Human Gene VIM (uc001iou.2) Description and Page Index
Description: Homo sapiens vimentin (VIM), mRNA. RefSeq Summary (NM_003380): This gene encodes a type III intermediate filament protein. Intermediate filaments, along with microtubules and actin microfilaments, make up the cytoskeleton. The encoded protein is responsible for maintaining cell shape and integrity of the cytoplasm, and stabilizing cytoskeletal interactions. This protein is involved in neuritogenesis and cholesterol transport and functions as an organizer of a number of other critical proteins involved in cell attachment, migration, and signaling. Bacterial and viral pathogens have been shown to attach to this protein on the host cell surface. Mutations in this gene are associated with congenital cataracts in human patients. [provided by RefSeq, Aug 2017]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: BC066956.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA2144120, SAMEA2148093 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000544301.7/ ENSP00000446007.1 RefSeq Select criteria :: based on conservation, longest protein ##RefSeq-Attributes-END## Transcript (Including UTRs) Position: hg19 chr10:17,270,258-17,279,592 Size: 9,335 Total Exon Count: 10 Strand: + Coding Region Position: hg19 chr10:17,271,422-17,279,270 Size: 7,849 Coding Exon Count: 9
ID:VIME_HUMAN DESCRIPTION: RecName: Full=Vimentin; FUNCTION: Vimentins are class-III intermediate filaments found in various non-epithelial cells, especially mesenchymal cells. Vimentin is attached to the nucleus, endoplasmic reticulum, and mitochondria, either laterally or terminally. FUNCTION: Involved with LARP6 in the stabilization of type I collagen mRNAs for CO1A1 and CO1A2. SUBUNIT: Homopolymer assembled from elementary dimers. Interacts with HCV core protein. Interacts with LGSN and SYNM. Interacts (via rod region) with PLEC (via CH 1 domain) (By similarity). Interacts with SLC6A4. Interacts with STK33. Interacts with LARP6. Interacts with RAB8B (By similarity). INTERACTION: Self; NbExp=5; IntAct=EBI-353844, EBI-353844; P31749:AKT1; NbExp=29; IntAct=EBI-353844, EBI-296087; P31751:AKT2; NbExp=6; IntAct=EBI-353844, EBI-296058; Q9H6U6:BCAS3; NbExp=3; IntAct=EBI-353844, EBI-6083685; Q14194:CRMP1; NbExp=2; IntAct=EBI-353844, EBI-473101; O95251:KAT7; NbExp=3; IntAct=EBI-353844, EBI-473199; O95361:TRIM16; NbExp=3; IntAct=EBI-353844, EBI-727384; SUBCELLULAR LOCATION: Cytoplasm. TISSUE SPECIFICITY: Highly expressed in fibroblasts, some expression in T- and B-lymphocytes, and little or no expression in Burkitt's lymphoma cell lines. Expressed in many hormone- independent mammary carcinoma cell lines. DOMAIN: The central alpha-helical coiled-coil rod region mediates elementary homodimerization. PTM: Filament disassembly during mitosis is promoted by phosphorylation at Ser-55 as well as by nestin (By similarity). One of the most prominent phosphoproteins in various cells of mesenchymal origin. Phosphorylation is enhanced during cell division, at which time vimentin filaments are significantly reorganized. Phosphorylation by PKN1 inhibits the formation of filaments. Phosphorylated at Ser-56 by CDK5 during neutrophil secretion in the cytoplasm. Phosphorylated by STK33. SIMILARITY: Belongs to the intermediate filament family. SEQUENCE CAUTION: Sequence=BAB71275.1; Type=Miscellaneous discrepancy; Note=Intron retention; WEB RESOURCE: Name=Wikipedia; Note=Vimentin entry; URL="http://en.wikipedia.org/wiki/Vimentin";
Genetic Association Studies of Complex Diseases and Disorders
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.
ModBase Predicted Comparative 3D Structure on P08670
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.