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P08670

- VIME_HUMAN

UniProt

P08670 - VIME_HUMAN

Protein

Vimentin

Gene

VIM

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 192 (01 Oct 2014)
      Sequence version 4 (23 Jan 2007)
      Previous versions | rss
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    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 binding Source: UniProtKB
    5. protein C-terminus binding Source: UniProtKB
    6. scaffold protein binding Source: BHF-UCL
    7. structural constituent of cytoskeleton Source: UniProtKB
    8. 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. viral process Source: UniProtKB-KW

    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

    Organism-specific databases

    HGNCiHGNC:12692. VIM.

    Subcellular locationi

    Cytoplasm 1 Publication

    GO - Cellular componenti

    1. cell leading edge Source: Ensembl
    2. cell projection Source: Ensembl
    3. cytoplasm Source: UniProtKB
    4. cytoskeleton Source: UniProtKB
    5. cytosol Source: UniProtKB
    6. extracellular vesicular exosome Source: UniProtKB
    7. intermediate filament Source: UniProtKB
    8. intermediate filament cytoskeleton Source: HPA
    9. peroxisome Source: UniProtKB

    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

    ArrayExpressiP08670.
    BgeeiP08670.
    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 TOR1AIP1.7 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. 196 interactions.
    DIPiDIP-32507N.
    IntActiP08670. 132 interactions.
    MINTiMINT-118802.

    Structurei

    Secondary structure

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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]
    ProtoNetiSearch...

    Sequencei

    Sequence statusi: Complete.

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

    P08670-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSTRSVSSSS YRRMFGGPGT ASRPSSSRSY VTTSTRTYSL GSALRPSTSR    50
    SLYASSPGGV YATRSSAVRL RSSVPGVRLL QDSVDFSLAD AINTEFKNTR 100
    TNEKVELQEL NDRFANYIDK VRFLEQQNKI LLAELEQLKG QGKSRLGDLY 150
    EEEMRELRRQ VDQLTNDKAR VEVERDNLAE DIMRLREKLQ EEMLQREEAE 200
    NTLQSFRQDV DNASLARLDL ERKVESLQEE IAFLKKLHEE EIQELQAQIQ 250
    EQHVQIDVDV SKPDLTAALR DVRQQYESVA AKNLQEAEEW YKSKFADLSE 300
    AANRNNDALR QAKQESTEYR RQVQSLTCEV DALKGTNESL ERQMREMEEN 350
    FAVEAANYQD TIGRLQDEIQ NMKEEMARHL REYQDLLNVK MALDIEIATY 400
    RKLLEGEESR ISLPLPNFSS LNLRETNLDS LPLVDTHSKR TLLIKTVETR 450
    DGQVINETSQ HHDDLE 466
    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.

    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 conflict

    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

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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:
    PDBe
    RCSB PDB
    PDBj
    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. 196 interactions.
    DIPi DIP-32507N.
    IntActi P08670. 132 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

    ArrayExpressi P08670.
    Bgeei P08670.
    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

    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. "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.
    29. "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.
    30. "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.
    31. 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.
    32. "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.
    33. "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].
    34. "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.
    35. "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.
    36. "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].
    37. "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.
    38. "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.
    39. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    40. "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.
    41. "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].
    42. "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.
    43. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    44. "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.
    45. "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.
    46. Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 263-334, COILED-COIL DOMAINS, SUBUNIT.
    47. "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.
    48. "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: October 1, 2014
    This is version 192 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

    Dasty 3

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