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P08670 (VIME_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 190. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Vimentin
Gene names
Name:VIM
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

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. Ref.40

Involved with LARP6 in the stabilization of type I collagen mRNAs for CO1A1 and CO1A2. Ref.40

Subunit structure

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. Ref.23 Ref.26 Ref.28 Ref.32 Ref.34 Ref.40 Ref.46

Subcellular location

Cytoplasm Ref.42.

Tissue specificity

Highly expressed in fibroblasts, some expression in T- and B-lymphocytes, and little or no expression in Burkitt's lymphoma cell lines. Expressed in many hormone-independent mammary carcinoma cell lines. Ref.12 Ref.17

Domain

The central alpha-helical coiled-coil rod region mediates elementary homodimerization. Ref.46

Post-translational modification

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. Phosphorylation by PKN1 inhibits the formation of filaments. Phosphorylated at Ser-56 by CDK5 during neutrophil secretion in the cytoplasm. Phosphorylated by STK33. Ref.14 Ref.19 Ref.20 Ref.21 Ref.28 Ref.42

O-glycosylated during cytokinesis at sites identical or close to phosphorylation sites, this interferes with the phosphorylation status. Ref.37

Involvement in disease

Cataract 30 (CTRCT30) [MIM:116300]: An opacification of the crystalline lens of the eye that frequently results in visual impairment or blindness. Opacities vary in morphology, are often confined to a portion of the lens, and may be static or progressive. In general, the more posteriorly located and dense an opacity, the greater the impact on visual function.
Note: The disease is caused by mutations affecting the gene represented in this entry.

Sequence similarities

Belongs to the intermediate filament family.

Sequence caution

The sequence BAB71275.1 differs from that shown. Reason: Product of a cloning artifact.

Ontologies

Keywords
   Biological processHost-virus interaction
   Cellular componentCytoplasm
Intermediate filament
   DiseaseCataract
Disease mutation
   DomainCoiled coil
   PTMAcetylation
Glycoprotein
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processBergmann glial cell differentiation

Inferred from electronic annotation. Source: Ensembl

apoptotic process

Traceable author statement. Source: Reactome

astrocyte development

Inferred from electronic annotation. Source: Ensembl

cellular component disassembly involved in execution phase of apoptosis

Traceable author statement. Source: Reactome

cellular component movement

Traceable author statement PubMed 16130169. Source: UniProtKB

intermediate filament organization

Inferred from electronic annotation. Source: Ensembl

lens fiber cell development

Inferred from electronic annotation. Source: Ensembl

muscle filament sliding

Traceable author statement. Source: Reactome

negative regulation of neuron projection development

Inferred from electronic annotation. Source: Ensembl

viral process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcell leading edge

Inferred from electronic annotation. Source: Ensembl

cell projection

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Inferred from direct assay Ref.15. Source: UniProtKB

cytoskeleton

Traceable author statement PubMed 16130169. Source: UniProtKB

cytosol

Inferred from direct assay Ref.34. Source: UniProtKB

extracellular vesicular exosome

Inferred from direct assay PubMed 21362503. Source: UniProtKB

intermediate filament

Inferred from direct assay Ref.45. Source: UniProtKB

intermediate filament cytoskeleton

Inferred from direct assay. Source: HPA

peroxisome

Inferred from direct assay PubMed 17881773. Source: UniProtKB

   Molecular_functiondouble-stranded RNA binding

Inferred from direct assay PubMed 21266579. Source: MGI

glycoprotein binding

Inferred from physical interaction PubMed 19420356. Source: UniProt

identical protein binding

Inferred from physical interaction PubMed 15383276PubMed 16169070PubMed 21900206. Source: IntAct

protein C-terminus binding

Inferred from physical interaction Ref.34. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 11827972Ref.26Ref.28Ref.32. Source: UniProtKB

scaffold protein binding

Inferred from physical interaction PubMed 10852826. Source: BHF-UCL

structural constituent of cytoskeleton

Inferred from direct assay Ref.45. Source: UniProtKB

structural constituent of eye lens

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.13
Chain2 – 466465Vimentin
PRO_0000063754

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 Ref.46
Coiled coil154 – 24592 Ref.46
Coiled coil303 – 407105 Ref.46

Sites

Site3511Stutter

Amino acid modifications

Modified residue21N-acetylserine Ref.13
Modified residue51Phosphoserine Ref.21 Ref.31
Modified residue71Phosphoserine; by PKA and PKC; alternate Ref.21
Modified residue81Phosphoserine Ref.21
Modified residue91Phosphoserine; by PKC Ref.21
Modified residue101Phosphoserine; by PKC Ref.21
Modified residue201Phosphothreonine Ref.38
Modified residue251Phosphoserine Ref.31
Modified residue261Phosphoserine; by PKC By similarity
Modified residue271Phosphoserine
Modified residue291Phosphoserine
Modified residue331Phosphothreonine; alternate
Modified residue341Phosphoserine; alternate Ref.31
Modified residue381Phosphotyrosine
Modified residue391Phosphoserine; by CaMK2, PKA, PKC and ROCK2 Ref.21 Ref.31
Modified residue421Phosphoserine; by PKC Ref.21 Ref.31 Ref.38
Modified residue471Phosphoserine Ref.38
Modified residue491Phosphoserine By similarity
Modified residue511Phosphoserine Ref.31 Ref.35 Ref.38 Ref.41
Modified residue531Phosphotyrosine
Modified residue551Phosphoserine
Modified residue561Phosphoserine; by CDK5 and CDK1 Ref.14 Ref.25 Ref.31 Ref.35 Ref.38 Ref.42
Modified residue611Phosphotyrosine Ref.31 Ref.35
Modified residue661Phosphoserine; by PKA and PKC By similarity
Modified residue721Phosphoserine; by AURKB and ROCK2 Ref.20 Ref.21 Ref.31
Modified residue731Phosphoserine Ref.21 Ref.31 Ref.38
Modified residue831Phosphoserine Ref.31 Ref.38
Modified residue1171Phosphotyrosine Ref.22
Modified residue1201N6-acetyllysine; alternate Ref.36
Modified residue1201N6-succinyllysine; alternate By similarity
Modified residue1291N6-acetyllysine; alternate By similarity
Modified residue1291N6-succinyllysine; alternate By similarity
Modified residue1391N6-acetyllysine Ref.36
Modified residue1441Phosphoserine Ref.31 Ref.38 Ref.41
Modified residue1681N6-acetyllysine By similarity
Modified residue1881N6-acetyllysine; alternate By similarity
Modified residue1881N6-succinyllysine; alternate By similarity
Modified residue2141Phosphoserine Ref.24 Ref.38
Modified residue2231N6-acetyllysine By similarity
Modified residue2261Phosphoserine Ref.38
Modified residue2351N6-acetyllysine By similarity
Modified residue2611Phosphoserine
Modified residue2661Phosphothreonine
Modified residue2941N6-acetyllysine; alternate By similarity
Modified residue2941N6-succinyllysine; alternate By similarity
Modified residue2991Phosphoserine Ref.38
Modified residue3731N6-acetyllysine Ref.36
Modified residue4091Phosphoserine Ref.31
Modified residue4121Phosphoserine Ref.24 Ref.27 Ref.30 Ref.31 Ref.38
Modified residue4191Phosphoserine Ref.38
Modified residue4201Phosphoserine Ref.21 Ref.38
Modified residue4261Phosphothreonine Ref.38
Modified residue4301Phosphoserine Ref.21 Ref.38
Modified residue4361Phosphothreonine Ref.38
Modified residue4451N6-acetyllysine; alternate Ref.36
Modified residue4451N6-succinyllysine; alternate By similarity
Modified residue4461Phosphothreonine
Modified residue4581Phosphothreonine Ref.21
Modified residue4591Phosphoserine Ref.21 Ref.31 Ref.38 Ref.41
Glycosylation71O-linked (GlcNAc); alternate Ref.37
Glycosylation331O-linked (GlcNAc); alternate Ref.37
Glycosylation341O-linked (GlcNAc); alternate Ref.37

