BRE1_DROME
ID BRE1_DROME Reviewed; 1044 AA.
AC Q9VRP9; C3KGI2; Q8IGT1; Q95TN7;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 2.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=E3 ubiquitin-protein ligase Bre1;
DE EC=2.3.2.27 {ECO:0000250|UniProtKB:O75150};
DE AltName: Full=RING-type E3 ubiquitin transferase Bre1 {ECO:0000305};
DE AltName: Full=dBre1;
GN Name=Bre1; ORFNames=CG10542;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1] {ECO:0000312|EMBL:AAF50744.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000269|PubMed:10731132};
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAF50744.2}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3] {ECO:0000305, ECO:0000312|EMBL:AAN71372.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAN71372.1};
RC TISSUE=Embryo {ECO:0000269|PubMed:12537569};
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley;
RA Carlson J.W., Booth B., Frise E., Park S., Wan K.H., Yu C., Celniker S.E.;
RL Submitted (APR-2009) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15691768; DOI=10.1016/j.devcel.2004.11.020;
RA Bray S., Musisi H., Bienz M.;
RT "Bre1 is required for Notch signaling and histone modification.";
RL Dev. Cell 8:279-286(2005).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-242; SER-243; SER-632 AND
RP SER-638, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
CC -!- FUNCTION: E3 ubiquitin-protein ligase that mediates monoubiquitination
CC of 'Lys-117' of histone H2B. H2B 'Lys-117' ubiquitination gives a
CC specific tag for epigenetic transcriptional activation and is also
CC prerequisite for histone H3 'Lys-4' and 'Lys-79' methylation. It
CC thereby plays a central role in histone code and gene regulation.
CC Required for the expression of Notch target genes in development by
CC affecting the levels of Su(H) in imaginal disk cells and stimulating
CC the Su(H)-mediated transcription of Notch-specific genes.
CC {ECO:0000269|PubMed:15691768}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27; Evidence={ECO:0000250|UniProtKB:O75150};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the BRE1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL13880.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE014296; AAF50744.2; -; Genomic_DNA.
DR EMBL; AY058651; AAL13880.1; ALT_INIT; mRNA.
DR EMBL; BT001617; AAN71372.1; -; mRNA.
DR EMBL; BT082047; ACO95725.1; -; mRNA.
DR RefSeq; NP_001286950.1; NM_001300021.1.
DR RefSeq; NP_647989.2; NM_139732.3.
DR AlphaFoldDB; Q9VRP9; -.
DR SMR; Q9VRP9; -.
DR BioGRID; 64112; 9.
DR IntAct; Q9VRP9; 7.
DR STRING; 7227.FBpp0076822; -.
DR iPTMnet; Q9VRP9; -.
DR PaxDb; Q9VRP9; -.
DR PRIDE; Q9VRP9; -.
DR DNASU; 38652; -.
DR EnsemblMetazoa; FBtr0077116; FBpp0076822; FBgn0086694.
DR EnsemblMetazoa; FBtr0344538; FBpp0310889; FBgn0086694.
DR GeneID; 38652; -.
DR KEGG; dme:Dmel_CG10542; -.
DR CTD; 38652; -.
DR FlyBase; FBgn0086694; Bre1.
DR VEuPathDB; VectorBase:FBgn0086694; -.
DR eggNOG; KOG0978; Eukaryota.
DR HOGENOM; CLU_002640_0_0_1; -.
DR InParanoid; Q9VRP9; -.
DR OMA; THIEIMT; -.
DR OrthoDB; 782448at2759; -.
DR PhylomeDB; Q9VRP9; -.
DR Reactome; R-DME-8866654; E3 ubiquitin ligases ubiquitinate target proteins.
DR Reactome; R-DME-9013422; RHOBTB1 GTPase cycle.
DR SignaLink; Q9VRP9; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 38652; 1 hit in 3 CRISPR screens.
DR ChiTaRS; Bre1; fly.
DR GenomeRNAi; 38652; -.
DR PRO; PR:Q9VRP9; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0086694; Expressed in egg cell and 24 other tissues.
DR ExpressionAtlas; Q9VRP9; baseline and differential.
DR Genevisible; Q9VRP9; DM.
DR GO; GO:0033503; C:HULC complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; ISS:FlyBase.
DR GO; GO:0008270; F:zinc ion binding; ISM:FlyBase.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0071894; P:histone H2B conserved C-terminal lysine ubiquitination; IBA:GO_Central.
DR GO; GO:0016570; P:histone modification; IMP:FlyBase.
DR GO; GO:0010390; P:histone monoubiquitination; IBA:GO_Central.
DR GO; GO:0016574; P:histone ubiquitination; IMP:UniProtKB.
DR GO; GO:0007219; P:Notch signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0006513; P:protein monoubiquitination; IMP:UniProtKB.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR013956; E3_ubiquit_lig_Bre1.
DR InterPro; IPR018957; Znf_C3HC4_RING-type.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR23163; PTHR23163; 4.
DR Pfam; PF00097; zf-C3HC4; 1.
DR SMART; SM00184; RING; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Chromatin regulator; Coiled coil; Metal-binding; Notch signaling pathway;
KW Nucleus; Phosphoprotein; Reference proteome; Transferase;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..1044
FT /note="E3 ubiquitin-protein ligase Bre1"
FT /id="PRO_0000055846"
FT ZN_FING 991..1030
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 182..214
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 312..335
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 546..586
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 615..664
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 43..81
FT /evidence="ECO:0000255"
FT COILED 218..386
FT /evidence="ECO:0000255"
FT COILED 417..546
FT /evidence="ECO:0000255"
FT COILED 664..767
FT /evidence="ECO:0000255"
FT COILED 794..970
FT /evidence="ECO:0000255"
FT COMPBIAS 561..586
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 633..648
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 649..664
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 242
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 243
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 632
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 638
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT CONFLICT 17
FT /note="A -> V (in Ref. 3; AAN71372)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1044 AA; 119060 MW; 426B02E6C90B37BC CRC64;
MSKRSADDAT GSSCLVAAAA AGQPPIKKVH FEPHLIGPVS TLEEMDIKVL EFQNKKLAQR
IEQRMRTEAE LRHRIEQLEK RQTQDDAVLN VVNRYWNQLN EDIRVLLQRF DAETADELEN
RNENEVTTSF LAQLSTWDKE ELDEKLANRV QVSKRAVAKI VQVIDRLMQR NEKITHVLKG
DSLASAGSGS GAGAGGEEEQ QQASGDAETT TSSAGVHALE ETLKQTHIEI MSENHKLQNL
NTSLHEKFHT MSLKMKEYQD AHTAKETENA ELKNQIDELQ YDLEKIHCRN DKLENHLAEA
IEKLKAYHQI YGDPNKSTNS AKTPTTTGSG GATTSVNSQL LEELQKELEE YRELANNRLQ
ELDKLHATHR ETLKEVEKLK MDIRQLPESV IVETTEYKCL QSQFSVLYNE SMQIKTMLDE
TRNQLQTSKN QHLRQIEVME SEELIAQKKV RSEMIQMEDV LALIRKEYET LRIEFEQNMA
ANEQTAPINR EMRHLITSLQ NHNGQLKGEV QRYKRKYKDT STDNLKLRQE LADALATLEG
NKLQAATGAA GEEIKQENST GVKEENSNNV SASGQTNQTN SGNDTNVAIK EENHISAEDE
ADDEASGKDV KDGIKQEKLS SGDAAAAEKK DSPGPGNSTS SATNSVPVKN EKDSKDGVKG
KDVKAVESET VRDLKAQLKK ALNDQKEMKL LLDMYKGVSK DQRDKVQLMA TEKKLRSEIE
ELRQQLKKLQ ESKREERKKL ADEEALRKIK QLEEQKYELQ KQMANHKPTD NSWGSGAPGT
ANYTRPFVGS HEEEALLNEM EVTGQAFEDM QEQNSRLIQQ LREKDDANFK LMSERIKANQ
LHKLLREEKT VLEDQMATAT TQIEAMHIVL RKLEEKERSL QATVASIEKE LMLRQQAMEM
HKRKAIESAQ SAADLKLHLE KYHAQMKEAQ QVVAEKTSSL EAEAYKTKRL QEELAQFKRK
AERMKKMEMS GTTIDEVMIE EIREYKETLT CPSCKVKRKD AVLSKCFHVF CYDCLRTRYE
TRQRKCPKCN CAFGANDYHR LYLQ
