ID RN185_HUMAN Reviewed; 192 AA. AC Q96GF1; A8K5C1; A9X3T8; Q8N900; DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 1. DT 10-JUN-2026, entry version 177. DE RecName: Full=E3 ubiquitin-protein ligase RNF185 {ECO:0000305}; DE EC=2.3.2.27 {ECO:0000269|PubMed:21931693, ECO:0000269|PubMed:27485036, ECO:0000269|PubMed:28273161}; DE AltName: Full=RING finger protein 185; GN Name=RNF185 {ECO:0000303|Ref.1, ECO:0000312|HGNC:HGNC:26783}; 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] (ISOFORMS 1 AND 2). RC TISSUE=Pancreas, and Testis; RA Martinez Gamboa L., Stuhlmueller B., Burmester G.R.; RT "Multiple splice variants of the gene coding for ring finger protein RT RNF185."; RL Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84; RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., RA Beare D.M., Dunham I.; RT "A genome annotation-driven approach to cloning the human ORFeome."; RL Genome Biol. 5:R84.1-R84.11(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). 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=10591208; DOI=10.1038/990031; RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C., RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., RA Wright H.; RT "The DNA sequence of human chromosome 22."; RL Nature 402:489-495(1999). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton 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] (ISOFORM 1). RC TISSUE=Colon, Lung, Muscle, and Pancreas; 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 FUNCTION, CATALYTIC ACTIVITY, PATHWAY, SUBCELLULAR LOCATION, TOPOLOGY, AND RP INTERACTION WITH ATG5 AND BNIP1. RX PubMed=21931693; DOI=10.1371/journal.pone.0024367; RA Tang F., Wang B., Li N., Wu Y., Jia J., Suo T., Chen Q., Liu Y.J., Tang J.; RT "RNF185, a novel mitochondrial ubiquitin E3 ligase, regulates autophagy RT through interaction with BNIP1."; RL PLoS ONE 6:E24367-E24367(2011). RN [8] RP FUNCTION, INDUCTION, AND SUBCELLULAR LOCATION. RX PubMed=24019521; DOI=10.1074/jbc.m113.470500; RA El Khouri E., Le Pavec G., Toledano M.B., Delaunay-Moisan A.; RT "RNF185 is a novel E3 ligase of endoplasmic reticulum-associated RT degradation (ERAD) that targets cystic fibrosis transmembrane conductance RT regulator (CFTR)."; RL J. Biol. Chem. 288:31177-31191(2013). RN [9] RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, SUBCELLULAR LOCATION, TISSUE RP SPECIFICITY, INDUCTION, DOMAIN, AND MUTAGENESIS OF CYS-39. RX PubMed=27485036; DOI=10.1038/srep30955; RA Kaneko M., Iwase I., Yamasaki Y., Takai T., Wu Y., Kanemoto S., RA Matsuhisa K., Asada R., Okuma Y., Watanabe T., Imaizumi K., Nomura Y.; RT "Genome-wide identification and gene expression profiling of ubiquitin RT ligases for endoplasmic reticulum protein degradation."; RL Sci. Rep. 6:30955-30955(2016). RN [10] RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND MUTAGENESIS OF CYS-39 AND RP CYS-79. RX PubMed=28273161; DOI=10.1371/journal.ppat.1006264; RA Wang Q., Huang L., Hong Z., Lv Z., Mao Z., Tang Y., Kong X., Li S., Cui Y., RA Liu H., Zhang L., Zhang X., Jiang L., Wang C., Zhou Q.; RT "The E3 ubiquitin ligase RNF185 facilitates the cGAS-mediated innate immune RT response."; RL PLoS Pathog. 13:e1006264-e1006264(2017). CC -!- FUNCTION: E3 ubiquitin-protein ligase that regulates selective CC mitochondrial autophagy by mediating 'Lys-63'-linked polyubiquitination CC of BNIP1 (PubMed:21931693). Acts in the endoplasmic reticulum (ER)- CC associated degradation (ERAD) pathway, which targets misfolded proteins CC that accumulate in the endoplasmic reticulum (ER) for ubiquitination CC and subsequent proteasome-mediated degradation (PubMed:27485036). CC Protects cells from ER stress-induced apoptosis (PubMed:27485036). CC Responsible for the cotranslational ubiquitination and degradation of CC CFTR in the ERAD pathway (PubMed:24019521). Also acts as a regulator of CC the innate antiviral response by catalyzing 'Lys-27'-linked CC polyubiquitination of CGAS at 'Lys-173' and 'Lys-384', thereby CC promoting CGAS cyclic GMP-AMP synthase activity (PubMed:28273161). CC Preferentially associates with the E2 enzymes UBE2J1 and UBE2J2 CC (PubMed:24019521). {ECO:0000269|PubMed:21931693, CC ECO:0000269|PubMed:24019521, ECO:0000269|PubMed:27485036, CC ECO:0000269|PubMed:28273161}. 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:21931693, CC ECO:0000269|PubMed:27485036, ECO:0000269|PubMed:28273161}; CC -!- PATHWAY: Protein modification; protein ubiquitination. CC {ECO:0000269|PubMed:21931693, ECO:0000269|PubMed:27485036, CC ECO:0000269|PubMed:28273161}. CC -!- SUBUNIT: Interacts with ATG5 and BNIP1. {ECO:0000269|PubMed:21931693}. CC -!- INTERACTION: CC Q96GF1; O75915: ARL6IP5; NbExp=3; IntAct=EBI-2340249, EBI-2860752; CC Q96GF1; Q96DZ9: CMTM5; NbExp=3; IntAct=EBI-2340249, EBI-2548702; CC Q96GF1; Q8NBI2: CYB561A3; NbExp=3; IntAct=EBI-2340249, EBI-10269179; CC Q96GF1; Q96D05-2: FAM241B; NbExp=3; IntAct=EBI-2340249, EBI-12118888; CC Q96GF1; Q13021: MALL; NbExp=3; IntAct=EBI-2340249, EBI-750078; CC Q96GF1; Q5J8X5: MS4A13; NbExp=3; IntAct=EBI-2340249, EBI-12070086; CC Q96GF1; A6NDP7: MYADML2; NbExp=3; IntAct=EBI-2340249, EBI-17641390; CC Q96GF1; Q0D2K0: NIPAL4; NbExp=3; IntAct=EBI-2340249, EBI-9550165; CC Q96GF1; Q99942: RNF5; NbExp=4; IntAct=EBI-2340249, EBI-348482; CC Q96GF1; P55061: TMBIM6; NbExp=5; IntAct=EBI-2340249, EBI-1045825; CC Q96GF1; Q9BVK8: TMEM147; NbExp=3; IntAct=EBI-2340249, EBI-348587; CC Q96GF1; Q96HH6: TMEM19; NbExp=3; IntAct=EBI-2340249, EBI-741829; CC Q96GF1; Q8N2M4: TMEM86A; NbExp=3; IntAct=EBI-2340249, EBI-12015604; CC Q96GF1; P51668: UBE2D1; NbExp=4; IntAct=EBI-2340249, EBI-743540; CC Q96GF1; P62837: UBE2D2; NbExp=4; IntAct=EBI-2340249, EBI-347677; CC Q96GF1; Q9Y2X8: UBE2D4; NbExp=4; IntAct=EBI-2340249, EBI-745527; CC Q96GF1; Q96LR5: UBE2E2; NbExp=4; IntAct=EBI-2340249, EBI-2129763; CC Q96GF1; Q969T4: UBE2E3; NbExp=8; IntAct=EBI-2340249, EBI-348496; CC Q96GF1; P61086: UBE2K; NbExp=3; IntAct=EBI-2340249, EBI-473850; CC Q96GF1; Q9BWQ6: YIPF2; NbExp=6; IntAct=EBI-2340249, EBI-751204; CC Q96GF1; Q9BSR8: YIPF4; NbExp=3; IntAct=EBI-2340249, EBI-751253; CC Q96GF1; Q96EC8: YIPF6; NbExp=3; IntAct=EBI-2340249, EBI-751210; CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane CC {ECO:0000269|PubMed:21931693}; Multi-pass membrane protein CC {ECO:0000255}. Endoplasmic reticulum membrane CC {ECO:0000269|PubMed:24019521, ECO:0000269|PubMed:27485036}; Multi-pass CC membrane protein {ECO:0000255}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q96GF1-1; Sequence=Displayed; CC Name=2; CC IsoId=Q96GF1-2; Sequence=VSP_020004; CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. CC {ECO:0000269|PubMed:27485036}. CC -!- INDUCTION: Up-regulated by unfolded protein response (UPR) and CC endoplasmic reticulum (ER) stress triggered by thapsigargin or CC tunicamycin. {ECO:0000269|PubMed:24019521, CC ECO:0000269|PubMed:27485036}. CC -!- DOMAIN: The RING-type zinc finger domain is responsible for E3 CC ubiquitin ligase activity. {ECO:0000269|PubMed:27485036}. 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; DQ296559; ABB97506.1; -; mRNA. DR EMBL; DQ296561; ABB97508.1; -; mRNA. DR EMBL; DQ296562; ABB97509.1; -; mRNA. DR EMBL; DQ296565; ABB97512.1; -; mRNA. DR EMBL; CR456349; CAG30235.1; -; mRNA. DR EMBL; AK095947; BAC04659.1; -; mRNA. DR EMBL; AK291236; BAF83925.1; -; mRNA. DR EMBL; AC002073; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC005005; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471095; EAW59947.1; -; Genomic_DNA. DR EMBL; CH471095; EAW59949.1; -; Genomic_DNA. DR EMBL; BC009504; AAH09504.1; -; mRNA. DR EMBL; BC026040; AAH26040.1; -; mRNA. DR EMBL; BC033166; AAH33166.1; -; mRNA. DR EMBL; BC012817; AAH12817.1; -; mRNA. DR EMBL; BC035684; AAH35684.1; -; mRNA. DR CCDS; CCDS13890.1; -. [Q96GF1-1] DR CCDS; CCDS46689.1; -. [Q96GF1-2] DR RefSeq; NP_001129297.1; NM_001135825.2. [Q96GF1-2] DR RefSeq; NP_689480.2; NM_152267.3. [Q96GF1-1] DR AlphaFoldDB; Q96GF1; -. DR SMR; Q96GF1; -. DR BioGRID; 124834; 190. DR FunCoup; Q96GF1; 1258. DR IntAct; Q96GF1; 88. DR MINT; Q96GF1; -. DR NDEx; IQUERY-CP-RNF185; 1 NDEx IQuery Curated Pathway. DR STRING; 9606.ENSP00000320508; -. DR iPTMnet; Q96GF1; -. DR PhosphoSitePlus; Q96GF1; -. DR BioMuta; RNF185; -. DR DMDM; 74751883; -. DR jPOST; Q96GF1; -. DR MassIVE; Q96GF1; -. DR PaxDb; 9606-ENSP00000320508; -. DR PeptideAtlas; Q96GF1; -. DR ProteomicsDB; 76632; -. [Q96GF1-1] DR ProteomicsDB; 76633; -. [Q96GF1-2] DR Pumba; Q96GF1; -. DR TopDownProteomics; Q96GF1-1; -. [Q96GF1-1] DR TopDownProteomics; Q96GF1-2; -. [Q96GF1-2] DR Antibodypedia; 24963; 148 antibodies from 23 providers. DR DNASU; 91445; -. DR Ensembl; ENST00000266252.8; ENSP00000266252.7; ENSG00000138942.18. [Q96GF1-2] DR Ensembl; ENST00000326132.11; ENSP00000320508.5; ENSG00000138942.18. [Q96GF1-1] DR Ensembl; ENST00000518626.5; ENSP00000427755.1; ENSG00000138942.18. [Q96GF1-1] DR Ensembl; ENST00000883456.1; ENSP00000553515.1; ENSG00000138942.18. [Q96GF1-1] DR Ensembl; ENST00000883457.1; ENSP00000553516.1; ENSG00000138942.18. [Q96GF1-1] DR Ensembl; ENST00000883458.1; ENSP00000553517.1; ENSG00000138942.18. [Q96GF1-1] DR Ensembl; ENST00000883459.1; ENSP00000553518.1; ENSG00000138942.18. [Q96GF1-1] DR Ensembl; ENST00000927744.1; ENSP00000597803.1; ENSG00000138942.18. [Q96GF1-1] DR Ensembl; ENST00000964265.1; ENSP00000634324.1; ENSG00000138942.18. [Q96GF1-1] DR Ensembl; ENST00000964266.1; ENSP00000634325.1; ENSG00000138942.18. [Q96GF1-1] DR Ensembl; ENST00000964267.1; ENSP00000634326.1; ENSG00000138942.18. [Q96GF1-2] DR Ensembl; ENST00000964268.1; ENSP00000634327.1; ENSG00000138942.18. [Q96GF1-1] DR Ensembl; ENST00000964269.1; ENSP00000634328.1; ENSG00000138942.18. [Q96GF1-1] DR Ensembl; ENST00000964270.1; ENSP00000634329.1; ENSG00000138942.18. [Q96GF1-1] DR Ensembl; ENST00000964271.1; ENSP00000634330.1; ENSG00000138942.18. [Q96GF1-1] DR Ensembl; ENST00000964272.1; ENSP00000634331.1; ENSG00000138942.18. [Q96GF1-1] DR Ensembl; ENST00000964273.1; ENSP00000634332.1; ENSG00000138942.18. [Q96GF1-1] DR GeneID; 91445; -. DR KEGG; hsa:91445; -. DR MANE-Select; ENST00000326132.11; ENSP00000320508.5; NM_152267.4; NP_689480.2. DR UCSC; uc003akb.4; human. [Q96GF1-1] DR AGR; HGNC:26783; -. DR ClinPGx; PA142671056; -. DR CTD; 91445; -. DR DisGeNET; 91445; -. DR GeneCards; RNF185; -. DR HGNC; HGNC:26783; RNF185. DR HPA; ENSG00000138942; Low tissue specificity. DR MIM; 620096; gene. DR OpenTargets; ENSG00000138942; -. DR VEuPathDB; HostDB:ENSG00000138942; -. DR eggNOG; KOG0823; Eukaryota. DR GeneTree; ENSGT00390000014107; -. DR HOGENOM; CLU_055198_2_2_1; -. DR InParanoid; Q96GF1; -. DR OMA; RPNRQTC; -. DR OrthoDB; 302966at2759; -. DR PAN-GO; Q96GF1; 4 GO annotations based on evolutionary models. DR PhylomeDB; Q96GF1; -. DR PathwayCommons; Q96GF1; -. DR Reactome; R-HSA-382556; ABC-family proteins mediated transport. DR Reactome; R-HSA-5678895; Defective CFTR causes cystic fibrosis. DR Reactome; R-HSA-901032; ER Quality Control Compartment (ERQC). DR Reactome; R-HSA-9931269; AMPK-induced ERAD and lysosome mediated degradation of PD-L1(CD274). DR SignaLink; Q96GF1; -. DR SIGNOR; Q96GF1; -. DR UniPathway; UPA00143; -. DR Agora; ENSG00000138942; -. DR BioGRID-ORCS; 91445; 15 hits in 1194 CRISPR screens. DR ChiTaRS; RNF185; human. DR GenomeRNAi; 91445; -. DR Pharos; Q96GF1; Tbio. DR PRO; PR:Q96GF1; -. DR Proteomes; UP000005640; Chromosome 22. DR RNAct; Q96GF1; protein. DR Bgee; ENSG00000138942; Expressed in kidney epithelium and 181 other cell types or tissues. DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB. DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome. DR GO; GO:0044322; C:endoplasmic reticulum quality control compartment; IEA:GOC. DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell. DR GO; GO:0044877; F:protein-containing complex binding; IPI:ParkinsonsUK-UCL. DR GO; GO:0043130; F:ubiquitin binding; IDA:UniProtKB. DR GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:UniProtKB. DR GO; GO:0044390; F:ubiquitin-like protein conjugating enzyme binding; IPI:ParkinsonsUK-UCL. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW. DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW. DR GO; GO:0051607; P:defense response to virus; IDA:UniProtKB. DR GO; GO:1904380; P:endoplasmic reticulum mannose trimming; TAS:Reactome. DR GO; GO:0036503; P:ERAD pathway; IGI:ParkinsonsUK-UCL. DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW. DR GO; GO:1904294; P:positive regulation of ERAD pathway; IMP:UniProtKB. DR GO; GO:0045089; P:positive regulation of innate immune response; IDA:UniProt. DR GO; GO:0060340; P:positive regulation of type I interferon-mediated signaling pathway; IDA:UniProtKB. DR GO; GO:0051865; P:protein autoubiquitination; IDA:UniProtKB. DR GO; GO:0044314; P:protein K27-linked ubiquitination; IDA:UniProtKB. DR GO; GO:0055085; P:transmembrane transport; TAS:Reactome. DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IMP:ParkinsonsUK-UCL. DR CDD; cd16744; RING-HC_RNF185; 1. DR FunFam; 3.30.40.10:FF:000062; E3 ubiquitin-protein ligase RNF185; 1. DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1. DR InterPro; IPR045103; RNF5/RNF185-like. DR InterPro; IPR018957; Znf_C3HC4_RING-type. DR InterPro; IPR001841; Znf_RING. DR InterPro; IPR013083; Znf_RING/FYVE/PHD. DR InterPro; IPR017907; Znf_RING_CS. DR PANTHER; PTHR12313; E3 UBIQUITIN-PROTEIN LIGASE RNF5-RELATED; 1. DR Pfam; PF00097; zf-C3HC4; 1. DR SMART; SM00184; RING; 1. DR SUPFAM; SSF57850; RING/U-box; 1. DR PROSITE; PS00518; ZF_RING_1; 1. DR PROSITE; PS50089; ZF_RING_2; 1. PE 1: Evidence at protein level; KW Alternative splicing; Autophagy; Endoplasmic reticulum; Immunity; KW Innate immunity; Membrane; Metal-binding; Mitochondrion; KW Mitochondrion outer membrane; Proteomics identification; KW Reference proteome; Transferase; Transmembrane; Transmembrane helix; KW Ubl conjugation pathway; Zinc; Zinc-finger. FT CHAIN 1..192 FT /note="E3 ubiquitin-protein ligase RNF185" FT /id="PRO_0000247520" FT TOPO_DOM 1..130 FT /note="Cytoplasmic" FT /evidence="ECO:0000269|PubMed:21931693" FT TRANSMEM 131..151 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 152..171 FT /note="Mitochondrial intermembrane" FT /evidence="ECO:0000269|PubMed:21931693" FT TRANSMEM 172..192 FT /note="Helical" FT /evidence="ECO:0000255" FT ZN_FING 39..80 FT /note="RING-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175" FT REGION 1..30 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 29..80 FT /note="Required for ubiquitin ligase activity and FT protection against ER stress-induced cell death" FT /evidence="ECO:0000269|PubMed:27485036" FT REGION 90..123 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1..27 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT VAR_SEQ 66..121 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039, ECO:0000303|Ref.1" FT /id="VSP_020004" FT MUTAGEN 39 FT /note="C->A: Abolished E3 ubiquitin-protein ligase activity FT and ability to regulate the cGAS-STING pathway; when FT associated with A-79." FT /evidence="ECO:0000269|PubMed:28273161" FT MUTAGEN 39 FT /note="C->S: Decreased ubiquitin ligase activity." FT /evidence="ECO:0000269|PubMed:27485036" FT MUTAGEN 79 FT /note="C->A: Abolished E3 ubiquitin-protein ligase activity FT and ability to regulate the cGAS-STING pathway; when FT associated with A-39." FT /evidence="ECO:0000269|PubMed:28273161" SQ SEQUENCE 192 AA; 20459 MW; F24B49EA566740B3 CRC64; MASKGPSASA SPENSSAGGP SGSSNGAGES GGQDSTFECN ICLDTAKDAV ISLCGHLFCW PCLHQWLETR PNRQVCPVCK AGISRDKVIP LYGRGSTGQQ DPREKTPPRP QGQRPEPENR GGFQGFGFGD GGFQMSFGIG AFPFGIFATA FNINDGRPPP AVPGTPQYVD EQFLSRLFLF VALVIMFWLL IA //