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P31000

- VIME_RAT

UniProt

P31000 - VIME_RAT

Protein

Vimentin

Gene

Vim

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 129 (01 Oct 2014)
      Sequence version 2 (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.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei351 – 3511StutterBy similarity

    GO - Molecular functioni

    1. kinase binding Source: RGD
    2. protein binding Source: UniProtKB
    3. protein kinase binding Source: RGD
    4. protein phosphatase 2A binding Source: RGD
    5. structural constituent of cytoskeleton Source: UniProtKB
    6. structural molecule activity Source: RGD

    GO - Biological processi

    1. aging Source: RGD
    2. cellular response to fibroblast growth factor stimulus Source: RGD
    3. decidualization Source: RGD
    4. fat cell differentiation Source: RGD
    5. positive regulation of glial cell proliferation Source: RGD
    6. regulation of axonogenesis Source: RGD
    7. regulation of Schwann cell migration Source: RGD
    8. response to estradiol Source: RGD
    9. response to radiation Source: RGD
    10. response to selenium ion Source: RGD
    11. response to vitamin D Source: RGD
    12. response to zinc ion Source: RGD
    13. skeletal muscle tissue regeneration Source: RGD

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Vimentin
    Gene namesi
    Name:Vim
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Unplaced

    Organism-specific databases

    RGDi621646. Vim.

    Subcellular locationi

    Nucleus matrix 1 Publication. Cytoplasm By similarity

    GO - Cellular componenti

    1. axon Source: RGD
    2. cell body Source: RGD
    3. cell projection Source: RGD
    4. cytoplasm Source: UniProtKB
    5. cytoskeleton Source: RGD
    6. cytosol Source: RGD
    7. intermediate filament Source: UniProtKB
    8. nuclear matrix Source: UniProtKB-SubCell
    9. perinuclear region of cytoplasm Source: RGD
    10. type III intermediate filament Source: RGD

    Keywords - Cellular componenti

    Cytoplasm, Intermediate filament, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi55 – 551S → A: Retains filamentous network during mitosis when transfected alone and when coexpressed with nestin. 1 Publication
    Mutagenesisi458 – 4592TS → AA: Induces loss of filamentous network when coexpressed with nestin.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 466465VimentinPRO_0000063759Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserineBy similarity
    Modified residuei5 – 51PhosphoserineBy similarity
    Modified residuei7 – 71Phosphoserine; by PKA and PKC; alternateBy similarity
    Glycosylationi7 – 71O-linked (GlcNAc); alternateBy similarity
    Modified residuei8 – 81PhosphoserineBy similarity
    Modified residuei9 – 91Phosphoserine; by PKCBy similarity
    Modified residuei10 – 101Phosphoserine; by PKCBy similarity
    Modified residuei20 – 201PhosphothreonineBy similarity
    Modified residuei25 – 251PhosphoserineBy similarity
    Modified residuei26 – 261PhosphoserineBy similarity
    Modified residuei29 – 291PhosphoserineBy similarity
    Modified residuei33 – 331Phosphothreonine; alternateBy similarity
    Glycosylationi33 – 331O-linked (GlcNAc); alternateBy similarity
    Modified residuei34 – 341Phosphoserine; alternateBy similarity
    Glycosylationi34 – 341O-linked (GlcNAc); alternateBy similarity
    Modified residuei38 – 381PhosphotyrosineBy similarity
    Modified residuei39 – 391Phosphoserine; by CaMK2, PKA, PKC and ROCK2By similarity
    Modified residuei42 – 421Phosphoserine; by PKCBy similarity
    Modified residuei47 – 471Phosphoserine; by PKABy similarity
    Modified residuei49 – 491PhosphoserineBy similarity
    Modified residuei51 – 511Phosphoserine; by PKA and PKCBy similarity
    Modified residuei53 – 531PhosphotyrosineBy similarity
    Modified residuei55 – 551Phosphoserine1 Publication
    Modified residuei56 – 561Phosphoserine; by CDK5 and CDK1By similarity
    Modified residuei61 – 611PhosphotyrosineBy similarity
    Modified residuei66 – 661Phosphoserine; by PKA and PKCBy similarity
    Modified residuei72 – 721Phosphoserine; by AURKB and ROCK2By similarity
    Modified residuei73 – 731PhosphoserineBy similarity
    Modified residuei83 – 831Phosphoserine; by CaMK2By similarity
    Modified residuei117 – 1171PhosphotyrosineBy similarity
    Modified residuei120 – 1201N6-acetyllysine; alternateBy similarity
    Modified residuei120 – 1201N6-succinyllysine; alternateBy similarity
    Modified residuei129 – 1291N6-acetyllysine; alternateBy similarity
    Modified residuei129 – 1291N6-succinyllysine; alternateBy similarity
    Modified residuei139 – 1391N6-acetyllysineBy similarity
    Modified residuei144 – 1441PhosphoserineBy similarity
    Modified residuei168 – 1681N6-acetyllysineBy similarity
    Modified residuei188 – 1881N6-acetyllysine; alternateBy similarity
    Modified residuei188 – 1881N6-succinyllysine; alternateBy similarity
    Modified residuei214 – 2141PhosphoserineBy similarity
    Modified residuei223 – 2231N6-acetyllysineBy similarity
    Modified residuei226 – 2261PhosphoserineBy similarity
    Modified residuei235 – 2351N6-acetyllysineBy similarity
    Modified residuei261 – 2611PhosphoserineBy similarity
    Modified residuei266 – 2661PhosphothreonineBy similarity
    Modified residuei294 – 2941N6-acetyllysine; alternateBy similarity
    Modified residuei294 – 2941N6-succinyllysine; alternateBy similarity
    Modified residuei299 – 2991PhosphoserineBy similarity
    Modified residuei373 – 3731N6-acetyllysineBy similarity
    Modified residuei409 – 4091PhosphoserineBy similarity
    Modified residuei412 – 4121PhosphoserineBy similarity
    Modified residuei419 – 4191PhosphoserineBy similarity
    Modified residuei420 – 4201PhosphoserineBy similarity
    Modified residuei426 – 4261PhosphothreonineBy similarity
    Modified residuei430 – 4301PhosphoserineBy similarity
    Modified residuei436 – 4361PhosphothreonineBy similarity
    Modified residuei445 – 4451N6-acetyllysine; alternateBy similarity
    Modified residuei445 – 4451N6-succinyllysine; alternateBy similarity
    Modified residuei446 – 4461PhosphothreonineBy similarity
    Modified residuei458 – 4581PhosphothreonineBy similarity
    Modified residuei459 – 4591PhosphoserineBy similarity

    Post-translational modificationi

    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 inhibit the formation of filaments By similarity. Filament disassembly during mitosis is promoted by phosphorylation at Ser-55 as well as by nestin Probable. Phosphorylated at Ser-56 by CDK5 during neutrophil secretion in the cytoplasm. Phosphorylated by STK33 By similarity.By similarityCurated

    Keywords - PTMi

    Acetylation, Glycoprotein, Phosphoprotein

    Proteomic databases

    PaxDbiP31000.
    PRIDEiP31000.

    PTM databases

    PhosphoSiteiP31000.

    Expressioni

    Gene expression databases

    GenevestigatoriP31000.

    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 TOR1AIP1.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    YwhabP352133EBI-368510,EBI-917309

    Protein-protein interaction databases

    BioGridi249676. 9 interactions.
    IntActiP31000. 6 interactions.
    MINTiMINT-4563959.
    STRINGi10116.ENSRNOP00000024430.

    Structurei

    3D structure databases

    ProteinModelPortaliP31000.
    SMRiP31000. Positions 101-138, 328-406.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

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

    Coiled coil

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

    Domaini

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

    Sequence similaritiesi

    Belongs to the intermediate filament family.Curated

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiNOG146769.
    HOGENOMiHOG000230977.
    HOVERGENiHBG013015.
    InParanoidiP31000.
    KOiK07606.
    PhylomeDBiP31000.

    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.

    P31000-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSTRSVSSSS YRRMFGGSGT SSRPSSNRSY VTTSTRTYSL GSALRPSTSR    50
    SLYSSSPGGA YVTRSSAVRL RSSMPGVRLL QDSVDFSLAD AINTEFKNTR 100
    TNEKVELQEL NDRFANYIDK VRFLEQQNKI LLAELEQLKG QGKSRLGDLY 150
    EEEMRELRRQ VDQLTNDKAR VEVERDNLAE DIMRLREKLQ EEMLQREEAE 200
    STLQSFRQDV DNASLARLDL ERKVESLQEE IAFLKKLHDE EIQELQAQIQ 250
    EQHVQIDVDV SKPDLTAALR DVRQQYESVA AKNLQEAEEW YKSKFADLSE 300
    AANRNNDALR QAKQESNEYR RQVQSLTCEV DALKGTNESL ERQMREMEEN 350
    FALEAANYQD TIGRLQDEIQ NMKEEMARHL REYQDLLNVK MALDIEIATY 400
    RKLLEGEESR ISLPLPNFSS LNLRETNLES LPLVDTHSKR TLLIKTVETR 450
    DGQVINETSQ HHDDLE 466
    Length:466
    Mass (Da):53,733
    Last modified:January 23, 2007 - v2
    Checksum:i501CDCD706166829
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X62952 mRNA. Translation: CAA44722.1.
    BC061847 mRNA. Translation: AAH61847.1.
    M84481 mRNA. Translation: AAA42339.1.
    PIRiS22119.
    RefSeqiNP_112402.1. NM_031140.1.
    UniGeneiRn.2710.

    Genome annotation databases

    GeneIDi81818.
    KEGGirno:81818.
    UCSCiRGD:621646. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X62952 mRNA. Translation: CAA44722.1 .
    BC061847 mRNA. Translation: AAH61847.1 .
    M84481 mRNA. Translation: AAA42339.1 .
    PIRi S22119.
    RefSeqi NP_112402.1. NM_031140.1.
    UniGenei Rn.2710.

    3D structure databases

    ProteinModelPortali P31000.
    SMRi P31000. Positions 101-138, 328-406.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 249676. 9 interactions.
    IntActi P31000. 6 interactions.
    MINTi MINT-4563959.
    STRINGi 10116.ENSRNOP00000024430.

    PTM databases

    PhosphoSitei P31000.

    Proteomic databases

    PaxDbi P31000.
    PRIDEi P31000.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 81818.
    KEGGi rno:81818.
    UCSCi RGD:621646. rat.

    Organism-specific databases

    CTDi 7431.
    RGDi 621646. Vim.

    Phylogenomic databases

    eggNOGi NOG146769.
    HOGENOMi HOG000230977.
    HOVERGENi HBG013015.
    InParanoidi P31000.
    KOi K07606.
    PhylomeDBi P31000.

    Miscellaneous databases

    NextBioi 615731.
    PROi P31000.

    Gene expression databases

    Genevestigatori P31000.

    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. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: Fischer.
    2. "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: Prostate.
    3. "Proteome analysis of a rat liver nuclear insoluble protein fraction and localization of a novel protein, ISP36, to compartments in the interchromatin space."
      Segawa M., Niino K., Mineki R., Kaga N., Murayama K., Sugimoto K., Watanabe Y., Furukawa K., Horigome T.
      FEBS J. 272:4327-4338(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 37-50, SUBCELLULAR LOCATION.
      Tissue: Liver.
    4. Lubec G., Afjehi-Sadat L., Kang S.U., Lubec S.
      Submitted (SEP-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 51-64; 123-129; 223-235; 295-304; 321-341; 346-364; 391-401 AND 411-424, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: Sprague-Dawley.
      Tissue: Brain and Spinal cord.
    5. Paine M.L.
      Submitted (FEB-1992) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 86-160.
      Tissue: Mammary gland.
    6. "The role of the vimentin intermediate filaments in rat 3Y1 cells elucidated by immunoelectron microscopy and computer-graphic reconstruction."
      Katsumoto T., Mitsushima A., Kurimura T.
      Biol. Cell 68:139-146(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    7. "Rab8B GTPase and junction dynamics in the testis."
      Lau A.S., Mruk D.D.
      Endocrinology 144:1549-1563(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RAB8B.
    8. "Nestin promotes the phosphorylation-dependent disassembly of vimentin intermediate filaments during mitosis."
      Chou Y.-H., Khuon S., Herrmann H., Goldman R.D.
      Mol. Biol. Cell 14:1468-1478(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-55, MUTAGENESIS OF SER-55 AND 458-THR-SER-459.

    Entry informationi

    Entry nameiVIME_RAT
    AccessioniPrimary (citable) accession number: P31000
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1993
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 129 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3