Fntb farnesyltransferase, CAAX box, beta [Mus musculus (house mouse)] - Gene

Summary

Official Symbol: Fntbprovided by MGI
Official Full Name: farnesyltransferase, CAAX box, betaprovided by MGI
Primary source: MGI:MGI:1861305
See related: Ensembl:ENSMUSG00000033373 AllianceGenome:MGI:1861305
Gene type: protein coding
RefSeq status: VALIDATED
Organism: Mus musculus
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Mus; Mus
Also known as: 2010013E13Rik
Summary: Enables farnesyltranstransferase activity. Acts upstream of or within negative regulation of cell population proliferation; positive regulation of fibroblast proliferation; and wound healing. Predicted to be part of microtubule associated complex and protein farnesyltransferase complex. Human ortholog(s) of this gene implicated in anxiety disorder. Orthologous to several human genes including FNTB (farnesyltransferase, CAAX box, subunit beta). [provided by Alliance of Genome Resources, Oct 2024]
Expression: Ubiquitous expression in ovary adult (RPKM 14.1), limb E14.5 (RPKM 12.8) and 28 other tissues See more
Orthologs: human all
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Genomic context

Location:: 12 C3; 12 33.73 cM

Exon count:: 13

Annotation release	Status	Assembly	Chr	Location
RS_2024_02	current	GRCm39 (GCF_000001635.27)	12	NC_000078.7 (76884014..76968188)
108.20200622	previous assembly	GRCm38.p6 (GCF_000001635.26)	12	NC_000078.6 (76837400..76921412)

Chromosome 12 - NC_000078.7 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Genomic Sequence:

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Expression

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See details

Project title: Mouse ENCODE transcriptome data Mouse ENCODE transcriptome data
Description: RNA profiling data sets generated by the Mouse ENCODE project.
BioProject: PRJNA66167
Publication: PMID 25409824
Analysis date: n/a

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Protein farnesylation is upregulated in Alzheimer's human brains and neuron-specific suppression of farnesyltransferase mitigates pathogenic processes in Alzheimer's model mice.
Title: Protein farnesylation is upregulated in Alzheimer's human brains and neuron-specific suppression of farnesyltransferase mitigates pathogenic processes in Alzheimer's model mice.
the catalytic b subunit of farnesyl transferase associated with a cytoskeletal protein...lonafarnib remarkably inhibited he expression of the cytoskeletal protein and interrupted its interaction with farnesyl transferase.
Title: Lonafarnib is a potential inhibitor for neovascularization.
Data suggest that farnesyltransferase might constitute a target in the management of severe acute pancreatitis (AP).
Title: Farnesyltransferase regulates neutrophil recruitment and tissue damage in acute pancreatitis.
deficiencies in either FTase or GGTase-I lead to severe hepatocellular disease. Our studies lay to rest the earlier notion that FTase is dispensable in adult tissues
Title: Severe hepatocellular disease in mice lacking one or both CaaX prenyltransferases.
Both Fntb and Pggt1b are required for the homeostasis of skin keratinocytes.
Title: Genetic studies on the functional relevance of the protein prenyltransferases in skin keratinocytes.
FTase is essential for embryonic development, but dispensable for adult homeostasis. Elimination of FTase during tumor progression had a limited but significant inhibitory effect on tumor development.
Title: Protein farnesyltransferase in embryogenesis, adult homeostasis, and tumor development.

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Variation

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Alleles

Alleles of this type are documented at Mouse Genome Informatics (MGI)

Endonuclease-mediated (2)
Targeted (5) 1 citation

Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Gene Ontology Provided by MGI

Function	Evidence Code	Pubs
enables farnesyltranstransferase activity	IMP Inferred from Mutant Phenotype more info	PubMed
contributes_to peptide binding	ISO Inferred from Sequence Orthology more info
contributes_to protein farnesyltransferase activity	IBA Inferred from Biological aspect of Ancestor more info
contributes_to protein farnesyltransferase activity	ISO Inferred from Sequence Orthology more info
enables protein farnesyltransferase activity	ISO Inferred from Sequence Orthology more info
enables protein farnesyltransferase activity	ISS Inferred from Sequence or Structural Similarity more info
enables zinc ion binding	ISO Inferred from Sequence Orthology more info
enables zinc ion binding	ISS Inferred from Sequence or Structural Similarity more info

Process	Evidence Code	Pubs
acts_upstream_of cell population proliferation	IMP Inferred from Mutant Phenotype more info	PubMed
acts_upstream_of fibroblast proliferation	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in lipid metabolic process	IEA Inferred from Electronic Annotation more info
acts_upstream_of_or_within negative regulation of cell population proliferation	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in positive regulation of cell cycle	ISO Inferred from Sequence Orthology more info
acts_upstream_of_or_within positive regulation of cell population proliferation	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in positive regulation of cell population proliferation	ISO Inferred from Sequence Orthology more info
acts_upstream_of_or_within positive regulation of fibroblast proliferation	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in positive regulation of nitric-oxide synthase biosynthetic process	ISO Inferred from Sequence Orthology more info
involved_in protein farnesylation	ISS Inferred from Sequence or Structural Similarity more info
acts_upstream_of_or_within regulation of fibroblast proliferation	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in response to cytokine	ISO Inferred from Sequence Orthology more info
involved_in response to organic cyclic compound	ISO Inferred from Sequence Orthology more info
acts_upstream_of_or_within wound healing	IMP Inferred from Mutant Phenotype more info	PubMed

Component	Evidence Code	Pubs
part_of microtubule associated complex	ISO Inferred from Sequence Orthology more info
part_of protein farnesyltransferase complex	IBA Inferred from Biological aspect of Ancestor more info
part_of protein farnesyltransferase complex	ISO Inferred from Sequence Orthology more info	PubMed
part_of protein farnesyltransferase complex	ISS Inferred from Sequence or Structural Similarity more info

General protein information

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Preferred Names: protein farnesyltransferase subunit beta

Names: CAAX farnesyltransferase subunit beta; FTase-beta; ras proteins prenyltransferase subunit beta

NP_001405090.1

EC 2.5.1.58

NP_001405091.1

EC 2.5.1.58

NP_666039.1

EC 2.5.1.58

NCBI Reference Sequences (RefSeq)

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RefSeqs maintained independently of Annotated Genomes

These reference sequences exist independently of genome builds. Explain

These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

mRNA and Protein(s)

NM_001418161.1 → NP_001405090.1 protein farnesyltransferase subunit beta isoform 2

Status: VALIDATED

Source sequence(s)

AC124556, AC132331
NM_001418162.1 → NP_001405091.1 protein farnesyltransferase subunit beta isoform 3

Status: VALIDATED

Source sequence(s)

AC124556
NM_145927.3 → NP_666039.1 protein farnesyltransferase subunit beta isoform 1

See identical proteins and their annotated locations for NP_666039.1

Status: VALIDATED

Source sequence(s)

AC124556, AC132331

Consensus CDS

CCDS25998.1

UniProtKB/Swiss-Prot

Q8K2I1

UniProtKB/TrEMBL

D3YWJ4

Related

ENSMUSP00000035498.10, ENSMUST00000041008.10

Conserved Domains (2) summary

PLN02710
Location:42 → 419

PLN02710; farnesyltranstransferase subunit beta

cd02893
Location:75 → 373

FTase; Protein farnesyltransferase (FTase)_like proteins containing the protein prenyltransferase (PTase) domain, beta subunit (alpha 6 - alpha 6 barrel fold). FTases are a subgroup of PTase family of lipid-modifying enzymes. PTases catalyze the ...