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 27-MAR-2024, entry version 167. 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}; 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; 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 PDB; 7QP6; EM; 4.70 A; 6=1-374. DR PDB; 7QP7; EM; 3.70 A; 6=1-374. DR PDB; 8PPL; EM; 2.65 A; I6=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 PDBsum; 7QP6; -. DR PDBsum; 7QP7; -. DR PDBsum; 8PPL; -. DR AlphaFoldDB; Q7L2H7; -. DR EMDB; EMD-10769; -. DR EMDB; EMD-11302; -. DR EMDB; EMD-11325; -. DR EMDB; EMD-11335; -. DR EMDB; EMD-11458; -. DR EMDB; EMD-11602; -. DR EMDB; EMD-14113; -. DR EMDB; EMD-14114; -. DR EMDB; EMD-17805; -. DR EMDB; EMD-4242; -. DR SMR; Q7L2H7; -. DR BioGRID; 115743; 190. DR ComplexPortal; CPX-6036; Eukaryotic translation initiation factor 3 complex. DR CORUM; Q7L2H7; -. DR DIP; DIP-31256N; -. DR IntAct; Q7L2H7; 63. DR MINT; Q7L2H7; -. DR STRING; 9606.ENSP00000436049; -. DR GlyGen; Q7L2H7; 2 sites, 1 O-linked glycan (2 sites). 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; 9606-ENSP00000436049; -. DR PeptideAtlas; Q7L2H7; -. DR ProteomicsDB; 5844; -. DR ProteomicsDB; 68761; -. [Q7L2H7-1] DR Pumba; Q7L2H7; -. DR Antibodypedia; 25628; 294 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 AGR; HGNC:24460; -. 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; AQRCILA; -. DR OrthoDB; 2875448at2759; -. 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; 689 hits in 1168 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 206 other cell types or tissues. DR ExpressionAtlas; Q7L2H7; baseline and differential. 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; NAS: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; COP9 SIGNALOSOME COMPLEX SUBUNIT 7/DENDRITIC CELL PROTEIN GA17; 1. DR PANTHER; PTHR15350:SF2; EUKARYOTIC TRANSLATION INITIATION FACTOR 3 SUBUNIT M; 1. DR Pfam; PF18005; eIF3m_C_helix; 1. DR Pfam; PF01399; PCI; 1. DR SMART; SM00088; PINT; 1. DR SUPFAM; SSF48371; ARM repeat; 1. DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1. DR PROSITE; PS50250; PCI; 1. DR Genevisible; Q7L2H7; HS. 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 //