TOP3B_HUMAN
ID TOP3B_HUMAN Reviewed; 862 AA.
AC O95985; A0M8Q3; Q9BUP5;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 196.
DE RecName: Full=DNA topoisomerase 3-beta-1;
DE EC=5.6.2.1 {ECO:0000255|PROSITE-ProRule:PRU10131};
DE AltName: Full=DNA topoisomerase III beta-1;
GN Name=TOP3B; Synonyms=TOP3B1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ALTERNATIVE SPLICING, AND TISSUE
RP SPECIFICITY.
RX PubMed=9927731; DOI=10.1093/nar/27.4.993;
RA Ng S.-W., Liu Y., Hasselblatt K.T., Mok S.C., Berkowitz R.S.;
RT "A new human topoisomerase III that interacts with SGS1 protein.";
RL Nucleic Acids Res. 27:993-1000(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9074928; DOI=10.1101/gr.7.3.250;
RA Kawasaki K., Minoshima S., Nakato E., Shibuya K., Shintani A.,
RA Schmeits J.L., Wang J., Shimizu N.;
RT "One-megabase sequence analysis of the human immunoglobulin lambda gene
RT locus.";
RL Genome Res. 7:250-261(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Hanai R., Li W., Wang J.C.;
RL Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Riou J.F., Goulaouic H., Grondard L.;
RL Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
RA Beare D.M., Dunham I.;
RT "A genome annotation-driven approach to cloning the human ORFeome.";
RL Genome Biol. 5:R84.1-R84.11(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ASN-365.
RC TISSUE=Skin;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Releases the supercoiling and torsional tension of DNA
CC introduced during the DNA replication and transcription by transiently
CC cleaving and rejoining one strand of the DNA duplex. Introduces a
CC single-strand break via transesterification at a target site in duplex
CC DNA. The scissile phosphodiester is attacked by the catalytic tyrosine
CC of the enzyme, resulting in the formation of a DNA-(5'-phosphotyrosyl)-
CC enzyme intermediate and the expulsion of a 3'-OH DNA strand. The free
CC DNA strand than undergoes passage around the unbroken strand thus
CC removing DNA supercoils. Finally, in the religation step, the DNA 3'-OH
CC attacks the covalent intermediate to expel the active-site tyrosine and
CC restore the DNA phosphodiester backbone (By similarity). Possesses
CC negatively supercoiled DNA relaxing activity. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP-independent breakage of single-stranded DNA, followed by
CC passage and rejoining.; EC=5.6.2.1; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU10131};
CC -!- INTERACTION:
CC O95985; Q6UY14-3: ADAMTSL4; NbExp=3; IntAct=EBI-373403, EBI-10173507;
CC O95985; Q9Y2T1: AXIN2; NbExp=3; IntAct=EBI-373403, EBI-4400025;
CC O95985; Q6PI77: BHLHB9; NbExp=3; IntAct=EBI-373403, EBI-11519926;
CC O95985; O76071: CIAO1; NbExp=3; IntAct=EBI-373403, EBI-725145;
CC O95985; Q14296: FASTK; NbExp=3; IntAct=EBI-373403, EBI-1754067;
CC O95985; Q63ZY3: KANK2; NbExp=3; IntAct=EBI-373403, EBI-2556193;
CC O95985; Q9UJV3-2: MID2; NbExp=6; IntAct=EBI-373403, EBI-10172526;
CC O95985; Q9UL42: PNMA2; NbExp=3; IntAct=EBI-373403, EBI-302355;
CC O95985; Q7Z698: SPRED2; NbExp=4; IntAct=EBI-373403, EBI-7082156;
CC O95985; Q9Y2D8: SSX2IP; NbExp=4; IntAct=EBI-373403, EBI-2212028;
CC O95985; Q9H7E2-3: TDRD3; NbExp=4; IntAct=EBI-373403, EBI-10969939;
CC O95985; Q8WV44: TRIM41; NbExp=4; IntAct=EBI-373403, EBI-725997;
CC O95985; P15622-3: ZNF250; NbExp=3; IntAct=EBI-373403, EBI-10177272;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=O95985-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O95985-2; Sequence=VSP_006525, VSP_006526;
CC Name=3;
CC IsoId=O95985-3; Sequence=VSP_006527, VSP_006528;
CC -!- TISSUE SPECIFICITY: Isoform 1 is found in testis, heart and skeletal
CC muscle. A 4 kb transcript which probably represents isoform 2 is found
CC in thymus, kidney and pancreas. {ECO:0000269|PubMed:9927731}.
CC -!- SIMILARITY: Belongs to the type IA topoisomerase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA20009.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF053082; AAD15791.1; -; mRNA.
DR EMBL; D87012; BAA20009.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AF017146; AAD01614.1; -; mRNA.
