BRE1B_MOUSE
ID BRE1B_MOUSE Reviewed; 1001 AA.
AC Q3U319; Q6ZQ75; Q8BJA1; Q8BY03; Q8CHX4;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 2.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=E3 ubiquitin-protein ligase BRE1B;
DE Short=BRE1-B;
DE EC=2.3.2.27 {ECO:0000250|UniProtKB:O75150};
DE AltName: Full=RING finger protein 40;
DE AltName: Full=RING-type E3 ubiquitin transferase BRE1B {ECO:0000305};
GN Name=Rnf40; Synonyms=Bre1b, Kiaa0661;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryonic tail;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Cerebellum, and Spleen;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Salivary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-584 AND SER-585, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Liver, Lung, Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-20 AND LYS-517, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
CC -!- FUNCTION: Component of the RNF20/40 E3 ubiquitin-protein ligase complex
CC that mediates monoubiquitination of 'Lys-120' of histone H2B
CC (H2BK120ub1). H2BK120ub1 gives a specific tag for epigenetic
CC transcriptional activation and is also prerequisite for histone H3
CC 'Lys-4' and 'Lys-79' methylation (H3K4me and H3K79me, respectively). It
CC thereby plays a central role in histone code and gene regulation. The
CC RNF20/40 complex forms a H2B ubiquitin ligase complex in cooperation
CC with the E2 enzyme UBE2A or UBE2B; reports about the cooperation with
CC UBE2E1/UBCH are contradictory. Required for transcriptional activation
CC of Hox genes. {ECO:0000250|UniProtKB:O75150}.
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: Component of the RNF20/40 complex (also known as BRE1 complex)
CC probably composed of 2 copies of RNF20/BRE1A and 2 copies of
CC RNF40/BRE1B. Interacts with UBE2E1/UBCH6. Interacts with RB1 and WAC.
CC {ECO:0000250|UniProtKB:O75150}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O75150}.
CC -!- SIMILARITY: Belongs to the BRE1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC97994.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK129184; BAC97994.1; ALT_INIT; mRNA.
DR EMBL; AK042654; BAC31322.1; -; mRNA.
DR EMBL; AK089805; BAC40966.1; -; mRNA.
DR EMBL; AK154982; BAE32971.1; -; mRNA.
DR EMBL; AK171462; BAE42468.1; -; mRNA.
DR EMBL; BC038348; AAH38348.1; -; mRNA.
DR CCDS; CCDS21871.1; -.
DR RefSeq; NP_758485.2; NM_172281.2.
DR AlphaFoldDB; Q3U319; -.
DR SMR; Q3U319; -.
DR BioGRID; 231471; 9.
DR IntAct; Q3U319; 2.
DR MINT; Q3U319; -.
DR STRING; 10090.ENSMUSP00000033088; -.
DR iPTMnet; Q3U319; -.
DR PhosphoSitePlus; Q3U319; -.
DR EPD; Q3U319; -.
DR MaxQB; Q3U319; -.
DR PaxDb; Q3U319; -.
DR PeptideAtlas; Q3U319; -.
DR PRIDE; Q3U319; -.
DR ProteomicsDB; 273801; -.
DR Antibodypedia; 13809; 275 antibodies from 32 providers.
DR DNASU; 233900; -.
DR Ensembl; ENSMUST00000205694; ENSMUSP00000146310; ENSMUSG00000030816.
DR GeneID; 233900; -.
DR KEGG; mmu:233900; -.
DR UCSC; uc009jwe.2; mouse.
DR CTD; 9810; -.
DR MGI; MGI:2142048; Rnf40.
DR VEuPathDB; HostDB:ENSMUSG00000030816; -.
DR eggNOG; KOG0978; Eukaryota.
DR GeneTree; ENSGT00390000002866; -.
DR HOGENOM; CLU_002640_0_0_1; -.
DR InParanoid; Q3U319; -.
DR OMA; THIEIMT; -.
DR OrthoDB; 782448at2759; -.
DR PhylomeDB; Q3U319; -.
DR TreeFam; TF323183; -.
DR Reactome; R-MMU-8866654; E3 ubiquitin ligases ubiquitinate target proteins.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 233900; 31 hits in 79 CRISPR screens.
DR PRO; PR:Q3U319; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q3U319; protein.
DR Bgee; ENSMUSG00000030816; Expressed in granulocyte and 170 other tissues.
DR ExpressionAtlas; Q3U319; baseline and differential.
DR Genevisible; Q3U319; MM.
DR GO; GO:0043679; C:axon terminus; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0019898; C:extrinsic component of membrane; ISO:MGI.
DR GO; GO:0033503; C:HULC complex; ISS:UniProtKB.
DR GO; GO:0043005; C:neuron projection; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0000151; C:ubiquitin ligase complex; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0017075; F:syntaxin-1 binding; ISO:MGI.
DR GO; GO:0031624; F:ubiquitin conjugating enzyme binding; ISO:MGI.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; ISO:MGI.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0071894; P:histone H2B conserved C-terminal lysine ubiquitination; IBA:GO_Central.
DR GO; GO:0033523; P:histone H2B ubiquitination; ISO:MGI.
DR GO; GO:0010390; P:histone monoubiquitination; ISO:MGI.
DR GO; GO:1900364; P:negative regulation of mRNA polyadenylation; ISO:MGI.
DR GO; GO:2001168; P:positive regulation of histone H2B ubiquitination; ISO:MGI.
DR GO; GO:1901800; P:positive regulation of proteasomal protein catabolic process; ISO:MGI.
DR GO; GO:1902916; P:positive regulation of protein polyubiquitination; ISO:MGI.
DR GO; GO:0043434; P:response to peptide hormone; IEA:Ensembl.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; ISO:MGI.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR013956; E3_ubiquit_lig_Bre1.
DR InterPro; IPR018957; Znf_C3HC4_RING-type.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR23163; PTHR23163; 1.
DR Pfam; PF00097; zf-C3HC4; 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 Acetylation; Chromatin regulator; Coiled coil; Isopeptide bond;
KW Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Transferase;
KW Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..1001
FT /note="E3 ubiquitin-protein ligase BRE1B"
FT /id="PRO_0000055841"
FT ZN_FING 948..987
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 122..142
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 519..647
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 55..91
FT /evidence="ECO:0000255"
FT COILED 189..377
FT /evidence="ECO:0000255"
FT COILED 437..525
FT /evidence="ECO:0000255"
FT COILED 627..946
FT /evidence="ECO:0000255"
FT COMPBIAS 604..619
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 633..647
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 20
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 42
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5VTR2"
FT MOD_RES 355
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q5VTR2"
FT MOD_RES 517
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 584
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 585
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CROSSLNK 578
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O75150"
FT CROSSLNK 579
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O75150"
FT CONFLICT 385
FT /note="T -> A (in Ref. 2; BAE32971)"
FT /evidence="ECO:0000305"
FT CONFLICT 493
FT /note="H -> Y (in Ref. 3; AAH38348)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1001 AA; 113967 MW; F4368B7CA414BF01 CRC64;
MSGLSNKRAA GDGGSGPPEK KMNREEKTTT TLIEPIRLGG ISSTEEMDSK VLQFKNKKLA
ERLEQRQACE DELRERIEKL EKRQATDDAT LLIVNRYWAQ LDETVEALLQ CYENQRELSS
GTEVPGCQEG LTRDVIPRPD PGTSDLREPL PVQFRAPLSE PALAFVVALG ASSCEEVELQ
LQGRMEFSKA AVSRVVEASD RLQRQVEELC QRVYSRGDSE APGEVARVRT RELGRENRRL
QDLATQLQEK HHRISLEYSE LQDKVTSTET KVLEMETTVE DLQWDIEKLR KREQKLNKHL
AEALEQLNSG YYVSGSSTGF QGGQITLSMQ KFEMLNAELE ENQELANSRM AELEKLQAEL
QGAVRTNERL KVALRSLPEE VVRETGEYRM LQAQFSLLYN ESLQVKTQLD EARGLLLASK
NSHLRHIEHM ESDELGLQKK LRTEVIQLED TLAQVRKEYE MLRIEFEQNL AANEQAGPIN
REMRHLISSL QNHNHQLKGD AQRYKRKLRE VQAEIGKLRA QASGSSHCIP TLSHPDDPGL
NALAPGKEDS GPGPGGTPDC KKEMALLAGA TSATSSIKKE ELVSSEDDAQ ALTPVTQGLP
SRGREPEARP KRELREREGP SLGPPPAAST LSRADREKAK VEEAKRKESE LLKGLRAELK
KAQESQKEMK LLLDMYKSAP KEQRDKVQLM AAERKAKAEV DELRSRIREL EERDRRESKK
IADEDALRRI RQAEEQIEHL QRKLGATKQE EEALLSEMDV TGQAFEDMQE QNGRLLQQLR
EKDDANFKLM SERIKANQIH KLLREEKDEL GEQVLGLKSQ VDAQLLTVQK LEEKERALQG
SLGGVEKELT LRSQALELNK RKAVEAAQLA EDLKVQLEHV QTRLREIQPC LAESRAAREK
ESFNLKRAQE DISRLRRKLE KQRKVEVYAD ADEILQEEIK EYKARLTCPC CNTRKKDAVL
TKCFHVFCFE CVRGRYEARQ RKCPKCNAAF GAHDFHRVYI S
