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Protein

DNA topoisomerase 2-beta

Gene

TOP2B

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Control of topological states of DNA by transient breakage and subsequent rejoining of DNA strands. Topoisomerase II makes double-strand breaks.1 Publication

Catalytic activityi

ATP-dependent breakage, passage and rejoining of double-stranded DNA.PROSITE-ProRule annotation1 Publication

Cofactori

Mg2+PROSITE-ProRule annotation2 Publications, Mn2+PROSITE-ProRule annotation2 Publications, Ca2+PROSITE-ProRule annotation2 PublicationsNote: Binds two Mg2+ per subunit. The magnesium ions form salt bridges with both the protein and the DNA. Can also accept other divalent metal cations, such as Mn2+ or Ca2+.PROSITE-ProRule annotation2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei112ATPBy similarity1
Binding sitei141ATPBy similarity1
Metal bindingi482Magnesium 1; catalyticPROSITE-ProRule annotation1
Metal bindingi562Magnesium 1; catalyticPROSITE-ProRule annotation1
Metal bindingi562Magnesium 2PROSITE-ProRule annotation1 Publication1
Metal bindingi564Magnesium 2PROSITE-ProRule annotation1 Publication1
Sitei825Transition state stabilizer1
Active sitei826O-(5'-phospho-DNA)-tyrosine intermediate1 Publication1
Sitei877Important for DNA bending; intercalates between base pairs of target DNA1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi169 – 171ATPBy similarity3
Nucleotide bindingi182 – 189ATPBy similarity8
Nucleotide bindingi397 – 399ATPBy similarity3

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • chromatin binding Source: UniProtKB
  • DNA binding, bending Source: InterPro
  • DNA topoisomerase type II (ATP-hydrolyzing) activity Source: UniProtKB
  • enzyme binding Source: UniProtKB
  • histone deacetylase binding Source: UniProtKB
  • metal ion binding Source: UniProtKB-KW
  • protein C-terminus binding Source: UniProtKB
  • protein heterodimerization activity Source: UniProtKB
  • protein kinase C binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Isomerase, Topoisomerase

Keywords - Ligandi

ATP-binding, DNA-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciZFISH:HS01229-MONOMER.
BRENDAi5.99.1.3. 2681.
ReactomeiR-HSA-4615885. SUMOylation of DNA replication proteins.
SIGNORiQ02880.

Names & Taxonomyi

Protein namesi
Recommended name:
DNA topoisomerase 2-beta (EC:5.99.1.3)
Alternative name(s):
DNA topoisomerase II, beta isozyme
Gene namesi
Name:TOP2B
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 3

Organism-specific databases

HGNCiHGNC:11990. TOP2B.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: HPA
  • cytosol Source: UniProtKB
  • DNA topoisomerase complex (ATP-hydrolyzing) Source: GO_Central
  • nucleoplasm Source: UniProtKB
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi482E → Q: Strongly reduced enzyme activity. 1 Publication1
Mutagenesisi485S → A: Slightly reduced enzyme activity. 1 Publication1
Mutagenesisi508R → E: Slightly reduced enzyme activity. 1 Publication1
Mutagenesisi510K → E: Strongly reduced enzyme activity. 1 Publication1
Mutagenesisi515R → Q: Slightly reduced enzyme activity. 1 Publication1

Organism-specific databases

DisGeNETi7155.
OpenTargetsiENSG00000077097.
PharmGKBiPA36672.

Chemistry databases

ChEMBLiCHEMBL3396.
DrugBankiDB00970. Dactinomycin.
DB00694. Daunorubicin.
DB00380. Dexrazoxane.
DB00773. Etoposide.

