NMI_HUMAN
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 03-AUG-2022, entry version 185.
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; 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; Q9XRX5: HHLA3; NbExp=8; IntAct=EBI-372942, EBI-750554;
CC Q13287; Q9XRX5-2: HHLA3; NbExp=3; IntAct=EBI-372942, EBI-12051311;
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}.
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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; 87.
DR CORUM; Q13287; -.
DR IntAct; Q13287; 80.
DR MINT; Q13287; -.
DR STRING; 9606.ENSP00000243346; -.
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; Q13287; -.
DR PeptideAtlas; Q13287; -.
DR PRIDE; Q13287; -.
DR ProteomicsDB; 59282; -.
DR Antibodypedia; 1783; 272 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 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; KYQVFSG; -.
DR OrthoDB; 1133123at2759; -.
DR PhylomeDB; Q13287; -.
DR TreeFam; TF332752; -.
DR PathwayCommons; Q13287; -.
DR SignaLink; Q13287; -.
DR SIGNOR; Q13287; -.
DR BioGRID-ORCS; 9111; 27 hits in 1085 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 188 other tissues.
DR ExpressionAtlas; Q13287; baseline and differential.
DR Genevisible; Q13287; HS.
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:0003712; F:transcription coregulator activity; IEA:InterPro.
DR GO; GO:0060333; P:interferon-gamma-mediated signaling pathway; IEA:InterPro.
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 NIK/NF-kappaB signaling; 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 NIK/NF-kappaB signaling; 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 GO; GO:0006366; P:transcription by RNA polymerase II; IEA:InterPro.
DR Gene3D; 3.30.70.330; -; 2.
DR InterPro; IPR033527; NMI.
DR InterPro; IPR009909; Nmi/IFP35_dom.
DR InterPro; IPR009938; Nmi/IFP35_N.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR PANTHER; PTHR15225:SF4; PTHR15225:SF4; 1.
DR Pfam; PF07334; IFP_35_N; 1.
DR Pfam; PF07292; NID; 2.
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 I IFN-beta production.
FT Loss of TRIM21-mediated ubiquitination and decreased Sendai
FT virus-triggered type I IFN-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 I IFN-beta
FT production. Loss of TRIM21-mediated ubiquitination and
FT decreased Sendai virus-triggered type I IFN-beta
FT production; 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
