UniProt: F1R5P0

Database: UniProt
Entry: F1R5P0_DANRE

LinkDB:  F1R5P0_DANRE 
Original site:  F1R5P0_DANRE

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Ontology (7)   
   GO (7)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (8)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
   ENSEMBL-UP (5)   
   ZFIN (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (14)   
   InterPro (8)   
   Pfam (1)   
   PROSITE (3)   
   SMART (2)   
Literature (5)   
   PubMed (5)   
All databases (37)   

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ID   F1R5P0_DANRE            Unreviewed;       364 AA.
AC   F1R5P0; A0A8M1PDJ9; X1WDR1;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 87.
DE   RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|RuleBase:RU367115};
DE            EC=2.3.2.27 {ECO:0000256|RuleBase:RU367115};
GN   Name=rnf146 {ECO:0000313|Ensembl:ENSDARP00000121982,
GN   ECO:0000313|RefSeq:NP_956148.2,
GN   ECO:0000313|ZFIN:ZDB-GENE-030131-5997};
GN   Synonyms=wu:fi29e08 {ECO:0000313|RefSeq:NP_956148.2}, zgc:55909
GN   {ECO:0000313|RefSeq:NP_956148.2};
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955 {ECO:0000313|Ensembl:ENSDARP00000121982};
RN   [1] {ECO:0000313|RefSeq:NP_956148.2}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_956148.2};
RX   PubMed=16109975;
RA   Woods I.G., Wilson C., Friedlander B., Chang P., Reyes D.K., Nix R.,
RA   Kelly P.D., Chu F., Postlethwait J.H., Talbot W.S.;
RT   "The zebrafish gene map defines ancestral vertebrate chromosomes.";
RL   Genome Res. 15:1307-1314(2005).
RN   [2] {ECO:0000313|RefSeq:NP_956148.2}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_956148.2};
RX   PubMed=16466575;
RA   Steinke D., Salzburger W., Braasch I., Meyer A.;
RT   "Many genes in fish have species-specific asymmetric rates of molecular
RT   evolution.";
RL   BMC Genomics 7:20-20(2006).
RN   [3] {ECO:0000313|Ensembl:ENSDARP00000121982}
RP   IDENTIFICATION.
RC   STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000121982};
RG   Ensembl;
RL   Submitted (JUL-2011) to UniProtKB.
RN   [4] {ECO:0000313|Ensembl:ENSDARP00000121982, ECO:0000313|Proteomes:UP000000437}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000121982};
RX   PubMed=23594743; DOI=10.1038/nature12111;
RG   Genome Reference Consortium Zebrafish;
RA   Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA   Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA   Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA   White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA   Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA   Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA   Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA   Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA   Clee C., Oliver K., Clark R., Riddle C., Elliot D., Eliott D.,
RA   Threadgold G., Harden G., Ware D., Begum S., Mortimore B., Mortimer B.,
RA   Kerry G., Heath P., Phillimore B., Tracey A., Corby N., Dunn M.,
RA   Johnson C., Wood J., Clark S., Pelan S., Griffiths G., Smith M.,
RA   Glithero R., Howden P., Barker N., Lloyd C., Stevens C., Harley J.,
RA   Holt K., Panagiotidis G., Lovell J., Beasley H., Henderson C., Gordon D.,
RA   Auger K., Wright D., Collins J., Raisen C., Dyer L., Leung K.,
RA   Robertson L., Ambridge K., Leongamornlert D., McGuire S., Gilderthorp R.,
RA   Griffiths C., Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M.,
RA   Brown J., Murnane C., Gray E., Humphries M., Sycamore N., Barker D.,
RA   Saunders D., Wallis J., Babbage A., Hammond S., Mashreghi-Mohammadi M.,
RA   Barr L., Martin S., Wray P., Ellington A., Matthews N., Ellwood M.,
RA   Woodmansey R., Clark G., Cooper J., Cooper J., Tromans A., Grafham D.,
RA   Skuce C., Pandian R., Andrews R., Harrison E., Kimberley A., Garnett J.,
RA   Fosker N., Hall R., Garner P., Kelly D., Bird C., Palmer S., Gehring I.,
RA   Berger A., Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M.,
RA   Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M.,
RA   Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G., Osoegawa K., Zhu B.,
RA   Rapp A., Widaa S., Langford C., Yang F., Schuster S.C., Carter N.P.,
RA   Harrow J., Ning Z., Herrero J., Searle S.M., Enright A., Geisler R.,
RA   Plasterk R.H., Lee C., Westerfield M., de Jong P.J., Zon L.I.,
RA   Postlethwait J.H., Nusslein-Volhard C., Hubbard T.J., Roest Crollius H.,
RA   Rogers J., Stemple D.L.;
RT   "The zebrafish reference genome sequence and its relationship to the human
RT   genome.";
RL   Nature 496:498-503(2013).
RN   [5] {ECO:0000313|RefSeq:NP_956148.2}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_956148.2};
RX   PubMed=26469318;
RA   Elkon R., Milon B., Morrison L., Shah M., Vijayakumar S., Racherla M.,
RA   Leitch C.C., Silipino L., Hadi S., Weiss-Gayet M., Barras E., Schmid C.D.,
RA   Ait-Lounis A., Barnes A., Song Y., Eisenman D.J., Eliyahu E.,
