ID EF1A2_MOUSE Reviewed; 463 AA.
AC P62631; P27706;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 169.
DE RecName: Full=Elongation factor 1-alpha 2;
DE Short=EF-1-alpha-2;
DE AltName: Full=Eukaryotic elongation factor 1 A-2;
DE Short=eEF1A-2;
DE AltName: Full=Statin-S1;
GN Name=Eef1a2; Synonyms=Eef1al, Stn;
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].
RC TISSUE=Brain;
RX PubMed=7945283; DOI=10.1006/bbrc.1994.2336;
RA Lee S., Ann D.K., Wang E.;
RT "Cloning of human and mouse brain cDNAs coding for S1, the second member of
RT the mammalian elongation factor-1 alpha gene family: analysis of a possible
RT evolutionary pathway.";
RL Biochem. Biophys. Res. Commun. 203:1371-1377(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
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 PROTEIN SEQUENCE OF 6-30; 85-96; 135-146; 155-165; 248-266 AND 431-439, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J, and OF1; TISSUE=Brain, and Hippocampus;
RA Lubec G., Kang S.U., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, and Lung;
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).
CC -!- FUNCTION: This protein promotes the GTP-dependent binding of aminoacyl-
CC tRNA to the A-site of ribosomes during protein biosynthesis.
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- TISSUE SPECIFICITY: Found in a wide range of tissues.
CC -!- DEVELOPMENTAL STAGE: The statin expression is specific for
CC nonproliferating cells. Its message is most abundant in G0 phase of 3T3
CC mouse fibroblasts, but becomes significantly reduced in G1 and S1
CC phases cells.
CC -!- PTM: Trimethylated at Lys-165 by EEF1AKMT3. Mono-, di-, and
CC trimethylated at Lys-36 by EEF1AKMT4; trimethylated form is
CC predominant. Methylation by EEF1AKMT4 contributes to the fine-tuning of
CC translation rates for a subset of tRNAs. Trimethylated at the N-
CC terminus and dimethylated at Lys-55 by METTL13.
CC {ECO:0000250|UniProtKB:Q05639}.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A
CC subfamily. {ECO:0000305}.
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DR EMBL; L26479; AAA91870.1; -; mRNA.
DR EMBL; BC018235; AAH18235.1; -; mRNA.
DR CCDS; CCDS17201.1; -.
DR PIR; JC2445; JC2445.
DR RefSeq; NP_031932.1; NM_007906.2.
DR AlphaFoldDB; P62631; -.
DR SMR; P62631; -.
DR BioGRID; 199386; 31.
DR IntAct; P62631; 8.
DR STRING; 10090.ENSMUSP00000054556; -.
DR GlyGen; P62631; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P62631; -.
DR MetOSite; P62631; -.
DR PhosphoSitePlus; P62631; -.
DR SwissPalm; P62631; -.
DR EPD; P62631; -.
DR jPOST; P62631; -.
DR MaxQB; P62631; -.
DR PaxDb; 10090-ENSMUSP00000054556; -.
DR PeptideAtlas; P62631; -.
DR ProteomicsDB; 277686; -.
DR Antibodypedia; 29757; 313 antibodies from 38 providers.
DR DNASU; 13628; -.
DR Ensembl; ENSMUST00000055990.8; ENSMUSP00000054556.8; ENSMUSG00000016349.11.
DR GeneID; 13628; -.
DR KEGG; mmu:13628; -.
DR UCSC; uc008olh.1; mouse.
DR AGR; MGI:1096317; -.
DR CTD; 1917; -.
DR MGI; MGI:1096317; Eef1a2.
DR VEuPathDB; HostDB:ENSMUSG00000016349; -.
DR eggNOG; KOG0052; Eukaryota.
DR GeneTree; ENSGT00950000183029; -.
DR HOGENOM; CLU_007265_3_5_1; -.
DR InParanoid; P62631; -.
DR OMA; RDMGQTV; -.
DR OrthoDB; 5477300at2759; -.
DR PhylomeDB; P62631; -.
DR TreeFam; TF300304; -.
DR BioGRID-ORCS; 13628; 2 hits in 79 CRISPR screens.
DR PRO; PR:P62631; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; P62631; Protein.
DR Bgee; ENSMUSG00000016349; Expressed in perirhinal cortex and 191 other cell types or tissues.
DR Genevisible; P62631; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005853; C:eukaryotic translation elongation factor 1 complex; IDA:MGI.
DR GO; GO:0043209; C:myelin sheath; HDA:UniProtKB.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0045202; C:synapse; IDA:SynGO.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0003746; F:translation elongation factor activity; IDA:MGI.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IDA:MGI.
