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Translation initiation factor eIF-2B subunit epsilon (GCD complex subunit GCD6) (Guanine nucleotide exchange factor subunit GCD6) (eIF-2B GDP-GTP exchange factor subunit epsilon)

 EI2BE_YEAST             Reviewed;         712 AA.
P32501; D6VSJ5;
01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
01-OCT-1993, sequence version 1.
16-OCT-2019, entry version 186.
RecName: Full=Translation initiation factor eIF-2B subunit epsilon;
AltName: Full=GCD complex subunit GCD6;
AltName: Full=Guanine nucleotide exchange factor subunit GCD6;
AltName: Full=eIF-2B GDP-GTP exchange factor subunit epsilon;
Name=GCD6; Synonyms=TIF225; OrderedLocusNames=YDR211W;
ORFNames=YD8142.12, YD8142B.03;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=8441423; DOI=10.1128/mcb.13.3.1920;
Bushman J.L., Asuru A.I., Matts R.L., Hinnebusch A.G.;
"Evidence that GCD6 and GCD7, translational regulators of GCN4, are
subunits of the guanine nucleotide exchange factor for eIF-2 in
Saccharomyces cerevisiae.";
Mol. Cell. Biol. 13:1920-1932(1993).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169867;
Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N.,
Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M.,
Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L.,
Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M.,
Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S.,
Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M.,
Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S.,
Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K.,
Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D.,
Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C.,
Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T.,
Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E.,
Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W.,
Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K.,
Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S.,
Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A.,
Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S.,
Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M.,
Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y.,
Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M.,
Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E.,
Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R.,
Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
Mewes H.-W., Zollner A., Zaccaria P.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
Nature 387:75-78(1997).
[3]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[4]
IDENTIFICATION IN THE EIF2-B COMPLEX, AND FUNCTION OF THE EIF2-B
COMPLEX.
PubMed=8506384; DOI=10.1073/pnas.90.11.5350;
Cigan A.M., Bushman J.L., Boal T.R., Hinnebusch A.G.;
"A protein complex of translational regulators of GCN4 mRNA is the
guanine nucleotide-exchange factor for translation initiation factor 2
in yeast.";
Proc. Natl. Acad. Sci. U.S.A. 90:5350-5354(1993).
[5]
FUNCTION, AND IDENTIFICATION IN A EIF2-B SUBCOMPLEX.
PubMed=9472020; DOI=10.1101/gad.12.4.514;
Pavitt G.D., Ramaiah K.V., Kimball S.R., Hinnebusch A.G.;
"eIF2 independently binds two distinct eIF2B subcomplexes that
catalyze and regulate guanine-nucleotide exchange.";
Genes Dev. 12:514-526(1998).
[6]
INTERACTION WITH SUI3, AND MUTAGENESIS OF 655-THR--TRP-677 AND
696-TRP--GLU-706.
PubMed=10075937; DOI=10.1093/emboj/18.6.1673;
Asano K., Krishnamoorthy T., Phan L., Pavitt G.D., Hinnebusch A.G.;
"Conserved bipartite motifs in yeast eIF5 and eIF2Bepsilon, GTPase-
activating and GDP-GTP exchange factors in translation initiation,
mediate binding to their common substrate eIF2.";
EMBO J. 18:1673-1688(1999).
[7]
MUTAGENESIS OF THR-552 AND SER-576.
PubMed=10805739; DOI=10.1128/mcb.20.11.3965-3976.2000;
Gomez E., Pavitt G.D.;
"Identification of domains and residues within the epsilon subunit of
eukaryotic translation initiation factor 2B (eIF2Bepsilon) required
for guanine nucleotide exchange reveals a novel activation function
promoted by eIF2B complex formation.";
Mol. Cell. Biol. 20:3965-3976(2000).
[8]
IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=14690591; DOI=10.1016/s1097-2765(03)00476-3;
Hazbun T.R., Malmstroem L., Anderson S., Graczyk B.J., Fox B.,
Riffle M., Sundin B.A., Aranda J.D., McDonald W.H., Chiu C.-H.,
Snydsman B.E., Bradley P., Muller E.G.D., Fields S., Baker D.,
Yates J.R. III, Davis T.N.;
"Assigning function to yeast proteins by integration of
technologies.";
Mol. Cell 12:1353-1365(2003).
