ID RNF14_HUMAN Reviewed; 474 AA. AC Q9UBS8; A0AV26; A6NMR2; A8MTW5; B3KN72; B7ZLV2; D3DQE4; O94793; Q6IBV0; DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 28-JAN-2026, entry version 214. DE RecName: Full=E3 ubiquitin-protein ligase RNF14 {ECO:0000305}; DE EC=2.3.2.31 {ECO:0000269|PubMed:36638793, ECO:0000269|PubMed:37651229, ECO:0000269|PubMed:37951215, ECO:0000269|PubMed:37951216}; DE AltName: Full=Androgen receptor-associated protein 54 {ECO:0000303|PubMed:10085091}; DE AltName: Full=HFB30 {ECO:0000303|PubMed:10320776}; DE AltName: Full=RING finger protein 14 {ECO:0000305}; GN Name=RNF14 {ECO:0000303|PubMed:36638793, ECO:0000312|HGNC:HGNC:10058}; GN Synonyms=ARA54 {ECO:0000303|PubMed:10085091}; ORFNames=HRIHFB2038; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Fetal brain; RX PubMed=10320776; DOI=10.1016/s0167-4781(99)00045-7; RA Ueki N., Seki N., Yano K., Masuho Y., Saito T., Muramatsu M.-A.; RT "Isolation and characterization of a novel human gene (HFB30) which encodes RT a protein with a RING finger motif."; RL Biochim. Biophys. Acta 1445:232-236(1999). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH AR, AND TISSUE RP SPECIFICITY. RC TISSUE=Prostate; RX PubMed=10085091; DOI=10.1074/jbc.274.13.8570; RA Kang H.-Y., Yeh S., Fujimoto N., Chang C.; RT "Cloning and characterization of human prostate coactivator ARA54, a novel RT protein that associates with the androgen receptor."; RL J. Biol. Chem. 274:8570-8576(1999). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Brain, and Thyroid; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15372022; DOI=10.1038/nature02919; RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S., RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.; RT "The DNA sequence and comparative analysis of human chromosome 5."; RL Nature 431:268-274(2004). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 286-474 (ISOFORM 1), AND RP SUBCELLULAR LOCATION. RC TISSUE=Fetal brain; RX PubMed=9853615; DOI=10.1038/4315; RA Ueki N., Oda T., Kondo M., Yano K., Noguchi T., Muramatsu M.-A.; RT "Selection system for genes encoding nuclear-targeted proteins."; RL Nat. Biotechnol. 16:1338-1342(1998). RN [9] RP INTERACTION WITH UBE2E1 AND UBE2E2, AUTOUBIQUITINATION, AND MUTAGENESIS OF RP CYS-220. RX PubMed=11322894; DOI=10.1046/j.1432-1327.2001.02169.x; RA Ito K., Adachi S., Iwakami R., Yasuda H., Muto Y., Seki N., Okano Y.; RT "N-terminally extended human ubiquitin-conjugating enzymes (E2s) mediate RT the ubiquitination of RING-finger proteins, ARA54 and RNF8."; RL Eur. J. Biochem. 268:2725-2732(2001). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-348, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [11] RP FUNCTION, AND INTERACTION WITH AR. RX PubMed=19345326; DOI=10.1016/j.ccr.2009.02.021; RA Xu K., Shimelis H., Linn D.E., Jiang R., Yang X., Sun F., Guo Z., Chen H., RA Li W., Chen H., Kong X., Melamed J., Fang S., Xiao Z., Veenstra T.D., RA Qiu Y.; RT "Regulation of androgen receptor transcriptional activity and specificity RT by RNF6-induced ubiquitination."; RL Cancer Cell 15:270-282(2009). RN [12] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [13] RP FUNCTION, AND INTERACTION WITH TCF7; TCF7L1 AND TCF7L2. RX PubMed=23449499; DOI=10.1038/embor.2013.19; RA Wu B., Piloto S., Zeng W., Hoverter N.P., Schilling T.F., Waterman M.L.; RT "Ring Finger Protein 14 is a new regulator of TCF/beta-catenin-mediated RT transcription and colon cancer cell survival."; RL EMBO Rep. 14:347-355(2013). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-348, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [15] RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, ACTIVE SITE, INTERACTION WITH GCN1, RP AND MUTAGENESIS OF CYS-417. RX PubMed=36638793; DOI=10.1016/j.cell.2022.12.025; RA Oltion K., Carelli J.D., Yang T., See S.K., Wang H.Y., Kampmann M., RA Taunton J.; RT "An E3 ligase network engages GCN1 to promote the degradation of RT translation factors on stalled ribosomes."; RL Cell 0:0-0(2023). RN [16] RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND MUTAGENESIS OF CYS-220. RX PubMed=37651229; DOI=10.1016/j.celrep.2023.113056; RA Gurzeler L.A., Link M., Ibig Y., Schmidt I., Galuba O., Schoenbett J., RA Gasser-Didierlaurant C., Parker C.N., Mao X., Bitsch F., Schirle M., RA Couttet P., Sigoillot F., Ziegelmueller J., Uldry A.C., Teodorowicz W., RA Schmiedeberg N., Muehlemann O., Reinhardt J.; RT "Drug-induced eRF1 degradation promotes readthrough and reveals a new RT branch of ribosome quality control."; RL Cell Rep. 42:113056-113056(2023). RN [17] RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY. RX PubMed=37951215; DOI=10.1016/j.molcel.2023.10.011; RA Suryo Rahmanto A., Blum C.J., Scalera C., Heidelberger J.B., Mesitov M., RA Horn-Ghetko D., Graef J.F., Mikicic I., Hobrecht R., Orekhova A., RA Ostermaier M., Ebersberger S., Moeckel M.M., Krapoth N., RA Da Silva Fernandes N., Mizi A., Zhu Y., Chen J.X., Choudhary C., RA Papantonis A., Ulrich H.D., Schulman B.A., Koenig J., Beli P.; RT "K6-linked ubiquitylation marks formaldehyde-induced RNA-protein crosslinks RT for resolution."; RL Mol. Cell 0:0-0(2023). RN [18] RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY. RX PubMed=37951216; DOI=10.1016/j.molcel.2023.10.012; RA Zhao S., Cordes J., Caban K.M., Goetz M.J., Mackens-Kiani T., Veltri A.J., RA Sinha N.K., Weickert P., Kaya S., Hewitt G., Nedialkova D.D., Froehlich T., RA Beckmann R., Buskirk A.R., Green R., Stingele J.; RT "RNF14-dependent atypical ubiquitylation promotes translation-coupled RT resolution of RNA-protein crosslinks."; RL Mol. Cell 0:0-0(2023). CC -!- FUNCTION: E3 ubiquitin-protein ligase that plays a key role in the CC RNF14-RNF25 translation quality control pathway, a pathway that takes CC place when a ribosome has stalled during translation, and which CC promotes ubiquitination and degradation of translation factors on CC stalled ribosomes (PubMed:36638793, PubMed:37651229, PubMed:37951215, CC PubMed:37951216). Recruited to stalled ribosomes by the ribosome CC collision sensor GCN1 and mediates 'Lys-6'-linked ubiquitination of CC target proteins, leading to their degradation (PubMed:36638793, CC PubMed:37651229, PubMed:37951215, PubMed:37951216). Mediates CC ubiquitination of EEF1A1/eEF1A and ETF1/eRF1 translation factors on CC stalled ribosomes, leading to their degradation (PubMed:36638793, CC PubMed:37651229). Also catalyzes ubiquitination of ribosomal proteins CC RPL0, RPL1, RPL12, RPS13 and RPS17 (PubMed:36638793). Specifically CC required to resolve RNA-protein cross-links caused by reactive CC aldehydes, which trigger translation stress by stalling ribosomes: acts CC by catalying 'Lys-6'-linked ubiquitination of RNA-protein cross-links, CC leading to their removal by the ATP-dependent unfoldase VCP and CC subsequent degradation by the proteasome (PubMed:37951215, CC PubMed:37951216). Independently of its function in the response to CC stalled ribosomes, acts as a regulator of transcription in Wnt CC signaling via its interaction with TCF transcription factors CC (TCF7/TCF1, TCF7L1/TCF3 and TCF7L2/TCF4) (PubMed:23449499). May also CC play a role as a coactivator for androgen- and, to a lesser extent, CC progesterone-dependent transcription (PubMed:19345326). CC {ECO:0000269|PubMed:19345326, ECO:0000269|PubMed:23449499, CC ECO:0000269|PubMed:36638793, ECO:0000269|PubMed:37651229, CC ECO:0000269|PubMed:37951215, ECO:0000269|PubMed:37951216}. 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:0000269|PubMed:36638793, CC ECO:0000269|PubMed:37651229, ECO:0000269|PubMed:37951215, CC ECO:0000269|PubMed:37951216}; CC -!- PATHWAY: Protein modification; protein ubiquitination. CC {ECO:0000269|PubMed:36638793, ECO:0000269|PubMed:37651229, CC ECO:0000269|PubMed:37951215, ECO:0000269|PubMed:37951216}. CC -!- SUBUNIT: Interacts with GCN1; interaction takes place in response to CC ribosome collisions and is required for ubiquitination of EEF1A1/eEF1A CC (PubMed:36638793). Interacts with the ubiquitin-conjugating enzymes CC UBE2E1 and UBE2E2 (PubMed:11322894). Interacts with AR/androgen CC receptor (PubMed:10085091, PubMed:19345326). Interacts with TCF7/TCF1, CC TCF7L1/TCF3 and TCF7L2/TCF4; promoting Wnt signaling (PubMed:23449499). CC {ECO:0000269|PubMed:10085091, ECO:0000269|PubMed:11322894, CC ECO:0000269|PubMed:19345326, ECO:0000269|PubMed:23449499, CC ECO:0000269|PubMed:36638793}. CC -!- INTERACTION: CC Q9UBS8; P10275: AR; NbExp=2; IntAct=EBI-2130308, EBI-608057; CC Q9UBS8; Q9UI36-2: DACH1; NbExp=6; IntAct=EBI-2130308, EBI-10186082; CC Q9UBS8; P28799: GRN; NbExp=3; IntAct=EBI-2130308, EBI-747754; CC Q9UBS8; O60260-5: PRKN; NbExp=3; IntAct=EBI-2130308, EBI-21251460; CC Q9UBS8; Q9Y3C5: RNF11; NbExp=3; IntAct=EBI-2130308, EBI-396669; CC Q9UBS8; Q13148: TARDBP; NbExp=3; IntAct=EBI-2130308, EBI-372899; CC Q9UBS8; P51668: UBE2D1; NbExp=4; IntAct=EBI-2130308, EBI-743540; CC Q9UBS8; Q9Y2X8: UBE2D4; NbExp=5; IntAct=EBI-2130308, EBI-745527; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9853615}. Nucleus CC {ECO:0000269|PubMed:9853615}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q9UBS8-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9UBS8-2; Sequence=VSP_045780; CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:10085091}. CC -!- DOMAIN: The N-terminal destruction box (D-box) acts as a recognition CC signal for degradation via the ubiquitin-proteasome pathway. CC {ECO:0000305|PubMed:11322894}. CC -!- DOMAIN: Members of the RBR family are atypical E3 ligases. They CC interact with the E2 conjugating enzyme UBE2L3 and function like HECT- CC type E3 enzymes: they bind E2s via the first RING domain, but require CC an obligate trans-thiolation step during the ubiquitin transfer, CC requiring a conserved cysteine residue in the second RING domain. CC {ECO:0000250|UniProtKB:O60260}. CC -!- PTM: RING-type zinc finger-dependent and UBE2E2-dependent CC autoubiquitination. {ECO:0000269|PubMed:11322894}. CC -!- SIMILARITY: Belongs to the RBR family. RNF14 subfamily. {ECO:0000305}. CC -!- CAUTION: Lacks the His residue in the RING-type domain 2 that is one of CC the conserved features of the family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AB022663; BAA78677.1; -; mRNA. DR EMBL; AF060544; AAD21842.1; -; mRNA. DR EMBL; AK023884; BAG51234.1; -; mRNA. DR EMBL; AK057868; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; CR456702; CAG32983.1; -; mRNA. DR EMBL; AC005740; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471062; EAW61895.1; -; Genomic_DNA. DR EMBL; CH471062; EAW61896.1; -; Genomic_DNA. DR EMBL; CH471062; EAW61897.1; -; Genomic_DNA. DR EMBL; BC126185; AAI26186.1; -; mRNA. DR EMBL; BC144061; AAI44062.1; -; mRNA. DR EMBL; AB015333; BAA34792.1; -; mRNA. DR CCDS; CCDS4270.1; -. [Q9UBS8-1] DR CCDS; CCDS4271.1; -. [Q9UBS8-2] DR RefSeq; NP_001188294.1; NM_001201365.2. [Q9UBS8-1] DR RefSeq; NP_004281.1; NM_004290.5. [Q9UBS8-1] DR RefSeq; NP_899645.1; NM_183398.3. [Q9UBS8-2] DR RefSeq; NP_899646.1; NM_183399.3. [Q9UBS8-1] DR RefSeq; NP_899647.1; NM_183400.3. [Q9UBS8-1] DR RefSeq; NP_899648.1; NM_183401.3. [Q9UBS8-1] DR RefSeq; XP_011536016.1; XM_011537714.4. [Q9UBS8-1] DR RefSeq; XP_047273854.1; XM_047417898.1. [Q9UBS8-1] DR RefSeq; XP_047273855.1; XM_047417899.1. [Q9UBS8-1] DR RefSeq; XP_047273856.1; XM_047417900.1. [Q9UBS8-1] DR RefSeq; XP_047273857.1; XM_047417901.1. [Q9UBS8-1] DR RefSeq; XP_047273858.1; XM_047417902.1. [Q9UBS8-1] DR RefSeq; XP_047273859.1; XM_047417903.1. [Q9UBS8-1] DR RefSeq; XP_047273860.1; XM_047417904.1. [Q9UBS8-1] DR RefSeq; XP_047273861.1; XM_047417905.1. [Q9UBS8-1] DR RefSeq; XP_054209813.1; XM_054353838.1. [Q9UBS8-1] DR RefSeq; XP_054209814.1; XM_054353839.1. [Q9UBS8-1] DR RefSeq; XP_054209815.1; XM_054353840.1. [Q9UBS8-1] DR RefSeq; XP_054209816.1; XM_054353841.1. [Q9UBS8-1] DR RefSeq; XP_054209817.1; XM_054353842.1. [Q9UBS8-1] DR RefSeq; XP_054209818.1; XM_054353843.1. [Q9UBS8-1] DR RefSeq; XP_054209819.1; XM_054353844.1. [Q9UBS8-1] DR RefSeq; XP_054209820.1; XM_054353845.1. [Q9UBS8-1] DR RefSeq; XP_054209821.1; XM_054353846.1. [Q9UBS8-1] DR AlphaFoldDB; Q9UBS8; -. DR BioGRID; 114968; 45. DR CORUM; Q9UBS8; -. DR FunCoup; Q9UBS8; 1988. DR IntAct; Q9UBS8; 27. DR MINT; Q9UBS8; -. DR STRING; 9606.ENSP00000324956; -. DR GlyGen; Q9UBS8; 2 sites, 1 O-linked glycan (1 site). DR iPTMnet; Q9UBS8; -. DR PhosphoSitePlus; Q9UBS8; -. DR BioMuta; RNF14; -. DR DMDM; 17380293; -. DR jPOST; Q9UBS8; -. DR MassIVE; Q9UBS8; -. DR PaxDb; 9606-ENSP00000378028; -. DR PeptideAtlas; Q9UBS8; -. DR ProteomicsDB; 2057; -. DR ProteomicsDB; 84052; -. [Q9UBS8-1] DR Pumba; Q9UBS8; -. DR Antibodypedia; 1304; 265 antibodies from 30 providers. DR DNASU; 9604; -. DR Ensembl; ENST00000347642.7; ENSP00000324956.3; ENSG00000013561.19. [Q9UBS8-1] DR Ensembl; ENST00000356143.5; ENSP00000348462.1; ENSG00000013561.19. [Q9UBS8-1] DR Ensembl; ENST00000394514.6; ENSP00000378022.2; ENSG00000013561.19. [Q9UBS8-2] DR Ensembl; ENST00000394519.5; ENSP00000378027.1; ENSG00000013561.19. [Q9UBS8-1] DR Ensembl; ENST00000394520.7; ENSP00000378028.2; ENSG00000013561.19. [Q9UBS8-1] DR GeneID; 9604; -. DR KEGG; hsa:9604; -. DR MANE-Select; ENST00000394520.7; ENSP00000378028.2; NM_004290.5; NP_004281.1. DR UCSC; uc003lly.4; human. [Q9UBS8-1] DR AGR; HGNC:10058; -. DR ClinPGx; PA34423; -. DR CTD; 9604; -. DR DisGeNET; 9604; -. DR GeneCards; RNF14; -. DR HGNC; HGNC:10058; RNF14. DR HPA; ENSG00000013561; Low tissue specificity. DR MalaCards; RNF14; -. DR MIM; 605675; gene. DR OpenTargets; ENSG00000013561; -. DR VEuPathDB; HostDB:ENSG00000013561; -. DR eggNOG; KOG1814; Eukaryota. DR GeneTree; ENSGT00940000154507; -. DR HOGENOM; CLU_021364_2_0_1; -. DR InParanoid; Q9UBS8; -. DR OMA; PRSWCQG; -. DR OrthoDB; 1431934at2759; -. DR PAN-GO; Q9UBS8; 7 GO annotations based on evolutionary models. DR PhylomeDB; Q9UBS8; -. DR PathwayCommons; Q9UBS8; -. DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation. DR SignaLink; Q9UBS8; -. DR SIGNOR; Q9UBS8; -. DR UniPathway; UPA00143; -. DR Agora; ENSG00000013561; -. DR BioGRID-ORCS; 9604; 253 hits in 1174 CRISPR screens. DR ChiTaRS; RNF14; human. DR GeneWiki; RNF14; -. DR GenomeRNAi; 9604; -. DR Pharos; Q9UBS8; Tbio. DR PRO; PR:Q9UBS8; -. DR Proteomes; UP000005640; Chromosome 5. DR RNAct; Q9UBS8; protein. DR Bgee; ENSG00000013561; Expressed in adrenal tissue and 207 other cell types or tissues. DR ExpressionAtlas; Q9UBS8; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0022626; C:cytosolic ribosome; IDA:UniProt. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0000151; C:ubiquitin ligase complex; IBA:GO_Central. DR GO; GO:0050681; F:nuclear androgen receptor binding; IPI:UniProtKB. DR GO; GO:0003713; F:transcription coactivator activity; TAS:UniProtKB. DR GO; GO:0031624; F:ubiquitin conjugating enzyme binding; IBA:GO_Central. DR GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:UniProtKB. DR GO; GO:0019787; F:ubiquitin-like protein transferase activity; IDA:UniProtKB. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW. DR GO; GO:0030521; P:androgen receptor signaling pathway; NAS:UniProtKB. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; IDA:UniProtKB. DR GO; GO:0085020; P:protein K6-linked ubiquitination; IDA:UniProtKB. DR GO; GO:0016567; P:protein ubiquitination; IEP:UniProtKB. DR GO; GO:0160127; P:protein-RNA covalent cross-linking repair; IDA:UniProtKB. DR GO; GO:0060765; P:regulation of androgen receptor signaling pathway; IDA:UniProtKB. DR GO; GO:0060828; P:regulation of canonical Wnt signaling pathway; IDA:UniProtKB. DR GO; GO:0006355; P:regulation of DNA-templated transcription; IDA:UniProtKB. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; TAS:UniProtKB. DR GO; GO:0072344; P:rescue of stalled ribosome; IDA:UniProtKB. DR GO; GO:0007165; P:signal transduction; TAS:UniProtKB. DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IDA:UniProt. 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 1: Evidence at protein level; KW Alternative splicing; Coiled coil; Cytoplasm; Metal-binding; Nucleus; KW Phosphoprotein; Proteomics identification; Reference proteome; Repeat; KW Transcription; Transcription regulation; Transferase; Ubl conjugation; KW Ubl conjugation pathway; Zinc; Zinc-finger. FT CHAIN 1..474 FT /note="E3 ubiquitin-protein ligase RNF14" FT /id="PRO_0000056057" FT DOMAIN 11..137 FT /note="RWD" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00179" FT ZN_FING 220..270 FT /note="RING-type 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221" FT ZN_FING 289..350 FT /note="IBR-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221" FT ZN_FING 404..433 FT /note="RING-type 2; atypical" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221" FT REGION 216..457 FT /note="TRIAD supradomain" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221" FT REGION 361..474 FT /note="Interaction with androgen receptor" FT /evidence="ECO:0000269|PubMed:19345326" FT