EF1D_MOUSE
ID EF1D_MOUSE Reviewed; 281 AA.
AC P57776; Q68FG5; Q9CWW2; Q9CWY1; Q9CYD4; Q9CYJ5;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Elongation factor 1-delta;
DE Short=EF-1-delta;
GN Name=Eef1d;
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 [MRNA] (ISOFORM 1).
RC STRAIN=BALB/cJ;
RA Joseph P., Whong W.-Z., Ong T.-M.;
RT "Mus musculus eukaryotic translation elongation factor 1 delta mRNA.";
RL Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Embryo, and Embryonic stem cell;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [4]
RP PROTEIN SEQUENCE OF 2-10, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT
RP ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Liver;
RA Bienvenut W.V.;
RL Submitted (JUL-2005) to UniProtKB.
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-147 AND SER-162, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Teratocarcinoma;
RX PubMed=17622165; DOI=10.1021/pr070122r;
RA Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.;
RT "A differential phosphoproteomic analysis of retinoic acid-treated P19
RT cells.";
RL J. Proteome Res. 6:3174-3186(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-147 AND SER-162, AND
RP IDENTIFICATION BY 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-162, AND IDENTIFICATION BY
RP 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-162, 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-133 AND SER-162, AND
RP IDENTIFICATION BY 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-133; THR-147 AND SER-162, AND
RP IDENTIFICATION BY 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 [11]
RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-117, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
CC -!- FUNCTION: [Isoform 1]: EF-1-beta and EF-1-delta stimulate the exchange
CC of GDP bound to EF-1-alpha to GTP, regenerating EF-1-alpha for another
CC round of transfer of aminoacyl-tRNAs to the ribosome. {ECO:0000250}.
CC -!- FUNCTION: [Isoform 3]: Regulates induction of heat-shock-responsive
CC genes through association with heat shock transcription factors and
CC direct DNA-binding at heat shock promoter elements (HSE).
CC {ECO:0000250|UniProtKB:P29692}.
CC -!- SUBUNIT: EF-1 is composed of 4 subunits: alpha, beta, delta isoform 1,
CC and gamma. Isoform 3 interacts with HSF1 and NFE2L2.
CC {ECO:0000250|UniProtKB:P29692}.
CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Nucleus
CC {ECO:0000250|UniProtKB:P29692}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=P57776-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P57776-2; Sequence=VSP_001359;
CC Name=3; Synonyms=eEF1BdeltaL {ECO:0000250|UniProtKB:P29692};
CC IsoId=P57776-3; Sequence=VSP_037885;
CC -!- SIMILARITY: Belongs to the EF-1-beta/EF-1-delta family. {ECO:0000305}.
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DR EMBL; AF304351; AAG17466.1; -; mRNA.
DR EMBL; AK010308; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK010347; BAB26870.1; -; mRNA.
DR EMBL; AK017616; BAB30841.1; -; mRNA.
DR EMBL; AK017796; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC079855; AAH79855.1; -; mRNA.
DR CCDS; CCDS27553.1; -. [P57776-3]
DR CCDS; CCDS27554.1; -. [P57776-1]
DR CCDS; CCDS70638.1; -. [P57776-2]
DR RefSeq; NP_001272358.1; NM_001285429.1.
DR RefSeq; NP_001272359.1; NM_001285430.1.
DR RefSeq; NP_001272360.1; NM_001285431.1.
DR RefSeq; NP_001272361.1; NM_001285432.1.
DR RefSeq; NP_001272362.1; NM_001285433.1.
DR RefSeq; NP_001272363.1; NM_001285434.1.
DR RefSeq; NP_075729.2; NM_023240.3.
DR RefSeq; NP_083939.1; NM_029663.2.
DR AlphaFoldDB; P57776; -.
DR SMR; P57776; -.
DR BioGRID; 211625; 16.
DR IntAct; P57776; 3.
DR MINT; P57776; -.
DR STRING; 10090.ENSMUSP00000087110; -.
DR iPTMnet; P57776; -.
DR PhosphoSitePlus; P57776; -.
DR SwissPalm; P57776; -.
DR REPRODUCTION-2DPAGE; P57776; -.
DR EPD; P57776; -.
DR jPOST; P57776; -.
DR MaxQB; P57776; -.
DR PaxDb; P57776; -.
DR PeptideAtlas; P57776; -.
DR PRIDE; P57776; -.
DR ProteomicsDB; 277719; -. [P57776-1]
DR ProteomicsDB; 277720; -. [P57776-2]
DR ProteomicsDB; 277721; -. [P57776-3]
DR DNASU; 66656; -.
DR GeneID; 66656; -.
DR KEGG; mmu:66656; -.
DR UCSC; uc007whj.2; mouse. [P57776-3]
DR UCSC; uc007whm.2; mouse. [P57776-2]
DR CTD; 1936; -.
DR MGI; MGI:1913906; Eef1d.
DR eggNOG; KOG1668; Eukaryota.
DR InParanoid; P57776; -.
DR OrthoDB; 1464823at2759; -.
DR TreeFam; TF313134; -.
