BRE1A_MOUSE
ID BRE1A_MOUSE Reviewed; 973 AA.
AC Q5DTM8; A2AIR3; Q3UT10; Q3V350; Q7TT11; Q8BKA8; Q8BKN8; Q8BUF7; Q8BVU4;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 2.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=E3 ubiquitin-protein ligase BRE1A;
DE Short=BRE1-A;
DE EC=2.3.2.27 {ECO:0000250|UniProtKB:Q5VTR2};
DE AltName: Full=RING finger protein 20;
DE AltName: Full=RING-type E3 ubiquitin transferase BRE1A {ECO:0000305};
GN Name=Rnf20; Synonyms=Bre1a, Kiaa4116;
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=Fetal brain;
RA Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene. The
RT complete nucleotide sequences of mouse KIAA-homologous cDNAs identified by
RT screening of terminal sequences of cDNA clones randomly sampled from size-
RT fractionated libraries.";
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Olfactory epithelium;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-607 (ISOFORM 1), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 1-616 (ISOFORM 2).
RC STRAIN=C57BL/6J;
RC TISSUE=Cerebellum, Egg, Eye, Head, Kidney, and Spinal ganglion;
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-136 AND SER-138, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC 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).
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. Recruited to the MDM2 promoter, probably by being
CC recruited by p53/TP53, and thereby acts as a transcriptional
CC coactivator. Mediates the polyubiquitination of PA2G4 leading to its
CC proteasome-mediated degradation. {ECO:0000250|UniProtKB:Q5VTR2}.
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:Q5VTR2};
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 p53/TP53 and
CC WAC. Interacts with PAF1; the interaction mediates the association of
CC the PAF1 and RNF20/40 complexes which is a prerequsite for recruitment
CC of UBE2A/B. Interacts with PA2G4. {ECO:0000250|UniProtKB:Q5VTR2}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q5VTR2}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q5DTM8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5DTM8-2; Sequence=VSP_016679;
CC -!- SIMILARITY: Belongs to the BRE1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD90290.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK220492; BAD90290.1; ALT_INIT; mRNA.
DR EMBL; AL732521; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC052482; AAH52482.1; -; mRNA.
DR EMBL; AK048862; BAE43337.1; -; mRNA.
DR EMBL; AK051278; BAC34590.2; -; mRNA.
DR EMBL; AK053783; BAC35521.1; -; mRNA.
DR EMBL; AK076501; BAC36367.1; -; mRNA.
DR EMBL; AK085436; BAC39446.1; -; mRNA.
DR EMBL; AK139883; BAE24170.1; -; mRNA.
DR CCDS; CCDS18178.1; -. [Q5DTM8-1]
DR RefSeq; NP_001156735.1; NM_001163263.1. [Q5DTM8-1]
DR RefSeq; NP_892044.1; NM_182999.2. [Q5DTM8-1]
DR RefSeq; XP_006537616.1; XM_006537553.3. [Q5DTM8-1]
DR RefSeq; XP_011248208.1; XM_011249906.2. [Q5DTM8-1]
DR AlphaFoldDB; Q5DTM8; -.
DR SMR; Q5DTM8; -.
DR BioGRID; 224649; 17.
DR IntAct; Q5DTM8; 1.
DR MINT; Q5DTM8; -.
DR STRING; 10090.ENSMUSP00000029989; -.
DR iPTMnet; Q5DTM8; -.
DR PhosphoSitePlus; Q5DTM8; -.
DR EPD; Q5DTM8; -.
DR jPOST; Q5DTM8; -.
DR MaxQB; Q5DTM8; -.
DR PaxDb; Q5DTM8; -.
DR PeptideAtlas; Q5DTM8; -.
DR PRIDE; Q5DTM8; -.
DR ProteomicsDB; 265379; -. [Q5DTM8-1]
DR ProteomicsDB; 265380; -. [Q5DTM8-2]
DR Antibodypedia; 29174; 352 antibodies from 32 providers.
DR DNASU; 109331; -.
DR Ensembl; ENSMUST00000029989; ENSMUSP00000029989; ENSMUSG00000028309. [Q5DTM8-1]
DR Ensembl; ENSMUST00000167496; ENSMUSP00000128546; ENSMUSG00000028309. [Q5DTM8-1]
DR GeneID; 109331; -.
DR KEGG; mmu:109331; -.
DR UCSC; uc008swa.2; mouse. [Q5DTM8-1]
DR UCSC; uc012dec.1; mouse. [Q5DTM8-2]
DR CTD; 56254; -.
DR MGI; MGI:1925927; Rnf20.
DR VEuPathDB; HostDB:ENSMUSG00000028309; -.
DR eggNOG; KOG0978; Eukaryota.
DR GeneTree; ENSGT00390000002866; -.
DR HOGENOM; CLU_002640_0_0_1; -.
DR InParanoid; Q5DTM8; -.
DR OMA; DENTSCT; -.
DR OrthoDB; 782448at2759; -.
DR PhylomeDB; Q5DTM8; -.
DR TreeFam; TF323183; -.
DR Reactome; R-MMU-8866654; E3 ubiquitin ligases ubiquitinate target proteins.
DR Reactome; R-MMU-9013422; RHOBTB1 GTPase cycle.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 109331; 31 hits in 81 CRISPR screens.
DR ChiTaRS; Rnf20; mouse.
DR PRO; PR:Q5DTM8; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q5DTM8; protein.
DR Bgee; ENSMUSG00000028309; Expressed in embryonic post-anal tail and 250 other tissues.
DR ExpressionAtlas; Q5DTM8; baseline and differential.
DR Genevisible; Q5DTM8; MM.
DR GO; GO:0033503; C:HULC complex; ISS:UniProtKB.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0000151; C:ubiquitin ligase complex; ISO:MGI.
DR GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR GO; GO:0042393; F:histone binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; 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:0002039; F:p53 binding; ISO:MGI.
DR GO; GO:0003713; F:transcription coactivator activity; 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:0016574; P:histone ubiquitination; IMP:MGI.
DR GO; GO:0030336; P:negative regulation of cell migration; 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:0031062; P:positive regulation of histone methylation; IMP:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0000209; P:protein polyubiquitination; ISO:MGI.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISO:MGI.
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; Alternative splicing; Chromatin regulator; Coiled coil;
KW Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Transferase;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..973
FT /note="E3 ubiquitin-protein ligase BRE1A"
FT /id="PRO_0000055837"
FT ZN_FING 920..959
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 128..153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 507..620
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 43..90
FT /evidence="ECO:0000255"
FT COILED 168..378
FT /evidence="ECO:0000255"
FT COILED 429..896
FT /evidence="ECO:0000255"
FT COMPBIAS 128..152
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 510..527
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 528..544
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 552..620
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 21
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q3U319"
FT MOD_RES 41
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5VTR2"
FT MOD_RES 136
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 138
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 348
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q5VTR2"
FT MOD_RES 510
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q3U319"
FT MOD_RES 522
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5VTR2"
FT MOD_RES 560
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3U319"
FT VAR_SEQ 100..249
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_016679"
FT CONFLICT 199
FT /note="V -> L (in Ref. 4; BAC36367)"
FT /evidence="ECO:0000305"
FT CONFLICT 506
FT /note="S -> F (in Ref. 4; BAC36367)"
FT /evidence="ECO:0000305"
FT CONFLICT 540
FT /note="S -> F (in Ref. 4; BAC36367)"
FT /evidence="ECO:0000305"
FT CONFLICT 607
FT /note="D -> G (in Ref. 4; BAE43337)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 973 AA; 113520 MW; 6A89582C7ECD556C CRC64;
MSGIGNKRAA GEPGTSMPPE KKTAVEDSGT TVETIKLGGV SSTEELDIRT LQSKNRKLAE
MLDQRQAIED ELREHIEKLE RRQATDDASL LIVNRYWSQF DENIRIILKR YDLDQGLGDL
LTERKALVVP EPEPDSDSNQ ERKDDRERGD GQEPAFSFLA TLASSSSEEM ESQLQERVES
SRRAVSQIVT VYDKLQEKVD LLSRKLNSGD NLIVEEAVQE LNSFLAQENV RLQELTDLLQ
EKHHTMSQEF CKLQGKVETA ESRVSVLESM IDDLQWDIDK IRKREQRLNR HLAEVLERVN
SKGYKVYGAG SSLYGGTITI NARKFEEMNA ELEENKELAQ NRHCELEKLR QDFEEVTTQN
EKLKVELRSA VEEVVKETPE YRCMQSQFSV LYNESLQLKA HLDEARTLLH GTRGTHQRQV
ELIERDEVSL HKKLRTEVIQ LEDTLAQVRK EYEMLRIEFE QTLAANEQAG PINREMRHLI
SSLQNHNHQL KGEVLRYKRK LREAQSDLNK TRLRSGSALL QSQSSTEDPK DEPTELKQDS
EDLATHSSAL KASQEDEVKS KRDEEERERE RREKERERER EREKEKERER EKQKLKESEK
ERDSVKDKEK GKHDDGRKKE AEIIKQLKIE LKKAQESQKE MKLLLDMYRS APKEQRDKVQ
LMAAEKKSKA ELEDLRQRLK DLEDKEKKEN KKMADEDALR KIRAVEEQIE YLQKKLAMAK
QEEEALLSEM DVTGQAFEDM QEQNIRLMQQ LREKDDANFK LMSERIKSNQ IHKLLKEEKE
ELADQVLTLK TQVDAQLQVV RKLEEKEHLL QSNIGTGEKE LGLRTQALEM NKRKAMEAAQ
LADDLKAQLE LAQKKLHDFQ DEIVENSVTK EKDLFNFKRA QEDISRLRRK LETTKKPDNV
PKCDEILMEE IKDYKARLTC PCCNMRKKDA VLTKCFHVFC FECVKTRYDT RQRKCPKCNA
AFGANDFHRI YIG
