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   27-MAR-2024, entry version 121.
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; 27.
DR   MINT; Q5VTE0; -.
DR   GlyGen; Q5VTE0; 5 sites, 1 O-linked glycan (4 sites).
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   ProteomicsDB; 65322; -.
DR   Pumba; Q5VTE0; -.
DR   TopDownProteomics; Q5VTE0; -.
DR   AGR; HGNC:3200; -.
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   SIGNOR; 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   CDD; cd01883; EF1_alpha; 1.
DR   CDD; cd03693; EF1_alpha_II; 1.
DR   CDD; cd03705; EF1_alpha_III; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 2.40.30.10; Translation factors; 2.
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   NCBIfam; TIGR00483; EF-1_alpha; 1.
DR   PANTHER; PTHR23115:SF222; ELONGATION FACTOR 1-ALPHA 1-RELATED; 1.
DR   PANTHER; PTHR23115; TRANSLATION FACTOR; 1.
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; SSF50465; EF-Tu/eEF-1alpha/eIF2-gamma C-terminal domain; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF50447; Translation proteins; 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
//