ID ECSIT_HUMAN Reviewed; 431 AA.
AC Q9BQ95; E9PAN9; K7EMM0; Q96HQ7; Q9NYI1;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 24-JAN-2024, entry version 160.
DE RecName: Full=Evolutionarily conserved signaling intermediate in Toll pathway, mitochondrial {ECO:0000305};
DE AltName: Full=Protein SITPEC;
DE Flags: Precursor;
GN Name=ECSIT {ECO:0000312|HGNC:HGNC:29548};
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), AND VARIANT CYS-278.
RA Fitzgerald S.N., Brady K.J., Moynagh P.N.;
RT "Nucleotide sequence of the human ECSIT cDNA.";
RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
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 MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Eye, Lung, and Pancreas;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION
RP WITH NDUFAF1.
RX PubMed=17344420; DOI=10.1101/gad.408407;
RA Vogel R.O., Janssen R.J.R.J., van den Brand M.A.M., Dieteren C.E.J.,
RA Verkaart S., Koopman W.J.H., Willems P.H.G.M., Pluk W.,
RA van den Heuvel L.P.W.J., Smeitink J.A.M., Nijtmans L.G.J.;
RT "Cytosolic signaling protein Ecsit also localizes to mitochondria where it
RT interacts with chaperone NDUFAF1 and functions in complex I assembly.";
RL Genes Dev. 21:615-624(2007).
RN [7]
RP INTERACTION WITH ACAD9.
RX PubMed=20816094; DOI=10.1016/j.cmet.2010.08.002;
RA Nouws J., Nijtmans L., Houten S.M., van den Brand M., Huynen M.,
RA Venselaar H., Hoefs S., Gloerich J., Kronick J., Hutchin T., Willems P.,
RA Rodenburg R., Wanders R., van den Heuvel L., Smeitink J., Vogel R.O.;
RT "Acyl-CoA dehydrogenase 9 is required for the biogenesis of oxidative
RT phosphorylation complex I.";
RL Cell Metab. 12:283-294(2010).
RN [8]
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 [9]
RP FUNCTION, SUBCELLULAR LOCATION, AND UBIQUITINATION BY TRAF6.
RX PubMed=21525932; DOI=10.1038/nature09973;
RA West A.P., Brodsky I.E., Rahner C., Woo D.K., Erdjument-Bromage H.,
RA Tempst P., Walsh M.C., Choi Y., Shadel G.S., Ghosh S.;
RT "TLR signalling augments macrophage bactericidal activity through
RT mitochondrial ROS.";
RL Nature 472:476-480(2011).
RN [10]
RP FUNCTION, AND INTERACTION WITH TRIM59.
RX PubMed=22588174; DOI=10.1016/j.bbrc.2012.05.028;
RA Kondo T., Watanabe M., Hatakeyama S.;
RT "TRIM59 interacts with ECSIT and negatively regulates NF-kappaB and IRF-
RT 3/7-mediated signal pathways.";
RL Biochem. Biophys. Res. Commun. 422:501-507(2012).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [12]
RP FUNCTION, INTERACTION WITH RELA AND NFKB1, SUBCELLULAR LOCATION,
RP UBIQUITINATION AT LYS-372, AND MUTAGENESIS OF LYS-372.
RX PubMed=25355951; DOI=10.1091/mbc.e14-08-1277;
RA Mi Wi S., Park J., Shim J.H., Chun E., Lee K.Y.;
RT "Ubiquitination of ECSIT is crucial for the activation of p65/p50 NF-
RT kappaBs in Toll-like receptor 4 signaling.";
RL Mol. Biol. Cell 26:151-160(2015).
RN [13]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH RIGI; IFIH1 AND MAVS.
RX PubMed=25228397; DOI=10.1159/000365971;
RA Lei C.Q., Zhang Y., Li M., Jiang L.Q., Zhong B., Kim Y.H., Shu H.B.;
RT "ECSIT bridges RIG-I-like receptors to VISA in signaling events of innate
RT antiviral responses.";
RL J. Innate Immun. 7:153-164(2015).
RN [14]
RP FUNCTION, AND INTERACTION WITH SQSTM1.
