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Eukaryotic translation initiation factor 3 subunit M (eIF3m) (Fetal lung protein B5) (hFL-B5) (PCI domain-containing protein 1)

 EIF3M_HUMAN             Reviewed;         374 AA.
Q7L2H7; A8K7X4; B4E2Q4; O60735; Q2F836; Q53HL6; Q9BXW1;
23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
05-JUL-2005, sequence version 1.
10-OCT-2018, entry version 133.
RecName: Full=Eukaryotic translation initiation factor 3 subunit M {ECO:0000255|HAMAP-Rule:MF_03012};
Short=eIF3m {ECO:0000255|HAMAP-Rule:MF_03012};
AltName: Full=Fetal lung protein B5;
Short=hFL-B5;
AltName: Full=PCI domain-containing protein 1;
Name=EIF3M {ECO:0000255|HAMAP-Rule:MF_03012}; Synonyms=HFLB5, PCID1;
ORFNames=GA17, PNAS-125;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION (MICROBIAL
INFECTION), AND TISSUE SPECIFICITY.
TISSUE=Fetal lung;
PubMed=15919898; DOI=10.1128/JVI.79.12.7419-7430.2005;
Perez A., Li Q.-X., Perez-Romero P., DeLassus G., Lopez S.R.,
Sutter S., McLaren N., Fuller A.O.;
"A new class of receptor for herpes simplex virus has heptad repeat
motifs that are common to membrane fusion proteins.";
J. Virol. 79:7419-7430(2005).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
ARG-346.
TISSUE=Dendritic cell;
Zhao Z., Huang X., Li N., Zhu X., Cao X.;
"A novel gene from human dendritic cell.";
Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Synovium, Thalamus, and Trachea;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Coronary arterial endothelium;
Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
Tanaka A., Yokoyama S.;
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16554811; DOI=10.1038/nature04632;
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
Sakaki Y.;
"Human chromosome 11 DNA sequence and analysis including novel gene
identification.";
Nature 440:497-500(2006).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Muscle, and Uterus;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
PROTEIN SEQUENCE OF 2-19; 103-115; 184-201; 261-276 AND 279-290,
CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, AND
IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Hepatoma, and Lung carcinoma;
Bienvenut W.V., Boldt K., von Kriegsheim A.F., Kolch W., Vousden K.H.,
Lukashchuk N.;
Submitted (MAR-2008) to UniProtKB.
[10]
NUCLEOTIDE SEQUENCE [MRNA] OF 4-139 (ISOFORM 1), AND INDUCTION.
PubMed=17719568; DOI=10.1016/j.brainres.2007.07.042;
Kobayashi K., Xin Y., Ymer S.I., Werther G.A., Russo V.C.;
"Subtractive hybridisation screen identifies genes regulated by
glucose deprivation in human neuroblastoma cells.";
Brain Res. 1170:129-139(2007).
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 171-374 (ISOFORM 1/2).
Yu W.-Q., Sun B.-Z., Chai Y.-B., Zhu F., Liu X.-S., Li Z., Lu F.,
Yan W., Yang H., Zhao Z.-L.;
"Human acute promyelocytic leukemia cell line NB4's
apoptosis/differentiation related genes.";
Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
[12]
IDENTIFICATION IN THE EIF-3 COMPLEX, AND IDENTIFICATION BY MASS
SPECTROMETRY.
PubMed=15601822; DOI=10.1101/gad.1255704;
Unbehaun A., Borukhov S.I., Hellen C.U.T., Pestova T.V.;
"Release of initiation factors from 48S complexes during ribosomal
subunit joining and the link between establishment of codon-anticodon
base-pairing and hydrolysis of eIF2-bound GTP.";
Genes Dev. 18:3078-3093(2004).
[13]
IDENTIFICATION.
PubMed=15904532; DOI=10.1186/1741-7007-3-14;
Zhou C., Arslan F., Wee S., Krishnan S., Ivanov A.R., Oliva A.,
Leatherwood J., Wolf D.A.;
"PCI proteins eIF3e and eIF3m define distinct translation initiation
factor 3 complexes.";
BMC Biol. 3:14-14(2005).
[14]
MUTAGENESIS OF LEU-350; LEU-354; LEU-361 AND VAL-364.
PubMed=15919899; DOI=10.1128/JVI.79.12.7431-7437.2005;
Perez-Romero P., Fuller A.O.;
"The C-terminus of the B5 receptor for herpes simplex virus contains a
functional region important for infection.";
J. Virol. 79:7431-7437(2005).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=15592455; DOI=10.1038/nbt1046;
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
Zha X.-M., Polakiewicz R.D., Comb M.J.;
"Immunoaffinity profiling of tyrosine phosphorylation in cancer
cells.";
Nat. Biotechnol. 23:94-101(2005).
[16]
CHARACTERIZATION OF THE EIF-3 COMPLEX.
PubMed=15703437; DOI=10.1261/rna.7215305;
Kolupaeva V.G., Unbehaun A., Lomakin I.B., Hellen C.U.T.,
Pestova T.V.;
"Binding of eukaryotic initiation factor 3 to ribosomal 40S subunits
and its role in ribosomal dissociation and anti-association.";
RNA 11:470-486(2005).
[17]
IDENTIFICATION IN THE EIF-3 COMPLEX, AND IDENTIFICATION BY MASS
SPECTROMETRY.
PubMed=16766523; DOI=10.1074/jbc.M605418200;
LeFebvre A.K., Korneeva N.L., Trutschl M., Cvek U., Duzan R.D.,
Bradley C.A., Hershey J.W.B., Rhoads R.E.;
"Translation initiation factor eIF4G-1 binds to eIF3 through the eIF3e
subunit.";
J. Biol. Chem. 281:22917-22932(2006).
[18]
FUNCTION, AND IDENTIFICATION IN THE EIF-3 COMPLEX.
PubMed=17403899; DOI=10.1128/MCB.01724-06;
Luke-Glaser S., Roy M., Larsen B., Le Bihan T., Metalnikov P.,
Tyers M., Peter M., Pintard L.;
"CIF-1, a shared subunit of the COP9/signalosome and eukaryotic
initiation factor 3 complexes, regulates MEL-26 levels in the
Caenorhabditis elegans embryo.";
Mol. Cell. Biol. 27:4526-4540(2007).
[19]
IDENTIFICATION IN THE EIF-3 COMPLEX, CHARACTERIZATION OF THE EIF-3
COMPLEX, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, AND
MASS SPECTROMETRY.
PubMed=17322308; DOI=10.1074/mcp.M600399-MCP200;
Damoc E., Fraser C.S., Zhou M., Videler H., Mayeur G.L.,
Hershey J.W.B., Doudna J.A., Robinson C.V., Leary J.A.;
"Structural characterization of the human eukaryotic initiation factor
3 protein complex by mass spectrometry.";
Mol. Cell. Proteomics 6:1135-1146(2007).
[20]
IDENTIFICATION IN THE EIF-3 COMPLEX, CHARACTERIZATION OF THE EIF-3
COMPLEX, MASS SPECTROMETRY, AND INTERACTION WITH EIF3B; EIF3F AND
EIF3H.
PubMed=18599441; DOI=10.1073/pnas.0801313105;
Zhou M., Sandercock A.M., Fraser C.S., Ridlova G., Stephens E.,
Schenauer M.R., Yokoi-Fong T., Barsky D., Leary J.A., Hershey J.W.B.,
Doudna J.A., Robinson C.V.;
"Mass spectrometry reveals modularity and a complete subunit
interaction map of the eukaryotic translation factor eIF3.";
Proc. Natl. Acad. Sci. U.S.A. 105:18139-18144(2008).
[21]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[22]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-254, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[23]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[24]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE
SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE
SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[25]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[26]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2; SER-152 AND SER-367,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[27]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[28]
FUNCTION, AND IDENTIFICATION IN THE EIF-3 COMPLEX.
PubMed=25849773; DOI=10.1038/nature14267;
Lee A.S., Kranzusch P.J., Cate J.H.;
"eIF3 targets cell-proliferation messenger RNAs for translational
activation or repression.";
Nature 522:111-114(2015).
[29]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[30]
FUNCTION.
PubMed=27462815; DOI=10.1038/nature18954;
Lee A.S., Kranzusch P.J., Doudna J.A., Cate J.H.;
"eIF3d is an mRNA cap-binding protein that is required for specialized
translation initiation.";
Nature 536:96-99(2016).
[31]
VARIANT [LARGE SCALE ANALYSIS] GLY-80.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
-!- FUNCTION: Component of the eukaryotic translation initiation
factor 3 (eIF-3) complex, which is required for several steps in
the initiation of protein synthesis (PubMed:17403899,
PubMed:25849773, PubMed:27462815). The eIF-3 complex associates
with the 40S ribosome and facilitates the recruitment of eIF-1,
eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S pre-
initiation complex (43S PIC). The eIF-3 complex stimulates mRNA
recruitment to the 43S PIC and scanning of the mRNA for AUG
recognition. The eIF-3 complex is also required for disassembly
and recycling of post-termination ribosomal complexes and
subsequently prevents premature joining of the 40S and 60S
ribosomal subunits prior to initiation (PubMed:17403899). The eIF-
3 complex specifically targets and initiates translation of a
subset of mRNAs involved in cell proliferation, including cell
cycling, differentiation and apoptosis, and uses different modes
of RNA stem-loop binding to exert either translational activation
or repression (PubMed:25849773). {ECO:0000255|HAMAP-Rule:MF_03012,
ECO:0000269|PubMed:17403899, ECO:0000269|PubMed:25849773,
ECO:0000269|PubMed:27462815}.
-!- FUNCTION: (Microbial infection) May favor virus entry in case of
infection with herpes simplex virus 1 (HSV1) or herpes simplex
virus 2 (HSV2). {ECO:0000269|PubMed:15919898}.
-!- SUBUNIT: Component of the eukaryotic translation initiation factor
3 (eIF-3) complex, which is composed of 13 subunits: EIF3A, EIF3B,
EIF3C, EIF3D, EIF3E, EIF3F, EIF3G, EIF3H, EIF3I, EIF3J, EIF3K,
EIF3L and EIF3M. The eIF-3 complex appears to include 3 stable
modules: module A is composed of EIF3A, EIF3B, EIF3G and EIF3I;
module B is composed of EIF3F, EIF3H, and EIF3M; and module C is
composed of EIF3C, EIF3D, EIF3E, EIF3K and EIF3L. EIF3C of module
C binds EIF3B of module A and EIF3H of module B, thereby linking
the three modules. EIF3J is a labile subunit that binds to the
eIF-3 complex via EIF3B. The eIF-3 complex interacts with RPS6KB1
under conditions of nutrient depletion. Mitogenic stimulation
leads to binding and activation of a complex composed of MTOR and
RPTOR, leading to phosphorylation and release of RPS6KB1 and
binding of EIF4B to eIF-3. {ECO:0000255|HAMAP-Rule:MF_03012,
ECO:0000269|PubMed:15601822, ECO:0000269|PubMed:16766523,
ECO:0000269|PubMed:17322308, ECO:0000269|PubMed:17403899,
ECO:0000269|PubMed:18599441}.
-!- INTERACTION:
P55884:EIF3B; NbExp=4; IntAct=EBI-353901, EBI-366696;
O00303:EIF3F; NbExp=14; IntAct=EBI-353901, EBI-711990;
O15372:EIF3H; NbExp=5; IntAct=EBI-353901, EBI-709735;
Q9Q2G4:ORF (xeno); NbExp=2; IntAct=EBI-353901, EBI-6248094;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03012}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q7L2H7-1; Sequence=Displayed;
Name=2;
IsoId=Q7L2H7-2; Sequence=VSP_056911;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Broadly expressed.
{ECO:0000269|PubMed:15919898}.
-!- INDUCTION: By glucose deprivation in neuroblastoma cells.
{ECO:0000269|PubMed:17719568}.
-!- MASS SPECTROMETRY: Mass=42413.8; Method=Unknown; Range=1-374;
Evidence={ECO:0000269|PubMed:17322308};
-!- MASS SPECTROMETRY: Mass=42414.7; Mass_error=0.2; Method=MALDI;
Range=1-374; Evidence={ECO:0000269|PubMed:18599441};
-!- SIMILARITY: Belongs to the eIF-3 subunit M family.
{ECO:0000255|HAMAP-Rule:MF_03012}.
-!- SEQUENCE CAUTION:
Sequence=AAK07542.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAK07542.1; Type=Frameshift; Positions=371; Evidence={ECO:0000305};
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EMBL; AY769947; AAX12524.1; -; mRNA.
EMBL; AF064603; AAC17108.1; -; mRNA.
EMBL; CR450300; CAG29296.1; -; mRNA.
EMBL; AK292139; BAF84828.1; -; mRNA.
EMBL; AK304378; BAG65216.1; -; mRNA.
EMBL; AK312512; BAG35413.1; -; mRNA.
EMBL; AK222564; BAD96284.1; -; mRNA.
EMBL; AL078477; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471064; EAW68217.1; -; Genomic_DNA.
EMBL; BC019103; AAH19103.1; -; mRNA.
EMBL; BC051292; AAH51292.1; -; mRNA.
EMBL; DQ185042; ABD14422.1; -; mRNA.
EMBL; AF277183; AAK07542.1; ALT_SEQ; mRNA.
CCDS; CCDS76392.1; -. [Q7L2H7-2]
CCDS; CCDS7880.1; -. [Q7L2H7-1]
RefSeq; NP_001294858.1; NM_001307929.1. [Q7L2H7-2]
RefSeq; NP_006351.2; NM_006360.5. [Q7L2H7-1]
UniGene; Hs.502244; -.
PDB; 3J8B; EM; -; M=1-335.
PDB; 3J8C; EM; -; M=1-335.
PDB; 6FEC; EM; 6.30 A; 8=1-374.
PDBsum; 3J8B; -.
PDBsum; 3J8C; -.
PDBsum; 6FEC; -.
ProteinModelPortal; Q7L2H7; -.
BioGrid; 115743; 51.
CORUM; Q7L2H7; -.
DIP; DIP-31256N; -.
IntAct; Q7L2H7; 33.
MINT; Q7L2H7; -.
STRING; 9606.ENSP00000436049; -.
iPTMnet; Q7L2H7; -.
PhosphoSitePlus; Q7L2H7; -.
SwissPalm; Q7L2H7; -.
BioMuta; EIF3M; -.
DMDM; 74754296; -.
EPD; Q7L2H7; -.
MaxQB; Q7L2H7; -.
PaxDb; Q7L2H7; -.
PeptideAtlas; Q7L2H7; -.
PRIDE; Q7L2H7; -.
ProteomicsDB; 68761; -.
DNASU; 10480; -.
Ensembl; ENST00000524896; ENSP00000436787; ENSG00000149100. [Q7L2H7-2]
Ensembl; ENST00000531120; ENSP00000436049; ENSG00000149100. [Q7L2H7-1]
GeneID; 10480; -.
KEGG; hsa:10480; -.
UCSC; uc001mtu.5; human. [Q7L2H7-1]
CTD; 10480; -.
DisGeNET; 10480; -.
EuPathDB; HostDB:ENSG00000149100.12; -.
GeneCards; EIF3M; -.
HGNC; HGNC:24460; EIF3M.
HPA; HPA031063; -.
MIM; 609641; gene.
neXtProt; NX_Q7L2H7; -.
OpenTargets; ENSG00000149100; -.
PharmGKB; PA162384944; -.
eggNOG; KOG2753; Eukaryota.
eggNOG; ENOG410XNP7; LUCA.
GeneTree; ENSGT00390000004456; -.
HOGENOM; HOG000112351; -.
HOVERGEN; HBG107844; -.
InParanoid; Q7L2H7; -.
KO; K15030; -.
OMA; VFTGVDQ; -.
OrthoDB; EOG091G0H3D; -.
PhylomeDB; Q7L2H7; -.
TreeFam; TF106148; -.
Reactome; R-HSA-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
Reactome; R-HSA-72649; Translation initiation complex formation.
Reactome; R-HSA-72689; Formation of a pool of free 40S subunits.
Reactome; R-HSA-72695; Formation of the ternary complex, and subsequently, the 43S complex.
Reactome; R-HSA-72702; Ribosomal scanning and start codon recognition.
Reactome; R-HSA-72706; GTP hydrolysis and joining of the 60S ribosomal subunit.
ChiTaRS; EIF3M; human.
GeneWiki; EIF3M; -.
GenomeRNAi; 10480; -.
PRO; PR:Q7L2H7; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000149100; Expressed in 237 organ(s), highest expression level in female gonad.
CleanEx; HS_EIF3M; -.
ExpressionAtlas; Q7L2H7; baseline and differential.
Genevisible; Q7L2H7; HS.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0016282; C:eukaryotic 43S preinitiation complex; IEA:UniProtKB-UniRule.
GO; GO:0033290; C:eukaryotic 48S preinitiation complex; IEA:UniProtKB-UniRule.
GO; GO:0005852; C:eukaryotic translation initiation factor 3 complex; IDA:UniProtKB.
GO; GO:0071541; C:eukaryotic translation initiation factor 3 complex, eIF3m; IEA:UniProtKB-UniRule.
GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-UniRule.
GO; GO:0031369; F:translation initiation factor binding; IEA:Ensembl.
GO; GO:0002183; P:cytoplasmic translational initiation; IBA:GO_Central.
GO; GO:0001732; P:formation of cytoplasmic translation initiation complex; IEA:UniProtKB-UniRule.
GO; GO:0006413; P:translational initiation; TAS:Reactome.
HAMAP; MF_03012; eIF3m; 1.
InterPro; IPR016024; ARM-type_fold.
InterPro; IPR027528; eIF3m.
InterPro; IPR000717; PCI_dom.
InterPro; IPR036390; WH_DNA-bd_sf.
Pfam; PF01399; PCI; 1.
SMART; SM00088; PINT; 1.
SUPFAM; SSF46785; SSF46785; 1.
SUPFAM; SSF48371; SSF48371; 1.
PROSITE; PS50250; PCI; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Complete proteome;
Cytoplasm; Direct protein sequencing; Initiation factor;
Phosphoprotein; Polymorphism; Protein biosynthesis;
Reference proteome.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:22814378,
ECO:0000255|HAMAP-Rule:MF_03012,
ECO:0000269|PubMed:17322308,
ECO:0000269|Ref.9}.
CHAIN 2 374 Eukaryotic translation initiation factor
3 subunit M.
/FTId=PRO_0000308195.
DOMAIN 180 339 PCI. {ECO:0000255|PROSITE-
ProRule:PRU01185}.
REGION 344 374 Interaction with HSV-1 and HSV-2.
MOD_RES 2 2 N-acetylserine.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:22814378,
ECO:0000255|HAMAP-Rule:MF_03012,
ECO:0000269|PubMed:17322308,
ECO:0000269|Ref.9}.
MOD_RES 2 2 Phosphoserine.
{ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 152 152 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 254 254 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 367 367 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VAR_SEQ 13 144 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_056911.
VARIANT 37 37 G -> R (in dbSNP:rs11557143).
/FTId=VAR_036752.
VARIANT 80 80 E -> G (in a breast cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_036753.
VARIANT 346 346 Q -> R (in dbSNP:rs1802363).
{ECO:0000269|Ref.2}.
/FTId=VAR_036754.
MUTAGEN 350 350 L->P: Reduces HSV binding and entry.
{ECO:0000269|PubMed:15919899}.
MUTAGEN 354 354 L->P: Reduces HSV binding and entry.
{ECO:0000269|PubMed:15919899}.
MUTAGEN 361 361 L->P: Reduces HSV binding and entry.
{ECO:0000269|PubMed:15919899}.
MUTAGEN 364 364 V->P: Reduces HSV binding and entry.
{ECO:0000269|PubMed:15919899}.
CONFLICT 64 64 M -> V (in Ref. 2; AAC17108).
{ECO:0000305}.
CONFLICT 121 121 Y -> C (in Ref. 10; ABD14422).
{ECO:0000305}.
CONFLICT 129 131 KVA -> EVV (in Ref. 2; AAC17108).
{ECO:0000305}.
CONFLICT 173 173 V -> A (in Ref. 2; AAC17108).
{ECO:0000305}.
CONFLICT 210 211 RA -> EP (in Ref. 2; AAC17108).
{ECO:0000305}.
CONFLICT 287 287 V -> I (in Ref. 2; AAC17108).
{ECO:0000305}.
CONFLICT 297 297 M -> V (in Ref. 5; BAD96284).
{ECO:0000305}.
HELIX 189 196 {ECO:0000244|PDB:3J8B}.
HELIX 201 203 {ECO:0000244|PDB:3J8B}.
HELIX 204 213 {ECO:0000244|PDB:3J8B}.
HELIX 221 224 {ECO:0000244|PDB:3J8B}.
HELIX 227 230 {ECO:0000244|PDB:3J8B}.
HELIX 235 245 {ECO:0000244|PDB:3J8B}.
HELIX 249 255 {ECO:0000244|PDB:3J8B}.
HELIX 256 258 {ECO:0000244|PDB:3J8B}.
HELIX 261 267 {ECO:0000244|PDB:3J8B}.
HELIX 269 288 {ECO:0000244|PDB:3J8B}.
STRAND 290 293 {ECO:0000244|PDB:3J8B}.
HELIX 294 301 {ECO:0000244|PDB:3J8B}.
HELIX 305 313 {ECO:0000244|PDB:3J8B}.
HELIX 315 320 {ECO:0000244|PDB:3J8B}.
STRAND 324 326 {ECO:0000244|PDB:3J8B}.
TURN 327 330 {ECO:0000244|PDB:3J8B}.
STRAND 331 333 {ECO:0000244|PDB:3J8B}.
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


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