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P10126 (EF1A1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 153. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Elongation factor 1-alpha 1

Short name=EF-1-alpha-1
Alternative name(s):
Elongation factor Tu
Short name=EF-Tu
Eukaryotic elongation factor 1 A-1
Short name=eEF1A-1
Gene names
Name:Eef1a1
Synonyms:Eef1a
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length462 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis. With PARP1 and TXK, forms a complex that acts as a T helper 1 (Th1) cell-specific transcription factor and binds the promoter of IFN-gamma to directly regulate its transcription, and is thus involved importantly in Th1 cytokine production By similarity. HAMAP-Rule MF_00118_A

Subunit structure

Found in a nuclear export complex with XPO5, EEF1A1, Ran and aminoacylated tRNA. Interacts with PARP1, TXK, XPO5 and KARS By similarity. May interact with ERGIC2 By similarity. Interacts with DLC1, facilitating distribution to the membrane periphery and ruffles upon growth factor stimulation By similarity. Interacts with IFIT1 (via TPR repeats 4-7). Ref.10

Subcellular location

Cytoplasm. Nucleus By similarity. Note: Colocalizes with DLC1 at actin-rich regions in the cell periphery By similarity. Ref.10

Post-translational modification

ISGylated. Ref.9

Phosphorylated by TXK. Phosphorylation by PASK increases translation efficiency By similarity. HAMAP-Rule MF_00118_A

Sequence similarities

Belongs to the GTP-binding elongation factor family. EF-Tu/EF-1A subfamily.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

TSPY1Q015345EBI-773865,EBI-1973142From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 462462Elongation factor 1-alpha 1 HAMAP-Rule MF_00118_A
PRO_0000090886

Regions

Nucleotide binding14 – 218GTP By similarity
Nucleotide binding91 – 955GTP By similarity
Nucleotide binding153 – 1564GTP By similarity

Amino acid modifications

Modified residue361N6,N6,N6-trimethyllysine By similarity
Modified residue551N6,N6-dimethyllysine By similarity
Modified residue791N6,N6,N6-trimethyllysine By similarity
Modified residue1651N6,N6-dimethyllysine; alternate By similarity
Modified residue1651N6-acetyllysine; alternate Ref.11
Modified residue1721N6-acetyllysine Ref.11
Modified residue2731N6-acetyllysine Ref.11
Modified residue3001Phosphoserine; by TGFBR1 By similarity
Modified residue30115-glutamyl glycerylphosphorylethanolamine HAMAP-Rule MF_00118_A
Modified residue3181N6,N6,N6-trimethyllysine By similarity
Modified residue37415-glutamyl glycerylphosphorylethanolamine HAMAP-Rule MF_00118_A
Modified residue3921N6-acetyllysine; alternate Ref.11
Modified residue3921N6-succinyllysine; alternate Ref.11
Modified residue4321Phosphothreonine; by PASK By similarity
Modified residue4391N6-acetyllysine Ref.11

Experimental info

Sequence conflict71H → R in AAA37538. Ref.5
Sequence conflict151H → L in AAA37538. Ref.5
Sequence conflict231T → S in AAA37538. Ref.5
Sequence conflict77 – 782LW → QR in CAA31957. Ref.2
Sequence conflict831S → A in CAA27324. Ref.6
Sequence conflict91 – 922DA → ES in CAA31957. Ref.2
Sequence conflict1081Q → R in AAA37538. Ref.5
Sequence conflict1561D → G in BAC28085. Ref.3
Sequence conflict2221S → H in AAA50406. Ref.1
Sequence conflict224 – 2263SGT → VAP in CAA31957. Ref.2
Sequence conflict2251G → D in AAH04005. Ref.4
Sequence conflict2391Missing in CAA31957. Ref.2
Sequence conflict3501P → T in BAC36446. Ref.3

Sequences

Sequence LengthMass (Da)Tools
P10126 [UniParc].

