CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-014098
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
  
Protein Name
 Putative elongation factor 1-alpha-like 3 
Protein Synonyms/Alias
 EF-1-alpha-like 3; Eukaryotic elongation factor 1 A-like 3; eEF1A-like 3; Eukaryotic translation elongation factor 1 alpha-1 pseudogene 5 
Gene Name
 EEF1A1P5 
Gene Synonyms/Alias
 EEF1AL3 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
55EMGKGSFKYAWVLDKmethylation[1]
165TEPPYSQKRYEEIVKmethylation[1]
Reference
 [1] Update on activities at the Universal Protein Resource (UniProt) in 2013.
 e="String">UniProt Consortium.
 Nucleic Acids Res. 2013 Jan;41(Database issue):D43-7. [PMID: 23161681
Functional Description
 This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis (By similarity). 
Sequence Annotation
 NP_BIND 14 21 GTP (By similarity).
 NP_BIND 91 95 GTP (By similarity).
 NP_BIND 153 156 GTP (By similarity).
 MOD_RES 36 36 N6,N6,N6-trimethyllysine (By similarity).
 MOD_RES 55 55 N6,N6-dimethyllysine.
 MOD_RES 79 79 N6,N6,N6-trimethyllysine (By similarity).
 MOD_RES 165 165 N6,N6,N6-trimethyllysine; alternate.
 MOD_RES 165 165 N6,N6-dimethyllysine; alternate.
 MOD_RES 165 165 N6-methyllysine; alternate.
 MOD_RES 300 300 Phosphoserine (By similarity).
 MOD_RES 301 301 5-glutamyl glycerylphosphorylethanolamine
 MOD_RES 318 318 N6,N6,N6-trimethyllysine (By similarity).
 MOD_RES 374 374 5-glutamyl glycerylphosphorylethanolamine
 MOD_RES 432 432 Phosphothreonine (By similarity).  
Keyword
 Complete proteome; Cytoplasm; Direct protein sequencing; Elongation factor; GTP-binding; Methylation; Nucleotide-binding; Phosphoprotein; Protein biosynthesis; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 462 AA 
Protein Sequence
MGKEKTHINI VVIGHVDSGK STTTGHLIYK CGGIDKRTIE KFEKEAAEMG KGSFKYAWVL 60
DKLKAERERG ITIDISLWKF ETSKYYVTII DAPGHRDFIK NMITGTSQAD CAVLIVAAGV 120
GEFEAGISKN GQTREHALLA YTLGVKQLIV GVNKMDSTEP PYSQKRYEEI VKEVSTYIKK 180
IGYNPDTVAF VPISGWNGDN MLEPSANMPW FKGWKVTRKD GNASGTTLLE ALDCILPPTR 240
PTDKPLRLPL QDVYKIGGIG TVPVGRVETG VLKPGMVVTF APVNVTTEVK SVEMHHEALS 300
EALPGDNVGF KVKNVSVKDV RRGNVAGDSK NDPPMEAAGF TAQVIILNHP GQISAGYAPV 360
LDCHMAHIAC KFAELKEKID RRSGKKLEDG PKFLKSGDAA IVDMVPGKPM CVESFSDYPP 420
LGRFAVRDMR QTVAVGVIKA VDKKAAGAGK VTKSAQKAQK AK 462 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
 GO:0003924; F:GTPase activity; IEA:InterPro.
 GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
 GO:0006184; P:GTP catabolic process; IEA:GOC. 
Interpro
 IPR000795; EF_GTP-bd_dom.
 IPR027417; P-loop_NTPase.
 IPR009001; Transl_elong_EF1A/Init_IF2_C.
 IPR004539; Transl_elong_EF1A_euk/arc.
 IPR004161; Transl_elong_EFTu/EF1A_2.
 IPR004160; Transl_elong_EFTu/EF1A_C.
 IPR009000; Transl_elong_init/rib_B-barrel. 
Pfam
 PF00009; GTP_EFTU
 PF03144; GTP_EFTU_D2
 PF03143; GTP_EFTU_D3 
SMART
  
PROSITE
 PS00301; EFACTOR_GTP 
PRINTS
 PR00315; ELONGATNFCT.