ID A0A452RCT9_URSAM Unreviewed; 474 AA.
AC A0A452RCT9;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 18-JUN-2025, entry version 31.
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:ENSUAMP00000016538.1};
OS Ursus americanus (American black bear) (Euarctos americanus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ursus.
OX NCBI_TaxID=9643 {ECO:0000313|Ensembl:ENSUAMP00000016538.1, ECO:0000313|Proteomes:UP000291022};
RN [1] {ECO:0000313|Proteomes:UP000291022}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Korstanje R., Srivastava A., Sarsani V.K., Sheehan S.M., Seger R.L.,
RA Barter M.E., Lindqvist C., Brody L.C., Mullikin J.C.;
RT "De novo assembly and RNA-Seq shows season-dependent expression and editing
RT in black bear kidneys.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSUAMP00000016538.1}
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 STRING; 9643.ENSUAMP00000016538; -.
DR Ensembl; ENSUAMT00000018518.1; ENSUAMP00000016535.1; ENSUAMG00000013165.1.
DR Ensembl; ENSUAMT00000018521.1; ENSUAMP00000016538.1; ENSUAMG00000013165.1.
DR GeneTree; ENSGT00940000154507; -.
DR OMA; PRSWCQG; -.
DR Proteomes; UP000291022; Unassembled WGS sequence.
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:UP000291022};
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"
FT REGION 155..174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 474 AA; 53777 MW; F942F978F4AD5231 CRC64;
MSSEDREAQE DELLALASIY DGDEFRKAES VQGGETRIYL DLPQNFKIFV SGNSNECLQN
GGFEYTICFL PPLVLNFELP PDYPSSSPPS FTLSGKWLSP TQLSALCKHL DNLWEEHRGS
VVLFAWMQFL KEETLAYLNI VSPFELKMGS QKKVQRRTAQ ASPNTELDFG GAAGSDADQE
EAVDERAVQD VESLSSLIQE ILDFDQAQQI KCFNSKLFLC NICFCEKLGS ECMYFLECRH
VYCKACLKDY FEIQIRDGQV QCLNCPEPKC PSVATPGQVK ELVETELFAR YDRLLLQSTL
DLMADVVYCP RPCCQLPVMQ EPGCTMGICS SCNFAFCTLC RLTYHGVSPC KVTAEKLMDL
RNEYLQADEA NKRFLEQRYG KRVIQKALEE MESKEWLEKN SKSCPCCGTP IEKLDGCNKM
TCTGCMQYFC WICMGSLSRA NPYKHFTDPA SPCFNRLFHA VDVNGDIWED EIED
//
