BRE1B_MACFA
ID BRE1B_MACFA Reviewed; 1001 AA.
AC Q4R7K7;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 81.
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; ORFNames=QtsA-14984;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RG International consortium for macaque cDNA sequencing and analysis;
RT "DNA sequences of macaque genes expressed in brain or testis and its
RT evolutionary implications.";
RL Submitted (JUN-2005) 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. {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}.
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DR EMBL; AB168810; BAE00915.1; -; mRNA.
DR AlphaFoldDB; Q4R7K7; -.
DR SMR; Q4R7K7; -.
DR STRING; 9541.XP_005591734.1; -.
DR eggNOG; KOG0978; Eukaryota.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000233100; Unplaced.
DR GO; GO:0033503; C:HULC complex; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0000151; C:ubiquitin ligase complex; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISS:UniProtKB.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0033523; P:histone H2B ubiquitination; ISS:UniProtKB.
DR GO; GO:0010390; P:histone monoubiquitination; ISS:UniProtKB.
DR GO; GO:0031401; P:positive regulation of protein modification process; IEA:UniProt.
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; 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_0000055840"
FT ZN_FING 948..987
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 116..149
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 516..646
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 45..91
FT /evidence="ECO:0000255"
FT COILED 228..377
FT /evidence="ECO:0000255"
FT COILED 437..523
FT /evidence="ECO:0000255"
FT COILED 627..946
FT /evidence="ECO:0000255"
FT COMPBIAS 518..535
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 604..619
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 355
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q5VTR2"
FT MOD_RES 517
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q3U319"
FT MOD_RES 528
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5VTR2"
FT MOD_RES 585
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3U319"
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"
SQ SEQUENCE 1001 AA; 113592 MW; A7EE4FDDCC76C61A CRC64;
MSGLGNKRAA GDGGSGPPEK KLSREEKTTT TLIEPIRLGG ISSTEEIDLK VLQFKNKKLA
ERLEQRQACE DELRERIEKL EKRQATDDAT LLIVNRYWAQ LDETVEALLR CHEGQGELSS
APEAPGTQEG PTCDGTPLPE PGTSELREPL PLQLRPPLSE PALAFVVALG ASSSEEVELE
LQGRMEFSKA AVSHVVEASD RLQRRVEELC QRVYSRGDSE PLSEVARART RELGRENRRL
QDLATQLQEK HHRISLEYSE LQDKVTSAET KVLEMETTVE DLQWDIEKLR KREQKLNKHL
AEALEQLNSG YYVSGSSSGF QGGQITLSMQ KFEMLNAELE ENQELANSRM AELEKLQAEL
QGAVRTNERL KVALRSLPEE VVRETGEYRM LQAQFSLLYN ESLQVKTQLD EARGLLLATK
NSHLRHIEHM ESDELGLQKK LRTEVIQLED TLAQVRKEYE MLRIEFEQNL AANEQAGPIN
REMRHLISSL QNHNHQLKGD AQRYKRKLRE VQAEIGKLRA QTSGSTHSTP NLGHPEDSGL
SAPAPGKEEG GPGPVSTPDN RKEMAPVPGT TTTTTSVKKE ELVPSEEDVQ GLTLGAQGPS
SRGREPEARP KRELREREGP GLGPPPVASA LSRADREKAK VEEAKRKESE LLKGLRAELK
KAQESQKEMK LLLDMYKSAP KEQRDKVQLM AAERKAKAEV DELRSRIREL EERDRRESKK
IADGDALRRI 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 GAHDFHRIYI S
