VIME_HUMAN
ID VIME_HUMAN Reviewed; 466 AA.
AC P08670; B0YJC2; D3DRU4; Q15867; Q15868; Q15869; Q548L2; Q6LER9; Q8N850;
AC Q96ML2; Q9NTM3;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 262.
DE RecName: Full=Vimentin;
GN Name=VIM;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3467175; DOI=10.1128/mcb.6.11.3614-3620.1986;
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 human
RT 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 T-cell
RT 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., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., 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., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA 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., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., 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., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., 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 project:
RT 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., Valverius E.,
RA Clark R., McCormick F., Stampfer M., Abularach S., Gelmann E.P.;
RT "Vimentin rather than keratin expression in some hormone-independent breast
RT cancer cell lines and in oncogene-transformed mammary 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 IDENTIFICATION BY 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; 159-184;
RP 187-217; 223-236; 271-292; 295-313; 322-390 AND 403-466, PHOSPHORYLATION AT
RP SER-56, AND IDENTIFICATION BY 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., Simpson R.J.,
RA 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 lineage
RT 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 411-439,
RP AND IDENTIFICATION BY 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 from a
RT 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 acidic
RT 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 phosphorylation
RT in the cytokinetic process.";
RL J. Biol. Chem. 278:8526-8530(2003).
RN [21]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Lymphoblast;
RX PubMed=14654843; DOI=10.1038/nature02166;
RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.;
RT "Proteomic characterization of the human centrosome by protein correlation
RT profiling.";
RL Nature 426:570-574(2003).
RN [22]
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 IDENTIFICATION
RP BY MASS SPECTROMETRY.
RX PubMed=14762106; DOI=10.1242/jcs.00906;
RA Eriksson J.E., He T., Trejo-Skalli A.V., Harmala-Brasken A.-S., Hellman J.,
RA Chou Y.-H., Goldman R.D.;
RT "Specific in vivo phosphorylation sites determine the assembly dynamics of
RT vimentin intermediate filaments.";
RL J. Cell Sci. 117:919-932(2004).
RN [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-117, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [24]
RP INTERACTION WITH HCV CORE PROTEIN (MICROBIAL INFECTION).
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 hepatitis C
RT virus core protein.";
RL Proteomics 5:2227-2237(2005).
RN [25]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-214 AND SER-412, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [26]
RP INTERACTION WITH EPPK1.
RX PubMed=16923132; DOI=10.1111/j.1346-8138.2006.00127.x;
RA Wang W., Sumiyoshi H., Yoshioka H., Fujiwara S.;
RT "Interactions between epiplakin and intermediate filaments.";
RL J. Dermatol. 33:518-527(2006).
RN [27]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-56, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [28]
RP INTERACTION WITH TOR1A AND TOR1AIP1.
RX PubMed=16361107; DOI=10.1016/j.nbd.2005.10.012;
RA Hewett J.W., Zeng J., Niland B.P., Bragg D.C., Breakefield X.O.;
RT "Dystonia-causing mutant torsinA inhibits cell adhesion and neurite
RT extension through interference with cytoskeletal dynamics.";
RL Neurobiol. Dis. 22:98-111(2006).
RN [29]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-412, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 cells
RT and high confident phosphopeptide identification by cross-validation of
RT MS/MS and MS/MS/MS spectra.";
RL J. Proteome Res. 6:4150-4162(2007).
RN [30]
RP INTERACTION WITH BCAS3.
RX PubMed=17505058; DOI=10.1210/me.2006-0514;
RA Gururaj A.E., Peng S., Vadlamudi R.K., Kumar R.;
RT "Estrogen induces expression of BCAS3, a novel estrogen receptor-alpha
RT coactivator, through proline-, glutamic acid-, and leucine-rich protein-1
RT (PELP1).";
RL Mol. Endocrinol. 21:1847-1860(2007).
RN [31]
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 [32]
RP INTERACTION WITH PRKCE, AND SUBCELLULAR LOCATION.
RX PubMed=18408015; DOI=10.1074/jbc.m710436200;
RA Sunesson L., Hellman U., Larsson C.;
RT "Protein kinase Cepsilon binds peripherin and induces its aggregation,
RT which is accompanied by apoptosis of neuroblastoma cells.";
RL J. Biol. Chem. 283:16653-16664(2008).
RN [33]
RP INTERACTION WITH TOR1A.
RX PubMed=18827015; DOI=10.1242/jcs.029454;
RA Nery F.C., Zeng J., Niland B.P., Hewett J., Farley J., Irimia D., Li Y.,
RA Wiche G., Sonnenberg A., Breakefield X.O.;
RT "TorsinA binds the KASH domain of nesprins and participates in linkage
RT between nuclear envelope and cytoskeleton.";
RL J. Cell Sci. 121:3476-3486(2008).
RN [34]
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., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [35]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-412, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [36]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-5; SER-25; SER-34; SER-39;
RP SER-42; SER-51; SER-56; TYR-61; SER-72; SER-73; SER-83; SER-144; SER-409;
RP SER-412 AND SER-459, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
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 [37]
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., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [38]
RP RETRACTED PAPER.
RX PubMed=19270731; DOI=10.1371/journal.pone.0004730;
RA Ahmed B.A., Bukhari I.A., Jeffus B.C., Harney J.T., Thyparambil S., Ziu E.,
RA Fraer M., Rusch N.J., Zimniak P., Lupashin V., Tang D., 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 [39]
RP RETRACTION NOTICE OF PUBMED:19270731.
RX PubMed=30707744; DOI=10.1371/journal.pone.0211966;
RA Ahmed B.A., Bukhari I.A., Jeffus B.C., Harney J.T., Thyparambil S., Ziu E.,
RA Fraer M., Rusch N.J., Zimniak P., Lupashin V., Tang D., Kilic F.;
RT "Retraction: The Cellular Distribution of Serotonin Transporter Is Impeded
RT on Serotonin-Altered Vimentin Network.";
RL PLoS ONE 14:e0211966-e0211966(2019).
RN [40]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51; SER-56 AND TYR-61, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 [41]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-120; LYS-139; LYS-373 AND
RP LYS-445, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA 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 [42]
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., Cheung W.D.,
RA Shabanowitz J., Hunt D.F., Hart G.W.;
RT "Extensive crosstalk between O-GlcNAcylation and phosphorylation regulates
RT cytokinesis.";
RL Sci. Signal. 3:RA2-RA2(2010).
RN [43]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-20; SER-42; SER-47; SER-51;
RP SER-56; SER-73; SER-83; SER-144; SER-214; SER-226; SER-299; SER-412;
RP SER-419; SER-420; THR-426; SER-430; THR-436 AND SER-459, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [44]
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., Buerckstuemmer T.,
RA 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 [45]
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 collagen
RT mRNAs.";
RL Mol. Cell. Biol. 31:3773-3789(2011).
RN [46]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51; SER-144 AND SER-459, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [47]
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 secretion
RT by neutrophils.";
RL J. Cell. Physiol. 227:739-750(2012).
RN [48]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22905912; DOI=10.1021/pr300539b;
RA Rosenow A., Noben J.P., Jocken J., Kallendrusch S., Fischer-Posovszky P.,
RA Mariman E.C., Renes J.;
RT "Resveratrol-induced changes of the human adipocyte secretion profile.";
RL J. Proteome Res. 11:4733-4743(2012).
RN [49]
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., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [50]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25; SER-26; SER-39; SER-42;
RP SER-47; SER-49; SER-51; SER-56; TYR-61; SER-66; SER-73; SER-214; SER-226;
RP SER-299; SER-419; SER-420; SER-430; THR-436; SER-438; THR-446 AND SER-459,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [51]
RP INTERACTION WITH DIAPH1, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=23325789; DOI=10.1091/mbc.e12-08-0597;
RA Li D., Dammer E.B., Lucki N.C., Sewer M.B.;
RT "cAMP-stimulated phosphorylation of diaphanous 1 regulates protein
RT stability and interaction with binding partners in adrenocortical cells.";
RL Mol. Biol. Cell 24:848-857(2013).
RN [52]
RP S-NITROSYLATION, AND DOMAIN.
RX PubMed=25417112; DOI=10.1016/j.cell.2014.09.032;
RA Jia J., Arif A., Terenzi F., Willard B., Plow E.F., Hazen S.L., Fox P.L.;
RT "Target-selective protein S-nitrosylation by sequence motif recognition.";
RL Cell 159:623-634(2014).
RN [53]
RP INTERACTION WITH PLEC.
RX PubMed=24940650; DOI=10.1038/jid.2014.255;
RA Bouameur J.E., Favre B., Fontao L., Lingasamy P., Begre N., Borradori L.;
RT "Interaction of plectin with keratins 5 and 14: dependence on several
RT plectin domains and keratin quaternary structure.";
RL J. Invest. Dermatol. 134:2776-2783(2014).
RN [54]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-20; SER-25; SER-39; SER-83;
RP SER-87; SER-214; SER-419; THR-426 AND SER-430, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [55]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-445, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25114211; DOI=10.1073/pnas.1413825111;
RA Impens F., Radoshevich L., Cossart P., Ribet D.;
RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by
RT external stimuli.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
RN [56]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [57]
RP INTERACTION WITH HDGF.
RX PubMed=26845719; DOI=10.1515/hsz-2015-0273;
RA Nuesse J., Mirastschijski U., Waespy M., Oetjen J., Brandes N., Rebello O.,
RA Paroni F., Kelm S., Dietz F.;
RT "Two new isoforms of the human hepatoma-derived growth factor interact with
RT components of the cytoskeleton.";
RL Biol. Chem. 397:417-436(2016).
RN [58]
RP INVOLVEMENT IN CTRCT30.
RX PubMed=26694549; DOI=10.1002/humu.22948;
RA Ma A.S., Grigg J.R., Ho G., Prokudin I., Farnsworth E., Holman K.,
RA Cheng A., Billson F.A., Martin F., Fraser C., Mowat D., Smith J.,
RA Christodoulou J., Flaherty M., Bennetts B., Jamieson R.V.;
RT "Sporadic and familial congenital cataracts: mutational spectrum and new
RT diagnoses using next-generation sequencing.";
RL Hum. Mutat. 37:371-384(2016).
RN [59]
RP INTERACTION WITH NOD2, AND INDUCTION.
RX PubMed=27812135; DOI=10.1371/journal.pone.0165420;
RA Thiebaut R., Esmiol S., Lecine P., Mahfouz B., Hermant A., Nicoletti C.,
RA Parnis S., Perroy J., Borg J.P., Pascoe L., Hugot J.P., Ollendorff V.;
RT "Characterization and Genetic Analyses of New Genes Coding for NOD2
RT Interacting Proteins.";
RL PLoS ONE 11:E0165420-E0165420(2016).
RN [60]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-104; LYS-120; LYS-129; LYS-139;
RP LYS-223; LYS-262; LYS-294; LYS-313; LYS-373; LYS-439 AND LYS-445, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [61]
RP INTERACTION WITH SRMS, SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
RX PubMed=29496907; DOI=10.1074/mcp.ra118.000643;
RA Goel R.K., Paczkowska M., Reimand J., Napper S., Lukong K.E.;
RT "Phosphoproteomics analysis identifies novel candidate substrates of the
RT non-receptor tyrosine kinase, SRMS.";
RL Mol. Cell. Proteomics 17:925-947(2018).
RN [62]
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 structure
RT of intermediate filaments.";
RL J. Mol. Biol. 306:773-781(2001).
RN [63]
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., Aebi U.,
RA Burkhard P.;
RT "Conserved segments 1A and 2B of the intermediate filament dimer: their
RT atomic structures and role in filament assembly.";
RL EMBO J. 21:1255-1266(2002).
RN [64]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 263-334, COILED-COIL DOMAINS, AND
RP 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 [65]
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 disulfide.";
RL J. Struct. Biol. 177:46-53(2012).
RN [66]
RP VARIANT CTRCT30 LYS-151, AND CHARACTERIZATION OF VARIANT CTRCT30 LYS-151.
RX PubMed=19126778; DOI=10.1093/hmg/ddn440;
RA Muller M., Bhattacharya S.S., Moore T., Prescott Q., Wedig T., Herrmann H.,
RA Magin T.M.;
RT "Dominant cataract formation in association with a vimentin assembly
RT disrupting mutation.";
RL Hum. Mol. Genet. 18:1052-1057(2009).
RN [67]
RP VARIANT CTRCT30 ARG-208.
RX PubMed=28450710; DOI=10.1038/s41598-017-01182-9;
RA Zhai Y., Li J., Yu W., Zhu S., Yu Y., Wu M., Sun G., Gong X., Yao K.;
RT "Targeted exome sequencing of congenital cataracts related genes:
RT broadening the mutation spectrum and genotype-phenotype correlations in 27
RT Chinese Han families.";
RL Sci. Rep. 7:1219-1219(2017).
CC -!- FUNCTION: Vimentins are class-III intermediate filaments found in
CC various non-epithelial cells, especially mesenchymal cells. Vimentin is
CC attached to the nucleus, endoplasmic reticulum, and mitochondria,
CC either laterally or terminally. {ECO:0000269|PubMed:21746880}.
CC -!- FUNCTION: Involved with LARP6 in the stabilization of type I collagen
CC mRNAs for CO1A1 and CO1A2. {ECO:0000269|PubMed:21746880}.
CC -!- SUBUNIT: Homomer assembled from elementary dimers (PubMed:20176112).
CC Identified in complexes that contain VIM, EZR, AHNAK, BFSP1, BFSP2,
CC ANK2, PLEC, PRX and spectrin (By similarity). Interacts with BCAS3
CC (PubMed:17505058). Interacts with LGSN (By similarity). Interacts with
CC SYNM (By similarity). Interacts (via rod region) with PLEC (via CH 1
CC domain) (By similarity). Interacts with PLEC isoform 1C
CC (PubMed:24940650). Interacts with STK33 (PubMed:18811945). Interacts
CC with LARP6 (PubMed:21746880). Interacts with RAB8B (By similarity).
CC Interacts with TOR1A; the interaction associates TOR1A with the
CC cytoskeleton (PubMed:16361107, PubMed:18827015). Interacts with
CC TOR1AIP1 (PubMed:16361107). Interacts with DIAPH1 (PubMed:23325789).
CC Interacts with EPPK1; interaction is dependent of higher-order
CC structure of intermediate filament (PubMed:16923132). Interacts with
CC the non-receptor tyrosine kinase SRMS; the interaction leads to
CC phosphorylation of VIM (PubMed:29496907). Interacts with NOD2
CC (PubMed:27812135). Interacts (via head region) with CORO1C (By
CC similarity). Interacts with HDGF (isoform 2) (PubMed:26845719).
CC Interacts with PRKCE (via phorbol-ester/DAG-type 2 domain)
CC (PubMed:18408015). Interacts with BFSP2 (By similarity). Interacts with
CC PPL (By similarity). {ECO:0000250|UniProtKB:P20152,
CC ECO:0000250|UniProtKB:P31000, ECO:0000269|PubMed:16361107,
CC ECO:0000269|PubMed:16923132, ECO:0000269|PubMed:17505058,
CC ECO:0000269|PubMed:18408015, ECO:0000269|PubMed:18811945,
CC ECO:0000269|PubMed:18827015, ECO:0000269|PubMed:20176112,
CC ECO:0000269|PubMed:21746880, ECO:0000269|PubMed:23325789,
CC ECO:0000269|PubMed:24940650, ECO:0000269|PubMed:26845719,
CC ECO:0000269|PubMed:27812135, ECO:0000269|PubMed:29496907}.
CC -!- SUBUNIT: (Microbial infection) Interacts with HCV core protein.
CC {ECO:0000269|PubMed:15846844}.
CC -!- INTERACTION:
CC P08670; Q6DHV7-2: ADAL; NbExp=3; IntAct=EBI-353844, EBI-18899653;
CC P08670; Q8N302-2: AGGF1; NbExp=3; IntAct=EBI-353844, EBI-25838028;
CC P08670; P54819: AK2; NbExp=3; IntAct=EBI-353844, EBI-1056291;
CC P08670; P31749: AKT1; NbExp=29; IntAct=EBI-353844, EBI-296087;
CC P08670; P31751: AKT2; NbExp=6; IntAct=EBI-353844, EBI-296058;
CC P08670; Q9H6L4: ARMC7; NbExp=3; IntAct=EBI-353844, EBI-742909;
CC P08670; Q6XD76: ASCL4; NbExp=3; IntAct=EBI-353844, EBI-10254793;
CC P08670; Q9UBB4: ATXN10; NbExp=3; IntAct=EBI-353844, EBI-702390;
CC P08670; Q9H6U6: BCAS3; NbExp=3; IntAct=EBI-353844, EBI-6083685;
CC P08670; Q14457: BECN1; NbExp=3; IntAct=EBI-353844, EBI-949378;
CC P08670; P51451: BLK; NbExp=3; IntAct=EBI-353844, EBI-2105445;
CC P08670; Q13895: BYSL; NbExp=3; IntAct=EBI-353844, EBI-358049;
CC P08670; Q8TAB5: C1orf216; NbExp=3; IntAct=EBI-353844, EBI-747505;
CC P08670; Q9UQM7: CAMK2A; NbExp=3; IntAct=EBI-353844, EBI-1383687;
CC P08670; Q9HC52: CBX8; NbExp=3; IntAct=EBI-353844, EBI-712912;
CC P08670; Q96HB5: CCDC120; NbExp=3; IntAct=EBI-353844, EBI-744556;
CC P08670; Q9Y3D0: CIAO2B; NbExp=3; IntAct=EBI-353844, EBI-744045;
CC P08670; Q14194: CRMP1; NbExp=3; IntAct=EBI-353844, EBI-473101;
CC P08670; Q8WUE5: CT55; NbExp=3; IntAct=EBI-353844, EBI-6873363;
CC P08670; Q2TBE0: CWF19L2; NbExp=3; IntAct=EBI-353844, EBI-5453285;
CC P08670; P17661: DES; NbExp=6; IntAct=EBI-353844, EBI-1055572;
CC P08670; A0A024RCP2: DOM3Z; NbExp=3; IntAct=EBI-353844, EBI-25847826;
CC P08670; Q6NXG1: ESRP1; NbExp=3; IntAct=EBI-353844, EBI-10213520;
CC P08670; Q3B820: FAM161A; NbExp=3; IntAct=EBI-353844, EBI-719941;
CC P08670; Q96GL9: FAM163A; NbExp=3; IntAct=EBI-353844, EBI-11793142;
CC P08670; O15287: FANCG; NbExp=3; IntAct=EBI-353844, EBI-81610;
CC P08670; P55040: GEM; NbExp=3; IntAct=EBI-353844, EBI-744104;
CC P08670; P14136: GFAP; NbExp=7; IntAct=EBI-353844, EBI-744302;
CC P08670; Q4G1C9-2: GLIPR1L2; NbExp=3; IntAct=EBI-353844, EBI-20835942;
CC P08670; Q96LI6: HSFY2; NbExp=3; IntAct=EBI-353844, EBI-3957665;
CC P08670; P83110-1: HTRA3; NbExp=4; IntAct=EBI-353844, EBI-25469082;
CC P08670; P83110-2: HTRA3; NbExp=5; IntAct=EBI-353844, EBI-22017714;
CC P08670; P42858: HTT; NbExp=4; IntAct=EBI-353844, EBI-466029;
CC P08670; Q0VD86: INCA1; NbExp=3; IntAct=EBI-353844, EBI-6509505;
CC P08670; Q92551: IP6K1; NbExp=3; IntAct=EBI-353844, EBI-751911;
CC P08670; O95251: KAT7; NbExp=4; IntAct=EBI-353844, EBI-473199;
CC P08670; Q6ZU52: KIAA0408; NbExp=4; IntAct=EBI-353844, EBI-739493;
CC P08670; Q9HAQ2: KIF9; NbExp=3; IntAct=EBI-353844, EBI-8472129;
CC P08670; Q9BVG8-5: KIFC3; NbExp=3; IntAct=EBI-353844, EBI-14069005;
CC P08670; O14901: KLF11; NbExp=3; IntAct=EBI-353844, EBI-948266;
CC P08670; P35900: KRT20; NbExp=8; IntAct=EBI-353844, EBI-742094;
CC P08670; O95678: KRT75; NbExp=3; IntAct=EBI-353844, EBI-2949715;
CC P08670; P05787: KRT8; NbExp=2; IntAct=EBI-353844, EBI-297852;
CC P08670; Q6IAA8: LAMTOR1; NbExp=3; IntAct=EBI-353844, EBI-715385;
CC P08670; Q14847-2: LASP1; NbExp=3; IntAct=EBI-353844, EBI-9088686;
CC P08670; Q8TCE9: LGALS14; NbExp=3; IntAct=EBI-353844, EBI-10274069;
CC P08670; Q6ZQX7-4: LIAT1; NbExp=3; IntAct=EBI-353844, EBI-25830459;
CC P08670; Q9NS73-5: MBIP; NbExp=3; IntAct=EBI-353844, EBI-10182361;
CC P08670; Q8IVT4: MGC50722; NbExp=3; IntAct=EBI-353844, EBI-14086479;
CC P08670; O76036: NCR1; NbExp=3; IntAct=EBI-353844, EBI-13915737;
CC P08670; I6L9F6: NEFL; NbExp=3; IntAct=EBI-353844, EBI-10178578;
CC P08670; P07196: NEFL; NbExp=3; IntAct=EBI-353844, EBI-475646;
CC P08670; P07197: NEFM; NbExp=5; IntAct=EBI-353844, EBI-1105035;
CC P08670; P48681: NES; NbExp=3; IntAct=EBI-353844, EBI-10966836;
CC P08670; Q8NI38: NFKBID; NbExp=3; IntAct=EBI-353844, EBI-10271199;
CC P08670; Q9HC29: NOD2; NbExp=7; IntAct=EBI-353844, EBI-7445625;
CC P08670; Q96IZ0: PAWR; NbExp=2; IntAct=EBI-353844, EBI-595869;
CC P08670; Q16512: PKN1; NbExp=3; IntAct=EBI-353844, EBI-602382;
CC P08670; Q13835-2: PKP1; NbExp=3; IntAct=EBI-353844, EBI-9087684;
CC P08670; Q96PV4: PNMA5; NbExp=6; IntAct=EBI-353844, EBI-10171633;
CC P08670; O60437: PPL; NbExp=3; IntAct=EBI-353844, EBI-368321;
CC P08670; Q6NYC8: PPP1R18; NbExp=3; IntAct=EBI-353844, EBI-2557469;
CC P08670; P41219: PRPH; NbExp=4; IntAct=EBI-353844, EBI-752074;
CC P08670; A0A0C4DFM3: PRUNE2; NbExp=3; IntAct=EBI-353844, EBI-25830870;
CC P08670; P54727: RAD23B; NbExp=2; IntAct=EBI-353844, EBI-954531;
CC P08670; Q9UJD0: RIMS3; NbExp=3; IntAct=EBI-353844, EBI-3909436;
CC P08670; Q9BWG6: SCNM1; NbExp=3; IntAct=EBI-353844, EBI-748391;
CC P08670; P12757: SKIL; NbExp=3; IntAct=EBI-353844, EBI-2902468;
CC P08670; Q12824: SMARCB1; NbExp=4; IntAct=EBI-353844, EBI-358419;
CC P08670; Q7Z614-3: SNX20; NbExp=3; IntAct=EBI-353844, EBI-12336127;
CC P08670; Q96BD6: SPSB1; NbExp=3; IntAct=EBI-353844, EBI-2659201;
CC P08670; Q99619: SPSB2; NbExp=3; IntAct=EBI-353844, EBI-2323209;
CC P08670; B7ZLI8: STK19; NbExp=3; IntAct=EBI-353844, EBI-10176124;
CC P08670; Q9H7C4: SYNC; NbExp=3; IntAct=EBI-353844, EBI-11285923;
CC P08670; O60506-4: SYNCRIP; NbExp=3; IntAct=EBI-353844, EBI-11123832;
CC P08670; O15273: TCAP; NbExp=3; IntAct=EBI-353844, EBI-954089;
CC P08670; Q15560: TCEA2; NbExp=3; IntAct=EBI-353844, EBI-710310;
CC P08670; P15923-3: TCF3; NbExp=3; IntAct=EBI-353844, EBI-12000326;
CC P08670; Q13428-5: TCOF1; NbExp=3; IntAct=EBI-353844, EBI-25832010;
CC P08670; Q5T1C6: THEM4; NbExp=3; IntAct=EBI-353844, EBI-7684443;
CC P08670; Q08117-2: TLE5; NbExp=3; IntAct=EBI-353844, EBI-11741437;
CC P08670; Q7Z403: TMC6; NbExp=3; IntAct=EBI-353844, EBI-9088037;
CC P08670; Q12888: TP53BP1; NbExp=3; IntAct=EBI-353844, EBI-396540;
CC P08670; Q14142: TRIM14; NbExp=3; IntAct=EBI-353844, EBI-2820256;
CC P08670; O95361: TRIM16; NbExp=3; IntAct=EBI-353844, EBI-727384;
CC P08670; Q9BQE3: TUBA1C; NbExp=3; IntAct=EBI-353844, EBI-1103245;
CC P08670; Q5VYS8-5: TUT7; NbExp=3; IntAct=EBI-353844, EBI-9088812;
CC P08670; Q8N3L3: TXLNB; NbExp=6; IntAct=EBI-353844, EBI-6116822;
CC P08670; Q08AM6: VAC14; NbExp=3; IntAct=EBI-353844, EBI-2107455;
CC P08670; P08670: VIM; NbExp=11; IntAct=EBI-353844, EBI-353844;
CC P08670; Q9H270: VPS11; NbExp=3; IntAct=EBI-353844, EBI-373380;
CC P08670; P63104: YWHAZ; NbExp=2; IntAct=EBI-353844, EBI-347088;
CC P08670; P26651: ZFP36; NbExp=3; IntAct=EBI-353844, EBI-374248;
CC P08670; P17024: ZNF20; NbExp=3; IntAct=EBI-353844, EBI-717634;
CC P08670; Q7Z3I7: ZNF572; NbExp=3; IntAct=EBI-353844, EBI-10172590;
CC P08670; PRO_0000449633 [P0DTD1]: rep; Xeno; NbExp=3; IntAct=EBI-353844, EBI-25492395;
CC P08670; PRO_0000037966 [P14340]; Xeno; NbExp=10; IntAct=EBI-353844, EBI-9844509;
CC P08670; PRO_0000037566 [P27958]; Xeno; NbExp=4; IntAct=EBI-353844, EBI-6377335;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21465480,
CC ECO:0000269|PubMed:29496907}. Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:18408015, ECO:0000269|PubMed:29496907}. Nucleus
CC matrix {ECO:0000250|UniProtKB:P31000}. Cell membrane
CC {ECO:0000250|UniProtKB:P20152}.
CC -!- TISSUE SPECIFICITY: Highly expressed in fibroblasts, some expression in
CC T- and B-lymphocytes, and little or no expression in Burkitt's lymphoma
CC cell lines. Expressed in many hormone-independent mammary carcinoma
CC cell lines. {ECO:0000269|PubMed:2472876, ECO:0000269|PubMed:3371665}.
CC -!- INDUCTION: Up-regulated by muramyl-dipeptide and lipopolysaccharide.
CC {ECO:0000269|PubMed:27812135}.
CC -!- DOMAIN: The central alpha-helical coiled-coil IF rod domain mediates
CC elementary homodimerization.
CC -!- DOMAIN: The [IL]-x-C-x-x-[DE] motif is a proposed target motif for
CC cysteine S-nitrosylation mediated by the iNOS-S100A8/A9
CC transnitrosylase complex. {ECO:0000305|PubMed:25417112}.
CC -!- PTM: Filament disassembly during mitosis is promoted by phosphorylation
CC at Ser-55 as well as by nestin (By similarity). One of the most
CC prominent phosphoproteins in various cells of mesenchymal origin.
CC Phosphorylation is enhanced during cell division, at which time
CC vimentin filaments are significantly reorganized. Phosphorylation by
CC PKN1 inhibits the formation of filaments. Phosphorylated at Ser-56 by
CC CDK5 during neutrophil secretion in the cytoplasm (PubMed:21465480).
CC Phosphorylated by STK33 (PubMed:18811945). Phosphorylated on tyrosine
CC residues by SRMS (PubMed:29496907). {ECO:0000250|UniProtKB:P31000,
CC ECO:0000269|PubMed:18811945, ECO:0000269|PubMed:21465480,
CC ECO:0000269|PubMed:29496907, ECO:0000269|Ref.14}.
