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Protein

Vimentin

Gene

VIM

Organism
Homo sapiens (Human)
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.1 Publication
Involved with LARP6 in the stabilization of type I collagen mRNAs for CO1A1 and CO1A2.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei351Stutter1

GO - Molecular functioni

  • double-stranded RNA binding Source: MGI
  • glycoprotein binding Source: UniProtKB
  • identical protein binding Source: IntAct
  • keratin filament binding Source: AgBase
  • protein C-terminus binding Source: UniProtKB
  • scaffold protein binding Source: BHF-UCL
  • structural constituent of cytoskeleton Source: UniProtKB
  • structural constituent of eye lens Source: Ensembl

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Host-virus interaction

Enzyme and pathway databases

BioCyciZFISH:ENSG00000026025-MONOMER.
ReactomeiR-HSA-264870. Caspase-mediated cleavage of cytoskeletal proteins.
R-HSA-390522. Striated Muscle Contraction.
SIGNORiP08670.

Names & Taxonomyi

Protein namesi
Recommended name:
Vimentin
Gene namesi
Name:VIM
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 10

Organism-specific databases

HGNCiHGNC:12692. VIM.

Subcellular locationi

GO - Cellular componenti

  • cell leading edge Source: Ensembl
  • cytoplasm Source: UniProtKB
  • cytoskeleton Source: UniProtKB
  • cytosol Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • extracellular matrix Source: BHF-UCL
  • focal adhesion Source: UniProtKB
  • intermediate filament Source: UniProtKB
  • intermediate filament cytoskeleton Source: HPA
  • neuron projection Source: Ensembl
  • peroxisome Source: UniProtKB
  • plasma membrane Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Intermediate filament

Pathology & Biotechi

Involvement in diseasei

Cataract 30 (CTRCT30)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease 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 also OMIM:116300
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_070100151E → 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. 1 PublicationCorresponds to variant rs121917775dbSNPEnsembl.1

Keywords - Diseasei

Cataract, Disease mutation

Organism-specific databases

DisGeNETi7431.
MalaCardsiVIM.
MIMi116300. phenotype.
OpenTargetsiENSG00000026025.
Orphaneti98984. Pulverulent cataract.
PharmGKBiPA37311.

Polymorphism and mutation databases

BioMutaiVIM.
DMDMi55977767.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00000637542 – 466VimentinAdd BLAST465

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserine1 Publication1
Modified residuei5PhosphoserineCombined sources1 Publication1
Modified residuei7Phosphoserine; by PKA and PKC; alternate1 Publication1
Glycosylationi7O-linked (GlcNAc); alternate1 Publication1
Modified residuei8Phosphoserine1 Publication1
Modified residuei9Phosphoserine; by PKC1 Publication1
Modified residuei10Phosphoserine; by PKC1 Publication1
Modified residuei11Nitrated tyrosineBy similarity1
Modified residuei20PhosphothreonineCombined sources1
Modified residuei22PhosphoserineBy similarity1
Modified residuei25PhosphoserineCombined sources1
Modified residuei26PhosphoserineCombined sources1
Glycosylationi33O-linked (GlcNAc)1 Publication1
Modified residuei34Phosphoserine; by PKC; alternateCombined sources1
Glycosylationi34O-linked (GlcNAc); alternate1 Publication1
Modified residuei39Phosphoserine; by CaMK2, PKA, PKC and ROCK2Combined sources1 Publication1
Modified residuei42Phosphoserine; by PKCCombined sources1 Publication1
Modified residuei47PhosphoserineCombined sources1
Modified residuei49PhosphoserineCombined sources1
Modified residuei51PhosphoserineCombined sources1
Modified residuei53PhosphotyrosineBy similarity1
Modified residuei55PhosphoserineBy similarity1
Modified residuei56Phosphoserine; by CDK5 and CDK1Combined sources2 Publications1
Modified residuei61PhosphotyrosineCombined sources1
Modified residuei66PhosphoserineCombined sources1
Modified residuei72Phosphoserine; by AURKB and ROCK2Combined sources2 Publications1
Modified residuei73PhosphoserineCombined sources1 Publication1
Modified residuei83PhosphoserineCombined sources1
Modified residuei87PhosphoserineCombined sources1
Modified residuei117PhosphotyrosineCombined sources1
Modified residuei120N6-acetyllysine; alternateCombined sources1
Modified residuei120N6-succinyllysine; alternateBy similarity1
Modified residuei129N6-acetyllysine; alternateBy similarity1
Modified residuei129N6-succinyllysine; alternateBy similarity1
Modified residuei139N6-acetyllysineCombined sources1
Modified residuei144PhosphoserineCombined sources1
Modified residuei168N6-acetyllysineBy similarity1
Modified residuei188N6-acetyllysine; alternateBy similarity1
Modified residuei188N6-succinyllysine; alternateBy similarity1
Modified residuei214PhosphoserineCombined sources1
Modified residuei223N6-acetyllysineBy similarity1
Modified residuei226PhosphoserineCombined sources1
Modified residuei235N6-acetyllysineBy similarity1
Modified residuei294N6-acetyllysine; alternateBy similarity1
Modified residuei294N6-succinyllysine; alternateBy similarity1
Modified residuei299PhosphoserineCombined sources1
Modified residuei325PhosphoserineBy similarity1
Modified residuei373N6-acetyllysineCombined sources1
Modified residuei383Nitrated tyrosineBy similarity1
Modified residuei409PhosphoserineCombined sources1
Modified residuei412PhosphoserineCombined sources1
Modified residuei419PhosphoserineCombined sources1
Modified residuei420PhosphoserineCombined sources1 Publication1
Modified residuei426PhosphothreonineCombined sources1
Modified residuei430PhosphoserineCombined sources1 Publication1
Modified residuei436PhosphothreonineCombined sources1
Modified residuei438PhosphoserineCombined sources1
Modified residuei445N6-acetyllysine; alternateCombined sources1
Modified residuei445N6-succinyllysine; alternateBy similarity1
Cross-linki445Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateCombined sources
Cross-linki445Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Modified residuei446PhosphothreonineCombined sources1
Modified residuei458Phosphothreonine1 Publication1
Modified residuei459PhosphoserineCombined sources1 Publication1