DR EMBL; AF125216; AAD29670.1; -; mRNA.
DR EMBL; CR456596; CAG30482.1; -; mRNA.
DR EMBL; BC002432; AAH02432.1; -; mRNA.
DR CCDS; CCDS13797.1; -. [O95985-1]
DR RefSeq; NP_001269041.1; NM_001282112.1. [O95985-1]
DR RefSeq; NP_001269042.1; NM_001282113.1. [O95985-1]
DR RefSeq; NP_003926.1; NM_003935.4. [O95985-1]
DR RefSeq; XP_005261868.1; XM_005261811.1.
DR RefSeq; XP_006724412.1; XM_006724349.1.
DR RefSeq; XP_006724413.1; XM_006724350.1.
DR RefSeq; XP_011528784.1; XM_011530482.1.
DR PDB; 5GVC; X-ray; 2.44 A; A/B=1-612.
DR PDB; 5GVE; X-ray; 3.61 A; A=1-612.
DR PDBsum; 5GVC; -.
DR PDBsum; 5GVE; -.
DR AlphaFoldDB; O95985; -.
DR SMR; O95985; -.
DR BioGRID; 114452; 391.
DR ComplexPortal; CPX-1621; TDRD3-TOP3B type IA topoisomerase complex.
DR CORUM; O95985; -.
DR IntAct; O95985; 54.
DR MINT; O95985; -.
DR STRING; 9606.ENSP00000381773; -.
DR iPTMnet; O95985; -.
DR PhosphoSitePlus; O95985; -.
DR BioMuta; TOP3B; -.
DR EPD; O95985; -.
DR jPOST; O95985; -.
DR MassIVE; O95985; -.
DR MaxQB; O95985; -.
DR PaxDb; O95985; -.
DR PeptideAtlas; O95985; -.
DR PRIDE; O95985; -.
DR ProteomicsDB; 51161; -. [O95985-1]
DR ProteomicsDB; 51162; -. [O95985-2]
DR ProteomicsDB; 51163; -. [O95985-3]
DR Antibodypedia; 3974; 209 antibodies from 28 providers.
DR DNASU; 8940; -.
DR Ensembl; ENST00000357179.10; ENSP00000349705.5; ENSG00000100038.20. [O95985-1]
DR Ensembl; ENST00000398793.6; ENSP00000381773.2; ENSG00000100038.20. [O95985-1]
DR GeneID; 8940; -.
DR KEGG; hsa:8940; -.
DR MANE-Select; ENST00000357179.10; ENSP00000349705.5; NM_001282112.2; NP_001269041.1.
DR UCSC; uc002zvs.5; human. [O95985-1]
DR CTD; 8940; -.
DR DisGeNET; 8940; -.
DR GeneCards; TOP3B; -.
DR HGNC; HGNC:11993; TOP3B.
DR HPA; ENSG00000100038; Low tissue specificity.
DR MIM; 603582; gene.
DR neXtProt; NX_O95985; -.
DR OpenTargets; ENSG00000100038; -.
DR PharmGKB; PA36674; -.
DR VEuPathDB; HostDB:ENSG00000100038; -.
DR eggNOG; KOG1957; Eukaryota.
DR GeneTree; ENSGT00940000156516; -.
DR HOGENOM; CLU_002929_1_0_1; -.
DR InParanoid; O95985; -.
DR OMA; TYPRVDT; -.
DR OrthoDB; 373433at2759; -.
DR PhylomeDB; O95985; -.
DR TreeFam; TF105288; -.
DR PathwayCommons; O95985; -.
DR SignaLink; O95985; -.
DR BioGRID-ORCS; 8940; 23 hits in 1085 CRISPR screens.
DR ChiTaRS; TOP3B; human.
DR GeneWiki; TOP3B; -.
DR GenomeRNAi; 8940; -.
DR Pharos; O95985; Tbio.
DR PRO; PR:O95985; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; O95985; protein.
DR Bgee; ENSG00000100038; Expressed in paraflocculus and 106 other tissues.
DR ExpressionAtlas; O95985; baseline and differential.
DR Genevisible; O95985; HS.
DR GO; GO:0000793; C:condensed chromosome; IEA:Ensembl.
DR GO; GO:0140225; C:DNA topoisomerase III-beta-TDRD3 complex; IPI:ComplexPortal.
DR GO; GO:0005634; C:nucleus; IDA:ComplexPortal.
DR GO; GO:0003677; F:DNA binding; TAS:ProtInc.
DR GO; GO:0003916; F:DNA topoisomerase activity; IBA:GO_Central.
DR GO; GO:0003917; F:DNA topoisomerase type I (single strand cut, ATP-independent) activity; IEA:UniProtKB-EC.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0007059; P:chromosome segregation; IEA:Ensembl.
DR GO; GO:0006265; P:DNA topological change; IBA:GO_Central.
DR CDD; cd00186; TOP1Ac; 1.
DR CDD; cd03362; TOPRIM_TopoIA_TopoIII; 1.
DR Gene3D; 1.10.290.10; -; 1.
DR Gene3D; 1.10.460.10; -; 1.
DR Gene3D; 2.70.20.10; -; 1.
DR InterPro; IPR000380; Topo_IA.
DR InterPro; IPR003601; Topo_IA_2.
DR InterPro; IPR023406; Topo_IA_AS.
DR InterPro; IPR013497; Topo_IA_cen.
DR InterPro; IPR013824; Topo_IA_cen_sub1.
DR InterPro; IPR013825; Topo_IA_cen_sub2.
DR InterPro; IPR013826; Topo_IA_cen_sub3.
DR InterPro; IPR023405; Topo_IA_core_domain.
DR InterPro; IPR003602; Topo_IA_DNA-bd_dom.
DR InterPro; IPR006171; TOPRIM_domain.
DR InterPro; IPR034144; TOPRIM_TopoIII.
DR PANTHER; PTHR11390; PTHR11390; 1.
DR Pfam; PF01131; Topoisom_bac; 1.
DR Pfam; PF01751; Toprim; 1.
DR PRINTS; PR00417; PRTPISMRASEI.
DR SMART; SM00437; TOP1Ac; 1.
DR SMART; SM00436; TOP1Bc; 1.
DR SMART; SM00493; TOPRIM; 1.
DR SUPFAM; SSF56712; SSF56712; 1.
DR PROSITE; PS00396; TOPOISOMERASE_I_PROK; 1.
DR PROSITE; PS50880; TOPRIM; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; DNA-binding; Isomerase;
KW Reference proteome; Topoisomerase.
FT CHAIN 1..862
FT /note="DNA topoisomerase 3-beta-1"
FT /id="PRO_0000145192"
FT DOMAIN 3..153
FT /note="Toprim"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT REGION 821..854
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 826..844
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 336
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000250"
FT VAR_SEQ 703..730
FT /note="GMGCNECTHPSCQHSLSMLGIGQCVECE -> GECSHSLLSTGSCSLFSVPT
FT PALHQAGL (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_006525"
FT VAR_SEQ 703..707
FT /note="GMGCN -> VVPCV (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_006527"
FT VAR_SEQ 708..862
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_006528"
FT VAR_SEQ 731..862
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_006526"
FT VARIANT 365
FT /note="D -> N (in dbSNP:rs9610728)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_052591"
FT STRAND 3..10
FT /evidence="ECO:0007829|PDB:5GVC"
FT HELIX 11..21
FT /evidence="ECO:0007829|PDB:5GVC"
FT TURN 22..24
FT /evidence="ECO:0007829|PDB:5GVC"
FT STRAND 27..30
FT /evidence="ECO:0007829|PDB:5GVC"
FT STRAND 37..56
FT /evidence="ECO:0007829|PDB:5GVC"
FT STRAND 61..66
FT /evidence="ECO:0007829|PDB:5GVC"
FT HELIX 78..81
FT /evidence="ECO:0007829|PDB:5GVC"
FT TURN 82..84
FT /evidence="ECO:0007829|PDB:5GVC"
FT STRAND 87..92
FT /evidence="ECO:0007829|PDB:5GVC"
FT HELIX 94..96
FT /evidence="ECO:0007829|PDB:5GVC"
FT HELIX 98..106
FT /evidence="ECO:0007829|PDB:5GVC"
FT STRAND 110..115
FT /evidence="ECO:0007829|PDB:5GVC"
FT HELIX 120..133
FT /evidence="ECO:0007829|PDB:5GVC"
FT HELIX 134..136
FT /evidence="ECO:0007829|PDB:5GVC"
FT TURN 140..143
FT /evidence="ECO:0007829|PDB:5GVC"
FT STRAND 147..149
FT /evidence="ECO:0007829|PDB:5GVC"
FT STRAND 153..156
FT /evidence="ECO:0007829|PDB:5GVC"
