ID A0A5E4BFX2_MARMO Unreviewed; 474 AA.
AC A0A5E4BFX2;
DT 13-NOV-2019, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2019, sequence version 1.
DT 18-JUN-2025, entry version 24.
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 ORFNames=GHT09_010792 {ECO:0000313|EMBL:KAF7478183.1}, MONAX_5E024315
GN {ECO:0000313|EMBL:VTJ68593.1};
OS Marmota monax (Woodchuck).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha; Sciuridae;
OC Xerinae; Marmotini; Marmota.
OX NCBI_TaxID=9995 {ECO:0000313|EMBL:VTJ68593.1, ECO:0000313|Proteomes:UP000335636};
RN [1] {ECO:0000313|EMBL:VTJ68593.1, ECO:0000313|Proteomes:UP000335636}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Alioto T., Alioto T.;
RL Submitted (APR-2019) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KAF7478183.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=WC2-LM {ECO:0000313|EMBL:KAF7478183.1};
RC TISSUE=Liver {ECO:0000313|EMBL:KAF7478183.1};
RA Shumante A., Zimin A.V., Puiu D., Salzberg S.L.;
RL Submitted (AUG-2020) to the EMBL/GenBank/DDBJ databases.
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 EMBL; WJEC01001691; KAF7478183.1; -; Genomic_DNA.
DR EMBL; WJEC01001691; KAF7478184.1; -; Genomic_DNA.
DR EMBL; WJEC01001691; KAF7478185.1; -; Genomic_DNA.
DR EMBL; WJEC01001691; KAF7478186.1; -; Genomic_DNA.
DR EMBL; WJEC01001691; KAF7478187.1; -; Genomic_DNA.
DR EMBL; CABDUW010000435; VTJ68593.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5E4BFX2; -.
DR Proteomes; UP000335636; Unassembled WGS sequence.
DR Proteomes; UP000662637; Unassembled WGS sequence.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:UniProtKB-ARBA.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016567; P:protein ubiquitination; IEA:InterPro.
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:UP000335636};
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; 53948 MW; B40E5BB3549F4EA6 CRC64;
MSSEDREAQE DELLALASIY DGDEFRKAES VQGGETRIYL DLPQNFKIFV SGNSNECLQT
SGFEYTICFL PPLVLNFELP PDYPSSSPPS FTLSGKWLSP TQLSALCKHL DNLWEEHRGS
VVLFAWMQFL KEDTLAYLNI VSPFELKMGS QKKMQRRTAQ ASSNTELEFG GATGSDVDQE
EVVDERAVQD VESLSSLIQE ILDFDQAQQM KCFNSKLFLC NICFCEKLGS ECMYFLECRH
VYCKACLKDY FEIQIKDGQV QCLNCPEPKC PSVATPGQVK ELVEAELFAR YDRLLLQSTL
DLMADVVYCP RPCCQLPVMQ EPGCTMGICS SCNFAFCTLC RLTYHGVSPC KVTAEKLIDL
RNEYLQADEA NKRFLEQRYG KRVIQKALEE MESKEWLEKN SKSCPCCGTP IQKLDGCNKM
TCTGCMQYFC WICMGFLSRA NPYKHFTDPD SPCFNRLFHA VDVNGDIWED EIED
//
