EI2BE_MOUSE
ID EI2BE_MOUSE Reviewed; 717 AA.
AC Q8CHW4; Q3TU39;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Translation initiation factor eIF-2B subunit epsilon;
DE AltName: Full=eIF-2B GDP-GTP exchange factor subunit epsilon;
GN Name=Eif2b5;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Head;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Liver, and Mammary tumor;
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-540, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18630941; DOI=10.1021/pr800223m;
RA Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT "Specific phosphopeptide enrichment with immobilized titanium ion affinity
RT chromatography adsorbent for phosphoproteome analysis.";
RL J. Proteome Res. 7:3957-3967(2008).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-540, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-540, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-540, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [8]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-18, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Embryo;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: Catalyzes the exchange of eukaryotic initiation factor 2-
CC bound GDP for GTP. {ECO:0000250}.
CC -!- SUBUNIT: Complex of five different subunits; alpha, beta, gamma, delta
CC and epsilon. Interacts with RGS2 (By similarity). {ECO:0000250}.
CC -!- PTM: Phosphorylated at Ser-540 by DYRK2; this is required for
CC subsequent phosphorylation by GSK3B. Phosphorylated on serine and
CC threonine residues by GSK3B; phosphorylation inhibits its function (By
CC similarity). {ECO:0000250}.
CC -!- PTM: Polyubiquitinated, probably by NEDD4. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the eIF-2B gamma/epsilon subunits family.
CC {ECO:0000305}.
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DR EMBL; AK160985; BAE36132.1; -; mRNA.
DR EMBL; BC038620; AAH38620.1; -; mRNA.
DR EMBL; BC085255; AAH85255.1; -; mRNA.
DR CCDS; CCDS28047.1; -.
DR RefSeq; NP_758469.1; NM_172265.2.
DR AlphaFoldDB; Q8CHW4; -.
DR SMR; Q8CHW4; -.
DR BioGRID; 230231; 12.
DR STRING; 10090.ENSMUSP00000003320; -.
DR iPTMnet; Q8CHW4; -.
DR PhosphoSitePlus; Q8CHW4; -.
DR SwissPalm; Q8CHW4; -.
DR EPD; Q8CHW4; -.
DR jPOST; Q8CHW4; -.
DR MaxQB; Q8CHW4; -.
DR PaxDb; Q8CHW4; -.
DR PeptideAtlas; Q8CHW4; -.
DR PRIDE; Q8CHW4; -.
DR ProteomicsDB; 277578; -.
DR Antibodypedia; 4211; 170 antibodies from 27 providers.
DR DNASU; 224045; -.
DR Ensembl; ENSMUST00000003320; ENSMUSP00000003320; ENSMUSG00000003235.
DR GeneID; 224045; -.
DR KEGG; mmu:224045; -.
DR UCSC; uc007ypu.2; mouse.
DR CTD; 8893; -.
DR MGI; MGI:2446176; Eif2b5.
DR VEuPathDB; HostDB:ENSMUSG00000003235; -.
DR eggNOG; KOG1461; Eukaryota.
DR GeneTree; ENSGT00510000047568; -.
DR HOGENOM; CLU_012507_2_0_1; -.
DR InParanoid; Q8CHW4; -.
DR OMA; HYLYDKD; -.
DR OrthoDB; 369837at2759; -.
DR PhylomeDB; Q8CHW4; -.
DR TreeFam; TF101509; -.
DR Reactome; R-MMU-72731; Recycling of eIF2:GDP.
DR BioGRID-ORCS; 224045; 27 hits in 75 CRISPR screens.
DR ChiTaRS; Eif2b5; mouse.
DR PRO; PR:Q8CHW4; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q8CHW4; protein.
DR Bgee; ENSMUSG00000003235; Expressed in spermatocyte and 267 other tissues.
DR ExpressionAtlas; Q8CHW4; baseline and differential.
DR Genevisible; Q8CHW4; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005851; C:eukaryotic translation initiation factor 2B complex; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; ISO:MGI.
DR GO; GO:0003743; F:translation initiation factor activity; ISO:MGI.
DR GO; GO:0031369; F:translation initiation factor binding; ISO:MGI.
DR GO; GO:0007568; P:aging; ISO:MGI.
DR GO; GO:0014002; P:astrocyte development; ISS:UniProtKB.
DR GO; GO:0048708; P:astrocyte differentiation; ISS:UniProtKB.
DR GO; GO:0021766; P:hippocampus development; IEA:Ensembl.
DR GO; GO:0042552; P:myelination; ISS:UniProtKB.
