U.S. flag

An official website of the United States government

Format

Send to:

Choose Destination

Links from GEO Profiles

    • Showing Current items.

    Fmn1 formin 1 [ Mus musculus (house mouse) ]

    Gene ID: 14260, updated on 27-Nov-2024

    Summary

    Go to the top of the page Help
    Official Symbol
    Fmn1provided by MGI
    Official Full Name
    formin 1provided by MGI
    Primary source
    MGI:MGI:101815
    See related
    Ensembl:ENSMUSG00000044042 AllianceGenome:MGI:101815
    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
    ld; Fmn; formin-1
    Summary
    Enables SH3 domain binding activity. Acts upstream of or within several processes, including limb morphogenesis; positive regulation of cellular component organization; and ureteric bud invasion. Located in cytoplasm and nucleus. Is expressed in several structures, including alimentary system; brain; genitourinary system; hemolymphoid system gland; and limb bud. Human ortholog(s) of this gene implicated in alcohol dependence. Orthologous to human FMN1 (formin 1). [provided by Alliance of Genome Resources, Nov 2024]
    Expression
    Broad expression in testis adult (RPKM 2.9), kidney adult (RPKM 1.9) and 19 other tissues See more
    Orthologs
    human all
    NEW
    Try the new Gene table
    Try the new Transcript table

    Genomic context

    Go to the top of the page Help
    See Fmn1 in Genome Data Viewer
    Location:
    2 E4; 2 57.3 cM
    Exon count:
    27
    Annotation release Status Assembly Chr Location
    RS_2024_02 current GRCm39 (GCF_000001635.27) 2 NC_000068.8 (113158029..113547113)
    108.20200622 previous assembly GRCm38.p6 (GCF_000001635.26) 2 NC_000068.7 (113327664..113716768)

    Chromosome 2 - NC_000068.8Genomic Context describing neighboring genes Neighboring gene STARR-seq mESC enhancer starr_05389 Neighboring gene STARR-seq mESC enhancer starr_05390 Neighboring gene ryanodine receptor 3 Neighboring gene STARR-seq mESC enhancer starr_05392 Neighboring gene STARR-seq mESC enhancer starr_05393 Neighboring gene STARR-seq mESC enhancer starr_05394 Neighboring gene STARR-seq mESC enhancer starr_05395 Neighboring gene predicted gene, 26505 Neighboring gene STARR-seq mESC enhancer starr_05396 Neighboring gene transmembrane and coiled-coil domains 5B Neighboring gene STARR-seq mESC enhancer starr_05397 Neighboring gene STARR-seq mESC enhancer starr_05399 Neighboring gene STARR-seq mESC enhancer starr_05401 Neighboring gene RIKEN cDNA 4930533B01 gene Neighboring gene predicted gene, 54142 Neighboring gene predicted gene, 46756 Neighboring gene gremlin 1, DAN family BMP antagonist

    Genomic regions, transcripts, and products

    Go to the top of the page Help

    Go to nucleotide: Graphics FASTA GenBank

    Expression

    Go to the top of the page Help
    • Project title: 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

    Go to the top of the pageHelp

    Related articles in PubMed

    1. The mouse formin (Fmn) gene: abundant circular RNA transcripts and gene-targeted deletion analysis. Chao CW, et al. Mol Med, 1998 Sep. PMID 9848078, Free PMC Article
    2. Uncovering Modifier Genes of X-Linked Alport Syndrome Using a Novel Multiparent Mouse Model. Takemon Y, et al. J Am Soc Nephrol, 2021 Aug. PMID 34045313, Free PMC Article
    3. Adaptive mechanoproperties mediated by the formin FMN1 characterize glioblastoma fitness for invasion. Monzo P, et al. Dev Cell, 2021 Oct 25. PMID 34559979
    4. Molecular interaction between limb deformity proteins (formins) and Src family kinases. Uetz P, et al. J Biol Chem, 1996 Dec 27. PMID 8969217
    5. 'Formins': proteins deduced from the alternative transcripts of the limb deformity gene. Woychik RP, et al. Nature, 1990 Aug 30. PMID 2392150

    See all (68) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. Adaptive mechanoproperties mediated by the formin FMN1 characterize glioblastoma fitness for invasion.
      Title: Adaptive mechanoproperties mediated by the formin FMN1 characterize glioblastoma fitness for invasion.
    2. Uncovering Modifier Genes of X-Linked Alport Syndrome Using a Novel Multiparent Mouse Model.
      Title: Uncovering Modifier Genes of X-Linked Alport Syndrome Using a Novel Multiparent Mouse Model.
    3. Fmn1 and FlnB have shared and independent functions.
      Title: Formin 1 and filamin B physically interact to coordinate chondrocyte proliferation and differentiation in the growth plate.
    4. Results suggest that the regulation of microtubule acetylation is likely a general formin activity.
      Title: The ability to induce microtubule acetylation is a general feature of formin proteins.
    5. These results reveal a previously unknown involvement of Formin1 in dendritogenesis and synaptogenesis and indicate that this protein is a key component of the Ngn3 signaling pathway that controls neuronal differentiation.
      Title: Formin1 mediates the induction of dendritogenesis and synaptogenesis by neurogenin3 in mouse hippocampal neurons.
    6. Disruption of Fmn1 gene in mice increased Bmp signaling.
      Title: Formin1 disruption confers oligodactylism and alters Bmp signaling.
    7. Interaction of the N- and C-terminal autoregulatory domains of FRL2 does not inhibit FRL2 activity
      Title: Interaction of the N- and C-terminal autoregulatory domains of FRL2 does not inhibit FRL2 activity.
    8. It was determined that Fmn1-IV, as an actin nucleator, contributes to protrusion of the cell's leading edge and focal adhesion formation, thus contributing to cell motility
      Title: Formin 1-isoform IV deficient cells exhibit defects in cell spreading and focal adhesion formation.
    9. the mouse formin, FRLalpha, slows actin filament barbed end elongation, competes with capping protein, accelerates polymerization from monomers, and severs filaments
      Title: The mouse formin, FRLalpha, slows actin filament barbed end elongation, competes with capping protein, accelerates polymerization from monomers, and severs filaments.
    10. ATP hydrolysis control of filament assembly from profilin-actin requires formin
      Title: How ATP hydrolysis controls filament assembly from profilin-actin: implication for formin processivity.
    Submit: New GeneRIF Correction

    Variation

    Go to the top of the page Help

    Alleles

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

    Interactions

    Go to the top of the page Help
    Products Interactant Other Gene Complex Source Pubs Description

    General gene information

    Go to the top of the page Help

    Markers

    Homology

    Gene Ontology Provided by MGI

    Function Evidence Code Pubs
    enables SH3 domain binding IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 
    enables actin binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables microtubule binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables protein binding IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 
    Process Evidence Code Pubs
    involved_in actin cytoskeleton organization IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    involved_in actin nucleation IEA
    Inferred from Electronic Annotation
    more info
    		  
    acts_upstream_of_or_within forelimb morphogenesis IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    acts_upstream_of_or_within gene expression IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    acts_upstream_of_or_within hindlimb morphogenesis IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    acts_upstream_of_or_within limb development IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    acts_upstream_of_or_within positive regulation of actin filament polymerization IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    acts_upstream_of_or_within positive regulation of actin nucleation IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    acts_upstream_of_or_within positive regulation of focal adhesion assembly IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    acts_upstream_of_or_within skeletal system morphogenesis IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    acts_upstream_of_or_within ureteric bud invasion IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    Component Evidence Code Pubs
    located_in actin filament IEA
    Inferred from Electronic Annotation
    more info
    		  
    located_in adherens junction IEA
    Inferred from Electronic Annotation
    more info
    		  
    located_in cytoplasm IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    is_active_in endoplasmic reticulum membrane IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    is_active_in nucleus IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    located_in nucleus IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    located_in plasma membrane IEA
    Inferred from Electronic Annotation
    more info
    		  

    General protein information

    Go to the top of the page Help
    Preferred Names
    formin-1
    Names
    limb deformity protein

    NCBI Reference Sequences (RefSeq)

    Go to the top of the page Help

    NEW Try the new Transcript table

    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)

    1. NM_001285458.1 → NP_001272387.1  formin-1 isoform 3

      Status: VALIDATED

      Description
      Transcript Variant: This variant (3) lacks three alternate in-frame exons compared to variant 1. The resulting protein (isoform 3) is shorter compared to isoform 1.
      Source sequence(s)
      AL672253, AL691437, AL691466, AL929450
      Consensus CDS
      CCDS71112.1
      UniProtKB/TrEMBL
      B7ZW99, E9Q7P6
      Related
      ENSMUSP00000125052.2, ENSMUST00000161731.5
      Conserved Domains (1) summary
      smart00498
      Location:886 → 1283
      FH2; Formin Homology 2 Domain

    2. NM_001285459.1 → NP_001272388.1  formin-1 isoform 4

      Status: VALIDATED

      Description
      Transcript Variant: This variant (4) represents the use of an alternate promoter, differs in the 5' UTR, lacks 5' coding sequence and an alternate in-frame exon in the 3' coding region, and uses an alternate start codon compared to variant 1 (PMID: 1339380). The resulting protein (isoform 4, also known as IV) has a distinct N-terminus and is shorter compared to isoform 1.
      Source sequence(s)
      AL672253, AL691437
      Consensus CDS
      CCDS71113.1
      UniProtKB/Swiss-Prot
      Q05860
      Related
      ENSMUSP00000080093.7, ENSMUST00000081349.9
      Conserved Domains (1) summary
      smart00498
      Location:758 → 1155
      FH2; Formin Homology 2 Domain

    3. NM_001287817.1 → NP_001274746.1  formin-1 isoform 5

      See identical proteins and their annotated locations for NP_001274746.1

      Status: VALIDATED

      Description
      Transcript Variant: This variant (5) represents the use of an alternate promoter, differs in the 5' UTR, lacks a significant portion of the 5' coding sequence and uses a downstream start codon compared to variant 1. The resulting protein (isoform 5) has a shorter N-terminus compared to isoform 1. Variants 5 and 6 encode the same protein.
      Source sequence(s)
      AL672253

    4. NM_001287818.1 → NP_001274747.1  formin-1 isoform 5

      See identical proteins and their annotated locations for NP_001274747.1

      Status: VALIDATED

      Description
      Transcript Variant: This variant (6) represents the use of an alternate promoter, differs in the 5' UTR, lacks a significant portion of the 5' coding sequence and uses a downstream start codon compared to variant 1. The resulting protein (isoform 5) has a shorter N-terminus compared to isoform 1. Variants 5 and 6 encode the same protein.
      Source sequence(s)
      AL672253
      Conserved Domains (1) summary
      cl19758
      Location:3 → 48
      FH2; Formin Homology 2 Domain

    5. NM_010230.2 → NP_034360.2  formin-1 isoform 1

      See identical proteins and their annotated locations for NP_034360.2

      Status: VALIDATED

      Description
      Transcript Variant: This variant (1) represents the longest transcript and encodes the longest isoform (1, also known as IA).
      Source sequence(s)
      AK135758, AK142145, AL672253, AL691437, AL691466, AV256854, BY288387, CK391697, CN832512, CO814739
      Consensus CDS
      CCDS16559.1
      UniProtKB/Swiss-Prot
      A2AFY9, A2AFZ0, Q05859, Q05860
      UniProtKB/TrEMBL
      B7ZW99
      Related
      ENSMUSP00000099606.4, ENSMUST00000102547.10
      Conserved Domains (1) summary
      smart00498
      Location:984 → 1417
      FH2; Formin Homology 2 Domain

    RefSeqs of Annotated Genomes: GCF_000001635.27-RS_2024_02

    The following sections contain reference sequences that belong to a specific genome build. Explain

    Reference GRCm39 C57BL/6J

    Genomic

    1. NC_000068.8 Reference GRCm39 C57BL/6J

      Range
      113158029..113547113
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. XM_011239295.3 → XP_011237597.1  formin-1 isoform X1

      See identical proteins and their annotated locations for XP_011237597.1

      UniProtKB/TrEMBL
      B7ZW99
      Conserved Domains (2) summary
      smart00498
      Location:984 → 1381
      FH2; Formin Homology 2 Domain
      PHA03247
      Location:449 → 706
      PHA03247; large tegument protein UL36; Provisional

    2. XM_011239294.3 → XP_011237596.1  formin-1 isoform X1

      See identical proteins and their annotated locations for XP_011237596.1

      UniProtKB/TrEMBL
      B7ZW99
      Related
      ENSMUSP00000097171.3, ENSMUST00000099576.9
      Conserved Domains (2) summary
      smart00498
      Location:984 → 1381
      FH2; Formin Homology 2 Domain
      PHA03247
      Location:449 → 706
      PHA03247; large tegument protein UL36; Provisional

    3. XM_006498750.5 → XP_006498813.1  formin-1 isoform X2

      UniProtKB/TrEMBL
      A0A5F8MPL0
      Related
      ENSMUSP00000159010.2, ENSMUST00000238883.2
      Conserved Domains (1) summary
      smart00498
      Location:404 → 801
      FH2; Formin Homology 2 Domain

    4. XM_036158294.1 → XP_036014187.1  formin-1 isoform X3

      Conserved Domains (1) summary
      smart00498
      Location:200 → 597
      FH2; Formin Homology 2 Domain

    5. XM_017315533.3 → XP_017171022.1  formin-1 isoform X4

      Conserved Domains (1) summary
      cl19758
      Location:3 → 48
      FH2; Formin Homology 2 Domain

    6. XM_036158295.1 → XP_036014188.1  formin-1 isoform X4

      Conserved Domains (1) summary
      cl19758
      Location:3 → 48
      FH2; Formin Homology 2 Domain

    Suppressed Reference Sequence(s)

    The following Reference Sequences have been suppressed. Explain

    1. NM_001043322.1: Suppressed sequence

      Description
      NM_001043322.1: This RefSeq was permanently suppressed because currently there is insufficient support for the transcript and the protein.
    Nucleotide Protein Strain
    Heading Accession and Version
    Protein Accession Links
    GenPept Link UniProtKB Link
    Q05860.2 GenPept UniProtKB/Swiss-Prot:Q05860

    Gene LinkOut

    The following LinkOut resources are supplied by external providers. These providers are responsible for maintaining the links.

    Chemical Information
    Molecular Biology Databases
    Research Materials
    Tools