GFM2

Protein identityUniProt · HPA

UniProt accession

Q969S9

Gene

GFM2

Ensembl

ENSG00000164347

Chromosome

5

Canonical length

779 aa

Protein class

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

Subcellular location

Nucleoplasm,Midbody ring,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, which is a GTPase that plays a role at the termination of mitochondrial translation by mediating the disassembly of ribosomes from messenger RNA . Its role in the regulation of normal mitochondrial function and in disease states attributed to mitochondrial dysfunction is not known. Alternative splicing results in multiple transcript variants encoding distinct isoforms. [provided by RefSeq, Jul 2013]

Canonical amino-acid sequenceUniProt

779 residues, UniProt reviewed canonical sequence.

>Q969S9|GFM2
     1  MLTNLRIFAM SHQTIPSVYI NNICCYKIRA SLKRLKPHVP LGRNCSSLPG LIGNDIKSLH
    61  SIINPPIAKI RNIGIMAHID AGKTTTTERI LYYSGYTRSL GDVDDGDTVT DFMAQERERG
   121  ITIQSAAVTF DWKGYRVNLI DTPGHVDFTL EVERCLRVLD GAVAVFDASA GVEAQTLTVW
   181  RQADKHNIPR ICFLNKMDKT GASFKYAVES IREKLKAKPL LLQLPIGEAK TFKGVVDVVM
   241  KEKLLWNCNS NDGKDFERKP LLEMNDPELL KETTEARNAL IEQVADLDDE FADLVLEEFS
   301  ENFDLLPAEK LQTAIHRVTL AQTAVPVLCG SALKNKGIQP LLDAVTMYLP SPEERNYEFL
   361  QWYKDDLCAL AFKVLHDKQR GPLVFMRIYS GTIKPQLAIH NINGNCTERI SRLLLPFADQ
   421  HVEIPSLTAG NIALTVGLKH TATGDTIVSS KSSALAAARR AEREGEKKHR QNNEAERLLL
   481  AGVEIPEPVF FCTIEPPSLS KQPDLEHALK CLQREDPSLK VRLDPDSGQT VLCGMGELHI
   541  EIIHDRIKRE YGLETYLGPL QVAYRETILN SVRATDTLDR TLGDKRHLVT VEVEARPIET
   601  SSVMPVIEFE YAESINEGLL KVSQEAIENG IHSACLQGPL LGSPIQDVAI TLHSLTIHPG
   661  TSTTMISACV SRCVQKALKK ADKQVLEPLM NLEVTVARDY LSPVLADLAQ RRGNIQEIQT
   721  RQDNKVVIGF VPLAEIMGYS TVLRTLTSGS ATFALELSTY QAMNPQDQNT LLNRRSGLT

LocalizationUniProt · AlphaFold · HPA

Whether an antibody against GFM2 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)

0.28

Highest tissue expression

36 nTPM

Expression across tissuesHPA

DiseaseUniProt · ClinVar · IEDB · PubMed

Four sources answering four different questions about GFM2.

Disease | AllUniProt

Conditions GFM2 is implicated in, by any mechanism.

• Combined oxidative phosphorylation deficiency 39 (COXPD39) MIM:618397

Disease | GeneticClinVar

16 pathogenic / likely-pathogenic of 443 ClinVar records.

Conditions with pathogenic or likely-pathogenic variants.

• Combined oxidative phosphorylation deficiency 39
• Mitochondrial disease
• See cases
• GFM2-related disorder

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)

1.04

gnomAD pLI

0

gnomAD missense Z

0.8

DepMap mean gene effect

-0.25

DepMap dependency class

selective

Cancer expressionTCGA

Across TCGA tumor cohorts, this protein is over-expressed in roughly 4% of surveyed tumor types (aggregate summary; per-cohort expression, alteration, and survival load in the interactive view).

OntologyGO

Biological processes

• mitochondrial translation
• mitochondrial translational termination
• ribosome disassembly

Molecular functions

• GTP binding
• GTPase activity

Cellular components

• mitochondrial matrix
• mitochondrion

Protein domainsUniProt · Pfam · InterPro

• Elongation factor EFG, domain V-like
• Translational (tr)-type GTP-binding domain
• 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 G-like, domain II
• Elongation factor Tu GTP binding domain
• Elongation factor G C-terminus
• Elongation factor G, domain IV
• Elongation Factor G, domain III
• Elongation factor G domain 2
• Ribosome-releasing factor 2, mitochondrial

KeywordsUniProt

• GTP-binding
• Hydrolase
• Mitochondrion
• Nucleotide-binding
• Primary mitochondrial disease
• Protein biosynthesis