DR Reactome; R-MMU-156842; Eukaryotic Translation Elongation.
DR BioGRID-ORCS; 66656; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Eef1d; mouse.
DR PRO; PR:P57776; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P57776; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0005853; C:eukaryotic translation elongation factor 1 complex; IEA:InterPro.
DR GO; GO:0001650; C:fibrillar center; ISO:MGI.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0045202; C:synapse; IDA:SynGO.
DR GO; GO:0003677; F:DNA binding; ISO:MGI.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; ISO:MGI.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IBA:GO_Central.
DR GO; GO:0031072; F:heat shock protein binding; ISO:MGI.
DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
DR GO; GO:0071479; P:cellular response to ionizing radiation; ISO:MGI.
DR GO; GO:0009299; P:mRNA transcription; ISO:MGI.
DR GO; GO:0010941; P:regulation of cell death; ISO:MGI.
DR GO; GO:0006414; P:translational elongation; IBA:GO_Central.
DR CDD; cd00292; EF1B; 1.
DR Gene3D; 3.30.70.60; -; 1.
DR InterPro; IPR036219; eEF-1beta-like_sf.
DR InterPro; IPR018940; EF-1_beta_acid_region_euk.
DR InterPro; IPR014038; EF1B_bsu/dsu_GNE.
DR InterPro; IPR014717; Transl_elong_EF1B/ribosomal_S6.
DR InterPro; IPR001326; Transl_elong_EF1B_B/D_CS.
DR Pfam; PF10587; EF-1_beta_acid; 1.
DR Pfam; PF00736; EF1_GNE; 1.
DR SMART; SM01182; EF-1_beta_acid; 1.
DR SMART; SM00888; EF1_GNE; 1.
DR SUPFAM; SSF54984; SSF54984; 1.
DR PROSITE; PS00824; EF1BD_1; 1.
DR PROSITE; PS00825; EF1BD_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Direct protein sequencing; DNA-binding;
KW Elongation factor; Nucleus; Phosphoprotein; Protein biosynthesis;
KW Reference proteome; Transcription; Transcription regulation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.4"
FT CHAIN 2..281
FT /note="Elongation factor 1-delta"
FT /id="PRO_0000155047"
FT REGION 80..115
FT /note="Leucine-zipper"
FT /evidence="ECO:0000250"
FT REGION 113..172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 173..281
FT /note="Catalytic (GEF)"
FT /evidence="ECO:0000250"
FT COMPBIAS 113..136
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|Ref.4"
FT MOD_RES 17
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P29692"
FT MOD_RES 37
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P29692"
FT MOD_RES 44
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P29692"
FT MOD_RES 60
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P29692"
FT MOD_RES 86
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P29692"
FT MOD_RES 106
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q68FR9"
FT MOD_RES 107
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P29692"
FT MOD_RES 117
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P29692"
FT MOD_RES 117
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 119
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P29692"
FT MOD_RES 129
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P29692"
FT MOD_RES 133
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19131326,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 147
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:17622165, ECO:0007744|PubMed:21183079"
FT MOD_RES 162
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:17622165, ECO:0007744|PubMed:18630941,
FT ECO:0007744|PubMed:19131326, ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1
FT /note="M -> MRSGKASCALETVWEDRHKYEGAERRFHEQEATQVVAAAATAAATAS
FT ASVQQLLDEVPAVNGPSQEDTEDTEEAEAPNTSSRSDPGKSHECKKPIQKKRKRSPKSW
FT LGQADLALVGLSADHVWLDKPLFDQAESSYRQRLADVAAQAAQPPALAPRGPCTHGSHV
FT ACHHVTWGIWVNKSCFDQAERAFVEWSQSLLLAAEGSHRQGTPDTGQQAVTPDLALACQ
FT PCPPANGQPPLGSLQALVREVWLEKPRYDAAERGFYEALFDGHPPGKVRLQERASQAEG
FT TRRGRRDHRSCNNVGNKRAGSKRANGEAPPAFPYWYFLHKDAEAPWLSKPTYDSAECRH
FT HAVEALRIAWRLEAASLAHRPTPRSGPSMSSLRPNRKM (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_037885"
FT VAR_SEQ 40..63
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_001359"
FT CONFLICT 279
FT /note="D -> N (in Ref. 2; BAB26870/BAB30841 and 3;
FT AAH79855)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 281 AA; 31293 MW; FD55F872FDA06819 CRC64;
MATNFLAHEK IWFDKFKYDD AERRFYEQMN GPVTSGSRQE NGASVILRDI ARARENIQKS
LAGSSGPGAS SGPGGDHSEL IVRITSLEVE NQNLRGVVQD LQQAISKLEA RLSSLEKSSP
TPRATAPQTQ HVSPMRQVEP PTKKGATPAE DDEDKDIDLF GSDEEEEDKE AARLREERLR
QYAEKKAKKP TLVAKSSILL DVKPWDDETD MAQLETCVRS IQLDGLVWGA SKLVPVGYGI
RKLQIQCVVE DDKVGTDLLE EEITKFEEHV QSVDIAAFDK I
