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Protein

Vimentin

Gene

VIM

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -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

GO - Biological processi

Keywordsi

Biological processHost-virus interaction

Enzyme and pathway databases

ReactomeiR-HSA-264870 Caspase-mediated cleavage of cytoskeletal proteins
R-HSA-390522 Striated Muscle Contraction
R-HSA-6785807 Interleukin-4 and Interleukin-13 signaling
SIGNORiP08670

Protein family/group databases

MoonDBiP08670 Predicted

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

EuPathDBiHostDB:ENSG00000026025.13
HGNCiHGNC:12692 VIM
MIMi193060 gene
neXtProtiNX_P08670

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

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Intermediate filament, Nucleus

Pathology & Biotechi

Involvement in diseasei

Cataract 30, multiple types (CTRCT30)3 Publications
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 dbSNP:rs121917775EnsemblClinVar.1
Natural variantiVAR_078860208Q → R in CTRCT30; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs1085307141Ensembl.1

Keywords - Diseasei

Cataract, Disease mutation

Organism-specific databases

DisGeNETi7431
MalaCardsiVIM
MIMi116300 phenotype
OpenTargetsiENSG00000026025
Orphaneti98984 Pulverulent cataract
PharmGKBiPA37311

Chemistry databases

ChEMBLiCHEMBL3712854

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) serine; alternate1 Publication1
Modified residuei8Phosphoserine1 Publication1
Modified residuei9Phosphoserine; by PKC1 Publication1
Modified residuei10Phosphoserine; by PKC1 Publication1
Modified residuei20PhosphothreonineCombined sources1
Modified residuei25PhosphoserineCombined sources1
Modified residuei26PhosphoserineCombined sources1
Glycosylationi33O-linked (GlcNAc) threonine1 Publication1
Modified residuei34Phosphoserine; by PKC; alternateCombined sources1
Glycosylationi34O-linked (GlcNAc) serine; 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
Cross-linki104Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei117PhosphotyrosineCombined sources1
Modified residuei120N6-acetyllysine; alternateCombined sources1
Modified residuei120N6-succinyllysine; alternateBy similarity1
Cross-linki120Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Modified residuei129N6-acetyllysine; alternateBy similarity1
Modified residuei129N6-succinyllysine; alternateBy similarity1
Cross-linki129Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Modified residuei139N6-acetyllysine; alternateCombined sources1
Cross-linki139Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Modified residuei144PhosphoserineCombined sources1
Modified residuei168N6-acetyllysineBy similarity1
Modified residuei188N6-acetyllysine; alternateBy similarity1
Modified residuei188N6-succinyllysine; alternateBy similarity1
Modified residuei214PhosphoserineCombined sources1
Modified residuei223N6-acetyllysine; alternateBy similarity1
Cross-linki223Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Modified residuei226PhosphoserineCombined sources1
Modified residuei235N6-acetyllysineBy similarity1
Cross-linki262Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei294N6-acetyllysine; alternateBy similarity1
Modified residuei294N6-succinyllysine; alternateBy similarity1
Cross-linki294Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Modified residuei299PhosphoserineCombined sources1
Cross-linki313Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei325PhosphoserineBy similarity1
Modified residuei373N6-acetyllysine; alternateCombined sources1
Cross-linki373Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
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
Cross-linki439Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
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 (PubMed:21465480). Phosphorylated by STK33 (PubMed:18811945). Phosphorylated on tyrosine residues by SRMS (PubMed:29496907).By similarity4 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, Phosphoprotein, S-nitrosylation, Ubl conjugation

Proteomic databases

EPDiP08670
PaxDbiP08670
PeptideAtlasiP08670
PRIDEiP08670
ProteomicsDBi52153
TopDownProteomicsiP08670

2D gel databases

DOSAC-COBS-2DPAGEiP08670
OGPiP08670
REPRODUCTION-2DPAGEiIPI00418471
P08670
SWISS-2DPAGEiP08670
UCD-2DPAGEiP08670

PTM databases

CarbonylDBiP08670
iPTMnetiP08670
PhosphoSitePlusiP08670
SwissPalmiP08670

Miscellaneous databases

PMAP-CutDBiP08670

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

Inductioni

Up-regulated by muramyl-dipeptide and lipopolysaccharide.1 Publication

Gene expression databases

BgeeiENSG00000026025 Expressed in 241 organ(s), highest expression level in dorsal root ganglion
ExpressionAtlasiP08670 baseline and differential
GenevisibleiP08670 HS

