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Q8BFR5 (EFTU_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 100. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Elongation factor Tu, mitochondrial
Gene names
Name:Tufm
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

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 By similarity.

Subcellular location

Mitochondrion By similarity.

Sequence similarities

Belongs to the GTP-binding elongation factor family. EF-Tu/EF-1A subfamily.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8BFR5-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q8BFR5-2)

The sequence of this isoform differs from the canonical sequence as follows:
     357-452: YILSKEEGGR...TEEDKNIKWS → RAPVLSGFPC...TCHAWRGLEA
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 4343Mitochondrion By similarity
Chain44 – 452409Elongation factor Tu, mitochondrial
PRO_0000007463

Regions

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

Amino acid modifications

Modified residue791N6-acetyllysine By similarity
Modified residue881N6-acetyllysine By similarity
Modified residue2561N6-acetyllysine By similarity
Modified residue4181N6-acetyllysine By similarity

Natural variations

Alternative sequence357 – 45296YILSK…NIKWS → RAPVLSGFPCLEAGLVAKPF HPYCFSPLGLYPQQGGRWPP QTLCISFHARHVLPDLGHGL SSHLASREGTCHAWRGLEA in isoform 2.
VSP_013942

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: F8687A05FFCB337D

FASTA45249,508
        10         20         30         40         50         60 
MAAATLLRAT PRFSGLCASP TPFLQGRLRP LKAPASPFLC RGLAVEAKKT YVRDKPHVNV 

        70         80         90        100        110        120 
GTIGHVDHGK TTLTAAITKI LAEGGGAKFK KYEEIDNAPE ERARGITINA AHVEYSTAAR 

       130        140        150        160        170        180 
HYAHTDCPGH ADYVKNMITG TAPLDGCILV VAANDGPMPQ TREHLLLAKQ IGVEHVVVYV 

       190        200        210        220        230        240 
NKADAVQDSE MVELVELEIR ELLTEFGYKG EETPVIVGSA LCALEQRDPE LGVKSVQKLL 

       250        260        270        280        290        300 
DAVDTYIPVP TRDLDKPFLL PVESVYSIPG RGTVVTGTLE RGILKKGDEC ELLGHNKNIR 

       310        320        330        340        350        360 
TVVTGIEMFH KSLERAEAGD NLGALVRGLK REDLRRGLVM VKPGSIQPHQ KVEAQVYILS 

       370        380        390        400        410        420 
KEEGGRHKPF VSHFMPVMFS LTWDMACRVI LPPGKELAMP GEDLKLSLIL RQPMILEKGQ 

       430        440        450 
RFTLRDGNKT IGTGLVTDVP AMTEEDKNIK WS 

« Hide

Isoform 2 [UniParc].

Checksum: 6821088F0D8A5145
Show »

FASTA43547,222

References

« Hide 'large scale' references
[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Strain: C57BL/6J.
Tissue: Bone marrow, Heart and Tongue.
[2]"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] (ISOFORMS 1 AND 2).
Tissue: Kidney.
[3]Lubec G., Klug S., Kang S.U.
Submitted (APR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 91-102; 105-120; 210-227; 239-271; 316-327 AND 352-361, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: C57BL/6.
Tissue: Brain and Hippocampus.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK075857 mRNA. Translation: BAC36008.1.
AK084724 mRNA. Translation: BAC39263.1.
AK153135 mRNA. Translation: BAE31747.1.
AK152858 mRNA. Translation: BAE31551.1.
BC060959 mRNA. Translation: AAH60959.1.
BC100596 mRNA. Translation: AAI00597.1.
RefSeqNP_001157185.1. NM_001163713.1.
NP_766333.1. NM_172745.3.
UniGeneMm.197829.

3D structure databases

ProteinModelPortalQ8BFR5.
SMRQ8BFR5. Positions 55-451.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid231459. 3 interactions.
IntActQ8BFR5. 8 interactions.
MINTMINT-1860932.

PTM databases

PhosphoSiteQ8BFR5.

2D gel databases

REPRODUCTION-2DPAGEQ6P919.
Q8BFR5.

Proteomic databases

PaxDbQ8BFR5.
PRIDEQ8BFR5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000098048; ENSMUSP00000095656; ENSMUSG00000073838. [Q8BFR5-1]
ENSMUST00000106392; ENSMUSP00000102000; ENSMUSG00000073838. [Q8BFR5-2]
GeneID233870.
KEGGmmu:233870.
UCSCuc009jro.2. mouse. [Q8BFR5-1]
uc009jrq.2. mouse. [Q8BFR5-2]

Organism-specific databases

CTD7284.
MGIMGI:1923686. Tufm.

Phylogenomic databases

eggNOGCOG0050.
GeneTreeENSGT00550000074682.
HOGENOMHOG000229290.
HOVERGENHBG001535.
InParanoidQ8BFR5.
KOK02358.
OMANIKMVVN.
OrthoDBEOG73BVCN.
PhylomeDBQ8BFR5.
TreeFamTF300432.

Gene expression databases

BgeeQ8BFR5.
CleanExMM_TUFM.
GenevestigatorQ8BFR5.

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

NextBio381887.
PROQ8BFR5.
SOURCESearch...

Entry information

Entry nameEFTU_MOUSE
AccessionPrimary (citable) accession number: Q8BFR5
Secondary accession number(s): Q497E7, Q6P919
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: March 1, 2003
Last modified: April 16, 2014
This is version 100 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot