BRE1_CAEBR
ID BRE1_CAEBR Reviewed; 828 AA.
AC Q60YN5; A8XT60;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 103.
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 {ECO:0000250|UniProtKB:P34537}; Synonyms=bre-1;
GN ORFNames=CBG18162;
OS Caenorhabditis briggsae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6238;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16;
RX PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA Durbin R.M., Waterston R.H.;
RT "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT genomics.";
RL PLoS Biol. 1:166-192(2003).
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 (By similarity). {ECO:0000250|UniProtKB:O75150,
CC ECO:0000250|UniProtKB:P34537}.
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 (By similarity). Interacts with mrg-1 (By
CC similarity). {ECO:0000250|UniProtKB:P34537}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P34537}.
CC -!- SIMILARITY: Belongs to the BRE1 family. {ECO:0000305}.
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DR EMBL; HE600963; CAP35663.3; -; Genomic_DNA.
DR RefSeq; XP_002642194.1; XM_002642148.1.
DR AlphaFoldDB; Q60YN5; -.
DR SMR; Q60YN5; -.
DR STRING; 6238.CBG18162; -.
DR PRIDE; Q60YN5; -.
DR EnsemblMetazoa; CBG18162.1; CBG18162.1; WBGene00037633.
DR GeneID; 8584190; -.
DR KEGG; cbr:CBG_18162; -.
DR CTD; 8584190; -.
DR WormBase; CBG18162; CBP19234; WBGene00037633; Cbr-rfp-1.
DR eggNOG; KOG0978; Eukaryota.
DR HOGENOM; CLU_387448_0_0_1; -.
DR InParanoid; Q60YN5; -.
DR OMA; GAIYRQM; -.
DR OrthoDB; 782448at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000008549; Chromosome III.
DR GO; GO:0033503; C:HULC complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0031624; F:ubiquitin conjugating enzyme binding; IEA:EnsemblMetazoa.
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; IEA:EnsemblMetazoa.
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 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..828
FT /note="E3 ubiquitin-protein ligase bre-1"
FT /id="PRO_0000055844"
FT ZN_FING 776..815
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 1..309
FT /note="Interaction with ubc-1"
FT /evidence="ECO:0000250|UniProtKB:P34537"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 269..304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 53..92
FT /evidence="ECO:0000255"
FT COILED 185..251
FT /evidence="ECO:0000255"
FT COILED 311..345
FT /evidence="ECO:0000255"
FT COILED 460..616
FT /evidence="ECO:0000255"
FT COILED 660..756
FT /evidence="ECO:0000255"
FT COMPBIAS 270..300
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 828 AA; 96506 MW; 9D0ADE82EF79839C CRC64;
MMKRNNEGIG GEGVANSPPD DTQQKRRRIQ FEAVKMPAVQ SVTELRSRTV AIQAAKLRQT
VLIKNKRISD LERENERAKR RQLTDESNFL KVYNLFSELE KFIWAQTKDE FGEVKMTPSA
PAGTDVQGMT SEQYHSFVDT AKGNLRIAFN SYAKARHDRT TETANFIARL KTLMADPKLN
INDIHKELAA KTASLLAQID KLQAEAHRVQ SENHNLERKR RHMVDKNTLL ESRIQEMEKL
LEEAHFETEK QMRLACKYEA RLILEHEAAS GNATASSSAT LNQSEKKMGS PGSPPSESTS
REIEALRADR DEQAAIAARR LQELEDTNRK LQSMAQDISK LKMETQSSVP SDVITNSEEY
RNLKKYYSLA IKEHERICKD LEDVTVERDQ LRSVKENREK MMSEEHQKTI KEIQHQSEIH
NTFYRVSHDS EVLRAEFETV KEEYNKTVKQ SEWDEMKATV NTLRSLNKTM KSQMQRMKDR
EKASQKEHSA VKTELKTLKD QLEKSVLVPL EDSGNTSTED ANKIRAEYES LKREIRRIGA
MDKQEKQRQL DREIQRHIAD KVTELETLRK TNEALTNDEQ TLSDELEVVC LTIEEEQERN
AQLFMEKRDQ EDRNLKMMNE RMIQNQVQSR MREKLECLES KAQTDAQIAK MHEFEKKASD
EVLNKLTENL QFKTSEVTRL SNMMEVHRKQ TQELGFARDE NQVKVDRCEA QLKQYQDLYG
SKSREVEEAK FKRQRAEEEL ELVRVKYERA KRNDSAQTGD QVLQEANRQM KETLTCPSCK
TRPKDCIMLK CYHLFCETCI KTMYDTRQRK CPKCNSNFGA NDFHRIFI
