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Vimentin

 VIME_HUMAN              Reviewed;         466 AA.
P08670; B0YJC2; D3DRU4; Q15867; Q15868; Q15869; Q548L2; Q6LER9;
Q8N850; Q96ML2; Q9NTM3;
01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 4.
18-JUL-2018, entry version 234.
RecName: Full=Vimentin;
Name=VIM;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=3467175; DOI=10.1128/MCB.6.11.3614;
Ferrari S., Battini R., Kaczmarek L., Rittling S., Calabretta B.,
de Riel J.K., Philiponis V., Wei J.-F., Baserga R.;
"Coding sequence and growth regulation of the human vimentin gene.";
Mol. Cell. Biol. 6:3614-3620(1986).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2251132; DOI=10.1093/nar/18.22.6692;
Honore B., Madsen P., Basse B., Andersen A., Walbum E., Celis J.E.,
Leffers H.;
"Nucleotide sequence of cDNA covering the complete coding part of the
human vimentin gene.";
Nucleic Acids Res. 18:6692-6692(1990).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Lymphoma;
PubMed=14996095; DOI=10.1111/j.1365-2133.2004.05651.x;
Hartmann T.B., Thiel D., Dummer R., Schadendorf D., Eichmueller S.;
"SEREX identification of new tumour-associated antigens in cutaneous
T-cell lymphoma.";
Br. J. Dermatol. 150:252-258(2004).
[4]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Testis;
Zimbelmann R.;
Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Embryo, Placenta, and Stomach;
PubMed=14702039; DOI=10.1038/ng1285;
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.,
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Adipose tissue, and Coronary artery;
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.
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
NHLBI resequencing and genotyping service (RS&G);
Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164054; DOI=10.1038/nature02462;
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., 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.;
"The DNA sequence and comparative analysis of human chromosome 10.";
Nature 429:375-381(2004).
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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., 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.
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Cervix, Placenta, and Testis;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[12]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-135, AND TISSUE SPECIFICITY.
TISSUE=Mammary carcinoma;
PubMed=2472876;
Sommers C.L., Walker-Jones D., Heckford S.E., Worland P.,
Valverius E., Clark R., McCormick F., Stampfer M., Abularach S.,
Gelmann E.P.;
"Vimentin rather than keratin expression in some hormone-independent
breast cancer cell lines and in oncogene-transformed mammary
epithelial cells.";
Cancer Res. 49:4258-4263(1989).
[13]
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, AND IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=T-cell;
Bienvenut W.V., Kanor S., Tissot J.-D., Quadroni M.;
Submitted (MAY-2006) to UniProtKB.
[14]
PROTEIN SEQUENCE OF 5-12; 14-45; 51-64; 72-78; 105-113; 123-143;
159-184; 187-217; 223-236; 271-292; 295-313; 322-390 AND 403-466,
PHOSPHORYLATION AT SER-56, AND IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Hepatoma;
Bienvenut W.V., Fleming J., Leug H.Y.;
Submitted (JAN-2010) to UniProtKB.
[15]
PROTEIN SEQUENCE OF 17-25 AND 55-70.
TISSUE=Mammary carcinoma;
PubMed=9150946; DOI=10.1002/elps.1150180342;
Rasmussen R.K., Ji H., Eddes J.S., Moritz R.L., Reid G.E.,
Simpson R.J., Dorow D.S.;
"Two-dimensional electrophoretic analysis of human breast carcinoma
proteins: mapping of proteins that bind to the SH3 domain of mixed
lineage kinase MLK2.";
Electrophoresis 18:588-598(1997).
[16]
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, AND IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
Lubec G., Vishwanath V., Chen W.-Q., Sun Y.;
Submitted (DEC-2008) to UniProtKB.
[17]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 113-466, AND TISSUE SPECIFICITY.
TISSUE=Fibroblast;
PubMed=3371665; DOI=10.1016/0378-1119(88)90575-6;
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).
[18]
NUCLEOTIDE SEQUENCE [MRNA] OF 167-466.
TISSUE=Osteosarcoma;
PubMed=2323579; DOI=10.1016/0378-1119(90)90295-3;
Gupta A.K., Aubin J.E., Waye M.M.Y.;
"Isolation of a human vimentin cDNA with a long 3'-noncoding region
from a human osteosarcoma cell line (MG-63).";
Gene 86:303-304(1990).
[19]
PHOSPHORYLATION.
PubMed=9175763; DOI=10.1006/bbrc.1997.6669;
Matsuzawa K., Kosako H., Inagaki N., Shibata H., Mukai H., Ono Y.,
Amano M., Kaibuchi K., Matsuura Y., Azuma I., Inagaki M.;
"Domain-specific phosphorylation of vimentin and glial fibrillary
acidic protein by PKN.";
Biochem. Biophys. Res. Commun. 234:621-625(1997).
[20]
PHOSPHORYLATION AT SER-72.
PubMed=12458200; DOI=10.1074/jbc.M210892200;
Goto H., Yasui Y., Kawajiri A., Nigg E.A., Terada Y., Tatsuka M.,
Nagata K., Inagaki M.;
"Aurora-B regulates the cleavage furrow-specific vimentin
phosphorylation in the cytokinetic process.";
J. Biol. Chem. 278:8526-8530(2003).
[21]
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, AND
IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=14762106; DOI=10.1242/jcs.00906;
Eriksson J.E., He T., Trejo-Skalli A.V., Harmala-Brasken A.-S.,
Hellman J., Chou Y.-H., Goldman R.D.;
"Specific in vivo phosphorylation sites determine the assembly
dynamics of vimentin intermediate filaments.";
J. Cell Sci. 117:919-932(2004).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-117, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=15592455; DOI=10.1038/nbt1046;
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.;
"Immunoaffinity profiling of tyrosine phosphorylation in cancer
cells.";
Nat. Biotechnol. 23:94-101(2005).
[23]
INTERACTION WITH HCV CORE PROTEIN (MICROBIAL INFECTION).
PubMed=15846844; DOI=10.1002/pmic.200401093;
Kang S.-M., Shin M.-J., Kim J.-H., Oh J.-W.;
"Proteomic profiling of cellular proteins interacting with the
hepatitis C virus core protein.";
Proteomics 5:2227-2237(2005).
[24]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-214 AND SER-412, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[25]
INTERACTION WITH EPPK1.
PubMed=16923132; DOI=10.1111/j.1346-8138.2006.00127.x;
Wang W., Sumiyoshi H., Yoshioka H., Fujiwara S.;
"Interactions between epiplakin and intermediate filaments.";
J. Dermatol. 33:518-527(2006).
[26]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-56, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16964243; DOI=10.1038/nbt1240;
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein
phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[27]
INTERACTION WITH TOR1A AND TOR1AIP1.
PubMed=16361107; DOI=10.1016/j.nbd.2005.10.012;
Hewett J.W., Zeng J., Niland B.P., Bragg D.C., Breakefield X.O.;
"Dystonia-causing mutant torsinA inhibits cell adhesion and neurite
extension through interference with cytoskeletal dynamics.";
Neurobiol. Dis. 22:98-111(2006).
[28]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-412, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17924679; DOI=10.1021/pr070152u;
Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
"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.";
J. Proteome Res. 6:4150-4162(2007).
[29]
INTERACTION WITH BCAS3.
PubMed=17505058; DOI=10.1210/me.2006-0514;
Gururaj A.E., Peng S., Vadlamudi R.K., Kumar R.;
"Estrogen induces expression of BCAS3, a novel estrogen receptor-alpha
coactivator, through proline-, glutamic acid-, and leucine-rich
protein-1 (PELP1).";
Mol. Endocrinol. 21:1847-1860(2007).
[30]
INTERACTION WITH STK33, AND PHOSPHORYLATION BY STK33.
PubMed=18811945; DOI=10.1186/1471-2091-9-25;
Brauksiepe B., Mujica A.O., Herrmann H., Schmidt E.R.;
"The serine/threonine kinase Stk33 exhibits autophosphorylation and
phosphorylates the intermediate filament protein Vimentin.";
BMC Biochem. 9:25-25(2008).
[31]
INTERACTION WITH TOR1A.
PubMed=18827015; DOI=10.1242/jcs.029454;
Nery F.C., Zeng J., Niland B.P., Hewett J., Farley J., Irimia D.,
Li Y., Wiche G., Sonnenberg A., Breakefield X.O.;
"TorsinA binds the KASH domain of nesprins and participates in linkage
between nuclear envelope and cytoskeleton.";
J. Cell Sci. 121:3476-3486(2008).
[32]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18220336; DOI=10.1021/pr0705441;
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
efficient phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
[33]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-412, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[34]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-5; SER-25; SER-34;
SER-39; SER-42; SER-51; SER-56; TYR-61; SER-72; SER-73; SER-83;
SER-144; SER-409; SER-412 AND SER-459, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[35]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[36]
INTERACTION WITH SLC6A4.
PubMed=19270731; DOI=10.1371/journal.pone.0004730;
Ahmed B.A., Bukhari I.A., Jeffus B.C., Harney J.T., Thyparambil S.,
Ziu E., Fraer M., Rusch N.J., Zimniak P., Lupashin V., Tang D.,
Kilic F.;
"The cellular distribution of serotonin transporter is impeded on
serotonin-altered vimentin network.";
PLoS ONE 4:E4730-E4730(2009).
[37]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51; SER-56 AND TYR-61,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[38]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-120; LYS-139; LYS-373 AND
LYS-445, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[39]
GLYCOSYLATION AT SER-7; THR-33 AND SER-34.
PubMed=20068230; DOI=10.1126/scisignal.2000526;
Wang Z., Udeshi N.D., Slawson C., Compton P.D., Sakabe K.,
Cheung W.D., Shabanowitz J., Hunt D.F., Hart G.W.;
"Extensive crosstalk between O-GlcNAcylation and phosphorylation
regulates cytokinesis.";
Sci. Signal. 3:RA2-RA2(2010).
[40]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-20; SER-42; SER-47;
SER-51; SER-56; SER-73; SER-83; SER-144; SER-214; SER-226; SER-299;
SER-412; SER-419; SER-420; THR-426; SER-430; THR-436 AND SER-459, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[41]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[42]
FUNCTION IN COLLAGEN MRNA STABILIZATION, AND INTERACTION WITH LARP6.
PubMed=21746880; DOI=10.1128/MCB.05263-11;
Challa A.A., Stefanovic B.;
"A novel role of vimentin filaments: binding and stabilization of
collagen mRNAs.";
Mol. Cell. Biol. 31:3773-3789(2011).
[43]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51; SER-144 AND SER-459,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[44]
PHOSPHORYLATION AT SER-56, AND SUBCELLULAR LOCATION.
PubMed=21465480; DOI=10.1002/jcp.22782;
Lee K.Y., Liu L., Jin Y., Fu S.B., Rosales J.L.;
"Cdk5 mediates vimentin Ser56 phosphorylation during GTP-induced
secretion by neutrophils.";
J. Cell. Physiol. 227:739-750(2012).
[45]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22905912; DOI=10.1021/pr300539b;
Rosenow A., Noben J.P., Jocken J., Kallendrusch S.,
Fischer-Posovszky P., Mariman E.C., Renes J.;
"Resveratrol-induced changes of the human adipocyte secretion
profile.";
J. Proteome Res. 11:4733-4743(2012).
[46]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[47]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25; SER-26; SER-39;
SER-42; SER-47; SER-49; SER-51; SER-56; TYR-61; SER-66; SER-73;
SER-214; SER-226; SER-299; SER-419; SER-420; SER-430; THR-436;
SER-438; THR-446 AND SER-459, AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[48]
INTERACTION WITH DIAPH1, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=23325789; DOI=10.1091/mbc.E12-08-0597;
Li D., Dammer E.B., Lucki N.C., Sewer M.B.;
"cAMP-stimulated phosphorylation of diaphanous 1 regulates protein
stability and interaction with binding partners in adrenocortical
cells.";
Mol. Biol. Cell 24:848-857(2013).
[49]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-20; SER-25; SER-39;
SER-83; SER-87; SER-214; SER-419; THR-426 AND SER-430, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[50]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-445, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25114211; DOI=10.1073/pnas.1413825111;
Impens F., Radoshevich L., Cossart P., Ribet D.;
"Mapping of SUMO sites and analysis of SUMOylation changes induced by
external stimuli.";
Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
[51]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[52]
INVOLVEMENT IN CTRCT30.
PubMed=26694549; DOI=10.1002/humu.22948;
Ma A.S., Grigg J.R., Ho G., Prokudin I., Farnsworth E., Holman K.,
Cheng A., Billson F.A., Martin F., Fraser C., Mowat D., Smith J.,
Christodoulou J., Flaherty M., Bennetts B., Jamieson R.V.;
"Sporadic and familial congenital cataracts: mutational spectrum and
new diagnoses using next-generation sequencing.";
Hum. Mutat. 37:371-384(2016).
[53]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-104; LYS-120; LYS-129;
LYS-139; LYS-223; LYS-262; LYS-294; LYS-313; LYS-373; LYS-439 AND
LYS-445, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[54]
INTERACTION WITH SRMS, SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
PubMed=29496907; DOI=10.1074/mcp.RA118.000643;
Goel R.K., Paczkowska M., Reimand J., Napper S., Lukong K.E.;
"Phosphoproteomics analysis identifies novel candidate substrates of
the non-receptor tyrosine kinase, SRMS.";
Mol. Cell. Proteomics 17:925-947(2018).
[55]
X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 102-138.
PubMed=11243787; DOI=10.1006/jmbi.2001.4442;
Strelkov S.V., Herrmann H., Geisler N., Lustig A., Ivaninskii S.,
Zimbelmann R., Burkhard P., Aebi U.;
"Divide-and-conquer crystallographic approach towards an atomic
structure of intermediate filaments.";
J. Mol. Biol. 306:773-781(2001).
[56]
X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 103-139 AND 328-411.
PubMed=11889032; DOI=10.1093/emboj/21.6.1255;
Strelkov S.V., Herrmann H., Geisler N., Wedig T., Zimbelmann R.,
Aebi U., Burkhard P.;
"Conserved segments 1A and 2B of the intermediate filament dimer:
their atomic structures and role in filament assembly.";
EMBO J. 21:1255-1266(2002).
[57]
S-NITROSYLATION, AND DOMAIN.
PubMed=25417112; DOI=10.1016/j.cell.2014.09.032;
Jia J., Arif A., Terenzi F., Willard B., Plow E.F., Hazen S.L.,
Fox P.L.;
"Target-selective protein S-nitrosylation by sequence motif
recognition.";
Cell 159:623-634(2014).
[58]
X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 263-334, COILED-COIL DOMAINS,
AND SUBUNIT.
PubMed=20176112; DOI=10.1016/j.jsb.2010.02.012;
Nicolet S., Herrmann H., Aebi U., Strelkov S.V.;
"Atomic structure of vimentin coil 2.";
J. Struct. Biol. 170:369-376(2010).
[59]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 261-335 OF MUTANT CYS-265.
PubMed=22119849; DOI=10.1016/j.jsb.2011.11.014;
Chernyatina A.A., Strelkov S.V.;
"Stabilization of vimentin coil2 fragment via an engineered
disulfide.";
J. Struct. Biol. 177:46-53(2012).
[60]
VARIANT CTRCT30 LYS-151, AND CHARACTERIZATION OF VARIANT CTRCT30
LYS-151.
PubMed=19126778; DOI=10.1093/hmg/ddn440;
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. Mol. Genet. 18:1052-1057(2009).
[61]
VARIANT CTRCT30 ARG-208.
