BRE1_YEAST
ID BRE1_YEAST Reviewed; 700 AA.
AC Q07457; D6VRS5;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=E3 ubiquitin-protein ligase BRE1;
DE EC=2.3.2.27 {ECO:0000269|PubMed:12535538};
DE AltName: Full=Brefeldin A-sensitivity protein 1;
DE AltName: Full=RING-type E3 ubiquitin transferase BRE1 {ECO:0000305};
GN Name=BRE1; OrderedLocusNames=YDL074C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP FUNCTION.
RX PubMed=12876294; DOI=10.1074/jbc.c300269200;
RA Wood A., Schneider J., Dover J., Johnston M., Shilatifard A.;
RT "The Paf1 complex is essential for histone monoubiquitination by the Rad6-
RT Bre1 complex, which signals for histone methylation by COMPASS and Dot1p.";
RL J. Biol. Chem. 278:34739-34742(2003).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, AND INTERACTION WITH LGE1.
RX PubMed=12535538; DOI=10.1016/s1097-2765(02)00826-2;
RA Hwang W.W., Venkatasubrahmanyam S., Ianculescu A.G., Tong A., Boone C.,
RA Madhani H.D.;
RT "A conserved RING finger protein required for histone H2B
RT monoubiquitination and cell size control.";
RL Mol. Cell 11:261-266(2003).
RN [5]
RP FUNCTION, AND MUTAGENESIS OF CYS-663 AND HIS-665.
RX PubMed=12535539; DOI=10.1016/s1097-2765(02)00802-x;
RA Wood A., Krogan N.J., Dover J., Schneider J., Heidt J., Boateng M.A.,
RA Dean K., Golshani A., Zhang Y., Greenblatt J.F., Johnston M.,
RA Shilatifard A.;
RT "Bre1, an E3 ubiquitin ligase required for recruitment and substrate
RT selection of Rad6 at a promoter.";
RL Mol. Cell 11:267-274(2003).
RN [6]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [7]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [8]
RP FUNCTION.
RX PubMed=15280549; DOI=10.1073/pnas.0400078101;
RA Yamashita K., Shinohara M., Shinohara A.;
RT "Rad6-Bre1-mediated histone H2B ubiquitylation modulates the formation of
RT double-strand breaks during meiosis.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:11380-11385(2004).
RN [9]
RP FUNCTION.
RX PubMed=15632065; DOI=10.1128/mcb.25.2.637-651.2005;
RA Xiao T., Kao C.-F., Krogan N.J., Sun Z.-W., Greenblatt J.F., Osley M.A.,
RA Strahl B.D.;
RT "Histone H2B ubiquitylation is associated with elongating RNA polymerase
RT II.";
RL Mol. Cell. Biol. 25:637-651(2005).
CC -!- FUNCTION: E3 ubiquitin-protein ligase that mediates monoubiquitination
CC of histone H2B to form H2BK123ub1 in association with the E2 enzyme
CC RAD6/UBC2. H2BK123ub1 gives a specific tag for epigenetic
CC transcriptional activation, elongation by RNA polymerase II, telomeric
CC silencing, and is also a prerequisite for H3K4me and H3K79me formation.
CC It thereby plays a central role in histone code and gene regulation.
CC Also modulates the formation of double-strand breaks during meiosis.
CC {ECO:0000269|PubMed:12535538, ECO:0000269|PubMed:12535539,
CC ECO:0000269|PubMed:12876294, ECO:0000269|PubMed:15280549,
CC ECO:0000269|PubMed:15632065}.
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:0000269|PubMed:12535538};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Forms a complex with the E2 enzyme RAD6/UBC2. May interact
CC with LGE1.
CC -!- INTERACTION:
CC Q07457; Q07457: BRE1; NbExp=6; IntAct=EBI-31563, EBI-31563;
CC Q07457; P06104: RAD6; NbExp=4; IntAct=EBI-31563, EBI-19722;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 2980 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the BRE1 family. {ECO:0000305}.
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DR EMBL; Z74122; CAA98640.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11785.1; -; Genomic_DNA.
DR PIR; S67610; S67610.
DR RefSeq; NP_010209.1; NM_001180133.1.
DR PDB; 4R7E; X-ray; 2.25 A; A=632-700.
DR PDBsum; 4R7E; -.
DR AlphaFoldDB; Q07457; -.
DR SMR; Q07457; -.
DR BioGRID; 31987; 831.
DR ComplexPortal; CPX-2910; BRE1-RAD6 ubiquitin ligase complex.
DR ComplexPortal; CPX-2911; BRE1 E3 ubiquitin-protein ligase complex.
DR DIP; DIP-2999N; -.
DR IntAct; Q07457; 73.
DR MINT; Q07457; -.
DR STRING; 4932.YDL074C; -.
DR iPTMnet; Q07457; -.
DR MaxQB; Q07457; -.
DR PaxDb; Q07457; -.
DR PRIDE; Q07457; -.
DR EnsemblFungi; YDL074C_mRNA; YDL074C; YDL074C.
DR GeneID; 851485; -.
DR KEGG; sce:YDL074C; -.
DR SGD; S000002232; BRE1.
DR VEuPathDB; FungiDB:YDL074C; -.
DR eggNOG; KOG0978; Eukaryota.
DR GeneTree; ENSGT00390000002866; -.
DR HOGENOM; CLU_019713_1_0_1; -.
DR InParanoid; Q07457; -.
DR OMA; GAIYRQM; -.
DR BioCyc; YEAST:G3O-29485-MON; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q07457; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q07457; protein.
DR GO; GO:1990302; C:Bre1-Rad6 ubiquitin ligase complex; IPI:ComplexPortal.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:GOC.
DR GO; GO:0033503; C:HULC complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003688; F:DNA replication origin binding; IDA:SGD.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:SGD.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IDA:ComplexPortal.
DR GO; GO:0071894; P:histone H2B conserved C-terminal lysine ubiquitination; IBA:GO_Central.
DR GO; GO:0010390; P:histone monoubiquitination; IDA:ComplexPortal.
DR GO; GO:0016574; P:histone ubiquitination; IDA:ComplexPortal.
DR GO; GO:0042138; P:meiotic DNA double-strand break formation; IMP:SGD.
DR GO; GO:0031571; P:mitotic G1 DNA damage checkpoint signaling; IMP:SGD.
DR GO; GO:0031573; P:mitotic intra-S DNA damage checkpoint signaling; IMP:SGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IC:ComplexPortal.
DR GO; GO:0070534; P:protein K63-linked ubiquitination; IMP:SGD.
DR GO; GO:0030174; P:regulation of DNA-templated DNA replication initiation; IMP:SGD.
DR GO; GO:0040029; P:regulation of gene expression, epigenetic; IC:ComplexPortal.
DR GO; GO:0031509; P:subtelomeric heterochromatin assembly; IMP:SGD.
DR GO; GO:0000722; P:telomere maintenance via recombination; IGI:SGD.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IGI:SGD.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR013956; E3_ubiquit_lig_Bre1.
DR InterPro; IPR013087; Znf_C2H2_type.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR23163; PTHR23163; 2.
DR SMART; SM00184; RING; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chromatin regulator; Coiled coil; Metal-binding; Nucleus;
KW Reference proteome; Transferase; Ubl conjugation pathway; Zinc;
KW Zinc-finger.
FT CHAIN 1..700
FT /note="E3 ubiquitin-protein ligase BRE1"
FT /id="PRO_0000055857"
FT ZN_FING 648..687
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 200..250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 126..406
FT /evidence="ECO:0000255"
FT COILED 555..620
FT /evidence="ECO:0000255"
FT COMPBIAS 214..228
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 229..250
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 663
FT /note="C->A: Abolishes ability to monoubiquitinate histone
FT H2B."
FT /evidence="ECO:0000269|PubMed:12535539"
FT MUTAGEN 665
FT /note="H->A: Abolishes ability to monoubiquitinate histone
FT H2B."
FT /evidence="ECO:0000269|PubMed:12535539"
FT HELIX 633..646
FT /evidence="ECO:0007829|PDB:4R7E"
FT TURN 649..651
FT /evidence="ECO:0007829|PDB:4R7E"
FT STRAND 652..655
FT /evidence="ECO:0007829|PDB:4R7E"
FT STRAND 658..660
FT /evidence="ECO:0007829|PDB:4R7E"
FT TURN 661..663
FT /evidence="ECO:0007829|PDB:4R7E"
FT HELIX 669..677
FT /evidence="ECO:0007829|PDB:4R7E"
FT TURN 684..686
FT /evidence="ECO:0007829|PDB:4R7E"
FT HELIX 692..694
FT /evidence="ECO:0007829|PDB:4R7E"
FT STRAND 695..697
FT /evidence="ECO:0007829|PDB:4R7E"
SQ SEQUENCE 700 AA; 80692 MW; FC6B32825970D36F CRC64;
MTAEPATKKI KLELSDPSEP LTQSDVIAFQ KEALFRCINR RRVDFEALRK QYELSRRECI
DVSRKLANIM ALIVTLARFI ETFCTDANEK QLCREIAQGD ETLIVQRSDS FMKLLTKYGK
PNTTDSNTNS NASDHIQELT TELKNLRKSK EELFYENSQL TEEISALKEY YTNIIRKYDR
DESFTIKRVF KEDKTDAVKE LREDEKESNE NNIKSGNKDS SAINGDNTSK KSEKGDELVQ
AEDERKEDAE NEKLELDLKF SDLRAEINSL SSTIKDLENI RRENEEELIK TRSEVSNLKK
QQIAAADQDP DFKSYDHESL LAKIQHLTEQ NAELSEINSS FLSKFQVLAK EKEIYTKKVR
EEFQKSLDSL VEMNSSLEKD VVRIRTARDD LLSKIAILEA EKSKTEVLSD LQHAIDILKE
QWTKIDQRSN DTKSSSTQDA LIKEIQDLEK GFRELSDLTH KKYSEIINHE SVISKLTVEK
TKADQKYFAA MRSKDSILIE IKTLSKSLSK SNELILQLKD SDRLLQQKIG NLHKQLDLSQ
NNERRLIDSS KTETLKIIDL NNTSTKLKRS LEKLQEESNK SIADMTHLET KLNDTEIELK
HFKQKASHLE SKCEKLHDTL FRGNNKNKGS SDEALVEELA NFRTLVYCSL CSKNWKNMAI
KTCGHVFCEN CCKERLAARM RKCPTCNKAF SSNDLLTVHL