DR GO; GO:0014003; P:oligodendrocyte development; ISS:UniProtKB.
DR GO; GO:0001541; P:ovarian follicle development; ISS:UniProtKB.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISO:MGI.
DR GO; GO:0045727; P:positive regulation of translation; ISO:MGI.
DR GO; GO:0045948; P:positive regulation of translational initiation; ISS:UniProtKB.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; ISS:UniProtKB.
DR GO; GO:0009749; P:response to glucose; ISS:UniProtKB.
DR GO; GO:0009408; P:response to heat; ISS:UniProtKB.
DR GO; GO:0010226; P:response to lithium ion; IEA:Ensembl.
DR GO; GO:0043434; P:response to peptide hormone; ISS:UniProtKB.
DR GO; GO:0050852; P:T cell receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0006413; P:translational initiation; ISS:UniProtKB.
DR CDD; cd04197; eIF-2B_epsilon_N; 1.
DR CDD; cd11558; W2_eIF2B_epsilon; 1.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR035543; eIF-2B_epsilon_N.
DR InterPro; IPR001451; Hexapep.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR InterPro; IPR011004; Trimer_LpxA-like_sf.
DR InterPro; IPR003307; W2_domain.
DR InterPro; IPR044123; W2_eIF2B_epsilon.
DR Pfam; PF00132; Hexapep; 1.
DR Pfam; PF02020; W2; 1.
DR SMART; SM00515; eIF5C; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR SUPFAM; SSF51161; SSF51161; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
DR PROSITE; PS51363; W2; 1.
PE 1: Evidence at protein level;
KW Initiation factor; Isopeptide bond; Methylation; Phosphoprotein;
KW Protein biosynthesis; Reference proteome; Ubl conjugation.
FT CHAIN 1..717
FT /note="Translation initiation factor eIF-2B subunit
FT epsilon"
FT /id="PRO_0000239429"
FT DOMAIN 539..716
FT /note="W2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00695"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 442..479
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 517..538
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 464..478
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 18
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 23
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q64350"
FT MOD_RES 126
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q64350"
FT MOD_RES 318
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q64350"
FT MOD_RES 446
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13144"
FT MOD_RES 462
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13144"
FT MOD_RES 465
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13144"
FT MOD_RES 528
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q64350"
FT MOD_RES 536
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q64350"
FT MOD_RES 540
FT /note="Phosphoserine; by DYRK2"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19131326, ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 713
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13144"
FT CROSSLNK 57
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q64350"
FT CROSSLNK 99
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q64350"
FT CROSSLNK 137
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q64350"
FT CROSSLNK 213
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q64350"
FT CROSSLNK 501
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q64350"
FT CONFLICT 54
FT /note="P -> H (in Ref. 1; BAE36132)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 717 AA; 80086 MW; 61455A437B7D513B CRC64;
MAATAAVPGA AAGRASKRGG GGSGGGGTQG AEEEPPPPLQ AVLVADSFNR RFFPISKDQP
RVLLPLANVA LIDYTLEFLT ATGVQETFVF CCWKAAQIKE HLQKSKWCHP TSPNVVRIIT
SELYRSLGDV LRDVDAKALV RSDFLLIYGD VISNINICRA LEEHRLRRKL EKNVSVMTMV
FKESSPSHPT RCHEDNVVMA VDSATNRVLH FQKTQGLRRF SFPLSLFQGS GDGVEIRYDL
LDCHISICSP QVAQLFTDNF DYQTRDDFVR GILMNEEVLG NQIHLHVTTR EYGARVSNLH
MYSAVCADVI RRWVYPLTPE VNFTDSTTQS YTHSRHNIYR GPEVSLGHGS VLEENVLLGA
GTVIGSNCSI TNSVIGPNCH IGDNVVLDQA YLWQGVRVAA GAQIHQSLLC DRAEVKERVK
LKPYCVLTSQ VVVGPDITLP EGSVISLHPP DAEEDEDDGQ FSDDSGADQE KEKVKLKGYN
PAEVGLEGQG YLWKAEGVNS KEDEELRQSL WGLMIKTEEE SETESEGSVD PEELDSRAGS
PQLDDIRVFQ NEVLGTLQRG REENISCENL VLEINSLKHA YNISLKEVMQ VLTLVVLEFP
LQQVDGLLDP NRYCALLLPL LKAWSPVLRN YIKRAADHLE ALAAIEDFFL EHETLVTSMA
KVLMAFYQLE ILAEETILSW FSQRDTTDEG QQLRKNQQLQ RFIQWLREAE EESSEDD
