ID MCA3_HUMAN Reviewed; 174 AA. AC O43324; Q5THS2; DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1998, sequence version 1. DT 27-JUL-2011, entry version 99. 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]. 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]. RC TISSUE=Umbilical cord blood; RX MEDLINE=98318631; 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]. 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 MEDLINE=22935763; 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]. RC TISSUE=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-12; LYS-138 AND LYS-166, AND RP MASS SPECTROMETRY. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., RA 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 ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY. RC TISSUE=Embryonic kidney; RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., RA Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in RT a refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [10] 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). 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 -!- 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 -!- 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. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 IPI; IPI00003588; -. DR RefSeq; NP_004271.1; NM_004280.4. DR UniGene; Hs.602353; -. DR UniGene; Hs.726163; -. DR PDB; 2UZ8; X-ray; 2.00 A; A/B=1-174. DR PDBsum; 2UZ8; -. DR ProteinModelPortal; O43324; -. DR SMR; O43324; 1-169. DR IntAct; O43324; 2. DR STRING; O43324; -. DR PhosphoSite; O43324; -. DR PeptideAtlas; O43324; -. DR PRIDE; O43324; -. DR Ensembl; ENST00000379715; ENSP00000369038; ENSG00000124802. DR GeneID; 9521; -. DR KEGG; hsa:9521; -. DR UCSC; uc003mxz.1; human. DR CTD; 9521; -. DR GeneCards; GC06M008024; -. DR H-InvDB; HIX0200833; -. DR HGNC; HGNC:3212; EEF1E1. DR HPA; HPA027901; -. DR MIM; 609206; gene. DR neXtProt; NX_O43324; -. DR eggNOG; prNOG10876; -. DR GeneTree; ENSGT00390000003564; -. DR HOGENOM; HBG445723; -. DR HOVERGEN; HBG003019; -. DR InParanoid; O43324; -. DR OMA; EDKVYLA; -. DR OrthoDB; EOG4HHP3M; -. DR PhylomeDB; O43324; -. DR Reactome; REACT_71; Gene Expression. DR NextBio; 35684; -. DR ArrayExpress; O43324; -. DR Bgee; O43324; -. DR CleanEx; HS_EEF1E1; -. DR Genevestigator; O43324; -. DR GermOnline; ENSG00000124802; Homo sapiens. DR GO; GO:0005829; C:cytosol; EXP: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 apoptosis; 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 InterPro; IPR010987; Glutathione-S-Trfase_C-like. DR InterPro; IPR017933; Glutathione_S_Trfase/Cl_chnl_C. DR InterPro; IPR004046; GST_C. DR InterPro; IPR012336; Thioredoxin-like_fold. DR Gene3D; G3DSA:1.20.1050.10; GST_C_like; 1. DR Gene3D; G3DSA:3.40.30.10; Thioredoxin_fold; 1. DR Pfam; PF00043; GST_C; 1. DR SUPFAM; SSF47616; GST_C_like; 1. DR PROSITE; PS50405; GST_CTER; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Complete proteome; Cytoplasm; KW Direct protein sequencing; Nucleus; Protein biosynthesis. 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 MOD_RES 2 2 N-acetylalanine. FT MOD_RES 12 12 N6-acetyllysine. FT MOD_RES 138 138 N6-acetyllysine. FT MOD_RES 166 166 N6-acetyllysine. 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 //