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Details on Person UniProt:P08670 VIM
| Class:Id | ReferenceGeneProduct:67184 |
|---|---|
| _chainChangeLog | initiator methionine:1 added on Fri February 6 2015;chain:2-466 added on Fri February 6 2015;initiator methionine:1 for 67184 removed on Fri Nov 03 2023;initiator methionine: for 67184 added on Fri Nov 03 2023;initiator methionine: for 67184 removed on Fri Aug 15 2025;initiator methionine:1 for 67184 added on Fri Aug 15 2025 |
| _displayName | UniProt:P08670 VIM |
| _timestamp | 2026-02-20 21:45:52 |
| chain | initiator methionine:1 chain:2-466 |
| checksum | BAB54026665B015A |
| comment | 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 (By similarity).FUNCTION Involved with LARP6 in the stabilization of type I collagen mRNAs for CO1A1 and CO1A2.SUBUNIT Homomer assembled from elementary dimers (PubMed:20176112). Identified in complexes that contain VIM, EZR, AHNAK, BFSP1, BFSP2, ANK2, PLEC, PRX and spectrin (By similarity). Identified in a complex containing at least DSP, JUP, VIM and CDH2; the complex is more abundant following crush injury in regenerating motor neurons and may promote axon outgrowth and motor fiber repair (By similarity). Interacts with BCAS3 (PubMed:17505058). Interacts with LGSN (By similarity). Interacts with SYNM (By similarity). Interacts (via rod region) with PLEC (via CH 1 domain) (By similarity). Interacts with PLEC isoform 1C (PubMed:24940650). Interacts with STK33 (PubMed:18811945). Interacts with LARP6 (PubMed:21746880). Interacts with RAB8B (By similarity). Interacts with TOR1A; the interaction associates TOR1A with the cytoskeleton (PubMed:16361107, PubMed:18827015). Interacts with TOR1AIP1 (PubMed:16361107). Interacts with DIAPH1 (PubMed:23325789). Interacts with EPPK1; interaction is dependent of higher-order structure of intermediate filament (PubMed:16923132). Interacts with the non-receptor tyrosine kinase SRMS; the interaction leads to phosphorylation of VIM (PubMed:29496907). Interacts with NOD2 (PubMed:27812135). Interacts (via head region) with CORO1C (By similarity). Interacts with HDGF (isoform 2) (PubMed:26845719). Interacts with PRKCE (via phorbol-ester/DAG-type 2 domain) (PubMed:18408015). Interacts with BFSP2 (By similarity). Interacts with PPL (By similarity). Interacts (via rod domain) with PKP1 (PubMed:10852826). Interacts with PKP2 (PubMed:10852826). Interacts with SCRIB (via PDZ domains); the interaction protects SCRIB from proteasomal degradation and facilitates SCRIB localization to intermediate filaments, the interaction is reduced by cell contact inhibition (PubMed:19386766).SUBUNIT (Microbial infection) Interacts with HCV core protein.SUBUNIT (Microbial infection) Interacts with Chandipura virus glycoprotein; this interaction might facilitate the binding of the virus to the cells.INTERACTION 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.INDUCTION Up-regulated by muramyl-dipeptide and lipopolysaccharide.DOMAIN The central alpha-helical coiled-coil IF rod domain mediates elementary homodimerization.DOMAIN 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.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).PTM O-glycosylated during cytokinesis at sites identical or close to phosphorylation sites, this interferes with the phosphorylation status.PTM S-nitrosylation is induced by interferon-gamma and oxidatively-modified low-densitity lipoprotein (LDL(ox)) possibly implicating the iNOS-S100A8/9 transnitrosylase complex.DISEASE The disease is caused by variants affecting the gene represented in this entry.SIMILARITY Belongs to the intermediate filament family.CAUTION Was reported to interact with SLC6A4, however the paper was retracted as some results and conclusions are not reliable.SEQUENCE CAUTION Product of a cloning artifact.ONLINE INFORMATION Vimentin entry |
| description | recommendedName: fullName evidence="38"Vimentin |
| geneName | VIM |
| identifier | P08670 |
| isSequenceChanged | FALSE |
| keyword | 3D-structure Acetylation Cataract Cell membrane Cell projection Coiled coil Cytoplasm Cytoskeleton Direct protein sequencing Disease variant Glycoprotein Host-virus interaction Intermediate filament Isopeptide bond Membrane Nucleus Phosphoprotein Proteomics identification Reference proteome S-nitrosylation Ubl conjugation |
| modified | [InstanceEdit:9836292] Weiser, Joel, 2023-05-25 [InstanceEdit:9852000] Weiser, Joel, 2023-11-03 [InstanceEdit:9926675] Weiser, Joel, 2024-11-03 [InstanceEdit:9939033] Weiser, Joel, 2025-02-21 [InstanceEdit:9963647] Weiser, Joel, 2025-08-15 [InstanceEdit:9983091] Weiser, Joel, 2026-02-20 |
| name | VIM |
| referenceDatabase | [ReferenceDatabase:2] UniProt |
| referenceGene | [ReferenceDNASequence:8948482] ENSEMBL:ENSG00000026025 VIM [Homo sapiens] |
| secondaryIdentifier | VIME_HUMAN B0YJC2 D3DRU4 Q15867 Q15868 Q15869 Q548L2 Q6LER9 Q8N850 Q96ML2 Q9NTM3 |
| sequenceLength | 466 |
| species | [Species:48887] Homo sapiens |
| (referenceEntity) | [EntityWithAccessionedSequence:201600] VIM [cytosol] [Homo sapiens] [EntityWithAccessionedSequence:350264] VIM(2-85) [cytosol] [Homo sapiens] [EntityWithAccessionedSequence:350294] VIM(86-466) [cytosol] [Homo sapiens] [EntityWithAccessionedSequence:350314] VIM(260-466) [cytosol] [Homo sapiens] [EntityWithAccessionedSequence:350316] VIM(430-466) [cytosol] [Homo sapiens] [EntityWithAccessionedSequence:350317] VIM(2-429) [cytosol] [Homo sapiens] [EntityWithAccessionedSequence:350323] VIM(2-259) [cytosol] [Homo sapiens] [EntityWithAccessionedSequence:8957634] VIM [extracellular region] [Homo sapiens] [EntityWithAccessionedSequence:9646687] Vimentin [cytosol] [Homo sapiens] [EntityWithAccessionedSequence:9657898] Vimentin [microtubule organizing center] [Homo sapiens] |
| (referenceSequence) | [ModifiedResidue:9948110] O-phospho-L-serine at 39 |
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No pathways have been reviewed or authored by UniProt:P08670 VIM (67184)