PubMed=28450710; DOI=10.1038/s41598-017-01182-9;
Zhai Y., Li J., Yu W., Zhu S., Yu Y., Wu M., Sun G., Gong X., Yao K.;
"Targeted exome sequencing of congenital cataracts related genes:
broadening the mutation spectrum and genotype-phenotype correlations
in 27 Chinese Han families.";
Sci. Rep. 7:1219-1219(2017).
-!- FUNCTION: Vimentins are class-III intermediate filaments found in
various non-epithelial cells, especially mesenchymal cells.
Vimentin is attached to the nucleus, endoplasmic reticulum, and
mitochondria, either laterally or terminally.
{ECO:0000269|PubMed:21746880}.
-!- FUNCTION: Involved with LARP6 in the stabilization of type I
collagen mRNAs for CO1A1 and CO1A2. {ECO:0000269|PubMed:21746880}.
-!- SUBUNIT: Homopolymer assembled from elementary dimers. Interacts
with LGSN and SYNM. Interacts (via rod region) with PLEC (via CH 1
domain) (By similarity). Interacts with SLC6A4 (PubMed:19270731).
Interacts with STK33 (PubMed:18811945). Interacts with LARP6
(PubMed:21746880). Interacts with RAB8B (By similarity). Interacts
with TOR1A; the interaction associates TOR1A with the cytoskeleton
(PubMed:16361107, PubMed:18827015). Interacts with TOR1AIP1
(PubMed:16361107). Interacts with BCAS3 (PubMed:17505058).
Interacts with DIAPH1 (PubMed:23325789). Identified in complexes
that contain VIM, EZR, AHNAK, BFSP1, BFSP2, ANK2, PLEC, PRX and
spectrin (By similarity). Interacts with EPPK1; interaction is
dependent of higher-order structure of intermediate filament
(PubMed:16923132). Interacts with the non-receptor tyrosine kinase
SRMS; the interaction leads to phosphorylation of VIM
(PubMed:29496907). {ECO:0000250|UniProtKB:P20152,
ECO:0000250|UniProtKB:P31000, ECO:0000269|PubMed:15846844,
ECO:0000269|PubMed:16361107, ECO:0000269|PubMed:16923132,
ECO:0000269|PubMed:17505058, ECO:0000269|PubMed:18811945,
ECO:0000269|PubMed:18827015, ECO:0000269|PubMed:19270731,
ECO:0000269|PubMed:20176112, ECO:0000269|PubMed:21746880,
ECO:0000269|PubMed:23325789, ECO:0000269|PubMed:29496907}.
-!- SUBUNIT: (Microbial infection) Interacts with HCV core protein.
{ECO:0000269|PubMed:15846844}.
-!- INTERACTION:
Self; NbExp=11; IntAct=EBI-353844, EBI-353844;
P14340:- (xeno); NbExp=10; IntAct=EBI-353844, EBI-9844509;
P27958:- (xeno); NbExp=4; IntAct=EBI-353844, EBI-6377335;
P31749:AKT1; NbExp=29; IntAct=EBI-353844, EBI-296087;
P31751:AKT2; NbExp=6; IntAct=EBI-353844, EBI-296058;
Q9H6U6:BCAS3; NbExp=3; IntAct=EBI-353844, EBI-6083685;
Q14457:BECN1; NbExp=3; IntAct=EBI-353844, EBI-949378;
Q14194:CRMP1; NbExp=3; IntAct=EBI-353844, EBI-473101;
Q2TBE0:CWF19L2; NbExp=3; IntAct=EBI-353844, EBI-5453285;
P17661:DES; NbExp=4; IntAct=EBI-353844, EBI-1055572;
P14136:GFAP; NbExp=3; IntAct=EBI-353844, EBI-744302;
P11021:HSPA5; NbExp=3; IntAct=EBI-353844, EBI-354921;
O95251:KAT7; NbExp=4; IntAct=EBI-353844, EBI-473199;
P35900:KRT20; NbExp=6; IntAct=EBI-353844, EBI-742094;
O76036:NCR1; NbExp=3; IntAct=EBI-353844, EBI-13915737;
P07196:NEFL; NbExp=3; IntAct=EBI-353844, EBI-475646;
P07197:NEFM; NbExp=4; IntAct=EBI-353844, EBI-1105035;
Q9HC29:NOD2; NbExp=7; IntAct=EBI-353844, EBI-7445625;
Q96IZ0:PAWR; NbExp=2; IntAct=EBI-353844, EBI-595869;
Q925J2:Pkd1 (xeno); NbExp=2; IntAct=EBI-353844, EBI-7985677;
Q16512:PKN1; NbExp=3; IntAct=EBI-353844, EBI-602382;
Q13835-2:PKP1; NbExp=3; IntAct=EBI-353844, EBI-9087684;
Q96PV4:PNMA5; NbExp=3; IntAct=EBI-353844, EBI-10171633;
O60437:PPL; NbExp=3; IntAct=EBI-353844, EBI-368321;
P41219:PRPH; NbExp=3; IntAct=EBI-353844, EBI-752074;
P54727:RAD23B; NbExp=2; IntAct=EBI-353844, EBI-954531;
O95361:TRIM16; NbExp=3; IntAct=EBI-353844, EBI-727384;
Q9BQE3:TUBA1C; NbExp=3; IntAct=EBI-353844, EBI-1103245;
Q8N3L3:TXLNB; NbExp=5; IntAct=EBI-353844, EBI-6116822;
P63104:YWHAZ; NbExp=2; IntAct=EBI-353844, EBI-347088;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21465480,
ECO:0000269|PubMed:29496907}. Cytoplasm, cytoskeleton
{ECO:0000269|PubMed:29496907}. Nucleus matrix
{ECO:0000250|UniProtKB:P31000}.
-!- 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.
{ECO:0000269|PubMed:2472876, ECO:0000269|PubMed:3371665}.
-!- DOMAIN: The central alpha-helical coiled-coil IF rod domain
mediates elementary homodimerization.
-!- DOMAIN: The [IL]-x-C-x-x-[DE] motif is a proposed target motif for
cysteine S-nitrosylation mediated by the iNOS-S100A8/A9
transnitrosylase complex. {ECO:0000305|PubMed:25417112}.
-!- PTM: Filament disassembly during mitosis is promoted by
phosphorylation at Ser-55 as well as by nestin (By similarity).
One of the most prominent phosphoproteins in various cells of
mesenchymal origin. Phosphorylation is enhanced during cell
division, at which time vimentin filaments are significantly
reorganized. Phosphorylation by PKN1 inhibits the formation of
filaments. Phosphorylated at Ser-56 by CDK5 during neutrophil
secretion in the cytoplasm (PubMed:21465480). Phosphorylated by
STK33 (PubMed:18811945). Phosphorylated on tyrosine residues by
SRMS (PubMed:29496907). {ECO:0000250|UniProtKB:P31000,
ECO:0000269|PubMed:18811945, ECO:0000269|PubMed:21465480,
ECO:0000269|PubMed:29496907, ECO:0000269|Ref.14}.
-!- PTM: O-glycosylated during cytokinesis at sites identical or close
to phosphorylation sites, this interferes with the phosphorylation
status. {ECO:0000269|PubMed:20068230}.
-!- PTM: S-nitrosylation is induced by interferon-gamma and
oxidatively-modified low-densitity lipoprotein (LDL(ox)) possibly
implicating the iNOS-S100A8/9 transnitrosylase complex.
{ECO:0000305|PubMed:25417112}.
-!- DISEASE: Cataract 30, multiple types (CTRCT30) [MIM:116300]: An
opacification of the crystalline lens of the eye that frequently
results in visual impairment or blindness. Opacities vary in
morphology, are often confined to a portion of the lens, and may
be static or progressive. In general, the more posteriorly located
and dense an opacity, the greater the impact on visual function.
{ECO:0000269|PubMed:19126778, ECO:0000269|PubMed:26694549,
ECO:0000269|PubMed:28450710}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the intermediate filament family.
{ECO:0000255|PROSITE-ProRule:PRU01188}.
-!- SEQUENCE CAUTION:
Sequence=BAB71275.1; Type=Miscellaneous discrepancy; Note=Product of a cloning artifact.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Wikipedia; Note=Vimentin entry;
URL="https://en.wikipedia.org/wiki/Vimentin";
-----------------------------------------------------------------------
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EMBL; M14144; AAA61279.1; -; Genomic_DNA.
EMBL; X56134; CAA39600.1; -; mRNA.
EMBL; AF328728; AAN09720.1; -; mRNA.
EMBL; Z19554; CAA79613.2; -; mRNA.
EMBL; AK056766; BAB71275.1; ALT_SEQ; mRNA.
EMBL; AK097336; BAC05002.1; -; mRNA.
EMBL; AK290643; BAF83332.1; -; mRNA.
EMBL; CR407690; CAG28618.1; -; mRNA.
EMBL; AK222507; BAD96227.1; -; mRNA.
EMBL; AK222602; BAD96322.1; -; mRNA.
EMBL; EF445046; ACA06101.1; -; Genomic_DNA.
EMBL; EF445046; ACA06102.1; -; Genomic_DNA.
EMBL; AL133415; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471072; EAW86215.1; -; Genomic_DNA.
EMBL; CH471072; EAW86216.1; -; Genomic_DNA.
EMBL; BC000163; AAH00163.2; -; mRNA.
EMBL; BC030573; AAH30573.1; -; mRNA.
EMBL; BC066956; AAH66956.1; -; mRNA.
EMBL; X16478; CAA34499.1; -; mRNA.
EMBL; M18895; AAA61281.2; -; Genomic_DNA.
EMBL; M18888; AAA61281.2; JOINED; Genomic_DNA.
EMBL; M18889; AAA61281.2; JOINED; Genomic_DNA.
EMBL; M18890; AAA61281.2; JOINED; Genomic_DNA.
EMBL; M18891; AAA61281.2; JOINED; Genomic_DNA.
EMBL; M18892; AAA61281.2; JOINED; Genomic_DNA.
EMBL; M18893; AAA61281.2; JOINED; Genomic_DNA.
EMBL; M18894; AAA61281.2; JOINED; Genomic_DNA.
EMBL; M25246; AAA61282.1; -; mRNA.
CCDS; CCDS7120.1; -.
PIR; S13115; A25074.
RefSeq; NP_003371.2; NM_003380.3.
RefSeq; XP_006717563.1; XM_006717500.1.
UniGene; Hs.455493; -.
UniGene; Hs.691131; -.
UniGene; Hs.728090; -.
