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Q8BFR5

- EFTU_MOUSE

UniProt

Q8BFR5 - EFTU_MOUSE

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Protein

Elongation factor Tu, mitochondrial

Gene

Tufm

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 3 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.By similarity

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. translation elongation factor activity Source: UniProtKB

GO - Biological processi

  1. 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_270125. Mitochondrial translation elongation.

Names & Taxonomyi

Protein namesi
Recommended name:
Elongation factor Tu, mitochondrial
Gene namesi
Name:Tufm
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 7

Organism-specific databases

MGIiMGI:1923686. Tufm.

Subcellular locationi

Mitochondrion By similarity

GO - Cellular componenti

  1. mitochondrial inner membrane Source: MGI
  2. mitochondrion Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 4343MitochondrionBy similarityAdd
BLAST
Chaini44 – 452409Elongation factor Tu, mitochondrialPRO_0000007463Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ8BFR5.
PaxDbiQ8BFR5.
PRIDEiQ8BFR5.

2D gel databases

REPRODUCTION-2DPAGEQ6P919.
Q8BFR5.

PTM databases

PhosphoSiteiQ8BFR5.

Expressioni

Gene expression databases

BgeeiQ8BFR5.
CleanExiMM_TUFM.
GenevestigatoriQ8BFR5.

Interactioni

Protein-protein interaction databases

BioGridi231459. 4 interactions.
IntActiQ8BFR5. 8 interactions.
MINTiMINT-1860932.

Structurei

3D structure databases

ProteinModelPortaliQ8BFR5.
SMRiQ8BFR5. Positions 55-451.
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.
GeneTreeiENSGT00550000074682.
HOGENOMiHOG000229290.
HOVERGENiHBG001535.
InParanoidiQ8BFR5.
KOiK02358.
OMAiGTEMCMP.
OrthoDBiEOG73BVCN.
PhylomeDBiQ8BFR5.
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]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q8BFR5-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MAAATLLRAT PRFSGLCASP TPFLQGRLRP LKAPASPFLC 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 TREHLLLAKQ IGVEHVVVYV NKADAVQDSE MVELVELEIR
210 220 230 240 250
ELLTEFGYKG EETPVIVGSA LCALEQRDPE LGVKSVQKLL DAVDTYIPVP
260 270 280 290 300
TRDLDKPFLL PVESVYSIPG RGTVVTGTLE RGILKKGDEC ELLGHNKNIR
310 320 330 340 350
TVVTGIEMFH KSLERAEAGD NLGALVRGLK REDLRRGLVM VKPGSIQPHQ
360 370 380 390 400
KVEAQVYILS KEEGGRHKPF VSHFMPVMFS LTWDMACRVI LPPGKELAMP
410 420 430 440 450
GEDLKLSLIL RQPMILEKGQ RFTLRDGNKT IGTGLVTDVP AMTEEDKNIK

WS
Length:452
Mass (Da):49,508
Last modified:March 1, 2003 - v1
Checksum:iF8687A05FFCB337D
GO
Isoform 2 (identifier: Q8BFR5-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     357-452: YILSKEEGGR...TEEDKNIKWS → RAPVLSGFPC...TCHAWRGLEA

Note: No experimental confirmation available.

Show »
Length:435
Mass (Da):47,222
Checksum:i6821088F0D8A5145
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei357 – 45296YILSK…NIKWS → RAPVLSGFPCLEAGLVAKPF HPYCFSPLGLYPQQGGRWPP QTLCISFHARHVLPDLGHGL SSHLASREGTCHAWRGLEA in isoform 2. 1 PublicationVSP_013942Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS21830.1. [Q8BFR5-1]
CCDS52398.1. [Q8BFR5-2]
RefSeqiNP_001157185.1. NM_001163713.1. [Q8BFR5-2]
NP_766333.1. NM_172745.3. [Q8BFR5-1]
UniGeneiMm.197829.

Genome annotation databases

EnsembliENSMUST00000098048; ENSMUSP00000095656; ENSMUSG00000073838. [Q8BFR5-1]
ENSMUST00000106392; ENSMUSP00000102000; ENSMUSG00000073838. [Q8BFR5-2]
GeneIDi233870.
KEGGimmu:233870.
UCSCiuc009jro.2. mouse. [Q8BFR5-1]
uc009jrq.2. mouse. [Q8BFR5-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
CCDSi CCDS21830.1. [Q8BFR5-1 ]
CCDS52398.1. [Q8BFR5-2 ]
RefSeqi NP_001157185.1. NM_001163713.1. [Q8BFR5-2 ]
NP_766333.1. NM_172745.3. [Q8BFR5-1 ]
UniGenei Mm.197829.

3D structure databases

ProteinModelPortali Q8BFR5.
SMRi Q8BFR5. Positions 55-451.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 231459. 4 interactions.
IntActi Q8BFR5. 8 interactions.
MINTi MINT-1860932.

PTM databases

PhosphoSitei Q8BFR5.

2D gel databases

REPRODUCTION-2DPAGE Q6P919.
Q8BFR5.

Proteomic databases

MaxQBi Q8BFR5.
PaxDbi Q8BFR5.
PRIDEi Q8BFR5.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000098048 ; ENSMUSP00000095656 ; ENSMUSG00000073838 . [Q8BFR5-1 ]
ENSMUST00000106392 ; ENSMUSP00000102000 ; ENSMUSG00000073838 . [Q8BFR5-2 ]
GeneIDi 233870.
KEGGi mmu:233870.
UCSCi uc009jro.2. mouse. [Q8BFR5-1 ]
uc009jrq.2. mouse. [Q8BFR5-2 ]

Organism-specific databases

CTDi 7284.
MGIi MGI:1923686. Tufm.

Phylogenomic databases

eggNOGi COG0050.
GeneTreei ENSGT00550000074682.
HOGENOMi HOG000229290.
HOVERGENi HBG001535.
InParanoidi Q8BFR5.
KOi K02358.
OMAi GTEMCMP.
OrthoDBi EOG73BVCN.
PhylomeDBi Q8BFR5.
TreeFami TF300432.

Enzyme and pathway databases

Reactomei REACT_270125. Mitochondrial translation elongation.

Miscellaneous databases

NextBioi 381887.
PROi Q8BFR5.
SOURCEi Search...

Gene expression databases

Bgeei Q8BFR5.
CleanExi MM_TUFM.
Genevestigatori Q8BFR5.

Family and domain databases

Gene3Di 3.40.50.300. 1 hit.
InterProi IPR000795. 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 ]
Pfami PF00009. GTP_EFTU. 1 hit.
PF03144. GTP_EFTU_D2. 1 hit.
PF03143. GTP_EFTU_D3. 1 hit.
[Graphical view ]
PRINTSi PR00315. ELONGATNFCT.
SUPFAMi SSF50447. SSF50447. 1 hit.
SSF50465. SSF50465. 1 hit.
SSF52540. SSF52540. 1 hit.
TIGRFAMsi TIGR00485. EF-Tu. 1 hit.
PROSITEi PS00301. G_TR_1. 1 hit.
PS51722. G_TR_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiEFTU_MOUSE
AccessioniPrimary (citable) accession number: Q8BFR5
Secondary accession number(s): Q497E7, Q6P919
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: March 1, 2003
Last modified: November 26, 2014
This is version 106 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3