BRE1_KLULA
ID BRE1_KLULA Reviewed; 663 AA.
AC Q6CWM4;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=E3 ubiquitin-protein ligase BRE1;
DE EC=2.3.2.27 {ECO:0000250|UniProtKB:Q07457};
DE AltName: Full=RING-type E3 ubiquitin transferase BRE1 {ECO:0000305};
GN Name=BRE1; OrderedLocusNames=KLLA0B02981g;
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
CC -!- FUNCTION: E3 ubiquitin-protein ligase that mediates monoubiquitination
CC of histone H2B to form H2BK123ub1. H2BK123ub1 gives a specific tag for
CC epigenetic transcriptional activation and is also a prerequisite for
CC H3K4me and H3K79me formation. {ECO:0000250|UniProtKB:Q07457}.
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:Q07457};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q07457}.
CC -!- SIMILARITY: Belongs to the BRE1 family. {ECO:0000305}.
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DR EMBL; CR382122; CAH02058.1; -; Genomic_DNA.
DR RefSeq; XP_451665.1; XM_451665.1.
DR AlphaFoldDB; Q6CWM4; -.
DR SMR; Q6CWM4; -.
DR STRING; 28985.XP_451665.1; -.
DR EnsemblFungi; CAH02058; CAH02058; KLLA0_B02981g.
DR GeneID; 2897020; -.
DR KEGG; kla:KLLA0_B02981g; -.
DR eggNOG; KOG0978; Eukaryota.
DR HOGENOM; CLU_019713_1_0_1; -.
DR InParanoid; Q6CWM4; -.
DR OMA; DVVYFQK; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000000598; Chromosome B.
DR GO; GO:1990302; C:Bre1-Rad6 ubiquitin ligase complex; IEA:EnsemblFungi.
DR GO; GO:0000785; C:chromatin; IEA:EnsemblFungi.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:GOC.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003688; F:DNA replication origin binding; IEA:EnsemblFungi.
DR GO; GO:0042802; F:identical protein binding; IEA:EnsemblFungi.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:EnsemblFungi.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IEA:EnsemblFungi.
DR GO; GO:0010390; P:histone monoubiquitination; IEA:EnsemblFungi.
DR GO; GO:0042138; P:meiotic DNA double-strand break formation; IEA:EnsemblFungi.
DR GO; GO:0031571; P:mitotic G1 DNA damage checkpoint signaling; IEA:EnsemblFungi.
DR GO; GO:0031573; P:mitotic intra-S DNA damage checkpoint signaling; IEA:EnsemblFungi.
DR GO; GO:0070534; P:protein K63-linked ubiquitination; IEA:EnsemblFungi.
DR GO; GO:0030174; P:regulation of DNA-templated DNA replication initiation; IEA:EnsemblFungi.
DR GO; GO:0031509; P:subtelomeric heterochromatin assembly; IEA:EnsemblFungi.
DR GO; GO:0000722; P:telomere maintenance via recombination; IEA:EnsemblFungi.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IEA:EnsemblFungi.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR013956; E3_ubiquit_lig_Bre1.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR23163; PTHR23163; 1.
DR SMART; SM00184; RING; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Chromatin regulator; Coiled coil; Metal-binding; Nucleus;
KW Reference proteome; Transferase; Ubl conjugation pathway; Zinc;
KW Zinc-finger.
FT CHAIN 1..663
FT /note="E3 ubiquitin-protein ligase BRE1"
FT /id="PRO_0000055853"
FT ZN_FING 611..650
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 176..225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 273..293
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 133..172
FT /evidence="ECO:0000255"
FT COILED 225..424
FT /evidence="ECO:0000255"
FT COILED 463..588
FT /evidence="ECO:0000255"
FT COMPBIAS 194..222
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 663 AA; 75282 MW; 2B100CC475302FB6 CRC64;
MNDHFVKRPK LELSDPSEPL TQKDVIAFQK EALFRCLNKW RVKANQLVEE NEVLAAGLSK
TTESVSGCCS SIVVLARSVV EDCSDEQDKR FLQQLINTED EHTLTQIISN NSARICELIL
KTSGSNISDN IGRLQELESL TLTLQKLLKS SENKLKKATE YYENIIAQYD RQDSESVSRV
FNTADDDSNV KKEKQSSTGA SSVNDESNDN SDKSQSNKES AVSQAHHEIE INDLNTQISV
LEATVKELTE WKNQNERELS ELRQTVASNK SALSNNQLQS NSQHQPDASV TNEKISSLTK
QNEQLQQINE GYLTKFQQLS ADREIFNNKL TSEFNLAQET LKKHNASLEK DLVRIRTIRD
ELLAKVSLLE AQKTKSEMLE DLEKSLNIQQ EQLQKFESRS SENASQDALM KELQDLEKAF
REVSHLSNKK YAAYLNQESV LSKLTVEKTK ASEKYFAAMR SKDAIMIENK NLSKNLNKSN
ELIVQLKDLE KTLQQKIVNV HMQLSLSQEN EKRVKESNKE TSMKIVELTS ENNKLKKSTE
RLESETRNLI GTKTELESKI KDKDIENKQL KIKVSSAEAK SKKLYKTLLS NGGDNGALAE
ELENFRTIIY CSLCSKNWKN TALKTCGHVF CDVCCKERLA ARMRKCPTCN KPFSSNDLLS
IHL
