VIM.L

VIM1 is an unconventional methylcytosine-binding protein that interacts in vitro with 5mCpG- and 5mCpHpG-modified DNA (via its SRA domain), as well as recombinant histones (H2B, H3, H4, and HTR12) in plant extracts. Vimentin is attached to the nucleus, endoplasmic reticulum, and mitochondria, either laterally or terminally.

Full Name

Vimentin L homeolog

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.
Involved with LARP6 in the stabilization of type I collagen mRNAs for CO1A1 and CO1A2.

Biological Process

Astrocyte developmentIEA:Ensembl
Bergmann glial cell differentiationIEA:Ensembl
Cellular response to interferon-gammaIEA:Ensembl
Cellular response to lipopolysaccharideManual Assertion Based On ExperimentIMP:UniProtKB
Cellular response to muramyl dipeptideManual Assertion Based On ExperimentIMP:UniProtKB
Intermediate filament organizationISS:UniProtKB
Lens fiber cell developmentIEA:Ensembl
Negative regulation of neuron projection developmentIEA:Ensembl
Positive regulation of collagen biosynthetic processManual Assertion Based On ExperimentIMP:UniProtKB
Positive regulation of translationManual Assertion Based On ExperimentIMP:UniProtKB
Regulation of mRNA stabilityManual Assertion Based On ExperimentIMP:UniProtKB
SMAD protein signal transductionIEA:Ensembl

Cellular Location

Cytoplasm
Cytoplasm, cytoskeleton
Nucleus matrix
Cell membrane

Involvement in disease

Cataract 30, multiple types (CTRCT30):
An opacification of the crystalline lens of the eye that frequently results in visual impairment or blindness. Opacities vary in morphology, are often confined to a portion of the lens, and may be static or progressive. In general, the more posteriorly located and dense an opacity, the greater the impact on visual function.

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 (PubMed:21465480).
Phosphorylated by STK33 (PubMed:18811945).
Phosphorylated on tyrosine residues by SRMS (PubMed:29496907).
O-glycosylated during cytokinesis at sites identical or close to phosphorylation sites, this interferes with the phosphorylation status.
S-nitrosylation is induced by interferon-gamma and oxidatively-modified low-densitity lipoprotein (LDL(ox)) possibly implicating the iNOS-S100A8/9 transnitrosylase complex.