DR GO; GO:0006412; P:translation; IBA:GO_Central.
DR GO; GO:0006414; P:translational elongation; IDA:MGI.
DR CDD; cd01883; EF1_alpha; 1.
DR CDD; cd03693; EF1_alpha_II; 1.
DR CDD; cd03705; EF1_alpha_III; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 2.40.30.10; Translation factors; 2.
DR HAMAP; MF_00118_A; EF_Tu_A; 1.
DR InterPro; IPR004161; EFTu-like_2.
DR InterPro; IPR031157; G_TR_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR InterPro; IPR009001; Transl_elong_EF1A/Init_IF2_C.
DR InterPro; IPR004539; Transl_elong_EF1A_euk/arc.
DR InterPro; IPR004160; Transl_elong_EFTu/EF1A_C.
DR NCBIfam; TIGR00483; EF-1_alpha; 1.
DR PANTHER; PTHR23115:SF228; ELONGATION FACTOR 1-ALPHA 2; 1.
DR PANTHER; PTHR23115; TRANSLATION FACTOR; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF03144; GTP_EFTU_D2; 1.
DR Pfam; PF03143; GTP_EFTU_D3; 1.
DR PRINTS; PR00315; ELONGATNFCT.
DR SUPFAM; SSF50465; EF-Tu/eEF-1alpha/eIF2-gamma C-terminal domain; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF50447; Translation proteins; 1.
DR PROSITE; PS00301; G_TR_1; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Direct protein sequencing; Elongation factor; GTP-binding;
KW Methylation; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Protein biosynthesis; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..463
FT /note="Elongation factor 1-alpha 2"
FT /id="PRO_0000090892"
FT DOMAIN 5..242
FT /note="tr-type G"
FT REGION 14..21
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 70..74
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 91..94
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 153..156
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 194..196
FT /note="G5"
FT /evidence="ECO:0000250"
FT REGION 444..463
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 14..21
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 91..95
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 153..156
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N,N,N-trimethylglycine"
FT /evidence="ECO:0000250|UniProtKB:P68104"
FT MOD_RES 36
FT /note="N6,N6,N6-trimethyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q05639"
FT MOD_RES 36
FT /note="N6,N6-dimethyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q05639"
FT MOD_RES 36
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q05639"
FT MOD_RES 55
FT /note="N6,N6,N6-trimethyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q71V39"
FT MOD_RES 55
FT /note="N6,N6-dimethyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q05639"
FT MOD_RES 79
FT /note="N6,N6,N6-trimethyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q05639"
FT MOD_RES 165
FT /note="N6,N6,N6-trimethyllysine; alternate; by EEF1AKMT3"
FT /evidence="ECO:0000250|UniProtKB:Q05639"
FT MOD_RES 165
FT /note="N6,N6-dimethyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q05639"
FT MOD_RES 165
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q05639"
FT MOD_RES 179
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q05639"
FT MOD_RES 224
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P62632"
FT MOD_RES 301
FT /note="5-glutamyl glycerylphosphorylethanolamine"
FT /evidence="ECO:0000250|UniProtKB:Q71V39"
FT MOD_RES 374
FT /note="5-glutamyl glycerylphosphorylethanolamine"
FT /evidence="ECO:0000250|UniProtKB:Q71V39"
FT MOD_RES 439
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q05639"
SQ SEQUENCE 463 AA; 50454 MW; 31E4F59BC05D8F8C CRC64;
MGKEKTHINI VVIGHVDSGK STTTGHLIYK CGGIDKRTIE KFEKEAAEMG KGSFKYAWVL
DKLKAERERG ITIDISLWKF ETTKYYITII DAPGHRDFIK NMITGTSQAD CAVLIVAAGV
GEFEAGISKN GQTREHALLA YTLGVKQLIV GVNKMDSTEP AYSEKRYDEI VKEVSAYIKK
IGYNPATVPF VPISGWHGDN MLEPSPNMPW FKGWKVERKE GNASGVSLLE ALDTILPPTR
PTDKPLRLPL QDVYKIGGIG TVPVGRVETG ILRPGMVVTF APVNITTEVK SVEMHHEALS
EALPGDNVGF NVKNVSVKDI RRGNVCGDSK ADPPQEAAQF TSQVIILNHP GQISAGYSPV
IDCHTAHIAC KFAELKEKID RRSGKKLEDN PKSLKSGDAA IVEMVPGKPM CVESFSQYPP
LGRFAVRDMR QTVAVGVIKN VEKKSGGAGK VTKSAQKAQK AGK
//
