UniProt Accession

 E9PCY5_HUMAN; E9PCY5 

Genbank Protein ID

 AC093416 

Genbank Nucleotide ID

  

Protein Name

 DNA topoisomerase 2 

Protein Synonyms/Alias

  

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]
37	EESETANKNDSSKKL	ubiquitination	[2]
112	LVNAADNKQRDKNMT	ubiquitination	[1, 2, 3, 4, 5]
116	ADNKQRDKNMTCIKV	ubiquitination	[1]
139	ISIWNNGKGIPVVEH	ubiquitination	[1, 2]
147	GIPVVEHKVEKVYVP	ubiquitination	[1, 2, 3, 6]
150	VVEHKVEKVYVPALI	ubiquitination	[1, 6]
172	SNYDDDEKKVTGGRN	ubiquitination	[1, 5]
173	NYDDDEKKVTGGRNG	ubiquitination	[1]
184	GRNGYGAKLCNIFST	ubiquitination	[1, 6]
200	FTVETACKEYKHSFK	ubiquitination	[1]
216	TWMNNMMKTSEAKIK	ubiquitination	[1]
223	KTSEAKIKHFDGEDY	ubiquitination	[1]
249	FKMEKLDKDIVALMT	ubiquitination	[5, 7]
270	AGSCRGVKVMFNGKK	acetylation	[6, 8]
277	KVMFNGKKLPVNGFR	ubiquitination	[1]
292	SYVDLYVKDKLDETG	ubiquitination	[1]
294	VDLYVKDKLDETGVA	ubiquitination	[1, 2]
303	DETGVALKVIHELAN	ubiquitination	[1, 2, 3]
337	VNSIATTKGGRHVDY	ubiquitination	[1, 6, 7]
352	VVDQVVGKLIEVVKK	ubiquitination	[1]
360	LIEVVKKKNKAGVSV	ubiquitination	[1]
362	EVVKKKNKAGVSVKP	ubiquitination	[1, 2]
368	NKAGVSVKPFQVKNH	acetylation	[6]
368	NKAGVSVKPFQVKNH	ubiquitination	[1, 6]
402	ENMTLQPKSFGSKCQ	ubiquitination	[1, 7]
407	QPKSFGSKCQLSEKF	ubiquitination	[1, 3, 4, 6]
413	SKCQLSEKFFKAASN	ubiquitination	[1]
434	ILNWVKFKAQTQLNK	ubiquitination	[1]
447	NKKCSSVKYSKIKGI	acetylation	[6]
466	DANDAGGKHSLECTL	ubiquitination	[1]
482	LTEGDSAKSLAVSGL	ubiquitination	[1, 3]
505	GVFPLRGKILNVREA	ubiquitination	[1, 6, 7]
515	NVREASHKQIMENAE	ubiquitination	[1, 2, 3, 4, 5, 6, 7]
535	KIVGLQYKKSYDDAE	ubiquitination	[1, 4]
536	IVGLQYKKSYDDAES	ubiquitination	[1, 2, 6, 7]
545	YDDAESLKTLRYGKI	ubiquitination	[1, 2, 3, 5, 6, 7]
551	LKTLRYGKIMIMTDQ	ubiquitination	[1, 2, 5, 7]
595	EFITPIVKASKNKQE	ubiquitination	[1, 2, 5]
600	IVKASKNKQELSFYS	ubiquitination	[1, 2, 4, 5, 6]
615	IPEFDEWKKHIENQK	ubiquitination	[1, 2]
622	KKHIENQKAWKIKYY	ubiquitination	[1, 2, 3]
630	AWKIKYYKGLGTSTA	ubiquitination	[1, 2, 6]
638	GLGTSTAKEAKEYFA	ubiquitination	[1, 2, 6]
641	TSTAKEAKEYFADME	ubiquitination	[1, 2, 5, 6]
671	AITLAFSKKKIDDRK	ubiquitination	[1, 2, 3, 4, 5]
672	ITLAFSKKKIDDRKE	ubiquitination	[1, 6]
678	KKKIDDRKEWLTNFM	ubiquitination	[1, 2, 6, 7]
707	FLYGTATKHLTYNDF	ubiquitination	[1, 2, 3, 5]
739	PSLVDGFKPGQRKVL	ubiquitination	[1, 6, 7]
744	GFKPGQRKVLFTCFK	ubiquitination	[1]
751	KVLFTCFKRNDKREV	ubiquitination	[1]
912	LPNYKNFKGTIQELG	ubiquitination	[1]
965	PMLNGTDKTPALISD	ubiquitination	[2]
974	PALISDYKEYHTDTT	ubiquitination	[2]
983	YHTDTTVKFVVKMTE	ubiquitination	[7]
987	TTVKFVVKMTEEKLA	acetylation	[8]
987	TTVKFVVKMTEEKLA	ubiquitination	[1]
1003	AEAAGLHKVFKLQTT	ubiquitination	[7]
1063	MLGAESTKLNNQARF	ubiquitination	[2]
1074	QARFILEKIQGKITI	ubiquitination	[1, 6]
1078	ILEKIQGKITIENRS	ubiquitination	[1]
1086	ITIENRSKKDLIQML	ubiquitination	[1]
1104	GYESDPVKAWKEAQE	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] 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]
 [3] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [4] 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]
 [5] 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]
 [6] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [7] 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]
 [8] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377] 

Functional Description

 Control of topological states of DNA by transient breakage and subsequent rejoining of DNA strands. Topoisomerase II makes double-strand breaks (By similarity). 

Sequence Annotation

  

Keyword

 ATP-binding; Complete proteome; DNA-binding; Isomerase; Nucleotide-binding; Reference proteome; Topoisomerase. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 1150 AA 

Protein Sequence

Gene Ontology

 GO:0005694; C:chromosome; IEA:InterPro.
 GO:0005634; C:nucleus; IEA:Compara.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0003918; F:DNA topoisomerase type II (ATP-hydrolyzing) activity; IEA:EC.
 GO:0007409; P:axonogenesis; IEA:Compara.
 GO:0006265; P:DNA topological change; IEA:InterPro.
 GO:0030900; P:forebrain development; IEA:Compara.
 GO:0001764; P:neuron migration; IEA:Compara. 

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 

PRINTS

 PR00418; TPI2FAMILY.