Last modified October 25, 2004. Version 3.
Checksum: 71072871DE7405DC

FASTA46250,114
        10         20         30         40         50         60 
MGKEKTHINI VVIGHVDSGK STTTGHLIYK CGGIDKRTIE KFEKEAAEMG KGSFKYAWVL 

        70         80         90        100        110        120 
DKLKAERERG ITIDISLWKF ETSKYYVTII DAPGHRDFIK NMITGTSQAD CAVLIVAAGV 

       130        140        150        160        170        180 
GEFEAGISKN GQTREHALLA YTLGVKQLIV GVNKMDSTEP PYSQKRYEEI VKEVSTYIKK 

       190        200        210        220        230        240 
IGYNPDTVAF VPISGWNGDN MLEPSANMPW FKGWKVTRKD GSASGTTLLE ALDCILPPTR 

       250        260        270        280        290        300 
PTDKPLRLPL QDVYKIGGIG TVPVGRVETG VLKPGMVVTF APVNVTTEVK SVEMHHEALS 

       310        320        330        340        350        360 
EALPGDNVGF NVKNVSVKDV RRGNVAGDSK NDPPMEAAGF TAQVIILNHP GQISAGYAPV 

       370        380        390        400        410        420 
LDCHTAHIAC KFAELKEKID RRSGKKLEDG PKFLKSGDAA IVDMVPGKPM CVESFSDYPP 

       430        440        450        460 
LGRFAVRDMR QTVAVGVIKA VDKKAAGAGK VTKSAQKAQK AK 

« Hide

References

« Hide 'large scale' references
[1]"Isolation and mapping of a gene for protein synthesis initiation factor 4A and its expression during differentiation of murine erythroleukemia cells."
Reddy N.S., Roth W.W., Bragg P.W., Wahba A.J.
Gene 70:231-243(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"The complete cDNA sequence of mouse elongation factor 1 alpha (EF 1 alpha) mRNA."
Lu X., Werner D.
Nucleic Acids Res. 17:442-442(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Head, Testis and Thymus.
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Czech II.
Tissue: Mammary tumor and Olfactory epithelium.
[5]"Expression of a gene for mouse eucaryotic elongation factor Tu during murine erythroleukemic cell differentiation."
Roth W.W., Bragg P.W., Corrias M.V., Reddy N.S., Dholakia J.N., Wahba A.J.
Mol. Cell. Biol. 7:3929-3936(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-108.
[6]"Structure of the amino-terminal end of mammalian elongation factor Tu."
Rao T.R., Slobin L.I.
Nucleic Acids Res. 14:2409-2409(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-94.
[7]Lubec G., Kang S.U., Yang J.W., Zigmond M., Sunyer B., Chen W.-Q.
Submitted (JAN-2009) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 6-30; 85-96; 135-146; 155-165; 248-290 AND 431-439, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: C57BL/6 and OF1.
Tissue: Brain and Hippocampus.
[8]"Murine elongation factor 1 alpha (EF-1 alpha) is posttranslationally modified by novel amide-linked ethanolamine-phosphoglycerol moieties. Addition of ethanolamine-phosphoglycerol to specific glutamic acid residues on EF-1 alpha."
Whiteheart S.W., Shenbagarmurthi P., Chen L., Cotter R.J., Hart G.W.
J. Biol. Chem. 264:14334-14341(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 291-313 AND 372-376, ETHANOLAMINYLATION AT GLU-301 AND GLU-374.
[9]"Proteomic identification of proteins conjugated to ISG15 in mouse and human cells."
Giannakopoulos N.V., Luo J.K., Papov V., Zou W., Lenschow D.J., Jacobs B.S., Borden E.C., Li J., Virgin H.W., Zhang D.E.
Biochem. Biophys. Res. Commun. 336:496-506(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: ISGYLATION.
[10]"The interaction between interferon-induced protein with tetratricopeptide repeats-1 and eukaryotic elongation factor-1A."
Li H.T., Su Y.P., Cheng T.M., Xu J.M., Liao J., Chen J.C., Ji C.Y., Ai G.P., Wang J.P.
Mol. Cell. Biochem. 337:101-110(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH IFIT1, SUBCELLULAR LOCATION.
[11]"SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-165; LYS-172; LYS-273; LYS-392 AND LYS-439, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-392, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M22432 mRNA. Translation: AAA50406.1.
X13661 mRNA. Translation: CAA31957.1.
AK032914 mRNA. Translation: BAC28085.1.
AK076696 mRNA. Translation: BAC36446.1.
AK081725 mRNA. Translation: BAC38311.1.
AK083361 mRNA. Translation: BAC38884.1.
BC004005 mRNA. Translation: AAH04005.1.
BC004067 mRNA. Translation: AAH04067.1.
BC005660 mRNA. Translation: AAH05660.1.
BC018223 mRNA. Translation: AAH18223.1.
BC018485 mRNA. Translation: AAH18485.1.
BC083069 mRNA. Translation: AAH83069.1.
M17878 Genomic DNA. Translation: AAA37538.1.
X03688 mRNA. Translation: CAA27324.1.
PIREFMS1. S02114.
RefSeqNP_034236.2. NM_010106.2.
UniGeneMm.138471.
Mm.335315.
Mm.360075.
Mm.391071.
Mm.485669.
Mm.491424.

3D structure databases

ProteinModelPortalP10126.
SMRP10126. Positions 2-443.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid199385. 12 interactions.
DIPDIP-46609N.
IntActP10126. 25 interactions.
MINTMINT-1862449.

PTM databases

PhosphoSiteP10126.

2D gel databases

SWISS-2DPAGEP10126.

Proteomic databases

PaxDbP10126.
PRIDEP10126.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000042235; ENSMUSP00000042457; ENSMUSG00000037742.
GeneID13627.
KEGGmmu:101056619.
mmu:13627.
UCSCuc009qun.1. mouse.

Organism-specific databases

CTD1915.
MGIMGI:1096881. Eef1a1.

Phylogenomic databases

eggNOGCOG5256.
HOGENOMHOG000229291.
HOVERGENHBG000179.
InParanoidP10126.
KOK03231.
OMAAIRDMGM.
OrthoDBEOG7NKKK3.
PhylomeDBP10126.
TreeFamTF300304.

Gene expression databases

BgeeP10126.
GenevestigatorP10126.

Family and domain databases

Gene3D3.40.50.300. 1 hit.
HAMAPMF_00118_A. EF_Tu_A.
InterProIPR000795. EF_GTP-bd_dom.
IPR027417. P-loop_NTPase.
IPR009000. Transl_B-barrel.
IPR009001. Transl_elong_EF1A/Init_IF2_C.
IPR004539. Transl_elong_EF1A_euk/arc.
IPR004161. Transl_elong_EFTu/EF1A_2.
IPR004160. Transl_elong_EFTu/EF1A_C.
[Graphical view]
PfamPF00009. GTP_EFTU. 1 hit.
PF03144. GTP_EFTU_D2. 1 hit.
PF03143. GTP_EFTU_D3. 1 hit.
[Graphical view]
PRINTSPR00315. ELONGATNFCT.
SUPFAMSSF50447. SSF50447. 1 hit.
SSF50465. SSF50465. 1 hit.
SSF52540. SSF52540. 1 hit.
TIGRFAMsTIGR00483. EF-1_alpha. 1 hit.
PROSITEPS00301. EFACTOR_GTP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio284304.
PROP10126.
SOURCESearch...

Entry information

Entry nameEF1A1_MOUSE
AccessionPrimary (citable) accession number: P10126
Secondary accession number(s): Q61511 expand/collapse secondary AC list , Q6ZWN2, Q8BMB8, Q8BVS8, Q99KU5
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: October 25, 2004
Last modified: April 16, 2014
This is version 153 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot