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Q64511

- TOP2B_MOUSE

UniProt

Q64511 - TOP2B_MOUSE

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Protein

DNA topoisomerase 2-beta

Gene

Top2b

Organism
Mus musculus (Mouse)
Status
Reviewed - 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. 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 (By similarity).By similarity

Catalytic activityi

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

Cofactori

Magnesium. 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+ and Ca2+.PROSITE-ProRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei100 – 1001ATPBy similarity
Binding sitei129 – 1291ATPBy similarity
Metal bindingi470 – 4701Magnesium 1; catalyticPROSITE-ProRule annotation
Sitei498 – 4981Interaction with DNAPROSITE-ProRule annotation
Sitei501 – 5011Interaction with DNAPROSITE-ProRule annotation
Metal bindingi550 – 5501Magnesium 1; catalyticPROSITE-ProRule annotation
Metal bindingi550 – 5501Magnesium 2PROSITE-ProRule annotation
Metal bindingi552 – 5521Magnesium 2PROSITE-ProRule annotation
Sitei670 – 6701Interaction with DNAPROSITE-ProRule annotation
Sitei671 – 6711Interaction with DNAPROSITE-ProRule annotation
Sitei732 – 7321Interaction with DNAPROSITE-ProRule annotation
Sitei766 – 7661Interaction with DNAPROSITE-ProRule annotation
Sitei813 – 8131Transition state stabilizerBy similarity
Active sitei814 – 8141O-(5'-phospho-DNA)-tyrosine intermediateBy similarity
Sitei865 – 8651Important for DNA bending; intercalates between base pairs of target DNABy similarity
Sitei940 – 9401Interaction with DNAPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi157 – 1593ATPBy similarity
Nucleotide bindingi170 – 1778ATPBy similarity
Nucleotide bindingi385 – 3873ATPBy similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. chromatin binding Source: Ensembl
  3. DNA binding, bending Source: InterPro
  4. DNA topoisomerase type II (ATP-hydrolyzing) activity Source: UniProtKB
  5. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. ATP catabolic process Source: GOC
  2. axonogenesis Source: MGI
  3. DNA topological change Source: UniProtKB
  4. DNA unwinding involved in DNA replication Source: RefGenome
  5. forebrain development Source: MGI
  6. mitotic DNA integrity checkpoint Source: RefGenome
  7. mitotic recombination Source: RefGenome
  8. neuron migration Source: MGI
  9. resolution of meiotic recombination intermediates Source: RefGenome
  10. sister chromatid segregation Source: RefGenome
Complete GO annotation...

Keywords - Molecular functioni

Isomerase, Topoisomerase

Keywords - Ligandi

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

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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 14

Organism-specific databases

MGIiMGI:98791. Top2b.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Ensembl
  2. DNA topoisomerase complex (ATP-hydrolyzing) Source: RefGenome
  3. nucleoplasm Source: Ensembl
  4. nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 16121611DNA topoisomerase 2-betaPRO_0000145370Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Modified residuei3 – 31N6-acetyllysine1 Publication
Modified residuei1224 – 12241PhosphoserineBy similarity
Modified residuei1280 – 12801PhosphothreonineBy similarity
Modified residuei1324 – 13241PhosphoserineBy similarity
Modified residuei1328 – 13281PhosphoserineBy similarity
Modified residuei1330 – 13301PhosphoserineBy similarity
Modified residuei1332 – 13321PhosphoserineBy similarity
Modified residuei1346 – 13461PhosphoserineBy similarity
Modified residuei1363 – 13631PhosphoserineBy similarity
Modified residuei1387 – 13871Phosphoserine1 Publication
Modified residuei1390 – 13901PhosphothreonineBy similarity
Modified residuei1400 – 14001Phosphoserine1 Publication
Modified residuei1408 – 14081PhosphotyrosineBy similarity
Modified residuei1411 – 14111PhosphoserineBy similarity
Modified residuei1428 – 14281PhosphoserineBy similarity
Modified residuei1439 – 14391PhosphoserineBy similarity
Modified residuei1441 – 14411PhosphoserineBy similarity
Modified residuei1448 – 14481PhosphoserineBy similarity
Modified residuei1453 – 14531PhosphoserineBy similarity
Modified residuei1460 – 14601PhosphoserineBy similarity
Modified residuei1509 – 15091Phosphoserine3 Publications
Modified residuei1511 – 15111Phosphoserine3 Publications
Modified residuei1513 – 15131Phosphoserine1 Publication
Modified residuei1537 – 15371Phosphoserine1 Publication
Modified residuei1539 – 15391Phosphoserine1 Publication
Modified residuei1562 – 15621PhosphothreonineBy similarity
Modified residuei1568 – 15681PhosphoserineBy similarity
Modified residuei1596 – 15961PhosphotyrosineBy similarity
Modified residuei1600 – 16001PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ64511.
PaxDbiQ64511.
PRIDEiQ64511.

PTM databases

PhosphoSiteiQ64511.

Expressioni

Gene expression databases

BgeeiQ64511.
CleanExiMM_TOP2B.
ExpressionAtlasiQ64511. baseline and differential.
GenevestigatoriQ64511.

Interactioni

Subunit structurei

Homodimer. Component of the WINAC complex, at least composed of SMARCA2, SMARCA4, SMARCB1, SMARCC1, SMARCC2, SMARCD1, SMARCE1, ACTL6A, BAZ1B/WSTF, ARID1A, SUPT16H, CHAF1A and TOP2B (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
AicdaQ9WVE03EBI-2325586,EBI-3835567

Protein-protein interaction databases

BioGridi204277. 5 interactions.
IntActiQ64511. 6 interactions.
MINTiMINT-4138251.
STRINGi10090.ENSMUSP00000017629.

Structurei

3D structure databases

ProteinModelPortaliQ64511.
SMRiQ64511. Positions 38-1194.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini464 – 581118ToprimPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni351 – 3533Interaction with DNABy similarity
Regioni999 – 100810Interaction with DNABy similarity

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0187.
GeneTreeiENSGT00390000016222.
HOGENOMiHOG000216693.
HOVERGENiHBG052998.
InParanoidiQ64511.
KOiK03164.
OMAiEPLTQFM.
OrthoDBiEOG73JKTM.
PhylomeDBiQ64511.
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.
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.
[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.
[Graphical view]
PRINTSiPR00418. TPI2FAMILY.
SMARTiSM00387. HATPase_c. 1 hit.
SM00433. 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]

Sequencei

Sequence statusi: Complete.

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

Q64511-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAKSSLAGSD GALTWVNNAT KKEELETANK NDSTKKLSVE RVYQKKTQLE
60 70 80 90 100
HILLRPDTYI GSVEPLTQLM WVYDEDVGMN CREVTFVPGL YKIFDEILVN
110 120 130 140 150
AADNKQRDKN MTCIKVSIDP ESNIISIWNN GKGIPVVEHK VEKVYVPALI
160 170 180 190 200
FGQLLTSSNY DDDEKKVTGG RNGYGAKLCN IFSTKFTVET ACKEYKHSFK
210 220 230 240 250
QTWMNNMMKT SEAKIKHFDG EDYTCITFQP DLSKFKMEKL DKDIVALMTR
260 270 280 290 300
RAYDLAGSCK GVKVMFNGKK LPVNGFRSYV DLYVKDKLDE TGVALKVIHE
310 320 330 340 350
LANERWDVCL TLSEKGFQQI SFVNSIATTK GGRHVDYVVD QVVSKLIEVV
360 370 380 390 400
KKKNKAGVSV KPFQVKNHIW VFINCLIENP TFDSQTKENM TLQPKSFGSK
410 420 430 440 450
CQLSEKFFKA ASNCGIVESI LNWVKFKAQT QLNKKCSSVK YSKIKGIPKL
460 470 480 490 500
DDANDAGGKH SLECTLILTE GDSAKSLAVS GLGVIGRDRY GVFPLRGKIL
510 520 530 540 550
NVREASHKQI MENAEINNII KIVGLQYKKS YDDAESLKTL RYGKIMIMTD
560 570 580 590 600
QDQDGSHIKG LLINFIHHNW PSLLKHGFLE EFITPIVKAS KNKQELSFYS
610 620 630 640 650
IPEFDEWKKH IENQKAWKIK YYKGLGTSTA KEAKEYFADM ERHRILFRYA
660 670 680 690 700
GPEDDAAITL AFSKKKIDDR KEWLTNFMED RRQRRLHGLP EQFLYGTATK
710 720 730 740 750
HLTYNDFINK ELILFSNSDN ERSIPSLVDG FKPGQRKVLF TCFKRNDKRE
760 770 780 790 800
VKVAQLAGSV AEMSAYHHGE QALMMTIVNL AQNFVGSNNI NLLQPIGQFG
810 820 830 840 850
TRLHGGKDAA SPRYIFTMLS SLARLLFPAV DDNLLKFLYD DNQRVEPEWY
860 870 880 890 900
IPIIPMVLIN GAEGIGTGWA CKLPNYDARE IVNNVRRMLE GLDPHPMLPN
910 920 930 940 950
YKNFKGTIQE LGQNQYAVSG EIFVVDRNTV EITELPVRTW TQVYKEQVLE
960 970 980 990 1000
PMLNGTDKTP ALISDYKEYH TDTTVKFVVK MTEEKLAQAE AAGLHKVFKL
1010 1020 1030 1040 1050
QTTLTCNSMV LFDHMGCLKK YETVQDILKE FFDLRLSYYG LRKEWLVGML
1060 1070 1080 1090 1100
GAESTKLNNQ ARFILEKIQG KITIENRSKK DLIQMLVQRG YESDPVKAWK
1110 1120 1130 1140 1150
EAQEKAAEEE DSQNQHDDSS SDSGTPSGPD FNYILNMSLW SLTKEKVEEL
1160 1170 1180 1190 1200
IKQRDTKGRE VNDLKRKSPS DLWKEDLAAF VEELDKVEAQ EREDILAGMS
1210 1220 1230 1240 1250
GKAIKGKVGK PKVKKLQLEE TMPSPYGRRI VPEITAMKAD ASRKLLKKKK
1260 1270 1280 1290 1300
GDPDTTVVKV EFDEEFSGTP AEGTGEETLT PSAPVNKGPK PKREKKEPGT
1310 1320 1330 1340 1350
RVRKTPTSTG KTNAKKVKKR NPWSDDESKS ESDLEEAEPV VIPRDSLLRR
1360 1370 1380 1390 1400
AAAERPKYTF DFSEEEDDDA AAADDSNDLE ELKVKASPIT NDGEDEFVPS
1410 1420 1430 1440 1450
DGLDKDEYAF SSGKSKATPE KSSNDKKSQD FGNLFSFPSY SQKSEDDSAK
1460 1470 1480 1490 1500
FDSNEEDTAS VFAPSFGLKQ TDKLPSKTVA AKKGKPPSDT APKAKRAPKQ
1510 1520 1530 1540 1550
KKIVETINSD SDSEFGIPKK TTTPKGKGRG AKKRKASGSE NEGDYNPGRK
1560 1570 1580 1590 1600
PSKTASKKPK KTSFDQDSDV DIFPSDFTSE PPALPRTGRA RKEVKYFAES
1610
DEEEDVDFAM FN
Length:1,612
Mass (Da):181,909
Last modified:September 27, 2005 - v2
Checksum:i974D9D5DAD0DB96A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti16 – 161V → A in BAA07236. 1 PublicationCurated
Sequence conflicti1434 – 14341L → P in BAA07236. 1 PublicationCurated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D38046 mRNA. Translation: BAA07236.1.
BC041106 mRNA. Translation: AAH41106.1.
BC054541 mRNA. Translation: AAH54541.1.
CCDSiCCDS26833.1.
RefSeqiNP_033435.2. NM_009409.2.
UniGeneiMm.130362.

Genome annotation databases

EnsembliENSMUST00000017629; ENSMUSP00000017629; ENSMUSG00000017485.
GeneIDi21974.
KEGGimmu:21974.
UCSCiuc007shc.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D38046 mRNA. Translation: BAA07236.1 .
BC041106 mRNA. Translation: AAH41106.1 .
BC054541 mRNA. Translation: AAH54541.1 .
CCDSi CCDS26833.1.
RefSeqi NP_033435.2. NM_009409.2.
UniGenei Mm.130362.

3D structure databases

ProteinModelPortali Q64511.
SMRi Q64511. Positions 38-1194.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 204277. 5 interactions.
IntActi Q64511. 6 interactions.
MINTi MINT-4138251.
STRINGi 10090.ENSMUSP00000017629.

Chemistry

BindingDBi Q64511.
ChEMBLi CHEMBL5564.

PTM databases

PhosphoSitei Q64511.

Proteomic databases

MaxQBi Q64511.
PaxDbi Q64511.
PRIDEi Q64511.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000017629 ; ENSMUSP00000017629 ; ENSMUSG00000017485 .
GeneIDi 21974.
KEGGi mmu:21974.
UCSCi uc007shc.1. mouse.

Organism-specific databases

CTDi 7155.
MGIi MGI:98791. Top2b.

Phylogenomic databases

eggNOGi COG0187.
GeneTreei ENSGT00390000016222.
HOGENOMi HOG000216693.
HOVERGENi HBG052998.
InParanoidi Q64511.
KOi K03164.
OMAi EPLTQFM.
OrthoDBi EOG73JKTM.
PhylomeDBi Q64511.
TreeFami TF105282.

Miscellaneous databases

NextBioi 301674.
PROi Q64511.
SOURCEi Search...

Gene expression databases

Bgeei Q64511.
CleanExi MM_TOP2B.
ExpressionAtlasi Q64511. baseline and differential.
Genevestigatori Q64511.

Family and domain databases

Gene3Di 1.10.268.10. 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.
InterProi IPR024946. 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.
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.
[Graphical view ]
PANTHERi PTHR10169:SF36. PTHR10169:SF36. 1 hit.
Pfami PF00204. DNA_gyraseB. 1 hit.
PF00521. DNA_topoisoIV. 1 hit.
PF08070. DTHCT. 1 hit.
PF02518. HATPase_c. 1 hit.
PF01751. Toprim. 1 hit.
[Graphical view ]
PRINTSi PR00418. TPI2FAMILY.
SMARTi SM00387. HATPase_c. 1 hit.
SM00433. TOP2c. 1 hit.
SM00434. TOP4c. 1 hit.
[Graphical view ]
SUPFAMi SSF54211. SSF54211. 1 hit.
SSF55874. SSF55874. 1 hit.
SSF56719. SSF56719. 1 hit.
PROSITEi PS00177. TOPOISOMERASE_II. 1 hit.
PS50880. TOPRIM. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Miyaike M., Adachi N., Kikuchi A.
    Submitted (SEP-1994) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: BALB/c.
    Tissue: Brain.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6.
    Tissue: Brain and Eye.
  3. "Comprehensive identification of phosphorylation sites in postsynaptic density preparations."
    Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.
    Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.
  4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1387; SER-1509; SER-1511; SER-1513; SER-1537 AND SER-1539, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  5. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1400; SER-1509 AND SER-1511, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  6. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
    Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
    Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1509 AND SER-1511, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  7. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2 AND LYS-3, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiTOP2B_MOUSE
AccessioniPrimary (citable) accession number: Q64511
Secondary accession number(s): Q7TQG4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: September 27, 2005
Last modified: October 29, 2014
This is version 138 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

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

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3