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Q05639

- EF1A2_HUMAN

UniProt

Q05639 - EF1A2_HUMAN

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Protein

Elongation factor 1-alpha 2

Gene

EEF1A2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 4 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.

Regions

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

GO - Molecular functioni

  1. GTPase activity Source: InterPro
  2. GTP binding Source: UniProtKB-KW
  3. translation elongation factor activity Source: UniProtKB-KW
  4. translation factor activity, nucleic acid binding Source: ProtInc

GO - Biological processi

  1. positive regulation of apoptotic process Source: Ensembl
  2. response to inorganic substance Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Elongation factor

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_1477. Eukaryotic Translation Elongation.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:EEF1A2
Synonyms:EEF1AL, STN
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 20

Organism-specific databases

HGNCiHGNC:3192. EEF1A2.

Subcellular locationi

Nucleus By similarity

GO - Cellular componenti

  1. eukaryotic translation elongation factor 1 complex Source: Ensembl
  2. neuronal cell body Source: Ensembl
  3. nucleus Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA36219.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 463463Elongation factor 1-alpha 2PRO_0000090891Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei55 – 551N6,N6,N6-trimethyllysineBy similarity
Modified residuei165 – 1651N6,N6,N6-trimethyllysineBy similarity
Modified residuei179 – 1791N6-acetyllysine1 Publication
Modified residuei301 – 30115-glutamyl glycerylphosphorylethanolamineBy similarity
Modified residuei374 – 37415-glutamyl glycerylphosphorylethanolamineBy similarity
Modified residuei439 – 4391N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein

Proteomic databases

MaxQBiQ05639.
PaxDbiQ05639.
PeptideAtlasiQ05639.
PRIDEiQ05639.

PTM databases

PhosphoSiteiQ05639.

Expressioni

Tissue specificityi

Brain, heart, and skeletal muscle.

Gene expression databases

BgeeiQ05639.
CleanExiHS_EEF1A2.
GenevestigatoriQ05639.

Organism-specific databases

HPAiCAB034019.

Interactioni

Subunit structurei

Monomer.By similarity

Protein-protein interaction databases

BioGridi108238. 67 interactions.
IntActiQ05639. 24 interactions.
MINTiMINT-1141378.
STRINGi9606.ENSP00000217182.

Structurei

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3C5JX-ray1.80C343-355[»]
ProteinModelPortaliQ05639.
SMRiQ05639. Positions 2-443.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ05639.

Family & Domainsi

Domains and Repeats

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

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni14 – 218G1By similarity
Regioni70 – 745G2By similarity
Regioni91 – 944G3By similarity
Regioni153 – 1564G4By similarity
Regioni194 – 1963G5By similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG5256.
GeneTreeiENSGT00670000097815.
HOGENOMiHOG000229291.
HOVERGENiHBG000179.
InParanoidiQ05639.
KOiK03231.
OMAiVACTFES.
OrthoDBiEOG7NKKK3.
PhylomeDBiQ05639.
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.

Q05639-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MGKEKTHINI VVIGHVDSGK STTTGHLIYK CGGIDKRTIE KFEKEAAEMG
60 70 80 90 100
KGSFKYAWVL DKLKAERERG ITIDISLWKF ETTKYYITII DAPGHRDFIK
110 120 130 140 150
NMITGTSQAD CAVLIVAAGV GEFEAGISKN GQTREHALLA YTLGVKQLIV
160 170 180 190 200
GVNKMDSTEP AYSEKRYDEI VKEVSAYIKK IGYNPATVPF VPISGWHGDN
210 220 230 240 250
MLEPSPNMPW FKGWKVERKE GNASGVSLLE ALDTILPPTR PTDKPLRLPL
260 270 280 290 300
QDVYKIGGIG TVPVGRVETG ILRPGMVVTF APVNITTEVK SVEMHHEALS
310 320 330 340 350
EALPGDNVGF NVKNVSVKDI RRGNVCGDSK SDPPQEAAQF TSQVIILNHP
360 370 380 390 400
GQISAGYSPV IDCHTAHIAC KFAELKEKID RRSGKKLEDN PKSLKSGDAA
410 420 430 440 450
IVEMVPGKPM CVESFSQYPP LGRFAVRDMR QTVAVGVIKN VEKKSGGAGK
460
VTKSAQKAQK AGK
Length:463
Mass (Da):50,470
Last modified:June 1, 1994 - v1
Checksum:i31E4E341CEE797EC
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti427 – 4271R → P in AAA91835. (PubMed:7945283)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti70 – 701G → S Found in a patient with mental retardation, severe delay of psychomotor development, very limited speech, autistic features and aggressive behaviors. 1 Publication
VAR_069395

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS13522.1.
PIRiS35033. EFHUA2.
RefSeqiNP_001949.1. NM_001958.3.
UniGeneiHs.433839.

Genome annotation databases

EnsembliENST00000217182; ENSP00000217182; ENSG00000101210.
ENST00000298049; ENSP00000298049; ENSG00000101210.
GeneIDi1917.
KEGGihsa:1917.
UCSCiuc002yfe.2. human.

Polymorphism databases

DMDMi544231.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS13522.1.
PIRi S35033. EFHUA2.
RefSeqi NP_001949.1. NM_001958.3.
UniGenei Hs.433839.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3C5J X-ray 1.80 C 343-355 [» ]
ProteinModelPortali Q05639.
SMRi Q05639. Positions 2-443.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108238. 67 interactions.
IntActi Q05639. 24 interactions.
MINTi MINT-1141378.
STRINGi 9606.ENSP00000217182.

Chemistry

BindingDBi Q05639.
ChEMBLi CHEMBL1795122.

PTM databases

PhosphoSitei Q05639.

Polymorphism databases

DMDMi 544231.

Proteomic databases

MaxQBi Q05639.
PaxDbi Q05639.
PeptideAtlasi Q05639.
PRIDEi Q05639.

Protocols and materials databases

DNASUi 1917.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000217182 ; ENSP00000217182 ; ENSG00000101210 .
ENST00000298049 ; ENSP00000298049 ; ENSG00000101210 .
GeneIDi 1917.
KEGGi hsa:1917.
UCSCi uc002yfe.2. human.

Organism-specific databases

CTDi 1917.
GeneCardsi GC20M062119.
HGNCi HGNC:3192. EEF1A2.
HPAi CAB034019.
MIMi 602959. gene.
neXtProti NX_Q05639.
PharmGKBi PA36219.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5256.
GeneTreei ENSGT00670000097815.
HOGENOMi HOG000229291.
HOVERGENi HBG000179.
InParanoidi Q05639.
KOi K03231.
OMAi VACTFES.
OrthoDBi EOG7NKKK3.
PhylomeDBi Q05639.
TreeFami TF300304.

Enzyme and pathway databases

Reactomei REACT_1477. Eukaryotic Translation Elongation.

Miscellaneous databases

EvolutionaryTracei Q05639.
GeneWikii EEF1A2.
GenomeRNAii 1917.
NextBioi 7803.
PROi Q05639.
SOURCEi Search...

Gene expression databases

Bgeei Q05639.
CleanExi HS_EEF1A2.
Genevestigatori Q05639.

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. "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.
    , 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.
    , 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. 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. 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. Cited for: VARIANT SER-70.

Entry informationi

Entry nameiEF1A2_HUMAN
AccessioniPrimary (citable) accession number: Q05639
Secondary accession number(s): B5BUF3
, E1P5J1, P54266, Q0VGC7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: October 29, 2014
This is version 157 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 20
    Human chromosome 20: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3