Full text data of EEF1A2
EEF1A2
(EEF1AL, STN)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Elongation factor 1-alpha 2; EF-1-alpha-2 (Eukaryotic elongation factor 1 A-2; eEF1A-2; Statin-S1)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Elongation factor 1-alpha 2; EF-1-alpha-2 (Eukaryotic elongation factor 1 A-2; eEF1A-2; Statin-S1)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
hRBCD
IPI00014424
IPI00014424 Elongation factor 1-alpha 2 Elongation factor 1-alpha 2 membrane n/a n/a n/a n/a n/a n/a n/a n/a 7 n/a n/a n/a n/a n/a n/a n/a n/a n/a 1 n/a Nucleus n/a expected molecular weight found in band > 188 kDa together with ubiquitin
IPI00014424 Elongation factor 1-alpha 2 Elongation factor 1-alpha 2 membrane n/a n/a n/a n/a n/a n/a n/a n/a 7 n/a n/a n/a n/a n/a n/a n/a n/a n/a 1 n/a Nucleus n/a expected molecular weight found in band > 188 kDa together with ubiquitin
UniProt
Q05639
ID EF1A2_HUMAN Reviewed; 463 AA.
AC Q05639; B5BUF3; E1P5J1; P54266; Q0VGC7;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-JUN-1994, sequence version 1.
DT 22-JAN-2014, entry version 148.
DE RecName: Full=Elongation factor 1-alpha 2;
DE Short=EF-1-alpha-2;
DE AltName: Full=Eukaryotic elongation factor 1 A-2;
DE Short=eEF1A-2;
DE AltName: Full=Statin-S1;
GN Name=EEF1A2; Synonyms=EEF1AL, STN;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8354261; DOI=10.1111/j.1432-1033.1993.tb18064.x;
RA Knudsen S.M., Frydenberg J., Clark B.F.C., Leffers H.;
RT "Tissue-dependent variation in the expression of elongation factor-1
RT alpha isoforms: isolation and characterisation of a cDNA encoding a
RT novel variant of human elongation-factor 1 alpha.";
RL Eur. J. Biochem. 215:549-554(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10950927; DOI=10.1006/geno.2000.6271;
RA Bischoff C., Kahns S., Lund A., Joergensen H.F., Praestegaard M.,
RA Clark B.F.C., Leffers H.;
RT "The human elongation factor 1 A-2 gene (EEF1A2): complete sequence
RT and characterization of gene structure and promoter activity.";
RL Genomics 68:63-70(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=19054851; DOI=10.1038/nmeth.1273;
RA Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R.,
RA Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y.,
RA Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.,
RA Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H.,
RA Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M.,
RA Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T.,
RA Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A.,
RA Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K.,
RA Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S.,
RA Isogai T., Imai J., Watanabe S., Nomura N.;
RT "Human protein factory for converting the transcriptome into an in
RT vitro-expressed proteome.";
RL Nat. Methods 5:1011-1017(2008).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M.,
RA Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J.,
RA Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M.,
RA Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R.,
RA Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M.,
RA Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H.,
RA Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S.,
RA Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E.,
RA Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A.,
RA Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M.,
RA Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A.,
RA Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S.,
RA Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Duodenum, and Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 29-463.
RC TISSUE=Hippocampus;
RX PubMed=7945283; DOI=10.1006/bbrc.1994.2336;
RA Lee S., Ann D.K., Wang E.;
RT "Cloning of human and mouse brain cDNAs coding for S1, the second
RT member of the mammalian elongation factor-1 alpha gene family:
RT analysis of a possible evolutionary pathway.";
RL Biochem. Biophys. Res. Commun. 203:1371-1377(1994).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-179 AND LYS-439, AND MASS
RP SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 343-355 IN COMPLEX WITH
RP HLA-DRA/HLA-DRB3 HETERODIMER.
RX PubMed=18697946; DOI=10.1073/pnas.0805810105;
RA Dai S., Crawford F., Marrack P., Kappler J.W.;
RT "The structure of HLA-DR52c: comparison to other HLA-DRB3 alleles.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:11893-11897(2008).
RN [11]
RP VARIANT SER-70.
RX PubMed=23033978; DOI=10.1056/NEJMoa1206524;
RA de Ligt J., Willemsen M.H., van Bon B.W., Kleefstra T., Yntema H.G.,
RA Kroes T., Vulto-van Silfhout A.T., Koolen D.A., de Vries P.,
RA Gilissen C., del Rosario M., Hoischen A., Scheffer H., de Vries B.B.,
RA Brunner H.G., Veltman J.A., Vissers L.E.;
RT "Diagnostic exome sequencing in persons with severe intellectual
RT disability.";
RL N. Engl. J. Med. 367:1921-1929(2012).
CC -!- FUNCTION: This protein promotes the GTP-dependent binding of
CC aminoacyl-tRNA to the A-site of ribosomes during protein
CC biosynthesis.
CC -!- SUBUNIT: Monomer (By similarity).
CC -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC -!- TISSUE SPECIFICITY: Brain, heart, and skeletal muscle.
CC -!- SIMILARITY: Belongs to the GTP-binding elongation factor family.
CC EF-Tu/EF-1A subfamily.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC and Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/EEF1A2ID40408ch20q13.html";
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DR EMBL; X70940; CAA50280.1; -; mRNA.
DR EMBL; AF163763; AAF80488.1; -; Genomic_DNA.
DR EMBL; AB451389; BAG70203.1; -; mRNA.
DR EMBL; AL121829; CAC15522.1; -; Genomic_DNA.
DR EMBL; CH471077; EAW75260.1; -; Genomic_DNA.
DR EMBL; BC000432; AAH00432.1; -; mRNA.
DR EMBL; BC110409; AAI10410.1; -; mRNA.
DR EMBL; L10340; AAA91835.1; -; mRNA.
DR PIR; S35033; EFHUA2.
DR RefSeq; NP_001949.1; NM_001958.3.
DR UniGene; Hs.433839; -.
DR PDB; 3C5J; X-ray; 1.80 A; C=343-355.
DR PDBsum; 3C5J; -.
DR ProteinModelPortal; Q05639; -.
DR SMR; Q05639; 2-443.
DR IntAct; Q05639; 24.
DR MINT; MINT-1141378; -.
DR STRING; 9606.ENSP00000217182; -.
DR BindingDB; Q05639; -.
DR ChEMBL; CHEMBL1795122; -.
DR PhosphoSite; Q05639; -.
DR DMDM; 544231; -.
DR PaxDb; Q05639; -.
DR PeptideAtlas; Q05639; -.
DR PRIDE; Q05639; -.
DR DNASU; 1917; -.
DR Ensembl; ENST00000217182; ENSP00000217182; ENSG00000101210.
DR Ensembl; ENST00000298049; ENSP00000298049; ENSG00000101210.
DR GeneID; 1917; -.
DR KEGG; hsa:1917; -.
DR UCSC; uc002yfe.2; human.
DR CTD; 1917; -.
DR GeneCards; GC20M062119; -.
DR HGNC; HGNC:3192; EEF1A2.
DR HPA; CAB034019; -.
DR MIM; 602959; gene.
DR neXtProt; NX_Q05639; -.
DR PharmGKB; PA36219; -.
DR eggNOG; COG5256; -.
DR HOGENOM; HOG000229291; -.
DR HOVERGEN; HBG000179; -.
DR InParanoid; Q05639; -.
DR KO; K03231; -.
DR OMA; VACTFES; -.
DR OrthoDB; EOG7NKKK3; -.
DR PhylomeDB; Q05639; -.
DR Reactome; REACT_17015; Metabolism of proteins.
DR Reactome; REACT_71; Gene Expression.
DR EvolutionaryTrace; Q05639; -.
DR GeneWiki; EEF1A2; -.
DR GenomeRNAi; 1917; -.
DR NextBio; 7803; -.
DR PRO; PR:Q05639; -.
DR Bgee; Q05639; -.
DR CleanEx; HS_EEF1A2; -.
DR Genevestigator; Q05639; -.
DR GO; GO:0005853; C:eukaryotic translation elongation factor 1 complex; IEA:Ensembl.
DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
DR GO; GO:0008135; F:translation factor activity, nucleic acid binding; NAS:ProtInc.
DR GO; GO:0006184; P:GTP catabolic process; IEA:GOC.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
DR GO; GO:0010035; P:response to inorganic substance; IEA:Ensembl.
DR InterPro; IPR000795; EF_GTP-bd_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR009000; Transl_B-barrel.
DR InterPro; IPR009001; Transl_elong_EF1A/Init_IF2_C.
DR InterPro; IPR004539; Transl_elong_EF1A_euk/arc.
DR InterPro; IPR004161; Transl_elong_EFTu/EF1A_2.
DR InterPro; IPR004160; Transl_elong_EFTu/EF1A_C.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF03144; GTP_EFTU_D2; 1.
DR Pfam; PF03143; GTP_EFTU_D3; 1.
DR PRINTS; PR00315; ELONGATNFCT.
DR SUPFAM; SSF50447; SSF50447; 1.
DR SUPFAM; SSF50465; SSF50465; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00483; EF-1_alpha; 1.
DR PROSITE; PS00301; EFACTOR_GTP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Complete proteome; Elongation factor;
KW GTP-binding; Methylation; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Polymorphism; Protein biosynthesis; Reference proteome.
FT CHAIN 1 463 Elongation factor 1-alpha 2.
FT /FTId=PRO_0000090891.
FT NP_BIND 14 21 GTP (By similarity).
FT NP_BIND 91 95 GTP (By similarity).
FT NP_BIND 153 156 GTP (By similarity).
FT MOD_RES 55 55 N6,N6,N6-trimethyllysine (By similarity).
FT MOD_RES 165 165 N6,N6,N6-trimethyllysine (By similarity).
FT MOD_RES 179 179 N6-acetyllysine.
FT MOD_RES 301 301 5-glutamyl glycerylphosphorylethanolamine
FT (By similarity).
FT MOD_RES 374 374 5-glutamyl glycerylphosphorylethanolamine
FT (By similarity).
FT MOD_RES 439 439 N6-acetyllysine.
FT VARIANT 70 70 G -> S (found in a patient with mental
FT retardation, severe delay of psychomotor
FT development, very limited speech,
FT autistic features and aggressive
FT behaviors).
FT /FTId=VAR_069395.
FT CONFLICT 427 427 R -> P (in Ref. 7; AAA91835).
SQ SEQUENCE 463 AA; 50470 MW; 31E4E341CEE797EC 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 SDPPQEAAQF TSQVIILNHP GQISAGYSPV
IDCHTAHIAC KFAELKEKID RRSGKKLEDN PKSLKSGDAA IVEMVPGKPM CVESFSQYPP
LGRFAVRDMR QTVAVGVIKN VEKKSGGAGK VTKSAQKAQK AGK
//
ID EF1A2_HUMAN Reviewed; 463 AA.
AC Q05639; B5BUF3; E1P5J1; P54266; Q0VGC7;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-JUN-1994, sequence version 1.
DT 22-JAN-2014, entry version 148.
DE RecName: Full=Elongation factor 1-alpha 2;
DE Short=EF-1-alpha-2;
DE AltName: Full=Eukaryotic elongation factor 1 A-2;
DE Short=eEF1A-2;
DE AltName: Full=Statin-S1;
GN Name=EEF1A2; Synonyms=EEF1AL, STN;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8354261; DOI=10.1111/j.1432-1033.1993.tb18064.x;
RA Knudsen S.M., Frydenberg J., Clark B.F.C., Leffers H.;
RT "Tissue-dependent variation in the expression of elongation factor-1
RT alpha isoforms: isolation and characterisation of a cDNA encoding a
RT novel variant of human elongation-factor 1 alpha.";
RL Eur. J. Biochem. 215:549-554(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10950927; DOI=10.1006/geno.2000.6271;
RA Bischoff C., Kahns S., Lund A., Joergensen H.F., Praestegaard M.,
RA Clark B.F.C., Leffers H.;
RT "The human elongation factor 1 A-2 gene (EEF1A2): complete sequence
RT and characterization of gene structure and promoter activity.";
RL Genomics 68:63-70(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=19054851; DOI=10.1038/nmeth.1273;
RA Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R.,
RA Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y.,
RA Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.,
RA Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H.,
RA Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M.,
RA Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T.,
RA Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A.,
RA Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K.,
RA Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S.,
RA Isogai T., Imai J., Watanabe S., Nomura N.;
RT "Human protein factory for converting the transcriptome into an in
RT vitro-expressed proteome.";
RL Nat. Methods 5:1011-1017(2008).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M.,
RA Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J.,
RA Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M.,
RA Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R.,
RA Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M.,
RA Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H.,
RA Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S.,
RA Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E.,
RA Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A.,
RA Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M.,
RA Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A.,
RA Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S.,
RA Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Duodenum, and Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 29-463.
RC TISSUE=Hippocampus;
RX PubMed=7945283; DOI=10.1006/bbrc.1994.2336;
RA Lee S., Ann D.K., Wang E.;
RT "Cloning of human and mouse brain cDNAs coding for S1, the second
RT member of the mammalian elongation factor-1 alpha gene family:
RT analysis of a possible evolutionary pathway.";
RL Biochem. Biophys. Res. Commun. 203:1371-1377(1994).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-179 AND LYS-439, AND MASS
RP SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 343-355 IN COMPLEX WITH
RP HLA-DRA/HLA-DRB3 HETERODIMER.
RX PubMed=18697946; DOI=10.1073/pnas.0805810105;
RA Dai S., Crawford F., Marrack P., Kappler J.W.;
RT "The structure of HLA-DR52c: comparison to other HLA-DRB3 alleles.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:11893-11897(2008).
RN [11]
RP VARIANT SER-70.
RX PubMed=23033978; DOI=10.1056/NEJMoa1206524;
RA de Ligt J., Willemsen M.H., van Bon B.W., Kleefstra T., Yntema H.G.,
RA Kroes T., Vulto-van Silfhout A.T., Koolen D.A., de Vries P.,
RA Gilissen C., del Rosario M., Hoischen A., Scheffer H., de Vries B.B.,
RA Brunner H.G., Veltman J.A., Vissers L.E.;
RT "Diagnostic exome sequencing in persons with severe intellectual
RT disability.";
RL N. Engl. J. Med. 367:1921-1929(2012).
CC -!- FUNCTION: This protein promotes the GTP-dependent binding of
CC aminoacyl-tRNA to the A-site of ribosomes during protein
CC biosynthesis.
CC -!- SUBUNIT: Monomer (By similarity).
CC -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC -!- TISSUE SPECIFICITY: Brain, heart, and skeletal muscle.
CC -!- SIMILARITY: Belongs to the GTP-binding elongation factor family.
CC EF-Tu/EF-1A subfamily.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC and Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/EEF1A2ID40408ch20q13.html";
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
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DR EMBL; X70940; CAA50280.1; -; mRNA.
DR EMBL; AF163763; AAF80488.1; -; Genomic_DNA.
DR EMBL; AB451389; BAG70203.1; -; mRNA.
DR EMBL; AL121829; CAC15522.1; -; Genomic_DNA.
DR EMBL; CH471077; EAW75260.1; -; Genomic_DNA.
DR EMBL; BC000432; AAH00432.1; -; mRNA.
DR EMBL; BC110409; AAI10410.1; -; mRNA.
DR EMBL; L10340; AAA91835.1; -; mRNA.
DR PIR; S35033; EFHUA2.
DR RefSeq; NP_001949.1; NM_001958.3.
DR UniGene; Hs.433839; -.
DR PDB; 3C5J; X-ray; 1.80 A; C=343-355.
DR PDBsum; 3C5J; -.
DR ProteinModelPortal; Q05639; -.
DR SMR; Q05639; 2-443.
DR IntAct; Q05639; 24.
DR MINT; MINT-1141378; -.
DR STRING; 9606.ENSP00000217182; -.
DR BindingDB; Q05639; -.
DR ChEMBL; CHEMBL1795122; -.
DR PhosphoSite; Q05639; -.
DR DMDM; 544231; -.
DR PaxDb; Q05639; -.
DR PeptideAtlas; Q05639; -.
DR PRIDE; Q05639; -.
DR DNASU; 1917; -.
DR Ensembl; ENST00000217182; ENSP00000217182; ENSG00000101210.
DR Ensembl; ENST00000298049; ENSP00000298049; ENSG00000101210.
DR GeneID; 1917; -.
DR KEGG; hsa:1917; -.
DR UCSC; uc002yfe.2; human.
DR CTD; 1917; -.
DR GeneCards; GC20M062119; -.
DR HGNC; HGNC:3192; EEF1A2.
DR HPA; CAB034019; -.
DR MIM; 602959; gene.
DR neXtProt; NX_Q05639; -.
DR PharmGKB; PA36219; -.
DR eggNOG; COG5256; -.
DR HOGENOM; HOG000229291; -.
DR HOVERGEN; HBG000179; -.
DR InParanoid; Q05639; -.
DR KO; K03231; -.
DR OMA; VACTFES; -.
DR OrthoDB; EOG7NKKK3; -.
DR PhylomeDB; Q05639; -.
DR Reactome; REACT_17015; Metabolism of proteins.
DR Reactome; REACT_71; Gene Expression.
DR EvolutionaryTrace; Q05639; -.
DR GeneWiki; EEF1A2; -.
DR GenomeRNAi; 1917; -.
DR NextBio; 7803; -.
DR PRO; PR:Q05639; -.
DR Bgee; Q05639; -.
DR CleanEx; HS_EEF1A2; -.
DR Genevestigator; Q05639; -.
DR GO; GO:0005853; C:eukaryotic translation elongation factor 1 complex; IEA:Ensembl.
DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
DR GO; GO:0008135; F:translation factor activity, nucleic acid binding; NAS:ProtInc.
DR GO; GO:0006184; P:GTP catabolic process; IEA:GOC.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
DR GO; GO:0010035; P:response to inorganic substance; IEA:Ensembl.
DR InterPro; IPR000795; EF_GTP-bd_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR009000; Transl_B-barrel.
DR InterPro; IPR009001; Transl_elong_EF1A/Init_IF2_C.
DR InterPro; IPR004539; Transl_elong_EF1A_euk/arc.
DR InterPro; IPR004161; Transl_elong_EFTu/EF1A_2.
DR InterPro; IPR004160; Transl_elong_EFTu/EF1A_C.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF03144; GTP_EFTU_D2; 1.
DR Pfam; PF03143; GTP_EFTU_D3; 1.
DR PRINTS; PR00315; ELONGATNFCT.
DR SUPFAM; SSF50447; SSF50447; 1.
DR SUPFAM; SSF50465; SSF50465; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00483; EF-1_alpha; 1.
DR PROSITE; PS00301; EFACTOR_GTP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Complete proteome; Elongation factor;
KW GTP-binding; Methylation; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Polymorphism; Protein biosynthesis; Reference proteome.
FT CHAIN 1 463 Elongation factor 1-alpha 2.
FT /FTId=PRO_0000090891.
FT NP_BIND 14 21 GTP (By similarity).
FT NP_BIND 91 95 GTP (By similarity).
FT NP_BIND 153 156 GTP (By similarity).
FT MOD_RES 55 55 N6,N6,N6-trimethyllysine (By similarity).
FT MOD_RES 165 165 N6,N6,N6-trimethyllysine (By similarity).
FT MOD_RES 179 179 N6-acetyllysine.
FT MOD_RES 301 301 5-glutamyl glycerylphosphorylethanolamine
FT (By similarity).
FT MOD_RES 374 374 5-glutamyl glycerylphosphorylethanolamine
FT (By similarity).
FT MOD_RES 439 439 N6-acetyllysine.
FT VARIANT 70 70 G -> S (found in a patient with mental
FT retardation, severe delay of psychomotor
FT development, very limited speech,
FT autistic features and aggressive
FT behaviors).
FT /FTId=VAR_069395.
FT CONFLICT 427 427 R -> P (in Ref. 7; AAA91835).
SQ SEQUENCE 463 AA; 50470 MW; 31E4E341CEE797EC 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 SDPPQEAAQF TSQVIILNHP GQISAGYSPV
IDCHTAHIAC KFAELKEKID RRSGKKLEDN PKSLKSGDAA IVEMVPGKPM CVESFSQYPP
LGRFAVRDMR QTVAVGVIKN VEKKSGGAGK VTKSAQKAQK AGK
//
MIM
602959
*RECORD*
*FIELD* NO
602959
*FIELD* TI
*602959 EUKARYOTIC TRANSLATION ELONGATION FACTOR 1, ALPHA-2; EEF1A2
;;ELONGATION FACTOR 1, ALPHA-2
read more*FIELD* TX
The autosomal recessive mutation 'wasted' (wst) arose spontaneously in
an inbred mouse colony at the Jackson laboratory in 1972 (Shultz et al.,
1982). Homozygous wst/wst mice have neurologic defects, waste away, and
show immune system abnormalities that include a defective response to
DNA damage in lymphoid cells. Homozygous mice appear completely normal
until weaning; at approximately 21 days, they develop tremors and
ataxia. Histologic examination shows extensive neuronal vacuolar
degeneration of anterior horn cells of the spinal cord with less severe
abnormalities of motor nuclei in the brainstem. The mice then lose
weight (presumably through muscle wasting), develop progressive
paralysis, and die by approximately 28 days of age. The time course of
the disease progression varies little, regardless of genetic background,
weaning time, or environmental factors such as specific pathogen-free
conditions. During the postweaning period, wst/wst mice also develop
progressive atrophy of the spleen and thymus and a concomitant decrease
in circulating lymphocytes. Cells derived from lymphoid tissues of
wasted mice from 26 days onward show a defective response to
radiation-induced DNA damage, which is reminiscent of a checkpoint
defect; however, this defect is not seen in fibroblasts nor is it seen
in lymphoid-derived cells of mice at 22 days.
The wst gene maps within the most distal group of markers on chromosome
2. Chambers et al. (1998) used a positional cloning/positional candidate
approach to isolate the wst gene. Because those genes that map close to
wst on chromosome 2 are located on distal human 20q, genes that map to
20q13 in the human were considered as a source of new markers and/or
candidate genes. One such gene encodes a protein that displays a high
level of homology (92% identity and 98% similarity at the amino acid
level) to the translation elongation factor EF1-alpha (EEF1A1; 130590)
and is called EF1-alpha-2 or S1 (EEF1A2); see Ann et al. (1991) and Lund
et al. (1996). EF1-alpha is distributed widely, although expression is
very low or undetectable in skeletal and cardiac muscle postnatally, and
expression in the brain declines between embryonic life and adulthood in
rats. EF1-alpha-2 is found exclusively in terminally differentiated
cells of skeletal muscle, heart, and certain areas of the brain. In
those tissues where both genes are expressed, Eef1a2 is consistently
more highly expressed than Eef1a. In rat muscle and heart, EF1-alpha
levels declined by 95% within the first month of postnatal life;
EF1-alpha-2 levels, on the other hand, increased during this period and
are constant through adult life. There appears, therefore, to be some
degree of reciprocal expression of the 2 genes. Although fibroblasts
normally do not express Eef1a2, the mouse 3T3 fibroblast cell line does,
and this line was used to study regulation of Eef1a2 at different stages
of the cell cycle. It was found that the gene was highly expressed when
cells were serum-starved, in G0 phase, but expression declined
dramatically when cells were serum stimulated and reentered the cell
cycle. Eef1a, however, was expressed at all stages of the cell cycle in
this cell line (Ann et al., 1991). Whereas EEF1A2 appears to be a
single-copy gene, numerous pseudogenes for EEF1A1 exist in the human
genome (Lund et al., 1996).
By screening a genomic DNA library with probes derived from the 5-prime
and 3-prime untranslated regions (UTRs) of EEF1A2, followed by PCR
amplification, Bischoff et al. (2000) isolated the complete sequence of
the EEF1A2 gene. The gene spans 12 kb, including a 2-kb upstream
promoter region, and, like EEF1A1, it contains 8 exons. Although the
coding regions of the EEF1A genes are highly similar, the introns, UTRs,
and promoter regions are highly divergent. Primer extension analysis
localized the start site to an adenine 166 bp upstream of the initiator
codon in exon 1. Sequence analysis revealed no TATA box but did identify
a CpG island, 12 E boxes, 3 EGR-type binding sites, a GATA motif, and a
MEF2 (see 600660)-binding site. Transient transfection analysis mapped
the core promoter to a region spanning positions -16 to +92.
Chambers et al. (1998) showed that the wasted mutation is a deletion
spanning 15.8 kb that removes the promoter region and first noncoding
exon of the mouse Eef1a2 gene, abolishing transcription of the gene. No
other gene was detected within the deleted region. Expression of Eef1a2
was reciprocal with that of Eef1a. Expression of Eef1a2 takes over from
Eef1a in heart and muscle at precisely the time at which the wasted
phenotype becomes manifest. The findings suggested that there are
tissue-specific forms of the translation elongation apparatus essential
for postnatal survival in the mouse.
Anand et al. (2002) found that the EEF1A2 gene is amplified in 25% of
primary ovarian tumors and is highly expressed in approximately 30% of
ovarian tumors and established cell lines. They also demonstrated that
the EEF1A2 protein has oncogenic properties: it enhances focus
formation, allows anchorage-independent growth, and decreases the
doubling time of rodent fibroblasts. In addition, EEF1A2 expression made
NIH 3T3 fibroblasts tumorigenic and increased the growth rate of ovarian
carcinoma cells xenografted in nude mice. Thus, EEF1A2 and the process
of protein elongation are likely to be critical in the development of
ovarian cancer.
*FIELD* RF
1. Anand, N.; Murthy, S.; Amann, G.; Wernick, M.; Porter, L. A.; Cukier,
I. H.; Collins, C.; Gray, J. W.; Diebold, J.; Demetrick, D. J.; Lee,
J. M.: Protein elongation factor EEF1A2 is a putative oncogene in
ovarian cancer. Nature Genet. 31: 301-305, 2002.
2. Ann, D. K.; Moutsatsos, I. K.; Nakamura, T.; Lin, H. H.; Mao, P.-L.;
Lee, M.-J.; Chin, S.; Liem, R. K. H.; Wang, E.: Isolation and characterization
of the rat chromosomal gene for a polypeptide (p21) antigenically
related to statin. J. Biol. Chem. 266: 10429-10437, 1991.
3. Bischoff, C.; Kahns, S.; Lund, A.; Jorgensen, H. F.; Praestegaard,
M.; Clark, B. F. C.; Leffers, H.: The human elongation factor 1 A-2
gene (EEF1A2): complete sequence and characterization of gene structure
and promoter activity. Genomics 68: 63-70, 2000.
4. Chambers, D. M.; Peters, J.; Abbott, C. M.: The lethal mutation
of the mouse wasted (wst) is a deletion that abolishes expression
of a tissue-specific isoform of translation elongation factor 1-alpha,
encoded by the Eef1a2 gene. Proc. Nat. Acad. Sci. 95: 4463-4468,
1998.
5. Lund, A.; Knudsen, S. M.; Vissing, H.; Clark, B.; Tommerup, N.
: Assignment of human elongation factor 1-alpha genes: EEF1A maps
to chromosome 6q14 and EEF1A2 to 20q13.3. Genomics 36: 359-361,
1996.
6. Shultz, L. D.; Sweet, H. O.; Davisson, M. T.; Coman, D. R.: 'Wasted,'
a new mutant of the mouse with abnormalities characteristic of ataxia
telangiectasia. Nature 297: 402-404, 1982.
*FIELD* CN
Victor A. McKusick - updated: 6/10/2002
Paul J. Converse - updated: 12/4/2000
*FIELD* CD
Victor A. McKusick: 8/11/1998
*FIELD* ED
terry: 03/03/2005
alopez: 7/25/2002
terry: 6/10/2002
mgross: 12/4/2000
terry: 12/4/2000
dkim: 12/15/1998
carol: 8/11/1998
*RECORD*
*FIELD* NO
602959
*FIELD* TI
*602959 EUKARYOTIC TRANSLATION ELONGATION FACTOR 1, ALPHA-2; EEF1A2
;;ELONGATION FACTOR 1, ALPHA-2
read more*FIELD* TX
The autosomal recessive mutation 'wasted' (wst) arose spontaneously in
an inbred mouse colony at the Jackson laboratory in 1972 (Shultz et al.,
1982). Homozygous wst/wst mice have neurologic defects, waste away, and
show immune system abnormalities that include a defective response to
DNA damage in lymphoid cells. Homozygous mice appear completely normal
until weaning; at approximately 21 days, they develop tremors and
ataxia. Histologic examination shows extensive neuronal vacuolar
degeneration of anterior horn cells of the spinal cord with less severe
abnormalities of motor nuclei in the brainstem. The mice then lose
weight (presumably through muscle wasting), develop progressive
paralysis, and die by approximately 28 days of age. The time course of
the disease progression varies little, regardless of genetic background,
weaning time, or environmental factors such as specific pathogen-free
conditions. During the postweaning period, wst/wst mice also develop
progressive atrophy of the spleen and thymus and a concomitant decrease
in circulating lymphocytes. Cells derived from lymphoid tissues of
wasted mice from 26 days onward show a defective response to
radiation-induced DNA damage, which is reminiscent of a checkpoint
defect; however, this defect is not seen in fibroblasts nor is it seen
in lymphoid-derived cells of mice at 22 days.
The wst gene maps within the most distal group of markers on chromosome
2. Chambers et al. (1998) used a positional cloning/positional candidate
approach to isolate the wst gene. Because those genes that map close to
wst on chromosome 2 are located on distal human 20q, genes that map to
20q13 in the human were considered as a source of new markers and/or
candidate genes. One such gene encodes a protein that displays a high
level of homology (92% identity and 98% similarity at the amino acid
level) to the translation elongation factor EF1-alpha (EEF1A1; 130590)
and is called EF1-alpha-2 or S1 (EEF1A2); see Ann et al. (1991) and Lund
et al. (1996). EF1-alpha is distributed widely, although expression is
very low or undetectable in skeletal and cardiac muscle postnatally, and
expression in the brain declines between embryonic life and adulthood in
rats. EF1-alpha-2 is found exclusively in terminally differentiated
cells of skeletal muscle, heart, and certain areas of the brain. In
those tissues where both genes are expressed, Eef1a2 is consistently
more highly expressed than Eef1a. In rat muscle and heart, EF1-alpha
levels declined by 95% within the first month of postnatal life;
EF1-alpha-2 levels, on the other hand, increased during this period and
are constant through adult life. There appears, therefore, to be some
degree of reciprocal expression of the 2 genes. Although fibroblasts
normally do not express Eef1a2, the mouse 3T3 fibroblast cell line does,
and this line was used to study regulation of Eef1a2 at different stages
of the cell cycle. It was found that the gene was highly expressed when
cells were serum-starved, in G0 phase, but expression declined
dramatically when cells were serum stimulated and reentered the cell
cycle. Eef1a, however, was expressed at all stages of the cell cycle in
this cell line (Ann et al., 1991). Whereas EEF1A2 appears to be a
single-copy gene, numerous pseudogenes for EEF1A1 exist in the human
genome (Lund et al., 1996).
By screening a genomic DNA library with probes derived from the 5-prime
and 3-prime untranslated regions (UTRs) of EEF1A2, followed by PCR
amplification, Bischoff et al. (2000) isolated the complete sequence of
the EEF1A2 gene. The gene spans 12 kb, including a 2-kb upstream
promoter region, and, like EEF1A1, it contains 8 exons. Although the
coding regions of the EEF1A genes are highly similar, the introns, UTRs,
and promoter regions are highly divergent. Primer extension analysis
localized the start site to an adenine 166 bp upstream of the initiator
codon in exon 1. Sequence analysis revealed no TATA box but did identify
a CpG island, 12 E boxes, 3 EGR-type binding sites, a GATA motif, and a
MEF2 (see 600660)-binding site. Transient transfection analysis mapped
the core promoter to a region spanning positions -16 to +92.
Chambers et al. (1998) showed that the wasted mutation is a deletion
spanning 15.8 kb that removes the promoter region and first noncoding
exon of the mouse Eef1a2 gene, abolishing transcription of the gene. No
other gene was detected within the deleted region. Expression of Eef1a2
was reciprocal with that of Eef1a. Expression of Eef1a2 takes over from
Eef1a in heart and muscle at precisely the time at which the wasted
phenotype becomes manifest. The findings suggested that there are
tissue-specific forms of the translation elongation apparatus essential
for postnatal survival in the mouse.
Anand et al. (2002) found that the EEF1A2 gene is amplified in 25% of
primary ovarian tumors and is highly expressed in approximately 30% of
ovarian tumors and established cell lines. They also demonstrated that
the EEF1A2 protein has oncogenic properties: it enhances focus
formation, allows anchorage-independent growth, and decreases the
doubling time of rodent fibroblasts. In addition, EEF1A2 expression made
NIH 3T3 fibroblasts tumorigenic and increased the growth rate of ovarian
carcinoma cells xenografted in nude mice. Thus, EEF1A2 and the process
of protein elongation are likely to be critical in the development of
ovarian cancer.
*FIELD* RF
1. Anand, N.; Murthy, S.; Amann, G.; Wernick, M.; Porter, L. A.; Cukier,
I. H.; Collins, C.; Gray, J. W.; Diebold, J.; Demetrick, D. J.; Lee,
J. M.: Protein elongation factor EEF1A2 is a putative oncogene in
ovarian cancer. Nature Genet. 31: 301-305, 2002.
2. Ann, D. K.; Moutsatsos, I. K.; Nakamura, T.; Lin, H. H.; Mao, P.-L.;
Lee, M.-J.; Chin, S.; Liem, R. K. H.; Wang, E.: Isolation and characterization
of the rat chromosomal gene for a polypeptide (p21) antigenically
related to statin. J. Biol. Chem. 266: 10429-10437, 1991.
3. Bischoff, C.; Kahns, S.; Lund, A.; Jorgensen, H. F.; Praestegaard,
M.; Clark, B. F. C.; Leffers, H.: The human elongation factor 1 A-2
gene (EEF1A2): complete sequence and characterization of gene structure
and promoter activity. Genomics 68: 63-70, 2000.
4. Chambers, D. M.; Peters, J.; Abbott, C. M.: The lethal mutation
of the mouse wasted (wst) is a deletion that abolishes expression
of a tissue-specific isoform of translation elongation factor 1-alpha,
encoded by the Eef1a2 gene. Proc. Nat. Acad. Sci. 95: 4463-4468,
1998.
5. Lund, A.; Knudsen, S. M.; Vissing, H.; Clark, B.; Tommerup, N.
: Assignment of human elongation factor 1-alpha genes: EEF1A maps
to chromosome 6q14 and EEF1A2 to 20q13.3. Genomics 36: 359-361,
1996.
6. Shultz, L. D.; Sweet, H. O.; Davisson, M. T.; Coman, D. R.: 'Wasted,'
a new mutant of the mouse with abnormalities characteristic of ataxia
telangiectasia. Nature 297: 402-404, 1982.
*FIELD* CN
Victor A. McKusick - updated: 6/10/2002
Paul J. Converse - updated: 12/4/2000
*FIELD* CD
Victor A. McKusick: 8/11/1998
*FIELD* ED
terry: 03/03/2005
alopez: 7/25/2002
terry: 6/10/2002
mgross: 12/4/2000
terry: 12/4/2000
dkim: 12/15/1998
carol: 8/11/1998