BRE1B_RAT
ID BRE1B_RAT Reviewed; 1002 AA.
AC Q8CJB9;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=E3 ubiquitin-protein ligase BRE1B;
DE Short=BRE1-B;
DE EC=2.3.2.27 {ECO:0000269|PubMed:12121982};
DE AltName: Full=RING finger protein 40;
DE AltName: Full=RING-type E3 ubiquitin transferase BRE1B {ECO:0000305};
DE AltName: Full=Syntaxin-1-interacting RING finger protein;
DE Short=Protein staring;
GN Name=Rnf40; Synonyms=Bre1b;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], POSSIBLE FUNCTION, CATALYTIC ACTIVITY, TISSUE
RP SPECIFICITY, AND POSSIBLE INTERACTION WITH STX1A.
RC STRAIN=Sprague-Dawley;
RX PubMed=12121982; DOI=10.1074/jbc.m203300200;
RA Chin L.-S., Vavalle J.P., Li L.;
RT "Staring, a novel E3 ubiquitin-protein ligase that targets syntaxin 1 for
RT degradation.";
RL J. Biol. Chem. 277:35071-35079(2002).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-585 AND SER-586, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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:0000269|PubMed:12121982};
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 (By similarity). May interact with STX1A.
CC {ECO:0000250|UniProtKB:O75150}.
CC -!- INTERACTION:
CC Q8CJB9; P61265: Stx1b; NbExp=4; IntAct=EBI-6110162, EBI-2255905;
CC Q8CJB9; O14933: UBE2L6; Xeno; NbExp=2; IntAct=EBI-6110162, EBI-2129974;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O75150}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. Expressed in brain, testis,
CC heart, liver and kidney. Weakly expressed in lung, spleen and skeletal
CC muscle (at protein level). {ECO:0000269|PubMed:12121982}.
CC -!- SIMILARITY: Belongs to the BRE1 family. {ECO:0000305}.
CC -!- CAUTION: Was originally thought to be cytoplasmic and membrane-
CC associated and to mediate ubiquitination and subsequent degradation of
CC STX1A. {ECO:0000305|PubMed:12121982}.
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DR EMBL; AF352815; AAN16401.1; -; mRNA.
DR RefSeq; NP_703201.1; NM_153471.1.
DR AlphaFoldDB; Q8CJB9; -.
DR SMR; Q8CJB9; -.
DR IntAct; Q8CJB9; 2.
DR STRING; 10116.ENSRNOP00000025500; -.
DR iPTMnet; Q8CJB9; -.
DR PhosphoSitePlus; Q8CJB9; -.
DR PaxDb; Q8CJB9; -.
DR PRIDE; Q8CJB9; -.
DR GeneID; 266712; -.
DR KEGG; rno:266712; -.
DR UCSC; RGD:628638; rat.
DR CTD; 9810; -.
DR RGD; 628638; Rnf40.
DR VEuPathDB; HostDB:ENSRNOG00000018840; -.
DR eggNOG; KOG0978; Eukaryota.
DR HOGENOM; CLU_002640_0_0_1; -.
DR InParanoid; Q8CJB9; -.
DR OMA; THIEIMT; -.
DR OrthoDB; 782448at2759; -.
DR PhylomeDB; Q8CJB9; -.
DR TreeFam; TF323183; -.
DR BRENDA; 2.3.2.27; 5301.
DR Reactome; R-RNO-8866654; E3 ubiquitin ligases ubiquitinate target proteins.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q8CJB9; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000018840; Expressed in thymus and 18 other tissues.
DR Genevisible; Q8CJB9; RN.
DR GO; GO:0043679; C:axon terminus; IDA:RGD.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0019898; C:extrinsic component of membrane; IDA:RGD.
DR GO; GO:0033503; C:HULC complex; ISS:UniProtKB.
DR GO; GO:0043005; C:neuron projection; IDA:RGD.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0032991; C:protein-containing complex; IDA:RGD.
DR GO; GO:0000151; C:ubiquitin ligase complex; ISO:RGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; ISO:RGD.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:RGD.
DR GO; GO:0017075; F:syntaxin-1 binding; IPI:RGD.
DR GO; GO:0031624; F:ubiquitin conjugating enzyme binding; IDA:RGD.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:RGD.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:RGD.
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:RGD.
DR GO; GO:0010390; P:histone monoubiquitination; ISO:RGD.
DR GO; GO:1900364; P:negative regulation of mRNA polyadenylation; ISO:RGD.
DR GO; GO:2001168; P:positive regulation of histone H2B ubiquitination; ISO:RGD.
DR GO; GO:1901800; P:positive regulation of proteasomal protein catabolic process; IDA:RGD.
DR GO; GO:1902916; P:positive regulation of protein polyubiquitination; IDA:RGD.
DR GO; GO:0043434; P:response to peptide hormone; IEP:RGD.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IDA:RGD.
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..1002
FT /note="E3 ubiquitin-protein ligase BRE1B"
FT /id="PRO_0000055843"
FT ZN_FING 949..988
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 120..148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 520..562
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 579..652
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 55..91
FT /evidence="ECO:0000255"
FT COILED 190..378
FT /evidence="ECO:0000255"
FT COILED 438..526
FT /evidence="ECO:0000255"
FT COILED 628..947
FT /evidence="ECO:0000255"
FT COMPBIAS 605..620
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 634..652
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 20
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q3U319"
FT MOD_RES 42
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5VTR2"
FT MOD_RES 356
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q5VTR2"
FT MOD_RES 518
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q3U319"
FT MOD_RES 585
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 586
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CROSSLNK 579
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O75150"
FT CROSSLNK 580
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O75150"
SQ SEQUENCE 1002 AA; 113841 MW; EFF371C06B52D231 CRC64;
MSGLSNKRAA GDGGSGPPEK KLNREEKTTT TLIEPIRLGG ISSTEEMDSK VLQFKNKKLA
ERLEQRQACE DELRERIEKL EKRQATDDAT LLIVNRYWAQ LDETVEALLQ CYENQRELSS
SGTEVPGCQE GLTRDVIPRT DPGTSDLREP LPMQFRAPLS EPALAFVVAL GASSCEEVEL
QLQGRMEFSK AAVSRVVEAS DRLQRQVEEL CQRVYSRGDS EAPGEVARAR TRELGRENRR
LQDLATQLQE KHHRISLEYS ELQDKVTSTE TKVLEMETTV EDLQWDIEKL RKREQKLNKH
LAEALEQLNS GYYVSGSSTG FQGGQITLSM QKFEMLNAEL EENQELANSR MAELEKLQAE
LQGAVRTNER LKVALRSLPE EVVRETGEYR MLQAQFSLLY NESLQVKTQL DEARGLLLAS
KNSHLRHIEH MESDELGLQK KLRTEVIQLE DTLAQVRKEY EMLRIEFEQN LAANEQAGPI
NREMRHLISS LQNHNHQLKG DAQRYKRKLR EVQAEIGKLR AQASGSSHCG PNLSHPDDSG
LNALAPGKED SGPGPGGTPD SKKELALVAG ATSVASSVKK EELVSSEDDA QALAPGTQGL
PSRGREPEAR PKRELREREG PSLGPPPAAS TLSRADREKA KAEEARRKES ELLKGLRAEL
KKAQESQKEM KLLLDMYKSA PKEQRDKVQL MAAERKAKAE VDELRSRIRD LEERDRRESK
KIADEDALRR IRQAEEQIEH LQRKLGATKQ EEEALLSEMD VTGQAFEDMQ EQNGRLLQQL
REKDDANFKL MSERIKANQI HKLLREEKDE LGEQVLGLKS QVDAQLLTVQ KLEEKERALQ
GSLGGVEKEL TLRSQALELN KRKAVEAAQL AEDLKVQLEH VQTRLREIQP CLAESRAARE
KESFNLKRAQ EDISRLRRKL EKQRKVEVYA DADEILQEEI KEYKARLTCP CCNTRKKDAV
LTKCFHVFCF ECVRGRYEAR QRKCPKCNAA FGAHDFHRVY IS
