Full text data of EEF1E1
EEF1E1
(AIMP3, P18)
[Confidence: low (only semi-automatic identification from reviews)]
Eukaryotic translation elongation factor 1 epsilon-1 (Aminoacyl tRNA synthetase complex-interacting multifunctional protein 3; Elongation factor p18; Multisynthase complex auxiliary component p18)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Eukaryotic translation elongation factor 1 epsilon-1 (Aminoacyl tRNA synthetase complex-interacting multifunctional protein 3; Elongation factor p18; Multisynthase complex auxiliary component p18)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
O43324
ID MCA3_HUMAN Reviewed; 174 AA.
AC O43324; C9JLK5; Q5THS2;
DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-JUN-1998, sequence version 1.
DT 22-JAN-2014, entry version 124.
DE RecName: Full=Eukaryotic translation elongation factor 1 epsilon-1;
DE AltName: Full=Aminoacyl tRNA synthetase complex-interacting multifunctional protein 3;
DE AltName: Full=Elongation factor p18;
DE AltName: Full=Multisynthase complex auxiliary component p18;
GN Name=EEF1E1; Synonyms=AIMP3, P18;
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] (ISOFORM 1).
RC TISSUE=Testis;
RA Motegi H., Noda T., Shiba K.;
RT "Cloning of cDNA for human p18 from human testis.";
RL Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Umbilical cord blood;
RX PubMed=9653160; DOI=10.1073/pnas.95.14.8175;
RA Mao M., Fu G., Wu J.-S., Zhang Q.-H., Zhou J., Kan L.-X., Huang Q.-H.,
RA He K.-L., Gu B.-W., Han Z.-G., Shen Y., Gu J., Yu Y.-P., Xu S.-H.,
RA Wang Y.-X., Chen S.-J., Chen Z.;
RT "Identification of genes expressed in human CD34(+) hematopoietic
RT stem/progenitor cells by expressed sequence tags and efficient full-
RT length cDNA cloning.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:8175-8180(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
RA Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
RA Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain cortex, and Urinary bladder;
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 [6]
RP PROTEIN SEQUENCE OF 2-12 AND 79-88, CLEAVAGE OF INITIATOR METHIONINE,
RP ACETYLATION AT ALA-2, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma, and Ovarian carcinoma;
RA Bienvenut W.V., Calvo F., Lilla S., von Kriegsheim A., Lempens A.,
RA Kolch W.;
RL Submitted (DEC-2008) to UniProtKB.
RN [7]
RP INTERACTION WITH ATM, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=15680327; DOI=10.1016/j.cell.2004.11.054;
RA Park B.-J., Kang J.W., Lee S.W., Choi S.-J., Shin Y.K., Ahn Y.H.,
RA Choi Y.H., Choi D., Lee K.S., Kim S.;
RT "The haploinsufficient tumor suppressor p18 upregulates p53 via
RT interactions with ATM/ATR.";
RL Cell 120:209-221(2005).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-138, AND MASS 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 (2.0 ANGSTROMS), DOMAIN ARCHITECTURE, AND
RP COILED-COIL DOMAIN.
RX PubMed=18343821; DOI=10.1074/jbc.M800859200;
RA Kim K.J., Park M.C., Choi S.J., Oh Y.S., Choi E.C., Cho H.J.,
RA Kim M.H., Kim S.H., Kim D.W., Kim S., Kang B.S.;
RT "Determination of three-dimensional structure and residues of the
RT novel tumor suppressor AIMP3/p18 required for the interaction with
RT ATM.";
RL J. Biol. Chem. 283:14032-14040(2008).
CC -!- FUNCTION: Positive modulator of ATM response to DNA damage.
CC -!- SUBUNIT: Component of the multisynthase complex which is comprised
CC of a bifunctional glutamyl-prolyl-tRNA synthase, the monospecific
CC isoleucyl, leucyl, glutaminyl, methionyl, lysyl, arginyl and
CC aspartyl-tRNA synthases, and three auxiliary proteins, EEF1E1/p18,
CC AIMP2/p38 and AIMP1/p43. Interacts with ATM and ATR. The
CC interaction with ATM, which takes place independently of TP53, is
CC induced by DNA damage that may occur during genotoxic stress or
CC cell growth. The interaction with ATR is enhanced by UV
CC irradiation.
