RN114_MOUSE
ID RN114_MOUSE Reviewed; 229 AA.
AC Q9ET26; Q3UFU8; Q8K5A2;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 03-JUL-2003, sequence version 2.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=E3 ubiquitin-protein ligase RNF114;
DE EC=2.3.2.27 {ECO:0000250|UniProtKB:Q9Y508};
DE AltName: Full=RING finger protein 114;
DE AltName: Full=RING-type E3 ubiquitin transferase RNF114 {ECO:0000305};
DE AltName: Full=Zinc finger protein 228;
DE AltName: Full=Zinc finger protein 313;
GN Name=Rnf114; Synonyms=Zfp228, Zfp313, Znf228, Znf313;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Kunming; TISSUE=Testis;
RA Zhang S., Ma Y.-X., Xia Q., Xiao C., Zhang G.;
RT "Cloning of mouse homolog of human zinc finger-like gene ZNF228 possibly
RT associated with spermatogenesis.";
RL Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Aorta, Bone marrow, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, and Mammary tumor;
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Liver, Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=28625874; DOI=10.1016/j.cyto.2017.05.002;
RA Lin B., Ke Q., Li H., Pheifer N.S., Velliquette D.C., Leaman D.W.;
RT "Negative regulation of the RLH signaling by the E3 ubiquitin ligase
RT RNF114.";
RL Cytokine 99:186-193(2017).
CC -!- FUNCTION: E3 ubiquitin-protein ligase that promotes the ubiquitination
CC of various substrates. In turn, participates in the regulation of many
CC biological processes including cell cycle, apoptosis,
CC osteoclastogenesis as well as innate or adaptive immunity. Acts as
CC negative regulator of NF-kappa-B-dependent transcription by promoting
CC the ubiquitination and stabilization of the NF-kappa-B inhibitor
CC TNFAIP3. May promote the ubiquitination of TRAF6 as well. Acts also as
CC a negative regulator of T-cell activation. Inhibits cellular dsRNA
CC responses and interferon production by targeting MAVS component for
CC proteasomal degradation. Ubiquitinates the CDK inhibitor CDKN1A leading
CC to its degradationand probably also CDKN1B and CDKN1C. This activity
CC stimulates cell cycle G1-to-S phase transition and suppresses cellular
CC senescence. May play a role in spermatogenesis.
CC {ECO:0000250|UniProtKB:Q9Y508}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27; Evidence={ECO:0000250|UniProtKB:Q9Y508};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000250|UniProtKB:Q9Y508}.
CC -!- SUBUNIT: Interacts with XAF1, the interaction increases XAF1 stability
CC and proapoptotic effects, and may regulate IFN signaling.
CC {ECO:0000250|UniProtKB:Q9Y508}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9Y508}. Nucleus
CC {ECO:0000250|UniProtKB:Q9Y508}.
CC -!- PTM: Autoubiquitinated. Polyubiquitinated in the presence of E2 enzymes
CC UBE2D1, UBE2D2 and UBE2D3, but only monoubiquitinated in the presence
CC of UBE2E1. {ECO:0000250|UniProtKB:Q9Y508}.
CC -!- DISRUPTION PHENOTYPE: Mice show no significant difference of viral
CC resistance or augmented antiviral responses compared to WT when both
CC are infected with virus. {ECO:0000269|PubMed:28625874}.
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DR EMBL; AF282919; AAG01141.2; -; mRNA.
DR EMBL; AF502145; AAM22210.1; -; mRNA.
DR EMBL; AK088441; BAC40355.1; -; mRNA.
DR EMBL; AK139030; BAE23870.1; -; mRNA.
DR EMBL; AK148290; BAE28461.1; -; mRNA.
DR EMBL; AK148392; BAE28527.1; -; mRNA.
DR EMBL; AK150086; BAE29295.1; -; mRNA.
DR EMBL; AK150263; BAE29420.1; -; mRNA.
DR EMBL; AK152687; BAE31418.1; -; mRNA.
DR EMBL; AK153452; BAE32006.1; -; mRNA.
DR EMBL; AK159818; BAE35398.1; -; mRNA.
DR EMBL; BC054416; AAH54416.1; -; mRNA.
DR EMBL; BC085146; AAH85146.1; -; mRNA.
DR CCDS; CCDS17101.1; -.
DR RefSeq; NP_109668.2; NM_030743.5.
DR RefSeq; XP_006500502.1; XM_006500439.1.
DR AlphaFoldDB; Q9ET26; -.
DR BioGRID; 219874; 7.
DR STRING; 10090.ENSMUSP00000077197; -.
DR iPTMnet; Q9ET26; -.
DR PhosphoSitePlus; Q9ET26; -.
DR REPRODUCTION-2DPAGE; Q9ET26; -.
DR EPD; Q9ET26; -.
DR MaxQB; Q9ET26; -.
DR PaxDb; Q9ET26; -.
DR PeptideAtlas; Q9ET26; -.
DR PRIDE; Q9ET26; -.
DR ProteomicsDB; 300525; -.
DR Antibodypedia; 13722; 184 antibodies from 24 providers.
DR DNASU; 81018; -.
DR Ensembl; ENSMUST00000078050; ENSMUSP00000077197; ENSMUSG00000006418.
DR Ensembl; ENSMUST00000109214; ENSMUSP00000104837; ENSMUSG00000006418.
DR GeneID; 81018; -.
DR KEGG; mmu:81018; -.
DR UCSC; uc008nzv.1; mouse.
DR CTD; 55905; -.
DR MGI; MGI:1933159; Rnf114.
DR VEuPathDB; HostDB:ENSMUSG00000006418; -.
DR eggNOG; ENOG502QW3F; Eukaryota.
DR GeneTree; ENSGT00950000182909; -.
DR HOGENOM; CLU_092448_1_0_1; -.
DR InParanoid; Q9ET26; -.
DR OMA; DYIEEGV; -.
DR OrthoDB; 1097558at2759; -.
DR PhylomeDB; Q9ET26; -.
DR TreeFam; TF331012; -.
DR Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 81018; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Rnf114; mouse.
DR PRO; PR:Q9ET26; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q9ET26; protein.
DR Bgee; ENSMUSG00000006418; Expressed in animal zygote and 250 other tissues.
DR ExpressionAtlas; Q9ET26; baseline and differential.
DR Genevisible; Q9ET26; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR CDD; cd16540; RING-HC_RNF114; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR008598; Di19_Zn-bd.
DR InterPro; IPR042716; RNF114_RING-HC.
DR InterPro; IPR034734; ZF_C2HC_RNF.
DR InterPro; IPR027370; Znf-RING_LisH.
DR InterPro; IPR013087; Znf_C2H2_type.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR Pfam; PF05605; zf-Di19; 1.
DR Pfam; PF13445; zf-RING_UBOX; 1.
DR Pfam; PF18574; zf_C2HC_14; 1.
DR SMART; SM00184; RING; 1.
DR SMART; SM00355; ZnF_C2H2; 2.
DR PROSITE; PS51803; ZF_C2HC_RNF; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Developmental protein; Differentiation;
KW Metal-binding; Nucleus; Reference proteome; Spermatogenesis; Transferase;
KW Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..229
FT /note="E3 ubiquitin-protein ligase RNF114"
FT /id="PRO_0000056308"
FT ZN_FING 30..69
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 92..111
FT /note="C2HC RNF-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01144"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 92
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01144"
FT BINDING 95
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01144"
FT BINDING 107
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01144"
FT BINDING 111
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01144"
FT MOD_RES 103
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y508"
FT MOD_RES 113
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y508"
SQ SEQUENCE 229 AA; 25745 MW; 7E500B9687EA0DD8 CRC64;
MAAAQPESRD GAAQSAKPAS ETDPLSRFTC PVCLEVFEKP VQVPCGHVFC SACLQECLKP
KKPVCGVCRS ALAPGVRAVE LERQIESIET SCHGCRKNFI LSKIRAHVTS CSKYQNYIME
GVKATTKDAS LQPRNIPNRY TFPCPYCPEK NFDQEGLVEH CKLTHSTDTK SVVCPICASM
PWGDPSYRSA NFMEHIQRRH RFSYDTFVDY DVDEDDMINQ VLQRSIIDQ
