Full text data of VIM
VIM
[Confidence: low (only semi-automatic identification from reviews)]
Vimentin
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Vimentin
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P08670
ID VIME_HUMAN Reviewed; 466 AA.
AC P08670; B0YJC2; D3DRU4; Q15867; Q15868; Q15869; Q548L2; Q6LER9;
read moreAC Q8N850; Q96ML2; Q9NTM3;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 22-JAN-2014, entry version 184.
DE RecName: Full=Vimentin;
GN Name=VIM;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3467175;
RA Ferrari S., Battini R., Kaczmarek L., Rittling S., Calabretta B.,
RA de Riel J.K., Philiponis V., Wei J.-F., Baserga R.;
RT "Coding sequence and growth regulation of the human vimentin gene.";
RL Mol. Cell. Biol. 6:3614-3620(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2251132; DOI=10.1093/nar/18.22.6692;
RA Honore B., Madsen P., Basse B., Andersen A., Walbum E., Celis J.E.,
RA Leffers H.;
RT "Nucleotide sequence of cDNA covering the complete coding part of the
RT human vimentin gene.";
RL Nucleic Acids Res. 18:6692-6692(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Lymphoma;
RX PubMed=14996095; DOI=10.1111/j.1365-2133.2004.05651.x;
RA Hartmann T.B., Thiel D., Dummer R., Schadendorf D., Eichmueller S.;
RT "SEREX identification of new tumour-associated antigens in cutaneous
RT T-cell lymphoma.";
RL Br. J. Dermatol. 150:252-258(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Testis;
RA Zimbelmann R.;
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo, Placenta, and Stomach;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Adipose tissue, and Coronary artery;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG NHLBI resequencing and genotyping service (RS&G;);
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
RA Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
RA Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
RA Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
RA Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
RA Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
RA Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
RA Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
RA Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
RA Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
RA Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
RA Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
RA Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
RA Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
RA Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
RA Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
RA Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
RA Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [11]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Cervix, Placenta, and Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [12]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-135, AND TISSUE SPECIFICITY.
RC TISSUE=Mammary carcinoma;
RX PubMed=2472876;
RA Sommers C.L., Walker-Jones D., Heckford S.E., Worland P.,
RA Valverius E., Clark R., McCormick F., Stampfer M., Abularach S.,
RA Gelmann E.P.;
RT "Vimentin rather than keratin expression in some hormone-independent
RT breast cancer cell lines and in oncogene-transformed mammary
RT epithelial cells.";
RL Cancer Res. 49:4258-4263(1989).
RN [13]
RP PROTEIN SEQUENCE OF 2-11; 87-96; 129-138; 188-195; 223-234; 282-291;
RP 322-333 AND 381-389, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT
RP SER-2, AND MASS SPECTROMETRY.
RC TISSUE=T-cell;
RA Bienvenut W.V., Kanor S., Tissot J.-D., Quadroni M.;
RL Submitted (MAY-2006) to UniProtKB.
RN [14]
RP PROTEIN SEQUENCE OF 5-12; 14-45; 51-64; 72-78; 105-113; 123-143;
RP 159-184; 187-217; 223-236; 271-292; 295-313; 322-390 AND 403-466,
RP PHOSPHORYLATION AT SER-56, AND MASS SPECTROMETRY.
RC TISSUE=Hepatoma;
RA Bienvenut W.V., Fleming J., Leug H.Y.;
RL Submitted (JAN-2010) to UniProtKB.
RN [15]
RP PROTEIN SEQUENCE OF 17-25 AND 55-70.
RC TISSUE=Mammary carcinoma;
RX PubMed=9150946; DOI=10.1002/elps.1150180342;
RA Rasmussen R.K., Ji H., Eddes J.S., Moritz R.L., Reid G.E.,
RA Simpson R.J., Dorow D.S.;
RT "Two-dimensional electrophoretic analysis of human breast carcinoma
RT proteins: mapping of proteins that bind to the SH3 domain of mixed
RT lineage kinase MLK2.";
RL Electrophoresis 18:588-598(1997).
RN [16]
RP PROTEIN SEQUENCE OF 51-64; 79-97; 105-113; 130-139; 146-155; 176-184;
RP 189-207; 223-235; 283-292; 295-304; 322-334; 346-373; 382-401 AND
RP 411-439, AND MASS SPECTROMETRY.
RC TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
RA Lubec G., Vishwanath V., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [17]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 113-466, AND TISSUE SPECIFICITY.
RC TISSUE=Fibroblast;
RX PubMed=3371665; DOI=10.1016/0378-1119(88)90575-6;
RA Perreau J., Lilienbaum A., Vasseur M., Paulin D.;
RT "Nucleotide sequence of the human vimentin gene and regulation of its
RT transcription in tissues and cultured cells.";
RL Gene 62:7-16(1988).
RN [18]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 167-466.
RC TISSUE=Osteosarcoma;
RX PubMed=2323579; DOI=10.1016/0378-1119(90)90295-3;
RA Gupta A.K., Aubin J.E., Waye M.M.Y.;
RT "Isolation of a human vimentin cDNA with a long 3'-noncoding region
RT from a human osteosarcoma cell line (MG-63).";
RL Gene 86:303-304(1990).
RN [19]
RP PHOSPHORYLATION.
RX PubMed=9175763; DOI=10.1006/bbrc.1997.6669;
RA Matsuzawa K., Kosako H., Inagaki N., Shibata H., Mukai H., Ono Y.,
RA Amano M., Kaibuchi K., Matsuura Y., Azuma I., Inagaki M.;
RT "Domain-specific phosphorylation of vimentin and glial fibrillary
RT acidic protein by PKN.";
RL Biochem. Biophys. Res. Commun. 234:621-625(1997).
RN [20]
RP PHOSPHORYLATION AT SER-72.
RX PubMed=12458200; DOI=10.1074/jbc.M210892200;
RA Goto H., Yasui Y., Kawajiri A., Nigg E.A., Terada Y., Tatsuka M.,
RA Nagata K., Inagaki M.;
RT "Aurora-B regulates the cleavage furrow-specific vimentin
RT phosphorylation in the cytokinetic process.";
RL J. Biol. Chem. 278:8526-8530(2003).
RN [21]
RP PHOSPHORYLATION AT SER-5; SER-7; SER-8; SER-9; SER-10; SER-39; SER-42;
RP SER-72; SER-73; SER-420; SER-430; THR-458 AND SER-459, AND MASS
RP SPECTROMETRY.
RX PubMed=14762106; DOI=10.1242/jcs.00906;
RA Eriksson J.E., He T., Trejo-Skalli A.V., Harmala-Brasken A.-S.,
RA Hellman J., Chou Y.-H., Goldman R.D.;
RT "Specific in vivo phosphorylation sites determine the assembly
RT dynamics of vimentin intermediate filaments.";
RL J. Cell Sci. 117:919-932(2004).
RN [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-117, AND MASS
RP SPECTROMETRY.
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer
RT cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [23]
RP INTERACTION WITH HCV CORE PROTEIN.
RX PubMed=15846844; DOI=10.1002/pmic.200401093;
RA Kang S.-M., Shin M.-J., Kim J.-H., Oh J.-W.;
RT "Proteomic profiling of cellular proteins interacting with the
RT hepatitis C virus core protein.";
RL Proteomics 5:2227-2237(2005).
RN [24]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-214 AND SER-412, AND
RP MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [25]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-56, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein
RT phosphorylation analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [26]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-412, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=17924679; DOI=10.1021/pr070152u;
RA Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
RT "Improved titanium dioxide enrichment of phosphopeptides from HeLa
RT cells and high confident phosphopeptide identification by cross-
RT validation of MS/MS and MS/MS/MS spectra.";
RL J. Proteome Res. 6:4150-4162(2007).
RN [27]
RP INTERACTION WITH STK33, AND PHOSPHORYLATION BY STK33.
RX PubMed=18811945; DOI=10.1186/1471-2091-9-25;
RA Brauksiepe B., Mujica A.O., Herrmann H., Schmidt E.R.;
RT "The serine/threonine kinase Stk33 exhibits autophosphorylation and
RT phosphorylates the intermediate filament protein Vimentin.";
RL BMC Biochem. 9:25-25(2008).
RN [28]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
RA Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
RT efficient phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [29]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-412, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [30]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-5; SER-25; SER-34;
RP SER-39; SER-42; SER-51; SER-56; TYR-61; SER-72; SER-73; SER-83;
RP SER-144; SER-409; SER-412 AND SER-459, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [31]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [32]
RP INTERACTION WITH SLC6A4.
RX PubMed=19270731; DOI=10.1371/journal.pone.0004730;
RA Ahmed B.A., Bukhari I.A., Jeffus B.C., Harney J.T., Thyparambil S.,
RA Ziu E., Fraer M., Rusch N.J., Zimniak P., Lupashin V., Tang D.,
RA Kilic F.;
RT "The cellular distribution of serotonin transporter is impeded on
RT serotonin-altered vimentin network.";
RL PLoS ONE 4:E4730-E4730(2009).
RN [33]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51; SER-56 AND TYR-61,
RP AND MASS SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [34]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-120; LYS-139; LYS-373 AND
RP LYS-445, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [35]
RP GLYCOSYLATION AT SER-7; THR-33 AND SER-34.
RX PubMed=20068230; DOI=10.1126/scisignal.2000526;
RA Wang Z., Udeshi N.D., Slawson C., Compton P.D., Sakabe K.,
RA Cheung W.D., Shabanowitz J., Hunt D.F., Hart G.W.;
RT "Extensive crosstalk between O-GlcNAcylation and phosphorylation
RT regulates cytokinesis.";
RL Sci. Signal. 3:RA2-RA2(2010).
RN [36]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-20; SER-42; SER-47;
RP SER-51; SER-56; SER-73; SER-83; SER-144; SER-214; SER-226; SER-299;
RP SER-412; SER-419; SER-420; THR-426; SER-430; THR-436 AND SER-459, AND
RP MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [37]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [38]
RP FUNCTION IN COLLAGEN MRNA STABILIZATION, AND INTERACTION WITH LARP6.
RX PubMed=21746880; DOI=10.1128/MCB.05263-11;
RA Challa A.A., Stefanovic B.;
RT "A novel role of vimentin filaments: binding and stabilization of
RT collagen mRNAs.";
RL Mol. Cell. Biol. 31:3773-3789(2011).
RN [39]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51; SER-144 AND SER-459,
RP AND MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [40]
RP PHOSPHORYLATION AT SER-56, AND SUBCELLULAR LOCATION.
RX PubMed=21465480; DOI=10.1002/jcp.22782;
RA Lee K.Y., Liu L., Jin Y., Fu S.B., Rosales J.L.;
RT "Cdk5 mediates vimentin Ser56 phosphorylation during GTP-induced
RT secretion by neutrophils.";
RL J. Cell. Physiol. 227:739-750(2012).
RN [41]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [42]
RP X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 102-138.
RX PubMed=11243787; DOI=10.1006/jmbi.2001.4442;
RA Strelkov S.V., Herrmann H., Geisler N., Lustig A., Ivaninskii S.,
RA Zimbelmann R., Burkhard P., Aebi U.;
RT "Divide-and-conquer crystallographic approach towards an atomic
RT structure of intermediate filaments.";
RL J. Mol. Biol. 306:773-781(2001).
RN [43]
RP X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 103-139 AND 328-411.
RX PubMed=11889032; DOI=10.1093/emboj/21.6.1255;
RA Strelkov S.V., Herrmann H., Geisler N., Wedig T., Zimbelmann R.,
RA Aebi U., Burkhard P.;
RT "Conserved segments 1A and 2B of the intermediate filament dimer:
RT their atomic structures and role in filament assembly.";
RL EMBO J. 21:1255-1266(2002).
RN [44]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 263-334, COILED-COIL DOMAINS,
RP AND SUBUNIT.
RX PubMed=20176112; DOI=10.1016/j.jsb.2010.02.012;
RA Nicolet S., Herrmann H., Aebi U., Strelkov S.V.;
RT "Atomic structure of vimentin coil 2.";
RL J. Struct. Biol. 170:369-376(2010).
RN [45]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 261-335 OF MUTANT CYS-265.
RX PubMed=22119849; DOI=10.1016/j.jsb.2011.11.014;
RA Chernyatina A.A., Strelkov S.V.;
RT "Stabilization of vimentin coil2 fragment via an engineered
RT disulfide.";
RL J. Struct. Biol. 177:46-53(2012).
RN [46]
RP VARIANT CTRC30 LYS-151, AND CHARACTERIZATION OF VARIANT CTRC30
RP LYS-151.
RX PubMed=19126778; DOI=10.1093/hmg/ddn440;
RA Muller M., Bhattacharya S.S., Moore T., Prescott Q., Wedig T.,
RA Herrmann H., Magin T.M.;
RT "Dominant cataract formation in association with a vimentin assembly
RT disrupting mutation.";
RL Hum. Mol. Genet. 18:1052-1057(2009).
CC -!- FUNCTION: Vimentins are class-III intermediate filaments found in
CC various non-epithelial cells, especially mesenchymal cells.
CC Vimentin is attached to the nucleus, endoplasmic reticulum, and
CC mitochondria, either laterally or terminally.
CC -!- FUNCTION: Involved with LARP6 in the stabilization of type I
CC collagen mRNAs for CO1A1 and CO1A2.
CC -!- SUBUNIT: Homopolymer assembled from elementary dimers. Interacts
CC with HCV core protein. Interacts with LGSN and SYNM. Interacts
CC (via rod region) with PLEC (via CH 1 domain) (By similarity).
CC Interacts with SLC6A4. Interacts with STK33. Interacts with LARP6.
CC Interacts with RAB8B (By similarity).
CC -!- INTERACTION:
CC Self; NbExp=6; IntAct=EBI-353844, EBI-353844;
CC P31749:AKT1; NbExp=29; IntAct=EBI-353844, EBI-296087;
CC P31751:AKT2; NbExp=6; IntAct=EBI-353844, EBI-296058;
CC Q9H6U6:BCAS3; NbExp=3; IntAct=EBI-353844, EBI-6083685;
CC Q14194:CRMP1; NbExp=3; IntAct=EBI-353844, EBI-473101;
CC O95251:KAT7; NbExp=4; IntAct=EBI-353844, EBI-473199;
CC P54727:RAD23B; NbExp=2; IntAct=EBI-353844, EBI-954531;
CC O95361:TRIM16; NbExp=3; IntAct=EBI-353844, EBI-727384;
CC P63104:YWHAZ; NbExp=2; IntAct=EBI-353844, EBI-347088;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- TISSUE SPECIFICITY: Highly expressed in fibroblasts, some
CC expression in T- and B-lymphocytes, and little or no expression in
CC Burkitt's lymphoma cell lines. Expressed in many hormone-
CC independent mammary carcinoma cell lines.
CC -!- DOMAIN: The central alpha-helical coiled-coil rod region mediates
CC elementary homodimerization.
CC -!- PTM: Filament disassembly during mitosis is promoted by
CC phosphorylation at Ser-55 as well as by nestin (By similarity).
CC One of the most prominent phosphoproteins in various cells of
CC mesenchymal origin. Phosphorylation is enhanced during cell
CC division, at which time vimentin filaments are significantly
CC reorganized. Phosphorylation by PKN1 inhibits the formation of
CC filaments. Phosphorylated at Ser-56 by CDK5 during neutrophil
CC secretion in the cytoplasm. Phosphorylated by STK33.
CC -!- PTM: O-glycosylated during cytokinesis at sites identical or close
CC to phosphorylation sites, this interferes with the phosphorylation
CC status.
CC -!- DISEASE: Cataract 30 (CTRCT30) [MIM:116300]: An opacification of
CC the crystalline lens of the eye that frequently results in visual
CC impairment or blindness. Opacities vary in morphology, are often
CC confined to a portion of the lens, and may be static or
CC progressive. In general, the more posteriorly located and dense an
CC opacity, the greater the impact on visual function. Note=The
CC disease is caused by mutations affecting the gene represented in
CC this entry.
CC -!- SIMILARITY: Belongs to the intermediate filament family.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB71275.1; Type=Miscellaneous discrepancy; Note=Intron retention;
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Vimentin entry;
CC URL="http://en.wikipedia.org/wiki/Vimentin";
CC -----------------------------------------------------------------------
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DR EMBL; M14144; AAA61279.1; -; Genomic_DNA.
DR EMBL; X56134; CAA39600.1; -; mRNA.
DR EMBL; AF328728; AAN09720.1; -; mRNA.
DR EMBL; Z19554; CAA79613.2; -; mRNA.
DR EMBL; AK056766; BAB71275.1; ALT_FRAME; mRNA.
DR EMBL; AK097336; BAC05002.1; -; mRNA.
DR EMBL; AK290643; BAF83332.1; -; mRNA.
DR EMBL; CR407690; CAG28618.1; -; mRNA.
DR EMBL; AK222507; BAD96227.1; -; mRNA.
DR EMBL; AK222602; BAD96322.1; -; mRNA.
DR EMBL; EF445046; ACA06101.1; -; Genomic_DNA.
DR EMBL; EF445046; ACA06102.1; -; Genomic_DNA.
DR EMBL; AL133415; CAB87963.1; -; Genomic_DNA.
DR EMBL; CH471072; EAW86215.1; -; Genomic_DNA.
DR EMBL; CH471072; EAW86216.1; -; Genomic_DNA.
DR EMBL; BC000163; AAH00163.2; -; mRNA.
DR EMBL; BC030573; AAH30573.1; -; mRNA.
DR EMBL; BC066956; AAH66956.1; -; mRNA.
DR EMBL; X16478; CAA34499.1; -; mRNA.
DR EMBL; M18895; AAA61281.2; -; Genomic_DNA.
DR EMBL; M18888; AAA61281.2; JOINED; Genomic_DNA.
DR EMBL; M18889; AAA61281.2; JOINED; Genomic_DNA.
DR EMBL; M18890; AAA61281.2; JOINED; Genomic_DNA.
DR EMBL; M18891; AAA61281.2; JOINED; Genomic_DNA.
DR EMBL; M18892; AAA61281.2; JOINED; Genomic_DNA.
DR EMBL; M18893; AAA61281.2; JOINED; Genomic_DNA.
DR EMBL; M18894; AAA61281.2; JOINED; Genomic_DNA.
DR EMBL; M25246; AAA61282.1; -; mRNA.
DR PIR; S13115; A25074.
DR RefSeq; NP_003371.2; NM_003380.3.
DR RefSeq; XP_005252636.1; XM_005252579.1.
DR UniGene; Hs.455493; -.
DR UniGene; Hs.691131; -.
DR PDB; 1GK4; X-ray; 2.30 A; A/B/C/D/E/F=328-411.
DR PDB; 1GK6; X-ray; 1.90 A; A/B=385-412.
DR PDB; 1GK7; X-ray; 1.40 A; A=102-138.
DR PDB; 3G1E; X-ray; 1.83 A; A/B=102-138.
DR PDB; 3KLT; X-ray; 2.70 A; A/B/C/D=263-334.
DR PDB; 3S4R; X-ray; 2.45 A; A/B=99-189.
DR PDB; 3SSU; X-ray; 2.60 A; A/B=99-189.
DR PDB; 3SWK; X-ray; 1.70 A; A/B=153-238.
DR PDB; 3TRT; X-ray; 2.30 A; A/B=261-335.
DR PDB; 3UF1; X-ray; 2.81 A; A/B/C/D=144-251.
DR PDBsum; 1GK4; -.
DR PDBsum; 1GK6; -.
DR PDBsum; 1GK7; -.
DR PDBsum; 3G1E; -.
DR PDBsum; 3KLT; -.
DR PDBsum; 3S4R; -.
DR PDBsum; 3SSU; -.
DR PDBsum; 3SWK; -.
DR PDBsum; 3TRT; -.
DR PDBsum; 3UF1; -.
DR ProteinModelPortal; P08670; -.
DR SMR; P08670; 99-248, 263-406.
DR DIP; DIP-32507N; -.
DR IntAct; P08670; 129.
DR MINT; MINT-118802; -.
DR PhosphoSite; P08670; -.
DR DMDM; 55977767; -.
DR DOSAC-COBS-2DPAGE; P08670; -.
DR OGP; P08670; -.
DR REPRODUCTION-2DPAGE; IPI00418471; -.
DR REPRODUCTION-2DPAGE; P08670; -.
DR SWISS-2DPAGE; P08670; -.
DR UCD-2DPAGE; P08670; -.
DR PaxDb; P08670; -.
DR PeptideAtlas; P08670; -.
DR PRIDE; P08670; -.
DR DNASU; 7431; -.
DR Ensembl; ENST00000224237; ENSP00000224237; ENSG00000026025.
DR Ensembl; ENST00000544301; ENSP00000446007; ENSG00000026025.
DR GeneID; 7431; -.
DR KEGG; hsa:7431; -.
DR UCSC; uc001iou.2; human.
DR CTD; 7431; -.
DR GeneCards; GC10P017270; -.
DR H-InvDB; HIX0035657; -.
DR HGNC; HGNC:12692; VIM.
DR HPA; CAB000080; -.
DR HPA; CAB058687; -.
DR HPA; HPA001762; -.
DR MIM; 116300; phenotype.
DR MIM; 193060; gene.
DR neXtProt; NX_P08670; -.
DR Orphanet; 98984; Pulverulent cataract.
DR PharmGKB; PA37311; -.
DR eggNOG; NOG146769; -.
DR HOVERGEN; HBG013015; -.
DR InParanoid; P08670; -.
DR KO; K07606; -.
DR OMA; MQSFRQD; -.
DR OrthoDB; EOG7FV3Q8; -.
DR PhylomeDB; P08670; -.
DR Reactome; REACT_17044; Muscle contraction.
DR Reactome; REACT_578; Apoptosis.
DR ChiTaRS; VIM; human.
DR EvolutionaryTrace; P08670; -.
DR GeneWiki; Vimentin; -.
DR GenomeRNAi; 7431; -.
DR NextBio; 29104; -.
DR PMAP-CutDB; P08670; -.
DR PRO; PR:P08670; -.
DR ArrayExpress; P08670; -.
DR Bgee; P08670; -.
DR Genevestigator; P08670; -.
DR GO; GO:0031252; C:cell leading edge; IEA:Ensembl.
DR GO; GO:0042995; C:cell projection; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular vesicular exosome; IDA:UniProtKB.
DR GO; GO:0005882; C:intermediate filament; IDA:UniProtKB.
DR GO; GO:0005777; C:peroxisome; IDA:UniProtKB.
DR GO; GO:0003725; F:double-stranded RNA binding; IDA:MGI.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; IDA:UniProtKB.
DR GO; GO:0005212; F:structural constituent of eye lens; IEA:Ensembl.
DR GO; GO:0014002; P:astrocyte development; IEA:Ensembl.
DR GO; GO:0060020; P:Bergmann glial cell differentiation; IEA:Ensembl.
DR GO; GO:0006921; P:cellular component disassembly involved in execution phase of apoptosis; TAS:Reactome.
DR GO; GO:0045109; P:intermediate filament organization; IEA:Ensembl.
DR GO; GO:0070307; P:lens fiber cell development; IEA:Ensembl.
DR GO; GO:0019048; P:modulation by virus of host morphology or physiology; IEA:UniProtKB-KW.
DR GO; GO:0030049; P:muscle filament sliding; TAS:Reactome.
DR GO; GO:0010977; P:negative regulation of neuron projection development; IEA:Ensembl.
DR InterPro; IPR001664; IF.
DR InterPro; IPR006821; Intermed_filament_DNA-bd.
DR InterPro; IPR018039; Intermediate_filament_CS.
DR InterPro; IPR027699; Vimentin.
DR PANTHER; PTHR23239; PTHR23239; 1.
DR PANTHER; PTHR23239:SF27; PTHR23239:SF27; 1.
DR Pfam; PF00038; Filament; 1.
DR Pfam; PF04732; Filament_head; 1.
DR PROSITE; PS00226; IF; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cataract; Coiled coil; Complete proteome;
KW Cytoplasm; Direct protein sequencing; Disease mutation; Glycoprotein;
KW Host-virus interaction; Intermediate filament; Phosphoprotein;
KW Reference proteome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 466 Vimentin.
FT /FTId=PRO_0000063754.
FT REGION 2 95 Head.
FT REGION 96 407 Rod.
FT REGION 96 131 Coil 1A.
FT REGION 132 153 Linker 1.
FT REGION 154 245 Coil 1B.
FT REGION 246 268 Linker 12.
FT REGION 269 407 Coil 2.
FT REGION 408 466 Tail.
FT COILED 96 131
FT COILED 154 245
FT COILED 303 407
FT SITE 351 351 Stutter.
FT MOD_RES 2 2 N-acetylserine.
FT MOD_RES 5 5 Phosphoserine.
FT MOD_RES 7 7 Phosphoserine; by PKA and PKC; alternate.
FT MOD_RES 8 8 Phosphoserine.
FT MOD_RES 9 9 Phosphoserine; by PKC.
FT MOD_RES 10 10 Phosphoserine; by PKC.
FT MOD_RES 20 20 Phosphothreonine.
FT MOD_RES 25 25 Phosphoserine.
FT MOD_RES 26 26 Phosphoserine; by PKC (By similarity).
FT MOD_RES 27 27 Phosphoserine.
FT MOD_RES 29 29 Phosphoserine.
FT MOD_RES 33 33 Phosphothreonine; alternate.
FT MOD_RES 34 34 Phosphoserine; alternate.
FT MOD_RES 38 38 Phosphotyrosine.
FT MOD_RES 39 39 Phosphoserine; by CaMK2, PKA, PKC and
FT ROCK2.
FT MOD_RES 42 42 Phosphoserine; by PKC.
FT MOD_RES 47 47 Phosphoserine.
FT MOD_RES 49 49 Phosphoserine (By similarity).
FT MOD_RES 51 51 Phosphoserine.
FT MOD_RES 53 53 Phosphotyrosine.
FT MOD_RES 55 55 Phosphoserine.
FT MOD_RES 56 56 Phosphoserine; by CDK5 and CDK1.
FT MOD_RES 61 61 Phosphotyrosine.
FT MOD_RES 66 66 Phosphoserine; by PKA and PKC (By
FT similarity).
FT MOD_RES 72 72 Phosphoserine; by AURKB and ROCK2.
FT MOD_RES 73 73 Phosphoserine.
FT MOD_RES 83 83 Phosphoserine.
FT MOD_RES 104 104 N6-acetyllysine.
FT MOD_RES 117 117 Phosphotyrosine.
FT MOD_RES 120 120 N6-acetyllysine.
FT MOD_RES 139 139 N6-acetyllysine.
FT MOD_RES 144 144 Phosphoserine.
FT MOD_RES 214 214 Phosphoserine.
FT MOD_RES 226 226 Phosphoserine.
FT MOD_RES 261 261 Phosphoserine.
FT MOD_RES 266 266 Phosphothreonine.
FT MOD_RES 292 292 N6-acetyllysine.
FT MOD_RES 299 299 Phosphoserine.
FT MOD_RES 373 373 N6-acetyllysine.
FT MOD_RES 402 402 N6-acetyllysine.
FT MOD_RES 409 409 Phosphoserine.
FT MOD_RES 412 412 Phosphoserine.
FT MOD_RES 419 419 Phosphoserine.
FT MOD_RES 420 420 Phosphoserine.
FT MOD_RES 426 426 Phosphothreonine.
FT MOD_RES 430 430 Phosphoserine.
FT MOD_RES 436 436 Phosphothreonine.
FT MOD_RES 445 445 N6-acetyllysine.
FT MOD_RES 446 446 Phosphothreonine.
FT MOD_RES 458 458 Phosphothreonine.
FT MOD_RES 459 459 Phosphoserine.
FT CARBOHYD 7 7 O-linked (GlcNAc); alternate.
FT CARBOHYD 33 33 O-linked (GlcNAc); alternate.
FT CARBOHYD 34 34 O-linked (GlcNAc); alternate.
FT VARIANT 151 151 E -> K (in CTRC30; the mutation increases
FT the proteasome activity in transfected
FT cells; causes also a severe kinetic
FT defect in vimentin assembly both in vitro
FT and in vivo).
FT /FTId=VAR_070100.
FT CONFLICT 39 50 Missing (in Ref. 5; BAB71275).
FT CONFLICT 42 42 S -> D (in Ref. 1; AAA61279).
FT CONFLICT 68 76 Missing (in Ref. 5; BAB71275).
FT CONFLICT 113 113 R -> P (in Ref. 12; CAA34499).
FT CONFLICT 197 197 E -> G (in Ref. 6; CAG28618).
FT CONFLICT 201 201 N -> S (in Ref. 17; AAA61281).
FT CONFLICT 265 265 L -> S (in Ref. 17; AAA61281).
FT CONFLICT 278 278 S -> I (in Ref. 17; AAA61281).
FT CONFLICT 339 339 S -> C (in Ref. 17; AAA61281).
FT CONFLICT 350 350 N -> K (in Ref. 17; AAA61281).
FT CONFLICT 442 442 L -> F (in Ref. 1; AAA61279).
FT HELIX 102 135
FT HELIX 155 207
FT HELIX 210 234
FT TURN 244 248
FT HELIX 266 334
FT HELIX 385 405
SQ SEQUENCE 466 AA; 53652 MW; BAB54026665B015A CRC64;
MSTRSVSSSS YRRMFGGPGT ASRPSSSRSY VTTSTRTYSL GSALRPSTSR SLYASSPGGV
YATRSSAVRL RSSVPGVRLL QDSVDFSLAD AINTEFKNTR TNEKVELQEL NDRFANYIDK
VRFLEQQNKI LLAELEQLKG QGKSRLGDLY EEEMRELRRQ VDQLTNDKAR VEVERDNLAE
DIMRLREKLQ EEMLQREEAE NTLQSFRQDV DNASLARLDL ERKVESLQEE IAFLKKLHEE
EIQELQAQIQ EQHVQIDVDV SKPDLTAALR DVRQQYESVA AKNLQEAEEW YKSKFADLSE
AANRNNDALR QAKQESTEYR RQVQSLTCEV DALKGTNESL ERQMREMEEN FAVEAANYQD
TIGRLQDEIQ NMKEEMARHL REYQDLLNVK MALDIEIATY RKLLEGEESR ISLPLPNFSS
LNLRETNLDS LPLVDTHSKR TLLIKTVETR DGQVINETSQ HHDDLE
//
ID VIME_HUMAN Reviewed; 466 AA.
AC P08670; B0YJC2; D3DRU4; Q15867; Q15868; Q15869; Q548L2; Q6LER9;
read moreAC Q8N850; Q96ML2; Q9NTM3;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 22-JAN-2014, entry version 184.
DE RecName: Full=Vimentin;
GN Name=VIM;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3467175;
RA Ferrari S., Battini R., Kaczmarek L., Rittling S., Calabretta B.,
RA de Riel J.K., Philiponis V., Wei J.-F., Baserga R.;
RT "Coding sequence and growth regulation of the human vimentin gene.";
RL Mol. Cell. Biol. 6:3614-3620(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2251132; DOI=10.1093/nar/18.22.6692;
RA Honore B., Madsen P., Basse B., Andersen A., Walbum E., Celis J.E.,
RA Leffers H.;
RT "Nucleotide sequence of cDNA covering the complete coding part of the
RT human vimentin gene.";
RL Nucleic Acids Res. 18:6692-6692(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Lymphoma;
RX PubMed=14996095; DOI=10.1111/j.1365-2133.2004.05651.x;
RA Hartmann T.B., Thiel D., Dummer R., Schadendorf D., Eichmueller S.;
RT "SEREX identification of new tumour-associated antigens in cutaneous
RT T-cell lymphoma.";
RL Br. J. Dermatol. 150:252-258(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Testis;
RA Zimbelmann R.;
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo, Placenta, and Stomach;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Adipose tissue, and Coronary artery;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG NHLBI resequencing and genotyping service (RS&G;);
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
RA Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
RA Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
RA Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
RA Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
RA Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
RA Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
RA Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
RA Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
RA Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
RA Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
RA Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
RA Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
RA Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
RA Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
RA Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
RA Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
RA Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [11]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Cervix, Placenta, and Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [12]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-135, AND TISSUE SPECIFICITY.
RC TISSUE=Mammary carcinoma;
RX PubMed=2472876;
RA Sommers C.L., Walker-Jones D., Heckford S.E., Worland P.,
RA Valverius E., Clark R., McCormick F., Stampfer M., Abularach S.,
RA Gelmann E.P.;
RT "Vimentin rather than keratin expression in some hormone-independent
RT breast cancer cell lines and in oncogene-transformed mammary
RT epithelial cells.";
RL Cancer Res. 49:4258-4263(1989).
RN [13]
RP PROTEIN SEQUENCE OF 2-11; 87-96; 129-138; 188-195; 223-234; 282-291;
RP 322-333 AND 381-389, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT
RP SER-2, AND MASS SPECTROMETRY.
RC TISSUE=T-cell;
RA Bienvenut W.V., Kanor S., Tissot J.-D., Quadroni M.;
RL Submitted (MAY-2006) to UniProtKB.
RN [14]
RP PROTEIN SEQUENCE OF 5-12; 14-45; 51-64; 72-78; 105-113; 123-143;
RP 159-184; 187-217; 223-236; 271-292; 295-313; 322-390 AND 403-466,
RP PHOSPHORYLATION AT SER-56, AND MASS SPECTROMETRY.
RC TISSUE=Hepatoma;
RA Bienvenut W.V., Fleming J., Leug H.Y.;
RL Submitted (JAN-2010) to UniProtKB.
RN [15]
RP PROTEIN SEQUENCE OF 17-25 AND 55-70.
RC TISSUE=Mammary carcinoma;
RX PubMed=9150946; DOI=10.1002/elps.1150180342;
RA Rasmussen R.K., Ji H., Eddes J.S., Moritz R.L., Reid G.E.,
RA Simpson R.J., Dorow D.S.;
RT "Two-dimensional electrophoretic analysis of human breast carcinoma
RT proteins: mapping of proteins that bind to the SH3 domain of mixed
RT lineage kinase MLK2.";
RL Electrophoresis 18:588-598(1997).
RN [16]
RP PROTEIN SEQUENCE OF 51-64; 79-97; 105-113; 130-139; 146-155; 176-184;
RP 189-207; 223-235; 283-292; 295-304; 322-334; 346-373; 382-401 AND
RP 411-439, AND MASS SPECTROMETRY.
RC TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
RA Lubec G., Vishwanath V., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [17]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 113-466, AND TISSUE SPECIFICITY.
RC TISSUE=Fibroblast;
RX PubMed=3371665; DOI=10.1016/0378-1119(88)90575-6;
RA Perreau J., Lilienbaum A., Vasseur M., Paulin D.;
RT "Nucleotide sequence of the human vimentin gene and regulation of its
RT transcription in tissues and cultured cells.";
RL Gene 62:7-16(1988).
RN [18]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 167-466.
RC TISSUE=Osteosarcoma;
RX PubMed=2323579; DOI=10.1016/0378-1119(90)90295-3;
RA Gupta A.K., Aubin J.E., Waye M.M.Y.;
RT "Isolation of a human vimentin cDNA with a long 3'-noncoding region
RT from a human osteosarcoma cell line (MG-63).";
RL Gene 86:303-304(1990).
RN [19]
RP PHOSPHORYLATION.
RX PubMed=9175763; DOI=10.1006/bbrc.1997.6669;
RA Matsuzawa K., Kosako H., Inagaki N., Shibata H., Mukai H., Ono Y.,
RA Amano M., Kaibuchi K., Matsuura Y., Azuma I., Inagaki M.;
RT "Domain-specific phosphorylation of vimentin and glial fibrillary
RT acidic protein by PKN.";
RL Biochem. Biophys. Res. Commun. 234:621-625(1997).
RN [20]
RP PHOSPHORYLATION AT SER-72.
RX PubMed=12458200; DOI=10.1074/jbc.M210892200;
RA Goto H., Yasui Y., Kawajiri A., Nigg E.A., Terada Y., Tatsuka M.,
RA Nagata K., Inagaki M.;
RT "Aurora-B regulates the cleavage furrow-specific vimentin
RT phosphorylation in the cytokinetic process.";
RL J. Biol. Chem. 278:8526-8530(2003).
RN [21]
RP PHOSPHORYLATION AT SER-5; SER-7; SER-8; SER-9; SER-10; SER-39; SER-42;
RP SER-72; SER-73; SER-420; SER-430; THR-458 AND SER-459, AND MASS
RP SPECTROMETRY.
RX PubMed=14762106; DOI=10.1242/jcs.00906;
RA Eriksson J.E., He T., Trejo-Skalli A.V., Harmala-Brasken A.-S.,
RA Hellman J., Chou Y.-H., Goldman R.D.;
RT "Specific in vivo phosphorylation sites determine the assembly
RT dynamics of vimentin intermediate filaments.";
RL J. Cell Sci. 117:919-932(2004).
RN [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-117, AND MASS
RP SPECTROMETRY.
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer
RT cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [23]
RP INTERACTION WITH HCV CORE PROTEIN.
RX PubMed=15846844; DOI=10.1002/pmic.200401093;
RA Kang S.-M., Shin M.-J., Kim J.-H., Oh J.-W.;
RT "Proteomic profiling of cellular proteins interacting with the
RT hepatitis C virus core protein.";
RL Proteomics 5:2227-2237(2005).
RN [24]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-214 AND SER-412, AND
RP MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [25]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-56, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein
RT phosphorylation analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [26]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-412, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=17924679; DOI=10.1021/pr070152u;
RA Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
RT "Improved titanium dioxide enrichment of phosphopeptides from HeLa
RT cells and high confident phosphopeptide identification by cross-
RT validation of MS/MS and MS/MS/MS spectra.";
RL J. Proteome Res. 6:4150-4162(2007).
RN [27]
RP INTERACTION WITH STK33, AND PHOSPHORYLATION BY STK33.
RX PubMed=18811945; DOI=10.1186/1471-2091-9-25;
RA Brauksiepe B., Mujica A.O., Herrmann H., Schmidt E.R.;
RT "The serine/threonine kinase Stk33 exhibits autophosphorylation and
RT phosphorylates the intermediate filament protein Vimentin.";
RL BMC Biochem. 9:25-25(2008).
RN [28]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
RA Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
RT efficient phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [29]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-412, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [30]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-5; SER-25; SER-34;
RP SER-39; SER-42; SER-51; SER-56; TYR-61; SER-72; SER-73; SER-83;
RP SER-144; SER-409; SER-412 AND SER-459, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [31]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [32]
RP INTERACTION WITH SLC6A4.
RX PubMed=19270731; DOI=10.1371/journal.pone.0004730;
RA Ahmed B.A., Bukhari I.A., Jeffus B.C., Harney J.T., Thyparambil S.,
RA Ziu E., Fraer M., Rusch N.J., Zimniak P., Lupashin V., Tang D.,
RA Kilic F.;
RT "The cellular distribution of serotonin transporter is impeded on
RT serotonin-altered vimentin network.";
RL PLoS ONE 4:E4730-E4730(2009).
RN [33]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51; SER-56 AND TYR-61,
RP AND MASS SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [34]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-120; LYS-139; LYS-373 AND
RP LYS-445, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [35]
RP GLYCOSYLATION AT SER-7; THR-33 AND SER-34.
RX PubMed=20068230; DOI=10.1126/scisignal.2000526;
RA Wang Z., Udeshi N.D., Slawson C., Compton P.D., Sakabe K.,
RA Cheung W.D., Shabanowitz J., Hunt D.F., Hart G.W.;
RT "Extensive crosstalk between O-GlcNAcylation and phosphorylation
RT regulates cytokinesis.";
RL Sci. Signal. 3:RA2-RA2(2010).
RN [36]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-20; SER-42; SER-47;
RP SER-51; SER-56; SER-73; SER-83; SER-144; SER-214; SER-226; SER-299;
RP SER-412; SER-419; SER-420; THR-426; SER-430; THR-436 AND SER-459, AND
RP MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [37]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [38]
RP FUNCTION IN COLLAGEN MRNA STABILIZATION, AND INTERACTION WITH LARP6.
RX PubMed=21746880; DOI=10.1128/MCB.05263-11;
RA Challa A.A., Stefanovic B.;
RT "A novel role of vimentin filaments: binding and stabilization of
RT collagen mRNAs.";
RL Mol. Cell. Biol. 31:3773-3789(2011).
RN [39]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51; SER-144 AND SER-459,
RP AND MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [40]
RP PHOSPHORYLATION AT SER-56, AND SUBCELLULAR LOCATION.
RX PubMed=21465480; DOI=10.1002/jcp.22782;
RA Lee K.Y., Liu L., Jin Y., Fu S.B., Rosales J.L.;
RT "Cdk5 mediates vimentin Ser56 phosphorylation during GTP-induced
RT secretion by neutrophils.";
RL J. Cell. Physiol. 227:739-750(2012).
RN [41]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [42]
RP X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 102-138.
RX PubMed=11243787; DOI=10.1006/jmbi.2001.4442;
RA Strelkov S.V., Herrmann H., Geisler N., Lustig A., Ivaninskii S.,
RA Zimbelmann R., Burkhard P., Aebi U.;
RT "Divide-and-conquer crystallographic approach towards an atomic
RT structure of intermediate filaments.";
RL J. Mol. Biol. 306:773-781(2001).
RN [43]
RP X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 103-139 AND 328-411.
RX PubMed=11889032; DOI=10.1093/emboj/21.6.1255;
RA Strelkov S.V., Herrmann H., Geisler N., Wedig T., Zimbelmann R.,
RA Aebi U., Burkhard P.;
RT "Conserved segments 1A and 2B of the intermediate filament dimer:
RT their atomic structures and role in filament assembly.";
RL EMBO J. 21:1255-1266(2002).
RN [44]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 263-334, COILED-COIL DOMAINS,
RP AND SUBUNIT.
RX PubMed=20176112; DOI=10.1016/j.jsb.2010.02.012;
RA Nicolet S., Herrmann H., Aebi U., Strelkov S.V.;
RT "Atomic structure of vimentin coil 2.";
RL J. Struct. Biol. 170:369-376(2010).
RN [45]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 261-335 OF MUTANT CYS-265.
RX PubMed=22119849; DOI=10.1016/j.jsb.2011.11.014;
RA Chernyatina A.A., Strelkov S.V.;
RT "Stabilization of vimentin coil2 fragment via an engineered
RT disulfide.";
RL J. Struct. Biol. 177:46-53(2012).
RN [46]
RP VARIANT CTRC30 LYS-151, AND CHARACTERIZATION OF VARIANT CTRC30
RP LYS-151.
RX PubMed=19126778; DOI=10.1093/hmg/ddn440;
RA Muller M., Bhattacharya S.S., Moore T., Prescott Q., Wedig T.,
RA Herrmann H., Magin T.M.;
RT "Dominant cataract formation in association with a vimentin assembly
RT disrupting mutation.";
RL Hum. Mol. Genet. 18:1052-1057(2009).
CC -!- FUNCTION: Vimentins are class-III intermediate filaments found in
CC various non-epithelial cells, especially mesenchymal cells.
CC Vimentin is attached to the nucleus, endoplasmic reticulum, and
CC mitochondria, either laterally or terminally.
CC -!- FUNCTION: Involved with LARP6 in the stabilization of type I
CC collagen mRNAs for CO1A1 and CO1A2.
CC -!- SUBUNIT: Homopolymer assembled from elementary dimers. Interacts
CC with HCV core protein. Interacts with LGSN and SYNM. Interacts
CC (via rod region) with PLEC (via CH 1 domain) (By similarity).
CC Interacts with SLC6A4. Interacts with STK33. Interacts with LARP6.
CC Interacts with RAB8B (By similarity).
CC -!- INTERACTION:
CC Self; NbExp=6; IntAct=EBI-353844, EBI-353844;
CC P31749:AKT1; NbExp=29; IntAct=EBI-353844, EBI-296087;
CC P31751:AKT2; NbExp=6; IntAct=EBI-353844, EBI-296058;
CC Q9H6U6:BCAS3; NbExp=3; IntAct=EBI-353844, EBI-6083685;
CC Q14194:CRMP1; NbExp=3; IntAct=EBI-353844, EBI-473101;
CC O95251:KAT7; NbExp=4; IntAct=EBI-353844, EBI-473199;
CC P54727:RAD23B; NbExp=2; IntAct=EBI-353844, EBI-954531;
CC O95361:TRIM16; NbExp=3; IntAct=EBI-353844, EBI-727384;
CC P63104:YWHAZ; NbExp=2; IntAct=EBI-353844, EBI-347088;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- TISSUE SPECIFICITY: Highly expressed in fibroblasts, some
CC expression in T- and B-lymphocytes, and little or no expression in
CC Burkitt's lymphoma cell lines. Expressed in many hormone-
CC independent mammary carcinoma cell lines.
CC -!- DOMAIN: The central alpha-helical coiled-coil rod region mediates
CC elementary homodimerization.
CC -!- PTM: Filament disassembly during mitosis is promoted by
CC phosphorylation at Ser-55 as well as by nestin (By similarity).
CC One of the most prominent phosphoproteins in various cells of
CC mesenchymal origin. Phosphorylation is enhanced during cell
CC division, at which time vimentin filaments are significantly
CC reorganized. Phosphorylation by PKN1 inhibits the formation of
CC filaments. Phosphorylated at Ser-56 by CDK5 during neutrophil
CC secretion in the cytoplasm. Phosphorylated by STK33.
CC -!- PTM: O-glycosylated during cytokinesis at sites identical or close
CC to phosphorylation sites, this interferes with the phosphorylation
CC status.
CC -!- DISEASE: Cataract 30 (CTRCT30) [MIM:116300]: An opacification of
CC the crystalline lens of the eye that frequently results in visual
CC impairment or blindness. Opacities vary in morphology, are often
CC confined to a portion of the lens, and may be static or
CC progressive. In general, the more posteriorly located and dense an
CC opacity, the greater the impact on visual function. Note=The
CC disease is caused by mutations affecting the gene represented in
CC this entry.
CC -!- SIMILARITY: Belongs to the intermediate filament family.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB71275.1; Type=Miscellaneous discrepancy; Note=Intron retention;
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Vimentin entry;
CC URL="http://en.wikipedia.org/wiki/Vimentin";
CC -----------------------------------------------------------------------
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DR EMBL; M14144; AAA61279.1; -; Genomic_DNA.
DR EMBL; X56134; CAA39600.1; -; mRNA.
DR EMBL; AF328728; AAN09720.1; -; mRNA.
DR EMBL; Z19554; CAA79613.2; -; mRNA.
DR EMBL; AK056766; BAB71275.1; ALT_FRAME; mRNA.
DR EMBL; AK097336; BAC05002.1; -; mRNA.
DR EMBL; AK290643; BAF83332.1; -; mRNA.
DR EMBL; CR407690; CAG28618.1; -; mRNA.
DR EMBL; AK222507; BAD96227.1; -; mRNA.
DR EMBL; AK222602; BAD96322.1; -; mRNA.
DR EMBL; EF445046; ACA06101.1; -; Genomic_DNA.
DR EMBL; EF445046; ACA06102.1; -; Genomic_DNA.
DR EMBL; AL133415; CAB87963.1; -; Genomic_DNA.
DR EMBL; CH471072; EAW86215.1; -; Genomic_DNA.
DR EMBL; CH471072; EAW86216.1; -; Genomic_DNA.
DR EMBL; BC000163; AAH00163.2; -; mRNA.
DR EMBL; BC030573; AAH30573.1; -; mRNA.
DR EMBL; BC066956; AAH66956.1; -; mRNA.
DR EMBL; X16478; CAA34499.1; -; mRNA.
DR EMBL; M18895; AAA61281.2; -; Genomic_DNA.
DR EMBL; M18888; AAA61281.2; JOINED; Genomic_DNA.
DR EMBL; M18889; AAA61281.2; JOINED; Genomic_DNA.
DR EMBL; M18890; AAA61281.2; JOINED; Genomic_DNA.
DR EMBL; M18891; AAA61281.2; JOINED; Genomic_DNA.
DR EMBL; M18892; AAA61281.2; JOINED; Genomic_DNA.
DR EMBL; M18893; AAA61281.2; JOINED; Genomic_DNA.
DR EMBL; M18894; AAA61281.2; JOINED; Genomic_DNA.
DR EMBL; M25246; AAA61282.1; -; mRNA.
DR PIR; S13115; A25074.
DR RefSeq; NP_003371.2; NM_003380.3.
DR RefSeq; XP_005252636.1; XM_005252579.1.
DR UniGene; Hs.455493; -.
DR UniGene; Hs.691131; -.
DR PDB; 1GK4; X-ray; 2.30 A; A/B/C/D/E/F=328-411.
DR PDB; 1GK6; X-ray; 1.90 A; A/B=385-412.
DR PDB; 1GK7; X-ray; 1.40 A; A=102-138.
DR PDB; 3G1E; X-ray; 1.83 A; A/B=102-138.
DR PDB; 3KLT; X-ray; 2.70 A; A/B/C/D=263-334.
DR PDB; 3S4R; X-ray; 2.45 A; A/B=99-189.
DR PDB; 3SSU; X-ray; 2.60 A; A/B=99-189.
DR PDB; 3SWK; X-ray; 1.70 A; A/B=153-238.
DR PDB; 3TRT; X-ray; 2.30 A; A/B=261-335.
DR PDB; 3UF1; X-ray; 2.81 A; A/B/C/D=144-251.
DR PDBsum; 1GK4; -.
DR PDBsum; 1GK6; -.
DR PDBsum; 1GK7; -.
DR PDBsum; 3G1E; -.
DR PDBsum; 3KLT; -.
DR PDBsum; 3S4R; -.
DR PDBsum; 3SSU; -.
DR PDBsum; 3SWK; -.
DR PDBsum; 3TRT; -.
DR PDBsum; 3UF1; -.
DR ProteinModelPortal; P08670; -.
DR SMR; P08670; 99-248, 263-406.
DR DIP; DIP-32507N; -.
DR IntAct; P08670; 129.
DR MINT; MINT-118802; -.
DR PhosphoSite; P08670; -.
DR DMDM; 55977767; -.
DR DOSAC-COBS-2DPAGE; P08670; -.
DR OGP; P08670; -.
DR REPRODUCTION-2DPAGE; IPI00418471; -.
DR REPRODUCTION-2DPAGE; P08670; -.
DR SWISS-2DPAGE; P08670; -.
DR UCD-2DPAGE; P08670; -.
DR PaxDb; P08670; -.
DR PeptideAtlas; P08670; -.
DR PRIDE; P08670; -.
DR DNASU; 7431; -.
DR Ensembl; ENST00000224237; ENSP00000224237; ENSG00000026025.
DR Ensembl; ENST00000544301; ENSP00000446007; ENSG00000026025.
DR GeneID; 7431; -.
DR KEGG; hsa:7431; -.
DR UCSC; uc001iou.2; human.
DR CTD; 7431; -.
DR GeneCards; GC10P017270; -.
DR H-InvDB; HIX0035657; -.
DR HGNC; HGNC:12692; VIM.
DR HPA; CAB000080; -.
DR HPA; CAB058687; -.
DR HPA; HPA001762; -.
DR MIM; 116300; phenotype.
DR MIM; 193060; gene.
DR neXtProt; NX_P08670; -.
DR Orphanet; 98984; Pulverulent cataract.
DR PharmGKB; PA37311; -.
DR eggNOG; NOG146769; -.
DR HOVERGEN; HBG013015; -.
DR InParanoid; P08670; -.
DR KO; K07606; -.
DR OMA; MQSFRQD; -.
DR OrthoDB; EOG7FV3Q8; -.
DR PhylomeDB; P08670; -.
DR Reactome; REACT_17044; Muscle contraction.
DR Reactome; REACT_578; Apoptosis.
DR ChiTaRS; VIM; human.
DR EvolutionaryTrace; P08670; -.
DR GeneWiki; Vimentin; -.
DR GenomeRNAi; 7431; -.
DR NextBio; 29104; -.
DR PMAP-CutDB; P08670; -.
DR PRO; PR:P08670; -.
DR ArrayExpress; P08670; -.
DR Bgee; P08670; -.
DR Genevestigator; P08670; -.
DR GO; GO:0031252; C:cell leading edge; IEA:Ensembl.
DR GO; GO:0042995; C:cell projection; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular vesicular exosome; IDA:UniProtKB.
DR GO; GO:0005882; C:intermediate filament; IDA:UniProtKB.
DR GO; GO:0005777; C:peroxisome; IDA:UniProtKB.
DR GO; GO:0003725; F:double-stranded RNA binding; IDA:MGI.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; IDA:UniProtKB.
DR GO; GO:0005212; F:structural constituent of eye lens; IEA:Ensembl.
DR GO; GO:0014002; P:astrocyte development; IEA:Ensembl.
DR GO; GO:0060020; P:Bergmann glial cell differentiation; IEA:Ensembl.
DR GO; GO:0006921; P:cellular component disassembly involved in execution phase of apoptosis; TAS:Reactome.
DR GO; GO:0045109; P:intermediate filament organization; IEA:Ensembl.
DR GO; GO:0070307; P:lens fiber cell development; IEA:Ensembl.
DR GO; GO:0019048; P:modulation by virus of host morphology or physiology; IEA:UniProtKB-KW.
DR GO; GO:0030049; P:muscle filament sliding; TAS:Reactome.
DR GO; GO:0010977; P:negative regulation of neuron projection development; IEA:Ensembl.
DR InterPro; IPR001664; IF.
DR InterPro; IPR006821; Intermed_filament_DNA-bd.
DR InterPro; IPR018039; Intermediate_filament_CS.
DR InterPro; IPR027699; Vimentin.
DR PANTHER; PTHR23239; PTHR23239; 1.
DR PANTHER; PTHR23239:SF27; PTHR23239:SF27; 1.
DR Pfam; PF00038; Filament; 1.
DR Pfam; PF04732; Filament_head; 1.
DR PROSITE; PS00226; IF; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cataract; Coiled coil; Complete proteome;
KW Cytoplasm; Direct protein sequencing; Disease mutation; Glycoprotein;
KW Host-virus interaction; Intermediate filament; Phosphoprotein;
KW Reference proteome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 466 Vimentin.
FT /FTId=PRO_0000063754.
FT REGION 2 95 Head.
FT REGION 96 407 Rod.
FT REGION 96 131 Coil 1A.
FT REGION 132 153 Linker 1.
FT REGION 154 245 Coil 1B.
FT REGION 246 268 Linker 12.
FT REGION 269 407 Coil 2.
FT REGION 408 466 Tail.
FT COILED 96 131
FT COILED 154 245
FT COILED 303 407
FT SITE 351 351 Stutter.
FT MOD_RES 2 2 N-acetylserine.
FT MOD_RES 5 5 Phosphoserine.
FT MOD_RES 7 7 Phosphoserine; by PKA and PKC; alternate.
FT MOD_RES 8 8 Phosphoserine.
FT MOD_RES 9 9 Phosphoserine; by PKC.
FT MOD_RES 10 10 Phosphoserine; by PKC.
FT MOD_RES 20 20 Phosphothreonine.
FT MOD_RES 25 25 Phosphoserine.
FT MOD_RES 26 26 Phosphoserine; by PKC (By similarity).
FT MOD_RES 27 27 Phosphoserine.
FT MOD_RES 29 29 Phosphoserine.
FT MOD_RES 33 33 Phosphothreonine; alternate.
FT MOD_RES 34 34 Phosphoserine; alternate.
FT MOD_RES 38 38 Phosphotyrosine.
FT MOD_RES 39 39 Phosphoserine; by CaMK2, PKA, PKC and
FT ROCK2.
FT MOD_RES 42 42 Phosphoserine; by PKC.
FT MOD_RES 47 47 Phosphoserine.
FT MOD_RES 49 49 Phosphoserine (By similarity).
FT MOD_RES 51 51 Phosphoserine.
FT MOD_RES 53 53 Phosphotyrosine.
FT MOD_RES 55 55 Phosphoserine.
FT MOD_RES 56 56 Phosphoserine; by CDK5 and CDK1.
FT MOD_RES 61 61 Phosphotyrosine.
FT MOD_RES 66 66 Phosphoserine; by PKA and PKC (By
FT similarity).
FT MOD_RES 72 72 Phosphoserine; by AURKB and ROCK2.
FT MOD_RES 73 73 Phosphoserine.
FT MOD_RES 83 83 Phosphoserine.
FT MOD_RES 104 104 N6-acetyllysine.
FT MOD_RES 117 117 Phosphotyrosine.
FT MOD_RES 120 120 N6-acetyllysine.
FT MOD_RES 139 139 N6-acetyllysine.
FT MOD_RES 144 144 Phosphoserine.
FT MOD_RES 214 214 Phosphoserine.
FT MOD_RES 226 226 Phosphoserine.
FT MOD_RES 261 261 Phosphoserine.
FT MOD_RES 266 266 Phosphothreonine.
FT MOD_RES 292 292 N6-acetyllysine.
FT MOD_RES 299 299 Phosphoserine.
FT MOD_RES 373 373 N6-acetyllysine.
FT MOD_RES 402 402 N6-acetyllysine.
FT MOD_RES 409 409 Phosphoserine.
FT MOD_RES 412 412 Phosphoserine.
FT MOD_RES 419 419 Phosphoserine.
FT MOD_RES 420 420 Phosphoserine.
FT MOD_RES 426 426 Phosphothreonine.
FT MOD_RES 430 430 Phosphoserine.
FT MOD_RES 436 436 Phosphothreonine.
FT MOD_RES 445 445 N6-acetyllysine.
FT MOD_RES 446 446 Phosphothreonine.
FT MOD_RES 458 458 Phosphothreonine.
FT MOD_RES 459 459 Phosphoserine.
FT CARBOHYD 7 7 O-linked (GlcNAc); alternate.
FT CARBOHYD 33 33 O-linked (GlcNAc); alternate.
FT CARBOHYD 34 34 O-linked (GlcNAc); alternate.
FT VARIANT 151 151 E -> K (in CTRC30; the mutation increases
FT the proteasome activity in transfected
FT cells; causes also a severe kinetic
FT defect in vimentin assembly both in vitro
FT and in vivo).
FT /FTId=VAR_070100.
FT CONFLICT 39 50 Missing (in Ref. 5; BAB71275).
FT CONFLICT 42 42 S -> D (in Ref. 1; AAA61279).
FT CONFLICT 68 76 Missing (in Ref. 5; BAB71275).
FT CONFLICT 113 113 R -> P (in Ref. 12; CAA34499).
FT CONFLICT 197 197 E -> G (in Ref. 6; CAG28618).
FT CONFLICT 201 201 N -> S (in Ref. 17; AAA61281).
FT CONFLICT 265 265 L -> S (in Ref. 17; AAA61281).
FT CONFLICT 278 278 S -> I (in Ref. 17; AAA61281).
FT CONFLICT 339 339 S -> C (in Ref. 17; AAA61281).
FT CONFLICT 350 350 N -> K (in Ref. 17; AAA61281).
FT CONFLICT 442 442 L -> F (in Ref. 1; AAA61279).
FT HELIX 102 135
FT HELIX 155 207
FT HELIX 210 234
FT TURN 244 248
FT HELIX 266 334
FT HELIX 385 405
SQ SEQUENCE 466 AA; 53652 MW; BAB54026665B015A CRC64;
MSTRSVSSSS YRRMFGGPGT ASRPSSSRSY VTTSTRTYSL GSALRPSTSR SLYASSPGGV
YATRSSAVRL RSSVPGVRLL QDSVDFSLAD AINTEFKNTR TNEKVELQEL NDRFANYIDK
VRFLEQQNKI LLAELEQLKG QGKSRLGDLY EEEMRELRRQ VDQLTNDKAR VEVERDNLAE
DIMRLREKLQ EEMLQREEAE NTLQSFRQDV DNASLARLDL ERKVESLQEE IAFLKKLHEE
EIQELQAQIQ EQHVQIDVDV SKPDLTAALR DVRQQYESVA AKNLQEAEEW YKSKFADLSE
AANRNNDALR QAKQESTEYR RQVQSLTCEV DALKGTNESL ERQMREMEEN FAVEAANYQD
TIGRLQDEIQ NMKEEMARHL REYQDLLNVK MALDIEIATY RKLLEGEESR ISLPLPNFSS
LNLRETNLDS LPLVDTHSKR TLLIKTVETR DGQVINETSQ HHDDLE
//
MIM
116300
*RECORD*
*FIELD* NO
116300
*FIELD* TI
#116300 CATARACT 30; CTRCT30
;;CATARACT 30, PULVERULENT
*FIELD* TX
A number sign (#) is used with this entry because of evidence that
read morecataract-30 is caused by heterozygous mutation in the VIM gene (193060)
on chromosome 10p13.
CLINICAL FEATURES
Muller et al. (2009) screened 90 patients suffering from various types
of cataract for mutations in the VIM gene. They identified a mutation
(see MOLECULAR GENETICS) in only 1 patient, a 45-year-old female with
pulverulent (dust-like) opacities.
INHERITANCE
The transmission pattern in the family with cataracts described by
Muller et al. (2009) was consistent with autosomal dominant inheritance.
MOLECULAR GENETICS
In a 45-year-old woman with pulverulent cataracts, Muller et al. (2009)
identified a heterozygous missense mutation (E151K) in the VIM gene
(193060.0001). The patient's mother also had cataracts. The mutation was
not found in 192 healthy control individuals.
*FIELD* RF
1. Muller, M.; Bhattacharya, S. S.; Moore, T.; Prescott, Q.; Wedig,
T.; Herrmann, H.; Magin, T. M.: Dominant cataract formation in association
with a vimentin assembly disrupting mutation. Hum. Molec. Genet. 18:
1052-1057, 2009.
*FIELD* CS
Eyes:
Cataract, nuclear diffuse nonprogressive
Inheritance:
Autosomal dominant
*FIELD* CD
Victor A. McKusick: 6/4/1986
*FIELD* ED
carol: 07/19/2013
alopez: 3/18/2004
mimadm: 6/25/1994
supermim: 3/16/1992
supermim: 3/20/1990
ddp: 10/26/1989
marie: 3/25/1988
reenie: 10/17/1986
*RECORD*
*FIELD* NO
116300
*FIELD* TI
#116300 CATARACT 30; CTRCT30
;;CATARACT 30, PULVERULENT
*FIELD* TX
A number sign (#) is used with this entry because of evidence that
read morecataract-30 is caused by heterozygous mutation in the VIM gene (193060)
on chromosome 10p13.
CLINICAL FEATURES
Muller et al. (2009) screened 90 patients suffering from various types
of cataract for mutations in the VIM gene. They identified a mutation
(see MOLECULAR GENETICS) in only 1 patient, a 45-year-old female with
pulverulent (dust-like) opacities.
INHERITANCE
The transmission pattern in the family with cataracts described by
Muller et al. (2009) was consistent with autosomal dominant inheritance.
MOLECULAR GENETICS
In a 45-year-old woman with pulverulent cataracts, Muller et al. (2009)
identified a heterozygous missense mutation (E151K) in the VIM gene
(193060.0001). The patient's mother also had cataracts. The mutation was
not found in 192 healthy control individuals.
*FIELD* RF
1. Muller, M.; Bhattacharya, S. S.; Moore, T.; Prescott, Q.; Wedig,
T.; Herrmann, H.; Magin, T. M.: Dominant cataract formation in association
with a vimentin assembly disrupting mutation. Hum. Molec. Genet. 18:
1052-1057, 2009.
*FIELD* CS
Eyes:
Cataract, nuclear diffuse nonprogressive
Inheritance:
Autosomal dominant
*FIELD* CD
Victor A. McKusick: 6/4/1986
*FIELD* ED
carol: 07/19/2013
alopez: 3/18/2004
mimadm: 6/25/1994
supermim: 3/16/1992
supermim: 3/20/1990
ddp: 10/26/1989
marie: 3/25/1988
reenie: 10/17/1986
MIM
193060
*RECORD*
*FIELD* NO
193060
*FIELD* TI
*193060 VIMENTIN; VIM
*FIELD* TX
DESCRIPTION
Along with the microfilaments (actins) and microtubules (tubulins), the
read moreintermediate filaments represent a third class of well-characterized
cytoskeletal elements. The subunits display a tissue-specific pattern of
expression. Desmin (125660) is the subunit specific for muscle and
vimentin the subunit specific for mesenchymal tissue.
CLONING
By use of a genomic clone and several recombinant cDNA clones, Perreau
et al. (1988) determined the complete nucleotide sequence of the coding
region. Ninety percent homology was demonstrated between the hamster and
human genes at the nucleotide level. A single 2-kb mRNA species was
observed in a study of mRNA from multiple different mammalian species.
The 3-prime nontranslated region includes 2 canonic polyadenylation
signals. Marcus et al. (1988) identified a BclI RFLP in the VIM gene.
The VIM gene was one of many that Gieser and Swaroop (1992) recovered
from a subtracted cDNA library for retinal pigment epithelium. To
identify candidate genes for inherited eye diseases, they prepared
expressed sequence tags (ESTs) and in each instance compared the EST
with published DNA sequences. Using PCR-based EST assays, they assigned
to specific human chromosomes eight of the cDNAs for which the EST did
not match.
GENE FUNCTION
Zhang et al. (2003) demonstrated that SP1 (189906) activated
transcription from the vimentin promoter. Through N-terminal zinc
fingers, ZBP89 (ZNF148; 601897) repressed SP1-mediated activation.
Although vimentin has been presumed to be important for stabilizing the
architecture of the cytoplasm, Mor-Vaknin et al. (2003) found that
monocyte-derived macrophages secrete vimentin into the extracellular
space in vitro. Secretion of vimentin was enhanced by the
proinflammatory cytokine tumor necrosis factor-alpha (TNFA; 191160) and
inhibited by the antiinflammatory cytokine IL10 (124092), suggesting
that vimentin is involved in the immune response. Mor-Vaknin et al.
(2003) noted that vimentin likely has specialized functions that
contribute to specific dynamic cellular processes.
Wang et al. (2012) showed that beclin-1 (604378), an essential autophagy
and tumor suppressor protein, is a target of the protein kinase AKT
(164730). Expression of a beclin-1 mutant resistant to Akt-mediated
phosphorylation increased autophagy, reduced anchorage-independent
growth, and inhibited Akt-driven tumorigenesis. Akt-mediated
phosphorylation of beclin-1 enhanced its interactions with 14-3-3 (see
605066) and vimentin intermediate filament proteins, and vimentin
depletion increased autophagy and inhibited Akt-driven transformation.
Thus, Wang et al. (2012) concluded that Akt-mediated phosphorylation of
beclin-1 functions in autophagy inhibition, oncogenesis, and the
formation of an autophagy-inhibitory beclin-1/14-3-3/vimentin
intermediate filament complex, and suggested that their findings have
broad implications for understanding the role of Akt signaling and
intermediate filament proteins in autophagy and cancer.
MAPPING
Using cDNA clones of the VIM gene prepared from hamster lens mRNA, Quax
et al. (1985) demonstrated that a single-copy gene encodes vimentin in
man and that in man-rodent hybrid cells the gene segregates with human
chromosome 10. Ferrari et al. (1987) showed by Southern blot analysis of
DNA from somatic cell hybrids and by in situ chromosome hybridization
that there is only 1 copy of the VIM gene, which is located on 10p13,
close to IL2R (147730). Mathew et al. (1990) assigned the vimentin gene
to 10p by linkage analysis.
MOLECULAR GENETICS
Muller et al. (2009) screened 90 patients suffering from various types
of cataract for mutations in the VIM gene. They identified
heterozygosity for a mutation (193060.0001) in only 1 patient, a
45-year-old female with pulverulent (dust-like) cataracts (CTRCT30;
116300). The patient's mother also had cataracts.
ANIMAL MODEL
Colucci-Guyon et al. (1994) introduced a null mutation of the vimentin
gene into the germline of mice. Surprisingly, animals homozygous for
this mutation developed and reproduced without an obvious deviant
phenotype. Immunoblotting, immunofluorescence, and immunogold labeling
analyses confirmed the absence of vimentin and of the corresponding
filament network. Furthermore, no compensatory expression of another
intermediate filament could be demonstrated. The results leave open the
question of a possible role of vimentin in unusual situations or
pathologic conditions.
*FIELD* AV
.0001
CATARACT 30, PULVERULENT
VIM, GLU151LYS
In a 45-year-old female with pulverulent cataract (CTRCT30; 116300),
Muller et al. (2009) identified a heterozygous 596G-A transition in exon
1 of the VIM gene, resulting in a glu151-to-lys (E151K) substitution in
coil 1B of the protein. The mutation was not found in 192 healthy
control individuals. Glu151 is a highly conserved residue. The mutant
protein formed an aberrant vimentin cytoskeleton and increased the
proteasome activity in transfected cells. The mutation caused a severe
kinetic defect in vimentin assembly both in vitro and in vivo.
*FIELD* SA
Ferrari et al. (1986); Lilienbaum et al. (1986)
*FIELD* RF
1. Colucci-Guyon, E.; Portier, M.-M.; Dunia, I.; Paulin, D.; Pournin,
S.; Babinet, C.: Mice lacking vimentin develop and reproduce without
an obvious phenotype. Cell 79: 679-694, 1994.
2. Ferrari, S.; Battini, R.; Kaczmarek, L.; Rittling, S.; Calabretta,
B.; de Riel, J. K.; Philiponis, V.; Weil, J.-F.; Baserga, R.: Coding
sequence and growth regulation of the human vimentin gene. Molec.
Cell. Biol. 6: 3614-3620, 1986.
3. Ferrari, S.; Cannizzaro, L. A.; Battini, R.; Huebner, K.; Baserga,
R.: The gene encoding human vimentin is located on the short arm
of chromosome 10. Am. J. Hum. Genet. 41: 616-626, 1987.
4. Gieser, L.; Swaroop, A.: Expressed sequence tags and chromosomal
localization of cDNA clones from a subtracted retinal pigment epithelium
library. Genomics 13: 873-876, 1992.
5. Lilienbaum, A.; Legagneux, V.; Portier, M.-M.; Dellagi, K.; Paulin,
D.: Vimentin gene: expression in human lymphocytes and in Burkitt's
lymphoma cells. EMBO J. 5: 2809-2814, 1986.
6. Marcus, E. M.; Smith, B. A.; Telenius, H.; Landsvater, R. M.; Buys,
C. H. C. M.; Ferrari, S.; Ponder, B. A. J.; Mathew, C. G. P.: BclI
RFLP for the human vimentin gene. Nucleic Acids Res. 16: 9068 only,
1988.
7. Mathew, C. G.; Wakeling, W.; Jones, E.; Easton, D.; Fisher, R.;
Strong, C.; Smith, B.; Chin, K.; Little, P.; Nakamura, Y.; Shows,
T. B.; Jones, C.; Goodfellow, P. J.; Povey, S.; Ponder, B. A. J.:
Regional localization of polymorphic markers on chromosome 10 by physical
and genetic mapping. Ann. Hum. Genet. 54: 121-129, 1990.
8. Mor-Vaknin, N.; Punturieri, A.; Sitwala, K.; Markovitz, D. M.:
Vimentin is secreted by activated macrophages. Nature Cell Biol. 5:
59-63, 2003.
9. Muller, M.; Bhattacharya, S. S.; Moore, T.; Prescott, Q.; Wedig,
T.; Herrmann, H.; Magin, T. M.: Dominant cataract formation in association
with a vimentin assembly disrupting mutation. Hum. Molec. Genet. 18:
1052-1057, 2009.
10. Perreau, J.; Lilienbaum, A.; Vasseur, M.; Paulin, D.: Nucleotide
sequence of the human vimentin gene and regulation of its transcription
in tissues and cultured cells. Gene 62: 7-16, 1988.
11. Quax, W.; Meera Khan, P.; Quax-Jeuken, Y.; Bloemendal, H.: The
human desmin and vimentin genes are located on different chromosomes. Gene 38:
189-196, 1985.
12. Wang, R. C.; Wei, Y.; An, Z.; Zou, Z.; Xiao, G.; Bhagat, G.; White,
M.; Reichelt, J.; Levine, B.: Akt-mediated regulation of autophagy
and tumorigenesis through beclin 1 phosphorylation. Science 338:
956-959, 2012.
13. Zhang, X.; Diab, I. H.; Zehner, Z. E.: ZBP-89 represses vimentin
gene transcription by interacting with the transcriptional activator,
Sp1. Nucleic Acids Res. 31: 2900-2914, 2003.
*FIELD* CN
Ada Hamosh - updated: 1/7/2013
George E. Tiller - updated: 10/14/2009
Cassandra L. Kniffin - updated: 3/29/2004
Patricia A. Hartz - updated: 10/27/2003
*FIELD* CD
Victor A. McKusick: 6/2/1986
*FIELD* ED
carol: 07/19/2013
alopez: 1/7/2013
terry: 1/7/2013
carol: 10/14/2009
ckniffin: 4/1/2004
tkritzer: 3/31/2004
ckniffin: 3/29/2004
cwells: 11/3/2003
terry: 10/27/2003
dkim: 12/15/1998
carol: 12/7/1994
carol: 7/21/1992
supermim: 3/16/1992
carol: 3/21/1991
carol: 3/20/1991
supermim: 3/20/1990
*RECORD*
*FIELD* NO
193060
*FIELD* TI
*193060 VIMENTIN; VIM
*FIELD* TX
DESCRIPTION
Along with the microfilaments (actins) and microtubules (tubulins), the
read moreintermediate filaments represent a third class of well-characterized
cytoskeletal elements. The subunits display a tissue-specific pattern of
expression. Desmin (125660) is the subunit specific for muscle and
vimentin the subunit specific for mesenchymal tissue.
CLONING
By use of a genomic clone and several recombinant cDNA clones, Perreau
et al. (1988) determined the complete nucleotide sequence of the coding
region. Ninety percent homology was demonstrated between the hamster and
human genes at the nucleotide level. A single 2-kb mRNA species was
observed in a study of mRNA from multiple different mammalian species.
The 3-prime nontranslated region includes 2 canonic polyadenylation
signals. Marcus et al. (1988) identified a BclI RFLP in the VIM gene.
The VIM gene was one of many that Gieser and Swaroop (1992) recovered
from a subtracted cDNA library for retinal pigment epithelium. To
identify candidate genes for inherited eye diseases, they prepared
expressed sequence tags (ESTs) and in each instance compared the EST
with published DNA sequences. Using PCR-based EST assays, they assigned
to specific human chromosomes eight of the cDNAs for which the EST did
not match.
GENE FUNCTION
Zhang et al. (2003) demonstrated that SP1 (189906) activated
transcription from the vimentin promoter. Through N-terminal zinc
fingers, ZBP89 (ZNF148; 601897) repressed SP1-mediated activation.
Although vimentin has been presumed to be important for stabilizing the
architecture of the cytoplasm, Mor-Vaknin et al. (2003) found that
monocyte-derived macrophages secrete vimentin into the extracellular
space in vitro. Secretion of vimentin was enhanced by the
proinflammatory cytokine tumor necrosis factor-alpha (TNFA; 191160) and
inhibited by the antiinflammatory cytokine IL10 (124092), suggesting
that vimentin is involved in the immune response. Mor-Vaknin et al.
(2003) noted that vimentin likely has specialized functions that
contribute to specific dynamic cellular processes.
Wang et al. (2012) showed that beclin-1 (604378), an essential autophagy
and tumor suppressor protein, is a target of the protein kinase AKT
(164730). Expression of a beclin-1 mutant resistant to Akt-mediated
phosphorylation increased autophagy, reduced anchorage-independent
growth, and inhibited Akt-driven tumorigenesis. Akt-mediated
phosphorylation of beclin-1 enhanced its interactions with 14-3-3 (see
605066) and vimentin intermediate filament proteins, and vimentin
depletion increased autophagy and inhibited Akt-driven transformation.
Thus, Wang et al. (2012) concluded that Akt-mediated phosphorylation of
beclin-1 functions in autophagy inhibition, oncogenesis, and the
formation of an autophagy-inhibitory beclin-1/14-3-3/vimentin
intermediate filament complex, and suggested that their findings have
broad implications for understanding the role of Akt signaling and
intermediate filament proteins in autophagy and cancer.
MAPPING
Using cDNA clones of the VIM gene prepared from hamster lens mRNA, Quax
et al. (1985) demonstrated that a single-copy gene encodes vimentin in
man and that in man-rodent hybrid cells the gene segregates with human
chromosome 10. Ferrari et al. (1987) showed by Southern blot analysis of
DNA from somatic cell hybrids and by in situ chromosome hybridization
that there is only 1 copy of the VIM gene, which is located on 10p13,
close to IL2R (147730). Mathew et al. (1990) assigned the vimentin gene
to 10p by linkage analysis.
MOLECULAR GENETICS
Muller et al. (2009) screened 90 patients suffering from various types
of cataract for mutations in the VIM gene. They identified
heterozygosity for a mutation (193060.0001) in only 1 patient, a
45-year-old female with pulverulent (dust-like) cataracts (CTRCT30;
116300). The patient's mother also had cataracts.
ANIMAL MODEL
Colucci-Guyon et al. (1994) introduced a null mutation of the vimentin
gene into the germline of mice. Surprisingly, animals homozygous for
this mutation developed and reproduced without an obvious deviant
phenotype. Immunoblotting, immunofluorescence, and immunogold labeling
analyses confirmed the absence of vimentin and of the corresponding
filament network. Furthermore, no compensatory expression of another
intermediate filament could be demonstrated. The results leave open the
question of a possible role of vimentin in unusual situations or
pathologic conditions.
*FIELD* AV
.0001
CATARACT 30, PULVERULENT
VIM, GLU151LYS
In a 45-year-old female with pulverulent cataract (CTRCT30; 116300),
Muller et al. (2009) identified a heterozygous 596G-A transition in exon
1 of the VIM gene, resulting in a glu151-to-lys (E151K) substitution in
coil 1B of the protein. The mutation was not found in 192 healthy
control individuals. Glu151 is a highly conserved residue. The mutant
protein formed an aberrant vimentin cytoskeleton and increased the
proteasome activity in transfected cells. The mutation caused a severe
kinetic defect in vimentin assembly both in vitro and in vivo.
*FIELD* SA
Ferrari et al. (1986); Lilienbaum et al. (1986)
*FIELD* RF
1. Colucci-Guyon, E.; Portier, M.-M.; Dunia, I.; Paulin, D.; Pournin,
S.; Babinet, C.: Mice lacking vimentin develop and reproduce without
an obvious phenotype. Cell 79: 679-694, 1994.
2. Ferrari, S.; Battini, R.; Kaczmarek, L.; Rittling, S.; Calabretta,
B.; de Riel, J. K.; Philiponis, V.; Weil, J.-F.; Baserga, R.: Coding
sequence and growth regulation of the human vimentin gene. Molec.
Cell. Biol. 6: 3614-3620, 1986.
3. Ferrari, S.; Cannizzaro, L. A.; Battini, R.; Huebner, K.; Baserga,
R.: The gene encoding human vimentin is located on the short arm
of chromosome 10. Am. J. Hum. Genet. 41: 616-626, 1987.
4. Gieser, L.; Swaroop, A.: Expressed sequence tags and chromosomal
localization of cDNA clones from a subtracted retinal pigment epithelium
library. Genomics 13: 873-876, 1992.
5. Lilienbaum, A.; Legagneux, V.; Portier, M.-M.; Dellagi, K.; Paulin,
D.: Vimentin gene: expression in human lymphocytes and in Burkitt's
lymphoma cells. EMBO J. 5: 2809-2814, 1986.
6. Marcus, E. M.; Smith, B. A.; Telenius, H.; Landsvater, R. M.; Buys,
C. H. C. M.; Ferrari, S.; Ponder, B. A. J.; Mathew, C. G. P.: BclI
RFLP for the human vimentin gene. Nucleic Acids Res. 16: 9068 only,
1988.
7. Mathew, C. G.; Wakeling, W.; Jones, E.; Easton, D.; Fisher, R.;
Strong, C.; Smith, B.; Chin, K.; Little, P.; Nakamura, Y.; Shows,
T. B.; Jones, C.; Goodfellow, P. J.; Povey, S.; Ponder, B. A. J.:
Regional localization of polymorphic markers on chromosome 10 by physical
and genetic mapping. Ann. Hum. Genet. 54: 121-129, 1990.
8. Mor-Vaknin, N.; Punturieri, A.; Sitwala, K.; Markovitz, D. M.:
Vimentin is secreted by activated macrophages. Nature Cell Biol. 5:
59-63, 2003.
9. Muller, M.; Bhattacharya, S. S.; Moore, T.; Prescott, Q.; Wedig,
T.; Herrmann, H.; Magin, T. M.: Dominant cataract formation in association
with a vimentin assembly disrupting mutation. Hum. Molec. Genet. 18:
1052-1057, 2009.
10. Perreau, J.; Lilienbaum, A.; Vasseur, M.; Paulin, D.: Nucleotide
sequence of the human vimentin gene and regulation of its transcription
in tissues and cultured cells. Gene 62: 7-16, 1988.
11. Quax, W.; Meera Khan, P.; Quax-Jeuken, Y.; Bloemendal, H.: The
human desmin and vimentin genes are located on different chromosomes. Gene 38:
189-196, 1985.
12. Wang, R. C.; Wei, Y.; An, Z.; Zou, Z.; Xiao, G.; Bhagat, G.; White,
M.; Reichelt, J.; Levine, B.: Akt-mediated regulation of autophagy
and tumorigenesis through beclin 1 phosphorylation. Science 338:
956-959, 2012.
13. Zhang, X.; Diab, I. H.; Zehner, Z. E.: ZBP-89 represses vimentin
gene transcription by interacting with the transcriptional activator,
Sp1. Nucleic Acids Res. 31: 2900-2914, 2003.
*FIELD* CN
Ada Hamosh - updated: 1/7/2013
George E. Tiller - updated: 10/14/2009
Cassandra L. Kniffin - updated: 3/29/2004
Patricia A. Hartz - updated: 10/27/2003
*FIELD* CD
Victor A. McKusick: 6/2/1986
*FIELD* ED
carol: 07/19/2013
alopez: 1/7/2013
terry: 1/7/2013
carol: 10/14/2009
ckniffin: 4/1/2004
tkritzer: 3/31/2004
ckniffin: 3/29/2004
cwells: 11/3/2003
terry: 10/27/2003
dkim: 12/15/1998
carol: 12/7/1994
carol: 7/21/1992
supermim: 3/16/1992
carol: 3/21/1991
carol: 3/20/1991
supermim: 3/20/1990