Organism-specific databases

HPAiCAB000080
CAB058687
HPA001762

Interactioni

Subunit structurei

Homopolymer assembled from elementary dimers. 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). 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).By similarity12 Publications
(Microbial infection) Interacts with HCV core protein.1 Publication

Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

BioGridi113272, 273 interactors
CORUMiP08670
DIPiDIP-32507N
IntActiP08670, 203 interactors
MINTiP08670
STRINGi9606.ENSP00000224237

Structurei

Secondary structure

1466
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliP08670
SMRiP08670
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP08670

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini103 – 411IF rodPROSITE-ProRule annotationAdd BLAST309

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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
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 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.1 Publication

Sequence similaritiesi

Belongs to the intermediate filament family.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiENOG410IFZ1 Eukaryota
ENOG410XRBS LUCA
GeneTreeiENSGT00910000143989
HOVERGENiHBG013015
InParanoidiP08670
KOiK07606
OMAiQVINEST
OrthoDBiEOG091G12MK
PhylomeDBiP08670
TreeFamiTF330122

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

Sequence (1+)i

Sequence statusi: Complete.

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

This entry has 1 described isoform and 4 potential isoforms that are computationally mapped.Show allAlign All

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

Computationally mapped potential isoform sequencesi

There are 4 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
B0YJC5B0YJC5_HUMAN
Vimentin variant 4
VIM
228Annotation score:
B0YJC4B0YJC4_HUMAN
Vimentin variant 3
VIM
431Annotation score:
A0A1B0GTT5A0A1B0GTT5_HUMAN
Vimentin
VIM
149Annotation score:
A0A1B0GVG8A0A1B0GVG8_HUMAN
Vimentin
VIM
109Annotation score:

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 dbSNP:rs121917775EnsemblClinVar.1
Natural variantiVAR_078860208Q → R in CTRCT30; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs1085307141Ensembl.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 No translation available.
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
Hs.728090

Genome annotation databases

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

Similar proteinsi

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 No translation available.
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
Hs.728090

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[»]
5WHFX-ray2.25A/B/C/D/E/F/G/H153-238[»]
6ATFX-ray1.90C/F59-71[»]
6ATIX-ray1.98C/F59-71[»]
6BIRX-ray2.30C419-431[»]
ProteinModelPortaliP08670
SMRiP08670
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi113272, 273 interactors
CORUMiP08670
DIPiDIP-32507N
IntActiP08670, 203 interactors
MINTiP08670
STRINGi9606.ENSP00000224237

Chemistry databases

ChEMBLiCHEMBL3712854

Protein family/group databases

MoonDBiP08670 Predicted

PTM databases

CarbonylDBiP08670
iPTMnetiP08670
PhosphoSitePlusiP08670
SwissPalmiP08670

Polymorphism and mutation databases

BioMutaiVIM
DMDMi55977767

2D gel databases

DOSAC-COBS-2DPAGEiP08670
OGPiP08670
REPRODUCTION-2DPAGEiIPI00418471
P08670
SWISS-2DPAGEiP08670
UCD-2DPAGEiP08670

Proteomic databases

EPDiP08670
PaxDbiP08670
PeptideAtlasiP08670
PRIDEiP08670
ProteomicsDBi52153
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
EuPathDBiHostDB:ENSG00000026025.13
GeneCardsiVIM
H-InvDBiHIX0035657
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
GeneTreeiENSGT00910000143989
HOVERGENiHBG013015
InParanoidiP08670
KOiK07606
OMAiQVINEST
OrthoDBiEOG091G12MK
PhylomeDBiP08670
TreeFamiTF330122

Enzyme and pathway databases

ReactomeiR-HSA-264870 Caspase-mediated cleavage of cytoskeletal proteins
R-HSA-390522 Striated Muscle Contraction
R-HSA-6785807 Interleukin-4 and Interleukin-13 signaling
SIGNORiP08670

Miscellaneous databases

ChiTaRSiVIM human
EvolutionaryTraceiP08670
GeneWikiiVimentin
GenomeRNAii7431
PMAP-CutDBiP08670
PROiPR:P08670
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000026025 Expressed in 241 organ(s), highest expression level in dorsal root ganglion
ExpressionAtlasiP08670 baseline and differential
GenevisibleiP08670 HS

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
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 historyiIntegrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 23, 2007
Last modified: November 7, 2018
This is version 237 of the entry and version 4 of the sequence. See 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. SIMILARITY comments
    Index of protein domains and families
  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. Human chromosome 10
    Human chromosome 10: entries, gene names and cross-references to MIM
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