RA   Frolenkov G.I., Strome S.E., Durand B., Zaghloul N.A., Jones S.M.,
RA   Reith W., Hertzano R.;
RT   "RFX transcription factors are essential for hearing in mice.";
RL   Nat. Commun. 6:8549-8549(2015).
RN   [6] {ECO:0000313|RefSeq:NP_956148.2}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_956148.2};
RX   PubMed=27189481;
RA   Pasquier J., Cabau C., Nguyen T., Jouanno E., Severac D., Braasch I.,
RA   Journot L., Pontarotti P., Klopp C., Postlethwait J.H., Guiguen Y.,
RA   Bobe J.;
RT   "Gene evolution and gene expression after whole genome duplication in fish:
RT   the PhyloFish database.";
RL   BMC Genomics 17:368-368(2016).
RN   [7] {ECO:0000313|RefSeq:NP_956148.2}
RP   IDENTIFICATION.
RC   STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_956148.2};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- FUNCTION: E3 ubiquitin-protein ligase that specifically binds poly-ADP-
CC       ribosylated proteins and mediates their ubiquitination and subsequent
CC       degradation. {ECO:0000256|RuleBase:RU367115}.
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|ARBA:ARBA00000900,
CC         ECO:0000256|RuleBase:RU367115};
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000256|ARBA:ARBA00004906, ECO:0000256|RuleBase:RU367115}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000256|ARBA:ARBA00004514, ECO:0000256|RuleBase:RU367115}.
CC   -!- DOMAIN: The WWE domain mediates non-covalent poly(ADP-ribose)-binding.
CC       {ECO:0000256|RuleBase:RU367115}.
CC   -!- PTM: Ubiquitinated; autoubiquitinated. {ECO:0000256|RuleBase:RU367115}.
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DR   EMBL; CR354556; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; NP_956148.2; NM_199854.2.
DR   Ensembl; ENSDART00000133356.2; ENSDARP00000121982.1; ENSDARG00000089981.6.
DR   Ensembl; ENSDART00000153751.3; ENSDARP00000128360.2; ENSDARG00000089981.6.
DR   GeneID; 334065; -.
DR   KEGG; dre:334065; -.
DR   AGR; ZFIN:ZDB-GENE-030131-5997; -.
DR   CTD; 81847; -.
DR   ZFIN; ZDB-GENE-030131-5997; rnf146.
DR   HOGENOM; CLU_067425_0_0_1; -.
DR   OMA; QYFLRMA; -.
DR   OrthoDB; 2881299at2759; -.
DR   TreeFam; TF318925; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000000437; Chromosome 23.
DR   Bgee; ENSDARG00000089981; Expressed in early embryo and 26 other cell types or tissues.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0072572; F:poly-ADP-D-ribose binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0051865; P:protein autoubiquitination; IEA:UniProtKB-UniRule.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR   CDD; cd16546; RING-HC_RNF146; 1.
DR   Gene3D; 3.30.720.50; -; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR044110; RING-HC_RNF146.
DR   InterPro; IPR033509; RNF146.
DR   InterPro; IPR004170; WWE-dom.
DR   InterPro; IPR018123; WWE-dom_subgr.
DR   InterPro; IPR037197; WWE_dom_sf.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   PANTHER; PTHR13417:SF2; E3 UBIQUITIN-PROTEIN LIGASE RNF146; 1.
DR   PANTHER; PTHR13417; UNCHARACTERIZED; 1.
DR   Pfam; PF02825; WWE; 1.
DR   SMART; SM00184; RING; 1.
DR   SMART; SM00678; WWE; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   SUPFAM; SSF117839; WWE domain; 1.
DR   PROSITE; PS50918; WWE; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   4: Predicted;
KW   Cytoplasm {ECO:0000256|RuleBase:RU367115};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU367115};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000437};
KW   Transferase {ECO:0000256|RuleBase:RU367115};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW   ECO:0000256|RuleBase:RU367115};
KW   Wnt signaling pathway {ECO:0000256|ARBA:ARBA00022687};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU367115};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00175}.
FT   DOMAIN          42..80
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   DOMAIN          102..178
FT                   /note="WWE"
FT                   /evidence="ECO:0000259|PROSITE:PS50918"
FT   REGION          18..37
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          217..262
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          279..364
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        280..298
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        305..323
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   364 AA;  38815 MW;  021E960D782F9761 CRC64;
     MASCGEVNLT VDSLTSGKKV SGEAVPEGSG SPSSPSLPVP ECPICLQSCV HPVRLPCRHI
     FCFLCVKGAS WHSKRCALCR REVPEDFLER PTLLSPEELK ASATGGCGTG SSGHAWYYEG
     RNGWWQYDER TSRELEDAFS KGKKSAEMLI AGFLYVADLE NMVQYRRNEH GRRRRMKRDV
     VDIPKKGVAG LRLDPDPNSS AGAVPAPAVV NVSVDGAAAE RESSADGADT GVSGGRPQGT
     FVPAPIRPPT ILGGHLTSPA SSSDIQLVQT LAQLNISPNE QEPEEEDAED EDDSAAPDAS
     GYDSESGTSD DDEQVEDEDE DEHTDGSQGR HRLQQLDRPP PGGGPANSGD RSGCPDGQCT
     VTKV
//

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