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Protein

Vimentin

Gene

Vim

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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)LengthDescriptionGraphical viewFeature identifierActions
Sitei351 – 3511StutterBy similarity

GO - Molecular functioni

GO - Biological processi

  • astrocyte development Source: MGI
  • Bergmann glial cell differentiation Source: MGI
  • intermediate filament-based process Source: MGI
  • intermediate filament organization Source: MGI
  • lens fiber cell development Source: MGI
  • negative regulation of neuron projection development Source: MGI
  • positive regulation of gene expression Source: UniProtKB
  • SMAD protein signal transduction Source: MGI
Complete GO annotation...

Enzyme and pathway databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
Vimentin
Gene namesi
Name:Vim
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:98932. Vim.

Subcellular locationi

GO - Cellular componenti

  • cell leading edge Source: MGI
  • cell projection Source: MGI
  • cytoplasm Source: MGI
  • cytoskeleton Source: MGI
  • cytosol Source: MGI
  • extracellular exosome Source: MGI
  • focal adhesion Source: MGI
  • intermediate filament Source: MGI
  • intermediate filament cytoskeleton Source: MGI
  • neuron projection Source: MGI
  • peroxisome Source: MGI
  • plasma membrane Source: MGI
  • type III intermediate filament Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Intermediate filament

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 466465VimentinPRO_0000063756Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity
Modified residuei5 – 51PhosphoserineBy similarity
Modified residuei7 – 71Phosphoserine; by PKA and PKC; alternate1 Publication
Glycosylationi7 – 71O-linked (GlcNAc); alternateBy similarity
Modified residuei8 – 81PhosphoserineBy similarity
Modified residuei9 – 91Phosphoserine; by PKC1 Publication
Modified residuei10 – 101Phosphoserine; by PKC1 Publication
Modified residuei11 – 111Nitrated tyrosineBy similarity
Modified residuei20 – 201PhosphothreonineBy similarity
Modified residuei21 – 211Phosphoserine; by PKC1 Publication
Modified residuei22 – 221PhosphoserineBy similarity
Modified residuei25 – 251Phosphoserine; by PKA and PKC1 Publication
Modified residuei26 – 261Phosphoserine; by PKC1 Publication
Glycosylationi33 – 331O-linked (GlcNAc)By similarity
Modified residuei34 – 341Phosphoserine; by PKC; alternate1 Publication
Glycosylationi34 – 341O-linked (GlcNAc); alternateBy similarity
Modified residuei39 – 391Phosphoserine; by CaMK2, PKA, PKC and ROCK2Combined sources3 Publications
Modified residuei42 – 421Phosphoserine; by PKC1 Publication
Modified residuei47 – 471Phosphoserine; by PKA1 Publication
Modified residuei49 – 491PhosphoserineCombined sources
Modified residuei51 – 511Phosphoserine; by PKA and PKCCombined sources1 Publication
Modified residuei53 – 531PhosphotyrosineCombined sources
Modified residuei55 – 551PhosphoserineBy similarity
Modified residuei56 – 561PhosphoserineCombined sources
Modified residuei61 – 611PhosphotyrosineCombined sources
Modified residuei66 – 661Phosphoserine; by PKA and PKCCombined sources1 Publication
Modified residuei72 – 721Phosphoserine; by AURKB and ROCK21 Publication
Modified residuei73 – 731PhosphoserineBy similarity
Modified residuei83 – 831Phosphoserine; by CaMK2Combined sources1 Publication
Modified residuei87 – 871PhosphoserineBy similarity
Modified residuei117 – 1171PhosphotyrosineBy similarity
Modified residuei120 – 1201N6-acetyllysine; alternateCombined sources
Modified residuei120 – 1201N6-succinyllysine; alternateCombined sources
Modified residuei129 – 1291N6-acetyllysine; alternateCombined sources
Modified residuei129 – 1291N6-succinyllysine; alternateCombined sources
Modified residuei139 – 1391N6-acetyllysineCombined sources
Modified residuei144 – 1441PhosphoserineBy similarity
Modified residuei168 – 1681N6-acetyllysineCombined sources
Modified residuei188 – 1881N6-acetyllysine; alternateCombined sources
Modified residuei188 – 1881N6-succinyllysine; alternateCombined sources
Modified residuei214 – 2141PhosphoserineCombined sources
Modified residuei223 – 2231N6-acetyllysineCombined sources
Modified residuei226 – 2261PhosphoserineBy similarity
Modified residuei235 – 2351N6-acetyllysineCombined sources
Modified residuei294 – 2941N6-acetyllysine; alternateCombined sources
Modified residuei294 – 2941N6-succinyllysine; alternateCombined sources
Modified residuei299 – 2991PhosphoserineBy similarity
Modified residuei325 – 3251PhosphoserineCombined sources
Modified residuei373 – 3731N6-acetyllysineCombined sources
Modified residuei383 – 3831Nitrated tyrosineBy similarity
Modified residuei409 – 4091PhosphoserineBy similarity
Modified residuei412 – 4121PhosphoserineBy similarity
Modified residuei419 – 4191PhosphoserineCombined sources
Modified residuei420 – 4201PhosphoserineCombined sources
Modified residuei426 – 4261PhosphothreonineBy similarity
Modified residuei430 – 4301PhosphoserineCombined sources
Modified residuei436 – 4361PhosphothreonineBy similarity
Modified residuei438 – 4381PhosphoserineBy similarity
Modified residuei445 – 4451N6-acetyllysine; alternateBy similarity
Modified residuei445 – 4451N6-succinyllysine; alternateCombined sources
Cross-linki445 – 445Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateBy similarity
Cross-linki445 – 445Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei446 – 4461PhosphothreonineBy similarity
Modified residuei458 – 4581PhosphothreonineBy similarity
Modified residuei459 – 4591PhosphoserineCombined sources

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 (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. Phosphorylated at Ser-56 by CDK5 during neutrophil secretion in the cytoplasm. Phosphorylated by STK33 (By similarity).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, Nitration, Phosphoprotein, S-nitrosylation, Ubl conjugation

Proteomic databases

EPDiP20152.
PaxDbiP20152.
PeptideAtlasiP20152.
PRIDEiP20152.

2D gel databases

REPRODUCTION-2DPAGEIPI00227299.
SWISS-2DPAGEP20152.
UCD-2DPAGEP20152.

PTM databases

iPTMnetiP20152.
PhosphoSiteiP20152.
SwissPalmiP20152.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiENSMUSG00000026728.
CleanExiMM_VIM.
ExpressionAtlasiP20152. baseline and differential.
GenevisibleiP20152. MM.

Interactioni

Subunit structurei

Interacts with BCAS3 (By similarity). Homopolymer assembled from elementary dimers. Interacts with HCV core protein. 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).By similarity5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Pak1P354652EBI-299269,EBI-444379From a different organism.
PASKQ96RG22EBI-299269,EBI-1042651From a different organism.
PplQ9R2692EBI-299269,EBI-368293
toxAP174524EBI-299269,EBI-9541048From a different organism.

GO - Molecular functioni

Protein-protein interaction databases

BioGridi204524. 19 interactions.
DIPiDIP-188N.
IntActiP20152. 26 interactions.
MINTiMINT-1202726.
STRINGi10090.ENSMUSP00000028062.

Structurei

3D structure databases

ProteinModelPortaliP20152.
SMRiP20152. Positions 99-238, 263-406.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 9594HeadAdd
BLAST
Regioni96 – 407312RodAdd
BLAST
Regioni96 – 13136Coil 1AAdd
BLAST
Regioni132 – 15322Linker 1Add
BLAST
Regioni154 – 24592Coil 1BAdd
BLAST
Regioni246 – 26823Linker 12Add
BLAST
Regioni269 – 407139Coil 2Add
BLAST
Regioni408 – 46659TailAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili96 – 13136Add
BLAST
Coiled coili154 – 24592Add
BLAST
Coiled coili303 – 407105Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi326 – 3294[IL]-x-C-x-x-[DE] motifBy similarity

Domaini

The central alpha-helical coiled-coil rod region 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

Sequence similaritiesi

Belongs to the intermediate filament family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiENOG410IFZ1. Eukaryota.
ENOG410XRBS. LUCA.
HOGENOMiHOG000230977.
HOVERGENiHBG013015.
InParanoidiP20152.
KOiK07606.
OMAiDVDNACL.
OrthoDBiEOG091G12MK.
PhylomeDBiP20152.
TreeFamiTF330122.

Family and domain databases

InterProiIPR001664. IF.
IPR006821. Intermed_filament_DNA-bd.
IPR018039. Intermediate_filament_CS.
IPR027699. Vimentin.
[Graphical view]
PANTHERiPTHR23239. PTHR23239. 1 hit.
PTHR23239:SF27. PTHR23239:SF27. 1 hit.
PfamiPF00038. Filament. 1 hit.
PF04732. Filament_head. 1 hit.
[Graphical view]
SMARTiSM01391. Filament. 1 hit.
[Graphical view]
PROSITEiPS00226. IF. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

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
Checksum:iA94EECEA6D70C899
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti70 – 701L → S in BAA19834 (PubMed:8543176).Curated
Sequence conflicti110 – 1156LNDRFA → ILLAEL in BAA19834 (PubMed:8543176).Curated
Sequence conflicti156 – 1572EL → DV in CAA35803 (PubMed:2140597).Curated
Sequence conflicti164 – 1641L → F in CAA39807 (Ref. 2) Curated
Sequence conflicti338 – 3381E → V in CAA35803 (PubMed:2140597).Curated
Sequence conflicti374 – 3741E → D in AAA40555 (PubMed:2744479).Curated

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.

Genome annotation databases

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

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. Positions 99-238, 263-406.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi204524. 19 interactions.
DIPiDIP-188N.
IntActiP20152. 26 interactions.
MINTiMINT-1202726.
STRINGi10090.ENSMUSP00000028062.

PTM databases

iPTMnetiP20152.
PhosphoSiteiP20152.
SwissPalmiP20152.

2D gel databases

REPRODUCTION-2DPAGEIPI00227299.
SWISS-2DPAGEP20152.
UCD-2DPAGEP20152.

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

CTDi7431.
MGIiMGI:98932. Vim.

Phylogenomic databases

eggNOGiENOG410IFZ1. Eukaryota.
ENOG410XRBS. LUCA.
HOGENOMiHOG000230977.
HOVERGENiHBG013015.
InParanoidiP20152.
KOiK07606.
OMAiDVDNACL.
OrthoDBiEOG091G12MK.
PhylomeDBiP20152.
TreeFamiTF330122.

Enzyme and pathway databases

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

Miscellaneous databases

ChiTaRSiVim. mouse.
PROiP20152.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000026728.
CleanExiMM_VIM.
ExpressionAtlasiP20152. baseline and differential.
GenevisibleiP20152. MM.

Family and domain databases

InterProiIPR001664. IF.
IPR006821. Intermed_filament_DNA-bd.
IPR018039. Intermediate_filament_CS.
IPR027699. Vimentin.
[Graphical view]
PANTHERiPTHR23239. PTHR23239. 1 hit.
PTHR23239:SF27. PTHR23239:SF27. 1 hit.
PfamiPF00038. Filament. 1 hit.
PF04732. Filament_head. 1 hit.
[Graphical view]
SMARTiSM01391. Filament. 1 hit.
[Graphical view]
PROSITEiPS00226. IF. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiVIME_MOUSE
AccessioniPrimary (citable) accession number: P20152
Secondary accession number(s): O08704, Q8CCH1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: January 23, 2007
Last modified: September 7, 2016
This is version 177 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.