Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P49411 (EFTU_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 153. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Elongation factor Tu, mitochondrial

Short name=EF-Tu
Alternative name(s):
P43
Gene names
Name:TUFM
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length452 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 4343Mitochondrion Ref.6 Ref.7
Chain44 – 452409Elongation factor Tu, mitochondrial
PRO_0000007462

Regions

Nucleotide binding64 – 718GTP By similarity
Nucleotide binding126 – 1305GTP By similarity
Nucleotide binding181 – 1844GTP By similarity

Amino acid modifications

Modified residue791N6-acetyllysine Ref.10
Modified residue881N6-acetyllysine Ref.10
Modified residue2561N6-acetyllysine Ref.10
Modified residue4181N6-acetyllysine Ref.10

Natural variations

Natural variant3361R → Q in COXPD4. Ref.12
VAR_031902

Experimental info

Sequence conflict195 – 1973Missing in AAC60647. Ref.2
Sequence conflict3841D → N in AAB00499. Ref.1
Sequence conflict3841D → N in CAA72493. Ref.9

Sequences

Sequence LengthMass (Da)Tools
P49411 [UniParc].

Last modified October 1, 1996. Version 2.
Checksum: E37274ABFFDB5FC7

FASTA45249,542
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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, IDENTIFICATION BY 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[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.
PIRS62767.
S68466.
RefSeqNP_003312.3. NM_003321.4.
UniGeneHs.12084.

3D structure databases

ProteinModelPortalP49411.
SMRP49411. Positions 24-451.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113135. 133 interactions.
IntActP49411. 22 interactions.
MINTMINT-224570.
STRING9606.ENSP00000322439.

PTM databases

PhosphoSiteP49411.

Polymorphism databases

DMDM1706611.

2D gel databases

DOSAC-COBS-2DPAGEP49411.
OGPP49411.
REPRODUCTION-2DPAGEIPI00027107.
SWISS-2DPAGEP49411.
UCD-2DPAGEP49411.

Proteomic databases

MaxQBP49411.
PaxDbP49411.
PRIDEP49411.

Protocols and materials databases

DNASU7284.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000313511; ENSP00000322439; ENSG00000178952.
GeneID7284.
KEGGhsa:7284.
UCSCuc002drh.2. human.

Organism-specific databases

CTD7284.
GeneCardsGC16M028853.
HGNCHGNC:12420. TUFM.
HPAHPA018991.
HPA024087.
MIM602389. gene.
610678. phenotype.
neXtProtNX_P49411.
Orphanet254925. Combined oxidative phosphorylation defect type 4.
PharmGKBPA37082.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0050.
HOGENOMHOG000229290.
HOVERGENHBG001535.
InParanoidP49411.
KOK02358.
OrthoDBEOG73BVCN.
PhylomeDBP49411.
TreeFamTF300432.

Enzyme and pathway databases

SignaLinkP49411.

Gene expression databases

ArrayExpressP49411.
BgeeP49411.
CleanExHS_TUFM.
GenevestigatorP49411.

Family and domain databases

Gene3D3.40.50.300. 1 hit.
InterProIPR000795. EF_GTP-bd_dom.
IPR027417. P-loop_NTPase.
IPR009000. Transl_B-barrel.
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.
[Graphical view]
PfamPF00009. GTP_EFTU. 1 hit.
PF03144. GTP_EFTU_D2. 1 hit.
PF03143. GTP_EFTU_D3. 1 hit.
[Graphical view]
PRINTSPR00315. ELONGATNFCT.
SUPFAMSSF50447. SSF50447. 1 hit.
SSF50465. SSF50465. 1 hit.
SSF52540. SSF52540. 1 hit.
TIGRFAMsTIGR00485. EF-Tu. 1 hit.
PROSITEPS00301. EFACTOR_GTP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiTUFM.
GenomeRNAi7284.
NextBio28481.
PROP49411.
SOURCESearch...

Entry information

Entry nameEFTU_HUMAN
AccessionPrimary (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: July 9, 2014
This is version 153 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 16

Human chromosome 16: entries, gene names and cross-references to MIM