 MOD_RES 1526 1526 Phosphoserine.
 MOD_RES 1550 1550 Phosphoserine.
 MOD_RES 1552 1552 Phosphoserine.
 MOD_RES 1575 1575 Phosphothreonine.
 MOD_RES 1581 1581 Phosphoserine.
 MOD_RES 1592 1592 Phosphothreonine.
 MOD_RES 1596 1596 Phosphoserine.
 MOD_RES 1609 1609 Phosphotyrosine.
 MOD_RES 1613 1613 Phosphoserine.  

Keyword

 3D-structure; Alternative splicing; ATP-binding; Complete proteome; Cytoplasm; DNA-binding; Isomerase; Magnesium; Metal-binding; Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome; Topoisomerase. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 1626 AA 

Protein Sequence

Gene Ontology

 GO:0005829; C:cytosol; IDA:UniProtKB.
 GO:0005654; C:nucleoplasm; IDA:UniProtKB.
 GO:0000795; C:synaptonemal complex; IBA:RefGenome.
 GO:0071778; C:WINAC complex; IDA:BHF-UCL.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0003682; F:chromatin binding; IDA:UniProtKB.
 GO:0003918; F:DNA topoisomerase type II (ATP-hydrolyzing) activity; IDA:UniProtKB.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0007409; P:axonogenesis; IEA:Compara.
 GO:0006265; P:DNA topological change; IDA:UniProtKB.
 GO:0006261; P:DNA-dependent DNA replication; IBA:RefGenome.
 GO:0030900; P:forebrain development; IEA:Compara.
 GO:0006312; P:mitotic recombination; IBA:RefGenome.
 GO:0001764; P:neuron migration; 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.