P49411 (EFTU_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Elongation factor Tu, mitochondrial
Short name=EF-Tu

Alternative name(s):
P43

Gene names

Name:

TUFM

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	452 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.
Subcellular location	Mitochondrion.
Involvement in disease	Combined oxidative phosphorylation deficiency 4 (COXPD4) [MIM:610678]: A mitochondrial disease resulting in neonatal lactic acidosis, rapidly progressive encephalopathy, severely decreased mitochondrial protein synthesis, and combined deficiency of mtDNA-related mitochondrial respiratory chain complexes. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.12
Sequence similarities	Belongs to the GTP-binding elongation factor family. EF-Tu/EF-1A subfamily.
Sequence caution	The sequence AAC60647.1 differs from that shown. Reason: Erroneous initiation. The sequence AAH01633.2 differs from that shown. Reason: Erroneous initiation. The sequence AAH10041.2 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Protein biosynthesis
Cellular component	Mitochondrion
Disease	Disease mutation
Domain	Transit peptide
Ligand	GTP-binding Nucleotide-binding
Molecular function	Elongation factor
PTM	Acetylation
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	GTP catabolic process Inferred from electronic annotation. Source: GOC
Cellular_component	mitochondrial nucleoid Inferred from direct assay PubMed 18063578. Source: BHF-UCL
Molecular_function	GTP binding Inferred from electronic annotation. Source: UniProtKB-KW GTPase activity Inferred from electronic annotation. Source: InterPro translation elongation factor activity Inferred from direct assay Ref.3. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 43	43	Mitochondrion Ref.6 Ref.7
	Chain	44 – 452	409	Elongation factor Tu, mitochondrial		PRO_0000007462
Regions
	Nucleotide binding	64 – 71	8	GTP By similarity
	Nucleotide binding	126 – 130	5	GTP By similarity
	Nucleotide binding	181 – 184	4	GTP By similarity
Amino acid modifications
	Modified residue	79	1	N6-acetyllysine Ref.10
	Modified residue	88	1	N6-acetyllysine Ref.10
	Modified residue	256	1	N6-acetyllysine Ref.10
	Modified residue	418	1	N6-acetyllysine Ref.10
Natural variations
	Natural variant	336	1	R → Q in COXPD4. Ref.12		VAR_031902
Experimental info
	Sequence conflict	195 – 197	3	Missing in AAC60647. Ref.2
	Sequence conflict	384	1	D → N in AAB00499. Ref.1
	Sequence conflict	384	1	D → N in CAA72493. Ref.9

Sequences

	Sequence		Length	Mass (Da)
	P49411 [UniParc]. Last modified October 1, 1996. Version 2. Checksum: E37274ABFFDB5FC7	FASTA	452	49,542
	10 20 30 40 50 60 MAAATLLRAT PHFSGLAAGR TFLLQGLLRL LKAPALPLLC RGLAVEAKKT YVRDKPHVNV 70 80 90 100 110 120 GTIGHVDHGK TTLTAAITKI LAEGGGAKFK KYEEIDNAPE ERARGITINA AHVEYSTAAR 130 140 150 160 170 180 HYAHTDCPGH ADYVKNMITG TAPLDGCILV VAANDGPMPQ TREHLLLARQ IGVEHVVVYV 190 200 210 220 230 240 NKADAVQDSE MVELVELEIR ELLTEFGYKG EETPVIVGSA LCALEGRDPE LGLKSVQKLL 250 260 270 280 290 300 DAVDTYIPVP ARDLEKPFLL PVEAVYSVPG RGTVVTGTLE RGILKKGDEC ELLGHSKNIR 310 320 330 340 350 360 TVVTGIEMFH KSLERAEAGD NLGALVRGLK REDLRRGLVM VKPGSIKPHQ KVEAQVYILS 370 380 390 400 410 420 KEEGGRHKPF VSHFMPVMFS LTWDMACRII LPPEKELAMP GEDLKFNLIL RQPMILEKGQ 430 440 450 RFTLRDGNRT IGTGLVTNTL AMTEEEKNIK WG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning, sequence analysis and expression of mammalian mitochondrial protein synthesis elongation factor Tu." Woriax V.L., Burkhart W.A., Spremulli L.L. Biochim. Biophys. Acta 1264:347-356(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver.
[2]	"A mitochondrial elongation factor-like protein is over-expressed in tumours and differentially expressed in normal tissues." Wells J., Henkler F., Leversha M., Koshy R. FEBS Lett. 358:119-125(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver.
[3]	"The human mitochondrial elongation factor Tu (EF-Tu) gene: cDNA sequence, genomic localization, genomic structure, and identification of a pseudogene." Ling M., Merante F., Chen H.-S., Duff C., Duncan A.M.V., Robinson B.H. Gene 197:325-336(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Heart and Kidney.
[4]	"The sequence and analysis of duplication-rich human chromosome 16." Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J. , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A. Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Lung and Placenta.
[6]	Dunn M.J. Submitted (MAR-1996) to UniProtKB Cited for: PROTEIN SEQUENCE OF 44-54. Tissue: Heart.
[7]	"Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides." Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J. Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 44-53. Tissue: Platelet.
[8]	Lubec G., Vishwanath V. Submitted (MAR-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 239-271, MASS SPECTROMETRY. Tissue: Brain and Cajal-Retzius cell.
[9]	"Human genomic sequences encoding mitochondrial elongation factor EF-Tu: evidence for post-endosymbiotic intron insertion." Jacobs H.T., Smurthwaite L., Koshy R. Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 379-395.
[10]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-79; LYS-88; LYS-256 AND LYS-418, MASS SPECTROMETRY.
[11]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]	"Infantile encephalopathy and defective mitochondrial DNA translation in patients with mutations of mitochondrial elongation factors EFG1 and EFTu." Valente L., Tiranti V., Marsano R.M., Malfatti E., Fernandez-Vizarra E., Donnini C., Mereghetti P., De Gioia L., Burlina A., Castellan C., Comi G.P., Savasta S., Ferrero I., Zeviani M. Am. J. Hum. Genet. 80:44-58(2007) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT COXPD4 GLN-336.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L38995 mRNA. Translation: AAB00499.1. S75463 mRNA. Translation: AAC60647.1. Different initiation. X84694 mRNA. Translation: CAA59169.1. AC133550 Genomic DNA. No translation available. BC001633 mRNA. Translation: AAH01633.2. Different initiation. BC010041 mRNA. Translation: AAH10041.2. Different initiation. Y11797 Genomic DNA. Translation: CAA72493.1.
IPI	IPI00027107.
PIR	S62767. S68466.
RefSeq	NP_003312.3. NM_003321.4.
UniGene	Hs.12084.
3D structure databases
ProteinModelPortal	P49411.
ModBase	Search...
Protein-protein interaction databases
IntAct	P49411. 15 interactions.
MINT	MINT-224570.
STRING	9606.ENSP00000322439.
PTM databases
PhosphoSite	P49411.
Polymorphism databases
DMDM	1706611.
2D gel databases
DOSAC-COBS-2DPAGE	P49411.
OGP	P49411.
REPRODUCTION-2DPAGE	IPI00027107.
SWISS-2DPAGE	P49411.
UCD-2DPAGE	P49411.
Proteomic databases
PaxDb	P49411.
PRIDE	P49411.
Protocols and materials databases
DNASU	7284.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000313511; ENSP00000322439; ENSG00000178952.
GeneID	7284.
KEGG	hsa:7284.
UCSC	uc002drh.2. human.
Organism-specific databases
CTD	7284.
GeneCards	GC16M028853.
HGNC	HGNC:12420. TUFM.
HPA	HPA018991. HPA024087.
MIM	602389. gene. 610678. phenotype.
neXtProt	NX_P49411.
Orphanet	254925. Combined oxidative phosphorylation defect type 4.
PharmGKB	PA37082.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0050.
HOGENOM	HOG000229290.
HOVERGEN	HBG001535.
InParanoid	P49411.
KO	K02358.
OrthoDB	EOG4SXNCK.
Gene expression databases
ArrayExpress	P49411.
Bgee	P49411.
CleanEx	HS_TUFM.
Genevestigator	P49411.
GermOnline	ENSG00000178952. Homo sapiens.
Family and domain databases
InterPro	IPR000795. EF_GTP-bd_dom. IPR009001. Transl_elong_EF1A/Init_IF2_C. IPR004161. Transl_elong_EFTu/EF1A_2. IPR004541. Transl_elong_EFTu/EF1A_bac/org. IPR004160. Transl_elong_EFTu/EF1A_C. IPR009000. Transl_elong_init/rib_B-barrel. [Graphical view]
PANTHER	PTHR23115:SF31. PTHR23115:SF31. 1 hit.
Pfam	PF00009. GTP_EFTU. 1 hit. PF03144. GTP_EFTU_D2. 1 hit. PF03143. GTP_EFTU_D3. 1 hit. [Graphical view]
PRINTS	PR00315. ELONGATNFCT.
SUPFAM	SSF50465. Elong_init_C. 1 hit. SSF50447. Translat_factor. 1 hit.
TIGRFAMs	TIGR00485. EF-Tu. 1 hit.
PROSITE	PS00301. EFACTOR_GTP. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	7284.
NextBio	28481.
SOURCE	Search...

Entry information

Entry name

EFTU_HUMAN

Accession

Primary (citable) accession number: P49411
Secondary accession number(s): O15276

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1996
Last sequence update:	October 1, 1996
Last modified:	May 1, 2013
This is version 141 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.