FT HELIX 157..165
FT /evidence="ECO:0007829|PDB:5GVC"
FT HELIX 172..199
FT /evidence="ECO:0007829|PDB:5GVC"
FT TURN 200..203
FT /evidence="ECO:0007829|PDB:5GVC"
FT HELIX 209..211
FT /evidence="ECO:0007829|PDB:5GVC"
FT HELIX 218..233
FT /evidence="ECO:0007829|PDB:5GVC"
FT STRAND 239..248
FT /evidence="ECO:0007829|PDB:5GVC"
FT STRAND 254..259
FT /evidence="ECO:0007829|PDB:5GVC"
FT HELIX 267..275
FT /evidence="ECO:0007829|PDB:5GVC"
FT TURN 276..279
FT /evidence="ECO:0007829|PDB:5GVC"
FT STRAND 282..295
FT /evidence="ECO:0007829|PDB:5GVC"
FT HELIX 303..312
FT /evidence="ECO:0007829|PDB:5GVC"
FT HELIX 318..330
FT /evidence="ECO:0007829|PDB:5GVC"
FT STRAND 333..335
FT /evidence="ECO:0007829|PDB:5GVC"
FT HELIX 350..355
FT /evidence="ECO:0007829|PDB:5GVC"
FT TURN 356..359
FT /evidence="ECO:0007829|PDB:5GVC"
FT TURN 361..363
FT /evidence="ECO:0007829|PDB:5GVC"
FT HELIX 364..373
FT /evidence="ECO:0007829|PDB:5GVC"
FT HELIX 398..401
FT /evidence="ECO:0007829|PDB:5GVC"
FT HELIX 403..419
FT /evidence="ECO:0007829|PDB:5GVC"
FT STRAND 424..435
FT /evidence="ECO:0007829|PDB:5GVC"
FT STRAND 438..449
FT /evidence="ECO:0007829|PDB:5GVC"
FT HELIX 451..454
FT /evidence="ECO:0007829|PDB:5GVC"
FT HELIX 457..459
FT /evidence="ECO:0007829|PDB:5GVC"
FT STRAND 475..487
FT /evidence="ECO:0007829|PDB:5GVC"
FT HELIX 496..505
FT /evidence="ECO:0007829|PDB:5GVC"
FT TURN 510..513
FT /evidence="ECO:0007829|PDB:5GVC"
FT HELIX 514..523
FT /evidence="ECO:0007829|PDB:5GVC"
FT STRAND 526..530
FT /evidence="ECO:0007829|PDB:5GVC"
FT TURN 531..533
FT /evidence="ECO:0007829|PDB:5GVC"
FT STRAND 534..537
FT /evidence="ECO:0007829|PDB:5GVC"
FT HELIX 539..551
FT /evidence="ECO:0007829|PDB:5GVC"
FT HELIX 553..555
FT /evidence="ECO:0007829|PDB:5GVC"
FT HELIX 559..572
FT /evidence="ECO:0007829|PDB:5GVC"
FT HELIX 578..598
FT /evidence="ECO:0007829|PDB:5GVC"
FT HELIX 601..610
FT /evidence="ECO:0007829|PDB:5GVC"
SQ SEQUENCE 862 AA; 96662 MW; 75532827856CFF8F CRC64;
MKTVLMVAEK PSLAQSIAKI LSRGSLSSHK GLNGACSVHE YTGTFAGQPV RFKMTSVCGH
VMTLDFLGKY NKWDKVDPAE LFSQAPTEKK EANPKLNMVK FLQVEGRGCD YIVLWLDCDK
EGENICFEVL DAVLPVMNKA HGGEKTVFRA RFSSITDTDI CNAMACLGEP DHNEALSVDA
RQELDLRIGC AFTRFQTKYF QGKYGDLDSS LISFGPCQTP TLGFCVERHD KIQSFKPETY
WVLQAKVNTD KDRSLLLDWD RVRVFDREIA QMFLNMTKLE KEAQVEATSR KEKAKQRPLA
LNTVEMLRVA SSSLGMGPQH AMQTAERLYT QGYISYPRTE TTHYPENFDL KGSLRQQANH
PYWADTVKRL LAEGINRPRK GHDAGDHPPI TPMKSATEAE LGGDAWRLYE YITRHFIATV
SHDCKYLQST ISFRIGPELF TCSGKTVLSP GFTEVMPWQS VPLEESLPTC QRGDAFPVGE
VKMLEKQTNP PDYLTEAELI TLMEKHGIGT DASIPVHINN ICQRNYVTVE SGRRLKPTNL
GIVLVHGYYK IDAELVLPTI RSAVEKQLNL IAQGKADYRQ VLGHTLDVFK RKFHYFVDSI
AGMDELMEVS FSPLAATGKP LSRCGKCHRF MKYIQAKPSR LHCSHCDETY TLPQNGTIKL
YKELRCPLDD FELVLWSSGS RGKSYPLCPY CYNHPPFRDM KKGMGCNECT HPSCQHSLSM
LGIGQCVECE SGVLVLDPTS GPKWKVACNK CNVVAHCFEN AHRVRVSADT CSVCEAALLD
VDFNKAKSPL PGDETQHMGC VFCDPVFQEL VELKHAASCH PMHRGGPGRR QGRGRGRARR
PPGKPNPRRP KDKMSALAAY FV
