RN114_HUMAN
ID RN114_HUMAN Reviewed; 228 AA.
AC Q9Y508; B2RDQ9; B4DWY5; E1P627; Q6N0B0;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=E3 ubiquitin-protein ligase RNF114;
DE EC=2.3.2.27 {ECO:0000269|PubMed:23645206};
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=ZNF228, ZNF313;
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=Testis;
RX PubMed=12621547;
RA Ma Y.-X., Zhang S., Hou Y., Huang X., Wu Q., Sun Y.;
RT "Identification of a novel human zinc finger protein gene ZNF313.";
RL Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao 35:230-237(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Endometrial tumor;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Synovium, and Testis;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
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).
RC TISSUE=Brain, and Ovary;
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 TISSUE SPECIFICITY.
RX PubMed=18364390; DOI=10.1093/hmg/ddn091;
RA Capon F., Bijlmakers M.-J., Wolf N., Quaranta M., Huffmeier U., Allen M.,
RA Timms K., Abkevich V., Gutin A., Smith R., Warren R.B., Young H.S.,
RA Worthington J., Burden A.D., Griffiths C.E.M., Hayday A., Nestle F.O.,
RA Reis A., Lanchbury J., Barker J.N., Trembath R.C.;
RT "Identification of ZNF313/RNF114 as a novel psoriasis susceptibility
RT gene.";
RL Hum. Mol. Genet. 17:1938-1945(2008).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-102 AND LYS-112, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [11]
RP FUNCTION, UBIQUITINATION, SUBCELLULAR LOCATION, INTERACTION WITH XAF1,
RP CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=23645206; DOI=10.1038/cdd.2013.33;
RA Han J., Kim Y.L., Lee K.W., Her N.G., Ha T.K., Yoon S., Jeong S.I.,
RA Lee J.H., Kang M.J., Lee M.G., Ryu B.K., Baik J.H., Chi S.G.;
RT "ZNF313 is a novel cell cycle activator with an E3 ligase activity
RT inhibiting cellular senescence by destabilizing p21(WAF1.).";
RL Cell Death Differ. 20:1055-1067(2013).
RN [12]
RP FUNCTION.
RX PubMed=25165885; DOI=10.1038/cddis.2014.366;
RA Rodriguez M.S., Egana I., Lopitz-Otsoa F., Aillet F., Lopez-Mato M.P.,
RA Dorronsoro A., Dorronroso A., Lobato-Gil S., Sutherland J.D., Barrio R.,
RA Trigueros C., Lang V.;
RT "The RING ubiquitin E3 RNF114 interacts with A20 and modulates NF-kappaB
RT activity and T-cell activation.";
RL Cell Death Dis. 5:E1399-E1399(2014).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [14]
RP FUNCTION.
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).
RN [15]
RP FUNCTION.
RX PubMed=28708287; DOI=10.1002/jor.23654;
RA Lin B., Ke Q., Leaman D.W., Goel V., Agarwal A.;
RT "Regulation of RANKL-induced osteoclastogenesis by RING finger protein
RT RNF114.";
RL J. Orthop. Res. 36:159-166(2018).
CC -!- FUNCTION: E3 ubiquitin-protein ligase that promotes the ubiquitination
CC of various substrates (PubMed:23645206, PubMed:25165885). In turn,
CC participates in the regulation of many biological processes including
CC cell cycle, apoptosis, osteoclastogenesis as well as innate or adaptive
CC immunity (PubMed:25165885, PubMed:28708287). Acts as negative regulator
CC of NF-kappa-B-dependent transcription by promoting the ubiquitination
CC and stabilization of the NF-kappa-B inhibitor TNFAIP3
CC (PubMed:25165885). May promote the ubiquitination of TRAF6 as well
CC (PubMed:28708287). Acts also as a negative regulator of T-cell
CC activation (PubMed:25165885). Inhibits cellular dsRNA responses and
CC interferon production by targeting MAVS component for proteasomal
CC degradation (PubMed:25165885). Ubiquitinates the CDK inhibitor CDKN1A
CC leading to its degradationand probably also CDKN1B and CDKN1C
CC (PubMed:23645206). This activity stimulates cell cycle G1-to-S phase
CC transition and suppresses cellular senescence. May play a role in
CC spermatogenesis. {ECO:0000269|PubMed:23645206,
CC ECO:0000269|PubMed:25165885, ECO:0000269|PubMed:28625874,
CC ECO:0000269|PubMed:28708287}.
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:0000269|PubMed:23645206};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000269|PubMed:23645206}.
CC -!- SUBUNIT: Interacts with XAF1, the interaction increases XAF1 stability
CC and proapoptotic effects, and may regulate IFN signaling.
CC {ECO:0000269|PubMed:23645206}.
CC -!- INTERACTION:
CC Q9Y508; Q92993: KAT5; NbExp=3; IntAct=EBI-723587, EBI-399080;
CC Q9Y508; Q8TAP4-4: LMO3; NbExp=3; IntAct=EBI-723587, EBI-11742507;
CC Q9Y508; Q15047-2: SETDB1; NbExp=3; IntAct=EBI-723587, EBI-9090795;
CC Q9Y508; P61086: UBE2K; NbExp=3; IntAct=EBI-723587, EBI-473850;
CC Q9Y508; Q6GPH4: XAF1; NbExp=7; IntAct=EBI-723587, EBI-2815120;
CC Q9Y508; P61981: YWHAG; NbExp=3; IntAct=EBI-723587, EBI-359832;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23645206}. Nucleus
CC {ECO:0000269|PubMed:23645206}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9Y508-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Y508-2; Sequence=VSP_036843, VSP_036844;
CC -!- TISSUE SPECIFICITY: Expressed in numerous tissues, including skin, CD4
CC lymphocytes and dendritic cells. Highest levels in testis.
CC {ECO:0000269|PubMed:18364390}.
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:0000269|PubMed:23645206}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAE45709.1; Type=Erroneous initiation; Evidence={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; AF265215; AAF75763.1; -; mRNA.
DR EMBL; BX640603; CAE45709.1; ALT_INIT; mRNA.
DR EMBL; BT006795; AAP35441.1; -; mRNA.
DR EMBL; AK315638; BAG38006.1; -; mRNA.
DR EMBL; AK301731; BAG63197.1; -; mRNA.
DR EMBL; AL031685; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471077; EAW75641.1; -; Genomic_DNA.
DR EMBL; CH471077; EAW75643.1; -; Genomic_DNA.
DR EMBL; BC013695; AAH13695.1; -; mRNA.
DR EMBL; BC066919; AAH66919.1; -; mRNA.
DR CCDS; CCDS33482.1; -. [Q9Y508-1]
DR RefSeq; NP_061153.1; NM_018683.3. [Q9Y508-1]
DR AlphaFoldDB; Q9Y508; -.
DR BioGRID; 120991; 87.
DR IntAct; Q9Y508; 44.
DR MINT; Q9Y508; -.
DR STRING; 9606.ENSP00000244061; -.
DR iPTMnet; Q9Y508; -.
DR PhosphoSitePlus; Q9Y508; -.
DR BioMuta; RNF114; -.
DR DMDM; 20141070; -.
DR EPD; Q9Y508; -.
DR jPOST; Q9Y508; -.
DR MassIVE; Q9Y508; -.
DR MaxQB; Q9Y508; -.
DR PaxDb; Q9Y508; -.
DR PeptideAtlas; Q9Y508; -.
DR PRIDE; Q9Y508; -.
DR ProteomicsDB; 86269; -. [Q9Y508-1]
DR ProteomicsDB; 86270; -. [Q9Y508-2]
DR TopDownProteomics; Q9Y508-1; -. [Q9Y508-1]
DR Antibodypedia; 13722; 184 antibodies from 24 providers.
DR DNASU; 55905; -.
DR Ensembl; ENST00000244061.6; ENSP00000244061.2; ENSG00000124226.11. [Q9Y508-1]
DR GeneID; 55905; -.
DR KEGG; hsa:55905; -.
DR MANE-Select; ENST00000244061.6; ENSP00000244061.2; NM_018683.4; NP_061153.1.
DR UCSC; uc002xux.4; human. [Q9Y508-1]
DR CTD; 55905; -.
DR DisGeNET; 55905; -.
DR GeneCards; RNF114; -.
DR HGNC; HGNC:13094; RNF114.
DR HPA; ENSG00000124226; Tissue enhanced (testis).
DR MalaCards; RNF114; -.
DR MIM; 612451; gene.
DR neXtProt; NX_Q9Y508; -.
DR OpenTargets; ENSG00000124226; -.
DR PharmGKB; PA162401502; -.
DR VEuPathDB; HostDB:ENSG00000124226; -.
DR eggNOG; ENOG502QW3F; Eukaryota.
DR GeneTree; ENSGT00950000182909; -.
DR HOGENOM; CLU_092448_1_0_1; -.
DR InParanoid; Q9Y508; -.
DR OMA; DYIEEGV; -.
DR OrthoDB; 1097558at2759; -.
DR PhylomeDB; Q9Y508; -.
DR TreeFam; TF331012; -.
DR PathwayCommons; Q9Y508; -.
DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR SignaLink; Q9Y508; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 55905; 22 hits in 1121 CRISPR screens.
DR ChiTaRS; RNF114; human.
DR GenomeRNAi; 55905; -.
DR Pharos; Q9Y508; Tbio.
DR PRO; PR:Q9Y508; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; Q9Y508; protein.
DR Bgee; ENSG00000124226; Expressed in oocyte and 203 other tissues.
DR ExpressionAtlas; Q9Y508; baseline and differential.
DR Genevisible; Q9Y508; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
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; 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 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; Alternative splicing; Cytoplasm; Developmental protein;
KW Differentiation; Metal-binding; Nucleus; Reference proteome;
KW Spermatogenesis; Transferase; Ubl conjugation; Ubl conjugation pathway;
KW Zinc; Zinc-finger.
FT CHAIN 1..228
FT /note="E3 ubiquitin-protein ligase RNF114"
FT /id="PRO_0000056307"
FT ZN_FING 29..68
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 91..110
FT /note="C2HC RNF-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01144"
FT BINDING 91
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01144"
FT BINDING 94
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01144"
FT BINDING 106
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01144"
FT BINDING 110
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01144"
FT MOD_RES 102
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 112
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT VAR_SEQ 173..191
FT /note="CPICASMPWGDPNYRSANF -> SEQSPCLLSVSCYRASITY (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_036843"
FT VAR_SEQ 192..228
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_036844"
FT CONFLICT 13
FT /note="Q -> H (in Ref. 2; CAE45709)"
FT /evidence="ECO:0000305"
FT CONFLICT 20
FT /note="E -> K (in Ref. 2; CAE45709)"
FT /evidence="ECO:0000305"
FT CONFLICT 34
FT /note="E -> V (in Ref. 2; CAE45709)"
FT /evidence="ECO:0000305"
FT CONFLICT 205
FT /note="T -> A (in Ref. 2; CAE45709)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 228 AA; 25694 MW; DF5A962B1EC13A21 CRC64;
MAAQQRDCGG AAQLAGPAAE ADPLGRFTCP VCLEVYEKPV QVPCGHVFCS ACLQECLKPK
KPVCGVCRSA LAPGVRAVEL ERQIESTETS CHGCRKNFFL SKIRSHVATC SKYQNYIMEG
VKATIKDASL QPRNVPNRYT FPCPYCPEKN FDQEGLVEHC KLFHSTDTKS VVCPICASMP
WGDPNYRSAN FREHIQRRHR FSYDTFVDYD VDEEDMMNQV LQRSIIDQ