CC -!- PTM: O-glycosylated during cytokinesis at sites identical or close to
CC phosphorylation sites, this interferes with the phosphorylation status.
CC {ECO:0000269|PubMed:20068230}.
CC -!- PTM: S-nitrosylation is induced by interferon-gamma and oxidatively-
CC modified low-densitity lipoprotein (LDL(ox)) possibly implicating the
CC iNOS-S100A8/9 transnitrosylase complex. {ECO:0000305|PubMed:25417112}.
CC -!- DISEASE: Cataract 30, multiple types (CTRCT30) [MIM:116300]: An
CC opacification of the crystalline lens of the eye that frequently
CC results in visual impairment or blindness. Opacities vary in
CC morphology, are often confined to a portion of the lens, and may be
CC static or progressive. In general, the more posteriorly located and
CC dense an opacity, the greater the impact on visual function.
CC {ECO:0000269|PubMed:19126778, ECO:0000269|PubMed:26694549,
CC ECO:0000269|PubMed:28450710}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the intermediate filament family.
CC {ECO:0000255|PROSITE-ProRule:PRU01188}.
CC -!- CAUTION: Was reported to interact with SLC6A4, however the paper was
CC retracted as some results and conclusions are not reliable.
CC {ECO:0000269|PubMed:19270731, ECO:0000305|PubMed:30707744}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB71275.1; Type=Miscellaneous discrepancy; Note=Product of a cloning artifact.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Vimentin entry;
CC URL="https://en.wikipedia.org/wiki/Vimentin";
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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_SEQ; 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; -; NOT_ANNOTATED_CDS; 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 CCDS; CCDS7120.1; -.
DR PIR; S13115; A25074.
DR RefSeq; NP_003371.2; NM_003380.3.
DR RefSeq; XP_006717563.1; XM_006717500.1.
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 PDB; 4MCY; X-ray; 2.30 A; C=66-78.
DR PDB; 4MCZ; X-ray; 2.41 A; C=59-71.
DR PDB; 4MD0; X-ray; 2.19 A; C=59-71.
DR PDB; 4MD5; X-ray; 1.65 A; C=66-78.
DR PDB; 4MDI; X-ray; 2.00 A; C=66-78.
DR PDB; 4MDJ; X-ray; 1.70 A; C=66-78.
DR PDB; 4YPC; X-ray; 1.44 A; A=161-243.
DR PDB; 4YV3; X-ray; 2.00 A; A/B/C=161-238.
DR PDB; 5WHF; X-ray; 2.25 A; A/B/C/D/E/F/G/H=153-238.
DR PDB; 6ATF; X-ray; 1.90 A; C/F=59-71.
DR PDB; 6ATI; X-ray; 1.98 A; C/F=59-71.
DR PDB; 6BIR; X-ray; 2.30 A; C=419-431.
DR PDB; 6YXK; X-ray; 2.00 A; C=59-74.
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 PDBsum; 4MCY; -.
DR PDBsum; 4MCZ; -.
DR PDBsum; 4MD0; -.
DR PDBsum; 4MD5; -.
DR PDBsum; 4MDI; -.
DR PDBsum; 4MDJ; -.
DR PDBsum; 4YPC; -.
DR PDBsum; 4YV3; -.
DR PDBsum; 5WHF; -.
DR PDBsum; 6ATF; -.
DR PDBsum; 6ATI; -.
DR PDBsum; 6BIR; -.
DR PDBsum; 6YXK; -.
DR AlphaFoldDB; P08670; -.
DR SMR; P08670; -.
DR BioGRID; 113272; 655.
DR CORUM; P08670; -.
DR DIP; DIP-32507N; -.
DR IntAct; P08670; 334.
DR MINT; P08670; -.
DR STRING; 9606.ENSP00000446007; -.
DR ChEMBL; CHEMBL3712854; -.
DR DrugBank; DB11638; Artenimol.
DR DrugBank; DB12695; Phenethyl Isothiocyanate.
DR MoonDB; P08670; Predicted.
DR CarbonylDB; P08670; -.
DR GlyConnect; 2867; 1 O-Linked glycan (3 sites).
DR GlyGen; P08670; 17 sites, 2 O-linked glycans (17 sites).
DR iPTMnet; P08670; -.
DR MetOSite; P08670; -.
DR PhosphoSitePlus; P08670; -.
DR SwissPalm; P08670; -.
DR BioMuta; VIM; -.
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 CPTAC; CPTAC-1017; -.
DR CPTAC; CPTAC-1018; -.
DR CPTAC; CPTAC-1036; -.
DR CPTAC; CPTAC-1303; -.
DR CPTAC; CPTAC-297; -.
DR CPTAC; CPTAC-298; -.
DR EPD; P08670; -.
DR jPOST; P08670; -.
DR MassIVE; P08670; -.
DR PaxDb; P08670; -.
DR PeptideAtlas; P08670; -.
DR PRIDE; P08670; -.
DR ProteomicsDB; 52153; -.
DR TopDownProteomics; P08670; -.
DR ABCD; P08670; 12 sequenced antibodies.
DR Antibodypedia; 938; 3618 antibodies from 58 providers.
DR DNASU; 7431; -.
DR Ensembl; ENST00000224237.9; ENSP00000224237.5; ENSG00000026025.16.
DR Ensembl; ENST00000544301.7; ENSP00000446007.1; ENSG00000026025.16.
DR GeneID; 7431; -.
DR KEGG; hsa:7431; -.
DR MANE-Select; ENST00000544301.7; ENSP00000446007.1; NM_003380.5; NP_003371.2.
DR CTD; 7431; -.
DR DisGeNET; 7431; -.
DR GeneCards; VIM; -.
DR HGNC; HGNC:12692; VIM.
DR HPA; ENSG00000026025; Low tissue specificity.
DR MalaCards; VIM; -.
DR MIM; 116300; phenotype.
DR MIM; 193060; gene.
DR neXtProt; NX_P08670; -.
DR OpenTargets; ENSG00000026025; -.
DR Orphanet; 98984; Pulverulent cataract.
DR PharmGKB; PA37311; -.
DR VEuPathDB; HostDB:ENSG00000026025; -.
DR eggNOG; KOG0977; Eukaryota.
DR GeneTree; ENSGT00940000156146; -.
DR InParanoid; P08670; -.
DR OMA; PPMRLHD; -.
DR OrthoDB; 655109at2759; -.
DR PhylomeDB; P08670; -.
DR TreeFam; TF330122; -.
DR PathwayCommons; P08670; -.
DR Reactome; R-HSA-264870; Caspase-mediated cleavage of cytoskeletal proteins.
DR Reactome; R-HSA-390522; Striated Muscle Contraction.
DR Reactome; R-HSA-6785807; Interleukin-4 and Interleukin-13 signaling.
DR Reactome; R-HSA-9013422; RHOBTB1 GTPase cycle.
DR Reactome; R-HSA-9613829; Chaperone Mediated Autophagy.
DR Reactome; R-HSA-9615710; Late endosomal microautophagy.
DR Reactome; R-HSA-9646399; Aggrephagy.
DR SignaLink; P08670; -.
DR SIGNOR; P08670; -.
DR BioGRID-ORCS; 7431; 9 hits in 1085 CRISPR screens.
DR ChiTaRS; VIM; human.
DR EvolutionaryTrace; P08670; -.
DR GeneWiki; Vimentin; -.
DR GenomeRNAi; 7431; -.
DR Pharos; P08670; Tbio.
DR PRO; PR:P08670; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; P08670; protein.
DR Bgee; ENSG00000026025; Expressed in ventricular zone and 214 other tissues.
DR ExpressionAtlas; P08670; baseline and differential.
DR Genevisible; P08670; HS.
DR GO; GO:0030424; C:axon; IBA:GO_Central.
DR GO; GO:0031252; C:cell leading edge; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; IDA:MGI.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
DR GO; GO:0005882; C:intermediate filament; IDA:UniProtKB.
DR GO; GO:0045111; C:intermediate filament cytoskeleton; IDA:HPA.
DR GO; GO:0005815; C:microtubule organizing center; TAS:Reactome.
DR GO; GO:0016363; C:nuclear matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005777; C:peroxisome; IDA:UniProtKB.
DR GO; GO:0045335; C:phagocytic vesicle; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0005844; C:polysome; IDA:UniProtKB.
DR GO; GO:1990904; C:ribonucleoprotein complex; IDA:UniProtKB.
DR GO; GO:0003725; F:double-stranded RNA binding; IDA:MGI.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:1990254; F:keratin filament binding; IPI:AgBase.
DR GO; GO:0019904; F:protein domain specific binding; IPI:UniProtKB.
DR GO; GO:0097110; F:scaffold protein binding; IPI:BHF-UCL.
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:0071346; P:cellular response to interferon-gamma; IEA:Ensembl.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IMP:UniProtKB.
DR GO; GO:0071225; P:cellular response to muramyl dipeptide; IMP:UniProtKB.
DR GO; GO:0045109; P:intermediate filament organization; ISS:UniProtKB.
DR GO; GO:0070307; P:lens fiber cell development; IEA:Ensembl.
DR GO; GO:0010977; P:negative regulation of neuron projection development; IEA:Ensembl.
DR GO; GO:0031175; P:neuron projection development; IEA:Ensembl.
DR GO; GO:0032967; P:positive regulation of collagen biosynthetic process; IMP:UniProtKB.
DR GO; GO:0045727; P:positive regulation of translation; IMP:UniProtKB.
DR GO; GO:0043488; P:regulation of mRNA stability; IMP:UniProtKB.
DR GO; GO:0060395; P:SMAD protein signal transduction; IEA:Ensembl.
DR DisProt; DP02862; -.
DR InterPro; IPR018039; IF_conserved.
DR InterPro; IPR039008; IF_rod_dom.
DR InterPro; IPR006821; Intermed_filament_DNA-bd.
DR InterPro; IPR027699; Vimentin.
DR PANTHER; PTHR45652:SF5; PTHR45652:SF5; 1.
DR Pfam; PF00038; Filament; 1.
DR Pfam; PF04732; Filament_head; 1.
DR SMART; SM01391; Filament; 1.
DR PROSITE; PS00226; IF_ROD_1; 1.
DR PROSITE; PS51842; IF_ROD_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cataract; Cell membrane; Coiled coil; Cytoplasm;
KW Cytoskeleton; Direct protein sequencing; Disease variant; Glycoprotein;
KW Host-virus interaction; Intermediate filament; Isopeptide bond; Membrane;
KW Nucleus; Phosphoprotein; Reference proteome; S-nitrosylation;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.13"
FT CHAIN 2..466
FT /note="Vimentin"
FT /id="PRO_0000063754"
FT DOMAIN 103..411
FT /note="IF rod"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2..95
FT /note="Head"
FT REGION 96..131
FT /note="Coil 1A"
FT REGION 132..153
FT /note="Linker 1"
FT REGION 154..245
FT /note="Coil 1B"
FT REGION 246..268
FT /note="Linker 12"
FT REGION 269..407
FT /note="Coil 2"
FT REGION 408..466
FT /note="Tail"
FT COILED 96..131
FT /evidence="ECO:0000269|PubMed:20176112"
FT COILED 154..245
FT /evidence="ECO:0000269|PubMed:20176112"
FT COILED 303..407
FT /evidence="ECO:0000269|PubMed:20176112"
FT MOTIF 326..329
FT /note="[IL]-x-C-x-x-[DE] motif"
FT /evidence="ECO:0000305|PubMed:25417112"
FT SITE 351
FT /note="Stutter"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|Ref.13"
FT MOD_RES 5
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:14762106,
FT ECO:0007744|PubMed:18669648"
FT MOD_RES 7
FT /note="Phosphoserine; by PKA and PKC; alternate"
FT /evidence="ECO:0000269|PubMed:14762106"
FT MOD_RES 8
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:14762106"
FT MOD_RES 9
FT /note="Phosphoserine; by PKC"
FT /evidence="ECO:0000269|PubMed:14762106"
FT MOD_RES 10
FT /note="Phosphoserine; by PKC"
FT /evidence="ECO:0000269|PubMed:14762106"
FT MOD_RES 20
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 25
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 26
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 34
FT /note="Phosphoserine; by PKC; alternate"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 39
FT /note="Phosphoserine; by CaMK2, PKA, PKC and ROCK2"
FT /evidence="ECO:0000269|PubMed:14762106,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 42
FT /note="Phosphoserine; by PKC"
FT /evidence="ECO:0000269|PubMed:14762106,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 47
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 49
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 51
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 53
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P20152"
FT MOD_RES 55
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P31000"
FT MOD_RES 56
FT /note="Phosphoserine; by CDK5 and CDK1"
FT /evidence="ECO:0000269|PubMed:21465480, ECO:0000269|Ref.14,
FT ECO:0007744|PubMed:16964243, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 61
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
FT MOD_RES 66
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 72
FT /note="Phosphoserine; by AURKB and ROCK2"
FT /evidence="ECO:0000269|PubMed:12458200,
FT ECO:0000269|PubMed:14762106, ECO:0007744|PubMed:18669648"
FT MOD_RES 73
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:14762106,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 83
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:24275569"
FT MOD_RES 87
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 117
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:15592455"
FT MOD_RES 120
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 120
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P20152"
FT MOD_RES 129
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P20152"
FT MOD_RES 129
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P20152"
FT MOD_RES 139
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 144
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692"
FT MOD_RES 168
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P20152"
FT MOD_RES 188
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P20152"
FT MOD_RES 188
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P20152"
FT MOD_RES 214
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 223
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P20152"
FT MOD_RES 226
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 235
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P20152"
FT MOD_RES 294
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P20152"
FT MOD_RES 294
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P20152"
FT MOD_RES 299
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 325
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P20152"
FT MOD_RES 373
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 409
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 412
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:17924679, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231"
FT MOD_RES 419
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 420
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:14762106,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 426
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 430
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:14762106,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 436
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 438
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 445
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 445
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P20152"
FT MOD_RES 446
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 458
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:14762106"
FT MOD_RES 459
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:14762106,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT CARBOHYD 7
FT /note="O-linked (GlcNAc) serine; alternate"
FT /evidence="ECO:0000269|PubMed:20068230"
FT CARBOHYD 33
FT /note="O-linked (GlcNAc) threonine"
FT /evidence="ECO:0000269|PubMed:20068230"
FT CARBOHYD 34
FT /note="O-linked (GlcNAc) serine; alternate"
FT /evidence="ECO:0000269|PubMed:20068230"
FT CROSSLNK 104
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 120
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 129
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 139
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 223
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 262
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 294
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 313
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 373
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 439
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 445
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0007744|PubMed:25114211"
FT CROSSLNK 445
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:25114211,
FT ECO:0007744|PubMed:28112733"
FT VARIANT 151
FT /note="E -> K (in CTRCT30; the mutation increases the
FT proteasome activity in transfected cells; causes also a
FT severe kinetic defect in vimentin assembly both in vitro
FT and in vivo; dbSNP:rs121917775)"
FT /evidence="ECO:0000269|PubMed:19126778"
FT /id="VAR_070100"
FT VARIANT 208
FT /note="Q -> R (in CTRCT30; unknown pathological
FT significance; dbSNP:rs1085307141)"
FT /evidence="ECO:0000269|PubMed:28450710"
FT /id="VAR_078860"
FT CONFLICT 42
FT /note="S -> D (in Ref. 1; AAA61279)"
FT /evidence="ECO:0000305"
FT CONFLICT 113
FT /note="R -> P (in Ref. 12; CAA34499)"
FT /evidence="ECO:0000305"
FT CONFLICT 197
FT /note="E -> G (in Ref. 6; CAG28618)"
FT /evidence="ECO:0000305"
FT CONFLICT 201
FT /note="N -> S (in Ref. 17; AAA61281)"
FT /evidence="ECO:0000305"
FT CONFLICT 265
FT /note="L -> S (in Ref. 17; AAA61281)"
FT /evidence="ECO:0000305"
FT CONFLICT 278
FT /note="S -> I (in Ref. 17; AAA61281)"
FT /evidence="ECO:0000305"
FT CONFLICT 339
FT /note="S -> C (in Ref. 17; AAA61281)"
FT /evidence="ECO:0000305"
FT CONFLICT 350
FT /note="N -> K (in Ref. 17; AAA61281)"
FT /evidence="ECO:0000305"
FT CONFLICT 442
FT /note="L -> F (in Ref. 1; AAA61279)"
FT /evidence="ECO:0000305"
FT HELIX 101..135
FT /evidence="ECO:0007829|PDB:1GK7"
FT HELIX 167..235
FT /evidence="ECO:0007829|PDB:4YPC"
FT STRAND 238..241
FT /evidence="ECO:0007829|PDB:4YPC"
FT TURN 244..248
FT /evidence="ECO:0007829|PDB:3UF1"
FT HELIX 266..334
FT /evidence="ECO:0007829|PDB:3TRT"
FT HELIX 385..405
FT /evidence="ECO:0007829|PDB:1GK6"
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
