BRE1A_BOVIN
ID BRE1A_BOVIN Reviewed; 975 AA.
AC A2VDP1;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 105.
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;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Basal ganglia;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
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 -!- SIMILARITY: Belongs to the BRE1 family. {ECO:0000305}.
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DR EMBL; BC133334; AAI33335.1; -; mRNA.
DR RefSeq; NP_001075056.1; NM_001081587.1.
DR RefSeq; XP_010806508.1; XM_010808206.2.
DR RefSeq; XP_010806510.1; XM_010808208.2.
DR AlphaFoldDB; A2VDP1; -.
DR SMR; A2VDP1; -.
DR STRING; 9913.ENSBTAP00000012521; -.
DR PaxDb; A2VDP1; -.
DR PRIDE; A2VDP1; -.
DR Ensembl; ENSBTAT00000012521; ENSBTAP00000012521; ENSBTAG00000009516.
DR GeneID; 513326; -.
DR KEGG; bta:513326; -.
DR CTD; 56254; -.
DR VEuPathDB; HostDB:ENSBTAG00000009516; -.
DR VGNC; VGNC:34047; RNF20.
DR eggNOG; KOG0978; Eukaryota.
DR GeneTree; ENSGT00390000002866; -.
DR HOGENOM; CLU_002640_0_0_1; -.
DR InParanoid; A2VDP1; -.
DR OMA; DENTSCT; -.
DR OrthoDB; 782448at2759; -.
DR TreeFam; TF323183; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000009136; Chromosome 8.
DR Bgee; ENSBTAG00000009516; Expressed in thymus and 104 other tissues.
DR GO; GO:0033503; C:HULC complex; ISS:UniProtKB.
DR GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000151; C:ubiquitin ligase complex; ISS:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
DR GO; GO:0042393; F:histone binding; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; IEA:Ensembl.
DR GO; GO:0002039; F:p53 binding; ISS:UniProtKB.
DR GO; GO:0003713; F:transcription coactivator activity; ISS:UniProtKB.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISS:UniProtKB.
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; ISS:UniProtKB.
DR GO; GO:0010390; P:histone monoubiquitination; ISS:UniProtKB.
DR GO; GO:0030336; P:negative regulation of cell migration; ISS:UniProtKB.
DR GO; GO:0031062; P:positive regulation of histone methylation; IEA:Ensembl.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0000209; P:protein polyubiquitination; ISS:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
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 2: Evidence at transcript level;
KW Acetylation; Chromatin regulator; Coiled coil; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Transferase; Ubl conjugation pathway;
KW Zinc; Zinc-finger.
FT CHAIN 1..975
FT /note="E3 ubiquitin-protein ligase BRE1A"
FT /id="PRO_0000327716"
FT ZN_FING 922..961
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 125..155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 507..622
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 43..90
FT /evidence="ECO:0000255"
FT COILED 168..375
FT /evidence="ECO:0000255"
FT COILED 429..898
FT /evidence="ECO:0000255"
FT COMPBIAS 126..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 540..555
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 556..622
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:0000250|UniProtKB:Q5VTR2"
FT MOD_RES 138
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5VTR2"
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 562
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3U319"
SQ SEQUENCE 975 AA; 113658 MW; C297567458FC0C0C CRC64;
MSGIGSKRAA GEPGTSVPPE KKTAVEDSGT TVETIKLGGV SSTEELDIRT LQTKNRKLAE
MLDQRQAIED ELREHIEKLE RRQATDDASL LIVNRYWSQF DENIRIILKR YDLEQGLGDL
LTERKALVVP EPEPDSDSNQ ERKDDRERGE GQEPAFSFLA TLASSSSEEM ESQLQERVES
SRRAVSQIVT VYDKLQEKVE LLSRKLNSGD SLMVEEAVQE LNSFLAQENT RLQELTDLLQ
EKHCTMSQEF SKLQSKVETA ESRVSVLESM IDDLQWDIDK IRKREQRLNR HLAEVLERVN
SKGYKVYGAG SSLYGGTITI NARKFEEMNA ELEENKELAQ NRHCELEKLR QDFEEVTSQN
EKLKVELRSA VEEVVKETPE YRCMQSQFSV LYNESLQLKA HLDEARTLLH GTRGTHQRQV
ELIERDEVSL HKKLRTEVIQ LEDTLAQVRK EYEMLRIEFE QTLAANEQAG PINREMRHLI
SSLQNHNHQL KGEVLRYKRK LREAQSDLNK TRLRSGSALL QSQSSTEDPK DEPAELKQDS
EDLATQSAAS KASQEEVNEI KSKRDEEERE RERREKERER EREREKEKER EREKQKLKES
EKERESAKDK EKGKHDDGRK KEAEIIKQLK IELKKAQESQ KEMKLLLDMY RSAPKEQRDK
VQLMAAEKKS KAELEDLRQR LKDLEDKEKK ENKKMADEDA LRKIRAVEEQ IEYLQKKLAM
AKQEEEALLS EMDVTGQAFE DMQEQNIRLM QQLREKDDAN FKLMSERIKS NQIHKLLKEE
KEELADQVLT LKTQVDAQLQ VVRKLEEKEH LLQSNIGTGE KELGLRTQAL EMNKRKAMEA
AQLADDLKAQ LEMAQKKLHD FQDEIVENSV TKEKDMFNFK RAQEDISRLR RKLETTKKPD
NVPKCDEILM EEIKDYKARL TCPCCNMRKK DAVLTKCFHV FCFECVKTRY DTRQRKCPKC
NAAFGANDFH RIYIG