[9]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-478; SER-481 AND
SER-507, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
STRAIN=ADR376;
PubMed=17330950; DOI=10.1021/pr060559j;
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
Elias J.E., Gygi S.P.;
"Large-scale phosphorylation analysis of alpha-factor-arrested
Saccharomyces cerevisiae.";
J. Proteome Res. 6:1190-1197(2007).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-538, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth
phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-478; SER-481; SER-525;
SER-538 AND SER-707, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
PubMed=19779198; DOI=10.1126/science.1172867;
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
"Global analysis of Cdk1 substrate phosphorylation sites provides
insights into evolution.";
Science 325:1682-1686(2009).
[13]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 524-712, AND MUTAGENESIS OF
GLU-569.
PubMed=14681227; DOI=10.1074/jbc.m311055200;
Boesen T., Mohammad S.S., Pavitt G.D., Andersen G.R.;
"Structure of the catalytic fragment of translation initiation factor
2B and identification of a critically important catalytic residue.";
J. Biol. Chem. 279:10584-10592(2004).
-!- FUNCTION: Acts as a catalytic component of the translation
initiation factor 2B (eIF2-B or GCD complex), which catalyzes the
exchange of eukaryotic initiation factor 2 (eIF-2)-bound GDP for
GTP and is regulated by phosphorylated eIF-2. It activates the
synthesis of GCN4 in yeast under amino acid starvation conditions
by suppressing the inhibitory effects of multiple AUG codons
present in the leader of GCN4 mRNA. It may promote either
repression or activation of GCN4 expression depending on amino
acid availability. GCD6 and GCD7 repress GCN4 expression at the
translational level by ensuring that ribosomes which have
translated UORF1 will reinitiate at UORF2, -3, or -4 and thus fail
to reach the GCN4 start site. {ECO:0000269|PubMed:8506384,
ECO:0000269|PubMed:9472020}.
-!- SUBUNIT: Translation initiation factor 2B (eIF2-B) is composed of
five different subunits; alpha (GCN3), beta (GCD7), gamma (GCD1),
delta (GCD2) and epsilon (GCD6). A catalytic subcomplex comprising
GCD1 and GCD6 interacts with both, phosphorylated and non-
phosphorylated eIF-2 and has exchange activity in vitro. GCD6
interacts with SUI3. {ECO:0000269|PubMed:10075937,
ECO:0000269|PubMed:8506384, ECO:0000269|PubMed:9472020}.
-!- INTERACTION:
P09032:GCD1; NbExp=8; IntAct=EBI-6270, EBI-6275;
-!- MISCELLANEOUS: Present with 33800 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the eIF-2B gamma/epsilon subunits family.
{ECO:0000305}.
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EMBL; L07115; AAA65498.1; -; Genomic_DNA.
EMBL; Z68194; CAA92354.1; -; Genomic_DNA.
EMBL; Z68195; CAA92362.1; -; Genomic_DNA.
EMBL; BK006938; DAA12055.1; -; Genomic_DNA.
PIR; A48156; A48156.
RefSeq; NP_010497.3; NM_001180519.3.
PDB; 1PAQ; X-ray; 2.30 A; A=524-712.
PDB; 6I3M; EM; 3.93 A; G/H=1-712.
PDB; 6I7T; EM; 4.61 A; G/H=1-712.
PDB; 6QG0; EM; 4.20 A; I/J=1-712.
PDB; 6QG1; EM; 4.20 A; I/J=1-712.
PDB; 6QG2; EM; 4.60 A; I/J=1-712.
PDB; 6QG3; EM; 9.40 A; I/J=1-712.
PDB; 6QG5; EM; 10.10 A; I/J=1-712.
PDB; 6QG6; EM; 4.65 A; I/J=1-712.
PDBsum; 1PAQ; -.
PDBsum; 6I3M; -.
PDBsum; 6I7T; -.
PDBsum; 6QG0; -.
PDBsum; 6QG1; -.
PDBsum; 6QG2; -.
PDBsum; 6QG3; -.
PDBsum; 6QG5; -.
PDBsum; 6QG6; -.
SMR; P32501; -.
BioGrid; 32265; 96.
ComplexPortal; CPX-429; Eukaryotic translation initiation factor 2B complex.
DIP; DIP-2328N; -.
IntAct; P32501; 31.
MINT; P32501; -.
STRING; 4932.YDR211W; -.
iPTMnet; P32501; -.
MaxQB; P32501; -.
PaxDb; P32501; -.
PRIDE; P32501; -.
EnsemblFungi; YDR211W_mRNA; YDR211W; YDR211W.
GeneID; 851797; -.
KEGG; sce:YDR211W; -.
EuPathDB; FungiDB:YDR211W; -.
SGD; S000002619; GCD6.
HOGENOM; HOG000216610; -.
InParanoid; P32501; -.
KO; K03240; -.
OMA; NVAMIDY; -.
BioCyc; YEAST:G3O-29793-MONOMER; -.
BRENDA; 3.6.5.3; 984.
Reactome; R-SCE-72731; Recycling of eIF2:GDP.
EvolutionaryTrace; P32501; -.
PRO; PR:P32501; -.
Proteomes; UP000002311; Chromosome IV.
GO; GO:0005737; C:cytoplasm; HDA:SGD.
GO; GO:0005829; C:cytosol; HDA:SGD.
GO; GO:0005851; C:eukaryotic translation initiation factor 2B complex; IDA:SGD.
GO; GO:0032045; C:guanyl-nucleotide exchange factor complex; IDA:SGD.
GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IDA:SGD.
GO; GO:0016779; F:nucleotidyltransferase activity; IEA:InterPro.
GO; GO:0003743; F:translation initiation factor activity; IGI:SGD.
GO; GO:0031369; F:translation initiation factor binding; IBA:GO_Central.
GO; GO:0006446; P:regulation of translational initiation; IDA:SGD.
CDD; cd04197; eIF-2B_epsilon_N; 1.
Gene3D; 1.25.40.180; -; 1.
Gene3D; 3.90.550.10; -; 1.
InterPro; IPR016024; ARM-type_fold.
InterPro; IPR035543; eIF-2B_epsilon_N.
InterPro; IPR001451; Hexapep.
InterPro; IPR016021; MIF4-like_sf.
InterPro; IPR005835; NTP_transferase_dom.
InterPro; IPR029044; Nucleotide-diphossugar_trans.
InterPro; IPR011004; Trimer_LpxA-like_sf.
InterPro; IPR003307; W2_domain.
Pfam; PF00132; Hexapep; 2.
Pfam; PF00483; NTP_transferase; 1.
Pfam; PF02020; W2; 1.
SMART; SM00515; eIF5C; 1.
SUPFAM; SSF48371; SSF48371; 1.
SUPFAM; SSF51161; SSF51161; 1.
SUPFAM; SSF53448; SSF53448; 1.
PROSITE; PS51363; W2; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Initiation factor; Phosphoprotein;
Protein biosynthesis; Reference proteome; Translation regulation.
CHAIN 1 712 Translation initiation factor eIF-2B
subunit epsilon.
/FTId=PRO_0000156078.
DOMAIN 539 710 W2. {ECO:0000255|PROSITE-
ProRule:PRU00695}.
MOD_RES 478 478 Phosphoserine.
{ECO:0000244|PubMed:17330950,
ECO:0000244|PubMed:19779198}.
MOD_RES 481 481 Phosphoserine.
{ECO:0000244|PubMed:17330950,
ECO:0000244|PubMed:19779198}.
MOD_RES 507 507 Phosphoserine.
{ECO:0000244|PubMed:17330950}.
MOD_RES 525 525 Phosphoserine.
{ECO:0000244|PubMed:19779198}.
