GFM1

Protein identityUniProt · HPA

UniProt accession

Q96RP9

Gene

GFM1

Ensembl

ENSG00000168827

Chromosome

3

Canonical length

751 aa

Protein class

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

Subcellular location

Nucleoplasm,Mitochondria

OverviewNCBI Gene

Eukaryotes contain two protein translational systems, one in the cytoplasm and one in the mitochondria. Mitochondrial translation is crucial for maintaining mitochondrial function and mutations in this system lead to a breakdown in the respiratory chain-oxidative phosphorylation system and to impaired maintenance of mitochondrial DNA. This gene encodes one of the mitochondrial translation elongation factors. Its role in the regulation of normal mitochondrial function and in different disease states attributed to mitochondrial dysfunction is not known. [provided by RefSeq, Jul 2008]

Canonical amino-acid sequenceUniProt

751 residues, UniProt reviewed canonical sequence.

>Q96RP9|GFM1
     1  MRLLGAAAVA ALGRGRAPAS LGWQRKQVNW KACRWSSSGV IPNEKIRNIG ISAHIDSGKT
    61  TLTERVLYYT GRIAKMHEVK GKDGVGAVMD SMELERQRGI TIQSAATYTM WKDVNINIID
   121  TPGHVDFTIE VERALRVLDG AVLVLCAVGG VQCQTMTVNR QMKRYNVPFL TFINKLDRMG
   181  SNPARALQQM RSKLNHNAAF MQIPMGLEGN FKGIVDLIEE RAIYFDGDFG QIVRYGEIPA
   241  ELRAAATDHR QELIECVANS DEQLGEMFLE EKIPSISDLK LAIRRATLKR SFTPVFLGSA
   301  LKNKGVQPLL DAVLEYLPNP SEVQNYAILN KEDDSKEKTK ILMNSSRDNS HPFVGLAFKL
   361  EVGRFGQLTY VRSYQGELKK GDTIYNTRTR KKVRLQRLAR MHADMMEDVE EVYAGDICAL
   421  FGIDCASGDT FTDKANSGLS MESIHVPDPV ISIAMKPSNK NDLEKFSKGI GRFTREDPTF
   481  KVYFDTENKE TVISGMGELH LEIYAQRLER EYGCPCITGK PKVAFRETIT APVPFDFTHK
   541  KQSGGAGQYG KVIGVLEPLD PEDYTKLEFS DETFGSNIPK QFVPAVEKGF LDACEKGPLS
   601  GHKLSGLRFV LQDGAHHMVD SNEISFIRAG EGALKQALAN ATLCILEPIM AVEVVAPNEF
   661  QGQVIAGINR RHGVITGQDG VEDYFTLYAD VPLNDMFGYS TELRSCTEGK GEYTMEYSRY
   721  QPCLPSTQED VINKYLEATG QLPVKKGKAK N

LocalizationUniProt · AlphaFold · HPA

Whether an antibody against GFM1 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)

0.27

Highest tissue expression

59 nTPM

Expression across tissuesHPA

DiseaseUniProt · ClinVar · IEDB · PubMed

Four sources answering four different questions about GFM1.

Disease | AllUniProt

Conditions GFM1 is implicated in, by any mechanism.

• Combined oxidative phosphorylation deficiency 1 (COXPD1) MIM:609060

Disease | GeneticClinVar

202 pathogenic / likely-pathogenic of 1,007 ClinVar records.

Conditions with pathogenic or likely-pathogenic variants.

• Hepatoencephalopathy due to combined oxidative phosphorylation defect type 1
• GFM1-related disorder
• See cases
• Combined oxidative phosphorylation deficiency
• Malignant tumor of urinary bladder

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)

0.8

gnomAD pLI

0

gnomAD missense Z

1.28

DepMap mean gene effect

-0.42

DepMap dependency class

selective

Cancer expressionTCGA

Across TCGA tumor cohorts, this protein is over-expressed in roughly 14% of surveyed tumor types (aggregate summary; per-cohort expression, alteration, and survival load in the interactive view).

OntologyGO

Biological processes

• mitochondrial translational elongation

Molecular functions

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

Cellular components

• mitochondrial matrix
• mitochondrion

Protein domainsUniProt · Pfam · InterPro

• Elongation factor EFG, domain V-like
• Translational (tr)-type GTP-binding domain
• Translation elongation factor EFTu-like, domain 2
• Small GTP-binding domain
• Translation elongation factor EFG/EF2, domain IV
• Translation protein, beta-barrel domain superfamily
• Elongation factor G, domain III
• Small ribosomal subunit protein uS5 domain 2-type fold, subgroup
• Ribosomal protein uS5 domain 2-type superfamily
• P-loop containing nucleoside triphosphate hydrolase
• Tr-type G domain, conserved site
• EF-G domain III/V-like
• EFG, domain V
• Elongation Factor G, domain II
• Elongation factor Tu GTP binding domain
• Elongation factor G C-terminus
• Elongation factor Tu domain 2
• Elongation factor G, domain IV
• Elongation Factor G, domain III
• Translation elongation factor EFG/EF2
• Elongation factor G, domain IV

KeywordsUniProt

• Acetylation
• Elongation factor
• GTP-binding
• Hydrolase
• Mitochondrion
• Nucleotide-binding
• Phosphoprotein
• Primary mitochondrial disease
• Protein biosynthesis
• Transit peptide

InteractionsUniProt · HPA

Protein binding partners of GFM1 in the human serome: UniProt-annotated complex subunits plus reported interactors. Each links to its own Seroatlas record.

• MRPL21
• MRPS24
• NDUFS7
• TRIM63