RX PubMed=31281713; DOI=10.4110/in.2019.19.e16;
RA Kim M.J., Min Y., Kwon J., Son J., Im J.S., Shin J., Lee K.Y.;
RT "p62 Negatively Regulates TLR4 Signaling via Functional Regulation of the
RT TRAF6-ECSIT Complex.";
RL Immune Netw. 19:e16-e16(2019).
RN [15]
RP FUNCTION, AND INTERACTION WITH CRBN.
RX PubMed=31620128; DOI=10.3389/fimmu.2019.02203;
RA Kim M.J., Min Y., Shim J.H., Chun E., Lee K.Y.;
RT "CRBN Is a Negative Regulator of Bactericidal Activity and Autophagy
RT Activation Through Inhibiting the Ubiquitination of ECSIT and BECN1.";
RL Front. Immunol. 10:2203-2203(2019).
RN [16]
RP IDENTIFICATION IN THE MCIA COMPLEX, AND FUNCTION.
RX PubMed=32320651; DOI=10.1016/j.celrep.2020.107541;
RA Formosa L.E., Muellner-Wong L., Reljic B., Sharpe A.J., Jackson T.D.,
RA Beilharz T.H., Stojanovski D., Lazarou M., Stroud D.A., Ryan M.T.;
RT "Dissecting the Roles of Mitochondrial Complex I Intermediate Assembly
RT Complex Factors in the Biogenesis of Complex I.";
RL Cell Rep. 31:107541-107541(2020).
RN [17]
RP INTERACTION WITH TMEM70 AND TMEM242.
RX PubMed=33753518; DOI=10.1073/pnas.2100558118;
RA Carroll J., He J., Ding S., Fearnley I.M., Walker J.E.;
RT "TMEM70 and TMEM242 help to assemble the rotor ring of human ATP synthase
RT and interact with assembly factors for complex I.";
RL Proc. Natl. Acad. Sci. U.S.A. 118:0-0(2021).
CC -!- FUNCTION: Adapter protein that plays a role in different signaling
CC pathways including TLRs and IL-1 pathways or innate antiviral induction
CC signaling. Plays a role in the activation of NF-kappa-B by forming a
CC signal complex with TRAF6 and TAK1/MAP3K7 to activate TAK1/MAP3K7
CC leading to activation of IKKs (PubMed:25355951, PubMed:31281713). Once
CC ubiquitinated, interacts with the dissociated RELA and NFKB1 proteins
CC and translocates to the nucleus where it induces NF-kappa-B-dependent
CC gene expression (PubMed:25355951). Plays a role in innate antiviral
CC immune response by bridging the pattern recognition receptors RIGI and
CC MDA5/IFIT1 to the MAVS complex at the mitochondrion (PubMed:25228397).
CC Promotes proteolytic activation of MAP3K1. Involved in the BMP
CC signaling pathway. Required for normal embryonic development (By
CC similarity). {ECO:0000250, ECO:0000269|PubMed:25228397,
CC ECO:0000269|PubMed:25355951, ECO:0000269|PubMed:31281713}.
CC -!- FUNCTION: As part of the MCIA complex, involved in the assembly of the
CC mitochondrial complex I. {ECO:0000269|PubMed:32320651}.
CC -!- SUBUNIT: Interacts with MAP3K1, SMAD4 and TRAF6. Interacts with SMAD1
CC only after BMP4-treatment (By similarity). Part of the mitochondrial
CC complex I assembly/MCIA complex that comprises at least the core
CC subunits TMEM126B, NDUFAF1, ECSIT and ACAD9 and complement subunits
CC such as COA1 and TMEM186 (PubMed:32320651). Interacts with NDUFAF1
CC (PubMed:17344420). Interacts with ACAD9 (PubMed:20816094). Interacts
CC with TRIM59 (PubMed:22588174). Interacts with TMEM70 and TMEM242
CC (PubMed:33753518). Interacts (when ubiquitinated) with NF-kappa-B
CC subunits RELA and NFKB1 (PubMed:25355951). Interacts with RIGI, IFIT1
CC and MAVS; these interactions promote RLR-mediated type I IFN induction
CC (PubMed:25228397). Interacts with SQSTM1; this interaction inhibits
CC TLR4 signaling via functional regulation of the TRAF6-ECSIT complex
CC (PubMed:31281713). Interacts with cereblon/CRBN; this interaction
CC inhibits the ubiquitination of ECSIT (PubMed:31620128).
CC {ECO:0000250|UniProtKB:Q9QZH6, ECO:0000269|PubMed:17344420,
CC ECO:0000269|PubMed:20816094, ECO:0000269|PubMed:22588174,
CC ECO:0000269|PubMed:25228397, ECO:0000269|PubMed:25355951,
CC ECO:0000269|PubMed:31281713, ECO:0000269|PubMed:31620128,
CC ECO:0000269|PubMed:32320651, ECO:0000269|PubMed:33753518}.
CC -!- INTERACTION:
CC Q9BQ95; Q9NX04: AIRIM; NbExp=3; IntAct=EBI-712452, EBI-8643161;
CC Q9BQ95; P02649: APOE; NbExp=4; IntAct=EBI-712452, EBI-1222467;
CC Q9BQ95; Q13515: BFSP2; NbExp=3; IntAct=EBI-712452, EBI-10229433;
CC Q9BQ95; Q9UI47-2: CTNNA3; NbExp=3; IntAct=EBI-712452, EBI-11962928;
CC Q9BQ95; Q86UW9: DTX2; NbExp=3; IntAct=EBI-712452, EBI-740376;
CC Q9BQ95; Q9Y285: FARSA; NbExp=2; IntAct=EBI-712452, EBI-725361;
CC Q9BQ95; P55040: GEM; NbExp=3; IntAct=EBI-712452, EBI-744104;
CC Q9BQ95; O15479: MAGEB2; NbExp=3; IntAct=EBI-712452, EBI-1057615;
CC Q9BQ95; Q13064: MKRN3; NbExp=3; IntAct=EBI-712452, EBI-2340269;
CC Q9BQ95; Q9UBU9: NXF1; NbExp=3; IntAct=EBI-712452, EBI-398874;
CC Q9BQ95; P49768: PSEN1; NbExp=4; IntAct=EBI-712452, EBI-297277;
CC Q9BQ95; P49810: PSEN2; NbExp=4; IntAct=EBI-712452, EBI-2010251;
CC Q9BQ95; A2RTX5: TARS3; NbExp=3; IntAct=EBI-712452, EBI-1056629;
CC Q9BQ95; Q96PN8: TSSK3; NbExp=3; IntAct=EBI-712452, EBI-3918381;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17344420,
CC ECO:0000269|PubMed:25355951}. Nucleus {ECO:0000269|PubMed:17344420,
CC ECO:0000269|PubMed:25355951}. Mitochondrion
CC {ECO:0000269|PubMed:17344420, ECO:0000269|PubMed:25228397}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q9BQ95-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9BQ95-2; Sequence=VSP_026345, VSP_026346;
CC Name=3;
CC IsoId=Q9BQ95-3; Sequence=VSP_046689;
CC Name=4;
CC IsoId=Q9BQ95-4; Sequence=VSP_055626, VSP_026346;
CC -!- PTM: Ubiquitinated on Lys-372; leading to translocation in the nucleus
CC together with RELA and NFKB1 and expression of NF-kappa-B-dependent
CC genes. {ECO:0000269|PubMed:25355951}.
CC -!- SIMILARITY: Belongs to the ECSIT family. {ECO:0000305}.
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DR EMBL; AF243044; AAF62100.1; -; mRNA.
DR EMBL; AK314905; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; CR457204; CAG33485.1; -; mRNA.
DR EMBL; AC008481; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC000193; AAH00193.1; -; mRNA.
DR EMBL; BC005119; AAH05119.1; -; mRNA.
DR EMBL; BC008279; AAH08279.1; -; mRNA.
DR CCDS; CCDS12262.1; -. [Q9BQ95-1]
DR CCDS; CCDS45979.1; -. [Q9BQ95-3]
DR CCDS; CCDS45980.1; -. [Q9BQ95-2]
DR CCDS; CCDS59353.1; -. [Q9BQ95-4]
DR RefSeq; NP_001135936.1; NM_001142464.2. [Q9BQ95-2]
DR RefSeq; NP_001135937.1; NM_001142465.2. [Q9BQ95-3]
DR RefSeq; NP_001230133.1; NM_001243204.1. [Q9BQ95-4]
DR RefSeq; NP_057665.2; NM_016581.4. [Q9BQ95-1]
DR AlphaFoldDB; Q9BQ95; -.
DR SASBDB; Q9BQ95; -.
DR BioGRID; 119446; 268.
DR ComplexPortal; CPX-6322; Mitochondrial complex I intermediate assembly (MCIA) complex.
DR CORUM; Q9BQ95; -.
DR IntAct; Q9BQ95; 106.
DR MINT; Q9BQ95; -.
DR STRING; 9606.ENSP00000270517; -.
DR iPTMnet; Q9BQ95; -.
DR PhosphoSitePlus; Q9BQ95; -.
DR SwissPalm; Q9BQ95; -.
DR BioMuta; ECSIT; -.
DR DMDM; 74752234; -.
DR EPD; Q9BQ95; -.
DR jPOST; Q9BQ95; -.
DR MassIVE; Q9BQ95; -.
DR MaxQB; Q9BQ95; -.
DR PaxDb; 9606-ENSP00000270517; -.
DR PeptideAtlas; Q9BQ95; -.
DR ProteomicsDB; 19054; -.
DR ProteomicsDB; 78645; -. [Q9BQ95-1]
DR ProteomicsDB; 78646; -. [Q9BQ95-2]
DR Pumba; Q9BQ95; -.
DR TopDownProteomics; Q9BQ95-1; -. [Q9BQ95-1]
DR Antibodypedia; 13189; 239 antibodies from 30 providers.
DR DNASU; 51295; -.
DR Ensembl; ENST00000252440.11; ENSP00000252440.6; ENSG00000130159.15. [Q9BQ95-2]
DR Ensembl; ENST00000270517.12; ENSP00000270517.6; ENSG00000130159.15. [Q9BQ95-1]
DR Ensembl; ENST00000417981.6; ENSP00000412712.1; ENSG00000130159.15. [Q9BQ95-3]
DR Ensembl; ENST00000591104.5; ENSP00000466559.1; ENSG00000130159.15. [Q9BQ95-4]
DR Ensembl; ENST00000688351.1; ENSP00000508502.1; ENSG00000130159.15. [Q9BQ95-1]
DR Ensembl; ENST00000690346.1; ENSP00000510792.1; ENSG00000130159.15. [Q9BQ95-1]
DR GeneID; 51295; -.
DR KEGG; hsa:51295; -.
DR MANE-Select; ENST00000270517.12; ENSP00000270517.6; NM_016581.5; NP_057665.2.
DR UCSC; uc002msb.4; human. [Q9BQ95-1]
DR AGR; HGNC:29548; -.
DR CTD; 51295; -.
DR DisGeNET; 51295; -.
DR GeneCards; ECSIT; -.
DR HGNC; HGNC:29548; ECSIT.
DR HPA; ENSG00000130159; Low tissue specificity.
DR MIM; 608388; gene.
DR neXtProt; NX_Q9BQ95; -.
DR OpenTargets; ENSG00000130159; -.
DR PharmGKB; PA147358104; -.
DR VEuPathDB; HostDB:ENSG00000130159; -.
DR eggNOG; KOG3941; Eukaryota.
DR GeneTree; ENSGT00390000005147; -.
DR HOGENOM; CLU_046917_0_0_1; -.
DR InParanoid; Q9BQ95; -.
DR OMA; NMADFGV; -.
DR OrthoDB; 4098911at2759; -.
DR PhylomeDB; Q9BQ95; -.
DR TreeFam; TF314943; -.
DR PathwayCommons; Q9BQ95; -.
DR Reactome; R-HSA-166058; MyD88:MAL(TIRAP) cascade initiated on plasma membrane.
DR Reactome; R-HSA-6799198; Complex I biogenesis.
DR Reactome; R-HSA-975138; TRAF6 mediated induction of NFkB and MAP kinases upon TLR7/8 or 9 activation.
DR Reactome; R-HSA-975871; MyD88 cascade initiated on plasma membrane.
DR SignaLink; Q9BQ95; -.
DR SIGNOR; Q9BQ95; -.
DR BioGRID-ORCS; 51295; 95 hits in 1180 CRISPR screens.
DR ChiTaRS; ECSIT; human.
DR GenomeRNAi; 51295; -.
DR Pharos; Q9BQ95; Tbio.
DR PRO; PR:Q9BQ95; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q9BQ95; Protein.
DR Bgee; ENSG00000130159; Expressed in apex of heart and 193 other cell types or tissues.
DR ExpressionAtlas; Q9BQ95; baseline and differential.
DR Genevisible; Q9BQ95; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005743; C:mitochondrial inner membrane; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0060090; F:molecular adaptor activity; IDA:UniProt.
DR GO; GO:0045087; P:innate immune response; IBA:GO_Central.
DR GO; GO:0032981; P:mitochondrial respiratory chain complex I assembly; NAS:ComplexPortal.
DR GO; GO:0051341; P:regulation of oxidoreductase activity; IDA:UniProtKB.
DR GO; GO:0061635; P:regulation of protein complex stability; IDA:UniProtKB.
DR GO; GO:0034142; P:toll-like receptor 4 signaling pathway; IDA:UniProt.
DR GO; GO:0007178; P:transmembrane receptor protein serine/threonine kinase signaling pathway; IBA:GO_Central.
DR InterPro; IPR029342; ECIST_C.
DR InterPro; IPR010418; ECSIT.
DR InterPro; IPR046448; ECSIT_N.
DR PANTHER; PTHR13113; ECSIT EVOLUTIONARILY CONSERVED SIGNALING INTERMEDIATE IN TOLL PATHWAYS; 1.
DR PANTHER; PTHR13113:SF1; EVOLUTIONARILY CONSERVED SIGNALING INTERMEDIATE IN TOLL PATHWAY, MITOCHONDRIAL; 1.
DR Pfam; PF14784; ECSIT_C; 1.
DR Pfam; PF06239; ECSIT_N; 1.
DR SMART; SM01284; ECSIT_Cterm; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Immunity; Innate immunity;
KW Isopeptide bond; Mitochondrion; Nucleus; Reference proteome;
KW Transit peptide; Ubl conjugation.
FT TRANSIT 1..48
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 49..431
FT /note="Evolutionarily conserved signaling intermediate in
FT Toll pathway, mitochondrial"
FT /id="PRO_0000291985"
FT REGION 400..431
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 372
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:25355951"
FT VAR_SEQ 35..248
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_046689"
FT VAR_SEQ 266..296
FT /note="GIQSPDQQAALARHNPARPVFVEGPFSLWLR -> ELTCCPRRRGKWKRRRR
FT SGTSTTRCSWTWSM (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055626"
FT VAR_SEQ 267..296
FT /note="IQSPDQQAALARHNPARPVFVEGPFSLWLR -> SGRDAGGVEPLLPDAAGP
FT GVCEEWLGQLRV (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_026345"
FT VAR_SEQ 297..431
FT /note="Missing (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_026346"
FT VARIANT 278
FT /note="R -> C (in dbSNP:rs34803265)"
FT /evidence="ECO:0000269|Ref.1"
FT /id="VAR_032907"
FT VARIANT 406
FT /note="G -> R (in dbSNP:rs2302971)"
FT /id="VAR_032908"
FT MUTAGEN 372
FT /note="K->A: Complete loss of interaction with RELA and
FT NFKB1 together with loss of NF-kappa-B-dependent gene
FT expression."
FT /evidence="ECO:0000269|PubMed:25355951"
FT CONFLICT 242
FT /note="V -> A (in Ref. 2; AK314905)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 431 AA; 49148 MW; 42AFEBFFA6953C80 CRC64;
MSWVQATLLA RGLCRAWGGT CGAALTGTSI SQVPRRLPRG LHCSAAAHSS EQSLVPSPPE
PRQRPTKALV PFEDLFGQAP GGERDKASFL QTVQKFAEHS VRKRGHIDFI YLALRKMREY
GVERDLAVYN QLLNIFPKEV FRPRNIIQRI FVHYPRQQEC GIAVLEQMEN HGVMPNKETE
FLLIQIFGRK SYPMLKLVRL KLWFPRFMNV NPFPVPRDLP QDPVELAMFG LRHMEPDLSA
RVTIYQVPLP KDSTGAADPP QPHIVGIQSP DQQAALARHN PARPVFVEGP FSLWLRNKCV
YYHILRADLL PPEEREVEET PEEWNLYYPM QLDLEYVRSG WDNYEFDINE VEEGPVFAMC
MAGAHDQATM AKWIQGLQET NPTLAQIPVV FRLAGSTREL QTSSAGLEEP PLPEDHQEED
DNLQRQQQGQ S
//
