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
3	*****MAKSGGCGAG	ubiquitination	[1]
29	WVNNAAKKEESETAN	ubiquitination	[1]
112	LVNAADNKQRDKNMT	ubiquitination	[1, 2]
116	ADNKQRDKNMTCIKV	ubiquitination	[1]
139	ISIWNNGKGIPVVEH	ubiquitination	[1]
147	GIPVVEHKVEKVYVP	ubiquitination	[1]
150	VVEHKVEKVYVPALI	ubiquitination	[1]
172	SNYDDDEKKVTGGRN	ubiquitination	[1, 2]
173	NYDDDEKKVTGGRNG	ubiquitination	[1]
184	GRNGYGAKLCNIFST	ubiquitination	[1]
200	FTVETACKEYKHSFK	ubiquitination	[1]
216	TWMNNMMKTSEAKIK	ubiquitination	[1]
223	KTSEAKIKHFDGEDY	ubiquitination	[1]
249	FKMEKLDKDIVALMT	ubiquitination	[2]
277	KVMFNGKKLPVNGFR	ubiquitination	[1]
292	SYVDLYVKDKLDETG	ubiquitination	[1]
294	VDLYVKDKLDETGVA	ubiquitination	[1]
303	DETGVALKVIHELAN	ubiquitination	[1]
337	VNSIATTKGGRHVDY	ubiquitination	[1]
352	VVDQVVGKLIEVVKK	ubiquitination	[1]
360	LIEVVKKKNKAGVSV	ubiquitination	[1]
362	EVVKKKNKAGVSVKP	ubiquitination	[1]
368	NKAGVSVKPFQVKNH	ubiquitination	[1]
402	ENMTLQPKSFGSKCQ	ubiquitination	[1]
407	QPKSFGSKCQLSEKF	ubiquitination	[1]
413	SKCQLSEKFFKAASN	ubiquitination	[1]
434	ILNWVKFKAQTQLNK	ubiquitination	[1]
466	DANDAGGKHSLECTL	ubiquitination	[1]
482	LTEGDSAKSLAVSGL	ubiquitination	[1]
505	GVFPLRGKILNVREA	ubiquitination	[1]
515	NVREASHKQIMENAE	ubiquitination	[1, 2]
536	IVGLQYKKSYDDAES	ubiquitination	[1]
545	YDDAESLKTLRYGKI	ubiquitination	[1, 2]
551	LKTLRYGKIMIMTDQ	ubiquitination	[2]
595	EFITPIVKASKNKQE	ubiquitination	[1, 2]
600	IVKASKNKQELSFYS	ubiquitination	[1, 2]
615	IPEFDEWKKHIENQK	ubiquitination	[1]
616	PEFDEWKKHIENQKA	ubiquitination	[1]
622	KKHIENQKAWKIKYY	ubiquitination	[1]
630	AWKIKYYKGLGTSTA	ubiquitination	[1]
638	GLGTSTAKEAKEYFA	ubiquitination	[1]
641	TSTAKEAKEYFADME	ubiquitination	[1, 2]
671	AITLAFSKKKIDDRK	ubiquitination	[1, 2]
672	ITLAFSKKKIDDRKE	ubiquitination	[1]
678	KKKIDDRKEWLTNFM	ubiquitination	[1]
707	FLYGTATKHLTYNDF	ubiquitination	[1, 2]
739	PSLVDGFKPGQRKVL	ubiquitination	[1]
744	GFKPGQRKVLFTCFK	ubiquitination	[1]
751	KVLFTCFKRNDKREV	ubiquitination	[1]
912	LPNYKNFKGTIQELG	ubiquitination	[1]
987	TTVKFVVKMTEEKLA	ubiquitination	[1]
1074	QARFILEKIQGKITI	ubiquitination	[1]
1078	ILEKIQGKITIENRS	ubiquitination	[1]
1086	ITIENRSKKDLIQML	ubiquitination	[1]
1104	GYESDPVKAWKEAQE	ubiquitination	[1]
1222	VGKPKVKKLQLEETM	ubiquitination	[1]
1245	IPEITAMKADASKKL	ubiquitination	[1]
1435	EKSLHDKKSQDFGNL	ubiquitination	[1]

Reference

 [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [2] 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. 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.