COILED 351..395 FT /evidence="ECO:0000255" FT MOTIF 37..45 FT /note="D-box" FT /evidence="ECO:0000269|PubMed:11322894" FT ACT_SITE 417 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221, FT ECO:0000305|PubMed:36638793" FT BINDING 220 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221" FT BINDING 223 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221" FT BINDING 238 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221" FT BINDING 240 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221" FT BINDING 243 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221" FT BINDING 246 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221" FT BINDING 265 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221" FT BINDING 270 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221" FT BINDING 309 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221" FT BINDING 314 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221" FT BINDING 329 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221" FT BINDING 332 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221" FT BINDING 337 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221" FT BINDING 340 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221" FT BINDING 345 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221" FT BINDING 350 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221" FT BINDING 404 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221" FT BINDING 407 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221" FT BINDING 422 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221" FT BINDING 425 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221" FT BINDING 430 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="6" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221" FT BINDING 433 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="6" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221" FT BINDING 445 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="6" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221" FT BINDING 453 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="6" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221" FT MOD_RES 348 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163" FT VAR_SEQ 1..126 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_045780" FT MUTAGEN 220 FT /note="C->S: Abolished E3 ubiquitin-protein ligase FT activity. Loss of interaction with UBE2E2 and of FT autoubiquitination." FT /evidence="ECO:0000269|PubMed:11322894, FT ECO:0000269|PubMed:37651229" FT MUTAGEN 417 FT /note="C->A: Abolished E3 ubiquitin-protein ligase FT activity." FT /evidence="ECO:0000269|PubMed:36638793" FT CONFLICT 32 FT /note="Q -> R (in Ref. 4; CAG32983)" FT /evidence="ECO:0000305" SQ SEQUENCE 474 AA; 53837 MW; 529E3F5AF38A5DAD CRC64; MSSEDREAQE DELLALASIY DGDEFRKAES VQGGETRIYL DLPQNFKIFV SGNSNECLQN SGFEYTICFL PPLVLNFELP PDYPSSSPPS FTLSGKWLSP TQLSALCKHL DNLWEEHRGS VVLFAWMQFL KEETLAYLNI VSPFELKIGS QKKVQRRTAQ ASPNTELDFG GAAGSDVDQE EIVDERAVQD VESLSNLIQE ILDFDQAQQI KCFNSKLFLC SICFCEKLGS ECMYFLECRH VYCKACLKDY FEIQIRDGQV QCLNCPEPKC PSVATPGQVK ELVEAELFAR YDRLLLQSSL DLMADVVYCP RPCCQLPVMQ EPGCTMGICS SCNFAFCTLC RLTYHGVSPC KVTAEKLMDL RNEYLQADEA NKRLLDQRYG KRVIQKALEE MESKEWLEKN SKSCPCCGTP IEKLDGCNKM TCTGCMQYFC WICMGSLSRA NPYKHFNDPG SPCFNRLFYA VDVDDDIWED EVED //