Polymorphism and mutation databases

DMDMi20141946.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00001453692 – 1626DNA topoisomerase 2-betaAdd BLAST1625

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineBy similarity1
Modified residuei3N6-acetyllysineBy similarity1
Cross-linki34Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki177Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki373Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki437Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki605Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki643Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki1227Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei1236PhosphoserineCombined sources1
Cross-linki1250Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki1271Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei1292PhosphothreonineCombined sources1
Modified residuei1336PhosphoserineCombined sources1
Modified residuei1340PhosphoserineCombined sources1
Modified residuei1342PhosphoserineCombined sources1
Modified residuei1344PhosphoserineCombined sources1
Modified residuei1358PhosphoserineCombined sources1
Modified residuei1370PhosphotyrosineBy similarity1
Modified residuei1375PhosphoserineCombined sources1
Modified residuei1400PhosphoserineCombined sources1
Modified residuei1403PhosphothreonineCombined sources1
Modified residuei1413PhosphoserineCombined sources1
Modified residuei1421PhosphotyrosineCombined sources1
Modified residuei1424PhosphoserineCombined sources1
Cross-linki1440Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei1441PhosphoserineCombined sources1
Modified residuei1452PhosphoserineCombined sources1
Modified residuei1454PhosphoserineCombined sources1
Cross-linki1456Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei1461PhosphoserineCombined sources1
Modified residuei1466PhosphoserineCombined sources1
Modified residuei1473PhosphoserineCombined sources1
Modified residuei1476PhosphoserineCombined sources1
Modified residuei1522PhosphoserineCombined sources1
Modified residuei1524PhosphoserineCombined sources1
Modified residuei1526PhosphoserineCombined sources1
Modified residuei1550PhosphoserineCombined sources1
Modified residuei1552PhosphoserineCombined sources1
Modified residuei1575PhosphothreonineCombined sources1
Modified residuei1576PhosphoserineCombined sources1
Modified residuei1581PhosphoserineCombined sources1
Modified residuei1592PhosphothreonineCombined sources1
Modified residuei1596PhosphoserineCombined sources1
Modified residuei1609PhosphotyrosineCombined sources1
Modified residuei1613PhosphoserineCombined sources1
Isoform Beta-1 (identifier: Q02880-2)
Cross-linki28Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ02880.
MaxQBiQ02880.
PaxDbiQ02880.
PeptideAtlasiQ02880.
PRIDEiQ02880.

PTM databases

iPTMnetiQ02880.
PhosphoSitePlusiQ02880.
SwissPalmiQ02880.

Expressioni

Gene expression databases

BgeeiENSG00000077097.
CleanExiHS_TOP2B.
ExpressionAtlasiQ02880. baseline and differential.
GenevisibleiQ02880. HS.

Organism-specific databases

HPAiCAB004601.
HPA024120.
HPA050441.

Interactioni

Subunit structurei

Homodimer.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei510Interaction with DNA1
Sitei513Interaction with DNA1
Sitei682Interaction with DNA1
Sitei683Interaction with DNA1
Sitei744Interaction with DNA1
Sitei778Interaction with DNAPROSITE-ProRule annotation1
Sitei952Interaction with DNA1

GO - Molecular functioni

  • enzyme binding Source: UniProtKB
  • histone deacetylase binding Source: UniProtKB
  • protein C-terminus binding Source: UniProtKB
  • protein heterodimerization activity Source: UniProtKB
  • protein kinase C binding Source: UniProtKB

Protein-protein interaction databases

BioGridi113008. 72 interactors.
IntActiQ02880. 16 interactors.
MINTiMINT-155585.
STRINGi9606.ENSP00000396704.

Chemistry databases

BindingDBiQ02880.

