Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P20152

- VIME_MOUSE

UniProt

P20152 - VIME_MOUSE

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Vimentin

Gene

Vim

Organism
Mus musculus (Mouse)
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.
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. structural constituent of cytoskeleton Source: Ensembl
  3. structural constituent of eye lens Source: MGI
  4. 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
  8. SMAD protein signal transduction Source: MGI
Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_210562. Caspase-mediated cleavage of cytoskeletal proteins.
REACT_232053. Striated Muscle Contraction.

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
Complete GO annotation...

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

BgeeiP20152.
CleanExiMM_VIM.
ExpressionAtlasiP20152. baseline and differential.
GenevestigatoriP20152.

Interactioni

Subunit structurei

Interacts with BCAS3 (By similarity). 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.By similarity4 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

        10         20         30         40         50
MSTRSVSSSS YRRMFGGSGT SSRPSSNRSY VTTSTRTYSL GSALRPSTSR
60 70 80 90 100
SLYSSSPGGA YVTRSSAVRL 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
STLQSFRQDV DNASLARLDL ERKVESLQEE IAFLKKLHDE EIQELQAQIQ
260 270 280 290 300
EQHVQIDVDV SKPDLTAALR DVRQQYESVA AKNLQEAEEW YKSKFADLSE
310 320 330 340 350
AANRNNDALR QAKQESNEYR RQVQSLTCEV DALKGTNESL ERQMREMEEN
360 370 380 390 400
FALEAANYQD TIGRLQDEIQ NMKEEMARHL REYQDLLNVK MALDIEIATY
410 420 430 440 450
RKLLEGEESR ISLPLPTFSS LNLRETNLES LPLVDTHSKR TLLIKTVETR
460
DGQVINETSQ HHDDLE
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.
REACT_232053. Striated Muscle Contraction.

Miscellaneous databases

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

Gene expression databases

Bgeei P20152.
CleanExi MM_VIM.
ExpressionAtlasi P20152. baseline and differential.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 157 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