BRE1A_CHICK
ID BRE1A_CHICK Reviewed; 984 AA.
AC Q5ZLS3;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 104.
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; ORFNames=RCJMB04_5a23;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
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).
CC {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
CC complex). {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; AJ719661; CAG31320.1; -; mRNA.
DR RefSeq; NP_001026605.1; NM_001031434.1.
DR AlphaFoldDB; Q5ZLS3; -.
DR SMR; Q5ZLS3; -.
DR STRING; 9031.ENSGALP00000025019; -.
DR PaxDb; Q5ZLS3; -.
DR PRIDE; Q5ZLS3; -.
DR GeneID; 427310; -.
DR KEGG; gga:427310; -.
DR CTD; 56254; -.
DR VEuPathDB; HostDB:geneid_427310; -.
DR eggNOG; KOG0978; Eukaryota.
DR InParanoid; Q5ZLS3; -.
DR OrthoDB; 782448at2759; -.
DR PhylomeDB; Q5ZLS3; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q5ZLS3; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0033503; C:HULC complex; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
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:0010390; P:histone monoubiquitination; IBA:GO_Central.
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 Chromatin regulator; Coiled coil; Metal-binding; Nucleus;
KW Reference proteome; Transferase; Ubl conjugation pathway; Zinc;
KW Zinc-finger.
FT CHAIN 1..984
FT /note="E3 ubiquitin-protein ligase BRE1A"
FT /id="PRO_0000055838"
FT ZN_FING 931..970
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 128..150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 506..632
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 43..90
FT /evidence="ECO:0000255"
FT COILED 236..378
FT /evidence="ECO:0000255"
FT COILED 429..907
FT /evidence="ECO:0000255"
FT COMPBIAS 510..527
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 556..632
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 984 AA; 114808 MW; 61659ADF0A8FCB05 CRC64;
MSGAGNKRAA GEPGPSAPPE KKAGVEDSGT TVETIKLGGV SSTEELDIRT LQTKNRKLAE
MLDQRQAIED ELREHIEKLE RRQATDDASL LIINRYWNQF DENIRIILKR FDLDQGLGDL
LSERKALVVP EPEPDSDSNQ ERKDERERGE GLEPAFSFLA TLASSTSEEI ESQLQERVES
SRRAVAQIVT MYDKLQEKVD VLSHKLNSGD ISLMEEAVLE LNSYLSHENG RLQELADTLQ
EKHRIMSQEF SKLQEKVETA ESRVSVLETM IDDLQWNIDK IRKREQRLNR HLADVLERVN
SKGYKVYGAG SSLYGGTITI NARKFEEMNA ELEENKELAG NRLNELEELR HDLQEVTTQN
EKLKVELRRA VEEAVKETPE YRCMQSQFSV LYNESLQLKA HLDEARTLLH GTRTTHQRQV
ELIERDEVSL HKKLRTEVMQ LEDTLAQVRK EYEMLRIEFE QTLAANEQAG PINREMRHLI
SSLQNHNHQL KGEVLRYKRK LREAQSDLSK IRSRSGSALL QSQSSTEDTK EEPPEIKQEP
DDPSSQVSAP RAASEEASEV KARRDEEERE RERRERERER EKEKEKERER EKEKEKEKER
EREKQKQKES EKERESKEKE KGKHEDGRKK EAEVIKQLKA ELKKAQESQK EMKLLLDMYR
SAPKEQRDKV QLMAAEKKAK AELEELRQRV KELEDKEKKE SKKMADEDAL RKIRAVEEQI
EYLQKKLAMA KQEEEALLSE MDVTGQAFED MQEQNIRLMQ QLREKDDANF KLMSERIKSN
QIHKLLKEEK EELADQVLTL KTQVDAQLQV VRKLEEKEHL LQSSIGTGEK ELGLRTQALE
MNKRKAMDAA QLADDLKTQL ELAQKKLHDF QDEIVESRVT REKEMFNFKR AEEDISRLRR
KLETTKKPDM VPNCDEILME EIKDYKARLT CPCCNMRKKD AVLTKCFHVF CFECVKTRYD
TRQRKCPKCN AAFGANDFHR IYIG
