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Protein

Elongation factor Tu, mitochondrial

Gene

TUFM

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi64 – 718GTPBy similarity
Nucleotide bindingi126 – 1305GTPBy similarity
Nucleotide bindingi181 – 1844GTPBy similarity

GO - Molecular functioni

  1. GTPase activity Source: InterPro
  2. GTP binding Source: UniProtKB-KW
  3. poly(A) RNA binding Source: UniProtKB
  4. translation elongation factor activity Source: UniProtKB

GO - Biological processi

  1. mitochondrial translation Source: Reactome
  2. mitochondrial translational elongation Source: Reactome
  3. organelle organization Source: Reactome
  4. translational elongation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Elongation factor

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_267677. Mitochondrial translation elongation.
SignaLinkiP49411.

Names & Taxonomyi

Protein namesi
Recommended name:
Elongation factor Tu, mitochondrial
Short name:
EF-Tu
Alternative name(s):
P43
Gene namesi
Name:TUFM
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 16

Organism-specific databases

HGNCiHGNC:12420. TUFM.

Subcellular locationi

GO - Cellular componenti

  1. extracellular vesicular exosome Source: UniProtKB
  2. membrane Source: UniProtKB
  3. mitochondrial nucleoid Source: BHF-UCL
  4. mitochondrion Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Involvement in diseasei

Combined oxidative phosphorylation deficiency 41 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA 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.

See also OMIM:610678
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti336 – 3361R → Q in COXPD4. 1 Publication
VAR_031902

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi610678. phenotype.
Orphaneti254925. Combined oxidative phosphorylation defect type 4.
PharmGKBiPA37082.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 4343Mitochondrion2 PublicationsAdd
BLAST
Chaini44 – 452409Elongation factor Tu, mitochondrialPRO_0000007462Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei79 – 791N6-acetyllysine1 Publication
Modified residuei88 – 881N6-acetyllysine1 Publication
Modified residuei256 – 2561N6-acetyllysine1 Publication
Modified residuei418 – 4181N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP49411.
PaxDbiP49411.
PRIDEiP49411.

2D gel databases

DOSAC-COBS-2DPAGEP49411.
OGPiP49411.
REPRODUCTION-2DPAGEIPI00027107.
SWISS-2DPAGEP49411.
UCD-2DPAGEP49411.

PTM databases

PhosphoSiteiP49411.

Expressioni

Gene expression databases

BgeeiP49411.
CleanExiHS_TUFM.
ExpressionAtlasiP49411. baseline and differential.
GenevestigatoriP49411.

Organism-specific databases

HPAiHPA018991.
HPA024087.

Interactioni

Protein-protein interaction databases

BioGridi113135. 132 interactions.
IntActiP49411. 24 interactions.
MINTiMINT-224570.
STRINGi9606.ENSP00000322439.

Structurei

3D structure databases

ProteinModelPortaliP49411.
SMRiP49411. Positions 24-451.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini55 – 251197tr-type GPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni64 – 718G1PROSITE-ProRule annotation
Regioni105 – 1095G2PROSITE-ProRule annotation
Regioni126 – 1294G3PROSITE-ProRule annotation
Regioni181 – 1844G4PROSITE-ProRule annotation
Regioni219 – 2213G5PROSITE-ProRule annotation

Sequence similaritiesi

Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A subfamily.PROSITE-ProRule annotation
Contains 1 tr-type G (guanine nucleotide-binding) domain.PROSITE-ProRule annotation

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0050.
HOGENOMiHOG000229290.
HOVERGENiHBG001535.
InParanoidiP49411.
KOiK02358.
OrthoDBiEOG73BVCN.
PhylomeDBiP49411.
TreeFamiTF300432.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR000795. 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]
PfamiPF00009. GTP_EFTU. 1 hit.
PF03144. GTP_EFTU_D2. 1 hit.
PF03143. GTP_EFTU_D3. 1 hit.
[Graphical view]
PRINTSiPR00315. ELONGATNFCT.
SUPFAMiSSF50447. SSF50447. 1 hit.
SSF50465. SSF50465. 1 hit.
SSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00485. EF-Tu. 1 hit.
PROSITEiPS00301. G_TR_1. 1 hit.
PS51722. G_TR_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P49411-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAATLLRAT PHFSGLAAGR TFLLQGLLRL LKAPALPLLC RGLAVEAKKT
60 70 80 90 100
YVRDKPHVNV GTIGHVDHGK TTLTAAITKI LAEGGGAKFK KYEEIDNAPE
110 120 130 140 150
ERARGITINA AHVEYSTAAR HYAHTDCPGH ADYVKNMITG TAPLDGCILV
160 170 180 190 200
VAANDGPMPQ TREHLLLARQ IGVEHVVVYV NKADAVQDSE MVELVELEIR
210 220 230 240 250
ELLTEFGYKG EETPVIVGSA LCALEGRDPE LGLKSVQKLL DAVDTYIPVP
260 270 280 290 300
ARDLEKPFLL PVEAVYSVPG RGTVVTGTLE RGILKKGDEC ELLGHSKNIR
310 320 330 340 350
TVVTGIEMFH KSLERAEAGD NLGALVRGLK REDLRRGLVM VKPGSIKPHQ
360 370 380 390 400
KVEAQVYILS KEEGGRHKPF VSHFMPVMFS LTWDMACRII LPPEKELAMP
410 420 430 440 450
GEDLKFNLIL RQPMILEKGQ RFTLRDGNRT IGTGLVTNTL AMTEEEKNIK

WG
Length:452
Mass (Da):49,542
Last modified:October 1, 1996 - v2
Checksum:iE37274ABFFDB5FC7
GO

Sequence cautioni

The sequence AAC60647.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence AAH01633.2 differs from that shown. Reason: Erroneous initiation. Curated
The sequence AAH10041.2 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti195 – 1973Missing in AAC60647 (PubMed:7828719).Curated
Sequence conflicti384 – 3841D → N in AAB00499 (PubMed:8547323).Curated
Sequence conflicti384 – 3841D → N in CAA72493 (Ref. 9) Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti336 – 3361R → Q in COXPD4. 1 Publication
VAR_031902

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiS62767.
S68466.
RefSeqiNP_003312.3. NM_003321.4.
UniGeneiHs.12084.

Genome annotation databases

EnsembliENST00000313511; ENSP00000322439; ENSG00000178952.
GeneIDi7284.
KEGGihsa:7284.
UCSCiuc002drh.2. human.

Polymorphism databases

DMDMi1706611.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiS62767.
S68466.
RefSeqiNP_003312.3. NM_003321.4.
UniGeneiHs.12084.

3D structure databases

ProteinModelPortaliP49411.
SMRiP49411. Positions 24-451.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi113135. 132 interactions.
IntActiP49411. 24 interactions.
MINTiMINT-224570.
STRINGi9606.ENSP00000322439.

PTM databases

PhosphoSiteiP49411.

Polymorphism databases

DMDMi1706611.

2D gel databases

DOSAC-COBS-2DPAGEP49411.
OGPiP49411.
REPRODUCTION-2DPAGEIPI00027107.
SWISS-2DPAGEP49411.
UCD-2DPAGEP49411.

Proteomic databases

MaxQBiP49411.
PaxDbiP49411.
PRIDEiP49411.

Protocols and materials databases

DNASUi7284.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000313511; ENSP00000322439; ENSG00000178952.
GeneIDi7284.
KEGGihsa:7284.
UCSCiuc002drh.2. human.

Organism-specific databases

CTDi7284.
GeneCardsiGC16M028853.
HGNCiHGNC:12420. TUFM.
HPAiHPA018991.
HPA024087.
MIMi602389. gene.
610678. phenotype.
neXtProtiNX_P49411.
Orphaneti254925. Combined oxidative phosphorylation defect type 4.
PharmGKBiPA37082.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0050.
HOGENOMiHOG000229290.
HOVERGENiHBG001535.
InParanoidiP49411.
KOiK02358.
OrthoDBiEOG73BVCN.
PhylomeDBiP49411.
TreeFamiTF300432.

Enzyme and pathway databases

ReactomeiREACT_267677. Mitochondrial translation elongation.
SignaLinkiP49411.

Miscellaneous databases

GeneWikiiTUFM.
GenomeRNAii7284.
NextBioi28481.
PROiP49411.
SOURCEiSearch...

Gene expression databases

BgeeiP49411.
CleanExiHS_TUFM.
ExpressionAtlasiP49411. baseline and differential.
GenevestigatoriP49411.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR000795. 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]
PfamiPF00009. GTP_EFTU. 1 hit.
PF03144. GTP_EFTU_D2. 1 hit.
PF03143. GTP_EFTU_D3. 1 hit.
[Graphical view]
PRINTSiPR00315. ELONGATNFCT.
SUPFAMiSSF50447. SSF50447. 1 hit.
SSF50465. SSF50465. 1 hit.
SSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00485. EF-Tu. 1 hit.
PROSITEiPS00301. G_TR_1. 1 hit.
PS51722. G_TR_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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, 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  13. "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.

Entry informationi

Entry nameiEFTU_HUMAN
AccessioniPrimary (citable) accession number: P49411
Secondary accession number(s): O15276
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: October 1, 1996
Last modified: March 4, 2015
This is version 160 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 16
    Human chromosome 16: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.