Search Results
Overview
| Uniprot ID | P20152 |
|---|---|
| Protein Name | Vimentin |
| Gene Name | Vim |
| Organism | Mus musculus |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 104 | KNTRTNEKVELQELN |
| 120 | RFANYIDKVRFLEQQ |
| 402 | IEIATYRKLLEGEES |
| 445 | SKRTLLIKTVETRDG |
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. Plays a role in cell directional movement, orientation, cell sheet organization and Golgi complex polarization at the cell migration front (By similarity). Protects SCRIB from proteasomal degradation and facilitates its localization to intermediate filaments in a cell contact-mediated manner (By similarity). May promote axon outgrowth and motor fiber repair via DSP-mediated recruitment to outgrowth tips (PubMed:25496840)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0030424 | axon |
| Cellular Component | GO:0044297 | cell body |
| Cellular Component | GO:0031252 | cell leading edge |
| Cellular Component | GO:0042995 | cell projection |
| Cellular Component | GO:0005737 | cytoplasm |
| Cellular Component | GO:0005856 | cytoskeleton |
| Cellular Component | GO:0005829 | cytosol |
| Cellular Component | GO:0005882 | intermediate filament |
| Cellular Component | GO:0045111 | intermediate filament cytoskeleton |
| Cellular Component | GO:0043005 | neuron projection |
| Cellular Component | GO:0016363 | nuclear matrix |
| Cellular Component | GO:0048471 | perinuclear region of cytoplasm |
| Cellular Component | GO:0005777 | peroxisome |
| Cellular Component | GO:0045335 | phagocytic vesicle |
| Cellular Component | GO:0005886 | plasma membrane |
| Cellular Component | GO:0045098 | type III intermediate filament |
| Molecular Function | GO:0003725 | double-stranded RNA binding |
| Molecular Function | GO:0042802 | identical protein binding |
| Molecular Function | GO:1990254 | keratin filament binding |
| Molecular Function | GO:0019900 | kinase binding |
| Molecular Function | GO:0060090 | molecular adaptor activity |
| Molecular Function | GO:0019904 | protein domain specific binding |
| Molecular Function | GO:0051721 | protein phosphatase 2A binding |
| Molecular Function | GO:1990782 | protein tyrosine kinase binding |
| Molecular Function | GO:0003723 | RNA binding |
| Molecular Function | GO:0097110 | scaffold protein binding |
| Molecular Function | GO:0005200 | structural constituent of cytoskeleton |
| Molecular Function | GO:0005212 | structural constituent of eye lens |
| Biological Process | GO:0014002 | astrocyte development |
| Biological Process | GO:0060020 | Bergmann glial cell differentiation |
| Biological Process | GO:0071222 | cellular response to lipopolysaccharide |
| Biological Process | GO:0071225 | cellular response to muramyl dipeptide |
| Biological Process | GO:0071346 | cellular response to type II interferon |
| Biological Process | GO:0045109 | intermediate filament organization |
| Biological Process | GO:0045103 | intermediate filament-based process |
| Biological Process | GO:0070307 | lens fiber cell development |
| Biological Process | GO:0010977 | negative regulation of neuron projection development |
| Biological Process | GO:0032967 | positive regulation of collagen biosynthetic process |
| Biological Process | GO:0010634 | positive regulation of epithelial cell migration |
| Biological Process | GO:0010628 | positive regulation of gene expression |
| Biological Process | GO:0060252 | positive regulation of glial cell proliferation |
| Biological Process | GO:0050770 | regulation of axonogenesis |
| Biological Process | GO:0043488 | regulation of mRNA stability |
| Biological Process | GO:1900147 | regulation of Schwann cell migration |
Reference
[1] Sung E, Sim H, Cho YC, Lee W, Bae JS et al.. Global Profiling of Lysine Acetylation and Lactylation in Kupffer Cells.. J Proteome Res 22(12):3683-3691. 2023 Dec 1. PMID: 37897433.
[2] Chang J, Wu W, Qian P, Lu Z, He X et al.. Multi-omics study on the effect of moderate-intensity exercise on protein lactylation in mouse muscle tissue.. Front Cell Dev Biol 12:1472338. 2024. PMID: 39935788.
[3] Zhuo W, Zhang M, Tan J, Gao Y, Wang Y et al.. Lysine lactylation analysis of proteins in the heart of the Kawasaki disease mouse model.. Front Cell Dev Biol 13:1550220. 2025. PMID: 40114965.
[4] Wu D, Tang Y, Li X, Xiong S, Zhang Z et al.. Characterization of protein lactylation in healthy and ischemic mouse hearts.. Front Cardiovasc Med 12:1644886. 2025. PMID: 41089239.