RNF14_HUMAN
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 03-AUG-2022, entry version 197.
DE RecName: Full=E3 ubiquitin-protein ligase RNF14;
DE EC=2.3.2.31 {ECO:0000250|UniProtKB:O60260};
DE AltName: Full=Androgen receptor-associated protein 54;
DE AltName: Full=HFB30;
DE AltName: Full=RING finger protein 14;
DE AltName: Full=Triad2 protein;
GN Name=RNF14; Synonyms=ARA54; 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), AND CHARACTERIZATION.
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 MUTAGENESIS OF 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 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).
CC -!- FUNCTION: Might act as an E3 ubiquitin-protein ligase which accepts
CC ubiquitin from specific E2 ubiquitin-conjugating enzymes and then
CC transfers it to substrates, which could be nuclear proteins. Could play
CC a role as a coactivator for androgen- and, to a lesser extent,
CC progesterone-dependent transcription. {ECO:0000269|PubMed:19345326}.
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:0000250|UniProtKB:O60260};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Interacts with the ubiquitin-conjugating enzymes UBE2E1 and
CC UBE2E2. Interacts with AR/androgen receptor; testosterone- and RNF6-
CC regulated it promotes AR transcriptional activity.
CC {ECO:0000269|PubMed:19345326}.
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.
CC -!- DOMAIN: The N-terminal destruction box (D-box) acts as a recognition
CC signal for degradation via the ubiquitin-proteasome pathway.
CC {ECO:0000250}.
CC -!- DOMAIN: The RING-type zinc finger is essential for the interaction with
CC UBE2E2.
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.
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}.
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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_001201365.1. [Q9UBS8-1]
DR RefSeq; NP_004281.1; NM_004290.4. [Q9UBS8-1]
DR RefSeq; NP_899645.1; NM_183398.2. [Q9UBS8-2]
DR RefSeq; NP_899646.1; NM_183399.2. [Q9UBS8-1]
DR RefSeq; NP_899647.1; NM_183400.2. [Q9UBS8-1]
DR RefSeq; NP_899648.1; NM_183401.2. [Q9UBS8-1]
DR RefSeq; XP_005268593.1; XM_005268536.2.
DR RefSeq; XP_005268594.1; XM_005268537.2.
DR RefSeq; XP_005268596.1; XM_005268539.2. [Q9UBS8-2]
DR RefSeq; XP_005268597.1; XM_005268540.3. [Q9UBS8-2]
DR RefSeq; XP_005268598.1; XM_005268541.3. [Q9UBS8-2]
DR RefSeq; XP_011536016.1; XM_011537714.2. [Q9UBS8-1]
DR RefSeq; XP_016865559.1; XM_017010070.1.
DR RefSeq; XP_016865560.1; XM_017010071.1. [Q9UBS8-2]
DR RefSeq; XP_016865561.1; XM_017010072.1. [Q9UBS8-2]
DR AlphaFoldDB; Q9UBS8; -.
DR BioGRID; 114968; 38.
DR IntAct; Q9UBS8; 24.
DR MINT; Q9UBS8; -.
DR STRING; 9606.ENSP00000378028; -.
DR GlyGen; Q9UBS8; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9UBS8; -.
DR PhosphoSitePlus; Q9UBS8; -.
DR BioMuta; RNF14; -.
DR DMDM; 17380293; -.
DR EPD; Q9UBS8; -.
DR jPOST; Q9UBS8; -.
DR MassIVE; Q9UBS8; -.
DR MaxQB; Q9UBS8; -.
DR PaxDb; Q9UBS8; -.
DR PeptideAtlas; Q9UBS8; -.
DR PRIDE; Q9UBS8; -.
DR ProteomicsDB; 2057; -.
DR ProteomicsDB; 84052; -. [Q9UBS8-1]
DR Antibodypedia; 1304; 263 antibodies from 29 providers.
DR DNASU; 9604; -.
DR Ensembl; ENST00000347642.7; ENSP00000324956.3; ENSG00000013561.18. [Q9UBS8-1]
DR Ensembl; ENST00000356143.5; ENSP00000348462.1; ENSG00000013561.18. [Q9UBS8-1]
DR Ensembl; ENST00000394514.6; ENSP00000378022.2; ENSG00000013561.18. [Q9UBS8-2]
DR Ensembl; ENST00000394519.5; ENSP00000378027.1; ENSG00000013561.18. [Q9UBS8-1]
DR Ensembl; ENST00000394520.7; ENSP00000378028.2; ENSG00000013561.18. [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 CTD; 9604; -.
DR DisGeNET; 9604; -.
DR GeneCards; RNF14; -.
DR HGNC; HGNC:10058; RNF14.
DR HPA; ENSG00000013561; Low tissue specificity.
DR MIM; 605675; gene.
DR neXtProt; NX_Q9UBS8; -.
DR OpenTargets; ENSG00000013561; -.
DR PharmGKB; PA34423; -.
DR VEuPathDB; HostDB:ENSG00000013561; -.
DR eggNOG; KOG1814; Eukaryota.
DR GeneTree; ENSGT00940000154507; -.
DR HOGENOM; CLU_021364_2_0_1; -.
DR InParanoid; Q9UBS8; -.
DR OMA; RVAICED; -.
DR OrthoDB; 1188714at2759; -.
DR PhylomeDB; Q9UBS8; -.
DR TreeFam; TF314401; -.
DR PathwayCommons; Q9UBS8; -.
DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR SignaLink; Q9UBS8; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 9604; 250 hits in 1096 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 205 other tissues.
DR ExpressionAtlas; Q9UBS8; baseline and differential.
DR Genevisible; Q9UBS8; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; IBA:GO_Central.
DR GO; GO:0019787; F:ubiquitin-like protein transferase activity; IDA:UniProtKB.
DR GO; GO:0030521; P:androgen receptor signaling pathway; NAS:UniProtKB.
DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR GO; GO:0016567; P:protein ubiquitination; IEP:UniProtKB.
DR GO; GO:0060765; P:regulation of androgen receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; TAS:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0007165; P:signal transduction; TAS:UniProtKB.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR Gene3D; 3.10.110.10; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR031127; E3_UB_ligase_RBR.
DR InterPro; IPR002867; IBR_dom.
DR InterPro; IPR031128; RNF14.
DR InterPro; IPR006575; RWD-domain.
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; PTHR11685; 1.
DR PANTHER; PTHR11685:SF290; PTHR11685:SF290; 1.
DR Pfam; PF01485; IBR; 2.
DR Pfam; PF05773; RWD; 1.
DR SMART; SM00647; IBR; 2.
DR SMART; SM00591; RWD; 1.
DR SUPFAM; SSF54495; SSF54495; 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; Reference proteome; Repeat; Transcription;
KW 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 COILED 351..395
FT /evidence="ECO:0000255"
FT MOTIF 37..45
FT /note="D-box"
FT ACT_SITE 417
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
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: Loss of interaction with UBE2E2 and of
FT autoubiquitination."
FT /evidence="ECO:0000269|PubMed:11322894"
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
