EF1A3_HUMAN
ID EF1A3_HUMAN Reviewed; 462 AA.
AC Q5VTE0;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Putative elongation factor 1-alpha-like 3;
DE Short=EF-1-alpha-like 3;
DE AltName: Full=Eukaryotic elongation factor 1 A-like 3;
DE Short=eEF1A-like 3;
DE AltName: Full=Eukaryotic translation elongation factor 1 alpha-1 pseudogene 5;
GN Name=EEF1A1P5; Synonyms=EEF1AL3;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [2]
RP PROTEIN SEQUENCE OF 6-30; 52-62; 85-96; 135-166; 173-179; 248-290 AND
RP 431-439, METHYLATION AT LYS-55 AND LYS-165, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Colon carcinoma, and Ovarian carcinoma;
RA Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W.;
RL Submitted (DEC-2008) to UniProtKB.
RN [3]
RP PROTEIN SEQUENCE OF 6-30; 52-62; 85-96; 101-129; 135-179; 220-244; 248-290;
RP 396-423 AND 431-439, METHYLATION AT LYS-55 AND LYS-165, AND IDENTIFICATION
RP BY MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma, and Embryonic kidney;
RA Bienvenut W.V., Waridel P., Quadroni M.;
RL Submitted (MAR-2009) to UniProtKB.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 258-462.
RA Li W.B., Gruber C., Jessee J., Polayes D.;
RT "Full-length cDNA libraries and normalization.";
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP IDENTIFICATION.
RX PubMed=8812466; DOI=10.1006/geno.1996.0475;
RA Lund A., Knudsen S.M., Vissing H., Clark B., Tommerup N.;
RT "Assignment of human elongation factor 1alpha genes: EEF1A maps to
RT chromosome 6q14 and EEF1A2 to 20q13.3.";
RL Genomics 36:359-361(1996).
CC -!- FUNCTION: This protein promotes the GTP-dependent binding of aminoacyl-
CC tRNA to the A-site of ribosomes during protein biosynthesis.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A
CC subfamily. {ECO:0000305}.
CC -!- CAUTION: Could be the product of a pseudogene. {ECO:0000305}.
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DR EMBL; AL593851; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR595753; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; CR609311; -; NOT_ANNOTATED_CDS; mRNA.
DR AlphaFoldDB; Q5VTE0; -.
DR SMR; Q5VTE0; -.
DR IntAct; Q5VTE0; 25.
DR MINT; Q5VTE0; -.
DR GlyGen; Q5VTE0; 2 sites, 1 O-linked glycan (1 site).
DR iPTMnet; Q5VTE0; -.
DR MetOSite; Q5VTE0; -.
DR PhosphoSitePlus; Q5VTE0; -.
DR SwissPalm; Q5VTE0; -.
DR BioMuta; HGNC:3200; -.
DR DMDM; 74746925; -.
DR jPOST; Q5VTE0; -.
DR MassIVE; Q5VTE0; -.
DR MaxQB; Q5VTE0; -.
DR PeptideAtlas; Q5VTE0; -.
DR PRIDE; Q5VTE0; -.
DR ProteomicsDB; 65322; -.
DR TopDownProteomics; Q5VTE0; -.
DR GeneCards; EEF1A1P5; -.
DR HGNC; HGNC:3200; EEF1A1P5.
DR neXtProt; NX_Q5VTE0; -.
DR InParanoid; Q5VTE0; -.
DR PathwayCommons; Q5VTE0; -.
DR Reactome; R-HSA-156842; Eukaryotic Translation Elongation.
DR SignaLink; Q5VTE0; -.
DR ChiTaRS; EEF1A1P5; human.
DR Pharos; Q5VTE0; Tdark.
DR PRO; PR:Q5VTE0; -.
DR Proteomes; UP000005640; Unplaced.
DR RNAct; Q5VTE0; protein.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; HDA:UniProtKB.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0003746; F:translation elongation factor activity; IBA:GO_Central.
DR GO; GO:0006412; P:translation; IBA:GO_Central.
DR GO; GO:0006414; P:translational elongation; IBA:GO_Central.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00118_A; EF_Tu_A; 1.
DR InterPro; IPR004161; EFTu-like_2.
DR InterPro; IPR031157; G_TR_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR InterPro; IPR009001; Transl_elong_EF1A/Init_IF2_C.
DR InterPro; IPR004539; Transl_elong_EF1A_euk/arc.
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; G_TR_1; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 5: Uncertain;
KW Acetylation; Cytoplasm; Direct protein sequencing; Elongation factor;
KW GTP-binding; Methylation; Nucleotide-binding; Phosphoprotein;
KW Protein biosynthesis; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..462
FT /note="Putative elongation factor 1-alpha-like 3"
FT /id="PRO_0000340262"
FT DOMAIN 5..242
FT /note="tr-type G"
FT REGION 14..21
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 70..74
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 91..94
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 153..156
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 194..196
FT /note="G5"
FT /evidence="ECO:0000250"
FT BINDING 14..21
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 91..95
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 153..156
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N,N,N-trimethylglycine"
FT /evidence="ECO:0000250|UniProtKB:P68104"
FT MOD_RES 55
FT /note="N6,N6-dimethyllysine"
FT /evidence="ECO:0000269|Ref.2, ECO:0000269|Ref.3"
FT MOD_RES 165
FT /note="N6,N6,N6-trimethyllysine; alternate"
FT /evidence="ECO:0000269|Ref.2, ECO:0000269|Ref.3"
FT MOD_RES 165
FT /note="N6,N6-dimethyllysine; alternate"
FT /evidence="ECO:0000269|Ref.2, ECO:0000269|Ref.3"
FT MOD_RES 165
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P10126"
FT MOD_RES 165
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000269|Ref.2, ECO:0000269|Ref.3"
FT MOD_RES 172
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P10126"
FT MOD_RES 273
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P10126"
FT MOD_RES 301
FT /note="5-glutamyl glycerylphosphorylethanolamine"
FT /evidence="ECO:0000250|UniProtKB:P10126"
FT MOD_RES 374
FT /note="5-glutamyl glycerylphosphorylethanolamine"
FT /evidence="ECO:0000250|UniProtKB:P10126"
FT MOD_RES 392
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P10126"
FT MOD_RES 392
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P10126"
FT MOD_RES 439
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P10126"
SQ SEQUENCE 462 AA; 50185 MW; 7E53152607CE1E68 CRC64;
MGKEKTHINI VVIGHVDSGK STTTGHLIYK CGGIDKRTIE KFEKEAAEMG KGSFKYAWVL
DKLKAERERG ITIDISLWKF ETSKYYVTII DAPGHRDFIK NMITGTSQAD CAVLIVAAGV
GEFEAGISKN GQTREHALLA YTLGVKQLIV GVNKMDSTEP PYSQKRYEEI VKEVSTYIKK
IGYNPDTVAF VPISGWNGDN MLEPSANMPW FKGWKVTRKD GNASGTTLLE ALDCILPPTR
PTDKPLRLPL QDVYKIGGIG TVPVGRVETG VLKPGMVVTF APVNVTTEVK SVEMHHEALS
EALPGDNVGF KVKNVSVKDV RRGNVAGDSK NDPPMEAAGF TAQVIILNHP GQISAGYAPV
LDCHMAHIAC KFAELKEKID RRSGKKLEDG PKFLKSGDAA IVDMVPGKPM CVESFSDYPP
LGRFAVRDMR QTVAVGVIKA VDKKAAGAGK VTKSAQKAQK AK
