{"results":[{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"P08670","secondaryAccessions":["B0YJC2","D3DRU4","Q15867","Q15868","Q15869","Q548L2","Q6LER9","Q8N850","Q96ML2","Q9NTM3"],"uniProtkbId":"VIME_HUMAN","entryAudit":{"firstPublicDate":"1988-01-01","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2007-01-23","entryVersion":281,"sequenceVersion":4},"annotationScore":5.0,"organism":{"scientificName":"Homo sapiens","commonName":"Human","taxonId":9606,"lineage":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000312","source":"HGNC","id":"HGNC:12692"}],"value":"Vimentin"}}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000312","source":"HGNC","id":"HGNC:12692"}],"value":"VIM"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"A0A8C0N8E3"},{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P20152"},{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P31000"}],"value":"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)"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21746880"}],"value":"Involved with LARP6 in the stabilization of type I collagen mRNAs for CO1A1 and CO1A2"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P20152"},{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P31000"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10852826"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16361107"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16923132"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17505058"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18408015"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18811945"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18827015"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19386766"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20176112"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21746880"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23325789"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24940650"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26845719"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27812135"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29496907"}],"value":"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)"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15846844"}],"value":"(Microbial infection) Interacts with HCV core protein"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32418904"}],"value":"(Microbial infection) Interacts with Chandipura virus glycoprotein; this interaction might facilitate the binding of the virus to the 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