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Q05639 (EF1A2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 154. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Elongation factor 1-alpha 2

Short name=EF-1-alpha-2
Alternative name(s):
Eukaryotic elongation factor 1 A-2
Short name=eEF1A-2
Statin-S1
Gene names
Name:EEF1A2
Synonyms:EEF1AL, STN
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length463 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. HAMAP-Rule MF_00118_A

Subunit structure

Monomer By similarity. HAMAP-Rule MF_00118_A

Subcellular location

Nucleus By similarity HAMAP-Rule MF_00118_A.

Tissue specificity

Brain, heart, and skeletal muscle.

Sequence similarities

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 463463Elongation factor 1-alpha 2 HAMAP-Rule MF_00118_A
PRO_0000090891

Regions

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

Amino acid modifications

Modified residue551N6,N6,N6-trimethyllysine By similarity
Modified residue1651N6,N6,N6-trimethyllysine By similarity
Modified residue1791N6-acetyllysine Ref.8
Modified residue30115-glutamyl glycerylphosphorylethanolamine By similarity
Modified residue37415-glutamyl glycerylphosphorylethanolamine By similarity
Modified residue4391N6-acetyllysine Ref.8

Natural variations

Natural variant701G → S Found in a patient with mental retardation, severe delay of psychomotor development, very limited speech, autistic features and aggressive behaviors. Ref.11
VAR_069395

Experimental info

Sequence conflict4271R → P in AAA91835. Ref.7

Sequences

Sequence LengthMass (Da)Tools
Q05639 [UniParc].

Last modified June 1, 1994. Version 1.
Checksum: 31E4E341CEE797EC

FASTA46350,470
        10         20         30         40         50         60 
MGKEKTHINI VVIGHVDSGK STTTGHLIYK CGGIDKRTIE KFEKEAAEMG KGSFKYAWVL 

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

       130        140        150        160        170        180 
GEFEAGISKN GQTREHALLA YTLGVKQLIV GVNKMDSTEP AYSEKRYDEI VKEVSAYIKK 

       190        200        210        220        230        240 
IGYNPATVPF VPISGWHGDN MLEPSPNMPW FKGWKVERKE GNASGVSLLE ALDTILPPTR 

       250        260        270        280        290        300 
PTDKPLRLPL QDVYKIGGIG TVPVGRVETG ILRPGMVVTF APVNITTEVK SVEMHHEALS 

       310        320        330        340        350        360 
EALPGDNVGF NVKNVSVKDI RRGNVCGDSK SDPPQEAAQF TSQVIILNHP GQISAGYSPV 

       370        380        390        400        410        420 
IDCHTAHIAC KFAELKEKID RRSGKKLEDN PKSLKSGDAA IVEMVPGKPM CVESFSQYPP 

       430        440        450        460 
LGRFAVRDMR QTVAVGVIKN VEKKSGGAGK VTKSAQKAQK AGK 

« Hide

References

« Hide 'large scale' references
[1]"Tissue-dependent variation in the expression of elongation factor-1 alpha isoforms: isolation and characterisation of a cDNA encoding a novel variant of human elongation-factor 1 alpha."
Knudsen S.M., Frydenberg J., Clark B.F.C., Leffers H.
Eur. J. Biochem. 215:549-554(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"The human elongation factor 1 A-2 gene (EEF1A2): complete sequence and characterization of gene structure and promoter activity."
Bischoff C., Kahns S., Lund A., Joergensen H.F., Praestegaard M., Clark B.F.C., Leffers H.
Genomics 68:63-70(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Human protein factory for converting the transcriptome into an in vitro-expressed proteome."
Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R., Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y., Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B. expand/collapse author list , Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S., Nomura N.
Nat. Methods 5:1011-1017(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]"The DNA sequence and comparative analysis of human chromosome 20."
Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E. expand/collapse author list , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"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].
Tissue: Duodenum and Lung.
[7]"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."
Lee S., Ann D.K., Wang E.
Biochem. Biophys. Res. Commun. 203:1371-1377(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 29-463.
Tissue: Hippocampus.
[8]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-179 AND LYS-439, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[9]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"The structure of HLA-DR52c: comparison to other HLA-DRB3 alleles."
Dai S., Crawford F., Marrack P., Kappler J.W.
Proc. Natl. Acad. Sci. U.S.A. 105:11893-11897(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 343-355 IN COMPLEX WITH HLA-DRA/HLA-DRB3 HETERODIMER.
[11]"Diagnostic exome sequencing in persons with severe intellectual disability."
de Ligt J., Willemsen M.H., van Bon B.W., Kleefstra T., Yntema H.G., Kroes T., Vulto-van Silfhout A.T., Koolen D.A., de Vries P., Gilissen C., del Rosario M., Hoischen A., Scheffer H., de Vries B.B., Brunner H.G., Veltman J.A., Vissers L.E.
N. Engl. J. Med. 367:1921-1929(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT SER-70.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X70940 mRNA. Translation: CAA50280.1.
AF163763 Genomic DNA. Translation: AAF80488.1.
AB451389 mRNA. Translation: BAG70203.1.
AL121829 Genomic DNA. Translation: CAC15522.1.
CH471077 Genomic DNA. Translation: EAW75260.1.
BC000432 mRNA. Translation: AAH00432.1.
BC110409 mRNA. Translation: AAI10410.1.
L10340 mRNA. Translation: AAA91835.1.
CCDSCCDS13522.1.
PIREFHUA2. S35033.
RefSeqNP_001949.1. NM_001958.3.
UniGeneHs.433839.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3C5JX-ray1.80C343-355[»]
ProteinModelPortalQ05639.
SMRQ05639. Positions 2-443.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108238. 44 interactions.
IntActQ05639. 24 interactions.
MINTMINT-1141378.
STRING9606.ENSP00000217182.

Chemistry

BindingDBQ05639.
ChEMBLCHEMBL1795122.

PTM databases

PhosphoSiteQ05639.

Polymorphism databases

DMDM544231.

Proteomic databases

MaxQBQ05639.
PaxDbQ05639.
PeptideAtlasQ05639.
PRIDEQ05639.

Protocols and materials databases

DNASU1917.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000217182; ENSP00000217182; ENSG00000101210.
ENST00000298049; ENSP00000298049; ENSG00000101210.
GeneID1917.
KEGGhsa:1917.
UCSCuc002yfe.2. human.

Organism-specific databases

CTD1917.
GeneCardsGC20M062119.
HGNCHGNC:3192. EEF1A2.
HPACAB034019.
MIM602959. gene.
neXtProtNX_Q05639.
PharmGKBPA36219.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5256.
HOGENOMHOG000229291.
HOVERGENHBG000179.
InParanoidQ05639.
KOK03231.
OMAVACTFES.
OrthoDBEOG7NKKK3.
PhylomeDBQ05639.
TreeFamTF300304.

Enzyme and pathway databases

ReactomeREACT_17015. Metabolism of proteins.
REACT_71. Gene Expression.

Gene expression databases

BgeeQ05639.
CleanExHS_EEF1A2.
GenevestigatorQ05639.

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

EvolutionaryTraceQ05639.
GeneWikiEEF1A2.
GenomeRNAi1917.
NextBio7803.
PROQ05639.
SOURCESearch...

Entry information

Entry nameEF1A2_HUMAN
AccessionPrimary (citable) accession number: Q05639
Secondary accession number(s): B5BUF3 expand/collapse secondary AC list , E1P5J1, P54266, Q0VGC7
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: July 9, 2014
This is version 154 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 20

Human chromosome 20: entries, gene names and cross-references to MIM