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FLASH GENE
Symbol VIM contributors: mct/npt/pgu - updated : 30-01-2016
HGNC name vimentin
HGNC id 12692
DNA
TYPE functioning gene
SPECIAL FEATURE head to head
STRUCTURE 8.30 kb     9 Exon(s)
10 Kb 5' upstream gene genomic sequence study
MAPPING cloned Y linked Y status confirmed
RNA
TRANSCRIPTS type messenger
identificationnb exonstypebpproduct
ProteinkDaAAspecific expressionYearPubmed
9 - 2151 53.6 466 - 2008 18632620
EXPRESSION
Type ubiquitous
   expressed in (based on citations)
organ(s)
SystemOrgan level 1Organ level 2Organ level 3Organ level 4LevelPubmedSpeciesStageRna symbol
Cardiovascularheart   highly
Digestiveintestinesmall intestine  highly
Skin/Tegumentskin   highly
Visualeyeanterior segmentcornea  
tissue
SystemTissueTissue level 1Tissue level 2LevelPubmedSpeciesStageRna symbol
Connectivebone   
cell lineage cells of mesenchymal origin
cell lines
fluid/secretion
at STAGE
physiological period embryo, fetal
Text mesenchymal cell, cochlea
PROTEIN
PHYSICAL PROPERTIES
STRUCTURE
motifs/domains
mono polymer homomer , polymer
HOMOLOGY
interspecies ortholog to murine Vim
homolog to rattus Vim
homolog to Xenopus Xl.127
homolog to zebrafish vim
homolog to C.elegans F55C12.1
Homologene
FAMILY
  • intermediate filament family, type III
  • CATEGORY structural protein
    SUBCELLULAR LOCALIZATION     intracellular
    intracellular,cytoplasm,organelle,mitochondria
    intracellular,cytoplasm,organelle,peroxisome
    intracellular,cytoplasm,organelle,endoplasmic reticulum
    intracellular,cytoplasm,organelle,Golgi
    intracellular,cytoplasm,cytosolic
    intracellular,cytoplasm,cytoskeleton,intermed filament
    text
  • vimentin cytoskeleton co-localized and interacted with mitochondria to a greater extent than other cytoskeletal components known to support mitochondria
  • colocalized with VASP and PKG in endothelial cells
  • PPARG colocalized with vimentin in certain organelles, i.e. Golgi, mitochondria and endoplasmic reticulum
  • basic FUNCTION
  • intermediate filament subunit specific for mesenchymal tissue, involved in vascular tuning and wound repair
  • may be an organizer of a number of critical proteins involved in attachment, migration, and cell signaling
  • contribution of vimentin in mitochondrial morphology and organization
  • could participate in the mitochondrial association of microtubules (relatioship between the vimentin-based intermediate filaments and the regulation of mitochondria)
  • important role functional in the maintenance of lens integrity
  • scaffold provided by vimentin is essential for VASP localization and PKG mediated VASP phosphorylation and thus controls endothelial cell migration and proliferation
  • associates with focal adhesion sites which play a dominant role in cell adhesion, cell migration and cell detachment
  • vimentin filaments may play a role in the development of tissue fibrosis by stabilizing collagen mRNAs
  • exhibits a complex pattern of tissue-specific and developmentally regulated expression
  • required for sphingosine 1-phosphate (S1P)- and growth factor (GF)-induced endothelial cell invasion, and vimentin was cleaved by calpains during invasion
  • leucine zipper-containing intermediate filament protein, suppressing ATF4-dependent osteocalcin (Ocn) transcription and osteoblast differentiation
  • plays a pivotal role in epithelial-to-mesenchymal transition and is known to be overexpressed in the prognostically poor basal-like breast cancer subtype
  • CELLULAR PROCESS
    PHYSIOLOGICAL PROCESS
    PATHWAY
    metabolism
    signaling
    a component
  • vimentin complexed with MMP14 in a manner that required both the cytoplasmic domain of MMP14 and calpain activation, which increased the soluble pool of vimentin in endothelial cells
  • INTERACTION
    DNA
    RNA
    small molecule
    protein
  • interacting with GFAP and SYNM in astrocytes
  • interaction between vimentin and VASP constitutes an important step in endothelial cell migration and proliferation
  • binding of AKT1 (tail region) to VIM (head region) results in Vim Ser39 phosphorylation enhancing the ability of VIM to induce motility and invasion while protecting VIMfrom caspase-induced proteolysis
  • LARP6 interacts with vimentin filaments through its La domain and colocalizes with the filaments
  • YY1 is a key transcriptional activator regulating vimentin expression and CpG methylation is sufficient to prevent the binding of YY1 to the vimentin promoter
  • desmin and vimentin, two components of the intermediate filament in muscle, directly interacted with and were degraded by FBXO32 in response to MSTN
  • vimentin binds the ALOX15 promoter and regulates its promoter activity and protein expression
  • NOD2 interacting protein that regulates NOD2 activities including inflammatory NFKB1 signaling, autophagy and bacterial handling
  • TGFB stimulates vimentin production via PI3K-Akt-MTOR signaling, which leads to suppression of ATF4-dependent Ocn transcription and osteoblast differentiation
  • mediates MIR378 function in cellular self-renewal by regulating the expression of the SOX2 transcription factor
  • cytosolic PPARG interacts directly with cytoskeletal vimentin
  • DCN has an impact on the biology of ITGA2B1 integrin and the vimentin intermediate filament system
  • functional linkage between NSMCE3, VIM and FSCN1
  • INVS could upregulate the expression of CDH2, VIM, MMP2, and MMP9
  • TRIM56 is the ubiquitin ligase that is degrading vimentin in Moody cells
  • cell & other
    REGULATION
    Other phosphorylation enhanced during cell division
    ASSOCIATED DISORDERS
    corresponding disease(s) CZP2
    Other morbid association(s)
    TypeGene ModificationChromosome rearrangementProtein expressionProtein Function
    tumoral     --over  
    in breast tumor cells producing unique tubulin-based protrusions when detached from extracellular matrix and with high metastatic potential (significantly increased extension and frequency of microtubule protrusions, the tubulin microtentacles)
    tumoral     --low  
    inhibits migration and invasion of colon and breast cancer cell lines
    tumoral     --over  
    contributes to the aggressive phenotype and poor prognosis in triple-negative breast cancer
    Susceptibility
    Variant & Polymorphism
    Candidate gene
    Marker
  • vimentin methylation predicted poor overall survival independent of race, subtype, stage, nodal status, or metastatic disease and holds promise as a new prognostic biomarker for breast cancer patient
  • changes in VIM and FBLN1 methylation levels in cell-free DNA (cfDNA) are associated with Hepatocellular carcinoma (HCC) and could represent useful plasma-based biomarkers
  • positive VIM expression was shown to predict patients' relapse and poor outcome regarding patients' overall survival in laryngeal squamous cell carcinoma
  • Therapy target
    ANIMAL & CELL MODELS