PDB; 1GK4; X-ray; 2.30 A; A/B/C/D/E/F=328-411.
PDB; 1GK6; X-ray; 1.90 A; A/B=385-412.
PDB; 1GK7; X-ray; 1.40 A; A=102-138.
PDB; 3G1E; X-ray; 1.83 A; A/B=102-138.
PDB; 3KLT; X-ray; 2.70 A; A/B/C/D=263-334.
PDB; 3S4R; X-ray; 2.45 A; A/B=99-189.
PDB; 3SSU; X-ray; 2.60 A; A/B=99-189.
PDB; 3SWK; X-ray; 1.70 A; A/B=153-238.
PDB; 3TRT; X-ray; 2.30 A; A/B=261-335.
PDB; 3UF1; X-ray; 2.81 A; A/B/C/D=144-251.
PDB; 4MCY; X-ray; 2.30 A; C=66-78.
PDB; 4MCZ; X-ray; 2.41 A; C=59-71.
PDB; 4MD0; X-ray; 2.19 A; C=59-71.
PDB; 4MD5; X-ray; 1.65 A; C=66-78.
PDB; 4MDI; X-ray; 2.00 A; C=66-78.
PDB; 4MDJ; X-ray; 1.70 A; C=66-78.
PDB; 4YPC; X-ray; 1.44 A; A=161-243.
PDB; 4YV3; X-ray; 2.00 A; A/B/C=161-238.
PDB; 6ATF; X-ray; 1.90 A; C/F=59-71.
PDB; 6ATI; X-ray; 1.98 A; C/F=59-71.
PDB; 6BIR; X-ray; 2.30 A; C=419-431.
PDBsum; 1GK4; -.
PDBsum; 1GK6; -.
PDBsum; 1GK7; -.
PDBsum; 3G1E; -.
PDBsum; 3KLT; -.
PDBsum; 3S4R; -.
PDBsum; 3SSU; -.
PDBsum; 3SWK; -.
PDBsum; 3TRT; -.
PDBsum; 3UF1; -.
PDBsum; 4MCY; -.
PDBsum; 4MCZ; -.
PDBsum; 4MD0; -.
PDBsum; 4MD5; -.
PDBsum; 4MDI; -.
PDBsum; 4MDJ; -.
PDBsum; 4YPC; -.
PDBsum; 4YV3; -.
PDBsum; 6ATF; -.
PDBsum; 6ATI; -.
PDBsum; 6BIR; -.
ProteinModelPortal; P08670; -.
SMR; P08670; -.
BioGrid; 113272; 269.
CORUM; P08670; -.
DIP; DIP-32507N; -.
IntAct; P08670; 215.
MINT; P08670; -.
STRING; 9606.ENSP00000224237; -.
ChEMBL; CHEMBL3712854; -.
MoonDB; P08670; Predicted.
CarbonylDB; P08670; -.
iPTMnet; P08670; -.
PhosphoSitePlus; P08670; -.
SwissPalm; P08670; -.
BioMuta; VIM; -.
DMDM; 55977767; -.
DOSAC-COBS-2DPAGE; P08670; -.
OGP; P08670; -.
REPRODUCTION-2DPAGE; IPI00418471; -.
REPRODUCTION-2DPAGE; P08670; -.
SWISS-2DPAGE; P08670; -.
UCD-2DPAGE; P08670; -.
EPD; P08670; -.
PaxDb; P08670; -.
PeptideAtlas; P08670; -.
PRIDE; P08670; -.
ProteomicsDB; 52153; -.
TopDownProteomics; P08670; -.
DNASU; 7431; -.
Ensembl; ENST00000224237; ENSP00000224237; ENSG00000026025.
Ensembl; ENST00000544301; ENSP00000446007; ENSG00000026025.
GeneID; 7431; -.
KEGG; hsa:7431; -.
CTD; 7431; -.
DisGeNET; 7431; -.
EuPathDB; HostDB:ENSG00000026025.13; -.
GeneCards; VIM; -.
H-InvDB; HIX0035657; -.
HGNC; HGNC:12692; VIM.
HPA; CAB000080; -.
HPA; CAB058687; -.
HPA; HPA001762; -.
MalaCards; VIM; -.
MIM; 116300; phenotype.
MIM; 193060; gene.
neXtProt; NX_P08670; -.
OpenTargets; ENSG00000026025; -.
Orphanet; 98984; Pulverulent cataract.
PharmGKB; PA37311; -.
eggNOG; ENOG410IFZ1; Eukaryota.
eggNOG; ENOG410XRBS; LUCA.
GeneTree; ENSGT00910000143989; -.
HOVERGEN; HBG013015; -.
InParanoid; P08670; -.
KO; K07606; -.
OMA; QVINEST; -.
OrthoDB; EOG091G12MK; -.
PhylomeDB; P08670; -.
TreeFam; TF330122; -.
Reactome; R-HSA-264870; Caspase-mediated cleavage of cytoskeletal proteins.
Reactome; R-HSA-390522; Striated Muscle Contraction.
Reactome; R-HSA-6785807; Interleukin-4 and 13 signaling.
SIGNOR; P08670; -.
ChiTaRS; VIM; human.
EvolutionaryTrace; P08670; -.
GeneWiki; Vimentin; -.
GenomeRNAi; 7431; -.
PMAP-CutDB; P08670; -.
