ID A0A8B9YQV1_BOSMU Unreviewed; 474 AA.
AC A0A8B9YQV1;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2022, sequence version 1.
DT 18-JUN-2025, entry version 18.
DE RecName: Full=E3 ubiquitin-protein ligase RNF14 {ECO:0000256|ARBA:ARBA00067098};
DE EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
DE AltName: Full=RING finger protein 14 {ECO:0000256|ARBA:ARBA00075528};
GN Name=RNF14 {ECO:0000313|Ensembl:ENSBGRP00000040991.1};
OS Bos mutus grunniens (Wild yak) (Bos grunniens).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=30521 {ECO:0000313|Ensembl:ENSBGRP00000040991.1, ECO:0000313|Proteomes:UP000694520};
RN [1] {ECO:0000313|Ensembl:ENSBGRP00000040991.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Zhang S., Liu J.;
RL Submitted (MAY-2019) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSBGRP00000040991.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (MAR-2025) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + [acceptor protein]-N(6)-ubiquitinyl-L-lysine.;
CC EC=2.3.2.31; Evidence={ECO:0000256|ARBA:ARBA00001798};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
CC -!- SUBUNIT: Interacts with GCN1; interaction takes place in response to
CC ribosome collisions and is required for ubiquitination of EEF1A1/eEF1A.
CC Interacts with the ubiquitin-conjugating enzymes UBE2E1 and UBE2E2.
CC Interacts with AR/androgen receptor. Interacts with TCF7/TCF1,
CC TCF7L1/TCF3 and TCF7L2/TCF4; promoting Wnt signaling.
CC {ECO:0000256|ARBA:ARBA00062346}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the RBR family. RNF14 subfamily.
CC {ECO:0000256|ARBA:ARBA00044508}.
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DR Ensembl; ENSBGRT00000047539.1; ENSBGRP00000040991.1; ENSBGRG00000025698.1.
DR GeneTree; ENSGT00940000154507; -.
DR Proteomes; UP000694520; Chromosome 8.
DR GO; GO:0022626; C:cytosolic ribosome; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0050681; F:nuclear androgen receptor binding; IEA:Ensembl.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:Ensembl.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; IEA:Ensembl.
DR GO; GO:0085020; P:protein K6-linked ubiquitination; IEA:Ensembl.
DR GO; GO:0160127; P:protein-RNA covalent cross-linking repair; IEA:Ensembl.
DR GO; GO:0060765; P:regulation of androgen receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0060828; P:regulation of canonical Wnt signaling pathway; IEA:Ensembl.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:Ensembl.
DR CDD; cd20341; BRcat_RBR_RNF14; 1.
DR CDD; cd20354; Rcat_RBR_RNF14; 1.
DR CDD; cd16628; RING-HC_RBR_RNF14; 1.
DR CDD; cd23820; RWD_RNF14; 1.
DR FunFam; 1.20.120.1750:FF:000011; RBR-type E3 ubiquitin transferase; 1.
DR FunFam; 2.20.25.20:FF:000007; RBR-type E3 ubiquitin transferase; 1.
DR FunFam; 3.10.110.10:FF:000049; RBR-type E3 ubiquitin transferase; 1.
DR FunFam; 3.30.40.10:FF:000186; RBR-type E3 ubiquitin transferase; 1.
DR Gene3D; 1.20.120.1750; -; 1.
DR Gene3D; 2.20.25.20; -; 1.
DR Gene3D; 3.10.110.10; Ubiquitin Conjugating Enzyme; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR031127; E3_UB_ligase_RBR.
DR InterPro; IPR002867; IBR_dom.
DR InterPro; IPR047548; Rcat_RBR_RNF14.
DR InterPro; IPR031128; RNF14_RING-HC_Zfn.
DR InterPro; IPR006575; RWD_dom.
DR InterPro; IPR044066; TRIAD_supradom.
DR InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR11685; RBR FAMILY RING FINGER AND IBR DOMAIN-CONTAINING; 1.
DR Pfam; PF01485; IBR; 1.
DR Pfam; PF22191; IBR_1; 1.
DR Pfam; PF05773; RWD; 1.
DR SMART; SM00647; IBR; 2.
DR SMART; SM00591; RWD; 1.
DR SUPFAM; SSF57850; RING/U-box; 3.
DR SUPFAM; SSF54495; UBC-like; 1.
DR PROSITE; PS50908; RWD; 1.
DR PROSITE; PS51873; TRIAD; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000694520};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 11..137
FT /note="RWD"
FT /evidence="ECO:0000259|PROSITE:PS50908"
FT DOMAIN 216..457
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT DOMAIN 220..265
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
SQ SEQUENCE 474 AA; 53828 MW; C96EAF030B2B8772 CRC64;
MSSEDREAQE DELLALASIY DGDEFRKAES VQGGETRIHL DLPQNFKIFV SGNSNECLQN
SGFEYTICFL PPLVLNFELP PDYPSSSPPS FTLSGKWLSP TQLSALCKHL DNLWEEHRGS
VVLFAWMQFL KEETLAYLNI VSPFELTMGS QKKVQRRMAQ ASSNTELDFG GATGSDIDQE
EVVDERAVQD VESLSSLIQE ILDFDQAQQI KCFNSKLFLC NICFCEKLGS ECMYFLECRH
VYCKACLKDY FEIQIRDGQV QCLNCPEPKC PSVATPGQVK ELVEAELFAR YDRLLLQSTL
DLMADVVYCP RPSCQLPVMQ EPGCTMGICS SCNFAFCTLC RLTYHGVSPC KVTAEKLMDL
RNEYLQADEA NKRFLEQRYG KRVIQKALEE MESKEWLEKN SKSCPCCGTP IEKLDGCNKM
TCTGCMQYFC WICMGSLSRA NPYKHFTDPA SPCFNRLFHA VDVNGDIWED EIED
//
