RNF41_HUMAN
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 03-AUG-2022, entry version 161.
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. Acts also 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; 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=7; IntAct=EBI-2130266, EBI-6425205;
CC Q9H4P4; Q9NX04: C1orf109; NbExp=6; IntAct=EBI-2130266, EBI-8643161;
CC Q9H4P4; Q9UHY7: ENOPH1; NbExp=7; IntAct=EBI-2130266, EBI-726969;
CC Q9H4P4; Q9NSB8: HOMER2; NbExp=3; IntAct=EBI-2130266, EBI-2126733;
CC Q9H4P4; Q86U28: ISCA2; NbExp=6; 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=6; IntAct=EBI-2130266, EBI-9055653;
CC Q9H4P4; Q8N8B7-2: TCEANC; NbExp=3; IntAct=EBI-2130266, EBI-11955057;
CC Q9H4P4; Q99614: TTC1; NbExp=10; IntAct=EBI-2130266, EBI-742074;
CC Q9H4P4; P61086: UBE2K; NbExp=3; IntAct=EBI-2130266, EBI-473850;
CC Q9H4P4; Q8N1B4: VPS52; NbExp=6; 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};
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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_001242826.1. [Q9H4P4-1]
DR RefSeq; NP_005776.1; NM_005785.3. [Q9H4P4-1]
DR RefSeq; NP_919339.1; NM_194358.2. [Q9H4P4-2]
DR RefSeq; NP_919340.1; NM_194359.2. [Q9H4P4-1]
DR RefSeq; XP_005268618.1; XM_005268561.4. [Q9H4P4-2]
DR RefSeq; XP_011536036.1; XM_011537734.2. [Q9H4P4-2]
DR RefSeq; XP_011536037.1; XM_011537735.2. [Q9H4P4-2]
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; 149.
DR IntAct; Q9H4P4; 71.
DR MINT; Q9H4P4; -.
DR STRING; 9606.ENSP00000342755; -.
DR iPTMnet; Q9H4P4; -.
DR PhosphoSitePlus; Q9H4P4; -.
DR BioMuta; RNF41; -.
DR DMDM; 88909120; -.
DR EPD; Q9H4P4; -.
DR jPOST; Q9H4P4; -.
DR MassIVE; Q9H4P4; -.
DR MaxQB; Q9H4P4; -.
DR PaxDb; Q9H4P4; -.
DR PeptideAtlas; Q9H4P4; -.
DR PRIDE; Q9H4P4; -.
DR ProteomicsDB; 1082; -.
DR ProteomicsDB; 80869; -. [Q9H4P4-1]
DR Antibodypedia; 15762; 205 antibodies from 31 providers.
DR DNASU; 10193; -.
DR Ensembl; ENST00000345093.9; ENSP00000342755.4; ENSG00000181852.18. [Q9H4P4-1]
DR Ensembl; ENST00000394013.6; ENSP00000377581.2; ENSG00000181852.18. [Q9H4P4-2]
DR Ensembl; ENST00000552656.5; ENSP00000447303.1; ENSG00000181852.18. [Q9H4P4-1]
DR Ensembl; ENST00000615206.4; ENSP00000484671.1; ENSG00000181852.18. [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 CTD; 10193; -.
DR DisGeNET; 10193; -.
DR GeneCards; RNF41; -.
DR HGNC; HGNC:18401; RNF41.
DR HPA; ENSG00000181852; Low tissue specificity.
DR neXtProt; NX_Q9H4P4; -.
DR OpenTargets; ENSG00000181852; -.
DR PharmGKB; PA134875033; -.
DR VEuPathDB; HostDB:ENSG00000181852; -.
DR eggNOG; KOG0297; Eukaryota.
DR GeneTree; ENSGT00530000063647; -.
DR HOGENOM; CLU_076732_0_0_1; -.
DR InParanoid; Q9H4P4; -.
DR OMA; SRQPTCP; -.
DR PhylomeDB; Q9H4P4; -.
DR TreeFam; TF351947; -.
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 BioGRID-ORCS; 10193; 34 hits in 1126 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 185 other tissues.
DR ExpressionAtlas; Q9H4P4; baseline and differential.
DR Genevisible; Q9H4P4; HS.
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:InterPro.
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:1901525; P:negative regulation of mitophagy; IEA:Ensembl.
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:0016567; P:protein ubiquitination; IBA:GO_Central.
DR GO; GO:0045619; P:regulation of lymphocyte differentiation; IEA:Ensembl.
DR GO; GO:0043408; P:regulation of MAPK cascade; IDA:MGI.
DR GO; GO:0045637; P:regulation of myeloid cell differentiation; IEA:Ensembl.
DR GO; GO:0051896; P:regulation of protein kinase B signaling; IDA:MGI.
DR GO; GO:2000377; P:regulation of reactive oxygen species metabolic process; IMP:UniProtKB.
DR Gene3D; 3.30.40.10; -; 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 Pfam; PF08941; USP8_interact; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF160088; SSF160088; 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 Reference proteome; Transferase; Ubl conjugation; Ubl conjugation pathway;
KW 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
