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Elongation factor 1-alpha 2 (EF-1-alpha-2) (Eukaryotic elongation factor 1 A-2) (eEF1A-2) (Statin-S1)

 EF1A2_MOUSE             Reviewed;         463 AA.
P62631; P27706;
19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
19-JUL-2004, sequence version 1.
20-DEC-2017, entry version 132.
RecName: Full=Elongation factor 1-alpha 2;
Short=EF-1-alpha-2;
AltName: Full=Eukaryotic elongation factor 1 A-2;
Short=eEF1A-2;
AltName: Full=Statin-S1;
Name=Eef1a2; Synonyms=Eef1al, Stn;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Brain;
PubMed=7945283; DOI=10.1006/bbrc.1994.2336;
Lee S., Ann D.K., Wang E.;
"Cloning of human and mouse brain cDNAs coding for S1, the second
member of the mammalian elongation factor-1 alpha gene family:
analysis of a possible evolutionary pathway.";
Biochem. Biophys. Res. Commun. 203:1371-1377(1994).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Eye;
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).
[3]
PROTEIN SEQUENCE OF 6-30; 85-96; 135-146; 155-165; 248-266 AND
431-439, AND IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=C57BL/6J, and OF1; TISSUE=Brain, and Hippocampus;
Lubec G., Kang S.U., Sunyer B., Chen W.-Q.;
Submitted (JAN-2009) to UniProtKB.
[4]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, and Lung;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: This protein promotes the GTP-dependent binding of
aminoacyl-tRNA to the A-site of ribosomes during protein
biosynthesis.
-!- SUBUNIT: Monomer.
-!- SUBCELLULAR LOCATION: Nucleus.
-!- TISSUE SPECIFICITY: Found in a wide range of tissues.
-!- DEVELOPMENTAL STAGE: The statin expression is specific for
nonproliferating cells. Its message is most abundant in G0 phase
of 3T3 mouse fibroblasts, but becomes significantly reduced in G1
and S1 phases cells.
-!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A
subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; L26479; AAA91870.1; -; mRNA.
EMBL; BC018235; AAH18235.1; -; mRNA.
CCDS; CCDS17201.1; -.
PIR; JC2445; JC2445.
RefSeq; NP_031932.1; NM_007906.2.
UniGene; Mm.2645; -.
ProteinModelPortal; P62631; -.
SMR; P62631; -.
BioGrid; 199386; 9.
IntAct; P62631; 12.
MINT; MINT-1676226; -.
STRING; 10090.ENSMUSP00000054556; -.
iPTMnet; P62631; -.
PhosphoSitePlus; P62631; -.
SwissPalm; P62631; -.
EPD; P62631; -.
MaxQB; P62631; -.
PaxDb; P62631; -.
PeptideAtlas; P62631; -.
PRIDE; P62631; -.
Ensembl; ENSMUST00000055990; ENSMUSP00000054556; ENSMUSG00000016349.
GeneID; 13628; -.
KEGG; mmu:13628; -.
UCSC; uc008olh.1; mouse.
CTD; 1917; -.
MGI; MGI:1096317; Eef1a2.
eggNOG; KOG0052; Eukaryota.
eggNOG; COG5256; LUCA.
GeneTree; ENSGT00900000141045; -.
HOGENOM; HOG000229291; -.
HOVERGEN; HBG000179; -.
InParanoid; P62631; -.
KO; K03231; -.
OMA; ASEKMPW; -.
OrthoDB; EOG091G05LW; -.
TreeFam; TF300304; -.
PRO; PR:P62631; -.
Proteomes; UP000000589; Chromosome 2.
Bgee; ENSMUSG00000016349; -.
Genevisible; P62631; MM.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0005853; C:eukaryotic translation elongation factor 1 complex; IDA:MGI.
GO; GO:0043209; C:myelin sheath; IDA:UniProtKB.
GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
GO; GO:0019901; F:protein kinase binding; ISO:MGI.
GO; GO:0003746; F:translation elongation factor activity; IDA:MGI.
GO; GO:0043065; P:positive regulation of apoptotic process; IDA:MGI.
GO; GO:0090218; P:positive regulation of lipid kinase activity; ISO:MGI.
GO; GO:0051602; P:response to electrical stimulus; IEA:Ensembl.
GO; GO:0010035; P:response to inorganic substance; IEA:Ensembl.
GO; GO:0006414; P:translational elongation; IDA:MGI.
HAMAP; MF_00118_A; EF_Tu_A; 1.
InterPro; IPR004161; EFTu-like_2.
InterPro; IPR031157; G_TR_CS.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR000795; TF_GTP-bd_dom.
InterPro; IPR009000; Transl_B-barrel_sf.
InterPro; IPR009001; Transl_elong_EF1A/Init_IF2_C.
InterPro; IPR004539; Transl_elong_EF1A_euk/arc.
InterPro; IPR004160; Transl_elong_EFTu/EF1A_C.
Pfam; PF00009; GTP_EFTU; 1.
Pfam; PF03144; GTP_EFTU_D2; 1.
Pfam; PF03143; GTP_EFTU_D3; 1.
PRINTS; PR00315; ELONGATNFCT.
SUPFAM; SSF50447; SSF50447; 1.
SUPFAM; SSF50465; SSF50465; 1.
SUPFAM; SSF52540; SSF52540; 1.
TIGRFAMs; TIGR00483; EF-1_alpha; 1.
PROSITE; PS00301; G_TR_1; 1.
PROSITE; PS51722; G_TR_2; 1.
1: Evidence at protein level;
Acetylation; Complete proteome; Direct protein sequencing;
Elongation factor; GTP-binding; Methylation; Nucleotide-binding;
Nucleus; Phosphoprotein; Protein biosynthesis; Reference proteome.
INIT_MET 1 1 Removed.
CHAIN 2 463 Elongation factor 1-alpha 2.
/FTId=PRO_0000090892.
DOMAIN 5 242 tr-type G.
NP_BIND 14 21 GTP. {ECO:0000250}.
NP_BIND 91 95 GTP. {ECO:0000250}.
NP_BIND 153 156 GTP. {ECO:0000250}.
REGION 14 21 G1. {ECO:0000250}.
REGION 70 74 G2. {ECO:0000250}.
REGION 91 94 G3. {ECO:0000250}.
REGION 153 156 G4. {ECO:0000250}.
REGION 194 196 G5. {ECO:0000250}.
MOD_RES 2 2 N,N,N-trimethylglycine.
{ECO:0000250|UniProtKB:P68104}.
MOD_RES 55 55 N6,N6,N6-trimethyllysine; alternate.
{ECO:0000250|UniProtKB:Q71V39}.
MOD_RES 55 55 N6,N6-dimethyllysine; alternate.
{ECO:0000250|UniProtKB:Q5VTE0}.
MOD_RES 79 79 N6,N6,N6-trimethyllysine.
{ECO:0000250|UniProtKB:Q05639}.
MOD_RES 165 165 N6,N6,N6-trimethyllysine; alternate; by
EEF1AKMT3.
{ECO:0000250|UniProtKB:Q05639}.
MOD_RES 165 165 N6,N6-dimethyllysine; alternate.
{ECO:0000250|UniProtKB:Q05639}.
MOD_RES 165 165 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P10126}.
MOD_RES 165 165 N6-methyllysine; alternate.
{ECO:0000250|UniProtKB:Q05639}.
MOD_RES 172 172 N6-acetyllysine.
{ECO:0000250|UniProtKB:P10126}.
MOD_RES 179 179 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q05639}.
MOD_RES 224 224 Phosphoserine.
{ECO:0000250|UniProtKB:P62632}.
MOD_RES 301 301 5-glutamyl
glycerylphosphorylethanolamine.
{ECO:0000250|UniProtKB:Q71V39}.
MOD_RES 374 374 5-glutamyl
glycerylphosphorylethanolamine.
{ECO:0000250|UniProtKB:Q71V39}.
MOD_RES 392 392 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P10126}.
MOD_RES 392 392 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P10126}.
MOD_RES 439 439 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q05639}.
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


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