Structurei

Secondary structure

11626
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni466 – 469Combined sources4
Beta strandi470 – 472Combined sources3
Helixi473 – 475Combined sources3
Beta strandi477 – 482Combined sources6
Helixi483 – 491Combined sources9
Helixi497 – 499Combined sources3
Beta strandi502 – 507Combined sources6
Helixi514 – 516Combined sources3
Helixi519 – 524Combined sources6
Helixi526 – 535Combined sources10
Beta strandi545 – 547Combined sources3
Helixi548 – 551Combined sources4
Beta strandi555 – 560Combined sources6
Helixi565 – 581Combined sources17
Helixi583 – 587Combined sources5
Beta strandi591 – 594Combined sources4
Helixi644 – 650Combined sources7
Helixi652 – 655Combined sources4
Beta strandi656 – 660Combined sources5
Helixi664 – 674Combined sources11
Helixi676 – 678Combined sources3
Helixi679 – 698Combined sources20
Beta strandi713 – 715Combined sources3
Helixi716 – 722Combined sources7
Helixi724 – 735Combined sources12
Turni739 – 741Combined sources3
Helixi745 – 757Combined sources13
Helixi765 – 776Combined sources12
Helixi782 – 793Combined sources12
Turni814 – 820Combined sources7
Helixi824 – 826Combined sources3
Helixi835 – 838Combined sources4
Helixi841 – 844Combined sources4
Beta strandi849 – 852Combined sources4
Beta strandi855 – 860Combined sources6
Helixi868 – 871Combined sources4
Beta strandi875 – 877Combined sources3
Beta strandi882 – 884Combined sources3
Helixi890 – 901Combined sources12
Beta strandi918 – 924Combined sources7
Beta strandi927 – 931Combined sources5
Beta strandi933 – 938Combined sources6
Beta strandi941 – 946Combined sources6
Helixi953 – 959Combined sources7
Helixi961 – 966Combined sources6
Beta strandi969 – 971Combined sources3
Beta strandi976 – 980Combined sources5
Beta strandi989 – 992Combined sources4
Helixi995 – 1004Combined sources10
Helixi1006 – 1009Combined sources4
Beta strandi1013 – 1017Combined sources5
Beta strandi1021 – 1024Combined sources4
Beta strandi1030 – 1034Combined sources5
Helixi1036 – 1080Combined sources45
Helixi1091 – 1100Combined sources10
Helixi1107 – 1114Combined sources8
Helixi1144 – 1147Combined sources4
Helixi1151 – 1154Combined sources4
Helixi1156 – 1177Combined sources22
Helixi1181 – 1205Combined sources25

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3QX3X-ray2.16A/B450-1206[»]
4G0UX-ray2.70A/B450-1206[»]
4G0VX-ray2.55A/B450-1206[»]
4G0WX-ray2.70A/B450-1206[»]
4J3NX-ray2.30A/B450-1206[»]
ProteinModelPortaliQ02880.
SMRiQ02880.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini476 – 593ToprimPROSITE-ProRule annotationAdd BLAST118

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni363 – 365Interaction with DNABy similarity3
Regioni1011 – 1020Interaction with DNA10

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi1034 – 1044Nuclear export signalAdd BLAST11

Sequence similaritiesi

Belongs to the type II topoisomerase family.Curated
Contains 1 Toprim domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0355. Eukaryota.
COG0187. LUCA.
COG0188. LUCA.
GeneTreeiENSGT00390000016222.
HOGENOMiHOG000216693.
HOVERGENiHBG052998.
InParanoidiQ02880.
KOiK03164.
OMAiEETQNQH.
OrthoDBiEOG091G00U2.
PhylomeDBiQ02880.
TreeFamiTF105282.

