ID RN115_HUMAN Reviewed; 304 AA. AC Q9Y4L5; A8K3Y4; Q5T2V9; Q7Z2J2; DT 12-FEB-2003, integrated into UniProtKB/Swiss-Prot. DT 07-DEC-2004, sequence version 2. DT 27-MAR-2024, entry version 168. DE RecName: Full=E3 ubiquitin-protein ligase RNF115 {ECO:0000305}; DE EC=2.3.2.27 {ECO:0000269|PubMed:18819927}; DE AltName: Full=RING finger protein 115 {ECO:0000312|HGNC:HGNC:18154}; DE AltName: Full=RING-type E3 ubiquitin transferase RNF115 {ECO:0000305}; DE AltName: Full=Rab7-interacting RING finger protein {ECO:0000250|UniProtKB:Q9D0C1}; DE Short=Rabring 7 {ECO:0000250|UniProtKB:Q9D0C1}; DE AltName: Full=Zinc finger protein 364 {ECO:0000303|Ref.1}; GN Name=RNF115 {ECO:0000312|HGNC:HGNC:18154}; GN Synonyms=ZNF364 {ECO:0000303|Ref.1}; 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]. RA Zhang D.L., Cai J.J., Ma D.L.; RT "Cloning and characterization of zinc finger protein 364, C3HC4 type RT (ZNF364), a novel human member of zinc finger protein family."; RL Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Guo J.H., She X.Y., Yu L.; RL Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 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 GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [5] 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Pancreas, and Skin; 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 [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 73-304. RC TISSUE=Uterus; RG The European IMAGE consortium; RL Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases. RN [8] RP FUNCTION, AUTOUBIQUITINATION, AND TISSUE SPECIFICITY. RX PubMed=16288031; DOI=10.1158/0008-5472.can-05-2103; RA Burger A.M., Gao Y., Amemiya Y., Kahn H.J., Kitching R., Yang Y., Sun P., RA Narod S.A., Hanna W.M., Seth A.K.; RT "A novel RING-type ubiquitin ligase breast cancer-associated gene 2 RT correlates with outcome in invasive breast cancer."; RL Cancer Res. 65:10401-10412(2005). RN [9] RP INTERACTION WITH RAB7A. RX PubMed=16925951; DOI=10.1593/neo.06469; RA Burger A., Amemiya Y., Kitching R., Seth A.K.; RT "Novel RING E3 ubiquitin ligases in breast cancer."; RL Neoplasia 8:689-695(2006). RN [10] RP FUNCTION, PATHWAY, CATALYTIC ACTIVITY, AUTOUBIQUITINATION, AND MUTAGENESIS RP OF LYS-26; LYS-32; CYS-228 AND CYS-231. RX PubMed=18819927; DOI=10.1158/1541-7786.mcr-08-0094; RA Amemiya Y., Azmi P., Seth A.; RT "Autoubiquitination of BCA2 RING E3 ligase regulates its own stability and RT affects cell migration."; RL Mol. Cancer Res. 6:1385-1396(2008). RN [11] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [12] RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH BST2, AND MUTAGENESIS OF RP CYS-228 AND CYS-231. RX PubMed=20019814; DOI=10.1371/journal.ppat.1000700; RA Miyakawa K., Ryo A., Murakami T., Ohba K., Yamaoka S., Fukuda M., RA Guatelli J., Yamamoto N.; RT "BCA2/Rabring7 promotes tetherin-dependent HIV-1 restriction."; RL PLoS Pathog. 5:e1000700-e1000700(2009). RN [13] RP FUNCTION, AND INTERACTION WITH EGFR AND FLT3. RX PubMed=23418353; DOI=10.1242/jcs.116129; RA Smith C.J., Berry D.M., McGlade C.J.; RT "The E3 ubiquitin ligases RNF126 and Rabring7 regulate endosomal sorting of RT the epidermal growth factor receptor."; RL J. Cell Sci. 126:1366-1380(2013). RN [14] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=24852021; DOI=10.1371/journal.ppat.1004151; RA Nityanandam R., Serra-Moreno R.; RT "BCA2/Rabring7 targets HIV-1 Gag for lysosomal degradation in a tetherin- RT independent manner."; RL PLoS Pathog. 10:e1004151-e1004151(2014). RN [15] RP DEUBIQUITINATION BY USP9X, AND FUNCTION. RX PubMed=30689267; DOI=10.1111/cas.13953; RA Lu Q., Lu D., Shao Z.M., Li D.Q.; RT "Deubiquitinase ubiquitin-specific protease 9X regulates the stability and RT function of E3 ubiquitin ligase ring finger protein 115 in breast cancer RT cells."; RL Cancer Sci. 110:1268-1278(2019). RN [16] RP FUNCTION, AND INTERACTION WITH STX17. RX PubMed=32980859; DOI=10.1038/s41419-020-03011-w; RA Li R., Gu Z., Zhang X., Yu J., Feng J., Lou Y., Lv P., Chen Y.; RT "RNF115 deletion inhibits autophagosome maturation and growth of gastric RT cancer."; RL Cell Death Dis. 11:810-810(2020). RN [17] RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF CYS-228 AND CYS-231. RX PubMed=33139700; DOI=10.1038/s41467-020-19318-3; RA Zhang Z.D., Xiong T.C., Yao S.Q., Wei M.C., Chen M., Lin D., Zhong B.; RT "RNF115 plays dual roles in innate antiviral responses by catalyzing RT distinct ubiquitination of MAVS and MITA."; RL Nat. Commun. 11:5536-5536(2020). RN [18] RP FUNCTION, PHOSPHORYLATION AT SER-132 AND SER-133, MUTAGENESIS OF SER-132 RP AND SER-133, INTERACTION WITH YWHAE, AND SUBCELLULAR LOCATION. RX PubMed=35343654; DOI=10.1002/advs.202105391; RA Zhang Z.D., Li H.X., Gan H., Tang Z., Guo Y.Y., Yao S.Q., Liuyu T., RA Zhong B., Lin D.; RT "RNF115 Inhibits the Post-ER Trafficking of TLRs and TLRs-Mediated Immune RT Responses by Catalyzing K11-Linked Ubiquitination of RAB1A and RAB13."; RL Adv. Sci. 9:0-0(2022). CC -!- FUNCTION: E3 ubiquitin-protein ligase that catalyzes the 'Lys- CC 48'- and/or 'Lys-63'-linked polyubiquitination of various substrates CC and thereby plays a role in a number of signaling pathways including CC autophagy, innate immunity, cell proliferation and cell death CC (PubMed:20019814, PubMed:30689267). Plays a role in the endosomal CC trafficking and degradation of membrane receptors including EGFR, FLT3, CC MET and CXCR4 through their polyubiquitination. Participates together CC with BST2 in antiviral immunity by facilitating the internalization of CC HIV-1 virions into intracellular vesicles leading to their lysosomal CC degradation (PubMed:20019814). Possesses also an antiviral activity CC independently of BST2 by promoting retroviral GAG proteins CC ubiquitination, redistribution to endo-lysosomal compartments and, CC ultimately, lysosomal degradation (PubMed:24852021). Catalyzes distinct CC types of ubiquitination on MAVS and STING1 at different phases of viral CC infection to promote innate antiviral response (PubMed:33139700). CC Mediates the 'Lys-48'-linked ubiquitination of MAVS leading to its CC proteasomal degradation and ubiquitinates STING1 via 'Lys-63'-linked CC polyubiquitination, critical for its oligomerization and the subsequent CC recruitment of TBK1 (PubMed:33139700). Plays a positive role in the CC autophagosome-lysosome fusion by interacting with STX17 and enhancing CC its stability without affecting 'Lys-48'- or 'Lys-63'-linked CC polyubiquitination levels, which in turn promotes autophagosome CC maturation (PubMed:32980859). Negatively regulates TLR-induced CC expression of proinflammatory cytokines by catalyzing 'Lys-11'-linked CC ubiquitination of RAB1A and RAB13 to inhibit post-ER trafficking of CC TLRs to the Golgi by RAB1A and subsequently from the Golgi apparatus to CC the cell surface by RAB13 (PubMed:35343654). CC {ECO:0000269|PubMed:16288031, ECO:0000269|PubMed:18819927, CC ECO:0000269|PubMed:20019814, ECO:0000269|PubMed:24852021, CC ECO:0000269|PubMed:32980859, ECO:0000269|PubMed:33139700, CC ECO:0000269|PubMed:35343654, ECO:0000303|PubMed:23418353}. 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:18819927}; CC -!- PATHWAY: Protein modification; protein ubiquitination. CC {ECO:0000269|PubMed:18819927}. CC -!- SUBUNIT: Interacts with RAB7A. Interacts with EGFR and FLT3. Interacts CC with BST2 (PubMed:20019814). Interacts with STX17 (PubMed:32980859). CC Interacts with YWHAE (PubMed:35343654). {ECO:0000269|PubMed:16925951, CC ECO:0000269|PubMed:20019814, ECO:0000269|PubMed:23418353, CC ECO:0000269|PubMed:32980859, ECO:0000269|PubMed:35343654}. CC -!- INTERACTION: CC Q9Y4L5; Q15038: DAZAP2; NbExp=5; IntAct=EBI-2129242, EBI-724310; CC Q9Y4L5; Q00987: MDM2; NbExp=2; IntAct=EBI-2129242, EBI-389668; CC Q9Y4L5; O15151: MDM4; NbExp=3; IntAct=EBI-2129242, EBI-398437; CC Q9Y4L5; P51668: UBE2D1; NbExp=12; IntAct=EBI-2129242, EBI-743540; CC Q9Y4L5; P62837: UBE2D2; NbExp=6; IntAct=EBI-2129242, EBI-347677; CC Q9Y4L5; P61077: UBE2D3; NbExp=11; IntAct=EBI-2129242, EBI-348268; CC Q9Y4L5; Q9Y2X8: UBE2D4; NbExp=12; IntAct=EBI-2129242, EBI-745527; CC Q9Y4L5; Q96LR5: UBE2E2; NbExp=6; IntAct=EBI-2129242, EBI-2129763; CC Q9Y4L5; Q969T4: UBE2E3; NbExp=4; IntAct=EBI-2129242, EBI-348496; CC Q9Y4L5; P55072: VCP; NbExp=3; IntAct=EBI-2129242, EBI-355164; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20019814, CC ECO:0000269|PubMed:24852021}. Nucleus {ECO:0000269|PubMed:24852021}. CC Endoplasmic reticulum {ECO:0000269|PubMed:35343654}. Golgi apparatus CC {ECO:0000269|PubMed:35343654}. Note=The GTP-bound form of RAB7A CC recruits RNF115 from the cytosol onto late endosomes/lysosomes. CC {ECO:0000269|PubMed:20019814, ECO:0000269|PubMed:24852021}. CC -!- TISSUE SPECIFICITY: Expressed at extremely low levels in normal breast, CC prostate, lung, colon. Higher levels of expression are detected in CC heart, skeletal muscle, testis as well as in breast and prostate cancer CC cells. {ECO:0000269|PubMed:16288031}. CC -!- PTM: Phosphorylated by AKT1, allowing association with the 14-3-3 CC chaperones that facilitates associating with TLRs. CC {ECO:0000269|PubMed:35343654}. CC -!- PTM: RING-type zinc finger-dependent and E2-dependent CC autoubiquitination. {ECO:0000269|PubMed:16288031, CC ECO:0000269|PubMed:18819927}. CC -!- PTM: Deubiquitinated by USP9X; antogonizing its autoubiquitination and CC subsequent proteasomal degradation. {ECO:0000269|PubMed:30689267}. 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; AF542552; AAQ09535.1; -; mRNA. DR EMBL; AF419857; AAP97292.1; -; mRNA. DR EMBL; AK290749; BAF83438.1; -; mRNA. DR EMBL; AL390725; CAI13717.1; -; Genomic_DNA. DR EMBL; AL160282; CAI13717.1; JOINED; Genomic_DNA. DR EMBL; CH471244; EAW71437.1; -; Genomic_DNA. DR EMBL; BC054049; AAH54049.1; -; mRNA. DR EMBL; BC064903; AAH64903.1; -; mRNA. DR EMBL; AL079314; CAB45280.1; -; mRNA. DR CCDS; CCDS72863.1; -. DR RefSeq; NP_055270.1; NM_014455.3. DR AlphaFoldDB; Q9Y4L5; -. DR SMR; Q9Y4L5; -. DR BioGRID; 118094; 138. DR IntAct; Q9Y4L5; 24. DR MINT; Q9Y4L5; -. DR STRING; 9606.ENSP00000463650; -. DR MoonDB; Q9Y4L5; Predicted. DR iPTMnet; Q9Y4L5; -. DR PhosphoSitePlus; Q9Y4L5; -. DR BioMuta; RNF115; -. DR DMDM; 56405389; -. DR EPD; Q9Y4L5; -. DR jPOST; Q9Y4L5; -. DR MassIVE; Q9Y4L5; -. DR MaxQB; Q9Y4L5; -. DR PaxDb; 9606-ENSP00000463650; -. DR PeptideAtlas; Q9Y4L5; -. DR ProteomicsDB; 86228; -. DR Pumba; Q9Y4L5; -. DR Antibodypedia; 74554; 132 antibodies from 24 providers. DR DNASU; 27246; -. DR Ensembl; ENST00000582693.5; ENSP00000463650.1; ENSG00000265491.5. DR GeneID; 27246; -. DR KEGG; hsa:27246; -. DR MANE-Select; ENST00000582693.5; ENSP00000463650.1; NM_014455.4; NP_055270.1. DR UCSC; uc031utf.2; human. DR AGR; HGNC:18154; -. DR CTD; 27246; -. DR DisGeNET; 27246; -. DR GeneCards; RNF115; -. DR HGNC; HGNC:18154; RNF115. DR HPA; ENSG00000265491; Low tissue specificity. DR MIM; 619535; gene. DR neXtProt; NX_Q9Y4L5; -. DR OpenTargets; ENSG00000265491; -. DR PharmGKB; PA162401519; -. DR VEuPathDB; HostDB:ENSG00000265491; -. DR eggNOG; KOG0800; Eukaryota. DR GeneTree; ENSGT00940000157203; -. DR HOGENOM; CLU_034892_0_2_1; -. DR InParanoid; Q9Y4L5; -. DR OMA; RMDNSTS; -. DR OrthoDB; 5474929at2759; -. DR PhylomeDB; Q9Y4L5; -. DR TreeFam; TF317985; -. DR PathwayCommons; Q9Y4L5; -. DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation. DR SignaLink; Q9Y4L5; -. DR SIGNOR; Q9Y4L5; -. DR UniPathway; UPA00143; -. DR BioGRID-ORCS; 27246; 23 hits in 1189 CRISPR screens. DR ChiTaRS; RNF115; human. DR GeneWiki; ZNF364; -. DR GenomeRNAi; 27246; -. DR Pharos; Q9Y4L5; Tbio. DR PRO; PR:Q9Y4L5; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; Q9Y4L5; Protein. DR Bgee; ENSG00000265491; Expressed in gluteal muscle and 207 other cell types or tissues. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005829; C:cytosol; ISS:UniProtKB. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0061630; F:ubiquitin protein ligase activity; ISS:UniProtKB. DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB. DR GO; GO:0042059; P:negative regulation of epidermal growth factor receptor signaling pathway; IMP:UniProtKB. DR GO; GO:0051865; P:protein autoubiquitination; IDA:UniProtKB. DR GO; GO:0070936; P:protein K48-linked ubiquitination; ISS:UniProtKB. DR GO; GO:0070534; P:protein K63-linked ubiquitination; ISS:UniProtKB. DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central. DR GO; GO:0043162; P:ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway; IMP:UniProtKB. DR CDD; cd16800; RING-H2_RNF115; 1. DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1. DR InterPro; IPR001841; Znf_RING. DR InterPro; IPR013083; Znf_RING/FYVE/PHD. DR PANTHER; PTHR15710; E3 UBIQUITIN-PROTEIN LIGASE PRAJA; 1. DR PANTHER; PTHR15710:SF16; E3 UBIQUITIN-PROTEIN LIGASE RNF115; 1. DR Pfam; PF13639; zf-RING_2; 1. DR SMART; SM00184; RING; 1. DR SUPFAM; SSF57850; RING/U-box; 1. DR PROSITE; PS50089; ZF_RING_2; 1. DR Genevisible; Q9Y4L5; HS. PE 1: Evidence at protein level; KW Acetylation; Cytoplasm; Endoplasmic reticulum; Golgi apparatus; KW Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Transferase; KW Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0007744|PubMed:19413330" FT CHAIN 2..304 FT /note="E3 ubiquitin-protein ligase RNF115" FT /id="PRO_0000056314" FT ZN_FING 228..269 FT /note="RING-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175" FT REGION 95..138 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 272..304 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0007744|PubMed:19413330" FT MOD_RES 132 FT /note="Phosphoserine; by PKB/AKT1" FT /evidence="ECO:0000269|PubMed:35343654" FT MOD_RES 133 FT /note="Phosphoserine; by PKB/AKT1" FT /evidence="ECO:0000269|PubMed:35343654" FT VARIANT 194 FT /note="G -> R (in dbSNP:rs11577731)" FT /id="VAR_052105" FT MUTAGEN 26 FT /note="K->R: Loss of autoubiquitination; when associated FT with R-32." FT /evidence="ECO:0000269|PubMed:18819927" FT MUTAGEN 32 FT /note="K->R: Loss of autoubiquitination; when associated FT with R-26." FT /evidence="ECO:0000269|PubMed:18819927" FT MUTAGEN 132 FT /note="S->A: About 50% loss of phosphorylation; when FT associated with A-133." FT /evidence="ECO:0000269|PubMed:35343654" FT MUTAGEN 133 FT /note="S->A: About 50% loss of phosphorylation; when FT associated with A-132." FT /evidence="ECO:0000269|PubMed:35343654" FT MUTAGEN 228 FT /note="C->A: Loss of autoubiquitination." FT /evidence="ECO:0000269|PubMed:18819927" FT MUTAGEN 228 FT /note="C->A: Loss of E3 ligase activity. Maintains the FT ability to restrict viral particle production; when FT associated with A-232." FT /evidence="ECO:0000269|PubMed:20019814, FT ECO:0000269|PubMed:33139700" FT MUTAGEN 231 FT /note="C->A: Loss of autoubiquitination." FT /evidence="ECO:0000269|PubMed:18819927" FT MUTAGEN 231 FT /note="C->A: Loss of E3 ligase activity. Maintains the FT ability to restrict viral particle production; when FT associated with A-228." FT /evidence="ECO:0000269|PubMed:20019814, FT ECO:0000269|PubMed:33139700" FT CONFLICT 299 FT /note="H -> N (in Ref. 7; CAB45280)" FT /evidence="ECO:0000305" SQ SEQUENCE 304 AA; 33703 MW; 22F0C8FCC0F55045 CRC64; MAEASAAGAD SGAAVAAHRF FCHFCKGEVS PKLPEYICPR CESGFIEEVT DDSSFLGGGG SRIDNTTTTH FAELWGHLDH TMFFQDFRPF LSSSPLDQDN RANERGHQTH TDFWGARPPR LPLGRRYRSR GSSRPDRSPA IEGILQHIFA GFFANSAIPG SPHPFSWSGM LHSNPGDYAW GQTGLDAIVT QLLGQLENTG PPPADKEKIT SLPTVTVTQE QVDMGLECPV CKEDYTVEEE VRQLPCNHFF HSSCIVPWLE LHDTCPVCRK SLNGEDSTRQ SQSTEASASN RFSNDSQLHD RWTF //