BRE1_ASHGO
ID BRE1_ASHGO Reviewed; 643 AA.
AC Q757D9;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 121.
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=AER074W;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(2013).
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; AE016818; AAS52758.1; -; Genomic_DNA.
DR RefSeq; NP_984934.1; NM_210288.1.
DR AlphaFoldDB; Q757D9; -.
DR SMR; Q757D9; -.
DR STRING; 33169.AAS52758; -.
DR PRIDE; Q757D9; -.
DR EnsemblFungi; AAS52758; AAS52758; AGOS_AER074W.
DR GeneID; 4621137; -.
DR KEGG; ago:AGOS_AER074W; -.
DR eggNOG; KOG0978; Eukaryota.
DR HOGENOM; CLU_019713_1_0_1; -.
DR InParanoid; Q757D9; -.
DR OMA; GAIYRQM; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000000591; Chromosome V.
DR GO; GO:1990302; C:Bre1-Rad6 ubiquitin ligase complex; IEA:EnsemblFungi.
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; 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; IBA:GO_Central.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IEA:EnsemblFungi.
DR GO; GO:0071894; P:histone H2B conserved C-terminal lysine ubiquitination; IBA:GO_Central.
DR GO; GO:0010390; P:histone monoubiquitination; IBA:GO_Central.
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; 2.
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..643
FT /note="E3 ubiquitin-protein ligase BRE1"
FT /id="PRO_0000055847"
FT ZN_FING 591..630
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 173..200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 246..267
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 200..233
FT /evidence="ECO:0000255"
FT COILED 262..406
FT /evidence="ECO:0000255"
FT COILED 446..494
FT /evidence="ECO:0000255"
FT COILED 520..555
FT /evidence="ECO:0000255"
SQ SEQUENCE 643 AA; 72130 MW; 4A26E7EA0123C4D9 CRC64;
MEEPAAKRPK LSDRSEPLTQ RDVVLFQKEA LFRQLNRYRA EARAGQVQVE ELRRAHGQVG
ERLAAVCGVV RSVARAVADA RGDGDARALC ERVAGGDDDE VVARAAEFAA VVAGGLGRGA
AAGEGWHRLE AVNSRLAAEN AQLAAELGAV RGFYAELLRR YDRDESETVR RVFKVEESEP
PRAATPVEES SAKGAASDGE AATAVVEREM QIEELQTEIR VLEDTVAQLT DWKRLNEQEL
TKLRQMASSA ELSQRHPTPP SSSNLSADLQ VLRSKVEKLS HENKELAQLN EAYLGKFQQL
SADREIFNNR LSAEFQTAQE TLKKHNSNLE KDLVRIRTAR DELLSKVAVL EAQKSKSDML
EDLEKMLALQ QEQLKALSEH KPEPARDAVM KELQDLEKAF KELSQYSNKK YSEYVNQESL
MSKLTVEKTK ADQKYFAAMR SKDSILIENK NLSKNLSKSN ELIQQLKDIE KSLQAKIENL
NKQLHISRIN EKRLLDSNKT TSLKIMDLTS QLSKANKSST LVQQECNKLI EEKAKMESKL
NDLEIETKNL ATKLTYQENK SKKLHKTLVS NGGDNGALAE ELENFRTVVY CSLCSKNWKD
TVIKTCGHVF CADCCKERLA ARMRKCPTCN KGFSSNDLLV VHL
