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P10126

- EF1A1_MOUSE

UniProt

P10126 - EF1A1_MOUSE

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Protein

Elongation factor 1-alpha 1

Gene
Eef1a1, Eef1a
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi14 – 218GTP By similarity
Nucleotide bindingi91 – 955GTP By similarity
Nucleotide bindingi153 – 1564GTP By similarity

GO - Molecular functioni

  1. GTPase activity Source: InterPro
  2. GTP binding Source: UniProtKB-KW
  3. protein binding Source: UniProtKB
  4. translation elongation factor activity Source: UniProtKB-KW

GO - Biological processi

  1. cellular response to epidermal growth factor stimulus Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Elongation factor

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_225256. HSF1 activation.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:Eef1a1
Synonyms:Eef1a
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 9

Organism-specific databases

MGIiMGI:1096881. Eef1a1.

Subcellular locationi

Cytoplasm. Nucleus By similarity. Nucleusnucleolus By similarity
Note: Colocalizes with DLC1 at actin-rich regions in the cell periphery. Translocates together with ZPR1 from the cytoplasm to the nucleus and nucleolus after treatment with mitogens By similarity.

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. nucleolus Source: UniProtKB
  3. nucleus Source: UniProtKB
  4. plasma membrane Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 462462Elongation factor 1-alpha 1PRO_0000090886Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei36 – 361N6,N6,N6-trimethyllysine By similarity
Modified residuei55 – 551N6,N6-dimethyllysine By similarity
Modified residuei79 – 791N6,N6,N6-trimethyllysine By similarity
Modified residuei165 – 1651N6,N6-dimethyllysine; alternate By similarity
Modified residuei165 – 1651N6-acetyllysine; alternate
Modified residuei172 – 1721N6-acetyllysine
Modified residuei273 – 2731N6-acetyllysine
Modified residuei300 – 3001Phosphoserine; by TGFBR1 By similarity
Modified residuei301 – 30115-glutamyl glycerylphosphorylethanolamine1 Publication
Modified residuei318 – 3181N6,N6,N6-trimethyllysine By similarity
Modified residuei374 – 37415-glutamyl glycerylphosphorylethanolamine1 Publication
Modified residuei392 – 3921N6-acetyllysine; alternate
Modified residuei392 – 3921N6-succinyllysine; alternate
Modified residuei432 – 4321Phosphothreonine; by PASK By similarity
Modified residuei439 – 4391N6-acetyllysine

Post-translational modificationi

ISGylated.
Phosphorylated by TXK. Phosphorylation by PASK increases translation efficiency By similarity.

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP10126.
PaxDbiP10126.
PRIDEiP10126.

2D gel databases

SWISS-2DPAGEP10126.

PTM databases

PhosphoSiteiP10126.

Expressioni

Gene expression databases

BgeeiP10126.
GenevestigatoriP10126.

Interactioni

Subunit structurei

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 ZPR1; the interaction occurs in a epidermal growth factor (EGF)-dependent manner By similarity. Interacts with IFIT1 (via TPR repeats 4-7).

Binary interactionsi

WithEntry#Exp.IntActNotes
TSPY1Q015345EBI-773865,EBI-1973142From a different organism.

Protein-protein interaction databases

BioGridi199385. 13 interactions.
DIPiDIP-46609N.
IntActiP10126. 25 interactions.
MINTiMINT-1862449.

Structurei

3D structure databases

ProteinModelPortaliP10126.
SMRiP10126. Positions 2-443.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini5 – 242238tr-type GAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni14 – 218G1 By similarity
Regioni70 – 745G2 By similarity
Regioni91 – 944G3 By similarity
Regioni153 – 1564G4 By similarity
Regioni194 – 1963G5 By similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG5256.
HOGENOMiHOG000229291.
HOVERGENiHBG000179.
InParanoidiP10126.
KOiK03231.
OMAiADKPHMN.
OrthoDBiEOG7NKKK3.
PhylomeDBiP10126.
TreeFamiTF300304.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
HAMAPiMF_00118_A. EF_Tu_A.
InterProiIPR000795. 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]
PfamiPF00009. GTP_EFTU. 1 hit.
PF03144. GTP_EFTU_D2. 1 hit.
PF03143. GTP_EFTU_D3. 1 hit.
[Graphical view]
PRINTSiPR00315. ELONGATNFCT.
SUPFAMiSSF50447. SSF50447. 1 hit.
SSF50465. SSF50465. 1 hit.
SSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00483. EF-1_alpha. 1 hit.
PROSITEiPS00301. G_TR_1. 1 hit.
PS51722. G_TR_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P10126-1 [UniParc]FASTAAdd to Basket

« Hide

MGKEKTHINI VVIGHVDSGK STTTGHLIYK CGGIDKRTIE KFEKEAAEMG    50
KGSFKYAWVL DKLKAERERG ITIDISLWKF ETSKYYVTII DAPGHRDFIK 100
NMITGTSQAD CAVLIVAAGV GEFEAGISKN GQTREHALLA YTLGVKQLIV 150
GVNKMDSTEP PYSQKRYEEI VKEVSTYIKK IGYNPDTVAF VPISGWNGDN 200
MLEPSANMPW FKGWKVTRKD GSASGTTLLE ALDCILPPTR PTDKPLRLPL 250
QDVYKIGGIG TVPVGRVETG VLKPGMVVTF APVNVTTEVK SVEMHHEALS 300
EALPGDNVGF NVKNVSVKDV RRGNVAGDSK NDPPMEAAGF TAQVIILNHP 350
GQISAGYAPV LDCHTAHIAC KFAELKEKID RRSGKKLEDG PKFLKSGDAA 400
IVDMVPGKPM CVESFSDYPP LGRFAVRDMR QTVAVGVIKA VDKKAAGAGK 450
VTKSAQKAQK AK 462
Length:462
Mass (Da):50,114
Last modified:October 25, 2004 - v3
Checksum:i71072871DE7405DC
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti7 – 71H → R in AAA37538. 1 Publication
Sequence conflicti15 – 151H → L in AAA37538. 1 Publication
Sequence conflicti23 – 231T → S in AAA37538. 1 Publication
Sequence conflicti77 – 782LW → QR in CAA31957. 1 Publication
Sequence conflicti83 – 831S → A in CAA27324. 1 Publication
Sequence conflicti91 – 922DA → ES in CAA31957. 1 Publication
Sequence conflicti108 – 1081Q → R in AAA37538. 1 Publication
Sequence conflicti156 – 1561D → G in BAC28085. 1 Publication
Sequence conflicti222 – 2221S → H in AAA50406. 1 Publication
Sequence conflicti224 – 2263SGT → VAP in CAA31957. 1 Publication
Sequence conflicti225 – 2251G → D in AAH04005. 1 Publication
Sequence conflicti239 – 2391Missing in CAA31957. 1 Publication
Sequence conflicti350 – 3501P → T in BAC36446. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS40703.1.
PIRiS02114. EFMS1.
RefSeqiNP_034236.2. NM_010106.2.
UniGeneiMm.138471.
Mm.335315.
Mm.360075.
Mm.391071.
Mm.485669.
Mm.491424.

Genome annotation databases

EnsembliENSMUST00000042235; ENSMUSP00000042457; ENSMUSG00000037742.
GeneIDi13627.
KEGGimmu:13627.
UCSCiuc009qun.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS40703.1.
PIRi S02114. EFMS1.
RefSeqi NP_034236.2. NM_010106.2.
UniGenei Mm.138471.
Mm.335315.
Mm.360075.
Mm.391071.
Mm.485669.
Mm.491424.

3D structure databases

ProteinModelPortali P10126.
SMRi P10126. Positions 2-443.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 199385. 13 interactions.
DIPi DIP-46609N.
IntActi P10126. 25 interactions.
MINTi MINT-1862449.

PTM databases

PhosphoSitei P10126.

2D gel databases

SWISS-2DPAGE P10126.

Proteomic databases

MaxQBi P10126.
PaxDbi P10126.
PRIDEi P10126.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000042235 ; ENSMUSP00000042457 ; ENSMUSG00000037742 .
GeneIDi 13627.
KEGGi mmu:13627.
UCSCi uc009qun.1. mouse.

Organism-specific databases

CTDi 1915.
MGIi MGI:1096881. Eef1a1.

Phylogenomic databases

eggNOGi COG5256.
HOGENOMi HOG000229291.
HOVERGENi HBG000179.
InParanoidi P10126.
KOi K03231.
OMAi ADKPHMN.
OrthoDBi EOG7NKKK3.
PhylomeDBi P10126.
TreeFami TF300304.

Enzyme and pathway databases

Reactomei REACT_225256. HSF1 activation.

Miscellaneous databases

NextBioi 284304.
PROi P10126.
SOURCEi Search...

Gene expression databases

Bgeei P10126.
Genevestigatori P10126.

Family and domain databases

Gene3Di 3.40.50.300. 1 hit.
HAMAPi MF_00118_A. EF_Tu_A.
InterProi IPR000795. 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 ]
Pfami PF00009. GTP_EFTU. 1 hit.
PF03144. GTP_EFTU_D2. 1 hit.
PF03143. GTP_EFTU_D3. 1 hit.
[Graphical view ]
PRINTSi PR00315. ELONGATNFCT.
SUPFAMi SSF50447. SSF50447. 1 hit.
SSF50465. SSF50465. 1 hit.
SSF52540. SSF52540. 1 hit.
TIGRFAMsi TIGR00483. EF-1_alpha. 1 hit.
PROSITEi PS00301. G_TR_1. 1 hit.
PS51722. G_TR_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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.

Entry informationi

Entry nameiEF1A1_MOUSE
AccessioniPrimary (citable) accession number: P10126
Secondary accession number(s): Q61511
, Q6ZWN2, Q8BMB8, Q8BVS8, Q99KU5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: October 25, 2004
Last modified: September 3, 2014
This is version 157 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi