ID NMI_HUMAN Reviewed; 307 AA. AC Q13287; B5BU69; Q53TI8; Q8WTW2; Q9BVE5; DT 14-AUG-2001, integrated into UniProtKB/Swiss-Prot. DT 17-OCT-2006, sequence version 2. DT 24-JAN-2024, entry version 193. DE RecName: Full=N-myc-interactor {ECO:0000303|PubMed:8668343}; DE Short=Nmi {ECO:0000303|PubMed:8668343}; DE AltName: Full=N-myc and STAT interactor {ECO:0000303|PubMed:26342464}; GN Name=NMI {ECO:0000312|HGNC:HGNC:7854}; 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]. RC TISSUE=Cervix carcinoma; RX PubMed=8668343; RA Bao J., Zervos A.S.; RT "Isolation and characterization of Nmi, a novel partner of Myc proteins."; RL Oncogene 12:2171-2176(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RX PubMed=19054851; DOI=10.1038/nmeth.1273; RA Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R., RA Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y., RA Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B., RA Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y., RA Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A., RA Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y., RA Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T., RA Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y., RA Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S., RA Nomura N.; RT "Human protein factory for converting the transcriptome into an in vitro- RT expressed proteome."; RL Nat. Methods 5:1011-1017(2008). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15815621; DOI=10.1038/nature03466; RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., RA Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 and RT 4."; RL Nature 434:724-731(2005). 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Bone marrow, and Placenta; 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 SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INDUCTION BY IFN-ALPHA ET RP IFN-GAMMA. RX PubMed=9781816; DOI=10.1089/jir.1998.18.767; RA Lebrun S.J., Shpall R.L., Naumovski L.; RT "Interferon-induced upregulation and cytoplasmic localization of Myc- RT interacting protein Nmi."; RL J. Interferon Cytokine Res. 18:767-771(1998). RN [7] RP FUNCTION, INTERACTION WITH STATS, AND INDUCTION BY IL2 AND IFN-GAMMA. RX PubMed=9989503; DOI=10.1016/s0092-8674(00)80965-4; RA Zhu M.-H., John S., Berg M., Leonard W.J.; RT "Functional association of Nmi with Stat5 and Stat1 in IL-2- and IFNgamma- RT mediated signaling."; RL Cell 96:121-130(1999). RN [8] RP FUNCTION, INDUCTION BY IFN-ALPHA, SUBCELLULAR LOCATION, AND INTERACTION RP WITH IFI35. RX PubMed=10779520; DOI=10.1074/jbc.m003177200; RA Zhou X., Liao J., Meyerdierks A., Feng L., Naumovski L., Bottger E.C., RA Omary M.B.; RT "Interferon-alpha induces nmi-IFP35 heterodimeric complex formation that is RT affected by the phosphorylation of IFP35."; RL J. Biol. Chem. 275:21364-21371(2000). RN [9] RP FUNCTION, INDUCTION BY IFN-ALPHA, SUBCELLULAR LOCATION, INTERACTION WITH RP IFI35, AND DOMAIN. RX PubMed=10950963; DOI=10.1074/jbc.m006975200; RA Chen J., Shpall R.L., Meyerdierks A., Hagemeier M., Boettger E.C., RA Naumovski L.; RT "Interferon-inducible Myc/STAT-interacting protein Nmi associates with IFP RT 35 into a high molecular mass complex and inhibits proteasome-mediated RT degradation of IFP 35."; RL J. Biol. Chem. 275:36278-36284(2000). 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [12] RP FUNCTION, INTERACTION WITH IFI35 AND TRIM21, DOMAIN, UBIQUITINATION, RP INDUCTION BY SENDAI VIRUS, AND MUTAGENESIS OF 1-MET--VAL-92; LYS-22; RP LYS-27; LYS-56; LYS-61; 103-GLY--ASP-192; LYS-176; LYS-183 AND RP 201-GLY--GLU-307. RX PubMed=26342464; DOI=10.1016/j.virol.2015.08.013; RA Das A., Dinh P.X., Pattnaik A.K.; RT "Trim21 regulates Nmi-IFI35 complex-mediated inhibition of innate antiviral RT response."; RL Virology 485:383-392(2015). RN [13] RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INTERACTION WITH RP TLR4. RX PubMed=29038465; DOI=10.1038/s41467-017-00930-9; RA Xiahou Z., Wang X., Shen J., Zhu X., Xu F., Hu R., Guo D., Li H., Tian Y., RA Liu Y., Liang H.; RT "NMI and IFP35 serve as proinflammatory DAMPs during cellular infection and RT injury."; RL Nat. Commun. 8:950-950(2017). RN [14] RP FUNCTION. RX PubMed=29350881; DOI=10.1111/apha.13037; RA Jian D., Wang W., Zhou X., Jia Z., Wang J., Yang M., Zhao W., Jiang Z., RA Hu X., Zhu J.; RT "Interferon-induced protein 35 inhibits endothelial cell proliferation, RT migration and re-endothelialization of injured arteries by inhibiting the RT nuclear factor-kappa B pathway."; RL Acta Physiol. 223:e13037-e13037(2018). RN [15] RP FUNCTION, INTERACTION WITH HUMAN CYTOMEGALOVIRUS PROTEIN UL23, AND RP SUBCELLULAR LOCATION. RX PubMed=29377960; DOI=10.1371/journal.ppat.1006867; RA Feng L., Sheng J., Vu G.P., Liu Y., Foo C., Wu S., Trang P., RA Paliza-Carre M., Ran Y., Yang X., Sun X., Deng Z., Zhou T., Lu S., Li H., RA Liu F.; RT "Human cytomegalovirus UL23 inhibits transcription of interferon-gamma RT stimulated genes and blocks antiviral interferon-gamma responses by RT interacting with human N-myc interactor protein."; RL PLoS Pathog. 14:e1006867-e1006867(2018). CC -!- FUNCTION: Acts as a signaling pathway regulator involved in innate CC immune system response (PubMed:9989503, PubMed:26342464, CC PubMed:29038465, PubMed:29350881). In response to interleukin 2/IL2 and CC interferon IFN-gamma/IFNG, interacts with signal transducer and CC activator of transcription/STAT which activate the transcription of CC downstream genes involved in a multitude of signals for development and CC homeostasis (PubMed:9989503, PubMed:29377960). Enhances the recruitment CC of CBP/p300 coactivators to STAT1 and STAT5, resulting in increased CC STAT1- and STAT5-dependent transcription (PubMed:9989503). In response CC to interferon IFN-alpha, associates in a complex with signaling pathway CC regulator IFI35 to regulate immune response; the complex formation CC prevents proteasome-mediated degradation of IFI35 (PubMed:10779520, CC PubMed:10950963). In complex with IFI35, inhibits virus-triggered type CC I IFN-beta production when ubiquitinated by ubiquitin-protein ligase CC TRIM21 (PubMed:26342464). In complex with IFI35, negatively regulates CC nuclear factor NF-kappa-B signaling by inhibiting the nuclear CC translocation, activation and transcription of NF-kappa-B subunit CC p65/RELA, resulting in the inhibition of endothelial cell CC proliferation, migration and re-endothelialization of injured arteries CC (PubMed:29350881). Negatively regulates virus-triggered type I CC interferon/IFN production by inducing proteosome-dependent degradation CC of IRF7, a transcriptional regulator of type I IFN, thereby interfering CC with cellular antiviral responses (By similarity). Beside its role as CC an intracellular signaling pathway regulator, also functions CC extracellularly as damage-associated molecular patterns (DAMPs) to CC promote inflammation, when actively released by macrophage to the CC extracellular space during cell injury or pathogen invasion CC (PubMed:29038465). Macrophage-secreted NMI activates NF-kappa-B CC signaling in adjacent macrophages through Toll-like receptor 4/TLR4 CC binding and activation, thereby inducing NF-kappa-B translocation from CC the cytoplasm into the nucleus which promotes the release of pro- CC inflammatory cytokines (PubMed:29038465). CC {ECO:0000250|UniProtKB:O35309, ECO:0000269|PubMed:10779520, CC ECO:0000269|PubMed:10950963, ECO:0000269|PubMed:26342464, CC ECO:0000269|PubMed:29038465, ECO:0000269|PubMed:29350881, CC ECO:0000269|PubMed:9989503}. CC -!- SUBUNIT: Interacts with MYCN and MYC, as well as with other CC transcription factors with a Zip, HLH or a HLH-Zip motif CC (PubMed:8668343). Interacts with all STAT proteins except STAT2 CC (PubMed:9989503). Interacts with IRF7, the interaction is direct and CC leads to the inhibition of IRF7-mediated type I IFN production (By CC similarity). Interacts (via coiled-coil domain) with TRIM21 (via the CC SPRY domain); the interaction leads to 'Lys-63'-linked ubiquitination CC of NMI (PubMed:26342464). Interacts with IFI35; the interaction is CC direct and is facilitated by TRIM21 (PubMed:10779520, PubMed:10950963, CC PubMed:26342464). Interacts with TLR4; the interaction is direct and CC leads to NF-kappa-B activation (PubMed:29038465). CC {ECO:0000250|UniProtKB:O35309, ECO:0000269|PubMed:10779520, CC ECO:0000269|PubMed:10950963, ECO:0000269|PubMed:26342464, CC ECO:0000269|PubMed:29038465, ECO:0000269|PubMed:8668343, CC ECO:0000269|PubMed:9989503}. CC -!- SUBUNIT: (Microbial infection) Interacts with human cytomegalovirus CC protein UL23; this interaction inhibits NMI-mediated transcription of CC interferon-gamma stimulated genes. {ECO:0000269|PubMed:29377960}. CC -!- INTERACTION: CC Q13287; Q9XRX5: ANKRD13C-DT; NbExp=8; IntAct=EBI-372942, EBI-750554; CC Q13287; Q9XRX5-2: ANKRD13C-DT; NbExp=3; IntAct=EBI-372942, EBI-12051311; CC Q13287; Q6PJG6: BRAT1; NbExp=3; IntAct=EBI-372942, EBI-10826195; CC Q13287; Q9HCU9: BRMS1; NbExp=7; IntAct=EBI-372942, EBI-714781; CC Q13287; Q8TAB5: C1orf216; NbExp=6; IntAct=EBI-372942, EBI-747505; CC Q13287; Q96LT7: C9orf72; NbExp=6; IntAct=EBI-372942, EBI-2961725; CC Q13287; Q6P9H4: CNKSR3; NbExp=6; IntAct=EBI-372942, EBI-10253274; CC Q13287; Q9H9Q2: COPS7B; NbExp=9; IntAct=EBI-372942, EBI-2510162; CC Q13287; Q9Y6C2: EMILIN1; NbExp=4; IntAct=EBI-372942, EBI-744586; CC Q13287; P23434: GCSH; NbExp=4; IntAct=EBI-372942, EBI-715444; CC Q13287; Q53XL7: GCSH; NbExp=6; IntAct=EBI-372942, EBI-10242961; CC Q13287; Q0D2H9: GOLGA8DP; NbExp=6; IntAct=EBI-372942, EBI-10181276; CC Q13287; Q8N4P3: HDDC3; NbExp=7; IntAct=EBI-372942, EBI-750003; CC Q13287; Q8N4P3-2: HDDC3; NbExp=6; IntAct=EBI-372942, EBI-12037393; CC Q13287; A0A0S2Z4Q4: HGS; NbExp=3; IntAct=EBI-372942, EBI-16429135; CC Q13287; O14964: HGS; NbExp=10; IntAct=EBI-372942, EBI-740220; CC Q13287; Q96IS6: HSPA8; NbExp=6; IntAct=EBI-372942, EBI-10289199; CC Q13287; P80217-2: IFI35; NbExp=4; IntAct=EBI-372942, EBI-12823003; CC Q13287; O95447: LCA5L; NbExp=6; IntAct=EBI-372942, EBI-8473670; CC Q13287; Q15013: MAD2L1BP; NbExp=3; IntAct=EBI-372942, EBI-712181; CC Q13287; Q9Y217: MTMR6; NbExp=6; IntAct=EBI-372942, EBI-766064; CC Q13287; Q96QG7: MTMR9; NbExp=9; IntAct=EBI-372942, EBI-744593; CC Q13287; P04198: MYCN; NbExp=3; IntAct=EBI-372942, EBI-878369; CC Q13287; Q5VTT5-2: MYOM3; NbExp=6; IntAct=EBI-372942, EBI-12247808; CC Q13287; Q13287: NMI; NbExp=6; IntAct=EBI-372942, EBI-372942; CC Q13287; O95171: SCEL; NbExp=7; IntAct=EBI-372942, EBI-7543896; CC Q13287; O95171-2: SCEL; NbExp=3; IntAct=EBI-372942, EBI-12056699; CC Q13287; Q86XK3: SFR1; NbExp=6; IntAct=EBI-372942, EBI-1104535; CC Q13287; O75971: SNAPC5; NbExp=8; IntAct=EBI-372942, EBI-749483; CC Q13287; O75971-2: SNAPC5; NbExp=3; IntAct=EBI-372942, EBI-12004298; CC Q13287; P56693: SOX10; NbExp=2; IntAct=EBI-372942, EBI-1167533; CC Q13287; P51692: STAT5B; NbExp=7; IntAct=EBI-372942, EBI-1186119; CC Q13287; P42226: STAT6; NbExp=2; IntAct=EBI-372942, EBI-1186478; CC Q13287; Q8NA92: THAP8; NbExp=3; IntAct=EBI-372942, EBI-717429; CC Q13287; O00463: TRAF5; NbExp=12; IntAct=EBI-372942, EBI-523498; CC Q13287; Q6ZMU5: TRIM72; NbExp=3; IntAct=EBI-372942, EBI-2341648; CC Q13287; Q13748: TUBA3D; NbExp=2; IntAct=EBI-372942, EBI-355068; CC Q13287; Q6PEY2: TUBA3E; NbExp=9; IntAct=EBI-372942, EBI-2551023; CC Q13287; P40222: TXLNA; NbExp=9; IntAct=EBI-372942, EBI-359793; CC Q13287; Q8N3L3: TXLNB; NbExp=9; IntAct=EBI-372942, EBI-6116822; CC Q13287; Q7KZS0: UBE2I; NbExp=3; IntAct=EBI-372942, EBI-10180829; CC Q13287; A8K2R3; NbExp=6; IntAct=EBI-372942, EBI-9977437; CC Q13287; O55170: Sox10; Xeno; NbExp=4; IntAct=EBI-372942, EBI-1185693; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10779520, CC ECO:0000269|PubMed:10950963, ECO:0000269|PubMed:29377960, CC ECO:0000269|PubMed:9781816}. Nucleus {ECO:0000269|PubMed:10950963, CC ECO:0000269|PubMed:9781816}. Secreted {ECO:0000269|PubMed:29038465}. CC Note=Cytoplasmic NMI localizes in punctate granular structures CC (PubMed:9781816, PubMed:10950963). Nuclear localization increased CC following IFN-alpha treatment (PubMed:9781816, PubMed:10950963). CC Extracelullar following secretion by macrophage (PubMed:29038465). CC {ECO:0000269|PubMed:10950963, ECO:0000269|PubMed:29038465, CC ECO:0000269|PubMed:9781816}. CC -!- TISSUE SPECIFICITY: Expressed in adult spleen, liver, and kidney CC (PubMed:9781816). Expressed in fetal thymus, liver, placenta, spleen, CC lung, and kidney but not brain (PubMed:9781816). Expressed in CC macrophages (PubMed:29038465). {ECO:0000269|PubMed:29038465, CC ECO:0000269|PubMed:9781816}. CC -!- INDUCTION: Up-regulated by interferon IFN-alpha and IFN-gamma CC (PubMed:9781816, PubMed:9989503, PubMed:10779520, PubMed:10950963). CC Induced by IL2/interleukin-2 (PubMed:9989503). Induced by Sendai virus CC (PubMed:26342464). {ECO:0000269|PubMed:10779520, CC ECO:0000269|PubMed:10950963, ECO:0000269|PubMed:26342464, CC ECO:0000269|PubMed:9781816, ECO:0000269|PubMed:9989503}. CC -!- DOMAIN: The coiled-coil domain is necessary for interaction with TRIM21 CC and for TRIM21-mediated ubiquitination of NMI. CC {ECO:0000269|PubMed:26342464}. CC -!- DOMAIN: The NID domains are necessary for the interaction with IFI35 CC (PubMed:26342464). The NID domain 1 is necessary and IRF7 (By CC similarity). {ECO:0000250|UniProtKB:O35309, CC ECO:0000269|PubMed:26342464}. CC -!- PTM: Ubiquitinated. 'Lys-63'-linked ubiquitination by TRIM21 promotes CC interaction with IFI35 and inhibits virus-triggered type I IFN-beta CC production. {ECO:0000269|PubMed:26342464}. CC -!- SIMILARITY: Belongs to the NMI family. {ECO:0000305}. CC -!- CAUTION: The TRIM21-mediated ubiquitinated residue is not conserved in CC mice, therefore it remains unclear whether the physiological role of CC NMI ubiquitination is preserved throughout mammals. CC {ECO:0000305|PubMed:26342464}. 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; U32849; AAC12949.1; -; mRNA. DR EMBL; AB451305; BAG70119.1; -; mRNA. DR EMBL; AB451436; BAG70250.1; -; mRNA. DR EMBL; AC009311; AAY15066.1; -; Genomic_DNA. DR EMBL; CH471058; EAX11513.1; -; Genomic_DNA. DR EMBL; BC001268; AAH01268.1; -; mRNA. DR EMBL; BC021987; AAH21987.1; -; mRNA. DR CCDS; CCDS2192.1; -. DR RefSeq; NP_004679.2; NM_004688.2. DR RefSeq; XP_005246998.1; XM_005246941.2. DR RefSeq; XP_016860736.1; XM_017005247.1. DR AlphaFoldDB; Q13287; -. DR BioGRID; 114561; 117. DR CORUM; Q13287; -. DR IntAct; Q13287; 80. DR MINT; Q13287; -. DR STRING; 9606.ENSP00000243346; -. DR GlyGen; Q13287; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q13287; -. DR PhosphoSitePlus; Q13287; -. DR BioMuta; NMI; -. DR DMDM; 116242679; -. DR EPD; Q13287; -. DR jPOST; Q13287; -. DR MassIVE; Q13287; -. DR MaxQB; Q13287; -. DR PaxDb; 9606-ENSP00000243346; -. DR PeptideAtlas; Q13287; -. DR ProteomicsDB; 59282; -. DR Pumba; Q13287; -. DR Antibodypedia; 1783; 320 antibodies from 28 providers. DR DNASU; 9111; -. DR Ensembl; ENST00000243346.10; ENSP00000243346.5; ENSG00000123609.11. DR GeneID; 9111; -. DR KEGG; hsa:9111; -. DR MANE-Select; ENST00000243346.10; ENSP00000243346.5; NM_004688.3; NP_004679.2. DR UCSC; uc002txi.3; human. DR AGR; HGNC:7854; -. DR CTD; 9111; -. DR DisGeNET; 9111; -. DR GeneCards; NMI; -. DR HGNC; HGNC:7854; NMI. DR HPA; ENSG00000123609; Low tissue specificity. DR MIM; 603525; gene. DR neXtProt; NX_Q13287; -. DR OpenTargets; ENSG00000123609; -. DR PharmGKB; PA31659; -. DR VEuPathDB; HostDB:ENSG00000123609; -. DR eggNOG; ENOG502QVH1; Eukaryota. DR GeneTree; ENSGT00530000063686; -. DR HOGENOM; CLU_047262_0_0_1; -. DR InParanoid; Q13287; -. DR OMA; IYAQIPE; -. DR OrthoDB; 5308373at2759; -. DR PhylomeDB; Q13287; -. DR TreeFam; TF332752; -. DR PathwayCommons; Q13287; -. DR Reactome; R-HSA-9692916; SARS-CoV-1 activates/modulates innate immune responses. DR SignaLink; Q13287; -. DR SIGNOR; Q13287; -. DR BioGRID-ORCS; 9111; 27 hits in 1160 CRISPR screens. DR ChiTaRS; NMI; human. DR GeneWiki; N-myc-interactor; -. DR GenomeRNAi; 9111; -. DR Pharos; Q13287; Tbio. DR PRO; PR:Q13287; -. DR Proteomes; UP000005640; Chromosome 2. DR RNAct; Q13287; Protein. DR Bgee; ENSG00000123609; Expressed in monocyte and 190 other cell types or tissues. DR ExpressionAtlas; Q13287; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:UniProtKB. DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB. DR GO; GO:0016020; C:membrane; IDA:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW. DR GO; GO:0002281; P:macrophage activation involved in immune response; IDA:UniProtKB. DR GO; GO:0008285; P:negative regulation of cell population proliferation; IMP:UniProtKB. DR GO; GO:0045824; P:negative regulation of innate immune response; IMP:UniProtKB. DR GO; GO:0032687; P:negative regulation of interferon-alpha production; IEA:Ensembl. DR GO; GO:0032688; P:negative regulation of interferon-beta production; IEA:Ensembl. DR GO; GO:1901223; P:negative regulation of non-canonical NF-kappaB signal transduction; IDA:UniProtKB. DR GO; GO:0050729; P:positive regulation of inflammatory response; ISS:UniProtKB. DR GO; GO:0045089; P:positive regulation of innate immune response; ISS:UniProtKB. DR GO; GO:1901224; P:positive regulation of non-canonical NF-kappaB signal transduction; IDA:UniProtKB. DR GO; GO:1902524; P:positive regulation of protein K48-linked ubiquitination; IEA:Ensembl. DR GO; GO:0070936; P:protein K48-linked ubiquitination; IEA:Ensembl. DR GO; GO:0007259; P:receptor signaling pathway via JAK-STAT; TAS:UniProtKB. DR GO; GO:0009615; P:response to virus; ISS:UniProtKB. DR GO; GO:0034142; P:toll-like receptor 4 signaling pathway; ISS:UniProtKB. DR CDD; cd12544; RRM_NMI; 1. DR Gene3D; 3.30.70.330; -; 2. DR InterPro; IPR009909; Nmi/IFP35_dom. DR InterPro; IPR009938; Nmi/IFP35_N. DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf. DR PANTHER; PTHR15225; INTERFERON-INDUCED PROTEIN 35/NMI N-MYC/STAT INTERACTING PROTEIN; 1. DR PANTHER; PTHR15225:SF4; N-MYC-INTERACTOR; 1. DR Pfam; PF07334; IFP_35_N; 1. DR Pfam; PF07292; NID; 2. DR Genevisible; Q13287; HS. PE 1: Evidence at protein level; KW Coiled coil; Cytoplasm; Host-virus interaction; Immunity; Innate immunity; KW Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome; Secreted; KW Ubl conjugation. FT CHAIN 1..307 FT /note="N-myc-interactor" FT /id="PRO_0000159702" FT DOMAIN 103..192 FT /note="NID 1" FT /evidence="ECO:0000305|PubMed:10950963" FT DOMAIN 201..292 FT /note="NID 2" FT /evidence="ECO:0000305|PubMed:10950963" FT REGION 1..24 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 30..64 FT /evidence="ECO:0000255" FT MOD_RES 16 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT CROSSLNK 22 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin)" FT /evidence="ECO:0000269|PubMed:26342464" FT VARIANT 16 FT /note="S -> L (in dbSNP:rs1048135)" FT /id="VAR_028190" FT MUTAGEN 22 FT /note="K->R: Loss of TRIM21-mediated ubiquitination and FT loss of Sendai virus-triggered type IIFN-beta production. FT Loss of TRIM21-mediated ubiquitination and decreased Sendai FT virus-triggered type IIFN-beta production; when associated FT with R-27." FT /evidence="ECO:0000269|PubMed:26342464" FT MUTAGEN 27 FT /note="K->R: No change in TRIM21-mediated ubiquitination FT and no change in Sendai virus-triggered type IIFN-beta FT production. Loss of TRIM21-mediated ubiquitination and FT decreased Sendai virus-triggered type IIFN-beta production; FT when associated with R-22." FT /evidence="ECO:0000269|PubMed:26342464" FT MUTAGEN 56 FT /note="K->R: No change in TRIM21-mediated ubiquitination; FT when associated with R-61." FT /evidence="ECO:0000269|PubMed:26342464" FT MUTAGEN 61 FT /note="K->R: No change in TRIM21-mediated ubiquitination; FT when associated with R-56." FT /evidence="ECO:0000269|PubMed:26342464" FT MUTAGEN 176 FT /note="K->R: No change in TRIM21-mediated ubiquitination; FT when associated with R-183." FT /evidence="ECO:0000269|PubMed:26342464" FT MUTAGEN 183 FT /note="K->R: No change in TRIM21-mediated ubiquitination; FT when associated with R-176." FT /evidence="ECO:0000269|PubMed:26342464" FT CONFLICT 41 FT /note="K -> R (in Ref. 5; AAH21987)" FT /evidence="ECO:0000305" FT CONFLICT 184 FT /note="S -> F (in Ref. 1; AAC12949)" FT /evidence="ECO:0000305" SQ SEQUENCE 307 AA; 35057 MW; EC228BD0C9E643F1 CRC64; MEADKDDTQQ ILKEHSPDEF IKDEQNKGLI DEITKKNIQL KKEIQKLETE LQEATKEFQI KEDIPETKMK FLSVETPEND SQLSNISCSF QVSSKVPYEI QKGQALITFE KEEVAQNVVS MSKHHVQIKD VNLEVTAKPV PLNSGVRFQV YVEVSKMKIN VTEIPDTLRE DQMRDKLELS FSKSRNGGGE VDRVDYDRQS GSAVITFVEI GVADKILKKK EYPLYINQTC HRVTVSPYTE IHLKKYQIFS GTSKRTVLLT GMEGIQMDEE IVEDLINIHF QRAKNGGGEV DVVKCSLGQP HIAYFEE //