Family and domain databases

Gene3Di1.10.268.10. 1 hit.
3.30.1360.40. 1 hit.
3.30.230.10. 1 hit.
3.30.565.10. 1 hit.
3.40.50.670. 1 hit.
3.90.199.10. 1 hit.
InterProiIPR024946. Arg_repress_C-like.
IPR012542. DTHCT.
IPR003594. HATPase_C.
IPR020568. Ribosomal_S5_D2-typ_fold.
IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
IPR028467. Top2b.
IPR001241. Topo_IIA.
IPR013760. Topo_IIA-like_dom.
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.
IPR018522. TopoIIA_CS.
IPR031660. TOPRIM_C.
IPR006171. Toprim_domain.
[Graphical view]
PANTHERiPTHR10169:SF36. PTHR10169:SF36. 1 hit.
PfamiPF00204. DNA_gyraseB. 1 hit.
PF00521. DNA_topoisoIV. 1 hit.
PF08070. DTHCT. 1 hit.
PF02518. HATPase_c. 1 hit.
PF01751. Toprim. 1 hit.
PF16898. TOPRIM_C. 1 hit.
[Graphical view]
PRINTSiPR00418. TPI2FAMILY.
SMARTiSM00433. TOP2c. 1 hit.
SM00434. TOP4c. 1 hit.
[Graphical view]
SUPFAMiSSF54211. SSF54211. 1 hit.
SSF55874. SSF55874. 1 hit.
SSF56719. SSF56719. 1 hit.
PROSITEiPS00177. TOPOISOMERASE_II. 1 hit.
PS50880. TOPRIM. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform Beta-2 (identifier: Q02880-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAKSGGCGAG AGVGGGNGAL TWVTLFDQNN AAKKEESETA NKNDSSKKLS
60 70 80 90 100
VERVYQKKTQ LEHILLRPDT YIGSVEPLTQ FMWVYDEDVG MNCREVTFVP
110 120 130 140 150
GLYKIFDEIL VNAADNKQRD KNMTCIKVSI DPESNIISIW NNGKGIPVVE
160 170 180 190 200
HKVEKVYVPA LIFGQLLTSS NYDDDEKKVT GGRNGYGAKL CNIFSTKFTV
210 220 230 240 250
ETACKEYKHS FKQTWMNNMM KTSEAKIKHF DGEDYTCITF QPDLSKFKME
260 270 280 290 300
KLDKDIVALM TRRAYDLAGS CRGVKVMFNG KKLPVNGFRS YVDLYVKDKL
310 320 330 340 350
DETGVALKVI HELANERWDV CLTLSEKGFQ QISFVNSIAT TKGGRHVDYV
360 370 380 390 400
VDQVVGKLIE VVKKKNKAGV SVKPFQVKNH IWVFINCLIE NPTFDSQTKE
410 420 430 440 450
NMTLQPKSFG SKCQLSEKFF KAASNCGIVE SILNWVKFKA QTQLNKKCSS
460 470 480 490 500
VKYSKIKGIP KLDDANDAGG KHSLECTLIL TEGDSAKSLA VSGLGVIGRD
510 520 530 540 550
RYGVFPLRGK ILNVREASHK QIMENAEINN IIKIVGLQYK KSYDDAESLK
560 570 580 590 600
TLRYGKIMIM TDQDQDGSHI KGLLINFIHH NWPSLLKHGF LEEFITPIVK
610 620 630 640 650
ASKNKQELSF YSIPEFDEWK KHIENQKAWK IKYYKGLGTS TAKEAKEYFA
660 670 680 690 700
DMERHRILFR YAGPEDDAAI TLAFSKKKID DRKEWLTNFM EDRRQRRLHG
710 720 730 740 750
LPEQFLYGTA TKHLTYNDFI NKELILFSNS DNERSIPSLV DGFKPGQRKV
760 770 780 790 800
LFTCFKRNDK REVKVAQLAG SVAEMSAYHH GEQALMMTIV NLAQNFVGSN
810 820 830 840 850
NINLLQPIGQ FGTRLHGGKD AASPRYIFTM LSTLARLLFP AVDDNLLKFL
860 870 880 890 900
YDDNQRVEPE WYIPIIPMVL INGAEGIGTG WACKLPNYDA REIVNNVRRM
910 920 930 940 950
LDGLDPHPML PNYKNFKGTI QELGQNQYAV SGEIFVVDRN TVEITELPVR
960 970 980 990 1000
TWTQVYKEQV LEPMLNGTDK TPALISDYKE YHTDTTVKFV VKMTEEKLAQ
1010 1020 1030 1040 1050
AEAAGLHKVF KLQTTLTCNS MVLFDHMGCL KKYETVQDIL KEFFDLRLSY
1060 1070 1080 1090 1100
YGLRKEWLVG MLGAESTKLN NQARFILEKI QGKITIENRS KKDLIQMLVQ
1110 1120 1130 1140 1150
RGYESDPVKA WKEAQEKAAE EDETQNQHDD SSSDSGTPSG PDFNYILNMS
1160 1170 1180 1190 1200
LWSLTKEKVE ELIKQRDAKG REVNDLKRKS PSDLWKEDLA AFVEELDKVE
1210 1220 1230 1240 1250
SQEREDVLAG MSGKAIKGKV GKPKVKKLQL EETMPSPYGR RIIPEITAMK
1260 1270 1280 1290 1300
ADASKKLLKK KKGDLDTAAV KVEFDEEFSG APVEGAGEEA LTPSVPINKG
1310 1320 1330 1340 1350
PKPKREKKEP GTRVRKTPTS SGKPSAKKVK KRNPWSDDES KSESDLEETE
1360 1370 1380 1390 1400
PVVIPRDSLL RRAAAERPKY TFDFSEEEDD DADDDDDDNN DLEELKVKAS
1410 1420 1430 1440 1450
PITNDGEDEF VPSDGLDKDE YTFSPGKSKA TPEKSLHDKK SQDFGNLFSF
1460 1470 1480 1490 1500
PSYSQKSEDD SAKFDSNEED SASVFSPSFG LKQTDKVPSK TVAAKKGKPS
1510 1520 1530 1540 1550
SDTVPKPKRA PKQKKVVEAV NSDSDSEFGI PKKTTTPKGK GRGAKKRKAS
1560 1570 1580 1590 1600
GSENEGDYNP GRKTSKTTSK KPKKTSFDQD SDVDIFPSDF PTEPPSLPRT
1610 1620
GRARKEVKYF AESDEEEDDV DFAMFN
Length:1,626
Mass (Da):183,267
Last modified:January 31, 2002 - v3
Checksum:iE60E9262CC68B05D
GO
Isoform Beta-1 (identifier: Q02880-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     24-28: Missing.

