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P20152

- VIME_MOUSE

UniProt

P20152 - VIME_MOUSE

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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 – 3511Stutter By 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. Bergmann glial cell differentiation Source: MGI
  2. astrocyte development Source: MGI
  3. intermediate filament organization Source: MGI
  4. intermediate filament-based process 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
Complete GO annotation...

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
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Intermediate filament

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed By similarity
Chaini2 – 466465Vimentin
PRO_0000063756Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine By similarity
Modified residuei5 – 51Phosphoserine By similarity
Modified residuei7 – 71Phosphoserine; by PKA and PKC; alternate1 Publication
Glycosylationi7 – 71O-linked (GlcNAc); alternate By similarity
Modified residuei8 – 81Phosphoserine By similarity
Modified residuei9 – 91Phosphoserine; by PKC1 Publication
Modified residuei10 – 101Phosphoserine; by PKC1 Publication
Modified residuei20 – 201Phosphothreonine By similarity
Modified residuei21 – 211Phosphoserine; by PKC1 Publication
Modified residuei25 – 251Phosphoserine; by PKA and PKC1 Publication
Modified residuei26 – 261Phosphoserine; by PKC1 Publication
Modified residuei29 – 291Phosphoserine By similarity
Modified residuei33 – 331Phosphothreonine; alternate By similarity
Glycosylationi33 – 331O-linked (GlcNAc); alternate By similarity
Modified residuei34 – 341Phosphoserine; by PKC; alternate1 Publication
Glycosylationi34 – 341O-linked (GlcNAc); alternate By similarity
Modified residuei38 – 381Phosphotyrosine By 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 – 551Phosphoserine By similarity
Modified residuei56 – 561Phosphoserine; alternate3 Publications
Modified residuei56 – 561Phosphoserine; by CDK5 and CDK1; alternate By similarity
Modified residuei61 – 611Phosphotyrosine1 Publication
Modified residuei66 – 661Phosphoserine; by PKA and PKC2 Publications
Modified residuei72 – 721Phosphoserine; by AURKB and ROCK21 Publication
Modified residuei73 – 731Phosphoserine By similarity
Modified residuei83 – 831Phosphoserine; by CaMK22 Publications
Modified residuei117 – 1171Phosphotyrosine By 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 – 1441Phosphoserine By 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 – 2261Phosphoserine By similarity
Modified residuei235 – 2351N6-acetyllysine1 Publication
Modified residuei261 – 2611Phosphoserine By similarity
Modified residuei266 – 2661Phosphothreonine By similarity
Modified residuei294 – 2941N6-acetyllysine; alternate1 Publication
Modified residuei294 – 2941N6-succinyllysine; alternate1 Publication
Modified residuei299 – 2991Phosphoserine By similarity
Modified residuei373 – 3731N6-acetyllysine1 Publication
Modified residuei409 – 4091Phosphoserine By similarity
Modified residuei412 – 4121Phosphoserine By similarity
Modified residuei419 – 4191Phosphoserine By similarity
Modified residuei420 – 4201Phosphoserine1 Publication
Modified residuei426 – 4261Phosphothreonine By similarity
Modified residuei430 – 4301Phosphoserine1 Publication
Modified residuei436 – 4361Phosphothreonine By similarity
Modified residuei445 – 4451N6-acetyllysine; alternate By similarity
Modified residuei445 – 4451N6-succinyllysine; alternate1 Publication
Modified residuei446 – 4461Phosphothreonine By similarity
Modified residuei458 – 4581Phosphothreonine By 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.3 Publications

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.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 9594Head
Add
BLAST
Regioni96 – 407312Rod
Add
BLAST
Regioni96 – 13136Coil 1A
Add
BLAST
Regioni132 – 15322Linker 1
Add
BLAST
Regioni154 – 24592Coil 1B
Add
BLAST
Regioni246 – 26823Linker 12
Add
BLAST
Regioni269 – 407139Coil 2
Add
BLAST
Regioni408 – 46659Tail
Add
BLAST

Coiled coil

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

Domaini

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

Sequence similaritiesi

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

Sequence conflict

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

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

« 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: September 3, 2014
This is version 154 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

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