TUFM

Mitochondrial protein and coding gene in humans
TUFM
Identifiers
AliasesTUFM, COXPD4, EF-TuMT, EFTU, P43, Tu translation elongation factor, mitochondrial
External IDsOMIM: 602389; MGI: 1923686; HomoloGene: 2490; GeneCards: TUFM; OMA:TUFM - orthologs
Gene location (Human)
Chromosome 16 (human)
Chr.Chromosome 16 (human)[1]
Chromosome 16 (human)
Genomic location for TUFM
Genomic location for TUFM
Band16p11.2Start28,842,411 bp[1]
End28,846,348 bp[1]
Gene location (Mouse)
Chromosome 7 (mouse)
Chr.Chromosome 7 (mouse)[2]
Chromosome 7 (mouse)
Genomic location for TUFM
Genomic location for TUFM
Band7|7 F3Start126,086,533 bp[2]
End126,089,903 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • mucosa of transverse colon

  • apex of heart

  • right adrenal gland

  • left adrenal gland

  • body of pancreas

  • body of stomach

  • right adrenal cortex

  • left adrenal cortex

  • olfactory zone of nasal mucosa

  • granulocyte
Top expressed in
  • right kidney

  • muscle of thigh

  • neural layer of retina

  • yolk sac

  • lip

  • embryo

  • dentate gyrus of hippocampal formation granule cell

  • ventricular zone

  • embryo

  • blastocyst
More reference expression data
BioGPS
More reference expression data
Gene ontology
Molecular function
  • nucleotide binding
  • GTP binding
  • protein binding
  • translation elongation factor activity
  • RNA binding
  • GTPase activity
Cellular component
  • mitochondrial nucleoid
  • extracellular exosome
  • intracellular anatomical structure
  • mitochondrion
  • membrane
  • mitochondrial inner membrane
  • myelin sheath
  • synapse
Biological process
  • translational elongation
  • protein biosynthesis
  • response to ethanol
  • mitochondrial translational elongation
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

7284

233870

Ensembl

ENSG00000178952

ENSMUSG00000073838

UniProt

P49411

Q8BFR5

RefSeq (mRNA)

NM_003321
NM_001365360

NM_001163713
NM_172745

RefSeq (protein)

NP_003312
NP_001352289

NP_001157185
NP_766333

Location (UCSC)Chr 16: 28.84 – 28.85 MbChr 7: 126.09 – 126.09 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Elongation factor Tu, mitochondrial is a protein that in humans is encoded by the TUFM gene. It is an EF-Tu homolog.[5][6][7]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000178952 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000073838 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Ling M, Merante F, Chen HS, Duff C, Duncan AM, Robinson BH (Nov 1997). "The human mitochondrial elongation factor tu (EF-Tu) gene: cDNA sequence, genomic localization, genomic structure, and identification of a pseudogene". Gene. 197 (1–2): 325–36. doi:10.1016/S0378-1119(97)00279-5. PMID 9332382.
  6. ^ Shah ZH, Migliosi V, Miller SC, Wang A, Friedman TB, Jacobs HT (Jun 1998). "Chromosomal locations of three human nuclear genes (RPSM12, TUFM, and AFG3L1) specifying putative components of the mitochondrial gene expression apparatus". Genomics. 48 (3): 384–8. doi:10.1006/geno.1997.5166. PMID 9545647.
  7. ^ "Entrez Gene: TUFM Tu translation elongation factor, mitochondrial".

Further reading

  • Wells J, Henkler F, Leversha M, Koshy R (1995). "A mitochondrial elongation factor-like protein is over-expressed in tumours and differentially expressed in normal tissues". FEBS Lett. 358 (2): 119–25. doi:10.1016/0014-5793(94)01403-N. PMID 7828719. S2CID 24769779.
  • Woriax VL, Burkhart W, Spremulli LL (1996). "Cloning, sequence analysis and expression of mammalian mitochondrial protein synthesis elongation factor Tu". Biochim. Biophys. Acta. 1264 (3): 347–56. doi:10.1016/0167-4781(95)00176-x. PMID 8547323.
  • Chang SY, Park SG, Kim S, Kang CY (2002). "Interaction of the C-terminal domain of p43 and the alpha subunit of ATP synthase. Its functional implication in endothelial cell proliferation". J. Biol. Chem. 277 (10): 8388–94. doi:10.1074/jbc.M108792200. PMID 11741979.
  • Andersen JS, Lyon CE, Fox AH, et al. (2002). "Directed proteomic analysis of the human nucleolus". Curr. Biol. 12 (1): 1–11. doi:10.1016/S0960-9822(01)00650-9. PMID 11790298. S2CID 14132033.
  • Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
  • Blagoev B, Kratchmarova I, Ong SE, et al. (2003). "A proteomics strategy to elucidate functional protein-protein interactions applied to EGF signaling". Nat. Biotechnol. 21 (3): 315–8. doi:10.1038/nbt790. PMID 12577067. S2CID 26838266.
  • Gevaert K, Goethals M, Martens L, et al. (2004). "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides". Nat. Biotechnol. 21 (5): 566–9. doi:10.1038/nbt810. PMID 12665801. S2CID 23783563.
  • Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
  • Andersen JS, Lam YW, Leung AK, et al. (2005). "Nucleolar proteome dynamics". Nature. 433 (7021): 77–83. Bibcode:2005Natur.433...77A. doi:10.1038/nature03207. PMID 15635413. S2CID 4344740.
  • Ahmed M, Forsberg J, Bergsten P (2005). "Protein profiling of human pancreatic islets by two-dimensional gel electrophoresis and mass spectrometry". J. Proteome Res. 4 (3): 931–40. doi:10.1021/pr050024a. PMID 15952740.
  • Antonicka H, Sasarman F, Kennaway NG, Shoubridge EA (2006). "The molecular basis for tissue specificity of the oxidative phosphorylation deficiencies in patients with mutations in the mitochondrial translation factor EFG1". Hum. Mol. Genet. 15 (11): 1835–46. doi:10.1093/hmg/ddl106. PMID 16632485.
  • Smeitink JA, Elpeleg O, Antonicka H, et al. (2006). "Distinct clinical phenotypes associated with a mutation in the mitochondrial translation elongation factor EFTs". Am. J. Hum. Genet. 79 (5): 869–77. doi:10.1086/508434. PMC 1698578. PMID 17033963.
  • Valente L, Tiranti V, Marsano RM, et al. (2007). "Infantile encephalopathy and defective mitochondrial DNA translation in patients with mutations of mitochondrial elongation factors EFG1 and EFTu". Am. J. Hum. Genet. 80 (1): 44–58. doi:10.1086/510559. PMC 1785320. PMID 17160893.
  • Ewing RM, Chu P, Elisma F, et al. (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry". Mol. Syst. Biol. 3 (1): 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931.
  • v
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  • 1d2e: CRYSTAL STRUCTURE OF MITOCHONDRIAL EF-TU IN COMPLEX WITH GDP
    1d2e: CRYSTAL STRUCTURE OF MITOCHONDRIAL EF-TU IN COMPLEX WITH GDP
  • 1xb2: Crystal Structure of Bos taurus mitochondrial Elongation Factor Tu/Ts Complex
    1xb2: Crystal Structure of Bos taurus mitochondrial Elongation Factor Tu/Ts Complex


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