CC -!- INTERACTION:
CC P04591:gag (xeno); NbExp=4; IntAct=EBI-1048486, EBI-6179719;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Cytoplasmic under
CC growth arrest conditions. Translocated into the nucleus when
CC growth resumes (S phase) and following DNA damage.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O43324-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O43324-2; Sequence=VSP_045088;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Down-regulated in various cancer tissues.
CC -!- INDUCTION: By DNA damaging agents such as UV, adriamycin,
CC actinomycin-D and cisplatin.
CC -!- SIMILARITY: Contains 1 GST C-terminal domain.
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DR EMBL; AB011079; BAA24926.1; -; mRNA.
DR EMBL; AF054186; AAC39916.1; -; mRNA.
DR EMBL; BT007306; AAP35970.1; -; mRNA.
DR EMBL; AL355499; CAH72539.1; -; Genomic_DNA.
DR EMBL; AL023694; CAH72539.1; JOINED; Genomic_DNA.
DR EMBL; AL451187; CAH72539.1; JOINED; Genomic_DNA.
DR EMBL; AL023694; CAI21644.1; -; Genomic_DNA.
DR EMBL; AL355499; CAI21644.1; JOINED; Genomic_DNA.
DR EMBL; AL451187; CAI21644.1; JOINED; Genomic_DNA.
DR EMBL; AL451187; CAI14747.1; -; Genomic_DNA.
DR EMBL; AL023694; CAI14747.1; JOINED; Genomic_DNA.
DR EMBL; AL355499; CAI14747.1; JOINED; Genomic_DNA.
DR EMBL; BC005291; AAH05291.1; -; mRNA.
DR EMBL; CK002875; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; NP_001129122.1; NM_001135650.1.
DR RefSeq; NP_004271.1; NM_004280.4.
DR UniGene; Hs.602353; -.
DR UniGene; Hs.745033; -.
DR PDB; 2UZ8; X-ray; 2.00 A; A/B=1-174.
DR PDB; 4BJV; X-ray; 1.99 A; B=1-174.
DR PDB; 4BJW; X-ray; 1.60 A; B=1-169.
DR PDBsum; 2UZ8; -.
DR PDBsum; 4BJV; -.
DR PDBsum; 4BJW; -.
DR ProteinModelPortal; O43324; -.
DR SMR; O43324; 1-169.
DR IntAct; O43324; 3.
DR STRING; 9606.ENSP00000369038; -.
DR PhosphoSite; O43324; -.
DR PaxDb; O43324; -.
DR PeptideAtlas; O43324; -.
DR PRIDE; O43324; -.
DR DNASU; 9521; -.
DR Ensembl; ENST00000379715; ENSP00000369038; ENSG00000124802.
DR Ensembl; ENST00000429723; ENSP00000414363; ENSG00000124802.
DR GeneID; 9521; -.
DR KEGG; hsa:9521; -.
DR UCSC; uc011dic.2; human.
DR CTD; 9521; -.
DR GeneCards; GC06M008024; -.
DR HGNC; HGNC:3212; EEF1E1.
DR HPA; HPA027901; -.
DR MIM; 609206; gene.
DR neXtProt; NX_O43324; -.
DR PharmGKB; PA27648; -.
DR eggNOG; NOG257622; -.
DR HOGENOM; HOG000026786; -.
DR HOVERGEN; HBG003019; -.
DR InParanoid; O43324; -.
DR KO; K15439; -.
DR OMA; AVVQQWL; -.
DR OrthoDB; EOG7GQXX4; -.
DR PhylomeDB; O43324; -.
DR Reactome; REACT_71; Gene Expression.
DR SignaLink; O43324; -.
DR ChiTaRS; EEF1E1; human.
DR EvolutionaryTrace; O43324; -.
DR GeneWiki; EEF1E1; -.
DR GenomeRNAi; 9521; -.
DR NextBio; 35684; -.
DR PRO; PR:O43324; -.
DR ArrayExpress; O43324; -.
DR Bgee; O43324; -.
DR CleanEx; HS_EEF1E1; -.
DR Genevestigator; O43324; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0008285; P:negative regulation of cell proliferation; ISS:UniProtKB.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0043517; P:positive regulation of DNA damage response, signal transduction by p53 class mediator; ISS:UniProtKB.
DR GO; GO:0006418; P:tRNA aminoacylation for protein translation; TAS:Reactome.
DR Gene3D; 1.20.1050.10; -; 1.
DR InterPro; IPR010987; Glutathione-S-Trfase_C-like.
DR SUPFAM; SSF47616; SSF47616; 1.
DR PROSITE; PS50405; GST_CTER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Coiled coil;
KW Complete proteome; Cytoplasm; Direct protein sequencing; Nucleus;
KW Protein biosynthesis; Reference proteome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 174 Eukaryotic translation elongation factor
FT 1 epsilon-1.
FT /FTId=PRO_0000221132.
FT DOMAIN 50 173 GST C-terminal.
FT REGION 2 56 N-terminal.
FT REGION 57 63 Linker.
FT REGION 64 152 C-terminal.
FT COILED 153 169
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 138 138 N6-acetyllysine.
FT VAR_SEQ 129 174 VDLTVQEKEKYLNVSRWFCHIQHYPGIRQHLSSVVFIKNRL
FT YTNSH -> IRKLRHTEVGN (in isoform 2).
FT /FTId=VSP_045088.
FT HELIX 2 13
FT STRAND 23 25
FT TURN 26 29
FT STRAND 30 34
FT STRAND 40 43
FT HELIX 44 54
FT HELIX 58 61
FT HELIX 65 81
FT HELIX 90 101
FT HELIX 102 104
FT STRAND 110 112
FT HELIX 115 128
FT HELIX 133 138
FT HELIX 140 151
FT TURN 153 155
SQ SEQUENCE 174 AA; 19811 MW; 58AAE4BD9E1684E2 CRC64;
MAAAAELSLL EKSLGLSKGN KYSAQGERQI PVLQTNNGPS LTGLTTIAAH LVKQANKEYL
LGSTAEEKAI VQQWLEYRVT QVDGHSSKND IHTLLKDLNS YLEDKVYLTG YNFTLADILL
YYGLHRFIVD LTVQEKEKYL NVSRWFCHIQ HYPGIRQHLS SVVFIKNRLY TNSH
//
ID MCA3_HUMAN Reviewed; 174 AA.
AC O43324; C9JLK5; Q5THS2;
DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-JUN-1998, sequence version 1.
DT 22-JAN-2014, entry version 124.
DE RecName: Full=Eukaryotic translation elongation factor 1 epsilon-1;
DE AltName: Full=Aminoacyl tRNA synthetase complex-interacting multifunctional protein 3;
DE AltName: Full=Elongation factor p18;
DE AltName: Full=Multisynthase complex auxiliary component p18;
GN Name=EEF1E1; Synonyms=AIMP3, P18;
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] (ISOFORM 1).
RC TISSUE=Testis;
RA Motegi H., Noda T., Shiba K.;
RT "Cloning of cDNA for human p18 from human testis.";
RL Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Umbilical cord blood;
RX PubMed=9653160; DOI=10.1073/pnas.95.14.8175;
RA Mao M., Fu G., Wu J.-S., Zhang Q.-H., Zhou J., Kan L.-X., Huang Q.-H.,
RA He K.-L., Gu B.-W., Han Z.-G., Shen Y., Gu J., Yu Y.-P., Xu S.-H.,
RA Wang Y.-X., Chen S.-J., Chen Z.;
RT "Identification of genes expressed in human CD34(+) hematopoietic
RT stem/progenitor cells by expressed sequence tags and efficient full-
RT length cDNA cloning.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:8175-8180(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
RA Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
RA Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain cortex, and Urinary bladder;
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 [6]
RP PROTEIN SEQUENCE OF 2-12 AND 79-88, CLEAVAGE OF INITIATOR METHIONINE,
RP ACETYLATION AT ALA-2, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma, and Ovarian carcinoma;
RA Bienvenut W.V., Calvo F., Lilla S., von Kriegsheim A., Lempens A.,
RA Kolch W.;
RL Submitted (DEC-2008) to UniProtKB.
RN [7]
RP INTERACTION WITH ATM, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=15680327; DOI=10.1016/j.cell.2004.11.054;
RA Park B.-J., Kang J.W., Lee S.W., Choi S.-J., Shin Y.K., Ahn Y.H.,
RA Choi Y.H., Choi D., Lee K.S., Kim S.;
RT "The haploinsufficient tumor suppressor p18 upregulates p53 via
RT interactions with ATM/ATR.";
RL Cell 120:209-221(2005).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-138, AND MASS 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 (2.0 ANGSTROMS), DOMAIN ARCHITECTURE, AND
RP COILED-COIL DOMAIN.
RX PubMed=18343821; DOI=10.1074/jbc.M800859200;
RA Kim K.J., Park M.C., Choi S.J., Oh Y.S., Choi E.C., Cho H.J.,
RA Kim M.H., Kim S.H., Kim D.W., Kim S., Kang B.S.;
RT "Determination of three-dimensional structure and residues of the
RT novel tumor suppressor AIMP3/p18 required for the interaction with
RT ATM.";
RL J. Biol. Chem. 283:14032-14040(2008).
CC -!- FUNCTION: Positive modulator of ATM response to DNA damage.
CC -!- SUBUNIT: Component of the multisynthase complex which is comprised
CC of a bifunctional glutamyl-prolyl-tRNA synthase, the monospecific
CC isoleucyl, leucyl, glutaminyl, methionyl, lysyl, arginyl and
CC aspartyl-tRNA synthases, and three auxiliary proteins, EEF1E1/p18,
CC AIMP2/p38 and AIMP1/p43. Interacts with ATM and ATR. The
CC interaction with ATM, which takes place independently of TP53, is
CC induced by DNA damage that may occur during genotoxic stress or
CC cell growth. The interaction with ATR is enhanced by UV
CC irradiation.
CC -!- INTERACTION:
CC P04591:gag (xeno); NbExp=4; IntAct=EBI-1048486, EBI-6179719;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Cytoplasmic under
CC growth arrest conditions. Translocated into the nucleus when
CC growth resumes (S phase) and following DNA damage.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O43324-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O43324-2; Sequence=VSP_045088;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Down-regulated in various cancer tissues.
CC -!- INDUCTION: By DNA damaging agents such as UV, adriamycin,
CC actinomycin-D and cisplatin.
CC -!- SIMILARITY: Contains 1 GST C-terminal domain.
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DR EMBL; AB011079; BAA24926.1; -; mRNA.
DR EMBL; AF054186; AAC39916.1; -; mRNA.
DR EMBL; BT007306; AAP35970.1; -; mRNA.
DR EMBL; AL355499; CAH72539.1; -; Genomic_DNA.
DR EMBL; AL023694; CAH72539.1; JOINED; Genomic_DNA.
DR EMBL; AL451187; CAH72539.1; JOINED; Genomic_DNA.
DR EMBL; AL023694; CAI21644.1; -; Genomic_DNA.
DR EMBL; AL355499; CAI21644.1; JOINED; Genomic_DNA.
DR EMBL; AL451187; CAI21644.1; JOINED; Genomic_DNA.
DR EMBL; AL451187; CAI14747.1; -; Genomic_DNA.
DR EMBL; AL023694; CAI14747.1; JOINED; Genomic_DNA.
DR EMBL; AL355499; CAI14747.1; JOINED; Genomic_DNA.
DR EMBL; BC005291; AAH05291.1; -; mRNA.
DR EMBL; CK002875; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; NP_001129122.1; NM_001135650.1.
DR RefSeq; NP_004271.1; NM_004280.4.
DR UniGene; Hs.602353; -.
DR UniGene; Hs.745033; -.
DR PDB; 2UZ8; X-ray; 2.00 A; A/B=1-174.
DR PDB; 4BJV; X-ray; 1.99 A; B=1-174.
DR PDB; 4BJW; X-ray; 1.60 A; B=1-169.
DR PDBsum; 2UZ8; -.
DR PDBsum; 4BJV; -.
DR PDBsum; 4BJW; -.
DR ProteinModelPortal; O43324; -.
DR SMR; O43324; 1-169.
DR IntAct; O43324; 3.
DR STRING; 9606.ENSP00000369038; -.
DR PhosphoSite; O43324; -.
DR PaxDb; O43324; -.
DR PeptideAtlas; O43324; -.
DR PRIDE; O43324; -.
DR DNASU; 9521; -.
DR Ensembl; ENST00000379715; ENSP00000369038; ENSG00000124802.
DR Ensembl; ENST00000429723; ENSP00000414363; ENSG00000124802.
DR GeneID; 9521; -.
DR KEGG; hsa:9521; -.
DR UCSC; uc011dic.2; human.
DR CTD; 9521; -.
DR GeneCards; GC06M008024; -.
DR HGNC; HGNC:3212; EEF1E1.
DR HPA; HPA027901; -.
DR MIM; 609206; gene.
DR neXtProt; NX_O43324; -.
DR PharmGKB; PA27648; -.
DR eggNOG; NOG257622; -.
DR HOGENOM; HOG000026786; -.
DR HOVERGEN; HBG003019; -.
DR InParanoid; O43324; -.
DR KO; K15439; -.
DR OMA; AVVQQWL; -.
DR OrthoDB; EOG7GQXX4; -.
DR PhylomeDB; O43324; -.
DR Reactome; REACT_71; Gene Expression.
DR SignaLink; O43324; -.
DR ChiTaRS; EEF1E1; human.
DR EvolutionaryTrace; O43324; -.
DR GeneWiki; EEF1E1; -.
DR GenomeRNAi; 9521; -.
DR NextBio; 35684; -.
DR PRO; PR:O43324; -.
DR ArrayExpress; O43324; -.
DR Bgee; O43324; -.
DR CleanEx; HS_EEF1E1; -.
DR Genevestigator; O43324; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0008285; P:negative regulation of cell proliferation; ISS:UniProtKB.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0043517; P:positive regulation of DNA damage response, signal transduction by p53 class mediator; ISS:UniProtKB.
DR GO; GO:0006418; P:tRNA aminoacylation for protein translation; TAS:Reactome.
DR Gene3D; 1.20.1050.10; -; 1.
DR InterPro; IPR010987; Glutathione-S-Trfase_C-like.
DR SUPFAM; SSF47616; SSF47616; 1.
DR PROSITE; PS50405; GST_CTER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Coiled coil;
KW Complete proteome; Cytoplasm; Direct protein sequencing; Nucleus;
KW Protein biosynthesis; Reference proteome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 174 Eukaryotic translation elongation factor
FT 1 epsilon-1.
FT /FTId=PRO_0000221132.
FT DOMAIN 50 173 GST C-terminal.
FT REGION 2 56 N-terminal.
FT REGION 57 63 Linker.
FT REGION 64 152 C-terminal.
FT COILED 153 169
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 138 138 N6-acetyllysine.
FT VAR_SEQ 129 174 VDLTVQEKEKYLNVSRWFCHIQHYPGIRQHLSSVVFIKNRL
FT YTNSH -> IRKLRHTEVGN (in isoform 2).
FT /FTId=VSP_045088.
FT HELIX 2 13
FT STRAND 23 25
FT TURN 26 29
FT STRAND 30 34
FT STRAND 40 43
FT HELIX 44 54
FT HELIX 58 61
FT HELIX 65 81
FT HELIX 90 101
FT HELIX 102 104
FT STRAND 110 112
FT HELIX 115 128
FT HELIX 133 138
FT HELIX 140 151
FT TURN 153 155
SQ SEQUENCE 174 AA; 19811 MW; 58AAE4BD9E1684E2 CRC64;
MAAAAELSLL EKSLGLSKGN KYSAQGERQI PVLQTNNGPS LTGLTTIAAH LVKQANKEYL
LGSTAEEKAI VQQWLEYRVT QVDGHSSKND IHTLLKDLNS YLEDKVYLTG YNFTLADILL
YYGLHRFIVD LTVQEKEKYL NVSRWFCHIQ HYPGIRQHLS SVVFIKNRLY TNSH
//
MIM
609206
*RECORD*
*FIELD* NO
609206
*FIELD* TI
*609206 EUKARYOTIC TRANSLATION ELONGATION FACTOR 1, EPSILON-1; EEF1E1
;;ELONGATION FACTOR p18
read more*FIELD* TX
CLONING
By sequencing cDNAs randomly selected from a cDNA library derived from
human umbilical cord CD34 (142230)-positive cells, Mao et al. (1998)
obtained a full-length cDNA encoding EEF1E1. The deduced 174-amino acid
protein is a homolog of the rodent elongation factor p18.
GENE FUNCTION
Park et al. (2005) found that human p18 was induced and translocated to
the nucleus in response to DNA damage. Expression of p18 resulted in
elevated p53 (191170) levels, while p18 depletion blocked p53 induction.
p18 interacted directly with ATM (607585) and ATR (601215) in response
to DNA damage. ATM activity was dependent on the level of p18,
suggesting that p18 is required for activation of ATM. RT-PCR showed
that p18 expression was low in several different human cancer cell lines
and tissues. These results, as well as findings in p18 mutant mice,
suggested that p18 is a haploinsufficient tumor suppressor and a key
factor for ATM/ATR-mediated p53 activation.
MAPPING
By radiation hybrid analysis, Mao et al. (1998) mapped the EEF1E1 gene
to chromosome 6p25.1-p23.
ANIMAL MODEL
Park et al. (2005) found that inactivation of both p18 alleles in mice
caused embryonic lethality, whereas heterozygous mice showed high
susceptibility to spontaneous tumors.
*FIELD* RF
1. Mao, M.; Fu, G.; Wu, J.-S.; Zhang, Q.-H.; Zhou, J.; Kan, L.-X.;
Huang, Q.-H.; He, K.-L.; Gu, B.-W.; Han, Z.-G.; Shen, Y.; Gu, J.;
Yu, Y.-P.; Xu, S.-H.; Wang, Y.-X.; Chen, S.-J.; Chen, Z.: Identification
of genes expressed in human CD34+ hematopoietic stem/progenitor cells
by expressed sequence tags and efficient full-length cDNA cloning. Proc.
Nat. Acad. Sci. 95: 8175-8180, 1998.
2. Park, B.-J.; Kang, J. W.; Lee, S. W.; Choi, S.-J.; Shin, Y. K.;
Ahn, Y. H.; Choi, Y. H.; Choi, D.; Lee, K. S.; Kim, S.: The haploinsufficient
tumor suppressor p18 upregulates p53 via interactions with ATM/ATR. Cell 120:
209-221, 2005.
*FIELD* CN
Matthew B. Gross - updated: 2/16/2005
*FIELD* CD
Stylianos E. Antonarakis: 2/16/2005
*FIELD* ED
mgross: 02/16/2005
mgross: 2/16/2005
*RECORD*
*FIELD* NO
609206
*FIELD* TI
*609206 EUKARYOTIC TRANSLATION ELONGATION FACTOR 1, EPSILON-1; EEF1E1
;;ELONGATION FACTOR p18
read more*FIELD* TX
CLONING
By sequencing cDNAs randomly selected from a cDNA library derived from
human umbilical cord CD34 (142230)-positive cells, Mao et al. (1998)
obtained a full-length cDNA encoding EEF1E1. The deduced 174-amino acid
protein is a homolog of the rodent elongation factor p18.
GENE FUNCTION
Park et al. (2005) found that human p18 was induced and translocated to
the nucleus in response to DNA damage. Expression of p18 resulted in
elevated p53 (191170) levels, while p18 depletion blocked p53 induction.
p18 interacted directly with ATM (607585) and ATR (601215) in response
to DNA damage. ATM activity was dependent on the level of p18,
suggesting that p18 is required for activation of ATM. RT-PCR showed
that p18 expression was low in several different human cancer cell lines
and tissues. These results, as well as findings in p18 mutant mice,
suggested that p18 is a haploinsufficient tumor suppressor and a key
factor for ATM/ATR-mediated p53 activation.
MAPPING
By radiation hybrid analysis, Mao et al. (1998) mapped the EEF1E1 gene
to chromosome 6p25.1-p23.
ANIMAL MODEL
Park et al. (2005) found that inactivation of both p18 alleles in mice
caused embryonic lethality, whereas heterozygous mice showed high
susceptibility to spontaneous tumors.
*FIELD* RF
1. Mao, M.; Fu, G.; Wu, J.-S.; Zhang, Q.-H.; Zhou, J.; Kan, L.-X.;
Huang, Q.-H.; He, K.-L.; Gu, B.-W.; Han, Z.-G.; Shen, Y.; Gu, J.;
Yu, Y.-P.; Xu, S.-H.; Wang, Y.-X.; Chen, S.-J.; Chen, Z.: Identification
of genes expressed in human CD34+ hematopoietic stem/progenitor cells
by expressed sequence tags and efficient full-length cDNA cloning. Proc.
Nat. Acad. Sci. 95: 8175-8180, 1998.
2. Park, B.-J.; Kang, J. W.; Lee, S. W.; Choi, S.-J.; Shin, Y. K.;
Ahn, Y. H.; Choi, Y. H.; Choi, D.; Lee, K. S.; Kim, S.: The haploinsufficient
tumor suppressor p18 upregulates p53 via interactions with ATM/ATR. Cell 120:
209-221, 2005.
*FIELD* CN
Matthew B. Gross - updated: 2/16/2005
*FIELD* CD
Stylianos E. Antonarakis: 2/16/2005
*FIELD* ED
mgross: 02/16/2005
mgross: 2/16/2005