ID RNF41_HUMAN Reviewed; 317 AA. AC Q9H4P4; A6NFW0; B2RBT8; O75598; DT 21-FEB-2006, integrated into UniProtKB/Swiss-Prot. DT 21-FEB-2006, sequence version 2. DT 10-JUN-2026, entry version 179. DE RecName: Full=E3 ubiquitin-protein ligase NRDP1; DE EC=2.3.2.27; DE AltName: Full=RING finger protein 41; DE AltName: Full=RING-type E3 ubiquitin transferase NRDP1 {ECO:0000305}; GN Name=RNF41; Synonyms=FLRF, NRDP1; ORFNames=SBBI03; 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). RA Zhang W., Cao X., Wan T., Yuan Z., He L., Li N., Zhu X., Tao Q.; RT "Hypothetical protein SBBI03."; RL Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16541075; DOI=10.1038/nature04569; RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., RA Gibbs R.A.; RT "The finished DNA sequence of human chromosome 12."; RL Nature 440:346-351(2006). RN [4] 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Leiomyosarcoma, and Lymph; 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 [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 169-317 (ISOFORM 1). RC TISSUE=Lymphoblast; RA Zhou J., Yu W., Tang H., Mei G., Tsang Y.T.M., Bouck J., Gibbs R.A., RA Margolin J.F.; RL Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases. RN [7] RP FUNCTION, INTERACTION WITH ERBB3, MUTAGENESIS OF CYS-34; HIS-36 AND ASP-56, RP AND TISSUE SPECIFICITY. RX PubMed=12411582; DOI=10.1073/pnas.232580999; RA Qiu X.-B., Goldberg A.L.; RT "Nrdp1/FLRF is a ubiquitin ligase promoting ubiquitination and degradation RT of the epidermal growth factor receptor family member, ErbB3."; RL Proc. Natl. Acad. Sci. U.S.A. 99:14843-14848(2002). RN [8] RP FUNCTION, AND INTERACTION WITH BIRC6. RX PubMed=14765125; DOI=10.1038/sj.emboj.7600075; RA Qiu X.B., Markant S.L., Yuan J., Goldberg A.L.; RT "Nrdp1-mediated degradation of the gigantic IAP, BRUCE, is a novel pathway RT for triggering apoptosis."; RL EMBO J. 23:800-810(2004). RN [9] RP AUTOUBIQUITINATION, INTERACTION WITH USP8, DEUBIQUITINATION BY USP8, AND RP MUTAGENESIS OF CYS-34 AND HIS-36. RX PubMed=15314180; DOI=10.1128/mcb.24.17.7748-7757.2004; RA Wu X., Yen L., Irwin L., Sweeney C., Carraway K.L. III; RT "Stabilization of the E3 ubiquitin ligase Nrdp1 by the deubiquitinating RT enzyme USP8."; RL Mol. Cell. Biol. 24:7748-7757(2004). RN [10] RP FUNCTION, AND INTERACTION WITH PRKN. RX PubMed=15632191; DOI=10.1074/jbc.m408955200; RA Zhong L., Tan Y., Zhou A., Yu Q., Zhou J.; RT "RING finger ubiquitin-protein isopeptide ligase Nrdp1/FLRF regulates RT parkin stability and activity."; RL J. Biol. Chem. 280:9425-9430(2005). RN [11] RP FUNCTION, AND UBIQUITINATION. RX PubMed=17210635; DOI=10.1128/mcb.01245-06; RA Cao Z., Wu X., Yen L., Sweeney C., Carraway K.L. III; RT "Neuregulin-induced ErbB3 downregulation is mediated by a protein stability RT cascade involving the E3 ubiquitin ligase Nrdp1."; RL Mol. Cell. Biol. 27:2180-2188(2007). RN [12] RP FUNCTION, AND INTERACTION WITH PRKN. RX PubMed=18541373; DOI=10.1016/j.neulet.2008.05.052; RA Yu F., Zhou J.; RT "Parkin is ubiquitinated by Nrdp1 and abrogates Nrdp1-induced oxidative RT stress."; RL Neurosci. Lett. 440:4-8(2008). RN [13] RP FUNCTION, AND UBIQUITINATION OF MYD88 AND TBK1. RX PubMed=19483718; DOI=10.1038/ni.1742; RA Wang C., Chen T., Zhang J., Yang M., Li N., Xu X., Cao X.; RT "The E3 ubiquitin ligase Nrdp1 'preferentially' promotes TLR-mediated RT production of type I interferon."; RL Nat. Immunol. 10:744-752(2009). RN [14] RP FUNCTION IN MITOPHAGY. RX PubMed=24949970; DOI=10.1016/j.cell.2014.05.016; RA Soleimanpour S.A., Gupta A., Bakay M., Ferrari A.M., Groff D.N., RA Fadista J., Spruce L.A., Kushner J.A., Groop L., Seeholzer S.H., RA Kaufman B.A., Hakonarson H., Stoffers D.A.; RT "The diabetes susceptibility gene Clec16a regulates mitophagy."; RL Cell 157:1577-1590(2014). RN [15] RP X-RAY CRYSTALLOGRAPHY (1.87 ANGSTROMS) OF 193-317 IN COMPLEX WITH USP8. RX PubMed=17035239; DOI=10.1074/jbc.m606704200; RA Avvakumov G.V., Walker J.R., Xue S., Finerty P.J. Jr., Mackenzie F., RA Newman E.M., Dhe-Paganon S.; RT "Amino-terminal dimerization, NRDP1-rhodanese interaction, and inhibited RT catalytic domain conformation of the ubiquitin-specific protease 8 RT (USP8)."; RL J. Biol. Chem. 281:38061-38070(2006). CC -!- FUNCTION: Acts as E3 ubiquitin-protein ligase and regulates the CC degradation of target proteins. Polyubiquitinates MYD88. Negatively CC regulates MYD88-dependent production of pro-inflammatory cytokines. Can CC promote TRIF-dependent production of type I interferon and inhibits CC infection with vesicular stomatitis virus (By similarity). Promotes CC also activation of TBK1 and IRF3. Involved in the ubiquitination of CC erythropoietin (EPO) and interleukin-3 (IL-3) receptors. Thus, through CC maintaining basal levels of cytokine receptors, RNF41 is involved in CC the control of hematopoietic progenitor cell differentiation into CC myeloerythroid lineages (By similarity). Contributes to the maintenance CC of steady-state ERBB3 levels by mediating its growth factor-independent CC degradation. Involved in the degradation of the inhibitor of apoptosis CC BIRC6 and thus is an important regulator of cell death by promoting CC apoptosis. Also acts as a PRKN modifier that accelerates its CC degradation, resulting in a reduction of PRKN activity, influencing the CC balance of intracellular redox state. The RNF41-PRKN pathway regulates CC autophagosome-lysosome fusion during late mitophagy. Mitophagy is a CC selective form of autophagy necessary for mitochondrial quality control CC (PubMed:24949970). {ECO:0000250, ECO:0000250|UniProtKB:Q8BH75, CC ECO:0000269|PubMed:12411582, ECO:0000269|PubMed:14765125, CC ECO:0000269|PubMed:15632191, ECO:0000269|PubMed:17210635, CC ECO:0000269|PubMed:18541373, ECO:0000269|PubMed:19483718, CC ECO:0000269|PubMed:24949970}. 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; CC -!- PATHWAY: Protein modification; protein ubiquitination. CC -!- SUBUNIT: Interacts with USP8, ERBB3, PRKN and BIRC6. Interacts with CC CSF2RB, EPOR, IL3RA, MYD88 and TBK1. Interacts with CLEC16A (By CC similarity). {ECO:0000250}. CC -!- INTERACTION: CC Q9H4P4; Q9NX04: AIRIM; NbExp=6; IntAct=EBI-2130266, EBI-8643161; CC Q9H4P4; A0A0C4DG62: ARL6IP4; NbExp=3; IntAct=EBI-2130266, EBI-12248874; CC Q9H4P4; Q66PJ3-3: ARL6IP4; NbExp=3; IntAct=EBI-2130266, EBI-10248982; CC Q9H4P4; Q9NWX5: ASB6; NbExp=9; IntAct=EBI-2130266, EBI-6425205; CC Q9H4P4; Q9UHY7: ENOPH1; NbExp=10; IntAct=EBI-2130266, EBI-726969; CC Q9H4P4; Q9NSB8: HOMER2; NbExp=3; IntAct=EBI-2130266, EBI-2126733; CC Q9H4P4; Q86U28: ISCA2; NbExp=7; IntAct=EBI-2130266, EBI-10258659; CC Q9H4P4; Q9BRK4: LZTS2; NbExp=3; IntAct=EBI-2130266, EBI-741037; CC Q9H4P4; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-2130266, EBI-16439278; CC Q9H4P4; Q8N3F0: MTURN; NbExp=3; IntAct=EBI-2130266, EBI-11980301; CC Q9H4P4; O15049: N4BP3; NbExp=6; IntAct=EBI-2130266, EBI-2512055; CC Q9H4P4; P54725: RAD23A; NbExp=3; IntAct=EBI-2130266, EBI-746453; CC Q9H4P4; P35249: RFC4; NbExp=7; IntAct=EBI-2130266, EBI-476655; CC Q9H4P4; Q9H4P4: RNF41; NbExp=3; IntAct=EBI-2130266, EBI-2130266; CC Q9H4P4; Q7LG56: RRM2B; NbExp=3; IntAct=EBI-2130266, EBI-9009083; CC Q9H4P4; Q9GZT4: SRR; NbExp=7; IntAct=EBI-2130266, EBI-9055653; CC Q9H4P4; Q8N8B7-2: TCEANC; NbExp=3; IntAct=EBI-2130266, EBI-11955057; CC Q9H4P4; Q99614: TTC1; NbExp=13; IntAct=EBI-2130266, EBI-742074; CC Q9H4P4; P61086: UBE2K; NbExp=3; IntAct=EBI-2130266, EBI-473850; CC Q9H4P4; Q8N1B4: VPS52; NbExp=7; IntAct=EBI-2130266, EBI-2799833; CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q9H4P4-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9H4P4-2; Sequence=VSP_044670; CC -!- TISSUE SPECIFICITY: Detected in ovary, testis and prostate. CC {ECO:0000269|PubMed:12411582}. CC -!- PTM: Autoubiquitinated. Autoubiquitination leads to proteasomal CC degradation. Deubiquitinated by USP8 to get stabilized which induces CC apoptosis. {ECO:0000269|PubMed:15314180, ECO:0000269|PubMed:17210635, CC ECO:0000269|PubMed:19483718}. CC -!- SEQUENCE CAUTION: CC Sequence=AAG01988.1; Type=Erroneous initiation; Note=Truncated N-terminus.; 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; AF077599; AAC27647.1; -; mRNA. DR EMBL; AK314811; BAG37335.1; -; mRNA. DR EMBL; AC073896; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471054; EAW96909.1; -; Genomic_DNA. DR EMBL; CH471054; EAW96910.1; -; Genomic_DNA. DR EMBL; BC024284; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; BC032637; AAH32637.1; -; mRNA. DR EMBL; AY007109; AAG01988.1; ALT_INIT; mRNA. DR CCDS; CCDS8909.1; -. [Q9H4P4-1] DR CCDS; CCDS8910.1; -. [Q9H4P4-2] DR RefSeq; NP_001229755.1; NM_001242826.2. [Q9H4P4-1] DR RefSeq; NP_005776.1; NM_005785.4. [Q9H4P4-1] DR RefSeq; NP_919339.1; NM_194358.3. [Q9H4P4-2] DR RefSeq; NP_919340.1; NM_194359.2. [Q9H4P4-1] DR PDB; 2FZP; X-ray; 1.87 A; A=193-317. DR PDB; 2GWF; X-ray; 2.30 A; B/D/F=193-317. DR PDBsum; 2FZP; -. DR PDBsum; 2GWF; -. DR AlphaFoldDB; Q9H4P4; -. DR SMR; Q9H4P4; -. DR BioGRID; 115488; 158. DR FunCoup; Q9H4P4; 2299. DR IntAct; Q9H4P4; 95. DR MINT; Q9H4P4; -. DR NDEx; IQUERY-CP-RNF41; 4 NDEx IQuery Curated Pathways. DR STRING; 9606.ENSP00000342755; -. DR iPTMnet; Q9H4P4; -. DR PhosphoSitePlus; Q9H4P4; -. DR BioMuta; RNF41; -. DR DMDM; 88909120; -. DR jPOST; Q9H4P4; -. DR MassIVE; Q9H4P4; -. DR PaxDb; 9606-ENSP00000342755; -. DR PeptideAtlas; Q9H4P4; -. DR ProteomicsDB; 1082; -. DR ProteomicsDB; 80869; -. [Q9H4P4-1] DR Pumba; Q9H4P4; -. DR Antibodypedia; 15762; 201 antibodies from 31 providers. DR DNASU; 10193; -. DR Ensembl; ENST00000345093.9; ENSP00000342755.4; ENSG00000181852.19. [Q9H4P4-1] DR Ensembl; ENST00000394013.6; ENSP00000377581.2; ENSG00000181852.19. [Q9H4P4-2] DR Ensembl; ENST00000552656.5; ENSP00000447303.1; ENSG00000181852.19. [Q9H4P4-1] DR Ensembl; ENST00000615206.4; ENSP00000484671.1; ENSG00000181852.19. [Q9H4P4-1] DR Ensembl; ENST00000881816.1; ENSP00000551875.1; ENSG00000181852.19. [Q9H4P4-1] DR Ensembl; ENST00000881817.1; ENSP00000551876.1; ENSG00000181852.19. [Q9H4P4-1] DR Ensembl; ENST00000881818.1; ENSP00000551877.1; ENSG00000181852.19. [Q9H4P4-1] DR Ensembl; ENST00000881819.1; ENSP00000551878.1; ENSG00000181852.19. [Q9H4P4-1] DR Ensembl; ENST00000881820.1; ENSP00000551879.1; ENSG00000181852.19. [Q9H4P4-1] DR Ensembl; ENST00000881821.1; ENSP00000551880.1; ENSG00000181852.19. [Q9H4P4-1] DR Ensembl; ENST00000881822.1; ENSP00000551881.1; ENSG00000181852.19. [Q9H4P4-1] DR Ensembl; ENST00000959116.1; ENSP00000629175.1; ENSG00000181852.19. [Q9H4P4-1] DR Ensembl; ENST00000959117.1; ENSP00000629176.1; ENSG00000181852.19. [Q9H4P4-1] DR Ensembl; ENST00000959118.1; ENSP00000629177.1; ENSG00000181852.19. [Q9H4P4-1] DR GeneID; 10193; -. DR KEGG; hsa:10193; -. DR MANE-Select; ENST00000345093.9; ENSP00000342755.4; NM_005785.4; NP_005776.1. DR UCSC; uc001ske.3; human. [Q9H4P4-1] DR AGR; HGNC:18401; -. DR ClinPGx; PA134875033; -. DR CTD; 10193; -. DR DisGeNET; 10193; -. DR GeneCards; RNF41; -. DR HGNC; HGNC:18401; RNF41. DR HPA; ENSG00000181852; Low tissue specificity. DR MIM; 620051; gene. DR OpenTargets; ENSG00000181852; -. DR VEuPathDB; HostDB:ENSG00000181852; -. DR eggNOG; KOG0297; Eukaryota. DR GeneTree; ENSGT00530000063647; -. DR HOGENOM; CLU_076732_0_0_1; -. DR InParanoid; Q9H4P4; -. DR OMA; QYENYVC; -. DR OrthoDB; 1630758at2759; -. DR PAN-GO; Q9H4P4; 3 GO annotations based on evolutionary models. DR PhylomeDB; Q9H4P4; -. DR PathwayCommons; Q9H4P4; -. DR Reactome; R-HSA-1358803; Downregulation of ERBB2:ERBB3 signaling. DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation. DR SignaLink; Q9H4P4; -. DR SIGNOR; Q9H4P4; -. DR UniPathway; UPA00143; -. DR Agora; ENSG00000181852; -. DR BioGRID-ORCS; 10193; 36 hits in 1204 CRISPR screens. DR ChiTaRS; RNF41; human. DR EvolutionaryTrace; Q9H4P4; -. DR GeneWiki; RNF41; -. DR GenomeRNAi; 10193; -. DR Pharos; Q9H4P4; Tbio. DR PRO; PR:Q9H4P4; -. DR Proteomes; UP000005640; Chromosome 12. DR RNAct; Q9H4P4; protein. DR Bgee; ENSG00000181852; Expressed in Brodmann (1909) area 10 and 187 other cell types or tissues. DR ExpressionAtlas; Q9H4P4; baseline and differential. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0071782; C:endoplasmic reticulum tubular network; IDA:CAFA. DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:CAFA. DR GO; GO:0005128; F:erythropoietin receptor binding; IEA:Ensembl. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0005135; F:interleukin-3 receptor binding; IEA:Ensembl. DR GO; GO:0019904; F:protein domain specific binding; IPI:CAFA. DR GO; GO:0030971; F:receptor tyrosine kinase binding; IPI:CAFA. DR GO; GO:0031267; F:small GTPase binding; IPI:UniProtKB. DR GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:ParkinsonsUK-UCL. DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW. DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW. DR GO; GO:0097191; P:extrinsic apoptotic signaling pathway; IDA:UniProtKB. DR GO; GO:0030336; P:negative regulation of cell migration; IMP:MGI. DR GO; GO:0008285; P:negative regulation of cell population proliferation; IDA:MGI. DR GO; GO:0045732; P:positive regulation of protein catabolic process; IMP:CAFA. DR GO; GO:2000379; P:positive regulation of reactive oxygen species metabolic process; IMP:ParkinsonsUK-UCL. DR GO; GO:0010498; P:proteasomal protein catabolic process; IDA:ParkinsonsUK-UCL. DR GO; GO:0051865; P:protein autoubiquitination; IDA:FlyBase. DR GO; GO:0000209; P:protein polyubiquitination; IDA:UniProtKB. DR GO; GO:0043408; P:regulation of MAPK cascade; IDA:MGI. DR GO; GO:0051896; P:regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction; IDA:MGI. DR GO; GO:2000377; P:regulation of reactive oxygen species metabolic process; IMP:UniProtKB. DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central. DR CDD; cd16634; mRING-HC-C3HC3D_Nrdp1; 1. DR FunFam; 3.30.40.10:FF:000268; E3 ubiquitin-protein ligase NRDP1; 1. DR FunFam; 3.30.40.10:FF:000302; E3 ubiquitin-protein ligase NRDP1; 1. DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2. DR InterPro; IPR015036; NRDP1. DR InterPro; IPR037255; NRDP1_C. DR InterPro; IPR001841; Znf_RING. DR InterPro; IPR013083; Znf_RING/FYVE/PHD. DR InterPro; IPR017907; Znf_RING_CS. DR InterPro; IPR013010; Znf_SIAH. DR PANTHER; PTHR10131:SF157; RECEPTOR-ASSOCIATED FACTOR, PUTATIVE-RELATED; 1. DR PANTHER; PTHR10131; TNF RECEPTOR ASSOCIATED FACTOR; 1. DR Pfam; PF08941; USP8_interact; 1. DR Pfam; PF13923; zf-C3HC4_2; 1. DR SMART; SM00184; RING; 1. DR SUPFAM; SSF160088; NRDP1 C-terminal domain-like; 1. DR SUPFAM; SSF57850; RING/U-box; 1. DR SUPFAM; SSF49599; TRAF domain-like; 1. DR PROSITE; PS00518; ZF_RING_1; 1. DR PROSITE; PS50089; ZF_RING_2; 1. DR PROSITE; PS51081; ZF_SIAH; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Apoptosis; Autophagy; Metal-binding; KW Proteomics identification; Reference proteome; Transferase; KW Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger. FT CHAIN 1..317 FT /note="E3 ubiquitin-protein ligase NRDP1" FT /id="PRO_0000223954" FT ZN_FING 18..57 FT /note="RING-type; degenerate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175" FT ZN_FING 78..138 FT /note="SIAH-type; degenerate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00455" FT VAR_SEQ 1..71 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_044670" FT MUTAGEN 34 FT /note="C->S: Loss of activity; when associated with Q-36." FT /evidence="ECO:0000269|PubMed:12411582, FT ECO:0000269|PubMed:15314180" FT MUTAGEN 36 FT /note="H->Q: Loss of activity; when associated with S-34." FT /evidence="ECO:0000269|PubMed:12411582, FT ECO:0000269|PubMed:15314180" FT MUTAGEN 56 FT /note="D->V: Loss of activity." FT /evidence="ECO:0000269|PubMed:12411582" FT HELIX 193..205 FT /evidence="ECO:0007829|PDB:2FZP" FT STRAND 206..211 FT /evidence="ECO:0007829|PDB:2FZP" FT HELIX 214..216 FT /evidence="ECO:0007829|PDB:2FZP" FT STRAND 217..220 FT /evidence="ECO:0007829|PDB:2FZP" FT HELIX 223..235 FT /evidence="ECO:0007829|PDB:2FZP" FT HELIX 240..248 FT /evidence="ECO:0007829|PDB:2FZP" FT HELIX 252..254 FT /evidence="ECO:0007829|PDB:2FZP" FT TURN 257..259 FT /evidence="ECO:0007829|PDB:2FZP" FT HELIX 262..267 FT /evidence="ECO:0007829|PDB:2FZP" FT TURN 268..270 FT /evidence="ECO:0007829|PDB:2FZP" FT HELIX 271..274 FT /evidence="ECO:0007829|PDB:2FZP" FT STRAND 277..279 FT /evidence="ECO:0007829|PDB:2FZP" FT STRAND 283..289 FT /evidence="ECO:0007829|PDB:2FZP" FT HELIX 290..292 FT /evidence="ECO:0007829|PDB:2FZP" FT TURN 298..300 FT /evidence="ECO:0007829|PDB:2FZP" FT STRAND 303..312 FT /evidence="ECO:0007829|PDB:2FZP" FT STRAND 314..316 FT /evidence="ECO:0007829|PDB:2FZP" SQ SEQUENCE 317 AA; 35905 MW; 46AE87AF8BE1A369 CRC64; MGYDVTRFQG DVDEDLICPI CSGVLEEPVQ APHCEHAFCN ACITQWFSQQ QTCPVDRSVV TVAHLRPVPR IMRNMLSKLQ IACDNAVFGC SAVVRLDNLM SHLSDCEHNP KRPVTCEQGC GLEMPKDELP NHNCIKHLRS VVQQQQTRIA ELEKTSAEHK HQLAEQKRDI QLLKAYMRAI RSVNPNLQNL EETIEYNEIL EWVNSLQPAR VTRWGGMIST PDAVLQAVIK RSLVESGCPA SIVNELIENA HERSWPQGLA TLETRQMNRR YYENYVAKRI PGKQAVVVMA CENQHMGDDM VQEPGLVMIF AHGVEEI //