Post-translational modificationi

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. Phosphorylated by STK33.By similarity2 Publications
O-glycosylated during cytokinesis at sites identical or close to phosphorylation sites, this interferes with the phosphorylation status.1 Publication
S-nitrosylation is induced by interferon-gamma and oxidatively-modified low-densitity lipoprotein (LDL(ox)) possibly implicating the iNOS-S100A8/9 transnitrosylase complex.1 Publication

Keywords - PTMi

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

Proteomic databases

EPDiP08670.
PaxDbiP08670.
PeptideAtlasiP08670.
PRIDEiP08670.
TopDownProteomicsiP08670.

2D gel databases

DOSAC-COBS-2DPAGEP08670.
OGPiP08670.
REPRODUCTION-2DPAGEIPI00418471.
P08670.
SWISS-2DPAGEP08670.
UCD-2DPAGEP08670.

PTM databases

iPTMnetiP08670.
PhosphoSitePlusiP08670.
SwissPalmiP08670.

Miscellaneous databases

PMAP-CutDBP08670.

Expressioni

Tissue specificityi

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.2 Publications

Gene expression databases

BgeeiENSG00000026025.
ExpressionAtlasiP08670. baseline and differential.
GenevisibleiP08670. HS.

Organism-specific databases

HPAiCAB000080.
CAB058687.
HPA001762.

Interactioni

Subunit structurei

Homopolymer assembled from elementary dimers. Interacts with HCV core protein (PubMed:15846844). Interacts with LGSN and SYNM. Interacts (via rod region) with PLEC (via CH 1 domain) (By similarity). Interacts with SLC6A4 (PubMed:19270731). 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 BCAS3 (PubMed:17505058). Interacts with DIAPH1 (PubMed:23325789). Identified in complexes that contain VIM, EZR, AHNAK, BFSP1, BFSP2, ANK2, PLEC, PRX and spectrin (By similarity). Interacts with EPPK1; interaction is dependent of higher-order structure of intermediate filament (PubMed:16923132).By similarity10 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself6EBI-353844,EBI-353844
A8KAD63EBI-353844,EBI-10174974
P1434010EBI-353844,EBI-9844509From a different organism.
P279584EBI-353844,EBI-6377335From a different organism.
AKT1P3174929EBI-353844,EBI-296087
AKT2P317516EBI-353844,EBI-296058
BCAS3Q9H6U63EBI-353844,EBI-6083685
CRMP1Q141943EBI-353844,EBI-473101
DESP176614EBI-353844,EBI-1055572
DKFZp451B226Q5HYH73EBI-353844,EBI-10173842
GFAPP141363EBI-353844,EBI-744302
KAT7O952514EBI-353844,EBI-473199
KRT20P359004EBI-353844,EBI-742094
NEFMP071973EBI-353844,EBI-1105035
NOD2Q9HC297EBI-353844,EBI-7445625
PKN1Q165123EBI-353844,EBI-602382
PKP1Q13835-23EBI-353844,EBI-9087684
PNMA5Q96PV43EBI-353844,EBI-10171633
PPLO604373EBI-353844,EBI-368321
PRPHP412193EBI-353844,EBI-752074
RAD23BP547272EBI-353844,EBI-954531
TRIM16O953613EBI-353844,EBI-727384
TUBA1CQ9BQE33EBI-353844,EBI-1103245
YWHAZP631042EBI-353844,EBI-347088

GO - Molecular functioni

  • identical protein binding Source: IntAct
  • keratin filament binding Source: AgBase
  • protein C-terminus binding Source: UniProtKB
  • scaffold protein binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi113272. 243 interactors.
DIPiDIP-32507N.
IntActiP08670. 193 interactors.
MINTiMINT-118802.
STRINGi9606.ENSP00000224237.

Structurei

Secondary structure

1466
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi102 – 135Combined sources34
Helixi167 – 235Combined sources69
Beta strandi238 – 241Combined sources4
Turni244 – 248Combined sources5
Helixi266 – 334Combined sources69
Helixi385 – 405Combined sources21

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1GK4X-ray2.30A/B/C/D/E/F328-411[»]
1GK6X-ray1.90A/B385-412[»]
1GK7X-ray1.40A102-138[»]
3G1EX-ray1.83A/B102-138[»]
3KLTX-ray2.70A/B/C/D263-334[»]
3S4RX-ray2.45A/B99-189[»]
3SSUX-ray2.60A/B99-189[»]
3SWKX-ray1.70A/B153-238[»]
3TRTX-ray2.30A/B261-335[»]
3UF1X-ray2.81A/B/C/D144-251[»]
4MCYX-ray2.30C66-78[»]
4MCZX-ray2.41C59-71[»]
4MD0X-ray2.19C59-71[»]
4MD5X-ray1.65C66-78[»]
4MDIX-ray2.00C66-78[»]
4MDJX-ray1.70C66-78[»]
4YPCX-ray1.44A161-243[»]
4YV3X-ray2.00A/B/C161-238[»]
ProteinModelPortaliP08670.
SMRiP08670.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP08670.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni2 – 95HeadAdd BLAST94
Regioni96 – 407RodAdd BLAST312
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
Coiled coili96 – 1311 PublicationAdd BLAST36
Coiled coili154 – 2451 PublicationAdd BLAST92
Coiled coili303 – 4071 PublicationAdd BLAST105

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi326 – 329[IL]-x-C-x-x-[DE] motif1 Publication4

Domaini

The central alpha-helical coiled-coil rod region 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.1 Publication

Sequence similaritiesi

Belongs to the intermediate filament family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiENOG410IFZ1. Eukaryota.
ENOG410XRBS. LUCA.
GeneTreeiENSGT00830000128228.
HOVERGENiHBG013015.
InParanoidiP08670.
KOiK07606.
OMAiDVDNACL.
OrthoDBiEOG091G12MK.
PhylomeDBiP08670.
TreeFamiTF330122.

Family and domain databases

InterProiIPR001664. IF.
IPR006821. Intermed_filament_DNA-bd.
IPR018039. Intermediate_filament_CS.
[Graphical view]
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.

P08670-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSTRSVSSSS YRRMFGGPGT ASRPSSSRSY VTTSTRTYSL GSALRPSTSR
60 70 80 90 100
SLYASSPGGV YATRSSAVRL 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
NTLQSFRQDV DNASLARLDL ERKVESLQEE IAFLKKLHEE EIQELQAQIQ
260 270 280 290 300
EQHVQIDVDV SKPDLTAALR DVRQQYESVA AKNLQEAEEW YKSKFADLSE
310 320 330 340 350
AANRNNDALR QAKQESTEYR RQVQSLTCEV DALKGTNESL ERQMREMEEN
360 370 380 390 400
FAVEAANYQD TIGRLQDEIQ NMKEEMARHL REYQDLLNVK MALDIEIATY
410 420 430 440 450
RKLLEGEESR ISLPLPNFSS LNLRETNLDS LPLVDTHSKR TLLIKTVETR
460
DGQVINETSQ HHDDLE
Length:466
Mass (Da):53,652
Last modified:January 23, 2007 - v4
Checksum:iBAB54026665B015A
GO

Sequence cautioni

The sequence BAB71275 differs from that shown. Product of a cloning artifact.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti42S → D in AAA61279 (PubMed:3467175).Curated1
Sequence conflicti113R → P in CAA34499 (PubMed:2472876).Curated1
Sequence conflicti197E → G in CAG28618 (Ref. 6) Curated1
Sequence conflicti201N → S in AAA61281 (PubMed:3371665).Curated1
Sequence conflicti265L → S in AAA61281 (PubMed:3371665).Curated1
Sequence conflicti278S → I in AAA61281 (PubMed:3371665).Curated1
Sequence conflicti339S → C in AAA61281 (PubMed:3371665).Curated1
Sequence conflicti350N → K in AAA61281 (PubMed:3371665).Curated1
Sequence conflicti442L → F in AAA61279 (PubMed:3467175).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_070100151E → 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. 1 PublicationCorresponds to variant rs121917775dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M14144 Genomic DNA. Translation: AAA61279.1.
X56134 mRNA. Translation: CAA39600.1.
AF328728 mRNA. Translation: AAN09720.1.
Z19554 mRNA. Translation: CAA79613.2.
AK056766 mRNA. Translation: BAB71275.1. Sequence problems.
AK097336 mRNA. Translation: BAC05002.1.
AK290643 mRNA. Translation: BAF83332.1.
CR407690 mRNA. Translation: CAG28618.1.
AK222507 mRNA. Translation: BAD96227.1.
AK222602 mRNA. Translation: BAD96322.1.
EF445046 Genomic DNA. Translation: ACA06101.1.
EF445046 Genomic DNA. Translation: ACA06102.1.
AL133415 Genomic DNA. Translation: CAB87963.1.
CH471072 Genomic DNA. Translation: EAW86215.1.
CH471072 Genomic DNA. Translation: EAW86216.1.
BC000163 mRNA. Translation: AAH00163.2.
BC030573 mRNA. Translation: AAH30573.1.
BC066956 mRNA. Translation: AAH66956.1.
X16478 mRNA. Translation: CAA34499.1.
M18895
, M18888, M18889, M18890, M18891, M18892, M18893, M18894 Genomic DNA. Translation: AAA61281.2.
M25246 mRNA. Translation: AAA61282.1.
CCDSiCCDS7120.1.
PIRiS13115. A25074.
RefSeqiNP_003371.2. NM_003380.3.
XP_006717563.1. XM_006717500.1.
UniGeneiHs.455493.
Hs.691131.

Genome annotation databases

EnsembliENST00000224237; ENSP00000224237; ENSG00000026025.
ENST00000544301; ENSP00000446007; ENSG00000026025.
GeneIDi7431.
KEGGihsa:7431.

Cross-referencesi

Web resourcesi

Wikipedia

Vimentin entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M14144 Genomic DNA. Translation: AAA61279.1.
X56134 mRNA. Translation: CAA39600.1.
AF328728 mRNA. Translation: AAN09720.1.
Z19554 mRNA. Translation: CAA79613.2.
AK056766 mRNA. Translation: BAB71275.1. Sequence problems.
AK097336 mRNA. Translation: BAC05002.1.
AK290643 mRNA. Translation: BAF83332.1.
CR407690 mRNA. Translation: CAG28618.1.
AK222507 mRNA. Translation: BAD96227.1.
AK222602 mRNA. Translation: BAD96322.1.
EF445046 Genomic DNA. Translation: ACA06101.1.
EF445046 Genomic DNA. Translation: ACA06102.1.
AL133415 Genomic DNA. Translation: CAB87963.1.
CH471072 Genomic DNA. Translation: EAW86215.1.
CH471072 Genomic DNA. Translation: EAW86216.1.
BC000163 mRNA. Translation: AAH00163.2.
BC030573 mRNA. Translation: AAH30573.1.
BC066956 mRNA. Translation: AAH66956.1.
X16478 mRNA. Translation: CAA34499.1.
M18895
, M18888, M18889, M18890, M18891, M18892, M18893, M18894 Genomic DNA. Translation: AAA61281.2.
M25246 mRNA. Translation: AAA61282.1.
CCDSiCCDS7120.1.
PIRiS13115. A25074.
RefSeqiNP_003371.2. NM_003380.3.
XP_006717563.1. XM_006717500.1.
UniGeneiHs.455493.
Hs.691131.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1GK4X-ray2.30A/B/C/D/E/F328-411[»]
1GK6X-ray1.90A/B385-412[»]
1GK7X-ray1.40A102-138[»]
3G1EX-ray1.83A/B102-138[»]
3KLTX-ray2.70A/B/C/D263-334[»]
3S4RX-ray2.45A/B99-189[»]
3SSUX-ray2.60A/B99-189[»]
3SWKX-ray1.70A/B153-238[»]
3TRTX-ray2.30A/B261-335[»]
3UF1X-ray2.81A/B/C/D144-251[»]
4MCYX-ray2.30C66-78[»]
4MCZX-ray2.41C59-71[»]
4MD0X-ray2.19C59-71[»]
4MD5X-ray1.65C66-78[»]
4MDIX-ray2.00C66-78[»]
4MDJX-ray1.70C66-78[»]
4YPCX-ray1.44A161-243[»]
4YV3X-ray2.00A/B/C161-238[»]
ProteinModelPortaliP08670.
SMRiP08670.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi113272. 243 interactors.
DIPiDIP-32507N.
IntActiP08670. 193 interactors.
MINTiMINT-118802.
STRINGi9606.ENSP00000224237.

PTM databases

iPTMnetiP08670.
PhosphoSitePlusiP08670.
SwissPalmiP08670.

Polymorphism and mutation databases

BioMutaiVIM.
DMDMi55977767.

2D gel databases

DOSAC-COBS-2DPAGEP08670.
OGPiP08670.
REPRODUCTION-2DPAGEIPI00418471.
P08670.
SWISS-2DPAGEP08670.
UCD-2DPAGEP08670.

Proteomic databases

EPDiP08670.
PaxDbiP08670.
PeptideAtlasiP08670.
PRIDEiP08670.
TopDownProteomicsiP08670.

Protocols and materials databases

DNASUi7431.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000224237; ENSP00000224237; ENSG00000026025.
ENST00000544301; ENSP00000446007; ENSG00000026025.
GeneIDi7431.
KEGGihsa:7431.

Organism-specific databases

CTDi7431.
DisGeNETi7431.
GeneCardsiVIM.
H-InvDBHIX0035657.
HGNCiHGNC:12692. VIM.
HPAiCAB000080.
CAB058687.
HPA001762.
MalaCardsiVIM.
MIMi116300. phenotype.
193060. gene.
neXtProtiNX_P08670.
OpenTargetsiENSG00000026025.
Orphaneti98984. Pulverulent cataract.
PharmGKBiPA37311.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IFZ1. Eukaryota.
ENOG410XRBS. LUCA.
GeneTreeiENSGT00830000128228.
HOVERGENiHBG013015.
InParanoidiP08670.
KOiK07606.
OMAiDVDNACL.
OrthoDBiEOG091G12MK.
PhylomeDBiP08670.
TreeFamiTF330122.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000026025-MONOMER.
ReactomeiR-HSA-264870. Caspase-mediated cleavage of cytoskeletal proteins.
R-HSA-390522. Striated Muscle Contraction.
SIGNORiP08670.

Miscellaneous databases

ChiTaRSiVIM. human.
EvolutionaryTraceiP08670.
GeneWikiiVimentin.
GenomeRNAii7431.
PMAP-CutDBP08670.
PROiP08670.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000026025.
ExpressionAtlasiP08670. baseline and differential.
GenevisibleiP08670. HS.

Family and domain databases

InterProiIPR001664. IF.
IPR006821. Intermed_filament_DNA-bd.
IPR018039. Intermediate_filament_CS.
[Graphical view]
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_HUMAN
AccessioniPrimary (citable) accession number: P08670
Secondary accession number(s): B0YJC2
, D3DRU4, Q15867, Q15868, Q15869, Q548L2, Q6LER9, Q8N850, Q96ML2, Q9NTM3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 23, 2007
Last modified: November 30, 2016
This is version 216 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 10
    Human chromosome 10: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.