Natural variations

Natural variant1511E → K in CTRC30; the mutation increases the proteasome activity in transfected cells; causes also a severe kinetic defect in vimentin assembly both in vitro and in vivo. Ref.48
VAR_070100

Experimental info

Sequence conflict421S → D in AAA61279. Ref.1
Sequence conflict1131R → P in CAA34499. Ref.12
Sequence conflict1971E → G in CAG28618. Ref.6
Sequence conflict2011N → S in AAA61281. Ref.17
Sequence conflict2651L → S in AAA61281. Ref.17
Sequence conflict2781S → I in AAA61281. Ref.17
Sequence conflict3391S → C in AAA61281. Ref.17
Sequence conflict3501N → K in AAA61281. Ref.17
Sequence conflict4421L → F in AAA61279. Ref.1

Secondary structure

............. 466
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P08670 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: BAB54026665B015A

FASTA46653,652
        10         20         30         40         50         60 
MSTRSVSSSS YRRMFGGPGT ASRPSSSRSY VTTSTRTYSL GSALRPSTSR SLYASSPGGV 

        70         80         90        100        110        120 
YATRSSAVRL 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 NTLQSFRQDV DNASLARLDL ERKVESLQEE IAFLKKLHEE 

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

       310        320        330        340        350        360 
AANRNNDALR QAKQESTEYR RQVQSLTCEV DALKGTNESL ERQMREMEEN FAVEAANYQD 

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

       430        440        450        460 
LNLRETNLDS LPLVDTHSKR TLLIKTVETR DGQVINETSQ HHDDLE 

« Hide

References

« Hide 'large scale' references
[1]"Coding sequence and growth regulation of the human vimentin gene."
Ferrari S., Battini R., Kaczmarek L., Rittling S., Calabretta B., de Riel J.K., Philiponis V., Wei J.-F., Baserga R.
Mol. Cell. Biol. 6:3614-3620(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Nucleotide sequence of cDNA covering the complete coding part of the human vimentin gene."
Honore B., Madsen P., Basse B., Andersen A., Walbum E., Celis J.E., Leffers H.
Nucleic Acids Res. 18:6692-6692(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"SEREX identification of new tumour-associated antigens in cutaneous T-cell lymphoma."
Hartmann T.B., Thiel D., Dummer R., Schadendorf D., Eichmueller S.
Br. J. Dermatol. 150:252-258(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Lymphoma.
[4]Zimbelmann R.
Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Testis.
[5]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Embryo, Placenta and Stomach.
[6]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[7]Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Adipose tissue and Coronary artery.
[8]NHLBI resequencing and genotyping service (RS&G)
Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[9]"The DNA sequence and comparative analysis of human chromosome 10."
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J. expand/collapse author list , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[10]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[11]"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: Cervix, Placenta and Testis.
[12]"Vimentin rather than keratin expression in some hormone-independent breast cancer cell lines and in oncogene-transformed mammary epithelial cells."
Sommers C.L., Walker-Jones D., Heckford S.E., Worland P., Valverius E., Clark R., McCormick F., Stampfer M., Abularach S., Gelmann E.P.
Cancer Res. 49:4258-4263(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-135, TISSUE SPECIFICITY.
Tissue: Mammary carcinoma.
[13]Bienvenut W.V., Kanor S., Tissot J.-D., Quadroni M.
Submitted (MAY-2006) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-11; 87-96; 129-138; 188-195; 223-234; 282-291; 322-333 AND 381-389, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: T-cell.
[14]Bienvenut W.V., Fleming J., Leug H.Y.
Submitted (JAN-2010) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 5-12; 14-45; 51-64; 72-78; 105-113; 123-143; 159-184; 187-217; 223-236; 271-292; 295-313; 322-390 AND 403-466, PHOSPHORYLATION AT SER-56, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Hepatoma.
[15]"Two-dimensional electrophoretic analysis of human breast carcinoma proteins: mapping of proteins that bind to the SH3 domain of mixed lineage kinase MLK2."
Rasmussen R.K., Ji H., Eddes J.S., Moritz R.L., Reid G.E., Simpson R.J., Dorow D.S.
Electrophoresis 18:588-598(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 17-25 AND 55-70.
Tissue: Mammary carcinoma.
[16]Lubec G., Vishwanath V., Chen W.-Q., Sun Y.
Submitted (DEC-2008) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 51-64; 79-97; 105-113; 130-139; 146-155; 176-184; 189-207; 223-235; 283-292; 295-304; 322-334; 346-373; 382-401 AND 411-439, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
[17]"Nucleotide sequence of the human vimentin gene and regulation of its transcription in tissues and cultured cells."
Perreau J., Lilienbaum A., Vasseur M., Paulin D.
Gene 62:7-16(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 113-466, TISSUE SPECIFICITY.
Tissue: Fibroblast.
[18]"Isolation of a human vimentin cDNA with a long 3'-noncoding region from a human osteosarcoma cell line (MG-63)."
Gupta A.K., Aubin J.E., Waye M.M.Y.
Gene 86:303-304(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 167-466.
Tissue: Osteosarcoma.
[19]"Domain-specific phosphorylation of vimentin and glial fibrillary acidic protein by PKN."
Matsuzawa K., Kosako H., Inagaki N., Shibata H., Mukai H., Ono Y., Amano M., Kaibuchi K., Matsuura Y., Azuma I., Inagaki M.
Biochem. Biophys. Res. Commun. 234:621-625(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION.
[20]"Aurora-B regulates the cleavage furrow-specific vimentin phosphorylation in the cytokinetic process."
Goto H., Yasui Y., Kawajiri A., Nigg E.A., Terada Y., Tatsuka M., Nagata K., Inagaki M.
J. Biol. Chem. 278:8526-8530(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-72.
[21]"Specific in vivo phosphorylation sites determine the assembly dynamics of vimentin intermediate filaments."
Eriksson J.E., He T., Trejo-Skalli A.V., Harmala-Brasken A.-S., Hellman J., Chou Y.-H., Goldman R.D.
J. Cell Sci. 117:919-932(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-5; SER-7; SER-8; SER-9; SER-10; SER-39; SER-42; SER-72; SER-73; SER-420; SER-430; THR-458 AND SER-459, IDENTIFICATION BY MASS SPECTROMETRY.
[22]"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-117, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[23]"Proteomic profiling of cellular proteins interacting with the hepatitis C virus core protein."
Kang S.-M., Shin M.-J., Kim J.-H., Oh J.-W.
Proteomics 5:2227-2237(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HCV CORE PROTEIN.
[24]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-214 AND SER-412, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[25]"A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-56, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[26]"Dystonia-causing mutant torsinA inhibits cell adhesion and neurite extension through interference with cytoskeletal dynamics."
Hewett J.W., Zeng J., Niland B.P., Bragg D.C., Breakefield X.O.
Neurobiol. Dis. 22:98-111(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TOR1A AND TOR1AIP1.
[27]"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."
Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.
J. Proteome Res. 6:4150-4162(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-412, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[28]"The serine/threonine kinase Stk33 exhibits autophosphorylation and phosphorylates the intermediate filament protein Vimentin."
Brauksiepe B., Mujica A.O., Herrmann H., Schmidt E.R.
BMC Biochem. 9:25-25(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH STK33, PHOSPHORYLATION BY STK33.
[29]"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[30]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-412, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[31]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-5; SER-25; SER-34; SER-39; SER-42; SER-51; SER-56; TYR-61; SER-72; SER-73; SER-83; SER-144; SER-409; SER-412 AND SER-459, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[32]"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.
[33]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[34]"The cellular distribution of serotonin transporter is impeded on serotonin-altered vimentin network."
Ahmed B.A., Bukhari I.A., Jeffus B.C., Harney J.T., Thyparambil S., Ziu E., Fraer M., Rusch N.J., Zimniak P., Lupashin V., Tang D., Kilic F.
PLoS ONE 4:E4730-E4730(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SLC6A4.
[35]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51; SER-56 AND TYR-61, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[36]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-120; LYS-139; LYS-373 AND LYS-445, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[37]"Extensive crosstalk between O-GlcNAcylation and phosphorylation regulates cytokinesis."
Wang Z., Udeshi N.D., Slawson C., Compton P.D., Sakabe K., Cheung W.D., Shabanowitz J., Hunt D.F., Hart G.W.
Sci. Signal. 3:RA2-RA2(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT SER-7; THR-33 AND SER-34.
[38]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-20; SER-42; SER-47; SER-51; SER-56; SER-73; SER-83; SER-144; SER-214; SER-226; SER-299; SER-412; SER-419; SER-420; THR-426; SER-430; THR-436 AND SER-459, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[39]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[40]"A novel role of vimentin filaments: binding and stabilization of collagen mRNAs."
Challa A.A., Stefanovic B.
Mol. Cell. Biol. 31:3773-3789(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN COLLAGEN MRNA STABILIZATION, INTERACTION WITH LARP6.
[41]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51; SER-144 AND SER-459, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[42]"Cdk5 mediates vimentin Ser56 phosphorylation during GTP-induced secretion by neutrophils."
Lee K.Y., Liu L., Jin Y., Fu S.B., Rosales J.L.
J. Cell. Physiol. 227:739-750(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-56, SUBCELLULAR LOCATION.
[43]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[44]"Divide-and-conquer crystallographic approach towards an atomic structure of intermediate filaments."
Strelkov S.V., Herrmann H., Geisler N., Lustig A., Ivaninskii S., Zimbelmann R., Burkhard P., Aebi U.
J. Mol. Biol. 306:773-781(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 102-138.
[45]"Conserved segments 1A and 2B of the intermediate filament dimer: their atomic structures and role in filament assembly."
Strelkov S.V., Herrmann H., Geisler N., Wedig T., Zimbelmann R., Aebi U., Burkhard P.
EMBO J. 21:1255-1266(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 103-139 AND 328-411.
[46]"Atomic structure of vimentin coil 2."
Nicolet S., Herrmann H., Aebi U., Strelkov S.V.
J. Struct. Biol. 170:369-376(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 263-334, COILED-COIL DOMAINS, SUBUNIT.
[47]"Stabilization of vimentin coil2 fragment via an engineered disulfide."
Chernyatina A.A., Strelkov S.V.
J. Struct. Biol. 177:46-53(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 261-335 OF MUTANT CYS-265.
[48]"Dominant cataract formation in association with a vimentin assembly disrupting mutation."
Muller M., Bhattacharya S.S., Moore T., Prescott Q., Wedig T., Herrmann H., Magin T.M.
Hum. Mol. Genet. 18:1052-1057(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CTRC30 LYS-151, CHARACTERIZATION OF VARIANT CTRC30 LYS-151.
+Additional computationally mapped references.

Web resources

Wikipedia

Vimentin entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M14144 Genomic DNA. Translation: AAA61279.1.
X56134 mRNA. Translation: CAA39600.1.
AF328728 mRNA. Translation: AAN09720.1.
Z19554 mRNA. Translation: CAA79613.2.
AK056766 mRNA. Translation: BAB71275.1. Sequence problems.
AK097336 mRNA. Translation: BAC05002.1.
AK290643 mRNA. Translation: BAF83332.1.
CR407690 mRNA. Translation: CAG28618.1.
AK222507 mRNA. Translation: BAD96227.1.
AK222602 mRNA. Translation: BAD96322.1.
EF445046 Genomic DNA. Translation: ACA06101.1.
EF445046 Genomic DNA. Translation: ACA06102.1.
AL133415 Genomic DNA. Translation: CAB87963.1.
CH471072 Genomic DNA. Translation: EAW86215.1.
CH471072 Genomic DNA. Translation: EAW86216.1.
BC000163 mRNA. Translation: AAH00163.2.
BC030573 mRNA. Translation: AAH30573.1.
BC066956 mRNA. Translation: AAH66956.1.
X16478 mRNA. Translation: CAA34499.1.
M18895 expand/collapse EMBL AC list , M18888, M18889, M18890, M18891, M18892, M18893, M18894 Genomic DNA. Translation: AAA61281.2.
M25246 mRNA. Translation: AAA61282.1.
CCDSCCDS7120.1.
PIRA25074. S13115.
RefSeqNP_003371.2. NM_003380.3.
XP_006717563.1. XM_006717500.1.
UniGeneHs.455493.
Hs.691131.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1GK4X-ray2.30A/B/C/D/E/F328-411[»]
1GK6X-ray1.90A/B385-412[»]
1GK7X-ray1.40A102-138[»]
3G1EX-ray1.83A/B102-138[»]
3KLTX-ray2.70A/B/C/D263-334[»]
3S4RX-ray2.45A/B99-189[»]
3SSUX-ray2.60A/B99-189[»]
3SWKX-ray1.70A/B153-238[»]
3TRTX-ray2.30A/B261-335[»]
3UF1X-ray2.81A/B/C/D144-251[»]
4MCYX-ray2.30C66-78[»]
4MCZX-ray2.41C59-71[»]
4MD0X-ray2.19C59-71[»]
4MD5X-ray1.65C66-78[»]
4MDIX-ray2.00C66-78[»]
4MDJX-ray1.70C66-78[»]
ProteinModelPortalP08670.
SMRP08670. Positions 99-248, 263-406.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113272. 220 interactions.
DIPDIP-32507N.
IntActP08670. 132 interactions.
MINTMINT-118802.

PTM databases

PhosphoSiteP08670.

Polymorphism databases

DMDM55977767.

2D gel databases

DOSAC-COBS-2DPAGEP08670.
OGPP08670.
REPRODUCTION-2DPAGEIPI00418471.
P08670.
SWISS-2DPAGEP08670.
UCD-2DPAGEP08670.

Proteomic databases

MaxQBP08670.
PaxDbP08670.
PeptideAtlasP08670.
PRIDEP08670.

Protocols and materials databases

DNASU7431.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000224237; ENSP00000224237; ENSG00000026025.
ENST00000544301; ENSP00000446007; ENSG00000026025.
GeneID7431.
KEGGhsa:7431.
UCSCuc001iou.2. human.

Organism-specific databases

CTD7431.
GeneCardsGC10P017270.
H-InvDBHIX0035657.
HGNCHGNC:12692. VIM.
HPACAB000080.
CAB058687.
HPA001762.
MIM116300. phenotype.
193060. gene.
neXtProtNX_P08670.
Orphanet98984. Pulverulent cataract.
PharmGKBPA37311.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG146769.
HOVERGENHBG013015.
InParanoidP08670.
KOK07606.
OMAINTEFKA.
OrthoDBEOG7FV3Q8.
PhylomeDBP08670.
TreeFamTF330122.

Enzyme and pathway databases

ReactomeREACT_17044. Muscle contraction.
REACT_578. Apoptosis.

Gene expression databases

ArrayExpressP08670.
BgeeP08670.
GenevestigatorP08670.

Family and domain databases

InterProIPR001664. IF.
IPR006821. Intermed_filament_DNA-bd.
IPR018039. Intermediate_filament_CS.
IPR027699. Vimentin.
[Graphical view]
PANTHERPTHR23239. PTHR23239. 1 hit.
PTHR23239:SF27. PTHR23239:SF27. 1 hit.
PfamPF00038. Filament. 1 hit.
PF04732. Filament_head. 1 hit.
[Graphical view]
PROSITEPS00226. IF. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSVIM. human.
EvolutionaryTraceP08670.
GeneWikiVimentin.
GenomeRNAi7431.
NextBio29104.
PMAP-CutDBP08670.
PROP08670.
SOURCESearch...

Entry information

Entry nameVIME_HUMAN
AccessionPrimary (citable) accession number: P08670
Secondary accession number(s): B0YJC2 expand/collapse secondary AC list , D3DRU4, Q15867, Q15868, Q15869, Q548L2, Q6LER9, Q8N850, Q96ML2, Q9NTM3
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 190 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 10

Human chromosome 10: entries, gene names and cross-references to MIM