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Protein

Vimentin

Gene

Vim

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

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.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei351StutterBy similarity1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-MMU-264870 Caspase-mediated cleavage of cytoskeletal proteins
R-MMU-390522 Striated Muscle Contraction

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Vimentin
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:Vim
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiMus musculus (Mouse)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri10090 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000589 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 2

Organism-specific databases

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

More...
MGIi
MGI:98932 Vim

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Intermediate filament, Nucleus

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemovedBy similarity
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000637562 – 466VimentinAdd BLAST465

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei2N-acetylserineBy similarity1
Modified residuei5PhosphoserineBy similarity1
Modified residuei7Phosphoserine; by PKA and PKC; alternate1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi7O-linked (GlcNAc) serine; alternateBy similarity1
Modified residuei8PhosphoserineBy similarity1
Modified residuei9Phosphoserine; by PKC1 Publication1
Modified residuei10Phosphoserine; by PKC1 Publication1
Modified residuei20PhosphothreonineBy similarity1
Modified residuei21Phosphoserine; by PKC1 Publication1
Modified residuei25Phosphoserine; by PKA and PKC1 Publication1
Modified residuei26Phosphoserine; by PKC1 Publication1
Glycosylationi33O-linked (GlcNAc) threonineBy similarity1
Modified residuei34Phosphoserine; by PKC; alternate1 Publication1
Glycosylationi34O-linked (GlcNAc) serine; alternateBy similarity1
Modified residuei39Phosphoserine; by CaMK2, PKA, PKC and ROCK2Combined sources3 Publications1
Modified residuei42Phosphoserine; by PKC1 Publication1
Modified residuei47Phosphoserine; by PKA1 Publication1
Modified residuei49PhosphoserineCombined sources1
Modified residuei51Phosphoserine; by PKA and PKCCombined sources1 Publication1
Modified residuei53PhosphotyrosineCombined sources1
Modified residuei55PhosphoserineBy similarity1
Modified residuei56PhosphoserineCombined sources1
Modified residuei61PhosphotyrosineCombined sources1
Modified residuei66Phosphoserine; by PKA and PKCCombined sources1 Publication1
Modified residuei72Phosphoserine; by AURKB and ROCK21 Publication1
Modified residuei73PhosphoserineBy similarity1
Modified residuei83Phosphoserine; by CaMK2Combined sources1 Publication1
Modified residuei87PhosphoserineBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki104Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei117PhosphotyrosineBy similarity1
Modified residuei120N6-acetyllysine; alternateCombined sources1
Modified residuei120N6-succinyllysine; alternateCombined sources1
Cross-linki120Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei129N6-acetyllysine; alternateCombined sources1
Modified residuei129N6-succinyllysine; alternateCombined sources1
Cross-linki129Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei139N6-acetyllysine; alternateCombined sources1
Cross-linki139Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei144PhosphoserineBy similarity1
Modified residuei168N6-acetyllysineCombined sources1
Modified residuei188N6-acetyllysine; alternateCombined sources1
Modified residuei188N6-succinyllysine; alternateCombined sources1
Modified residuei214PhosphoserineCombined sources1
Modified residuei223N6-acetyllysine; alternateCombined sources1
Cross-linki223Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei226PhosphoserineBy similarity1
Modified residuei235N6-acetyllysineCombined sources1
Cross-linki262Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei294N6-acetyllysine; alternateCombined sources1
Modified residuei294N6-succinyllysine; alternateCombined sources1
Cross-linki294Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei299PhosphoserineBy similarity1
Cross-linki313Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei325PhosphoserineCombined sources1
Modified residuei373N6-acetyllysine; alternateCombined sources1
Cross-linki373Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei409PhosphoserineBy similarity1
Modified residuei412PhosphoserineBy similarity1
Modified residuei419PhosphoserineCombined sources1
Modified residuei420PhosphoserineCombined sources1
Modified residuei426PhosphothreonineBy similarity1
Modified residuei430PhosphoserineCombined sources1
Modified residuei436PhosphothreonineBy similarity1
Modified residuei438PhosphoserineBy similarity1
Cross-linki439Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei445N6-acetyllysine; alternateBy similarity1
Modified residuei445N6-succinyllysine; alternateCombined sources1
Cross-linki445Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateBy similarity
Cross-linki445Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei446PhosphothreonineBy similarity1
Modified residuei458PhosphothreonineBy similarity1
Modified residuei459PhosphoserineCombined sources1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Phosphorylation by PKN1 inhibits the formation of filaments. Filament disassembly during mitosis is promoted by phosphorylation at Ser-55 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-56 by CDK5 during neutrophil secretion in the cytoplasm. Phosphorylated by STK33. Phosphorylated on tyrosine residues by SRMS.By similarity
S-nitrosylation is induced by interferon-gamma and oxidatively-modified low-densitity lipoprotein (LDL(ox)) possibly implicating the iNOS-S100A8/9 transnitrosylase complex.By similarity

Keywords - PTMi

Acetylation, Glycoprotein, Isopeptide bond, Phosphoprotein, S-nitrosylation, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
P20152

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
P20152

PeptideAtlas

More...
PeptideAtlasi
P20152

PRoteomics IDEntifications database

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PRIDEi
P20152

2D gel databases

REPRODUCTION-2DPAGE

More...
REPRODUCTION-2DPAGEi
IPI00227299

Two-dimensional polyacrylamide gel electrophoresis database from the Geneva University Hospital

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SWISS-2DPAGEi
P20152

University College Dublin 2-DE Proteome Database

More...
UCD-2DPAGEi
P20152

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P20152

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...
PhosphoSitePlusi
P20152

SwissPalm database of S-palmitoylation events

More...
SwissPalmi
P20152

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Detected in eye lens fiber cells (at protein level).1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSMUSG00000026728 Expressed in 330 organ(s), highest expression level in dorsal root ganglion

CleanEx database of gene expression profiles

More...
CleanExi
MM_VIM

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
P20152 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
P20152 MM

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Interacts with BCAS3 (By similarity). Homopolymer assembled from elementary dimers. Interacts with LGSN (PubMed:18178558). Interacts with SYNM (PubMed:17356066). Interacts (via rod region) with PLEC (via CH 1 domain) (PubMed:15128297). Interacts with SLC6A4. Interacts with STK33. Interacts with LARP6. Interacts with RAB8B. Interacts with TOR1A; the interaction associates TOR1A with the cytoskeleton. Interacts with TOR1AIP1. Interacts with DIAPH1 (By similarity). Identified in complexes that contain VIM, EZR, AHNAK, BFSP1, BFSP2, ANK2, PLEC, PRX and spectrin (PubMed:21745462). 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 (PubMed:27178841).By similarity6 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
204524, 23 interactors

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
P20152

Database of interacting proteins

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DIPi
DIP-188N

Protein interaction database and analysis system

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IntActi
P20152, 32 interactors

Molecular INTeraction database

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MINTi
P20152

STRING: functional protein association networks

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STRINGi
10090.ENSMUSP00000028062

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P20152

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
P20152

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini103 – 411IF rodPROSITE-ProRule annotationAdd BLAST309

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni2 – 95HeadAdd BLAST94
Regioni96 – 131Coil 1AAdd BLAST36
Regioni132 – 153Linker 1Add BLAST22
Regioni154 – 245Coil 1BAdd BLAST92
Regioni246 – 268Linker 12Add BLAST23
Regioni269 – 407Coil 2Add BLAST139
Regioni408 – 466TailAdd BLAST59

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and domains’ section denotes the positions of regions of coiled coil within the protein.<p><a href='/help/coiled' target='_top'>More...</a></p>Coiled coili96 – 131Add BLAST36
Coiled coili154 – 245Add BLAST92
Coiled coili303 – 407Add BLAST105

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi326 – 329[IL]-x-C-x-x-[DE] motifBy similarity4

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The central alpha-helical coiled-coil IF rod domain mediates elementary homodimerization.By similarity
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.By similarity

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the intermediate filament family.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG410IFZ1 Eukaryota
ENOG410XRBS LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000156146

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000230977

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG013015

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P20152

KEGG Orthology (KO)

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KOi
K07606

Database of Orthologous Groups

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OrthoDBi
EOG091G12MK

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P20152

TreeFam database of animal gene trees

More...
TreeFami
TF330122

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR001664 IF
IPR018039 IF_conserved
IPR039008 IF_rod_dom
IPR006821 Intermed_filament_DNA-bd
IPR027699 Vimentin

The PANTHER Classification System

More...
PANTHERi
PTHR23239 PTHR23239, 1 hit
PTHR23239:SF27 PTHR23239:SF27, 1 hit

Pfam protein domain database

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Pfami
View protein in Pfam
PF00038 Filament, 1 hit
PF04732 Filament_head, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM01391 Filament, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00226 IF_ROD_1, 1 hit
PS51842 IF_ROD_2, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry has 1 described isoform and 2 potential isoforms that are computationally mapped.Show allAlign All

P20152-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSTRSVSSSS YRRMFGGSGT SSRPSSNRSY VTTSTRTYSL GSALRPSTSR
60 70 80 90 100
SLYSSSPGGA YVTRSSAVRL RSSVPGVRLL QDSVDFSLAD AINTEFKNTR
110 120 130 140 150
TNEKVELQEL NDRFANYIDK VRFLEQQNKI LLAELEQLKG QGKSRLGDLY
160 170 180 190 200
EEEMRELRRQ VDQLTNDKAR VEVERDNLAE DIMRLREKLQ EEMLQREEAE
210 220 230 240 250
STLQSFRQDV DNASLARLDL ERKVESLQEE IAFLKKLHDE EIQELQAQIQ
260 270 280 290 300
EQHVQIDVDV SKPDLTAALR DVRQQYESVA AKNLQEAEEW YKSKFADLSE
310 320 330 340 350
AANRNNDALR QAKQESNEYR RQVQSLTCEV DALKGTNESL ERQMREMEEN
360 370 380 390 400
FALEAANYQD TIGRLQDEIQ NMKEEMARHL REYQDLLNVK MALDIEIATY
410 420 430 440 450
RKLLEGEESR ISLPLPTFSS LNLRETNLES LPLVDTHSKR TLLIKTVETR
460
DGQVINETSQ HHDDLE
Length:466
Mass (Da):53,688
Last modified:January 23, 2007 - v3
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iA94EECEA6D70C899
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A2AKJ2A2AKJ2_MOUSE
Vimentin
Vim
134Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
A0A0A6YWC8A0A0A6YWC8_MOUSE
Vimentin
Vim
427Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti70L → S in BAA19834 (PubMed:8543176).Curated1
Sequence conflicti110 – 115LNDRFA → ILLAEL in BAA19834 (PubMed:8543176).Curated6
Sequence conflicti156 – 157EL → DV in CAA35803 (PubMed:2140597).Curated2
Sequence conflicti164L → F in CAA39807 (Ref. 2) Curated1
Sequence conflicti338E → V in CAA35803 (PubMed:2140597).Curated1
Sequence conflicti374E → D in AAA40555 (PubMed:2744479).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
M24849 mRNA Translation: AAA40555.1
X56397 mRNA Translation: CAA39807.1
M26251 mRNA Translation: AAA40556.1
Z22526 Genomic DNA Translation: CAA80251.1
X51438 mRNA Translation: CAA35803.1
Y07738 Genomic DNA Translation: CAA69019.1
AK033175 mRNA Translation: BAC28181.1
D50805 Genomic DNA Translation: BAA19834.1

The Consensus CDS (CCDS) project

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CCDSi
CCDS15696.1

Protein sequence database of the Protein Information Resource

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PIRi
A43803

NCBI Reference Sequences

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RefSeqi
NP_035831.2, NM_011701.4

UniGene gene-oriented nucleotide sequence clusters

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UniGenei
Mm.268000

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENSMUST00000028062; ENSMUSP00000028062; ENSMUSG00000026728

Database of genes from NCBI RefSeq genomes

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GeneIDi
22352

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
mmu:22352

UCSC genome browser

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UCSCi
uc008ikb.2 mouse

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M24849 mRNA Translation: AAA40555.1
X56397 mRNA Translation: CAA39807.1
M26251 mRNA Translation: AAA40556.1
Z22526 Genomic DNA Translation: CAA80251.1
X51438 mRNA Translation: CAA35803.1
Y07738 Genomic DNA Translation: CAA69019.1
AK033175 mRNA Translation: BAC28181.1
D50805 Genomic DNA Translation: BAA19834.1
CCDSiCCDS15696.1
PIRiA43803
RefSeqiNP_035831.2, NM_011701.4
UniGeneiMm.268000

3D structure databases

ProteinModelPortaliP20152
SMRiP20152
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi204524, 23 interactors
CORUMiP20152
DIPiDIP-188N
IntActiP20152, 32 interactors
MINTiP20152
STRINGi10090.ENSMUSP00000028062

PTM databases

iPTMnetiP20152
PhosphoSitePlusiP20152
SwissPalmiP20152

2D gel databases

REPRODUCTION-2DPAGEiIPI00227299
SWISS-2DPAGEiP20152
UCD-2DPAGEiP20152

Proteomic databases

EPDiP20152
PaxDbiP20152
PeptideAtlasiP20152
PRIDEiP20152

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000028062; ENSMUSP00000028062; ENSMUSG00000026728
GeneIDi22352
KEGGimmu:22352
UCSCiuc008ikb.2 mouse

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
7431
MGIiMGI:98932 Vim

Phylogenomic databases

eggNOGiENOG410IFZ1 Eukaryota
ENOG410XRBS LUCA
GeneTreeiENSGT00940000156146
HOGENOMiHOG000230977
HOVERGENiHBG013015
InParanoidiP20152
KOiK07606
OrthoDBiEOG091G12MK
PhylomeDBiP20152
TreeFamiTF330122

Enzyme and pathway databases

ReactomeiR-MMU-264870 Caspase-mediated cleavage of cytoskeletal proteins
R-MMU-390522 Striated Muscle Contraction

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

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ChiTaRSi
Vim mouse

Protein Ontology

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PROi
PR:P20152

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSMUSG00000026728 Expressed in 330 organ(s), highest expression level in dorsal root ganglion
CleanExiMM_VIM
ExpressionAtlasiP20152 baseline and differential
GenevisibleiP20152 MM

Family and domain databases

InterProiView protein in InterPro
IPR001664 IF
IPR018039 IF_conserved
IPR039008 IF_rod_dom
IPR006821 Intermed_filament_DNA-bd
IPR027699 Vimentin
PANTHERiPTHR23239 PTHR23239, 1 hit
PTHR23239:SF27 PTHR23239:SF27, 1 hit
PfamiView protein in Pfam
PF00038 Filament, 1 hit
PF04732 Filament_head, 1 hit
SMARTiView protein in SMART
SM01391 Filament, 1 hit
PROSITEiView protein in PROSITE
PS00226 IF_ROD_1, 1 hit
PS51842 IF_ROD_2, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiVIME_MOUSE
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P20152
Secondary accession number(s): O08704, Q8CCH1
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: January 23, 2007
Last modified: December 5, 2018
This is version 198 of the entry and version 3 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
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