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E3 ubiquitin-protein ligase Topors (EC 2.3.2.27) (RING-type E3 ubiquitin transferase Topors) (SUMO1-protein E3 ligase Topors) (Topoisomerase I-binding RING finger protein) (Topoisomerase I-binding arginine/serine-rich protein) (dTopors)

 TOPRS_DROME             Reviewed;        1038 AA.
Q9V8P9;
18-APR-2006, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
25-OCT-2017, entry version 136.
RecName: Full=E3 ubiquitin-protein ligase Topors;
EC=2.3.2.27;
AltName: Full=RING-type E3 ubiquitin transferase Topors {ECO:0000305};
AltName: Full=SUMO1-protein E3 ligase Topors;
AltName: Full=Topoisomerase I-binding RING finger protein;
AltName: Full=Topoisomerase I-binding arginine/serine-rich protein;
AltName: Full=dTopors;
Name=Topors; ORFNames=CG15104;
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
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.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[2]
GENOME REANNOTATION.
STRAIN=Berkeley;
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Berkeley; TISSUE=Embryo;
PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M.,
George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H.,
Rubin G.M., Celniker S.E.;
"A Drosophila full-length cDNA resource.";
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
[4]
FUNCTION, INTERACTION WITH H; P53 AND TOP1, AND MUTAGENESIS OF
CYS-102.
PubMed=14871887; DOI=10.1074/jbc.M310097200;
Secombe J., Parkhurst S.M.;
"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.";
J. Biol. Chem. 279:17126-17133(2004).
[5]
FUNCTION, INTERACTION WITH CP190; LAM; MOD(MDG4) AND SU(HW),
SUBCELLULAR LOCATION, AND MUTAGENESIS OF CYS-118.
PubMed=16209949; DOI=10.1016/j.molcel.2005.08.031;
Capelson M., Corces V.G.;
"The ubiquitin ligase dTopors directs the nuclear organization of a
chromatin insulator.";
Mol. Cell 20:105-116(2005).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-820 AND SER-822, AND
IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Embryo;
PubMed=18327897; DOI=10.1021/pr700696a;
Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
"Phosphoproteome analysis of Drosophila melanogaster embryos.";
J. Proteome Res. 7:1675-1682(2008).
-!- FUNCTION: 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.
{ECO:0000269|PubMed:14871887, ECO:0000269|PubMed:16209949}.
-!- CATALYTIC ACTIVITY: S-ubiquitinyl-[E2 ubiquitin-conjugating
enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-
conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor
protein]-L-lysine.
-!- SUBUNIT: 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. {ECO:0000269|PubMed:14871887,
ECO:0000269|PubMed:16209949}.
-!- INTERACTION:
P14003:h; NbExp=4; IntAct=EBI-147805, EBI-123011;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16209949}.
Chromosome {ECO:0000269|PubMed:16209949}. Note=Colocalizes with
the gypsy chromatin insulator complex on polytene chromosomes and
to nuclear insulator bodies. Also localizes to the nuclear lamina.
-----------------------------------------------------------------------
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EMBL; AE013599; AAF57614.1; -; Genomic_DNA.
EMBL; AY122186; AAM52698.1; -; mRNA.
RefSeq; NP_001261083.1; NM_001274154.1.
RefSeq; NP_611388.1; NM_137544.3.
UniGene; Dm.10778; -.
ProteinModelPortal; Q9V8P9; -.
SMR; Q9V8P9; -.
BioGrid; 62854; 10.
IntAct; Q9V8P9; 3.
STRING; 7227.FBpp0304302; -.
iPTMnet; Q9V8P9; -.
PaxDb; Q9V8P9; -.
PRIDE; Q9V8P9; -.
EnsemblMetazoa; FBtr0086570; FBpp0085754; FBgn0267351.
EnsemblMetazoa; FBtr0331977; FBpp0304302; FBgn0267351.
GeneID; 37188; -.
KEGG; dme:Dmel_CG15104; -.
CTD; 10210; -.
FlyBase; FBgn0267351; Topors.
eggNOG; KOG4430; Eukaryota.
eggNOG; ENOG410XQZR; LUCA.
GeneTree; ENSGT00530000064170; -.
InParanoid; Q9V8P9; -.
KO; K10631; -.
OMA; QAVMTND; -.
OrthoDB; EOG091G089U; -.
PhylomeDB; Q9V8P9; -.
ChiTaRS; Topors; fly.
GenomeRNAi; 37188; -.
PRO; PR:Q9V8P9; -.
Proteomes; UP000000803; Chromosome 2R.
Bgee; FBgn0267351; -.
ExpressionAtlas; Q9V8P9; differential.
Genevisible; Q9V8P9; DM.
GO; GO:0005652; C:nuclear lamina; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:FlyBase.
GO; GO:0005700; C:polytene chromosome; IDA:UniProtKB.
GO; GO:0005521; F:lamin binding; IDA:UniProtKB.
GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:FlyBase.
GO; GO:0008270; F:zinc ion binding; ISM:FlyBase.
