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P08670

- VIME_HUMAN

UniProt

P08670 - VIME_HUMAN

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Protein

Vimentin

Gene

VIM

Organism
Homo sapiens (Human)
Status
Reviewed - 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)LengthDescriptionGraphical viewFeature identifierActions
Sitei351 – 3511Stutter

GO - Molecular functioni

  1. double-stranded RNA binding Source: MGI
  2. glycoprotein binding Source: UniProt
  3. identical protein binding Source: IntAct
  4. protein C-terminus binding Source: UniProtKB
  5. scaffold protein binding Source: BHF-UCL
  6. structural constituent of cytoskeleton Source: UniProtKB
  7. structural constituent of eye lens Source: Ensembl

GO - Biological processi

  1. apoptotic process Source: Reactome
  2. astrocyte development Source: Ensembl
  3. Bergmann glial cell differentiation Source: Ensembl
  4. cellular component disassembly involved in execution phase of apoptosis Source: Reactome
  5. cellular component movement Source: UniProtKB
  6. intermediate filament organization Source: Ensembl
  7. lens fiber cell development Source: Ensembl
  8. muscle filament sliding Source: Reactome
  9. negative regulation of neuron projection development Source: Ensembl
  10. positive regulation of gene expression Source: Ensembl
  11. viral process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Host-virus interaction

Enzyme and pathway databases

ReactomeiREACT_13541. Caspase-mediated cleavage of cytoskeletal proteins.
REACT_16969. Striated Muscle Contraction.

Names & Taxonomyi

Protein namesi
Recommended name:
Vimentin
Gene namesi
Name:VIM
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 10

Organism-specific databases

HGNCiHGNC:12692. VIM.

Subcellular locationi

Cytoplasm 1 Publication

GO - Cellular componenti

  1. cell leading edge Source: Ensembl
  2. cytoplasm Source: UniProtKB
  3. cytoskeleton Source: UniProtKB
  4. cytosol Source: UniProtKB
  5. extracellular vesicular exosome Source: UniProtKB
  6. focal adhesion Source: UniProtKB
  7. intermediate filament Source: UniProtKB
  8. intermediate filament cytoskeleton Source: HPA
  9. neuron projection Source: Ensembl
  10. peroxisome Source: UniProtKB
  11. plasma membrane Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Intermediate filament

Pathology & Biotechi

Involvement in diseasei

Cataract 30 (CTRCT30) [MIM:116300]: An 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.
Note: The disease is caused by mutations affecting the gene represented in this entry.

Keywords - Diseasei

Cataract, Disease mutation

Organism-specific databases

MIMi116300. phenotype.
Orphaneti98984. Pulverulent cataract.
PharmGKBiPA37311.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 466465VimentinPRO_0000063754Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine1 Publication
Modified residuei5 – 51Phosphoserine2 Publications
Modified residuei7 – 71Phosphoserine; by PKA and PKC; alternate1 Publication
Glycosylationi7 – 71O-linked (GlcNAc); alternate1 Publication
Modified residuei8 – 81Phosphoserine1 Publication
Modified residuei9 – 91Phosphoserine; by PKC1 Publication
Modified residuei10 – 101Phosphoserine; by PKC1 Publication
Modified residuei20 – 201Phosphothreonine1 Publication
Modified residuei25 – 251Phosphoserine1 Publication
Modified residuei26 – 261Phosphoserine; by PKCBy similarity
Modified residuei27 – 271Phosphoserine
Modified residuei29 – 291Phosphoserine
Modified residuei33 – 331Phosphothreonine; alternate
Glycosylationi33 – 331O-linked (GlcNAc); alternate1 Publication
Modified residuei34 – 341Phosphoserine; alternate1 Publication
Glycosylationi34 – 341O-linked (GlcNAc); alternate1 Publication
Modified residuei38 – 381Phosphotyrosine
Modified residuei39 – 391Phosphoserine; by CaMK2, PKA, PKC and ROCK22 Publications
Modified residuei42 – 421Phosphoserine; by PKC3 Publications
Modified residuei47 – 471Phosphoserine1 Publication
Modified residuei49 – 491PhosphoserineBy similarity
Modified residuei51 – 511Phosphoserine4 Publications
Modified residuei53 – 531Phosphotyrosine
Modified residuei55 – 551Phosphoserine
Modified residuei56 – 561Phosphoserine; by CDK5 and CDK16 Publications
Modified residuei61 – 611Phosphotyrosine2 Publications
Modified residuei66 – 661Phosphoserine; by PKA and PKCBy similarity
Modified residuei72 – 721Phosphoserine; by AURKB and ROCK23 Publications
Modified residuei73 – 731Phosphoserine3 Publications
Modified residuei83 – 831Phosphoserine2 Publications
Modified residuei117 – 1171Phosphotyrosine1 Publication
Modified residuei120 – 1201N6-acetyllysine; alternate1 Publication
Modified residuei120 – 1201N6-succinyllysine; alternateBy similarity
Modified residuei129 – 1291N6-acetyllysine; alternateBy similarity
Modified residuei129 – 1291N6-succinyllysine; alternateBy similarity
Modified residuei139 – 1391N6-acetyllysine1 Publication
Modified residuei144 – 1441Phosphoserine3 Publications
Modified residuei168 – 1681N6-acetyllysineBy similarity
Modified residuei188 – 1881N6-acetyllysine; alternateBy similarity
Modified residuei188 – 1881N6-succinyllysine; alternateBy similarity
Modified residuei214 – 2141Phosphoserine2 Publications
Modified residuei223 – 2231N6-acetyllysineBy similarity
Modified residuei226 – 2261Phosphoserine1 Publication
Modified residuei235 – 2351N6-acetyllysineBy similarity
Modified residuei261 – 2611Phosphoserine
Modified residuei266 – 2661Phosphothreonine
Modified residuei294 – 2941N6-acetyllysine; alternateBy similarity
Modified residuei294 – 2941N6-succinyllysine; alternateBy similarity
Modified residuei299 – 2991Phosphoserine1 Publication
Modified residuei373 – 3731N6-acetyllysine1 Publication
Modified residuei409 – 4091Phosphoserine1 Publication
Modified residuei412 – 4121Phosphoserine5 Publications
Modified residuei419 – 4191Phosphoserine1 Publication
Modified residuei420 – 4201Phosphoserine2 Publications
Modified residuei426 – 4261Phosphothreonine1 Publication
Modified residuei430 – 4301Phosphoserine2 Publications
Modified residuei436 – 4361Phosphothreonine1 Publication
Modified residuei445 – 4451N6-acetyllysine; alternate1 Publication
Modified residuei445 – 4451N6-succinyllysine; alternateBy similarity
Modified residuei446 – 4461Phosphothreonine
Modified residuei458 – 4581Phosphothreonine1 Publication
Modified residuei459 – 4591Phosphoserine4 Publications

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 similarity6 Publications
O-glycosylated during cytokinesis at sites identical or close to phosphorylation sites, this interferes with the phosphorylation status.1 Publication

Keywords - PTMi

Acetylation, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiP08670.
PaxDbiP08670.
PeptideAtlasiP08670.
PRIDEiP08670.

2D gel databases

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

PTM databases

PhosphoSiteiP08670.

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

BgeeiP08670.
ExpressionAtlasiP08670. baseline and differential.
GenevestigatoriP08670.

Organism-specific databases

HPAiCAB000080.
CAB058687.
HPA001762.

Interactioni

Subunit structurei

Homopolymer assembled from elementary dimers. Interacts with HCV core protein. Interacts with LGSN and SYNM. Interacts (via rod region) with PLEC (via CH 1 domain). 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 BCAS3.8 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself6EBI-353844,EBI-353844
AKT1P3174929EBI-353844,EBI-296087
AKT2P317516EBI-353844,EBI-296058
BCAS3Q9H6U63EBI-353844,EBI-6083685
CRMP1Q141943EBI-353844,EBI-473101
KAT7O952514EBI-353844,EBI-473199
PKP1Q13835-23EBI-353844,EBI-9087684
RAD23BP547272EBI-353844,EBI-954531
TRIM16O953613EBI-353844,EBI-727384
YWHAZP631042EBI-353844,EBI-347088

Protein-protein interaction databases

BioGridi113272. 200 interactions.
DIPiDIP-32507N.
IntActiP08670. 133 interactions.
MINTiMINT-118802.

Structurei

Secondary structure

1
466
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi102 – 13534Combined sources
Helixi155 – 20753Combined sources
Helixi210 – 23425Combined sources
Turni244 – 2485Combined sources
Helixi266 – 33469Combined sources
Helixi385 – 40521Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP08670.
SMRiP08670. Positions 99-248, 263-406.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP08670.

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 – 131361 PublicationAdd
BLAST
Coiled coili154 – 245921 PublicationAdd
BLAST
Coiled coili303 – 4071051 PublicationAdd
BLAST

Domaini

The central alpha-helical coiled-coil rod region mediates elementary homodimerization.

Sequence similaritiesi

Belongs to the intermediate filament family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG146769.
HOVERGENiHBG013015.
InParanoidiP08670.
KOiK07606.
OMAiINTEFKA.
OrthoDBiEOG7FV3Q8.
PhylomeDBiP08670.
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]
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 BAB71275.1 differs from that shown. Reason: Product of a cloning artifact.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti42 – 421S → D in AAA61279. (PubMed:3467175)Curated
Sequence conflicti113 – 1131R → P in CAA34499. (PubMed:2472876)Curated
Sequence conflicti197 – 1971E → G in CAG28618. 1 PublicationCurated
Sequence conflicti201 – 2011N → S in AAA61281. (PubMed:3371665)Curated
Sequence conflicti265 – 2651L → S in AAA61281. (PubMed:3371665)Curated
Sequence conflicti278 – 2781S → I in AAA61281. (PubMed:3371665)Curated
Sequence conflicti339 – 3391S → C in AAA61281. (PubMed:3371665)Curated
Sequence conflicti350 – 3501N → K in AAA61281. (PubMed:3371665)Curated
Sequence conflicti442 – 4421L → F in AAA61279. (PubMed:3467175)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti151 – 1511E → K in CTRC30; 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 Publication
VAR_070100

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.
UCSCiuc001iou.2. human.

Polymorphism databases

DMDMi55977767.

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 .
CCDSi CCDS7120.1.
PIRi S13115. A25074.
RefSeqi NP_003371.2. NM_003380.3.
XP_006717563.1. XM_006717500.1.
UniGenei Hs.455493.
Hs.691131.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1GK4 X-ray 2.30 A/B/C/D/E/F 328-411 [» ]
1GK6 X-ray 1.90 A/B 385-412 [» ]
1GK7 X-ray 1.40 A 102-138 [» ]
3G1E X-ray 1.83 A/B 102-138 [» ]
3KLT X-ray 2.70 A/B/C/D 263-334 [» ]
3S4R X-ray 2.45 A/B 99-189 [» ]
3SSU X-ray 2.60 A/B 99-189 [» ]
3SWK X-ray 1.70 A/B 153-238 [» ]
3TRT X-ray 2.30 A/B 261-335 [» ]
3UF1 X-ray 2.81 A/B/C/D 144-251 [» ]
4MCY X-ray 2.30 C 66-78 [» ]
4MCZ X-ray 2.41 C 59-71 [» ]
4MD0 X-ray 2.19 C 59-71 [» ]
4MD5 X-ray 1.65 C 66-78 [» ]
4MDI X-ray 2.00 C 66-78 [» ]
4MDJ X-ray 1.70 C 66-78 [» ]
ProteinModelPortali P08670.
SMRi P08670. Positions 99-248, 263-406.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 113272. 200 interactions.
DIPi DIP-32507N.
IntActi P08670. 133 interactions.
MINTi MINT-118802.

PTM databases

PhosphoSitei P08670.

Polymorphism databases

DMDMi 55977767.

2D gel databases

DOSAC-COBS-2DPAGE P08670.
OGPi P08670.
REPRODUCTION-2DPAGE IPI00418471.
P08670.
SWISS-2DPAGE P08670.
UCD-2DPAGE P08670.

Proteomic databases

MaxQBi P08670.
PaxDbi P08670.
PeptideAtlasi P08670.
PRIDEi P08670.

Protocols and materials databases

DNASUi 7431.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000224237 ; ENSP00000224237 ; ENSG00000026025 .
ENST00000544301 ; ENSP00000446007 ; ENSG00000026025 .
GeneIDi 7431.
KEGGi hsa:7431.
UCSCi uc001iou.2. human.

Organism-specific databases

CTDi 7431.
GeneCardsi GC10P017270.
H-InvDB HIX0035657.
HGNCi HGNC:12692. VIM.
HPAi CAB000080.
CAB058687.
HPA001762.
MIMi 116300. phenotype.
193060. gene.
neXtProti NX_P08670.
Orphaneti 98984. Pulverulent cataract.
PharmGKBi PA37311.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG146769.
HOVERGENi HBG013015.
InParanoidi P08670.
KOi K07606.
OMAi INTEFKA.
OrthoDBi EOG7FV3Q8.
PhylomeDBi P08670.
TreeFami TF330122.

Enzyme and pathway databases

Reactomei REACT_13541. Caspase-mediated cleavage of cytoskeletal proteins.
REACT_16969. Striated Muscle Contraction.

Miscellaneous databases

ChiTaRSi VIM. human.
EvolutionaryTracei P08670.
GeneWikii Vimentin.
GenomeRNAii 7431.
NextBioi 29104.
PMAP-CutDB P08670.
PROi P08670.
SOURCEi Search...

Gene expression databases

Bgeei P08670.
ExpressionAtlasi P08670. baseline and differential.
Genevestigatori P08670.

Family and domain databases

InterProi IPR001664. IF.
IPR006821. Intermed_filament_DNA-bd.
IPR018039. Intermediate_filament_CS.
IPR027699. Vimentin.
[Graphical view ]
PANTHERi PTHR23239. PTHR23239. 1 hit.
PTHR23239:SF27. PTHR23239:SF27. 1 hit.
Pfami PF00038. Filament. 1 hit.
PF04732. Filament_head. 1 hit.
[Graphical view ]
PROSITEi PS00226. IF. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Coding sequence and growth regulation of the human vimentin gene."
    Ferrari S., Battini R., Kaczmarek L., Rittling S., Calabretta B., de Riel J.K., Philiponis V., Wei J.-F., Baserga R.
    Mol. Cell. Biol. 6:3614-3620(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Nucleotide sequence of cDNA covering the complete coding part of the human vimentin gene."
    Honore B., Madsen P., Basse B., Andersen A., Walbum E., Celis J.E., Leffers H.
    Nucleic Acids Res. 18:6692-6692(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "SEREX identification of new tumour-associated antigens in cutaneous T-cell lymphoma."
    Hartmann T.B., Thiel D., Dummer R., Schadendorf D., Eichmueller S.
    Br. J. Dermatol. 150:252-258(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Lymphoma.
  4. Zimbelmann R.
    Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Testis.
  5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Embryo, Placenta and Stomach.
  6. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  7. Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
    Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Adipose tissue and Coronary artery.
  8. NHLBI resequencing and genotyping service (RS&G)
    Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  9. "The DNA sequence and comparative analysis of human chromosome 10."
    Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
    , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
    Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  10. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  11. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Cervix, Placenta and Testis.
  12. "Vimentin rather than keratin expression in some hormone-independent breast cancer cell lines and in oncogene-transformed mammary epithelial cells."
    Sommers C.L., Walker-Jones D., Heckford S.E., Worland P., Valverius E., Clark R., McCormick F., Stampfer M., Abularach S., Gelmann E.P.
    Cancer Res. 49:4258-4263(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-135, TISSUE SPECIFICITY.
    Tissue: Mammary carcinoma.
  13. Bienvenut W.V., Kanor S., Tissot J.-D., Quadroni M.
    Submitted (MAY-2006) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-11; 87-96; 129-138; 188-195; 223-234; 282-291; 322-333 AND 381-389, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: T-cell.
  14. Bienvenut W.V., Fleming J., Leug H.Y.
    Submitted (JAN-2010) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 5-12; 14-45; 51-64; 72-78; 105-113; 123-143; 159-184; 187-217; 223-236; 271-292; 295-313; 322-390 AND 403-466, PHOSPHORYLATION AT SER-56, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Hepatoma.
  15. "Two-dimensional electrophoretic analysis of human breast carcinoma proteins: mapping of proteins that bind to the SH3 domain of mixed lineage kinase MLK2."
    Rasmussen R.K., Ji H., Eddes J.S., Moritz R.L., Reid G.E., Simpson R.J., Dorow D.S.
    Electrophoresis 18:588-598(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 17-25 AND 55-70.
    Tissue: Mammary carcinoma.
  16. Lubec G., Vishwanath V., Chen W.-Q., Sun Y.
    Submitted (DEC-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 51-64; 79-97; 105-113; 130-139; 146-155; 176-184; 189-207; 223-235; 283-292; 295-304; 322-334; 346-373; 382-401 AND 411-439, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
  17. "Nucleotide sequence of the human vimentin gene and regulation of its transcription in tissues and cultured cells."
    Perreau J., Lilienbaum A., Vasseur M., Paulin D.
    Gene 62:7-16(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 113-466, TISSUE SPECIFICITY.
    Tissue: Fibroblast.
  18. "Isolation of a human vimentin cDNA with a long 3'-noncoding region from a human osteosarcoma cell line (MG-63)."
    Gupta A.K., Aubin J.E., Waye M.M.Y.
    Gene 86:303-304(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 167-466.
    Tissue: Osteosarcoma.
  19. "Domain-specific phosphorylation of vimentin and glial fibrillary acidic protein by PKN."
    Matsuzawa K., Kosako H., Inagaki N., Shibata H., Mukai H., Ono Y., Amano M., Kaibuchi K., Matsuura Y., Azuma I., Inagaki M.
    Biochem. Biophys. Res. Commun. 234:621-625(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION.
  20. "Aurora-B regulates the cleavage furrow-specific vimentin phosphorylation in the cytokinetic process."
    Goto H., Yasui Y., Kawajiri A., Nigg E.A., Terada Y., Tatsuka M., Nagata K., Inagaki M.
    J. Biol. Chem. 278:8526-8530(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-72.
  21. "Specific in vivo phosphorylation sites determine the assembly dynamics of vimentin intermediate filaments."
    Eriksson J.E., He T., Trejo-Skalli A.V., Harmala-Brasken A.-S., Hellman J., Chou Y.-H., Goldman R.D.
    J. Cell Sci. 117:919-932(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-5; SER-7; SER-8; SER-9; SER-10; SER-39; SER-42; SER-72; SER-73; SER-420; SER-430; THR-458 AND SER-459, IDENTIFICATION BY MASS SPECTROMETRY.
  22. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
    Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
    Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-117, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  23. "Proteomic profiling of cellular proteins interacting with the hepatitis C virus core protein."
    Kang S.-M., Shin M.-J., Kim J.-H., Oh J.-W.
    Proteomics 5:2227-2237(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HCV CORE PROTEIN.
  24. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-214 AND SER-412, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  25. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
    Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
    Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-56, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  26. "Dystonia-causing mutant torsinA inhibits cell adhesion and neurite extension through interference with cytoskeletal dynamics."
    Hewett J.W., Zeng J., Niland B.P., Bragg D.C., Breakefield X.O.
    Neurobiol. Dis. 22:98-111(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TOR1A AND TOR1AIP1.
  27. "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."
    Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.
    J. Proteome Res. 6:4150-4162(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-412, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  28. "Estrogen induces expression of BCAS3, a novel estrogen receptor-alpha coactivator, through proline-, glutamic acid-, and leucine-rich protein-1 (PELP1)."
    Gururaj A.E., Peng S., Vadlamudi R.K., Kumar R.
    Mol. Endocrinol. 21:1847-1860(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH BCAS3.
  29. "The serine/threonine kinase Stk33 exhibits autophosphorylation and phosphorylates the intermediate filament protein Vimentin."
    Brauksiepe B., Mujica A.O., Herrmann H., Schmidt E.R.
    BMC Biochem. 9:25-25(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH STK33, PHOSPHORYLATION BY STK33.
  30. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
    Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
    J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  31. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-412, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  32. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-5; SER-25; SER-34; SER-39; SER-42; SER-51; SER-56; TYR-61; SER-72; SER-73; SER-83; SER-144; SER-409; SER-412 AND SER-459, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  33. "TorsinA binds the KASH domain of nesprins and participates in linkage between nuclear envelope and cytoskeleton."
    Nery F.C., Zeng J., Niland B.P., Hewett J., Farley J., Irimia D., Li Y., Wiche G., Sonnenberg A., Breakefield X.O.
    J. Cell Sci. 121:3476-3486(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TOR1A.
  34. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  35. "The cellular distribution of serotonin transporter is impeded on serotonin-altered vimentin network."
    Ahmed B.A., Bukhari I.A., Jeffus B.C., Harney J.T., Thyparambil S., Ziu E., Fraer M., Rusch N.J., Zimniak P., Lupashin V., Tang D., Kilic F.
    PLoS ONE 4:E4730-E4730(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SLC6A4.
  36. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51; SER-56 AND TYR-61, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  37. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-120; LYS-139; LYS-373 AND LYS-445, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  38. "Extensive crosstalk between O-GlcNAcylation and phosphorylation regulates cytokinesis."
    Wang Z., Udeshi N.D., Slawson C., Compton P.D., Sakabe K., Cheung W.D., Shabanowitz J., Hunt D.F., Hart G.W.
    Sci. Signal. 3:RA2-RA2(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION AT SER-7; THR-33 AND SER-34.
  39. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-20; SER-42; SER-47; SER-51; SER-56; SER-73; SER-83; SER-144; SER-214; SER-226; SER-299; SER-412; SER-419; SER-420; THR-426; SER-430; THR-436 AND SER-459, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  40. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  41. "A novel role of vimentin filaments: binding and stabilization of collagen mRNAs."
    Challa A.A., Stefanovic B.
    Mol. Cell. Biol. 31:3773-3789(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN COLLAGEN MRNA STABILIZATION, INTERACTION WITH LARP6.
  42. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51; SER-144 AND SER-459, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  43. "Cdk5 mediates vimentin Ser56 phosphorylation during GTP-induced secretion by neutrophils."
    Lee K.Y., Liu L., Jin Y., Fu S.B., Rosales J.L.
    J. Cell. Physiol. 227:739-750(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-56, SUBCELLULAR LOCATION.
  44. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  45. "Divide-and-conquer crystallographic approach towards an atomic structure of intermediate filaments."
    Strelkov S.V., Herrmann H., Geisler N., Lustig A., Ivaninskii S., Zimbelmann R., Burkhard P., Aebi U.
    J. Mol. Biol. 306:773-781(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 102-138.
  46. "Conserved segments 1A and 2B of the intermediate filament dimer: their atomic structures and role in filament assembly."
    Strelkov S.V., Herrmann H., Geisler N., Wedig T., Zimbelmann R., Aebi U., Burkhard P.
    EMBO J. 21:1255-1266(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 103-139 AND 328-411.
  47. Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 263-334, COILED-COIL DOMAINS, SUBUNIT.
  48. "Stabilization of vimentin coil2 fragment via an engineered disulfide."
    Chernyatina A.A., Strelkov S.V.
    J. Struct. Biol. 177:46-53(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 261-335 OF MUTANT CYS-265.
  49. "Dominant cataract formation in association with a vimentin assembly disrupting mutation."
    Muller M., Bhattacharya S.S., Moore T., Prescott Q., Wedig T., Herrmann H., Magin T.M.
    Hum. Mol. Genet. 18:1052-1057(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT CTRC30 LYS-151, CHARACTERIZATION OF VARIANT CTRC30 LYS-151.

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 26, 2014
This is version 194 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

External Data

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