Human Gene GFM1 (ENST00000486715.6_7) from GENCODE V47lift37
  Description: G elongation factor mitochondrial 1, transcript variant 2 (from RefSeq NM_024996.7)
Gencode Transcript: ENST00000486715.6_7
Gencode Gene: ENSG00000168827.15_14
Transcript (Including UTRs)
   Position: hg19 chr3:158,362,316-158,413,370 Size: 51,055 Total Exon Count: 18 Strand: +
Coding Region
   Position: hg19 chr3:158,362,424-158,409,256 Size: 46,833 Coding Exon Count: 18 

Page IndexSequence and LinksUniProtKB CommentsPrimersMalaCardsCTD
Gene AllelesRNA-Seq ExpressionMicroarray ExpressionRNA StructureProtein StructureOther Species
GO AnnotationsmRNA DescriptionsPathwaysOther NamesModel InformationMethods
Data last updated at UCSC: 2024-08-22 23:36:26

-  Sequence and Links to Tools and Databases
 
Genomic Sequence (chr3:158,362,316-158,413,370)mRNA (may differ from genome)Protein (751 aa)
Gene SorterGenome BrowserOther Species FASTAVisiGeneGene interactionsTable Schema
AlphaFoldBioGPSEnsemblEntrez GeneExonPrimerGeneCards
HGNCMalacardsMGIOMIMPubMedReactome
UniProtKBWikipediaBioGrid CRISPR DB

-  Comments and Description Text from UniProtKB
  ID: EFGM_HUMAN
DESCRIPTION: RecName: Full=Elongation factor G, mitochondrial; Short=EF-Gmt; AltName: Full=Elongation factor G 1, mitochondrial; Short=mEF-G 1; AltName: Full=Elongation factor G1; Short=hEFG1; Flags: Precursor;
FUNCTION: Mitochondrial GTPase that catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A- site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome. Does not mediate the disassembly of ribosomes from messenger RNA at the termination of mitochondrial protein biosynthesis.
PATHWAY: Protein biosynthesis; polypeptide chain elongation.
SUBCELLULAR LOCATION: Mitochondrion (By similarity).
DISEASE: Defects in GFM1 are the cause of combined oxidative phosphorylation deficiency type 1 (COXPD1) [MIM:609060]. It leads to early fatal progressive hepatoencephalopathy.
SIMILARITY: Belongs to the GTP-binding elongation factor family. EF-G/EF-2 subfamily.
SEQUENCE CAUTION: Sequence=EAW78682.1; Type=Erroneous gene model prediction;
WEB RESOURCE: Name=GeneReviews; URL="http://www.ncbi.nlm.nih.gov/sites/GeneTests/lab/gene/GFM1";

-  Primer design for this transcript
 

Primer3Plus can design qPCR Primers that straddle exon-exon-junctions, which amplify only cDNA, not genomic DNA.
Click here to load the transcript sequence and exon structure into Primer3Plus

Exonprimer can design one pair of Sanger sequencing primers around every exon, located in non-genic sequence.
Click here to open Exonprimer with this transcript

To design primers for a non-coding sequence, zoom to a region of interest and select from the drop-down menu: View > In External Tools > Primer3


-  MalaCards Disease Associations
  MalaCards Gene Search: GFM1
Diseases sorted by gene-association score: combined oxidative phosphorylation deficiency 1* (1680), combined oxidative phosphorylation deficiency (23), amyotrophic lateral sclerosis 9 (10), kidney cortex necrosis (9), amyotrophic lateral sclerosis 3 (8), factor vii deficiency (8), amyotrophic lateral sclerosis 7 (8), heart aneurysm (6), denture stomatitis (6), amyotrophic lateral sclerosis 1 (2)
* = Manually curated disease association

-  Comparative Toxicogenomics Database (CTD)
  The following chemicals interact with this gene           more ... click here to view the complete list

+  Common Gene Haplotype Alleles
  Press "+" in the title bar above to open this section.

-  RNA-Seq Expression Data from GTEx (53 Tissues, 570 Donors)
  Highest median expression: 20.15 RPKM in Brain - Cerebellar Hemisphere
Total median expression: 494.11 RPKM



View in GTEx track of Genome Browser    View at GTEx portal     View GTEx Body Map

+  Microarray Expression Data
  Press "+" in the title bar above to open this section.

-  mRNA Secondary Structure of 3' and 5' UTRs
 
RegionFold EnergyBasesEnergy/Base
Display As
5' UTR -36.40108-0.337 Picture PostScript Text
3' UTR -1158.324114-0.282 Picture PostScript Text

The RNAfold program from the Vienna RNA Package is used to perform the secondary structure predictions and folding calculations. The estimated folding energy is in kcal/mol. The more negative the energy, the more secondary structure the RNA is likely to have.

-  Protein Domain and Structure Information
  InterPro Domains: Graphical view of domain structure
IPR009022 - Elongation_fac_G/III/V
IPR000795 - ProtSyn_GTP-bd
IPR020568 - Ribosomal_S5_D2-typ_fold
IPR014721 - Ribosomal_S5_D2-typ_fold_subgr
IPR005225 - Small_GTP-bd_dom
IPR004540 - Transl_elong_EFG/EF2
IPR000640 - Transl_elong_EFG/EF2_C
IPR005517 - Transl_elong_EFG/EF2_IV
IPR004161 - Transl_elong_EFTu/EF1A_2
IPR009000 - Transl_elong_init/rib_B-barrel

Pfam Domains:
PF00009 - Elongation factor Tu GTP binding domain
PF00679 - Elongation factor G C-terminus
PF03144 - Elongation factor Tu domain 2
PF03764 - Elongation factor G, domain IV
PF14492 - Elongation Factor G, domain III

SCOP Domains:
50447 - Translation proteins
52540 - P-loop containing nucleoside triphosphate hydrolases
54211 - Ribosomal protein S5 domain 2-like
54980 - EF-G C-terminal domain-like

ModBase Predicted Comparative 3D Structure on Q96RP9
FrontTopSide
The pictures above may be empty if there is no ModBase structure for the protein. The ModBase structure frequently covers just a fragment of the protein. You may be asked to log onto ModBase the first time you click on the pictures. It is simplest after logging in to just click on the picture again to get to the specific info on that model.

-  Orthologous Genes in Other Species
  Orthologies between human, mouse, and rat are computed by taking the best BLASTP hit, and filtering out non-syntenic hits. For more distant species reciprocal-best BLASTP hits are used. Note that the absence of an ortholog in the table below may reflect incomplete annotations in the other species rather than a true absence of the orthologous gene.
MouseRatZebrafishD. melanogasterC. elegansS. cerevisiae
No orthologNo orthologNo orthologNo orthologGenome BrowserGenome Browser
Gene DetailsGene Details Gene DetailsGene DetailsGene Details
Gene SorterGene Sorter Gene SorterGene SorterGene Sorter
 RGDEnsembl WormBaseSGD
    Protein SequenceProtein Sequence
    AlignmentAlignment

-  Gene Ontology (GO) Annotations with Structured Vocabulary
  Molecular Function:
GO:0000166 nucleotide binding
GO:0003723 RNA binding
GO:0003746 translation elongation factor activity
GO:0003924 GTPase activity
GO:0005515 protein binding
GO:0005525 GTP binding

Biological Process:
GO:0006412 translation
GO:0006414 translational elongation
GO:0070125 mitochondrial translational elongation

Cellular Component:
GO:0005622 intracellular
GO:0005739 mitochondrion
GO:0005759 mitochondrial matrix


-  Descriptions from all associated GenBank mRNAs
  AK000780 - Homo sapiens cDNA FLJ20773 fis, clone COL06050, highly similar to EFGM_RAT ELONGATION FACTOR G.
AF367998 - Homo sapiens elongation factor G1 (EFG1) mRNA, complete cds; nuclear gene for mitochondrial product.
AF309777 - Homo sapiens elongation factor G (EFG) mRNA, complete cds; nuclear gene for mitochondrial product.
BC049210 - Homo sapiens G elongation factor, mitochondrial 1, mRNA (cDNA clone MGC:51775 IMAGE:5574223), complete cds.
AK315031 - Homo sapiens cDNA, FLJ95973, highly similar to Homo sapiens G elongation factor, mitochondrial 1 (GFM1), nuclear gene encoding mitochondrial protein, mRNA.
CU690604 - Synthetic construct Homo sapiens gateway clone IMAGE:100021549 5' read GFM1 mRNA.
KJ895090 - Synthetic construct Homo sapiens clone ccsbBroadEn_04484 GFM1 gene, encodes complete protein.
KR711044 - Synthetic construct Homo sapiens clone CCSBHm_00019434 GFM1 (GFM1) mRNA, encodes complete protein.
KR711045 - Synthetic construct Homo sapiens clone CCSBHm_00019435 GFM1 (GFM1) mRNA, encodes complete protein.
KR711046 - Synthetic construct Homo sapiens clone CCSBHm_00019436 GFM1 (GFM1) mRNA, encodes complete protein.
KU178816 - Homo sapiens G elongation factor mitochondrial 1 isoform 1 (GFM1) mRNA, partial cds; nuclear gene for mitochondrial product.
KU178817 - Homo sapiens G elongation factor mitochondrial 1 isoform 3 (GFM1) mRNA, complete cds, alternatively spliced; nuclear gene for mitochondrial product.
AK092293 - Homo sapiens cDNA FLJ34974 fis, clone NTONG2005520, highly similar to Elongation factor G1, mitochondrial precursor.
AX747457 - Sequence 982 from Patent EP1308459.
AK023694 - Homo sapiens cDNA FLJ13632 fis, clone PLACE1011109, weakly similar to ELONGATION FACTOR G, MITOCHONDRIAL PRECURSOR.
AK022724 - Homo sapiens cDNA FLJ12662 fis, clone NT2RM4002205, moderately similar to ELONGATION FACTOR G, MITOCHONDRIAL PRECURSOR.
JD357655 - Sequence 338679 from Patent EP1572962.
JD184104 - Sequence 165128 from Patent EP1572962.
JD235351 - Sequence 216375 from Patent EP1572962.
JD355963 - Sequence 336987 from Patent EP1572962.
JD274319 - Sequence 255343 from Patent EP1572962.
JD164284 - Sequence 145308 from Patent EP1572962.

-  Biochemical and Signaling Pathways
  Reactome (by CSHL, EBI, and GO)

Protein Q96RP9 (Reactome details) participates in the following event(s):

R-HSA-5419279 Translocation of peptidyl-tRNA from A-site to P-site (and translocation of 55S ribosome by 3 bases along mRNA)
R-HSA-5419261 55S ribosome with peptidyl-tRNA in A site binds GFM1:GTP
R-HSA-5389840 Mitochondrial translation elongation
R-HSA-5368287 Mitochondrial translation
R-HSA-72766 Translation
R-HSA-392499 Metabolism of proteins

-  Other Names for This Gene
  Alternate Gene Symbols: A6NCI9, B2RCB9, B3KRW1, EFG, EFG1 , EFGM_HUMAN, ENST00000486715.1, ENST00000486715.2, ENST00000486715.3, ENST00000486715.4, ENST00000486715.5, GFM, GFM1 , NM_024996, Q6GTN2, Q96RP9, Q96T39, uc322gup.1, uc322gup.2
UCSC ID: ENST00000486715.6_7
RefSeq Accession: NM_024996.7
Protein: Q96RP9 (aka EFGM_HUMAN)

-  Gene Model Information
  Click here for a detailed description of the fields of the table above.

-  Methods, Credits, and Use Restrictions
  Click here for details on how this gene model was made and data restrictions if any.