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Reviewed, UniProtKB/Swiss-Prot P08670 (VIME_HUMAN)

Last modified June 16, 2009. Version 132. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Vimentin
Gene names
Name: VIM
OrganismHomo sapiens (Human)
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.

Subunit structure

Homopolymer. Interacts with HCV core protein. Interacts with LGSN and SYNM By similarity.

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.16

Post-translational modification

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.

Sequence similarities

Belongs to the intermediate filament family.

Sequence caution

The sequence BAB71275.1 differs from that shown. Reason: Miscellaneous discrepancy. Intron retention.

Ontologies

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

Amino acid modifications

Modified residue21N-acetylserine Ref.13
Modified residue51Phosphoserine Ref.18 Ref.29
Modified residue71Phosphoserine; by PKA and PKC Ref.18
Modified residue81Phosphoserine Ref.18
Modified residue91Phosphoserine; by PKC Ref.18
Modified residue101Phosphoserine; by PKC Ref.18
Modified residue251Phosphoserine; by PKA and PKC By similarity
Modified residue261Phosphoserine; by PKC By similarity
Modified residue271Phosphoserine Ref.21
Modified residue341Phosphoserine Ref.29
Modified residue381Phosphotyrosine Ref.24
Modified residue391Phosphoserine; by CaMK2, PKA and PKC Ref.18 Ref.29 Ref.26
Modified residue421Phosphoserine; by PKC Ref.18 Ref.29
Modified residue471Phosphoserine Ref.26
Modified residue491Phosphoserine By similarity
Modified residue511Phosphoserine; by PKA and PKC By similarity
Modified residue531Phosphotyrosine Ref.24
Modified residue551Phosphoserine Ref.26
Modified residue561Phosphoserine Ref.29 Ref.21 Ref.26 Ref.22 Ref.23 Ref.25 Ref.28
Modified residue611Phosphotyrosine Ref.29 Ref.24 Ref.26
Modified residue661Phosphoserine; by PKA and PKC By similarity
Modified residue721Phosphoserine Ref.18 Ref.29
Modified residue731Phosphoserine Ref.18 Ref.29 Ref.21
Modified residue831Phosphoserine Ref.29
Modified residue1171Phosphotyrosine Ref.24 Ref.19
Modified residue1441Phosphoserine Ref.29
Modified residue2141Phosphoserine Ref.21
Modified residue2261Phosphoserine Ref.29
Modified residue2991Phosphoserine Ref.29
Modified residue4091Phosphoserine Ref.29
Modified residue4121Phosphoserine Ref.29 Ref.21 Ref.25 Ref.28 Ref.27
Modified residue4191Phosphoserine By similarity
Modified residue4201Phosphoserine Ref.18
Modified residue4301Phosphoserine Ref.18 Ref.26
Modified residue4461Phosphothreonine Ref.25
Modified residue4581Phosphothreonine Ref.18 Ref.26
Modified residue4591Phosphoserine Ref.18 Ref.29 Ref.26 Ref.25 Ref.28

Experimental info

Sequence conflict39 – 5012Missing in BAB71275. Ref.5
Sequence conflict421S → D in AAA61279. Ref.1
Sequence conflict68 – 769Missing in BAB71275. Ref.5
Sequence conflict1131R → P in CAA34499. Ref.12
Sequence conflict1971E → G in CAG28618. Ref.6
Sequence conflict2011N → S in AAA61281. Ref.16
Sequence conflict2651L → S in AAA61281. Ref.16
Sequence conflict2781S → I in AAA61281. Ref.16
Sequence conflict3391S → C in AAA61281. Ref.16
Sequence conflict3501N → K in AAA61281. Ref.16
Sequence conflict4421L → F in AAA61279. Ref.1

Secondary structure

..... 466
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P08670-1 [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: 3467175] [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: 2251132] [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: 14996095] [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: 14702039] [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: 15164054] [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: 15489334] [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: 2472876] [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, MASS SPECTROMETRY.
Tissue: T-cell.
[14]"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: 9150946] [Abstract]
Cited for: PROTEIN SEQUENCE OF 17-25 AND 55-70.
Tissue: Mammary carcinoma.
[15]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, MASS SPECTROMETRY.
Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
[16]"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: 3371665] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 113-466, TISSUE SPECIFICITY.
Tissue: Fibroblast.
[17]"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: 2323579] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 167-466.
Tissue: Osteosarcoma.
[18]"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: 14762106] [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, MASS SPECTROMETRY.
[19]"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: 15592455] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-117, MASS SPECTROMETRY.
[20]"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: 15846844] [Abstract]
Cited for: INTERACTION WITH HCV CORE PROTEIN.
[21]"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: 17081983] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27; SER-56; SER-73; SER-214 AND SER-412, MASS SPECTROMETRY.
Tissue: Epithelium.
[22]"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: 16964243] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-56, MASS SPECTROMETRY.
Tissue: Epithelium.
[23]"Phosphoproteome analysis of the human mitotic spindle."
Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R.
Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006) [PubMed: 16565220] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-56, MASS SPECTROMETRY.
Tissue: Epithelium.
[24]"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer."
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M. expand/collapse author list , Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.
Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-38; TYR-53; TYR-61 AND TYR-117, MASS SPECTROMETRY.
[25]"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: 17924679] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-56; SER-412; THR-446 AND SER-459, MASS SPECTROMETRY.
Tissue: Epithelium.
[26]"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry."
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007) [PubMed: 17287340] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-39; SER-47; SER-55; SER-56; TYR-61; SER-430; THR-458 AND SER-459, MASS SPECTROMETRY.
[27]"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: 18220336] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51 AND SER-412, MASS SPECTROMETRY.
[28]"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: 18691976] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-56; SER-412 AND SER-459, MASS SPECTROMETRY.
[29]"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: 18669648] [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-226; SER-299; SER-409; SER-412 AND SER-459, MASS SPECTROMETRY.
[30]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[31]"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: 11243787] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 102-138.
[32]"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: 11889032] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 103-139 AND 328-411.
+Additional computationally mapped references.

Web resources

Wikipedia

Vimentin entry

Cross-references

Sequence databases

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. Frameshift.
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.
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.
IPIIPI00418471.
PIRA25074. S13115.
RefSeqNP_003371.2.
UniGeneHs.642813

3D structure databases

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[»]
ModBaseSearch...

Protein-protein interaction databases

IntActP08670. 86 interactions.

PTM databases

PhosphoSiteP08670.

2-D gel databases

SWISS-2DPAGEP08670.
Aarhus/Ghent-2DPAGE8417. IEF.
Cornea-2DPAGEP08670.
DOSAC-COBS-2DPAGEP08670.
HSC-2DPAGEP08670.
OGPP08670.
PHCI-2DPAGEP08670.
REPRODUCTION-2DPAGEIPI00418471.
P08670.

Proteomic databases

PeptideAtlasP08670.
PRIDEP08670.

Genome annotation databases

EnsemblENSG00000026025. Homo sapiens. [Contig view]
GeneID7431.
KEGGhsa:7431.

Organism-specific databases

GeneCardsGC10P017310.
H-InvDBHIX0008682.
HIX0035657.
HGNCHGNC:12692. VIM.
HPACAB000080.
HPA001762.
MIM193060. gene.
PharmGKBPA37311.
GenAtlasSearch...

Phylogenomic databases

HOVERGENP08670.
OMAP08670. ANRTNEK.

Enzyme and pathway databases

Pathway_Interaction_DBaurora_b_pathway. Aurora B signaling.
caspase_pathway. Caspase cascade in apoptosis.
ReactomeREACT_578. Apoptosis.

Gene expression databases

ArrayExpressP08670.
BgeeP08670.
GermOnlineENSG00000026025. Homo sapiens.

Family and domain databases

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

Other Resources

NextBio29104.
PMAP-CutDBP08670.
SOURCESearch...

Entry information

Entry nameVIME_HUMAN
AccessionPrimary (citable) accession number: P08670
Secondary accession number(s): B0YJC2 expand/collapse secondary AC list , 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: June 16, 2009
This is version 132 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Human chromosome 10

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

MIM cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents