EIF3M_HUMAN
ID EIF3M_HUMAN Reviewed; 374 AA.
AC Q7L2H7; A8K7X4; B4E2Q4; O60735; Q2F836; Q53HL6; Q9BXW1;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Eukaryotic translation initiation factor 3 subunit M {ECO:0000255|HAMAP-Rule:MF_03012};
DE Short=eIF3m {ECO:0000255|HAMAP-Rule:MF_03012};
DE AltName: Full=Fetal lung protein B5;
DE Short=hFL-B5;
DE AltName: Full=PCI domain-containing protein 1;
GN Name=EIF3M {ECO:0000255|HAMAP-Rule:MF_03012}; Synonyms=HFLB5, PCID1;
GN ORFNames=GA17, PNAS-125;
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), FUNCTION (MICROBIAL INFECTION), AND
RP TISSUE SPECIFICITY.
RC TISSUE=Fetal lung;
RX PubMed=15919898; DOI=10.1128/jvi.79.12.7419-7430.2005;
RA Perez A., Li Q.-X., Perez-Romero P., DeLassus G., Lopez S.R., Sutter S.,
RA McLaren N., Fuller A.O.;
RT "A new class of receptor for herpes simplex virus has heptad repeat motifs
RT that are common to membrane fusion proteins.";
RL J. Virol. 79:7419-7430(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ARG-346.
RC TISSUE=Dendritic cell;
RA Zhao Z., Huang X., Li N., Zhu X., Cao X.;
RT "A novel gene from human dendritic cell.";
RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
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 (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Synovium, Thalamus, and Trachea;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Coronary arterial endothelium;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [7]
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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Muscle, and Uterus;
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 [9]
RP PROTEIN SEQUENCE OF 2-19; 103-115; 184-201; 261-276 AND 279-290, CLEAVAGE
RP OF INITIATOR METHIONINE, ACETYLATION AT SER-2, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Hepatoma, and Lung carcinoma;
RA Bienvenut W.V., Boldt K., von Kriegsheim A.F., Kolch W., Vousden K.H.,
RA Lukashchuk N.;
RL Submitted (MAR-2008) to UniProtKB.
RN [10]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 4-139 (ISOFORM 1), AND INDUCTION.
RX PubMed=17719568; DOI=10.1016/j.brainres.2007.07.042;
RA Kobayashi K., Xin Y., Ymer S.I., Werther G.A., Russo V.C.;
RT "Subtractive hybridisation screen identifies genes regulated by glucose
RT deprivation in human neuroblastoma cells.";
RL Brain Res. 1170:129-139(2007).
RN [11]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 171-374 (ISOFORM 1/2).
RA Yu W.-Q., Sun B.-Z., Chai Y.-B., Zhu F., Liu X.-S., Li Z., Lu F., Yan W.,
RA Yang H., Zhao Z.-L.;
RT "Human acute promyelocytic leukemia cell line NB4's
RT apoptosis/differentiation related genes.";
RL Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
RN [12]
RP IDENTIFICATION IN THE EIF-3 COMPLEX, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=15601822; DOI=10.1101/gad.1255704;
RA Unbehaun A., Borukhov S.I., Hellen C.U.T., Pestova T.V.;
RT "Release of initiation factors from 48S complexes during ribosomal subunit
RT joining and the link between establishment of codon-anticodon base-pairing
RT and hydrolysis of eIF2-bound GTP.";
RL Genes Dev. 18:3078-3093(2004).
RN [13]
RP IDENTIFICATION.
RX PubMed=15904532; DOI=10.1186/1741-7007-3-14;
RA Zhou C., Arslan F., Wee S., Krishnan S., Ivanov A.R., Oliva A.,
RA Leatherwood J., Wolf D.A.;
RT "PCI proteins eIF3e and eIF3m define distinct translation initiation factor
RT 3 complexes.";
RL BMC Biol. 3:14-14(2005).
RN [14]
RP MUTAGENESIS OF LEU-350; LEU-354; LEU-361 AND VAL-364.
RX PubMed=15919899; DOI=10.1128/jvi.79.12.7431-7437.2005;
RA Perez-Romero P., Fuller A.O.;
RT "The C-terminus of the B5 receptor for herpes simplex virus contains a
RT functional region important for infection.";
RL J. Virol. 79:7431-7437(2005).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [16]
RP CHARACTERIZATION OF THE EIF-3 COMPLEX.
RX PubMed=15703437; DOI=10.1261/rna.7215305;
RA Kolupaeva V.G., Unbehaun A., Lomakin I.B., Hellen C.U.T., Pestova T.V.;
RT "Binding of eukaryotic initiation factor 3 to ribosomal 40S subunits and
RT its role in ribosomal dissociation and anti-association.";
RL RNA 11:470-486(2005).
RN [17]
RP IDENTIFICATION IN THE EIF-3 COMPLEX, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=16766523; DOI=10.1074/jbc.m605418200;
RA LeFebvre A.K., Korneeva N.L., Trutschl M., Cvek U., Duzan R.D.,
RA Bradley C.A., Hershey J.W.B., Rhoads R.E.;
RT "Translation initiation factor eIF4G-1 binds to eIF3 through the eIF3e
RT subunit.";
RL J. Biol. Chem. 281:22917-22932(2006).
RN [18]
RP FUNCTION, AND IDENTIFICATION IN THE EIF-3 COMPLEX.
RX PubMed=17403899; DOI=10.1128/mcb.01724-06;
RA Luke-Glaser S., Roy M., Larsen B., Le Bihan T., Metalnikov P., Tyers M.,
RA Peter M., Pintard L.;
RT "CIF-1, a shared subunit of the COP9/signalosome and eukaryotic initiation
RT factor 3 complexes, regulates MEL-26 levels in the Caenorhabditis elegans
RT embryo.";
RL Mol. Cell. Biol. 27:4526-4540(2007).
RN [19]
RP IDENTIFICATION IN THE EIF-3 COMPLEX, CHARACTERIZATION OF THE EIF-3 COMPLEX,
RP CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, AND MASS
RP SPECTROMETRY.
RX PubMed=17322308; DOI=10.1074/mcp.m600399-mcp200;
RA Damoc E., Fraser C.S., Zhou M., Videler H., Mayeur G.L., Hershey J.W.B.,
RA Doudna J.A., Robinson C.V., Leary J.A.;
RT "Structural characterization of the human eukaryotic initiation factor 3
RT protein complex by mass spectrometry.";
RL Mol. Cell. Proteomics 6:1135-1146(2007).
RN [20]
RP IDENTIFICATION IN THE EIF-3 COMPLEX, CHARACTERIZATION OF THE EIF-3 COMPLEX,
RP MASS SPECTROMETRY, AND INTERACTION WITH EIF3B; EIF3F AND EIF3H.
RX PubMed=18599441; DOI=10.1073/pnas.0801313105;
RA Zhou M., Sandercock A.M., Fraser C.S., Ridlova G., Stephens E.,
RA Schenauer M.R., Yokoi-Fong T., Barsky D., Leary J.A., Hershey J.W.B.,
RA Doudna J.A., Robinson C.V.;
RT "Mass spectrometry reveals modularity and a complete subunit interaction
RT map of the eukaryotic translation factor eIF3.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:18139-18144(2008).
RN [21]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [22]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-254, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [23]
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 [24]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE
RP ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [25]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [26]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2; SER-152 AND SER-367, AND
RP IDENTIFICATION BY 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 [27]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [28]
RP FUNCTION, AND IDENTIFICATION IN THE EIF-3 COMPLEX.
RX PubMed=25849773; DOI=10.1038/nature14267;
RA Lee A.S., Kranzusch P.J., Cate J.H.;
RT "eIF3 targets cell-proliferation messenger RNAs for translational
RT activation or repression.";
RL Nature 522:111-114(2015).
RN [29]
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 [30]
RP FUNCTION.
RX PubMed=27462815; DOI=10.1038/nature18954;
RA Lee A.S., Kranzusch P.J., Doudna J.A., Cate J.H.;
RT "eIF3d is an mRNA cap-binding protein that is required for specialized
RT translation initiation.";
RL Nature 536:96-99(2016).
RN [31]
RP VARIANT [LARGE SCALE ANALYSIS] GLY-80.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Component of the eukaryotic translation initiation factor 3
CC (eIF-3) complex, which is required for several steps in the initiation
CC of protein synthesis (PubMed:17403899, PubMed:25849773,
CC PubMed:27462815). The eIF-3 complex associates with the 40S ribosome
CC and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-
CC tRNAi and eIF-5 to form the 43S pre-initiation complex (43S PIC). The
CC eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning
CC of the mRNA for AUG recognition. The eIF-3 complex is also required for
CC disassembly and recycling of post-termination ribosomal complexes and
CC subsequently prevents premature joining of the 40S and 60S ribosomal
CC subunits prior to initiation (PubMed:17403899). The eIF-3 complex
CC specifically targets and initiates translation of a subset of mRNAs
CC involved in cell proliferation, including cell cycling, differentiation
CC and apoptosis, and uses different modes of RNA stem-loop binding to
CC exert either translational activation or repression (PubMed:25849773).
CC {ECO:0000255|HAMAP-Rule:MF_03012, ECO:0000269|PubMed:17403899,
CC ECO:0000269|PubMed:25849773, ECO:0000269|PubMed:27462815}.
CC -!- FUNCTION: (Microbial infection) May favor virus entry in case of
CC infection with herpes simplex virus 1 (HSV1) or herpes simplex virus 2
CC (HSV2). {ECO:0000269|PubMed:15919898}.
CC -!- SUBUNIT: Component of the eukaryotic translation initiation factor 3
CC (eIF-3) complex, which is composed of 13 subunits: EIF3A, EIF3B, EIF3C,
CC EIF3D, EIF3E, EIF3F, EIF3G, EIF3H, EIF3I, EIF3J, EIF3K, EIF3L and
CC EIF3M. The eIF-3 complex appears to include 3 stable modules: module A
CC is composed of EIF3A, EIF3B, EIF3G and EIF3I; module B is composed of
CC EIF3F, EIF3H, and EIF3M; and module C is composed of EIF3C, EIF3D,
CC EIF3E, EIF3K and EIF3L. EIF3C of module C binds EIF3B of module A and
CC EIF3H of module B, thereby linking the three modules. EIF3J is a labile
CC subunit that binds to the eIF-3 complex via EIF3B. The eIF-3 complex
CC interacts with RPS6KB1 under conditions of nutrient depletion.
CC Mitogenic stimulation leads to binding and activation of a complex
CC composed of MTOR and RPTOR, leading to phosphorylation and release of
CC RPS6KB1 and binding of EIF4B to eIF-3. {ECO:0000255|HAMAP-
CC Rule:MF_03012, ECO:0000269|PubMed:15601822,
CC ECO:0000269|PubMed:16766523, ECO:0000269|PubMed:17322308,
CC ECO:0000269|PubMed:17403899, ECO:0000269|PubMed:18599441}.
CC -!- INTERACTION:
CC Q7L2H7; Q9P2A4: ABI3; NbExp=3; IntAct=EBI-353901, EBI-742038;
CC Q7L2H7; P55884: EIF3B; NbExp=4; IntAct=EBI-353901, EBI-366696;
CC Q7L2H7; O00303: EIF3F; NbExp=19; IntAct=EBI-353901, EBI-711990;
CC Q7L2H7; O15372: EIF3H; NbExp=6; IntAct=EBI-353901, EBI-709735;
CC Q7L2H7; Q8N7C3: TRIML2; NbExp=3; IntAct=EBI-353901, EBI-11059915;
CC Q7L2H7; O75800: ZMYND10; NbExp=3; IntAct=EBI-353901, EBI-747061;
CC Q7L2H7; Q6ZMS7-2: ZNF783; NbExp=3; IntAct=EBI-353901, EBI-17789949;
CC Q7L2H7; Q9Q2G4: ORF; Xeno; NbExp=2; IntAct=EBI-353901, EBI-6248094;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03012}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q7L2H7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q7L2H7-2; Sequence=VSP_056911;
CC -!- TISSUE SPECIFICITY: Broadly expressed. {ECO:0000269|PubMed:15919898}.
CC -!- INDUCTION: By glucose deprivation in neuroblastoma cells.
CC {ECO:0000269|PubMed:17719568}.
CC -!- MASS SPECTROMETRY: Mass=42413.8; Method=Unknown;
CC Evidence={ECO:0000269|PubMed:17322308};
CC -!- MASS SPECTROMETRY: Mass=42414.7; Mass_error=0.2; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:18599441};
CC -!- SIMILARITY: Belongs to the eIF-3 subunit M family. {ECO:0000255|HAMAP-
CC Rule:MF_03012}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK07542.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAK07542.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AY769947; AAX12524.1; -; mRNA.
DR EMBL; AF064603; AAC17108.1; -; mRNA.
DR EMBL; CR450300; CAG29296.1; -; mRNA.
DR EMBL; AK292139; BAF84828.1; -; mRNA.
DR EMBL; AK304378; BAG65216.1; -; mRNA.
DR EMBL; AK312512; BAG35413.1; -; mRNA.
DR EMBL; AK222564; BAD96284.1; -; mRNA.
DR EMBL; AL078477; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471064; EAW68217.1; -; Genomic_DNA.
DR EMBL; BC019103; AAH19103.1; -; mRNA.
DR EMBL; BC051292; AAH51292.1; -; mRNA.
DR EMBL; DQ185042; ABD14422.1; -; mRNA.
DR EMBL; AF277183; AAK07542.1; ALT_SEQ; mRNA.
DR CCDS; CCDS76392.1; -. [Q7L2H7-2]
DR CCDS; CCDS7880.1; -. [Q7L2H7-1]
DR RefSeq; NP_001294858.1; NM_001307929.1. [Q7L2H7-2]
DR RefSeq; NP_006351.2; NM_006360.5. [Q7L2H7-1]
DR PDB; 3J8B; EM; -; M=1-335.
DR PDB; 3J8C; EM; -; M=1-335.
DR PDB; 6FEC; EM; 6.30 A; 8=1-374.
DR PDB; 6YBD; EM; 3.30 A; 6=1-374.
DR PDB; 6ZMW; EM; 3.70 A; 6=1-374.
DR PDB; 6ZON; EM; 3.00 A; M=1-374.
DR PDB; 6ZP4; EM; 2.90 A; M=1-374.
DR PDB; 6ZVJ; EM; 3.80 A; M=11-372.
DR PDB; 7A09; EM; 3.50 A; M=1-374.
DR PDBsum; 3J8B; -.
DR PDBsum; 3J8C; -.
DR PDBsum; 6FEC; -.
DR PDBsum; 6YBD; -.
DR PDBsum; 6ZMW; -.
DR PDBsum; 6ZON; -.
DR PDBsum; 6ZP4; -.
DR PDBsum; 6ZVJ; -.
DR PDBsum; 7A09; -.
DR AlphaFoldDB; Q7L2H7; -.
DR SMR; Q7L2H7; -.
DR BioGRID; 115743; 123.
DR ComplexPortal; CPX-6036; Eukaryotic translation initiation factor 3 complex.
DR CORUM; Q7L2H7; -.
DR DIP; DIP-31256N; -.
DR IntAct; Q7L2H7; 59.
DR MINT; Q7L2H7; -.
DR STRING; 9606.ENSP00000436049; -.
DR GlyGen; Q7L2H7; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q7L2H7; -.
DR MetOSite; Q7L2H7; -.
DR PhosphoSitePlus; Q7L2H7; -.
DR SwissPalm; Q7L2H7; -.
DR BioMuta; EIF3M; -.
DR DMDM; 74754296; -.
DR EPD; Q7L2H7; -.
DR jPOST; Q7L2H7; -.
DR MassIVE; Q7L2H7; -.
DR MaxQB; Q7L2H7; -.
DR PaxDb; Q7L2H7; -.
DR PeptideAtlas; Q7L2H7; -.
DR PRIDE; Q7L2H7; -.
DR ProteomicsDB; 5844; -.
DR ProteomicsDB; 68761; -. [Q7L2H7-1]
DR Antibodypedia; 25628; 265 antibodies from 35 providers.
DR DNASU; 10480; -.
DR Ensembl; ENST00000524896.5; ENSP00000436787.1; ENSG00000149100.13. [Q7L2H7-2]
DR Ensembl; ENST00000531120.6; ENSP00000436049.1; ENSG00000149100.13. [Q7L2H7-1]
DR GeneID; 10480; -.
DR KEGG; hsa:10480; -.
DR MANE-Select; ENST00000531120.6; ENSP00000436049.1; NM_006360.6; NP_006351.2.
DR UCSC; uc001mtu.5; human. [Q7L2H7-1]
DR CTD; 10480; -.
DR DisGeNET; 10480; -.
DR GeneCards; EIF3M; -.
DR HGNC; HGNC:24460; EIF3M.
DR HPA; ENSG00000149100; Low tissue specificity.
DR MIM; 609641; gene.
DR neXtProt; NX_Q7L2H7; -.
DR OpenTargets; ENSG00000149100; -.
DR PharmGKB; PA162384944; -.
DR VEuPathDB; HostDB:ENSG00000149100; -.
DR eggNOG; KOG2753; Eukaryota.
DR GeneTree; ENSGT00390000004456; -.
DR HOGENOM; CLU_035254_1_0_1; -.
DR InParanoid; Q7L2H7; -.
DR OMA; REDAQRC; -.
DR OrthoDB; 679771at2759; -.
DR PhylomeDB; Q7L2H7; -.
DR TreeFam; TF106148; -.
DR PathwayCommons; Q7L2H7; -.
DR Reactome; R-HSA-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR Reactome; R-HSA-72649; Translation initiation complex formation.
DR Reactome; R-HSA-72689; Formation of a pool of free 40S subunits.
DR Reactome; R-HSA-72695; Formation of the ternary complex, and subsequently, the 43S complex.
DR Reactome; R-HSA-72702; Ribosomal scanning and start codon recognition.
DR Reactome; R-HSA-72706; GTP hydrolysis and joining of the 60S ribosomal subunit.
DR SignaLink; Q7L2H7; -.
DR SIGNOR; Q7L2H7; -.
DR BioGRID-ORCS; 10480; 662 hits in 1090 CRISPR screens.
DR ChiTaRS; EIF3M; human.
DR GeneWiki; EIF3M; -.
DR GenomeRNAi; 10480; -.
DR Pharos; Q7L2H7; Tbio.
DR PRO; PR:Q7L2H7; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q7L2H7; protein.
DR Bgee; ENSG00000149100; Expressed in germinal epithelium of ovary and 204 other tissues.
DR ExpressionAtlas; Q7L2H7; baseline and differential.
DR Genevisible; Q7L2H7; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0016282; C:eukaryotic 43S preinitiation complex; IEA:UniProtKB-UniRule.
DR GO; GO:0033290; C:eukaryotic 48S preinitiation complex; IEA:UniProtKB-UniRule.
DR GO; GO:0005852; C:eukaryotic translation initiation factor 3 complex; IDA:UniProtKB.
DR GO; GO:0071541; C:eukaryotic translation initiation factor 3 complex, eIF3m; IEA:UniProtKB-UniRule.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-UniRule.
DR GO; GO:0031369; F:translation initiation factor binding; IEA:Ensembl.
DR GO; GO:0002183; P:cytoplasmic translational initiation; IBA:GO_Central.
DR GO; GO:0001732; P:formation of cytoplasmic translation initiation complex; IC:ComplexPortal.
DR GO; GO:0006413; P:translational initiation; IC:UniProtKB.
DR HAMAP; MF_03012; eIF3m; 1.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR045237; COPS7/eIF3m.
DR InterPro; IPR027528; eIF3m.
DR InterPro; IPR040750; eIF3m_C_helix.
DR InterPro; IPR000717; PCI_dom.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR15350; PTHR15350; 1.
DR Pfam; PF18005; eIF3m_C_helix; 1.
DR Pfam; PF01399; PCI; 1.
DR SMART; SM00088; PINT; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS50250; PCI; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm;
KW Direct protein sequencing; Host-virus interaction; Initiation factor;
KW Phosphoprotein; Protein biosynthesis; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03012,
FT ECO:0000269|PubMed:17322308, ECO:0000269|Ref.9,
FT ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:22814378"
FT CHAIN 2..374
FT /note="Eukaryotic translation initiation factor 3 subunit
FT M"
FT /id="PRO_0000308195"
FT DOMAIN 180..339
FT /note="PCI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT REGION 344..374
FT /note="Interaction with HSV-1 and HSV-2"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03012,
FT ECO:0000269|PubMed:17322308, ECO:0000269|Ref.9,
FT ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:22814378"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 152
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 254
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 367
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 13..144
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056911"
FT VARIANT 37
FT /note="G -> R (in dbSNP:rs11557143)"
FT /id="VAR_036752"
FT VARIANT 80
FT /note="E -> G (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036753"
FT VARIANT 346
FT /note="Q -> R (in dbSNP:rs1802363)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_036754"
FT MUTAGEN 350
FT /note="L->P: Reduces HSV binding and entry."
FT /evidence="ECO:0000269|PubMed:15919899"
FT MUTAGEN 354
FT /note="L->P: Reduces HSV binding and entry."
FT /evidence="ECO:0000269|PubMed:15919899"
FT MUTAGEN 361
FT /note="L->P: Reduces HSV binding and entry."
FT /evidence="ECO:0000269|PubMed:15919899"
FT MUTAGEN 364
FT /note="V->P: Reduces HSV binding and entry."
FT /evidence="ECO:0000269|PubMed:15919899"
FT CONFLICT 64
FT /note="M -> V (in Ref. 2; AAC17108)"
FT /evidence="ECO:0000305"
FT CONFLICT 121
FT /note="Y -> C (in Ref. 10; ABD14422)"
FT /evidence="ECO:0000305"
FT CONFLICT 129..131
FT /note="KVA -> EVV (in Ref. 2; AAC17108)"
FT /evidence="ECO:0000305"
FT CONFLICT 173
FT /note="V -> A (in Ref. 2; AAC17108)"
FT /evidence="ECO:0000305"
FT CONFLICT 210..211
FT /note="RA -> EP (in Ref. 2; AAC17108)"
FT /evidence="ECO:0000305"
FT CONFLICT 287
FT /note="V -> I (in Ref. 2; AAC17108)"
FT /evidence="ECO:0000305"
FT CONFLICT 297
FT /note="M -> V (in Ref. 5; BAD96284)"
FT /evidence="ECO:0000305"
FT STRAND 10..14
FT /evidence="ECO:0007829|PDB:6YBD"
FT HELIX 18..24
FT /evidence="ECO:0007829|PDB:6YBD"
FT HELIX 31..34
FT /evidence="ECO:0007829|PDB:6YBD"
FT TURN 35..38
FT /evidence="ECO:0007829|PDB:6YBD"
FT STRAND 39..41
FT /evidence="ECO:0007829|PDB:6YBD"
FT STRAND 44..50
FT /evidence="ECO:0007829|PDB:6YBD"
FT TURN 51..53
FT /evidence="ECO:0007829|PDB:6YBD"
FT TURN 61..63
FT /evidence="ECO:0007829|PDB:6YBD"
FT HELIX 64..67
FT /evidence="ECO:0007829|PDB:6YBD"
FT TURN 68..71
FT /evidence="ECO:0007829|PDB:6YBD"
FT TURN 74..76
FT /evidence="ECO:0007829|PDB:6YBD"
FT STRAND 80..87
FT /evidence="ECO:0007829|PDB:6YBD"
FT HELIX 88..91
FT /evidence="ECO:0007829|PDB:6YBD"
FT TURN 92..94
FT /evidence="ECO:0007829|PDB:6YBD"
FT HELIX 99..105
FT /evidence="ECO:0007829|PDB:6YBD"
FT HELIX 106..108
FT /evidence="ECO:0007829|PDB:6YBD"
FT STRAND 111..114
FT /evidence="ECO:0007829|PDB:6YBD"
FT HELIX 117..127
FT /evidence="ECO:0007829|PDB:6YBD"
FT TURN 128..130
FT /evidence="ECO:0007829|PDB:6YBD"
FT STRAND 133..135
FT /evidence="ECO:0007829|PDB:6YBD"
FT TURN 136..139
FT /evidence="ECO:0007829|PDB:6YBD"
FT TURN 142..144
FT /evidence="ECO:0007829|PDB:6YBD"
FT STRAND 149..152
FT /evidence="ECO:0007829|PDB:6YBD"
FT HELIX 155..167
FT /evidence="ECO:0007829|PDB:6YBD"
FT TURN 168..171
FT /evidence="ECO:0007829|PDB:6YBD"
FT HELIX 175..192
FT /evidence="ECO:0007829|PDB:6YBD"
FT HELIX 199..211
FT /evidence="ECO:0007829|PDB:6YBD"
FT STRAND 220..223
FT /evidence="ECO:0007829|PDB:6YBD"
FT TURN 228..230
FT /evidence="ECO:0007829|PDB:6YBD"
FT TURN 234..238
FT /evidence="ECO:0007829|PDB:6YBD"
FT TURN 240..242
FT /evidence="ECO:0007829|PDB:6YBD"
FT HELIX 252..256
FT /evidence="ECO:0007829|PDB:6YBD"
FT HELIX 263..266
FT /evidence="ECO:0007829|PDB:6YBD"
FT HELIX 269..277
FT /evidence="ECO:0007829|PDB:6YBD"
FT HELIX 281..284
FT /evidence="ECO:0007829|PDB:6YBD"
FT STRAND 286..290
FT /evidence="ECO:0007829|PDB:6YBD"
FT TURN 294..296
FT /evidence="ECO:0007829|PDB:6YBD"
FT HELIX 297..300
FT /evidence="ECO:0007829|PDB:6YBD"
FT HELIX 308..317
FT /evidence="ECO:0007829|PDB:6YBD"
FT STRAND 326..328
FT /evidence="ECO:0007829|PDB:6YBD"
FT HELIX 342..345
FT /evidence="ECO:0007829|PDB:6YBD"
FT HELIX 348..354
FT /evidence="ECO:0007829|PDB:6YBD"
SQ SEQUENCE 374 AA; 42503 MW; 63736CA2B093D794 CRC64;
MSVPAFIDIS EEDQAAELRA YLKSKGAEIS EENSEGGLHV DLAQIIEACD VCLKEDDKDV
ESVMNSVVSL LLILEPDKQE ALIESLCEKL VKFREGERPS LRLQLLSNLF HGMDKNTPVR
YTVYCSLIKV AASCGAIQYI PTELDQVRKW ISDWNLTTEK KHTLLRLLYE ALVDCKKSDA
ASKVMVELLG SYTEDNASQA RVDAHRCIVR ALKDPNAFLF DHLLTLKPVK FLEGELIHDL
LTIFVSAKLA SYVKFYQNNK DFIDSLGLLH EQNMAKMRLL TFMGMAVENK EISFDTMQQE
LQIGADDVEA FVIDAVRTKM VYCKIDQTQR KVVVSHSTHR TFGKQQWQQL YDTLNAWKQN
LNKVKNSLLS LSDT