Show »
Length:1,621
Mass (Da):182,663
Checksum:iB1C091BF539F2391
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti1431T → S in CAA78821 (PubMed:10095062).Curated1
Sequence conflicti1431T → S in CAA09753 (PubMed:10095062).Curated1
Sequence conflicti1611A → T in CAA48197 (PubMed:1333583).Curated1
Sequence conflicti1621D → H in CAA09753 (PubMed:10095062).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_00653224 – 28Missing in isoform Beta-1. Curated5

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X68060 mRNA. Translation: CAA48197.1.
X71911 Genomic DNA. No translation available.
Z15111 mRNA. Translation: CAA78815.1.
Z15115 mRNA. Translation: CAA78821.1.
M27504 mRNA. Translation: AAA61210.1.
AJ011721
, AJ011722, AJ011723, AJ011724, AJ011725, AJ011726, AJ011727, AJ011728, AJ011729, AJ011730, AJ011731, AJ011732 Genomic DNA. Translation: CAA09753.1.
X53662 mRNA. Translation: CAA37706.1.
U54831 mRNA. Translation: AAB01982.1.
CCDSiCCDS46776.1. [Q02880-2]
CCDS82746.1. [Q02880-1]
PIRiS26730. A39242.
RefSeqiNP_001059.2. NM_001068.3. [Q02880-2]
NP_001317629.1. NM_001330700.1.
UniGeneiHs.475733.

Genome annotation databases

EnsembliENST00000264331; ENSP00000264331; ENSG00000077097. [Q02880-1]
ENST00000435706; ENSP00000396704; ENSG00000077097. [Q02880-2]
GeneIDi7155.
KEGGihsa:7155.
UCSCiuc003cdj.4. human. [Q02880-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X68060 mRNA. Translation: CAA48197.1.
X71911 Genomic DNA. No translation available.
Z15111 mRNA. Translation: CAA78815.1.
Z15115 mRNA. Translation: CAA78821.1.
M27504 mRNA. Translation: AAA61210.1.
AJ011721
, AJ011722, AJ011723, AJ011724, AJ011725, AJ011726, AJ011727, AJ011728, AJ011729, AJ011730, AJ011731, AJ011732 Genomic DNA. Translation: CAA09753.1.
X53662 mRNA. Translation: CAA37706.1.
U54831 mRNA. Translation: AAB01982.1.
CCDSiCCDS46776.1. [Q02880-2]
CCDS82746.1. [Q02880-1]
PIRiS26730. A39242.
RefSeqiNP_001059.2. NM_001068.3. [Q02880-2]
NP_001317629.1. NM_001330700.1.
UniGeneiHs.475733.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3QX3X-ray2.16A/B450-1206[»]
4G0UX-ray2.70A/B450-1206[»]
4G0VX-ray2.55A/B450-1206[»]
4G0WX-ray2.70A/B450-1206[»]
4J3NX-ray2.30A/B450-1206[»]
ProteinModelPortaliQ02880.
SMRiQ02880.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi113008. 72 interactors.
IntActiQ02880. 16 interactors.
MINTiMINT-155585.
STRINGi9606.ENSP00000396704.

Chemistry databases

BindingDBiQ02880.
ChEMBLiCHEMBL3396.
DrugBankiDB00970. Dactinomycin.
DB00694. Daunorubicin.
DB00380. Dexrazoxane.
DB00773. Etoposide.

PTM databases

iPTMnetiQ02880.
PhosphoSitePlusiQ02880.
SwissPalmiQ02880.

Polymorphism and mutation databases

DMDMi20141946.

Proteomic databases

EPDiQ02880.
MaxQBiQ02880.
PaxDbiQ02880.
PeptideAtlasiQ02880.
PRIDEiQ02880.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000264331; ENSP00000264331; ENSG00000077097. [Q02880-1]
ENST00000435706; ENSP00000396704; ENSG00000077097. [Q02880-2]
GeneIDi7155.
KEGGihsa:7155.
UCSCiuc003cdj.4. human. [Q02880-1]

Organism-specific databases

CTDi7155.
DisGeNETi7155.
GeneCardsiTOP2B.
H-InvDBHIX0030807.
HGNCiHGNC:11990. TOP2B.
HPAiCAB004601.
HPA024120.
HPA050441.
MIMi126431. gene.
neXtProtiNX_Q02880.
OpenTargetsiENSG00000077097.
PharmGKBiPA36672.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0355. Eukaryota.
COG0187. LUCA.
COG0188. LUCA.
GeneTreeiENSGT00390000016222.
HOGENOMiHOG000216693.
HOVERGENiHBG052998.
InParanoidiQ02880.
KOiK03164.
OMAiEETQNQH.
OrthoDBiEOG091G00U2.
PhylomeDBiQ02880.
TreeFamiTF105282.

Enzyme and pathway databases

BioCyciZFISH:HS01229-MONOMER.
BRENDAi5.99.1.3. 2681.
ReactomeiR-HSA-4615885. SUMOylation of DNA replication proteins.
SIGNORiQ02880.

Miscellaneous databases

ChiTaRSiTOP2B. human.
GeneWikiiTOP2B.
GenomeRNAii7155.
PROiQ02880.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000077097.
CleanExiHS_TOP2B.
ExpressionAtlasiQ02880. baseline and differential.
GenevisibleiQ02880. HS.

Family and domain databases

Gene3Di1.10.268.10. 1 hit.
3.30.1360.40. 1 hit.
3.30.230.10. 1 hit.
3.30.565.10. 1 hit.
3.40.50.670. 1 hit.
3.90.199.10. 1 hit.
InterProiIPR024946. Arg_repress_C-like.
IPR012542. DTHCT.
IPR003594. HATPase_C.
IPR020568. Ribosomal_S5_D2-typ_fold.
IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
IPR028467. Top2b.
IPR001241. Topo_IIA.
IPR013760. Topo_IIA-like_dom.
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.
IPR018522. TopoIIA_CS.
IPR031660. TOPRIM_C.
IPR006171. Toprim_domain.
[Graphical view]
PANTHERiPTHR10169:SF36. PTHR10169:SF36. 1 hit.
PfamiPF00204. DNA_gyraseB. 1 hit.
PF00521. DNA_topoisoIV. 1 hit.
PF08070. DTHCT. 1 hit.
PF02518. HATPase_c. 1 hit.
PF01751. Toprim. 1 hit.
PF16898. TOPRIM_C. 1 hit.
[Graphical view]
PRINTSiPR00418. TPI2FAMILY.
SMARTiSM00433. TOP2c. 1 hit.
SM00434. TOP4c. 1 hit.
[Graphical view]
SUPFAMiSSF54211. SSF54211. 1 hit.
SSF55874. SSF55874. 1 hit.
SSF56719. SSF56719. 1 hit.
PROSITEiPS00177. TOPOISOMERASE_II. 1 hit.
PS50880. TOPRIM. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiTOP2B_HUMAN
AccessioniPrimary (citable) accession number: Q02880
Secondary accession number(s): Q13600, Q9UMG8, Q9UQP8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: January 31, 2002
Last modified: November 30, 2016
This is version 189 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Miscellaneous

Eukaryotic topoisomerase I and II can relax both negative and positive supercoils, whereas prokaryotic enzymes relax only negative supercoils.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.