BRE1_CAEEL
ID BRE1_CAEEL Reviewed; 837 AA.
AC P34537; Q65ZS6;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 2.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=E3 ubiquitin-protein ligase bre-1;
DE EC=2.3.2.27 {ECO:0000250|UniProtKB:O75150};
DE AltName: Full=RING finger protein rfp-1;
DE AltName: Full=RING-type E3 ubiquitin transferase bre-1 {ECO:0000305};
GN Name=rfp-1; Synonyms=bre-1; ORFNames=R05D3.4;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), INTERACTION WITH UBC-1,
RP DEVELOPMENTAL STAGE, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=14732404; DOI=10.1016/j.ydbio.2003.09.037;
RA Crowe E., Candido E.P.M.;
RT "Characterization of C. elegans RING finger protein 1, a binding partner of
RT ubiquitin-conjugating enzyme 1.";
RL Dev. Biol. 265:446-459(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=7906398; DOI=10.1038/368032a0;
RA Wilson R., Ainscough R., Anderson K., Baynes C., Berks M., Bonfield J.,
RA Burton J., Connell M., Copsey T., Cooper J., Coulson A., Craxton M.,
RA Dear S., Du Z., Durbin R., Favello A., Fraser A., Fulton L., Gardner A.,
RA Green P., Hawkins T., Hillier L., Jier M., Johnston L., Jones M.,
RA Kershaw J., Kirsten J., Laisster N., Latreille P., Lightning J., Lloyd C.,
RA Mortimore B., O'Callaghan M., Parsons J., Percy C., Rifken L., Roopra A.,
RA Saunders D., Shownkeen R., Sims M., Smaldon N., Smith A., Smith M.,
RA Sonnhammer E., Staden R., Sulston J., Thierry-Mieg J., Thomas K.,
RA Vaudin M., Vaughan K., Waterston R., Watson A., Weinstock L.,
RA Wilkinson-Sproat J., Wohldman P.;
RT "2.2 Mb of contiguous nucleotide sequence from chromosome III of C.
RT elegans.";
RL Nature 368:32-38(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [4] {ECO:0000305}
RP FUNCTION, INTERACTION WITH MRG-1, AND DISRUPTION PHENOTYPE.
RX PubMed=25564623; DOI=10.1242/dev.115147;
RA Gupta P., Leahul L., Wang X., Wang C., Bakos B., Jasper K., Hansen D.;
RT "Proteasome regulation of the chromodomain protein MRG-1 controls the
RT balance between proliferative fate and differentiation in the C. elegans
RT germ line.";
RL Development 142:291-302(2015).
CC -!- FUNCTION: E3 ubiquitin-protein ligase that mediates monoubiquitination
CC of 'Lys-117' of histone H2B (By similarity). H2B 'Lys-117'
CC ubiquitination gives a specific tag for epigenetic transcriptional
CC activation and is also prerequisite for histone H3 'Lys-4' and 'Lys-79'
CC methylation (By similarity). Involved in regulating stem cell
CC proliferative fate (PubMed:25564623). {ECO:0000250|UniProtKB:O75150,
CC ECO:0000269|PubMed:25564623}.
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 -!- SUBUNIT: Interacts with ubc-1 (PubMed:14732404). Interacts with mrg-1
CC (PubMed:25564623). {ECO:0000269|PubMed:14732404,
CC ECO:0000269|PubMed:25564623}.
CC -!- INTERACTION:
CC P34537; P52478: ubc-1; NbExp=7; IntAct=EBI-316712, EBI-316677;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14732404}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=b;
CC IsoId=P34537-1; Sequence=Displayed;
CC Name=a;
CC IsoId=P34537-2; Sequence=VSP_016614;
CC -!- TISSUE SPECIFICITY: In adult animals, expressed in oocytes, germ cells,
CC pharyngeal and intestinal cells. {ECO:0000269|PubMed:14732404}.
CC -!- DEVELOPMENTAL STAGE: Expressed at all life stages.
CC {ECO:0000269|PubMed:14732404}.
CC -!- DISRUPTION PHENOTYPE: Worms arrest their development at L1 stage, and
CC show tail abnormalities (PubMed:14732404). RNAi-mediated knockdown on a
CC glp-1 mutant background causes significant overproliferation of
CC germline cells (PubMed:25564623). {ECO:0000269|PubMed:14732404,
CC ECO:0000269|PubMed:25564623}.
CC -!- SIMILARITY: Belongs to the BRE1 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FO081667; CCD73190.1; -; Genomic_DNA.
DR EMBL; FO081667; CCD73191.1; -; Genomic_DNA.
DR PIR; S44866; S44866.
DR RefSeq; NP_001022699.1; NM_001027528.3. [P34537-2]
DR RefSeq; NP_001022700.1; NM_001027529.3. [P34537-1]
DR AlphaFoldDB; P34537; -.
DR SMR; P34537; -.
DR BioGRID; 41384; 12.
DR DIP; DIP-24823N; -.
DR IntAct; P34537; 3.
DR MINT; P34537; -.
DR STRING; 6239.R05D3.4b; -.
DR iPTMnet; P34537; -.
DR EPD; P34537; -.
DR PaxDb; P34537; -.
DR PeptideAtlas; P34537; -.
DR PRIDE; P34537; -.
DR EnsemblMetazoa; R05D3.4a.1; R05D3.4a.1; WBGene00007008. [P34537-2]
DR EnsemblMetazoa; R05D3.4b.1; R05D3.4b.1; WBGene00007008. [P34537-1]
DR GeneID; 176180; -.
DR KEGG; cel:CELE_R05D3.4; -.
DR UCSC; R05D3.4b; c. elegans. [P34537-1]
DR CTD; 176180; -.
DR WormBase; R05D3.4a; CE00283; WBGene00007008; rfp-1. [P34537-2]
DR WormBase; R05D3.4b; CE37396; WBGene00007008; rfp-1. [P34537-1]
DR eggNOG; KOG0978; Eukaryota.
DR GeneTree; ENSGT00390000002866; -.
DR HOGENOM; CLU_387448_0_0_1; -.
DR InParanoid; P34537; -.
DR OMA; GAIYRQM; -.
DR OrthoDB; 782448at2759; -.
DR PhylomeDB; P34537; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:P34537; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00007008; Expressed in embryo and 4 other tissues.
DR GO; GO:0033503; C:HULC complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0031624; F:ubiquitin conjugating enzyme binding; IPI:WormBase.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0006664; P:glycolipid metabolic process; IMP:UniProtKB.
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 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 InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR23163; PTHR23163; 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 Alternative splicing; Chromatin regulator; Coiled coil; Metal-binding;
KW Nucleus; Reference proteome; Transferase; Ubl conjugation pathway; Zinc;
KW Zinc-finger.
FT CHAIN 1..837
FT /note="E3 ubiquitin-protein ligase bre-1"
FT /id="PRO_0000055845"
FT ZN_FING 785..824
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 1..313
FT /note="Interaction with ubc-1"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 269..302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 54..89
FT /evidence="ECO:0000255"
FT COILED 185..253
FT /evidence="ECO:0000255"
FT COILED 300..397
FT /evidence="ECO:0000255"
FT COILED 458..651
FT /evidence="ECO:0000255"
FT COILED 677..763
FT /evidence="ECO:0000255"
FT COMPBIAS 269..291
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 556..558
FT /note="Missing (in isoform a)"
FT /evidence="ECO:0000303|PubMed:14732404"
FT /id="VSP_016614"
SQ SEQUENCE 837 AA; 97444 MW; 6654DC4EB6A8E86A CRC64;
MMKRSNEGIG GENYASSPSD DGQQKRRKIQ FEPVRMPAVS NVNDIRARAV VYQTSKLKQQ
LLYKNKRIAE LEKENERSKR RQQTDESNFL KVYNMFSDIE KYICTQTKNE FGEYIGGDTA
PTGIDVLGMT NETYNKFFDQ AKQNLRNAFV SYAKARHDRA HESTIFIDKL KTLIDSPTFN
PNGVHKELTA KAASLAIQNE KLQSEVTKVQ SDCYNLERKK RILTDKLSVQ ENRVQELEHQ
LEDARFETDK HMRLANKFEY KLATLVSEGQ SGGNGGATPS SSGTTNATEK KISAPDIPPS
ETAAKEIENL RLERDEQESI ASRRLQDLEE MNKKVQTLTQ ENSKLRLETQ TFFSVDSIVN
SEEYKNLKKY YSLAIKEYER VSKDLEDITT ERDAFRSAKE ARAMLMSEEH QKTLKEIQCQ
SDIHNSFYKV SHDSEVLRCE FETVKEEYNK TVKQSEWDEM KATLNTLRSM NRSLKSEKIR
LREKDKQSQK DINTLKSELT SLKEAQDKCL LVPLEDVSNA PPEDVNKIRQ EYESLCKEVK
RLGAMEKQEK QKQVENLQKE VNRQIADKLS ELETLRKTNE MLTNDEECIS DELEAIGTAV
EEEQERNAQL YIEKREQEDR NLKMMNDRMI QNQTFNRLRE KLSCLESKAQ TDAQIAKMHE
FEKKANEELV TKLSESVQFK SAELTRLTNL MEQHRKNIQE VGMSRDENQI KADRCEGQMK
QIQELYAAKA REIEDFKFKR QRAEEELETL RIKYERVKRN ESVPAQSGDQ VLEEANRQMK
ETLTCPSCKT RPKDCIMLKC YHLFCETCIK TMYDTRQRKC PKCNSNFGAN DFHRIFI
