ID A0A3Q7SXZ0_VULVU Unreviewed; 1035 AA.
AC A0A3Q7SXZ0;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=E3 ubiquitin protein ligase {ECO:0000256|RuleBase:RU365038};
DE EC=2.3.2.27 {ECO:0000256|RuleBase:RU365038};
GN Name=RNF20 {ECO:0000313|RefSeq:XP_025868984.1};
OS Vulpes vulpes (Red fox).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Vulpes.
OX NCBI_TaxID=9627 {ECO:0000313|Proteomes:UP000286640, ECO:0000313|RefSeq:XP_025868984.1};
RN [1]
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (JAN-2019) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_025868984.1}
RP IDENTIFICATION.
RC STRAIN=TameXAggressive cross {ECO:0000313|RefSeq:XP_025868984.1};
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_025868984.1};
RG RefSeq;
RL Submitted (SEP-2023) to UniProtKB.
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 -!- 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.
CC {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 RefSeq; XP_025868984.1; XM_026013199.1.
DR STRING; 9627.ENSVVUP00000026200; -.
DR KEGG; vvp:112930789; -.
DR OrthoDB; 53681at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000286640; Unplaced.
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-UniPathway.
DR CDD; cd16814; RING-HC_RNF20; 1.
DR Gene3D; 1.20.1170.10; -; 1.
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:SF2; E3 UBIQUITIN-PROTEIN LIGASE BRE1A; 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:UP000286640};
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 982..1021
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 73..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 185..215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 566..686
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 111..145
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 252..358
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 382..433
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 897..924
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 186..212
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 570..587
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 616..686
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1035 AA; 120962 MW; 9DA189AE914FC45C CRC64;
MAGPLSKAAR CLSIHFSSSE LRDPGRQFGQ TRRAXQDVEL EIKEQLESLA HPCLQRRRQP
LKIQGPQWRQ LSLEVSPPRE IRGDSSESED GGGSVGGLKR QEKEELDIRT LQTKNRKLAE
MLDQRQAIED ELREHIEKLE RRQATDDASL LIVNRYWSQF DENIRIILKR YDLEQGLGDL
LTERKALVVP EPEPDSDSNQ ERKDDRERGE GQEPAFSFLA TLASSSSEEM ESQLQERVES
SRRAVSQIVT VYDKLQEKVE LLSRKLNSGD NLIVEEAVQE LNSFLAQENM RLQELTDLLQ
EKHRTMSQEF SKLQSKVETA ESRVSVLESM IDDLQWDIDK IRKREQRLNR HLAEVLERVN
SKGYKVYGAG SSLYGGTITI NARKFEEMNA ELEENKELAQ NRHCELEKLR QDLEEVTTQN
EKLKVELRSA VEEAVKETPE YRCMQSQFSV LYNESLQLKA HLDEARTLLH GTRGTHQRQV
ELIERDEVSL HKKLRTEVIQ LEDTLAQVRK EYEMLRIEFE QTLAANEQAG PINREMRHLI
SSLQNHNHQL KGEVLRYKRK LREAQSDLNK TRLRSGSALL QSQSSTEDPK DEPAELKQDP
EDVPAQSSAS KASQEEVNEI KSKRDEEERE RERREKERER EREREKEKER EREKQKLKES
EKERDSAKDK EKGKHDDGRK KEAEVIKQLK IELKKAQESQ KEMKLLLDMY RSAPKEQRDK
VQLMAAEKKS KAELEDLRQR LKDLEDKEKK ENKKMADEDA LRKIRAVEEQ IEYLQKKLAM
AKQEEEALLS EMDVTGQAFE DMQEQNIRLM QQLREKDDAN FKLMSERIKS NQIHKLLKEE
KEELADQVLT LKTQVDAQLQ VVRKLEEKEH LLQSNIGTGE KELGLRTQAL EMNKRKAMEA
AQLADDLKAQ LELAQKKLHD FQDEIVENSV TKEKDMFNFK RAQEDISRLR RKLETTKKPD
NVPKCDEILM EEIKDYKARL TCPCCNMRKK DAVLTKCFHV FCFECVKTRY DTRQRKCPKC
NAAFGANDFH RIYIG
//