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P20152 (VIME_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 139. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Vimentin
Gene names
Name:Vim
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length466 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subunit structure

Homopolymer assembled from elementary dimers. Interacts with SLC6A4 By similarity. Interacts with LGSN and SYNM. Interacts (via rod region) with PLEC (via CH 1 domain). Interacts with STK33 By similarity. Interacts with LARP6 By similarity. Interacts with RAB8B By similarity. Ref.12 Ref.14 Ref.16

Subcellular location

Cytoplasm By similarity.

Domain

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

Post-translational modification

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. Ref.8 Ref.10 Ref.11

Sequence similarities

Belongs to the intermediate filament family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Pak1P354652EBI-299269,EBI-444379From a different organism.
PplQ9R2692EBI-299269,EBI-368293

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 466465Vimentin
PRO_0000063756

Regions

Region2 – 9594Head
Region96 – 407312Rod
Region96 – 13136Coil 1A
Region132 – 15322Linker 1
Region154 – 24592Coil 1B
Region246 – 26823Linker 12
Region269 – 407139Coil 2
Region408 – 46659Tail
Coiled coil96 – 13136
Coiled coil154 – 24592
Coiled coil303 – 407105

Sites

Site3511Stutter By similarity

Amino acid modifications

Modified residue21N-acetylserine By similarity
Modified residue51Phosphoserine By similarity
Modified residue71Phosphoserine; by PKA and PKC Ref.8 Ref.18
Modified residue81Phosphoserine By similarity
Modified residue91Phosphoserine; by PKC Ref.8
Modified residue101Phosphoserine; by PKC Ref.8
Modified residue201Phosphothreonine By similarity
Modified residue211Phosphoserine; by PKC Ref.8
Modified residue251Phosphoserine; by PKA and PKC Ref.8
Modified residue261Phosphoserine; by PKC Ref.8
Modified residue291Phosphoserine By similarity
Modified residue331Phosphothreonine By similarity
Modified residue341Phosphoserine; by PKC Ref.8
Modified residue381Phosphotyrosine By similarity
Modified residue391Phosphoserine; by CaMK2, PKA, PKC and ROCK2 Ref.8 Ref.10 Ref.11 Ref.17 Ref.19
Modified residue421Phosphoserine; by PKC Ref.8
Modified residue471Phosphoserine; by PKA Ref.8
Modified residue491Phosphoserine Ref.19
Modified residue511Phosphoserine; by PKA and PKC Ref.8
Modified residue531Phosphotyrosine Ref.15
Modified residue551Phosphoserine By similarity
Modified residue561Phosphoserine; by CDK5 and CDK1 By similarity
Modified residue611Phosphotyrosine Ref.15
Modified residue661Phosphoserine; by PKA and PKC Ref.8 Ref.19
Modified residue721Phosphoserine; by AURKB and ROCK2 Ref.11 Ref.13 Ref.17
Modified residue731Phosphoserine Ref.13 Ref.17
Modified residue831Phosphoserine; by CaMK2 Ref.10
Modified residue1041N6-acetyllysine By similarity
Modified residue1171Phosphotyrosine By similarity
Modified residue1201N6-acetyllysine By similarity
Modified residue1391N6-acetyllysine By similarity
Modified residue1441Phosphoserine Ref.17
Modified residue2141Phosphoserine Ref.18
Modified residue2261Phosphoserine Ref.17
Modified residue2611Phosphoserine By similarity
Modified residue2661Phosphothreonine By similarity
Modified residue2921N6-acetyllysine By similarity
Modified residue2991Phosphoserine By similarity
Modified residue3731N6-acetyllysine By similarity
Modified residue4021N6-acetyllysine By similarity
Modified residue4091Phosphoserine By similarity
Modified residue4121Phosphoserine By similarity
Modified residue4191Phosphoserine Ref.19
Modified residue4201Phosphoserine Ref.19
Modified residue4261Phosphothreonine By similarity
Modified residue4301Phosphoserine Ref.17 Ref.19
Modified residue4361Phosphothreonine By similarity
Modified residue4451N6-acetyllysine By similarity
Modified residue4461Phosphothreonine By similarity
Modified residue4581Phosphothreonine By similarity
Modified residue4591Phosphoserine Ref.17 Ref.19

Experimental info

Sequence conflict701L → S in BAA19834. Ref.6
Sequence conflict110 – 1156LNDRFA → ILLAEL in BAA19834. Ref.6
Sequence conflict156 – 1572EL → DV in CAA35803. Ref.4
Sequence conflict1641L → F in CAA39807. Ref.2
Sequence conflict3381E → V in CAA35803. Ref.4
Sequence conflict3741E → D in AAA40555. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P20152 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: A94EECEA6D70C899

FASTA46653,688
        10         20         30         40         50         60 
MSTRSVSSSS YRRMFGGSGT SSRPSSNRSY VTTSTRTYSL GSALRPSTSR SLYSSSPGGA 

        70         80         90        100        110        120 
YVTRSSAVRL RSSVPGVRLL QDSVDFSLAD AINTEFKNTR TNEKVELQEL NDRFANYIDK 

       130        140        150        160        170        180 
VRFLEQQNKI LLAELEQLKG QGKSRLGDLY EEEMRELRRQ VDQLTNDKAR VEVERDNLAE 

       190        200        210        220        230        240 
DIMRLREKLQ EEMLQREEAE STLQSFRQDV DNASLARLDL ERKVESLQEE IAFLKKLHDE 

       250        260        270        280        290        300 
EIQELQAQIQ EQHVQIDVDV SKPDLTAALR DVRQQYESVA AKNLQEAEEW YKSKFADLSE 

       310        320        330        340        350        360 
AANRNNDALR QAKQESNEYR RQVQSLTCEV DALKGTNESL ERQMREMEEN FALEAANYQD 

       370        380        390        400        410        420 
TIGRLQDEIQ NMKEEMARHL REYQDLLNVK MALDIEIATY RKLLEGEESR ISLPLPTFSS 

       430        440        450        460 
LNLRETNLES LPLVDTHSKR TLLIKTVETR DGQVINETSQ HHDDLE

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"Identification of phosphoproteins and their phosphorylation sites in the WEHI-231 B lymphoma cell line."
Shu H., Chen S., Bi Q., Mumby M., Brekken D.L.
Mol. Cell. Proteomics 3:279-286(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-72 AND SER-73, MASS SPECTROMETRY.
Tissue: B-cell lymphoma.
[14]"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.
[15]"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, MASS SPECTROMETRY.
Tissue: Mast cell.
[16]"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.
[17]"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry."
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M.
J. Proteome Res. 7:5314-5326(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-39; SER-72; SER-73; SER-144; SER-226; SER-430 AND SER-459, MASS SPECTROMETRY.
Tissue: Melanoma.
[18]"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-7 AND SER-214, MASS SPECTROMETRY.
Tissue: Macrophage.
[19]"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-419; SER-420; SER-430 AND SER-459, MASS SPECTROMETRY.
Tissue: Embryonic fibroblast.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		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.
IPIIPI00227299.
PIRA43803.
RefSeqNP_035831.2. NM_011701.4.
UniGeneMm.268000.

3D structure databases

ProteinModelPortalP20152.
SMRP20152. Positions 99-238, 263-406.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-188N.
IntActP20152. 11 interactions.
MINTMINT-1202726.

PTM databases

PhosphoSiteP20152.

2D gel databases

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

Proteomic databases

PaxDbP20152.
PRIDEP20152.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000028062; ENSMUSP00000028062; ENSMUSG00000026728.
GeneID22352.
KEGGmmu:22352.

Organism-specific databases

CTD7431.
MGIMGI:98932. Vim.

Phylogenomic databases

eggNOGNOG146769.
HOGENOMHOG000230977.
HOVERGENHBG013015.
InParanoidP20152.
KOK07606.
OMAINTEFKA.
OrthoDBEOG4GHZPD.

Gene expression databases

ArrayExpressP20152.
BgeeP20152.
CleanExMM_VIM.
GenevestigatorP20152.
GermOnlineENSMUSG00000026728. Mus musculus.

Family and domain databases

InterProIPR016044. F.
IPR001664. IF.
IPR006821. Intermed_filament_DNA-bd.
IPR018039. Intermediate_filament_CS.
[Graphical view]
PANTHERPTHR23239. PTHR23239. 1 hit.
PfamPF00038. Filament. 1 hit.
PF04732. Filament_head. 1 hit.
[Graphical view]
PROSITEPS00226. IF. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSVIM. mouse.
NextBio302643.
SOURCESearch...

Entry information

Entry nameVIME_MOUSE
AccessionPrimary (citable) accession number: P20152
Secondary accession number(s): O08704, Q8CCH1
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: January 23, 2007
Last modified: April 3, 2013
This is version 139 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents