TUFM

Protein identityUniProt · HPA

UniProt accession

P49411

Gene

TUFM

Ensembl

ENSG00000178952

Chromosome

16

Canonical length

455 aa

Protein class

Disease related genes, Human disease related genes, Metabolic proteins, Plasma proteins, Predicted intracellular proteins

Subcellular location

Mitochondria

OverviewNCBI Gene

This gene encodes a protein which participates in protein translation in mitochondria. Mutations in this gene have been associated with combined oxidative phosphorylation deficiency resulting in lactic acidosis and fatal encephalopathy. A pseudogene has been identified on chromosome 17. [provided by RefSeq, Jul 2008]

Canonical amino-acid sequenceUniProt

455 residues, UniProt reviewed canonical sequence.

>P49411|TUFM
     1  MTTMAAATLL RATPHFSGLA AGRTFLLQGL LRLLKAPALP LLCRGLAVEA KKTYVRDKPH
    61  VNVGTIGHVD HGKTTLTAAI TKILAEGGGA KFKKYEEIDN APEERARGIT INAAHVEYST
   121  AARHYAHTDC PGHADYVKNM ITGTAPLDGC ILVVAANDGP MPQTREHLLL ARQIGVEHVV
   181  VYVNKADAVQ DSEMVELVEL EIRELLTEFG YKGEETPVIV GSALCALEGR DPELGLKSVQ
   241  KLLDAVDTYI PVPARDLEKP FLLPVEAVYS VPGRGTVVTG TLERGILKKG DECELLGHSK
   301  NIRTVVTGIE MFHKSLERAE AGDNLGALVR GLKREDLRRG LVMVKPGSIK PHQKVEAQVY
   361  ILSKEEGGRH KPFVSHFMPV MFSLTWDMAC RIILPPEKEL AMPGEDLKFN LILRQPMILE
   421  KGQRFTLRDG NRTIGTGLVT NTLAMTEEEK NIKWG

LocalizationUniProt · AlphaFold · HPA

Whether an antibody against TUFM can act on the native protein depends on physical access: surface and secreted proteins are reachable by circulating antibodies, intracellular proteins usually are not.

Antibody reachability

Intracellular

Secreted

No

Transmembrane segments

0

Mean surface accessibility (rSASA)

0.29

Highest tissue expression

228 nTPM

Expression across tissuesHPA

DiseaseUniProt · ClinVar · IEDB · PubMed

Four sources answering four different questions about TUFM.

Disease | AllUniProt

Conditions TUFM is implicated in, by any mechanism.

• Combined oxidative phosphorylation deficiency 4 (COXPD4) MIM:610678

Disease | GeneticClinVar

6 pathogenic / likely-pathogenic of 241 ClinVar records.

Conditions with pathogenic or likely-pathogenic variants.

• Combined oxidative phosphorylation defect type 4

Genetic constraint and essentialitygnomAD · DepMap

Does the body need this protein intact? Low LOEUF or a strong DepMap dependency means loss or blockade of the protein is likely to be felt.

gnomAD LOEUF (loss-of-function intolerance)

0.74

gnomAD pLI

0

gnomAD missense Z

1.4

DepMap mean gene effect

-0.4

DepMap dependency class

selective

Cancer expressionTCGA

Across TCGA tumor cohorts, this protein is over-expressed in roughly 6% of surveyed tumor types (aggregate summary; per-cohort expression, alteration, and survival load in the interactive view).

OntologyGO

Biological processes

• mitochondrial large ribosomal subunit assembly
• mitochondrial translation
• mitochondrial translational elongation
• translational elongation

Molecular functions

• GTP binding
• GTPase activity
• magnesium ion binding
• RNA binding
• translation elongation factor activity

Cellular components

• extracellular exosome
• membrane
• mitochondrial nucleoid
• mitochondrial outer membrane
• mitochondrion

Protein domainsUniProt · Pfam · InterPro

• Translational (tr)-type GTP-binding domain
• Translation elongation factor EFTu-like, domain 2
• Translation protein, beta-barrel domain superfamily
• Translation elongation factor EF1A/initiation factor IF2gamma, C-terminal
• P-loop containing nucleoside triphosphate hydrolase
• Tr-type G domain, conserved site
• Elongation factor Tu GTPase
• Elongation factor Tu GTP binding domain
• Elongation factor Tu domain 2
• Translation elongation factor EFTu/EF1A, C-terminal
• Translation elongation factor EFTu/EF1A, bacterial/organelle
• Elongation factor Tu, domain 2
• Elongation factor Tu (EF-Tu), GTP-binding domain
• Elongation factor Tu C-terminal domain

KeywordsUniProt

• Acetylation
• Elongation factor
• GTP-binding
• Host-virus interaction
• Hydrolase
• Magnesium
• Metal-binding
• Mitochondrion
• Nucleotide-binding
• Phosphoprotein
• Primary mitochondrial disease
• Protein biosynthesis
• Transit peptide

InteractionsUniProt · HPA

Protein binding partners of TUFM in the human serome: UniProt-annotated complex subunits plus reported interactors. Each links to its own Seroatlas record.

• ATG16L1
• NLRX1