Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-9606-00208
Entry Name
UniProt Accession
Theoretical PI
7.26
Molecular Weight
49541.54
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Elongation factor Tu, mitochondrial
Protein Synonyms/Alias
EF-Tu; P43;
Gene Name
TUFM
Gene Synonyms/Alias
Created Date
01-FEB-1996
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
40
Canonical
APALPLLCRGLAVEA
[1]
S-Palmitoylation
Organism
Homo sapiens (Human)
NCBI Taxa ID
9606
Reference
[1] Predicted from GPS-Lipid
Functional Description
This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.
Sequence Annotation
Domain: 55 251 tr-type G.
Nucleotide-binding: 64 71 GTP.
Nucleotide-binding: 126 130 GTP.
Nucleotide-binding: 181 184 GTP.
Region: 64 71 G1.
Region: 105 109 G2.
Region: 126 129 G3.
Region: 181 184 G4.
Region: 219 221 G5.
Modified residue: 79 79 N6-acetyllysine.
Modified residue: 88 88 N6-acetyllysine.
Modified residue: 256 256 N6-acetyllysine.
Modified residue: 418 418 N6-acetyllysine.
Protein Length
452 AA.
Protein Sequence
(Canonical)
MAAATLLRAT PHFSGLAAGR TFLLQGLLRL LKAPALPLLC RGLAVEAKKT YVRDKPHVNV  60
GTIGHVDHGK TTLTAAITKI LAEGGGAKFK KYEEIDNAPE ERARGITINA AHVEYSTAAR  120
HYAHTDCPGH ADYVKNMITG TAPLDGCILV VAANDGPMPQ TREHLLLARQ IGVEHVVVYV  180
NKADAVQDSE MVELVELEIR ELLTEFGYKG EETPVIVGSA LCALEGRDPE LGLKSVQKLL  240
DAVDTYIPVP ARDLEKPFLL PVEAVYSVPG RGTVVTGTLE RGILKKGDEC ELLGHSKNIR  300
TVVTGIEMFH KSLERAEAGD NLGALVRGLK REDLRRGLVM VKPGSIKPHQ KVEAQVYILS  360
KEEGGRHKPF VSHFMPVMFS LTWDMACRII LPPEKELAMP GEDLKFNLIL RQPMILEKGQ  420
RFTLRDGNRT IGTGLVTNTL AMTEEEKNIK WG                                452
FASTA
(Canonical)
>LipidDB-9606-00208|P49411
MAAATLLRATPHFSGLAAGRTFLLQGLLRLLKAPALPLLCRGLAVEAKKTYVRDKPHVNV
GTIGHVDHGKTTLTAAITKILAEGGGAKFKKYEEIDNAPEERARGITINAAHVEYSTAAR
HYAHTDCPGHADYVKNMITGTAPLDGCILVVAANDGPMPQTREHLLLARQIGVEHVVVYV
NKADAVQDSEMVELVELEIRELLTEFGYKGEETPVIVGSALCALEGRDPELGLKSVQKLL
DAVDTYIPVPARDLEKPFLLPVEAVYSVPGRGTVVTGTLERGILKKGDECELLGHSKNIR
TVVTGIEMFHKSLERAEAGDNLGALVRGLKREDLRRGLVMVKPGSIKPHQKVEAQVYILS
KEEGGRHKPFVSHFMPVMFSLTWDMACRIILPPEKELAMPGEDLKFNLILRQPMILEKGQ
RFTLRDGNRTIGTGLVTNTLAMTEEEKNIKWG
Gene Ontology
GO:0070062; C:extracellular vesicular exosome; IDA:UniProt
GO:0016020; C:membrane; IDA:UniProtKB
GO:0042645; C:mitochondrial nucleoid; IDA:BHF-UCL
GO:0005739; C:mitochondrion; IDA:UniProtKB
GO:0005525; F:GTP binding; IEA:UniProtKB-KW
GO:0003924; F:GTPase activity; IEA:InterPro
GO:0044822; F:poly(A) RNA binding; IDA:UniProtKB
GO:0003746; F:translation elongation factor activity; IDA:UniProtKB
GO:0006414; P:translational elongation; IDA:UniProtKB
Interpro
InterPro; IPR000795; EF_GTP-bd_dom
InterPro; IPR027417; P-loop_NTPase
InterPro; IPR009000; Transl_B-barrel
InterPro; IPR009001; Transl_elong_EF1A/Init_IF2_C
InterPro; IPR004161; Transl_elong_EFTu/EF1A_2
InterPro; IPR004541; Transl_elong_EFTu/EF1A_bac/org
InterPro; IPR004160; Transl_elong_EFTu/EF1A_C
Pfam
Pfam; PF00009; GTP_EFTU;
Pfam; PF03144; GTP_EFTU_D2;
Pfam; PF03143; GTP_EFTU_D3;
SMART
PROSITE
PROSITE; PS00301; G_TR_1;
PROSITE; PS51722; G_TR_2;
PRINTS
PRINTS; PR00315; ELONGATNFCT;