R146B_BOVIN
ID R146B_BOVIN Reviewed; 347 AA.
AC Q3T139;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=E3 ubiquitin-protein ligase RNF146-B;
DE EC=2.3.2.27;
DE AltName: Full=RING finger protein 146-B;
DE AltName: Full=RING-type E3 ubiquitin transferase RNF146-B {ECO:0000305};
GN Name=RNF146B;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: E3 ubiquitin-protein ligase that specifically binds poly-ADP-
CC ribosylated proteins and mediates their ubiquitination and subsequent
CC degradation. Acts as an activator of the Wnt signaling pathway by
CC mediating the ubiquitination of poly-ADP-ribosylated AXIN1 and AXIN2, 2
CC key components of the beta-catenin destruction complex. Acts in
CC cooperation with tankyrase proteins (TNKS and TNKS2), which mediate
CC poly-ADP-ribosylation of target proteins AXIN1, AXIN2, BLZF1, CASC3,
CC TNKS and TNKS2. Recognizes and binds tankyrase-dependent poly-ADP-
CC ribosylated proteins via its WWE domain and mediates their
CC ubiquitination (By similarity). {ECO:0000250}.
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;
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Interacts with poly-ADP-ribosylated AXIN1, AXIN2, BLZF1 and
CC CASC3. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}.
CC -!- DOMAIN: The WWE domain mediates non-covalent poly(ADP-ribose)-binding.
CC {ECO:0000250}.
CC -!- PTM: Ubiquitinated; autoubiquitinated. Autoubiquitination is enhanced
CC upon poly(ADP-ribose)-binding (By similarity). {ECO:0000250}.
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DR EMBL; BC102139; AAI02140.1; -; mRNA.
DR RefSeq; NP_001070448.1; NM_001076980.1.
DR RefSeq; XP_005210757.1; XM_005210700.1.
DR AlphaFoldDB; Q3T139; -.
DR BMRB; Q3T139; -.
DR SMR; Q3T139; -.
DR STRING; 9913.ENSBTAP00000037915; -.
DR PaxDb; Q3T139; -.
DR PRIDE; Q3T139; -.
DR Ensembl; ENSBTAT00000038099; ENSBTAP00000037915; ENSBTAG00000034531.
DR GeneID; 767901; -.
DR KEGG; bta:767901; -.
DR CTD; 81847; -.
DR VEuPathDB; HostDB:ENSBTAG00000034531; -.
DR eggNOG; KOG0824; Eukaryota.
DR GeneTree; ENSGT00390000000358; -.
DR HOGENOM; CLU_067425_0_0_1; -.
DR InParanoid; Q3T139; -.
DR OMA; KTNESCA; -.
DR OrthoDB; 1469576at2759; -.
DR TreeFam; TF318925; -.
DR Reactome; R-BTA-201681; TCF dependent signaling in response to WNT.
DR Reactome; R-BTA-4641257; Degradation of AXIN.
DR Reactome; R-BTA-5689880; Ub-specific processing proteases.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000009136; Chromosome 9.
DR Bgee; ENSBTAG00000034531; Expressed in cerebellum and 101 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0072572; F:poly-ADP-D-ribose binding; ISS:UniProtKB.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; ISS:UniProtKB.
DR GO; GO:0051865; P:protein autoubiquitination; ISS:UniProtKB.
DR GO; GO:0070936; P:protein K48-linked ubiquitination; ISS:UniProtKB.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR CDD; cd16546; RING-HC_RNF146; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR Gene3D; 3.30.720.50; -; 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; PTHR13417:SF2; 1.
DR Pfam; PF02825; WWE; 1.
DR SMART; SM00184; RING; 1.
DR SMART; SM00678; WWE; 1.
DR SUPFAM; SSF117839; SSF117839; 1.
DR PROSITE; PS50918; WWE; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Isopeptide bond; Metal-binding; Phosphoprotein;
KW Reference proteome; Transferase; Ubl conjugation; Ubl conjugation pathway;
KW Wnt signaling pathway; Zinc; Zinc-finger.
FT CHAIN 1..347
FT /note="E3 ubiquitin-protein ligase RNF146-B"
FT /id="PRO_0000409503"
FT DOMAIN 92..168
FT /note="WWE"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00248"
FT ZN_FING 37..75
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 196..241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 257..347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 196..239
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 257..273
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 293..328
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 288
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5XIK5"
FT MOD_RES 292
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5XIK5"
FT CROSSLNK 85
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q9NTX7"
FT CROSSLNK 95
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q9NTX7"
FT CROSSLNK 131
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q9NTX7"
FT CROSSLNK 176
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q9NTX7"
SQ SEQUENCE 347 AA; 37616 MW; 9C250F817E4BD2CD CRC64;
MMAGCGEIDH SINMLPTNRK ANESCSNTAP SLTVPECAIC LQTCVHPVSL PCKHVFCYLC
VKGASWLGKR CALCRQEIPE DFLDKPTLLS PEELKAASRG NGEYAWYYEG RNGWWQYDER
TSRELEDAFS KGKKSTEMLI AGFLYVADLE NMVQYRRNEH GRRRKIKRDI IDIPKKGVAG
LRLDCDANTV NLARESSADG ADSVPAQSGA SVQSSSVRPL TSVDGQLTSP ATPSPDAGTS
LEDSFAHLQL GGDSIAERSH RGEGEEEHES PSSGRVPAPD TSIEETESDA SSDSEDVSAL
VAQHSLTQQR LLVPNPSQTV SDRSVAAGGT VSVRSRRPDG QCTVTEV