MOD_RES 538 538 Phosphoserine.
{ECO:0000244|PubMed:18407956,
ECO:0000244|PubMed:19779198}.
MOD_RES 707 707 Phosphoserine.
{ECO:0000244|PubMed:19779198}.
MUTAGEN 552 552 T->I: Reduced exchange activity.
{ECO:0000269|PubMed:10805739}.
MUTAGEN 569 569 E->A: Lethal.
{ECO:0000269|PubMed:14681227}.
MUTAGEN 576 576 S->N: Reduced exchange activity.
{ECO:0000269|PubMed:10805739}.
MUTAGEN 655 677 LFSALVSLYDNDIIEEDVIYKWW->AFSAAVSAADNDAAEA
AVAAKWA: Abolishes binding to SUI3.
{ECO:0000269|PubMed:10075937}.
MUTAGEN 696 706 WVEWLQNADEE->AAEAAQNAAAA: Abolishes
binding to SUI3; probably impairs the
conversion of eIF-2-GDP to eIF-2-GTP.
{ECO:0000269|PubMed:10075937}.
HELIX 545 558 {ECO:0000244|PDB:1PAQ}.
HELIX 563 576 {ECO:0000244|PDB:1PAQ}.
HELIX 581 601 {ECO:0000244|PDB:1PAQ}.
HELIX 607 618 {ECO:0000244|PDB:1PAQ}.
HELIX 619 624 {ECO:0000244|PDB:1PAQ}.
HELIX 629 646 {ECO:0000244|PDB:1PAQ}.
HELIX 651 664 {ECO:0000244|PDB:1PAQ}.
HELIX 670 678 {ECO:0000244|PDB:1PAQ}.
HELIX 684 686 {ECO:0000244|PDB:1PAQ}.
HELIX 687 702 {ECO:0000244|PDB:1PAQ}.
SEQUENCE 712 AA; 81161 MW; EFE87F6AE2941619 CRC64;
MAGKKGQKKS GLGNHGKNSD MDVEDRLQAV VLTDSYETRF MPLTAVKPRC LLPLANVPLI
EYTLEFLAKA GVHEVFLICS SHANQINDYI ENSKWNLPWS PFKITTIMSP EARCTGDVMR
DLDNRGIITG DFILVSGDVL TNIDFSKMLE FHKKMHLQDK DHISTMCLSK ASTYPKTRTI
EPAAFVLDKS TSRCIYYQDL PLPSSREKTS IQIDPELLDN VDEFVIRNDL IDCRIDICTS
HVPLIFQENF DYQSLRTDFV KGVISSDILG KHIYAYLTDE YAVRVESWQT YDTISQDFLG
RWCYPLVLDS NIQDDQTYSY ESRHIYKEKD VVLAQSCKIG KCTAIGSGTK IGEGTKIENS
VIGRNCQIGE NIRIKNSFIW DDCIIGNNSI IDHSLIASNA TLGSNVRLND GCIIGFNVKI
DDNMDLDRNT KISASPLKNA GSRMYDNESN EQFDQDLDDQ TLAVSIVGDK GVGYIYESEV
SDDEDSSTEA CKEINTLSNQ LDELYLSDDS ISSATKKTKK RRTMSVNSIY TDREEIDSEF
EDEDFEKEGI ATVERAMENN HDLDTALLEL NTLRMSMNVT YHEVRIATIT ALLRRVYHFI
ATQTLGPKDA VVKVFNQWGL LFKRQAFDEE EYIDLMNIIM EKIVEQSFDK PDLILFSALV
SLYDNDIIEE DVIYKWWDNV STDPRYDEVK KLTVKWVEWL QNADEESSSE EE


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WP1644: DNA replication
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WP1680: Oxidative phosphorylation
WP1566: Citrate cycle (TCA cycle)
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WP1614: 1- and 2-Methylnaphthalene degradation
WP1634: Butanoate metabolism
WP1663: Homologous recombination
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WP193: Signaling of Hepatocyte Growth Factor Receptor
WP32: Translation Factors
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WP810: Signaling of Hepatocyte Growth Factor Receptor
WP1162: Signaling of Hepatocyte Growth Factor Receptor
WP444: Signaling of Hepatocyte Growth Factor Receptor
WP1206: Signaling of Hepatocyte Growth Factor Receptor

Related Genes :
[GCD6 TIF225 YDR211W YD8142.12 YD8142B.03] Translation initiation factor eIF-2B subunit epsilon (GCD complex subunit GCD6) (Guanine nucleotide exchange factor subunit GCD6) (eIF-2B GDP-GTP exchange factor subunit epsilon)
[GCN3 AAS2 TIF221 YKR026C] Translation initiation factor eIF-2B subunit alpha (GCD complex subunit GCN3) (Guanine nucleotide exchange factor subunit GCN3) (Transcriptional activator GCN3) (eIF-2B GDP-GTP exchange factor subunit alpha)
[GCD2 TIF224 YGR083C] Translation initiation factor eIF-2B subunit delta (GCD complex subunit GCD2) (Guanine nucleotide exchange factor subunit GCD2) (eIF-2B GDP-GTP exchange factor subunit delta)
[GCD1 TIF223 TRA3 YOR260W] Translation initiation factor eIF-2B subunit gamma (GCD complex subunit GCD1) (Guanine nucleotide exchange factor subunit GCD1) (eIF-2B GDP-GTP exchange factor subunit gamma)
[GCD7 TIF222 YLR291C L8003.17] Translation initiation factor eIF-2B subunit beta (GCD complex subunit GCD7) (Guanine nucleotide exchange factor subunit GCD7) (eIF-2B GDP-GTP exchange factor subunit beta)
[EIF2B5 EIF2BE] Translation initiation factor eIF-2B subunit epsilon (eIF-2B GDP-GTP exchange factor subunit epsilon)
[EIF2B3] Translation initiation factor eIF-2B subunit gamma (eIF-2B GDP-GTP exchange factor subunit gamma)
[EIF2B2 EIF2BB] Translation initiation factor eIF-2B subunit beta (S20I15) (S20III15) (eIF-2B GDP-GTP exchange factor subunit beta)
[EIF2B4 EIF2BD] Translation initiation factor eIF-2B subunit delta (eIF-2B GDP-GTP exchange factor subunit delta)
[EIF2B1 EIF2BA] Translation initiation factor eIF-2B subunit alpha (eIF-2B GDP-GTP exchange factor subunit alpha)
[EIF3F EIF3S5] Eukaryotic translation initiation factor 3 subunit F (eIF3f) (Deubiquitinating enzyme eIF3f) (EC 3.4.19.12) (Eukaryotic translation initiation factor 3 subunit 5) (eIF-3-epsilon) (eIF3 p47)
[Eif3f Eif3s5] Eukaryotic translation initiation factor 3 subunit F (eIF3f) (Deubiquitinating enzyme eIF3f) (EC 3.4.19.12) (Eukaryotic translation initiation factor 3 subunit 5) (eIF-3-epsilon) (eIF3 p47)
[EIF3G EIF3S4] Eukaryotic translation initiation factor 3 subunit G (eIF3g) (Eukaryotic translation initiation factor 3 RNA-binding subunit) (eIF-3 RNA-binding subunit) (Eukaryotic translation initiation factor 3 subunit 4) (eIF-3-delta) (eIF3 p42) (eIF3 p44)
[EIF3L EIF3EIP EIF3S6IP HSPC021 HSPC025 MSTP005] Eukaryotic translation initiation factor 3 subunit L (eIF3l) (Eukaryotic translation initiation factor 3 subunit 6-interacting protein) (Eukaryotic translation initiation factor 3 subunit E-interacting protein)
[EIF3H EIF3S3] Eukaryotic translation initiation factor 3 subunit H (eIF3h) (Eukaryotic translation initiation factor 3 subunit 3) (eIF-3-gamma) (eIF3 p40 subunit)
[EIF3A EIF3S10 KIAA0139] Eukaryotic translation initiation factor 3 subunit A (eIF3a) (Eukaryotic translation initiation factor 3 subunit 10) (eIF-3-theta) (eIF3 p167) (eIF3 p180) (eIF3 p185)
[EIF3B EIF3S9] Eukaryotic translation initiation factor 3 subunit B (eIF3b) (Eukaryotic translation initiation factor 3 subunit 9) (Prt1 homolog) (hPrt1) (eIF-3-eta) (eIF3 p110) (eIF3 p116)
[EIF3J EIF3S1 PRO0391] Eukaryotic translation initiation factor 3 subunit J (eIF3j) (Eukaryotic translation initiation factor 3 subunit 1) (eIF-3-alpha) (eIF3 p35)
[Eif3a Csma Eif3 Eif3s10] Eukaryotic translation initiation factor 3 subunit A (eIF3a) (Centrosomin) (Eukaryotic translation initiation factor 3 subunit 10) (eIF-3-theta) (eIF3 p167) (eIF3 p180) (eIF3 p185) (p162)
[EIF3I EIF3S2 TRIP1] Eukaryotic translation initiation factor 3 subunit I (eIF3i) (Eukaryotic translation initiation factor 3 subunit 2) (TGF-beta receptor-interacting protein 1) (TRIP-1) (eIF-3-beta) (eIF3 p36)
[EIF3D EIF3S7] Eukaryotic translation initiation factor 3 subunit D (eIF3d) (Eukaryotic translation initiation factor 3 subunit 7) (eIF-3-zeta) (eIF3 p66)
[EIF3K EIF3S12 ARG134 HSPC029 MSTP001 PTD001] Eukaryotic translation initiation factor 3 subunit K (eIF3k) (Eukaryotic translation initiation factor 3 subunit 12) (Muscle-specific gene M9 protein) (PLAC-24) (eIF-3 p25) (eIF-3 p28)
[Grin2b] Glutamate receptor ionotropic, NMDA 2B (GluN2B) (Glutamate [NMDA] receptor subunit epsilon-2) (N-methyl D-aspartate receptor subtype 2B) (NMDAR2B) (NR2B)
[EIF3E EIF3S6 INT6] Eukaryotic translation initiation factor 3 subunit E (eIF3e) (Eukaryotic translation initiation factor 3 subunit 6) (Viral integration site protein INT-6 homolog) (eIF-3 p48)
[EIF3C EIF3S8] Eukaryotic translation initiation factor 3 subunit C (eIF3c) (Eukaryotic translation initiation factor 3 subunit 8) (eIF3 p110)
[sum1 eif3i tif34 SPAC4D7.05] Eukaryotic translation initiation factor 3 subunit I (eIF3i) (Eukaryotic translation initiation factor 3 39 kDa subunit homolog) (eIF-3 39 kDa subunit homolog) (eIF3 p39) (Suppressor of uncontrolled mitosis 1)
[Eif3b Eif3s9] Eukaryotic translation initiation factor 3 subunit B (eIF3b) (Eukaryotic translation initiation factor 3 subunit 9) (eIF-3-eta) (eIF3 p116)
[Eif3e Eif3s6 Int6] Eukaryotic translation initiation factor 3 subunit E (eIF3e) (Eukaryotic translation initiation factor 3 subunit 6) (MMTV integration site 6) (Mammary tumor-associated protein INT-6) (Viral integration site protein INT-6) (eIF-3 p48)
[Eif3a Eif3s10] Eukaryotic translation initiation factor 3 subunit A (eIF3a) (Eukaryotic translation initiation factor 3 subunit 10) (eIF-3-theta)
[Eif3l Eif3eip Eif3s6ip Paf67] Eukaryotic translation initiation factor 3 subunit L (eIF3l) (66 kDa tyrosine-rich heat shock protein) (67 kDa polymerase-associated factor) (Eukaryotic translation initiation factor 3 subunit 6-interacting protein) (Eukaryotic translation initiation factor 3 subunit E-interacting protein) (HSP-66Y) (PAF67)

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