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P20152

- VIME_MOUSE

UniProt

P20152 - VIME_MOUSE

Protein

Vimentin

Gene

Vim

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 155 (01 Oct 2014)
      Sequence version 3 (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.
    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. double-stranded RNA binding Source: MGI
    2. protein binding Source: UniProtKB
    3. structural constituent of cytoskeleton Source: Ensembl
    4. structural constituent of eye lens Source: MGI
    5. structural molecule activity Source: MGI

    GO - Biological processi

    1. astrocyte development Source: MGI
    2. Bergmann glial cell differentiation Source: MGI
    3. intermediate filament-based process Source: MGI
    4. intermediate filament organization Source: MGI
    5. lens fiber cell development Source: MGI
    6. negative regulation of neuron projection development Source: MGI
    7. positive regulation of gene expression Source: UniProt

    Enzyme and pathway databases

    ReactomeiREACT_210562. Caspase-mediated cleavage of cytoskeletal proteins.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Vimentin
    Gene namesi
    Name:Vim
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 2

    Organism-specific databases

    MGIiMGI:98932. Vim.

    Subcellular locationi

    Cytoplasm By similarity

    GO - Cellular componenti

    1. cell leading edge Source: MGI
    2. cell projection Source: MGI
    3. cytoplasm Source: MGI
    4. cytoskeleton Source: MGI
    5. cytosol Source: Ensembl
    6. extracellular vesicular exosome Source: Ensembl
    7. intermediate filament Source: MGI
    8. neuron projection Source: MGI
    9. peroxisome Source: Ensembl
    10. plasma membrane Source: MGI
    11. type III intermediate filament Source: MGI

    Keywords - Cellular componenti

    Cytoplasm, Intermediate filament

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 466465VimentinPRO_0000063756Add
    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; alternate1 Publication
    Glycosylationi7 – 71O-linked (GlcNAc); alternateBy similarity
    Modified residuei8 – 81PhosphoserineBy similarity
    Modified residuei9 – 91Phosphoserine; by PKC1 Publication
    Modified residuei10 – 101Phosphoserine; by PKC1 Publication
    Modified residuei20 – 201PhosphothreonineBy similarity
    Modified residuei21 – 211Phosphoserine; by PKC1 Publication
    Modified residuei25 – 251Phosphoserine; by PKA and PKC1 Publication
    Modified residuei26 – 261Phosphoserine; by PKC1 Publication
    Modified residuei29 – 291PhosphoserineBy similarity
    Modified residuei33 – 331Phosphothreonine; alternateBy similarity
    Glycosylationi33 – 331O-linked (GlcNAc); alternateBy similarity
    Modified residuei34 – 341Phosphoserine; by PKC; alternate1 Publication
    Glycosylationi34 – 341O-linked (GlcNAc); alternateBy similarity
    Modified residuei38 – 381PhosphotyrosineBy similarity
    Modified residuei39 – 391Phosphoserine; by CaMK2, PKA, PKC and ROCK24 Publications
    Modified residuei42 – 421Phosphoserine; by PKC1 Publication
    Modified residuei47 – 471Phosphoserine; by PKA1 Publication
    Modified residuei49 – 491Phosphoserine1 Publication
    Modified residuei51 – 511Phosphoserine; by PKA and PKC1 Publication
    Modified residuei53 – 531Phosphotyrosine1 Publication
    Modified residuei55 – 551PhosphoserineBy similarity
    Modified residuei56 – 561Phosphoserine; alternate3 Publications
    Modified residuei56 – 561Phosphoserine; by CDK5 and CDK1; alternateBy similarity
    Modified residuei61 – 611Phosphotyrosine1 Publication
    Modified residuei66 – 661Phosphoserine; by PKA and PKC2 Publications
    Modified residuei72 – 721Phosphoserine; by AURKB and ROCK21 Publication
    Modified residuei73 – 731PhosphoserineBy similarity
    Modified residuei83 – 831Phosphoserine; by CaMK22 Publications
    Modified residuei117 – 1171PhosphotyrosineBy similarity
    Modified residuei120 – 1201N6-acetyllysine; alternate1 Publication
    Modified residuei120 – 1201N6-succinyllysine; alternate1 Publication
    Modified residuei129 – 1291N6-acetyllysine; alternate1 Publication
    Modified residuei129 – 1291N6-succinyllysine; alternate1 Publication
    Modified residuei139 – 1391N6-acetyllysine1 Publication
    Modified residuei144 – 1441PhosphoserineBy similarity
    Modified residuei168 – 1681N6-acetyllysine1 Publication
    Modified residuei188 – 1881N6-acetyllysine; alternate1 Publication
    Modified residuei188 – 1881N6-succinyllysine; alternate1 Publication
    Modified residuei214 – 2141Phosphoserine1 Publication
    Modified residuei223 – 2231N6-acetyllysine1 Publication
    Modified residuei226 – 2261PhosphoserineBy similarity
    Modified residuei235 – 2351N6-acetyllysine1 Publication
    Modified residuei261 – 2611PhosphoserineBy similarity
    Modified residuei266 – 2661PhosphothreonineBy similarity
    Modified residuei294 – 2941N6-acetyllysine; alternate1 Publication
    Modified residuei294 – 2941N6-succinyllysine; alternate1 Publication
    Modified residuei299 – 2991PhosphoserineBy similarity
    Modified residuei373 – 3731N6-acetyllysine1 Publication
    Modified residuei409 – 4091PhosphoserineBy similarity
    Modified residuei412 – 4121PhosphoserineBy similarity
    Modified residuei419 – 4191PhosphoserineBy similarity
    Modified residuei420 – 4201Phosphoserine1 Publication
    Modified residuei426 – 4261PhosphothreonineBy similarity
    Modified residuei430 – 4301Phosphoserine1 Publication
    Modified residuei436 – 4361PhosphothreonineBy similarity
    Modified residuei445 – 4451N6-acetyllysine; alternateBy similarity
    Modified residuei445 – 4451N6-succinyllysine; alternate1 Publication
    Modified residuei446 – 4461PhosphothreonineBy similarity
    Modified residuei458 – 4581PhosphothreonineBy similarity
    Modified residuei459 – 4591Phosphoserine1 Publication

    Post-translational modificationi

    Phosphorylation by PKN1 inhibits the formation of filaments. 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. Phosphorylated at Ser-56 by CDK5 during neutrophil secretion in the cytoplasm. Phosphorylated by STK33 By similarity.By similarity

    Keywords - PTMi

    Acetylation, Glycoprotein, Phosphoprotein

    Proteomic databases

    MaxQBiP20152.
    PaxDbiP20152.
    PRIDEiP20152.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00227299.
    SWISS-2DPAGEP20152.
    UCD-2DPAGEP20152.

    PTM databases

    PhosphoSiteiP20152.

    Expressioni

    Gene expression databases

    ArrayExpressiP20152.
    BgeeiP20152.
    CleanExiMM_VIM.
    GenevestigatoriP20152.

    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 TOR1AIP1.4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Pak1P354652EBI-299269,EBI-444379From a different organism.
    PASKQ96RG22EBI-299269,EBI-1042651From a different organism.
    PplQ9R2692EBI-299269,EBI-368293

    Protein-protein interaction databases

    BioGridi204524. 20 interactions.
    DIPiDIP-188N.
    IntActiP20152. 19 interactions.
    MINTiMINT-1202726.

    Structurei

    3D structure databases

    ProteinModelPortaliP20152.
    SMRiP20152. Positions 99-238, 263-406.
    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.
    InParanoidiP20152.
    KOiK07606.
    OMAiINTEFKA.
    PhylomeDBiP20152.
    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.

    P20152-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSTRSVSSSS YRRMFGGSGT SSRPSSNRSY VTTSTRTYSL GSALRPSTSR    50
    SLYSSSPGGA YVTRSSAVRL RSSVPGVRLL 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 ISLPLPTFSS LNLRETNLES LPLVDTHSKR TLLIKTVETR 450
    DGQVINETSQ HHDDLE 466
    Length:466
    Mass (Da):53,688
    Last modified:January 23, 2007 - v3
    Checksum:iA94EECEA6D70C899
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti70 – 701L → S in BAA19834. (PubMed:8543176)Curated
    Sequence conflicti110 – 1156LNDRFA → ILLAEL in BAA19834. (PubMed:8543176)Curated
    Sequence conflicti156 – 1572EL → DV in CAA35803. (PubMed:2140597)Curated
    Sequence conflicti164 – 1641L → F in CAA39807. 1 PublicationCurated
    Sequence conflicti338 – 3381E → V in CAA35803. (PubMed:2140597)Curated
    Sequence conflicti374 – 3741E → D in AAA40555. (PubMed:2744479)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M24849 mRNA. Translation: AAA40555.1.
    X56397 mRNA. Translation: CAA39807.1.
    M26251 mRNA. Translation: AAA40556.1.
    Z22526 Genomic DNA. Translation: CAA80251.1.
    X51438 mRNA. Translation: CAA35803.1.
    Y07738 Genomic DNA. Translation: CAA69019.1.
    AK033175 mRNA. Translation: BAC28181.1.
    D50805 Genomic DNA. Translation: BAA19834.1.
    CCDSiCCDS15696.1.
    PIRiA43803.
    RefSeqiNP_035831.2. NM_011701.4.
    UniGeneiMm.268000.

    Genome annotation databases

    EnsembliENSMUST00000028062; ENSMUSP00000028062; ENSMUSG00000026728.
    GeneIDi22352.
    KEGGimmu:22352.
    UCSCiuc008ikb.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M24849 mRNA. Translation: AAA40555.1 .
    X56397 mRNA. Translation: CAA39807.1 .
    M26251 mRNA. Translation: AAA40556.1 .
    Z22526 Genomic DNA. Translation: CAA80251.1 .
    X51438 mRNA. Translation: CAA35803.1 .
    Y07738 Genomic DNA. Translation: CAA69019.1 .
    AK033175 mRNA. Translation: BAC28181.1 .
    D50805 Genomic DNA. Translation: BAA19834.1 .
    CCDSi CCDS15696.1.
    PIRi A43803.
    RefSeqi NP_035831.2. NM_011701.4.
    UniGenei Mm.268000.

    3D structure databases

    ProteinModelPortali P20152.
    SMRi P20152. Positions 99-238, 263-406.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 204524. 20 interactions.
    DIPi DIP-188N.
    IntActi P20152. 19 interactions.
    MINTi MINT-1202726.

    PTM databases

    PhosphoSitei P20152.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00227299.
    SWISS-2DPAGE P20152.
    UCD-2DPAGE P20152.

    Proteomic databases

    MaxQBi P20152.
    PaxDbi P20152.
    PRIDEi P20152.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000028062 ; ENSMUSP00000028062 ; ENSMUSG00000026728 .
    GeneIDi 22352.
    KEGGi mmu:22352.
    UCSCi uc008ikb.2. mouse.

    Organism-specific databases

    CTDi 7431.
    MGIi MGI:98932. Vim.

    Phylogenomic databases

    eggNOGi NOG146769.
    HOGENOMi HOG000230977.
    HOVERGENi HBG013015.
    InParanoidi P20152.
    KOi K07606.
    OMAi INTEFKA.
    PhylomeDBi P20152.
    TreeFami TF330122.

    Enzyme and pathway databases

    Reactomei REACT_210562. Caspase-mediated cleavage of cytoskeletal proteins.

    Miscellaneous databases

    ChiTaRSi VIM. mouse.
    NextBioi 302643.
    PROi P20152.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P20152.
    Bgeei P20152.
    CleanExi MM_VIM.
    Genevestigatori P20152.

    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. "Vimentin cDNA clones covering the complete intermediate-filament protein are found in an EHS tumor cDNA library."
      Wood L., Theriault N., Vogeli G.
      Gene 76:171-175(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. Podolin P.L., Prystowsky M.B.
      Submitted (OCT-1990) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: C57BL/6.
      Tissue: Spleen.
    3. "Coding sequence and flanking regions of the mouse vimentin gene."
      Hennekes H., Kuehn S., Traub P.
      Mol. Gen. Genet. 221:33-36(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    4. "Mouse vimentin: structural relationship to fos, jun, CREB and tpr."
      Capetanaki Y., Kuisk I., Rothblum K., Starnes S.
      Oncogene 5:645-655(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Smooth muscle.
    5. Rauscher A.
      Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    6. "Transcriptional regulation of the vimentin-encoding gene in mouse myeloid leukemia M1 cells."
      Nakamura N., Shida M., Hirayoshi K., Nagata K.
      Gene 166:281-286(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-115.
      Strain: BALB/c.
    7. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 32-188.
      Strain: C57BL/6J.
      Tissue: Testis.
    8. "Domain- and sequence-specific phosphorylation of vimentin induces disassembly of the filament structure."
      Ando S., Tanabe K., Gonda Y., Sato C., Inagaki M.
      Biochemistry 28:2974-2979(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 5-69, PHOSPHORYLATION AT SER-7; SER-9; SER-10; SER-21; SER-25; SER-26; SER-34; SER-39; SER-42; SER-47; SER-51 AND SER-66.
      Tissue: Smooth muscle.
    9. "Separation and sequencing of familiar and novel murine proteins using preparative two-dimensional gel electrophoresis."
      Merrick B.A., Patterson R.M., Wichter L.L., He C., Selkirk J.K.
      Electrophoresis 15:735-745(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 72-91.
      Tissue: Fibroblast.
    10. "Evidence that Ser-82 is a unique phosphorylation site on vimentin for Ca2(+)-calmodulin-dependent protein kinase II."
      Ando S., Tokui T., Yamauchi T., Sugiura H., Tanabe K., Inagaki M.
      Biochem. Biophys. Res. Commun. 175:955-962(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-39 AND SER-83.
    11. "Phosphorylation of vimentin by Rho-associated kinase at a unique amino-terminal site that is specifically phosphorylated during cytokinesis."
      Goto H., Kosako H., Tanabe K., Yanagida M., Sakurai M., Amano M., Kaibuchi K., Inagaki M.
      J. Biol. Chem. 273:11728-11736(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-39 AND SER-72.
    12. "Actin-binding domain of mouse plectin. Crystal structure and binding to vimentin."
      Sevcik J., Urbanikova L., Kost'an J., Janda L., Wiche G.
      Eur. J. Biochem. 271:1873-1884(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PLEC.
    13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic brain.
    14. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "Synemin is expressed in reactive astrocytes in neurotrauma and interacts differentially with vimentin and GFAP intermediate filament networks."
      Jing R., Wilhelmsson U., Goodwill W., Li L., Pan Y., Pekny M., Skalli O.
      J. Cell Sci. 120:1267-1277(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SYNM.
    16. "Quantitative time-resolved phosphoproteomic analysis of mast cell signaling."
      Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y., Kawakami T., Salomon A.R.
      J. Immunol. 179:5864-5876(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-53 AND TYR-61, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Mast cell.
    17. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-56, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    18. "A role for lengsin, a recruited enzyme, in terminal differentiation in the vertebrate lens."
      Wyatt K., Gao C., Tsai J.-Y., Fariss R.N., Ray S., Wistow G.
      J. Biol. Chem. 283:6607-6615(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH LGSN.
    19. "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.
    20. "The phagosomal proteome in interferon-gamma-activated macrophages."
      Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
      Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-56; SER-214 AND SER-459, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    21. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
      Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
      Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-39; SER-49; SER-56; SER-66; SER-420 AND SER-430, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.
    22. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
      Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
      Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-120; LYS-129; LYS-139; LYS-168; LYS-188; LYS-223; LYS-235; LYS-294 AND LYS-373, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-120; LYS-129; LYS-188; LYS-294 AND LYS-445, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.

    Entry informationi

    Entry nameiVIME_MOUSE
    AccessioniPrimary (citable) accession number: P20152
    Secondary accession number(s): O08704, Q8CCH1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1991
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 155 of the entry and version 3 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. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3