P08670 · VIME_HUMAN
- ProteinVimentin
- GeneVIM
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids466 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
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).
Protects SCRIB from proteasomal degradation and facilitates its localization to intermediate filaments in a cell contact-mediated manner (By similarity).
Involved with LARP6 in the stabilization of type I collagen mRNAs for CO1A1 and CO1A2.
Features
Showing features for site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 351 | Stutter | ||||
Sequence: F |
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Keywords
- Biological process
Enzyme and pathway databases
Protein family/group databases
Vimentin is involved in the localization of autophagosomes and lysosomes.
Names & Taxonomy
Protein names
- Recommended nameVimentin
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionP08670
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Keywords
- Cellular component
Disease & Variants
Involvement in disease
Cataract 30, multiple types (CTRCT30)
- Note
- DescriptionAn 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.
- See alsoMIM:116300
Natural variants in CTRCT30
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_070100 | 151 | E>K | in CTRCT30; the mutation increases the proteasome activity in transfected cells; causes also a severe kinetic defect in vimentin assembly both in vitro and in vivo; dbSNP:rs121917775 | |
VAR_078860 | 208 | Q>R | in CTRCT30; uncertain significance; dbSNP:rs1085307141 |
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_070100 | 151 | in CTRCT30; the mutation increases the proteasome activity in transfected cells; causes also a severe kinetic defect in vimentin assembly both in vitro and in vivo; dbSNP:rs121917775 | |||
Sequence: E → K | ||||||
Natural variant | VAR_078860 | 208 | in CTRCT30; uncertain significance; dbSNP:rs1085307141 | |||
Sequence: Q → R |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 667 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for initiator methionine, modified residue, modified residue (large scale data), chain, glycosylation, cross-link.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Initiator methionine | 1 | UniProt | Removed | ||||
Sequence: M | |||||||
Modified residue | 2 | UniProt | N-acetylserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Chain | PRO_0000063754 | 2-466 | UniProt | Vimentin | |||
Sequence: STRSVSSSSYRRMFGGPGTASRPSSSRSYVTTSTRTYSLGSALRPSTSRSLYASSPGGVYATRSSAVRLRSSVPGVRLLQDSVDFSLADAINTEFKNTRTNEKVELQELNDRFANYIDKVRFLEQQNKILLAELEQLKGQGKSRLGDLYEEEMRELRRQVDQLTNDKARVEVERDNLAEDIMRLREKLQEEMLQREEAENTLQSFRQDVDNASLARLDLERKVESLQEEIAFLKKLHEEEIQELQAQIQEQHVQIDVDVSKPDLTAALRDVRQQYESVAAKNLQEAEEWYKSKFADLSEAANRNNDALRQAKQESTEYRRQVQSLTCEVDALKGTNESLERQMREMEENFAVEAANYQDTIGRLQDEIQNMKEEMARHLREYQDLLNVKMALDIEIATYRKLLEGEESRISLPLPNFSSLNLRETNLDSLPLVDTHSKRTLLIKTVETRDGQVINETSQHHDDLE | |||||||
Modified residue (large scale data) | 3 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 5 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 5 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 7 | UniProt | Phosphoserine; by PKA and PKC; alternate | ||||
Sequence: S | |||||||
Glycosylation | 7 | UniProt | O-linked (GlcNAc) serine; alternate | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 7 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 8 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 8 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 9 | UniProt | Phosphoserine; by PKC | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 9 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 10 | UniProt | Phosphoserine; by PKC | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 10 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 20 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 20 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 22 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 25 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 25 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 26 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 26 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 27 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 29 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Glycosylation | 33 | UniProt | O-linked (GlcNAc) threonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 33 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 34 | UniProt | Phosphoserine; by PKC; alternate | ||||
Sequence: S | |||||||
Glycosylation | 34 | UniProt | O-linked (GlcNAc) serine; alternate | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 34 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 37 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 39 | UniProt | Phosphoserine; by CaMK2, PKA, PKC and ROCK2 | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 39 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 42 | UniProt | Phosphoserine; by PKC | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 42 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 47 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 47 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 48 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 49 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 49 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 51 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 51 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 53 | UniProt | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 53 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 55 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 55 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 56 | UniProt | Phosphoserine; by CDK5 and CDK1 | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 56 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 61 | UniProt | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 61 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 63 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 65 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 66 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 66 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 72 | UniProt | Phosphoserine; by AURKB and ROCK2 | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 72 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 73 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 73 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 83 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 83 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 87 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 87 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 104 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue | 117 | UniProt | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 117 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 120 | UniProt | N6-acetyllysine; alternate | ||||
Sequence: K | |||||||
Modified residue | 120 | UniProt | N6-succinyllysine; alternate | ||||
Sequence: K | |||||||
Cross-link | 120 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate | ||||
Sequence: K | |||||||
Modified residue | 129 | UniProt | N6-acetyllysine; alternate | ||||
Sequence: K | |||||||
Modified residue | 129 | UniProt | N6-succinyllysine; alternate | ||||
Sequence: K | |||||||
Cross-link | 129 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate | ||||
Sequence: K | |||||||
Modified residue | 139 | UniProt | N6-acetyllysine; alternate | ||||
Sequence: K | |||||||
Cross-link | 139 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate | ||||
Sequence: K | |||||||
Modified residue | 144 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 144 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 168 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue | 188 | UniProt | N6-acetyllysine; alternate | ||||
Sequence: K | |||||||
Modified residue | 188 | UniProt | N6-succinyllysine; alternate | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 202 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 205 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 214 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 214 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 223 | UniProt | N6-acetyllysine; alternate | ||||
Sequence: K | |||||||
Cross-link | 223 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate | ||||
Sequence: K | |||||||
Modified residue | 226 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 226 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 235 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Cross-link | 262 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 276 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 278 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 294 | UniProt | N6-acetyllysine; alternate | ||||
Sequence: K | |||||||
Modified residue | 294 | UniProt | N6-succinyllysine; alternate | ||||
Sequence: K | |||||||
Cross-link | 294 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate | ||||
Sequence: K | |||||||
Modified residue | 299 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 299 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 313 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue | 325 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 325 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 339 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 361 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 373 | UniProt | N6-acetyllysine; alternate | ||||
Sequence: K | |||||||
Cross-link | 373 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate | ||||
Sequence: K | |||||||
Modified residue | 409 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 412 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 412 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 419 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 419 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 420 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 420 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 426 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 426 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 430 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 430 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 436 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 436 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 438 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 438 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 439 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue | 445 | UniProt | N6-acetyllysine; alternate | ||||
Sequence: K | |||||||
Modified residue | 445 | UniProt | N6-succinyllysine; alternate | ||||
Sequence: K | |||||||
Cross-link | 445 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate | ||||
Sequence: K | |||||||
Cross-link | 445 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate | ||||
Sequence: K | |||||||
Modified residue | 446 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 446 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 449 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 458 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 458 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 459 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 459 | PRIDE | Phosphoserine | ||||
Sequence: S |
Post-translational modification
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).
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.
Keywords
- PTM
Proteomic databases
2D gel databases
PTM databases
Expression
Tissue specificity
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.
Gene expression databases
Organism-specific databases
Interaction
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).
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).
Identified in complexes that contain VIM, EZR, AHNAK, BFSP1, BFSP2, ANK2, PLEC, PRX and spectrin (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).
(Microbial infection) Interacts with HCV core protein.
Binary interactions
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, coiled coil, domain, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-32 | Disordered | ||||
Sequence: MSTRSVSSSSYRRMFGGPGTASRPSSSRSYVT | ||||||
Region | 2-95 | Head | ||||
Sequence: STRSVSSSSYRRMFGGPGTASRPSSSRSYVTTSTRTYSLGSALRPSTSRSLYASSPGGVYATRSSAVRLRSSVPGVRLLQDSVDFSLADAINTE | ||||||
Region | 96-131 | Coil 1A | ||||
Sequence: FKNTRTNEKVELQELNDRFANYIDKVRFLEQQNKIL | ||||||
Coiled coil | 96-131 | |||||
Sequence: FKNTRTNEKVELQELNDRFANYIDKVRFLEQQNKIL | ||||||
Domain | 103-411 | IF rod | ||||
Sequence: EKVELQELNDRFANYIDKVRFLEQQNKILLAELEQLKGQGKSRLGDLYEEEMRELRRQVDQLTNDKARVEVERDNLAEDIMRLREKLQEEMLQREEAENTLQSFRQDVDNASLARLDLERKVESLQEEIAFLKKLHEEEIQELQAQIQEQHVQIDVDVSKPDLTAALRDVRQQYESVAAKNLQEAEEWYKSKFADLSEAANRNNDALRQAKQESTEYRRQVQSLTCEVDALKGTNESLERQMREMEENFAVEAANYQDTIGRLQDEIQNMKEEMARHLREYQDLLNVKMALDIEIATYRKLLEGEESRI | ||||||
Region | 132-153 | Linker 1 | ||||
Sequence: LAELEQLKGQGKSRLGDLYEEE | ||||||
Region | 154-245 | Coil 1B | ||||
Sequence: MRELRRQVDQLTNDKARVEVERDNLAEDIMRLREKLQEEMLQREEAENTLQSFRQDVDNASLARLDLERKVESLQEEIAFLKKLHEEEIQEL | ||||||
Coiled coil | 154-245 | |||||
Sequence: MRELRRQVDQLTNDKARVEVERDNLAEDIMRLREKLQEEMLQREEAENTLQSFRQDVDNASLARLDLERKVESLQEEIAFLKKLHEEEIQEL | ||||||
Region | 246-268 | Linker 12 | ||||
Sequence: QAQIQEQHVQIDVDVSKPDLTAA | ||||||
Region | 269-407 | Coil 2 | ||||
Sequence: LRDVRQQYESVAAKNLQEAEEWYKSKFADLSEAANRNNDALRQAKQESTEYRRQVQSLTCEVDALKGTNESLERQMREMEENFAVEAANYQDTIGRLQDEIQNMKEEMARHLREYQDLLNVKMALDIEIATYRKLLEGE | ||||||
Coiled coil | 303-407 | |||||
Sequence: NRNNDALRQAKQESTEYRRQVQSLTCEVDALKGTNESLERQMREMEENFAVEAANYQDTIGRLQDEIQNMKEEMARHLREYQDLLNVKMALDIEIATYRKLLEGE | ||||||
Motif | 326-329 | [IL]-x-C-x-x-[DE] motif | ||||
Sequence: LTCE | ||||||
Region | 408-466 | Tail | ||||
Sequence: ESRISLPLPNFSSLNLRETNLDSLPLVDTHSKRTLLIKTVETRDGQVINETSQHHDDLE |
Domain
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.
Sequence similarities
Belongs to the intermediate filament family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length466
- Mass (Da)53,652
- Last updated2007-01-23 v4
- ChecksumBAB54026665B015A
Computationally mapped potential isoform sequences
There are 4 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A1B0GTT5 | A0A1B0GTT5_HUMAN | VIM | 149 | ||
A0A1B0GVG8 | A0A1B0GVG8_HUMAN | VIM | 109 | ||
B0YJC4 | B0YJC4_HUMAN | VIM | 431 | ||
B0YJC5 | B0YJC5_HUMAN | VIM | 228 |
Sequence caution
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 42 | in Ref. 1; AAA61279 | ||||
Sequence: S → D | ||||||
Sequence conflict | 113 | in Ref. 12; CAA34499 | ||||
Sequence: R → P | ||||||
Sequence conflict | 197 | in Ref. 6; CAG28618 | ||||
Sequence: E → G | ||||||
Sequence conflict | 201 | in Ref. 17; AAA61281 | ||||
Sequence: N → S | ||||||
Sequence conflict | 265 | in Ref. 17; AAA61281 | ||||
Sequence: L → S | ||||||
Sequence conflict | 278 | in Ref. 17; AAA61281 | ||||
Sequence: S → I | ||||||
Sequence conflict | 339 | in Ref. 17; AAA61281 | ||||
Sequence: S → C | ||||||
Sequence conflict | 350 | in Ref. 17; AAA61281 | ||||
Sequence: N → K | ||||||
Sequence conflict | 442 | in Ref. 1; AAA61279 | ||||
Sequence: L → F |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
M14144 EMBL· GenBank· DDBJ | AAA61279.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X56134 EMBL· GenBank· DDBJ | CAA39600.1 EMBL· GenBank· DDBJ | mRNA | ||
AF328728 EMBL· GenBank· DDBJ | AAN09720.1 EMBL· GenBank· DDBJ | mRNA | ||
Z19554 EMBL· GenBank· DDBJ | CAA79613.2 EMBL· GenBank· DDBJ | mRNA | ||
AK056766 EMBL· GenBank· DDBJ | BAB71275.1 EMBL· GenBank· DDBJ | mRNA | Sequence problems. | |
AK097336 EMBL· GenBank· DDBJ | BAC05002.1 EMBL· GenBank· DDBJ | mRNA | ||
AK290643 EMBL· GenBank· DDBJ | BAF83332.1 EMBL· GenBank· DDBJ | mRNA | ||
CR407690 EMBL· GenBank· DDBJ | CAG28618.1 EMBL· GenBank· DDBJ | mRNA | ||
AK222507 EMBL· GenBank· DDBJ | BAD96227.1 EMBL· GenBank· DDBJ | mRNA | ||
AK222602 EMBL· GenBank· DDBJ | BAD96322.1 EMBL· GenBank· DDBJ | mRNA | ||
EF445046 EMBL· GenBank· DDBJ | ACA06101.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
EF445046 EMBL· GenBank· DDBJ | ACA06102.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AL133415 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471072 EMBL· GenBank· DDBJ | EAW86215.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471072 EMBL· GenBank· DDBJ | EAW86216.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC000163 EMBL· GenBank· DDBJ | AAH00163.2 EMBL· GenBank· DDBJ | mRNA | ||
BC030573 EMBL· GenBank· DDBJ | AAH30573.1 EMBL· GenBank· DDBJ | mRNA | ||
BC066956 EMBL· GenBank· DDBJ | AAH66956.1 EMBL· GenBank· DDBJ | mRNA | ||
X16478 EMBL· GenBank· DDBJ | CAA34499.1 EMBL· GenBank· DDBJ | mRNA | ||
M18895 EMBL· GenBank· DDBJ | AAA61281.2 EMBL· GenBank· DDBJ | Genomic DNA | ||
M18888 EMBL· GenBank· DDBJ | AAA61281.2 EMBL· GenBank· DDBJ | Genomic DNA | ||
M18889 EMBL· GenBank· DDBJ | AAA61281.2 EMBL· GenBank· DDBJ | Genomic DNA | ||
M18890 EMBL· GenBank· DDBJ | AAA61281.2 EMBL· GenBank· DDBJ | Genomic DNA | ||
M18891 EMBL· GenBank· DDBJ | AAA61281.2 EMBL· GenBank· DDBJ | Genomic DNA | ||
M18892 EMBL· GenBank· DDBJ | AAA61281.2 EMBL· GenBank· DDBJ | Genomic DNA | ||
M18893 EMBL· GenBank· DDBJ | AAA61281.2 EMBL· GenBank· DDBJ | Genomic DNA | ||
M18894 EMBL· GenBank· DDBJ | AAA61281.2 EMBL· GenBank· DDBJ | Genomic DNA | ||
M25246 EMBL· GenBank· DDBJ | AAA61282.1 EMBL· GenBank· DDBJ | mRNA |