PRO; PR:P08670; -.
Proteomes; UP000005640; Chromosome 10.
Bgee; ENSG00000026025; -.
ExpressionAtlas; P08670; baseline and differential.
Genevisible; P08670; HS.
GO; GO:0031252; C:cell leading edge; IEA:Ensembl.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005856; C:cytoskeleton; IDA:MGI.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
GO; GO:0005882; C:intermediate filament; IDA:UniProtKB.
GO; GO:0043005; C:neuron projection; IEA:Ensembl.
GO; GO:0016363; C:nuclear matrix; IEA:UniProtKB-SubCell.
GO; GO:0005777; C:peroxisome; IDA:UniProtKB.
GO; GO:0045335; C:phagocytic vesicle; IEA:Ensembl.
GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
GO; GO:0005844; C:polysome; IDA:UniProtKB.
GO; GO:1990904; C:ribonucleoprotein complex; IDA:UniProtKB.
GO; GO:0003725; F:double-stranded RNA binding; IDA:MGI.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:1990254; F:keratin filament binding; IPI:AgBase.
GO; GO:0008022; F:protein C-terminus binding; IPI:UniProtKB.
GO; GO:0019904; F:protein domain specific binding; IPI:UniProtKB.
GO; GO:0097110; F:scaffold protein binding; IPI:BHF-UCL.
GO; GO:0005200; F:structural constituent of cytoskeleton; IDA:UniProtKB.
GO; GO:0005212; F:structural constituent of eye lens; IEA:Ensembl.
GO; GO:0014002; P:astrocyte development; IEA:Ensembl.
GO; GO:0060020; P:Bergmann glial cell differentiation; IEA:Ensembl.
GO; GO:0071346; P:cellular response to interferon-gamma; IEA:Ensembl.
GO; GO:0019221; P:cytokine-mediated signaling pathway; TAS:Reactome.
GO; GO:0045109; P:intermediate filament organization; IEA:Ensembl.
GO; GO:0070307; P:lens fiber cell development; IEA:Ensembl.
GO; GO:0030049; P:muscle filament sliding; TAS:Reactome.
GO; GO:0010977; P:negative regulation of neuron projection development; IEA:Ensembl.
GO; GO:0032967; P:positive regulation of collagen biosynthetic process; IMP:UniProtKB.
GO; GO:0045727; P:positive regulation of translation; IMP:UniProtKB.
GO; GO:0043488; P:regulation of mRNA stability; IMP:UniProtKB.
GO; GO:0060395; P:SMAD protein signal transduction; IEA:Ensembl.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
InterPro; IPR001664; IF.
InterPro; IPR018039; IF_conserved.
InterPro; IPR039008; IF_rod_dom.
InterPro; IPR006821; Intermed_filament_DNA-bd.
InterPro; IPR027699; Vimentin.
PANTHER; PTHR23239; PTHR23239; 1.
PANTHER; PTHR23239:SF27; PTHR23239:SF27; 1.
Pfam; PF00038; Filament; 1.
Pfam; PF04732; Filament_head; 1.
SMART; SM01391; Filament; 1.
PROSITE; PS00226; IF_ROD_1; 1.
PROSITE; PS51842; IF_ROD_2; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Cataract; Coiled coil; Complete proteome;
Cytoplasm; Cytoskeleton; Direct protein sequencing; Disease mutation;
Glycoprotein; Host-virus interaction; Intermediate filament;
Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome;
S-nitrosylation; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000269|Ref.13}.
CHAIN 2 466 Vimentin.
/FTId=PRO_0000063754.
DOMAIN 103 411 IF rod. {ECO:0000255|PROSITE-
ProRule:PRU01188}.
REGION 2 95 Head.
REGION 96 131 Coil 1A.
REGION 132 153 Linker 1.
REGION 154 245 Coil 1B.
REGION 246 268 Linker 12.
REGION 269 407 Coil 2.
REGION 408 466 Tail.
COILED 96 131 {ECO:0000269|PubMed:20176112}.
COILED 154 245 {ECO:0000269|PubMed:20176112}.
COILED 303 407 {ECO:0000269|PubMed:20176112}.
MOTIF 326 329 [IL]-x-C-x-x-[DE] motif.
{ECO:0000305|PubMed:25417112}.
SITE 351 351 Stutter.
MOD_RES 2 2 N-acetylserine. {ECO:0000269|Ref.13}.
MOD_RES 5 5 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000269|PubMed:14762106}.
MOD_RES 7 7 Phosphoserine; by PKA and PKC; alternate.
{ECO:0000269|PubMed:14762106}.
MOD_RES 8 8 Phosphoserine.
{ECO:0000269|PubMed:14762106}.
MOD_RES 9 9 Phosphoserine; by PKC.
{ECO:0000269|PubMed:14762106}.
MOD_RES 10 10 Phosphoserine; by PKC.
{ECO:0000269|PubMed:14762106}.
MOD_RES 20 20 Phosphothreonine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:24275569}.
MOD_RES 25 25 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 26 26 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 34 34 Phosphoserine; by PKC; alternate.
{ECO:0000244|PubMed:18669648}.
MOD_RES 39 39 Phosphoserine; by CaMK2, PKA, PKC and
ROCK2. {ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569,
ECO:0000269|PubMed:14762106}.
MOD_RES 42 42 Phosphoserine; by PKC.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:14762106}.
MOD_RES 47 47 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 49 49 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 51 51 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 53 53 Phosphotyrosine.
{ECO:0000250|UniProtKB:P20152}.
MOD_RES 55 55 Phosphoserine.
{ECO:0000250|UniProtKB:P31000}.
MOD_RES 56 56 Phosphoserine; by CDK5 and CDK1.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:21465480,
ECO:0000269|Ref.14}.
MOD_RES 61 61 Phosphotyrosine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
MOD_RES 66 66 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 72 72 Phosphoserine; by AURKB and ROCK2.
{ECO:0000244|PubMed:18669648,
ECO:0000269|PubMed:12458200,
ECO:0000269|PubMed:14762106}.
MOD_RES 73 73 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:14762106}.
MOD_RES 83 83 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:24275569}.
MOD_RES 87 87 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 117 117 Phosphotyrosine.
{ECO:0000244|PubMed:15592455}.
MOD_RES 120 120 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:19608861}.
MOD_RES 120 120 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P20152}.
MOD_RES 129 129 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P20152}.
MOD_RES 129 129 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P20152}.
MOD_RES 139 139 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:19608861}.
MOD_RES 144 144 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692}.
MOD_RES 168 168 N6-acetyllysine.
{ECO:0000250|UniProtKB:P20152}.
MOD_RES 188 188 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P20152}.
MOD_RES 188 188 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P20152}.
MOD_RES 214 214 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 223 223 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P20152}.
MOD_RES 226 226 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 235 235 N6-acetyllysine.
{ECO:0000250|UniProtKB:P20152}.
MOD_RES 294 294 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P20152}.
MOD_RES 294 294 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P20152}.
MOD_RES 299 299 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 325 325 Phosphoserine.
{ECO:0000250|UniProtKB:P20152}.
MOD_RES 373 373 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:19608861}.
MOD_RES 409 409 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 412 412 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:17924679,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:20068231}.
MOD_RES 419 419 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 420 420 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:14762106}.
MOD_RES 426 426 Phosphothreonine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:24275569}.
MOD_RES 430 430 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569,
ECO:0000269|PubMed:14762106}.
MOD_RES 436 436 Phosphothreonine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 438 438 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 445 445 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:19608861}.
MOD_RES 445 445 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P20152}.
MOD_RES 446 446 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 458 458 Phosphothreonine.
{ECO:0000269|PubMed:14762106}.
MOD_RES 459 459 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:14762106}.
CARBOHYD 7 7 O-linked (GlcNAc) serine; alternate.
{ECO:0000269|PubMed:20068230}.
CARBOHYD 33 33 O-linked (GlcNAc) threonine.
{ECO:0000269|PubMed:20068230}.
CARBOHYD 34 34 O-linked (GlcNAc) serine; alternate.
{ECO:0000269|PubMed:20068230}.
CROSSLNK 104 104 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 120 120 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:28112733}.
CROSSLNK 129 129 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:28112733}.
CROSSLNK 139 139 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:28112733}.
CROSSLNK 223 223 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:28112733}.
CROSSLNK 262 262 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 294 294 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:28112733}.
CROSSLNK 313 313 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 373 373 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:28112733}.
CROSSLNK 439 439 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 445 445 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1);
alternate. {ECO:0000244|PubMed:25114211}.
CROSSLNK 445 445 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:25114211,
ECO:0000244|PubMed:28112733}.
VARIANT 151 151 E -> K (in CTRCT30; the mutation
increases the proteasome activity in
transfected cells; causes also a severe
kinetic defect in vimentin assembly both
in vitro and in vivo; dbSNP:rs121917775).
{ECO:0000269|PubMed:19126778}.
/FTId=VAR_070100.
VARIANT 208 208 Q -> R (in CTRCT30; unknown pathological
significance; dbSNP:rs1085307141).
{ECO:0000269|PubMed:28450710}.
/FTId=VAR_078860.
CONFLICT 42 42 S -> D (in Ref. 1; AAA61279).
{ECO:0000305}.
CONFLICT 113 113 R -> P (in Ref. 12; CAA34499).
{ECO:0000305}.
CONFLICT 197 197 E -> G (in Ref. 6; CAG28618).
{ECO:0000305}.
CONFLICT 201 201 N -> S (in Ref. 17; AAA61281).
{ECO:0000305}.
CONFLICT 265 265 L -> S (in Ref. 17; AAA61281).
{ECO:0000305}.
CONFLICT 278 278 S -> I (in Ref. 17; AAA61281).
{ECO:0000305}.
CONFLICT 339 339 S -> C (in Ref. 17; AAA61281).
{ECO:0000305}.
CONFLICT 350 350 N -> K (in Ref. 17; AAA61281).
{ECO:0000305}.
CONFLICT 442 442 L -> F (in Ref. 1; AAA61279).
{ECO:0000305}.
HELIX 101 135 {ECO:0000244|PDB:1GK7}.
HELIX 167 235 {ECO:0000244|PDB:4YPC}.
STRAND 238 241 {ECO:0000244|PDB:4YPC}.
TURN 244 248 {ECO:0000244|PDB:3UF1}.
HELIX 266 334 {ECO:0000244|PDB:3TRT}.
HELIX 385 405 {ECO:0000244|PDB:1GK6}.
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


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