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. Involved with LARP6 in the stabilization of type I collagen mRNAs for CO1A1 and CO1A2. Homomer assembled from elementary dimers (By similarity). Identified in complexes that contain VIM, EZR, AHNAK, BFSP1, BFSP2, ANK2, PLEC, PRX and spectrin (By similarity). Interacts with BCAS3 (By similarity). Interacts with LGSN (By similarity). Interacts with SYNM (By similarity). Interacts (via rod region) with PLEC (via CH 1 domain) (By similarity). Interacts with STK33 (By similarity). Interacts with LARP6 (By similarity). Interacts with RAB8B (By similarity). Interacts with TOR1A; the interaction associates TOR1A with the cytoskeleton. Interacts with TOR1AIP1 (By similarity). Interacts with TOR1AIP1 (By similarity). Interacts with DIAPH1 (By similarity). Interacts with EPPK1; interaction is dependent of higher-order structure of intermediate filament (By similarity). Interacts with the non-receptor tyrosine kinase SRMS; the interaction leads to phosphorylation of VIM (By similarity). Interacts with NOD2 (By similarity). Interacts (via head region) with CORO1C (By similarity). Interacts with HDGF (By similarity). Interacts with PRKCE (via phorbol-ester/DAG-type 2 domain) (By similarity). Interacts with BFSP2 (By similarity). Interacts with PPL (By similarity). The central alpha-helical coiled-coil IF rod domain mediates elementary homodimerization. The [IL]-x-C-x-x-[DE] motif is a proposed target motif for cysteine S-nitrosylation mediated by the iNOS-S100A8/A9 transnitrosylase complex. Phosphorylation by PKN1 inhibits the formation of filaments. Filament disassembly during mitosis is promoted by phosphorylation at Ser-54 as well as by nestin. 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. Phosphorylated at Ser-55 by CDK5 during neutrophil secretion in the cytoplasm. Phosphorylated by STK33. Phosphorylated on tyrosine residues by SRMS. S-nitrosylation is induced by interferon-gamma and oxidatively-modified low-densitity lipoprotein (LDL(ox)) possibly implicating the iNOS-S100A8/9 transnitrosylase complex. Belongs to the intermediate filament family.