ID A0A3P8XZE1_ESOLU Unreviewed; 985 AA.
AC A0A3P8XZE1;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 02-DEC-2020, sequence version 2.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=E3 ubiquitin protein ligase {ECO:0000256|RuleBase:RU365038};
DE EC=2.3.2.27 {ECO:0000256|RuleBase:RU365038};
GN Name=RNF40 {ECO:0000313|Ensembl:ENSELUP00000009813.2};
OS Esox lucius (Northern pike).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Esociformes;
OC Esocidae; Esox.
OX NCBI_TaxID=8010 {ECO:0000313|Ensembl:ENSELUP00000009813.2, ECO:0000313|Proteomes:UP000265140};
RN [1] {ECO:0000313|Ensembl:ENSELUP00000009813.2, ECO:0000313|Proteomes:UP000265140}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=25069045;
RA Rondeau E.B., Minkley D.R., Leong J.S., Messmer A.M., Jantzen J.R.,
RA von Schalburg K.R., Lemon C., Bird N.H., Koop B.F.;
RT "The genome and linkage map of the northern pike (Esox lucius): conserved
RT synteny revealed between the salmonid sister group and the Neoteleostei.";
RL PLoS ONE 9:e102089-e102089(2014).
RN [2] {ECO:0000313|Ensembl:ENSELUP00000009813.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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:0000256|ARBA:ARBA00037123}.
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:0000256|RuleBase:RU365038};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906, ECO:0000256|RuleBase:RU365038}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|RuleBase:RU365038}.
CC -!- SIMILARITY: Belongs to the BRE1 family. {ECO:0000256|ARBA:ARBA00005555,
CC ECO:0000256|RuleBase:RU365038}.
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DR AlphaFoldDB; A0A3P8XZE1; -.
DR Ensembl; ENSELUT00000003196.2; ENSELUP00000009813.2; ENSELUG00000010378.2.
DR GeneTree; ENSGT00390000002866; -.
DR InParanoid; A0A3P8XZE1; -.
DR OMA; THIEIMT; -.
DR OrthoDB; 53681at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000265140; LG05.
DR Bgee; ENSELUG00000010378; Expressed in testis and 14 other cell types or tissues.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 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:SF4; E3 UBIQUITIN-PROTEIN LIGASE BRE1B; 1.
DR PANTHER; PTHR23163; RING FINGER PROTEIN-RELATED; 1.
DR Pfam; PF00097; zf-C3HC4; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Chromatin regulator {ECO:0000256|ARBA:ARBA00022853,
KW ECO:0000256|RuleBase:RU365038};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|RuleBase:RU365038};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU365038}; Nucleus {ECO:0000256|RuleBase:RU365038};
KW Reference proteome {ECO:0000313|Proteomes:UP000265140};
KW Transferase {ECO:0000256|RuleBase:RU365038};
KW Ubl conjugation pathway {ECO:0000256|RuleBase:RU365038};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU365038};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 932..971
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 135..169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 599..630
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 58..88
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 312..413
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 135..167
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 985 AA; 113541 MW; 455264E8735F6434 CRC64;
MSGTGAGKRP SGGDSPPGPP EKKSKKEEKT TTTLIEPIRI GGVSSTEEMD MKVIQFKNKK
LSERLEQRQT MEDELREKIE KLEKRQATDD TTLLIVNRYW SQLEENVNVL CQRIDPTVVP
APPATPVPVP TPMEDDGIMV PPPPPPAPLP ASEHEEQQPP PPDGLAPEPH EFLLLPVLTA
DLSLWSAAPP SSPAPLSDSA KALLAILDNS SEEELGLQLQ DRMKFSKEAA ACMVCIQSAG
NYSPSIHHTQ GLVGLPFCED ESQEELLRLN RTLLQENGRL QDLASNLQGR HHKMSLEYNE
LVDKVTSSET KVSEMETAVE DLQWDIEKLR KREQKLNKHL AEALEQLNSG HYATGSSGGL
PGGQITLNIQ KFESLNAELE QNQELANSRM AELEKLQQEL QEAVRESEKL KLDLKNIPEE
VVKETAEYKC LQSQFSLLYN ESLGVKTQLD EARALLLTAK NAHLRQIEHM ESDELSLQKK
LRTEVIQLED TLAQVRKEYE MLRIEFEQNL AANEQAGPIN REMRHLISSL QNHNHQLKGD
VQRYKRKLRE TQMEINKLRC QSGDTGLLSL EEPVSDCLDV KKEEDEDQEE EEERRRELER
QRAREREREV ERERERERER ERQRSEELKR KDSDTLKMLR AELKKAQESQ KEMKLLLDMY
KSAPKEQRDK VQLMAAERKS KAEVEELRVR VRELEERERK ESKKLADEDA LRKIRVAEET
IDHLQKKLTA TKQEEEALLS EMDVTGQAFE DMQEQNSRLM QQLREKDDAN FKLMSERIKS
NQIYKLLREE KEELADQVLT FKTQVEAQLL VVQKLEEKEG VLQSSLAALE KELGVRTQAL
ELNKRKAVEA AQLAEDLKVQ LEHTQSKLRE IQVSVSENRT ARERELGNLK RAQEDLSRLR
RKLEKQKKVE VYTDADEILQ EEINQYKAKL RCPCCNTRDK ETVLTKCFHV FCYECLKTRY
DTRQRKCPKC NCAFGANDFH RIYIT
//