GO; GO:0051299; P:centrosome separation; IMP:FlyBase.
GO; GO:0016569; P:covalent chromatin modification; IEA:UniProtKB-KW.
GO; GO:0007060; P:male meiosis chromosome segregation; IMP:FlyBase.
GO; GO:0007140; P:male meiotic nuclear division; IMP:FlyBase.
GO; GO:0010032; P:meiotic chromosome condensation; IMP:FlyBase.
GO; GO:0007095; P:mitotic G2 DNA damage checkpoint; IGI:FlyBase.
GO; GO:0071763; P:nuclear membrane organization; IMP:FlyBase.
GO; GO:0006997; P:nucleus organization; IMP:UniProtKB.
GO; GO:0000209; P:protein polyubiquitination; IDA:UniProtKB.
GO; GO:0042787; P:protein ubiquitination involved in ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IGI:UniProtKB.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IDA:FlyBase.
Gene3D; 2.130.10.10; -; 2.
Gene3D; 3.30.40.10; -; 1.
InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
InterPro; IPR018957; Znf_C3HC4_RING-type.
InterPro; IPR001841; Znf_RING.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
InterPro; IPR017907; Znf_RING_CS.
Pfam; PF00097; zf-C3HC4; 1.
SMART; SM00184; RING; 1.
PROSITE; PS00518; ZF_RING_1; 1.
PROSITE; PS50089; ZF_RING_2; 1.
1: Evidence at protein level;
Chromatin regulator; Chromosome; Complete proteome; Metal-binding;
Nucleus; Phosphoprotein; Reference proteome; Transcription;
Transcription regulation; Transferase; Ubl conjugation pathway; Zinc;
Zinc-finger.
CHAIN 1 1038 E3 ubiquitin-protein ligase Topors.
/FTId=PRO_0000232628.
ZN_FING 102 141 RING-type. {ECO:0000255|PROSITE-
ProRule:PRU00175}.
REGION 495 682 Interaction with h/hairy.
MOD_RES 820 820 Phosphothreonine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 822 822 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
MUTAGEN 102 102 C->A: Abrogates ubiquitin-protein E3
ligase activity.
{ECO:0000269|PubMed:14871887}.
MUTAGEN 118 118 C->S: Abrogates enhancement of gypsy
chromatin insulator activity.
{ECO:0000269|PubMed:16209949}.
SEQUENCE 1038 AA; 113313 MW; BEB3E63AA131E9E8 CRC64;
MAEENPGALA ANVPYLGVDE LGASVIVEPG LEGSNAGGRT LPAAAIKFAD LTESGSESGD
NEAEEPVSAG PDNANAIGEP GTSASAAEEN GTVERNSPPP NCAICLSRCR RKCFTDSCMH
QFCFKCLCEW SKIKPECPLC KQPFRTIIHN VRTLDDYDRY PVQTTSPVPT ENPSLRYHIV
RRPRYTPLVQ NQAVIVNDIE AAIAAGAAGE DVLSAAEVAA GRRSYSRFEP YRSELMNYYQ
HDQDASTSGS LSQLWRRYVY DRKLYALPVS DSVTGHFREW SARFYRNNPA QIHRLMPWIH
RDIMCLLRNA AHSVNTVMTL MSDLLPMTSL LGPTFRRRLS PYLGERTSHF IHELFNFARS
PYDINGYDHV VQYSARVAEE VEVDLLDMVE TQSSNGDDLN LEVGDSDADA INAGFSPDWS
PPRVRPSTSV IVTNPGATHS FSVTMASDGS ELPGISIRRT TNVGSQTVAI NLSMRRPAAV
ASEEPEVIEI DDGDAAANAE VAAINDGSNT SRRHAGATLP VTAHIELESS SSSGDEDECV
FVLELKPPHM RTPEQVSLDS NSDSDVVFVN EQHEAAPDAI AENRSTQSPL DLASRDQGLF
MGPSTSGAAA NRGKNWKLVM AQTRRLDQLR TLRSIRSKKS RRSSMPARSD SGSSPSSCSS
SSFHFSSSSD EDSSDSSTTN SEPPKKKSRK RVANNKRSKK ESIGKRTSRK RKAKDQNMEM
LEQQQISQKK PQRQPESSSD SPSSSDDESG GDSSESSGQP NTNNNKSSSD SDDDSAVNMQ
LSALRATLKA EATLEDRKPV KLELQLPDDD QAGPLHSRMT PSPREDNEPG CSAPKRRRSC
SHSNQSSQSA SLASSSTATS SSAPLSSFAW GAAGFSGDPL MRGHPAMEEH DIANSLIELS
TLTQPVNIGL FNEHYNSAEN SMGMLSNTLC DSPQTLAADD ANLENYFDTD ADPEASRERD
AYSLEAAIDV VGESELQIAE DTATATEEQD EEDEEDEDQE EDDQEEEKAA EEEEEEEEDD
DDSDNHDEND ENQGLLPY


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