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Protein

E3 ubiquitin-protein ligase Topors

Gene

Topors

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Functions as a ubiquitin-protein E3 ligase. Negatively regulates the transcriptional repressor h/hairy by promoting its ubiquitination and subsequent degradation. Also directs the nuclear organization of the gypsy chromatin insulator. Chromatin insulators are regulatory elements which establish independent domains of transcriptional activity within eukaryotic genomes. Insulators have two defining properties; they can block the communication between an enhancer and a promoter when placed between them, and can also buffer transgenes from position effect variegation (PEV). Insulators are proposed to structure the chromatin fiber into independent domains of differing transcriptional potential by promoting the formation of distinct chromatin loops. This chromatin looping may require the formation of insulator bodies, where homotypic interactions between individual subunits of the insulator complex could promote the clustering of widely spaced insulators at the nuclear periphery. Within the gypsy insulator complex, this protein may promote formation of nuclear insulator bodies by recruiting individual insulator complexes to the nuclear lamina.2 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri102 – 14140RING-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  • lamin binding Source: UniProtKB
  • ligase activity Source: UniProtKB-KW
  • ubiquitin protein ligase activity Source: FlyBase
  • zinc ion binding Source: FlyBase

GO - Biological processi

  • centrosome separation Source: FlyBase
  • chromatin modification Source: UniProtKB-KW
  • male meiosis Source: FlyBase
  • male meiosis chromosome segregation Source: FlyBase
  • meiotic chromosome condensation Source: FlyBase
  • mitotic G2 DNA damage checkpoint Source: FlyBase
  • nuclear membrane organization Source: FlyBase
  • nucleus organization Source: UniProtKB
  • protein polyubiquitination Source: UniProtKB
  • protein ubiquitination involved in ubiquitin-dependent protein catabolic process Source: UniProtKB
  • regulation of transcription, DNA-templated Source: UniProtKB
  • transcription, DNA-templated Source: UniProtKB-KW
  • ubiquitin-dependent protein catabolic process Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Ligase

Keywords - Biological processi

Transcription, Transcription regulation, Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
E3 ubiquitin-protein ligase Topors (EC:6.3.2.-)
Alternative name(s):
SUMO1-protein E3 ligase Topors
Topoisomerase I-binding RING finger protein
Topoisomerase I-binding arginine/serine-rich protein
dTopors
Gene namesi
Name:Topors
ORF Names:CG15104
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 2R

Organism-specific databases

FlyBaseiFBgn0267351. Topors.

Subcellular locationi

  • Nucleus 1 Publication
  • Chromosome 1 Publication

  • Note: Colocalizes with the gypsy chromatin insulator complex on polytene chromosomes and to nuclear insulator bodies. Also localizes to the nuclear lamina.

GO - Cellular componenti

  • nuclear lamina Source: UniProtKB
  • nucleus Source: FlyBase
  • polytene chromosome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi102 – 1021C → A: Abrogates ubiquitin-protein E3 ligase activity. 1 Publication
Mutagenesisi118 – 1181C → S: Abrogates enhancement of gypsy chromatin insulator activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10381038E3 ubiquitin-protein ligase ToporsPRO_0000232628Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei820 – 8201Phosphothreonine1 Publication
Modified residuei822 – 8221Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ9V8P9.
PRIDEiQ9V8P9.

PTM databases

iPTMnetiQ9V8P9.

Expressioni

Gene expression databases

BgeeiQ9V8P9.
GenevisibleiQ9V8P9. DM.

Interactioni

Subunit structurei

Interacts with h/hairy, p53 and Top1. Interacts with the gypsy chromatin insulator complex, composed of Cp190, mod(mdg4) and su(Hw); interacts directly with mod(mdg4) and su(Hw). Interacts with Lam/lamin.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
hP140034EBI-147805,EBI-123011

GO - Molecular functioni

  • lamin binding Source: UniProtKB

Protein-protein interaction databases

BioGridi62854. 2 interactions.
IntActiQ9V8P9. 3 interactions.
STRINGi7227.FBpp0304302.

Structurei

3D structure databases

ProteinModelPortaliQ9V8P9.
SMRiQ9V8P9. Positions 102-157.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni495 – 682188Interaction with h/hairyAdd
BLAST

Sequence similaritiesi

Contains 1 RING-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri102 – 14140RING-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiKOG4430. Eukaryota.
ENOG410XQZR. LUCA.
GeneTreeiENSGT00530000064170.
InParanoidiQ9V8P9.
KOiK10631.
OMAiELMNYYR.
OrthoDBiEOG722J8G.
PhylomeDBiQ9V8P9.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR018957. Znf_C3HC4_RING-type.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PfamiPF00097. zf-C3HC4. 1 hit.
[Graphical view]
SMARTiSM00184. RING. 1 hit.
[Graphical view]
PROSITEiPS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9V8P9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAEENPGALA ANVPYLGVDE LGASVIVEPG LEGSNAGGRT LPAAAIKFAD
60 70 80 90 100
LTESGSESGD NEAEEPVSAG PDNANAIGEP GTSASAAEEN GTVERNSPPP
110 120 130 140 150
NCAICLSRCR RKCFTDSCMH QFCFKCLCEW SKIKPECPLC KQPFRTIIHN
160 170 180 190 200
VRTLDDYDRY PVQTTSPVPT ENPSLRYHIV RRPRYTPLVQ NQAVIVNDIE
210 220 230 240 250
AAIAAGAAGE DVLSAAEVAA GRRSYSRFEP YRSELMNYYQ HDQDASTSGS
260 270 280 290 300
LSQLWRRYVY DRKLYALPVS DSVTGHFREW SARFYRNNPA QIHRLMPWIH
310 320 330 340 350
RDIMCLLRNA AHSVNTVMTL MSDLLPMTSL LGPTFRRRLS PYLGERTSHF
360 370 380 390 400
IHELFNFARS PYDINGYDHV VQYSARVAEE VEVDLLDMVE TQSSNGDDLN
410 420 430 440 450
LEVGDSDADA INAGFSPDWS PPRVRPSTSV IVTNPGATHS FSVTMASDGS
460 470 480 490 500
ELPGISIRRT TNVGSQTVAI NLSMRRPAAV ASEEPEVIEI DDGDAAANAE
510 520 530 540 550
VAAINDGSNT SRRHAGATLP VTAHIELESS SSSGDEDECV FVLELKPPHM
560 570 580 590 600
RTPEQVSLDS NSDSDVVFVN EQHEAAPDAI AENRSTQSPL DLASRDQGLF
610 620 630 640 650
MGPSTSGAAA NRGKNWKLVM AQTRRLDQLR TLRSIRSKKS RRSSMPARSD
660 670 680 690 700
SGSSPSSCSS SSFHFSSSSD EDSSDSSTTN SEPPKKKSRK RVANNKRSKK
710 720 730 740 750
ESIGKRTSRK RKAKDQNMEM LEQQQISQKK PQRQPESSSD SPSSSDDESG
760 770 780 790 800
GDSSESSGQP NTNNNKSSSD SDDDSAVNMQ LSALRATLKA EATLEDRKPV
810 820 830 840 850
KLELQLPDDD QAGPLHSRMT PSPREDNEPG CSAPKRRRSC SHSNQSSQSA
860 870 880 890 900
SLASSSTATS SSAPLSSFAW GAAGFSGDPL MRGHPAMEEH DIANSLIELS
910 920 930 940 950
TLTQPVNIGL FNEHYNSAEN SMGMLSNTLC DSPQTLAADD ANLENYFDTD
960 970 980 990 1000
ADPEASRERD AYSLEAAIDV VGESELQIAE DTATATEEQD EEDEEDEDQE
1010 1020 1030
EDDQEEEKAA EEEEEEEEDD DDSDNHDEND ENQGLLPY
Length:1,038
Mass (Da):113,313
Last modified:May 1, 2000 - v1
Checksum:iBEB3E63AA131E9E8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE013599 Genomic DNA. Translation: AAF57614.1.
AY122186 mRNA. Translation: AAM52698.1.
RefSeqiNP_001261083.1. NM_001274154.1.
NP_611388.1. NM_137544.3.
UniGeneiDm.10778.

Genome annotation databases

EnsemblMetazoaiFBtr0086570; FBpp0085754; FBgn0267351.
FBtr0331977; FBpp0304302; FBgn0267351.
GeneIDi37188.
KEGGidme:Dmel_CG15104.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE013599 Genomic DNA. Translation: AAF57614.1.
AY122186 mRNA. Translation: AAM52698.1.
RefSeqiNP_001261083.1. NM_001274154.1.
NP_611388.1. NM_137544.3.
UniGeneiDm.10778.

3D structure databases

ProteinModelPortaliQ9V8P9.
SMRiQ9V8P9. Positions 102-157.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi62854. 2 interactions.
IntActiQ9V8P9. 3 interactions.
STRINGi7227.FBpp0304302.

PTM databases

iPTMnetiQ9V8P9.

Proteomic databases

PaxDbiQ9V8P9.
PRIDEiQ9V8P9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0086570; FBpp0085754; FBgn0267351.
FBtr0331977; FBpp0304302; FBgn0267351.
GeneIDi37188.
KEGGidme:Dmel_CG15104.

Organism-specific databases

CTDi10210.
FlyBaseiFBgn0267351. Topors.

Phylogenomic databases

eggNOGiKOG4430. Eukaryota.
ENOG410XQZR. LUCA.
GeneTreeiENSGT00530000064170.
InParanoidiQ9V8P9.
KOiK10631.
OMAiELMNYYR.
OrthoDBiEOG722J8G.
PhylomeDBiQ9V8P9.

Miscellaneous databases

ChiTaRSiTopors. fly.
GenomeRNAii37188.
PROiQ9V8P9.

Gene expression databases

BgeeiQ9V8P9.
GenevisibleiQ9V8P9. DM.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR018957. Znf_C3HC4_RING-type.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PfamiPF00097. zf-C3HC4. 1 hit.
[Graphical view]
SMARTiSM00184. RING. 1 hit.
[Graphical view]
PROSITEiPS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  2. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Embryo.
  4. "Drosophila Topors is a RING finger-containing protein that functions as a ubiquitin-protein isopeptide ligase for the hairy basic helix-loop-helix repressor protein."
    Secombe J., Parkhurst S.M.
    J. Biol. Chem. 279:17126-17133(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH H; P53 AND TOP1, MUTAGENESIS OF CYS-102.
  5. "The ubiquitin ligase dTopors directs the nuclear organization of a chromatin insulator."
    Capelson M., Corces V.G.
    Mol. Cell 20:105-116(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH CP190; LAM; MOD(MDG4) AND SU(HW), SUBCELLULAR LOCATION, MUTAGENESIS OF CYS-118.
  6. "Phosphoproteome analysis of Drosophila melanogaster embryos."
    Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.
    J. Proteome Res. 7:1675-1682(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-820 AND SER-822, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Embryo.

Entry informationi

Entry nameiTOPRS_DROME
AccessioniPrimary (citable) accession number: Q9V8P9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 18, 2006
Last sequence update: May 1, 2000
Last modified: July 6, 2016
This is version 122 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. 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.