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 27-MAR-2024, entry version 271. 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 INTERACTION WITH PKP1 AND PKP2. RX PubMed=10852826; DOI=10.1242/jcs.113.13.2471; RA Hofmann I., Mertens C., Brettel M., Nimmrich V., Schnoelzer M., RA Herrmann H.; RT "Interaction of plakophilins with desmoplakin and intermediate filament RT proteins: an in vitro analysis."; RL J. Cell Sci. 113:2471-2483(2000). RN [21] 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 [22] 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 [23] 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 [24] 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 [25] 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 [26] 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 [27] 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 [28] 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 [29] 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 [30] 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 [31] 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 [32] 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 [33] 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 [34] 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 [35] 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 [36] 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 [37] 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 [38] 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 [39] 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 [40] 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 [41] 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 [42] 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 [43] 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 [44] 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 [45] 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 [46] 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 [47] 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 [48] 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 [49] 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 [50] 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 [51] 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 [52] 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 [53] 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 [54] 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 [55] 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 [56] 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 [57] 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 [58] 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 [59] 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 [60] 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 [61] 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 [62] 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 [63] 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 [64] 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 [65] 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 [66] 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 [67] 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 [68] 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:0000250|UniProtKB:P31000}. 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). Interacts (via rod domain) with PKP1 CC (PubMed:10852826). Interacts with PKP2 (PubMed:10852826). CC {ECO:0000250|UniProtKB:P20152, ECO:0000250|UniProtKB:P31000, CC ECO:0000269|PubMed:10852826, 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; Q9BYF1: ACE2; NbExp=4; IntAct=EBI-353844, EBI-7730807; 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; Q9Y4K0: LOXL2; NbExp=6; IntAct=EBI-353844, EBI-7172227; 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; Q8WUY3: PRUNE2; NbExp=3; IntAct=EBI-353844, EBI-743880; 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=3; 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=4; IntAct=EBI-353844, EBI-25492395; CC P08670; P0DTC2: S; Xeno; NbExp=4; IntAct=EBI-353844, EBI-25474821; 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"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 750. DR CORUM; P08670; -. DR DIP; DIP-32507N; -. DR IntAct; P08670; 349. 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-GlcNAc glycan (3 sites). DR GlyCosmos; P08670; 17 sites, 2 glycans. DR GlyGen; P08670; 27 sites, 2 O-linked glycans (27 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 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; 9606-ENSP00000446007; -. DR PeptideAtlas; P08670; -. DR PRIDE; P08670; -. DR ProteomicsDB; 52153; -. DR Pumba; P08670; -. DR TopDownProteomics; P08670; -. DR ABCD; P08670; 12 sequenced antibodies. DR Antibodypedia; 938; 4214 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 AGR; HGNC:12692; -. 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; GGMYATK; -. DR OrthoDB; 4640531at2759; -. 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 1163 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 216 other cell types or tissues. DR ExpressionAtlas; P08670; baseline and differential. 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: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:0060090; F:molecular adaptor activity; EXP:DisProt. 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:0071222; P:cellular response to lipopolysaccharide; IMP:UniProtKB. DR GO; GO:0071225; P:cellular response to muramyl dipeptide; IMP:UniProtKB. DR GO; GO:0071346; P:cellular response to type II interferon; IEA:Ensembl. 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:0010628; P:positive regulation of gene expression; IEA:Ensembl. DR GO; GO:0043488; P:regulation of mRNA stability; IMP:UniProtKB. DR DisProt; DP02862; -. DR Gene3D; 1.20.5.170; -; 1. DR Gene3D; 1.20.5.500; Single helix bin; 1. DR Gene3D; 1.20.5.1160; Vasodilator-stimulated phosphoprotein; 1. DR InterPro; IPR018039; IF_conserved. DR InterPro; IPR039008; IF_rod_dom. DR InterPro; IPR006821; Intermed_filament_DNA-bd. DR PANTHER; PTHR45652; GLIAL FIBRILLARY ACIDIC PROTEIN; 1. DR PANTHER; PTHR45652:SF5; VIMENTIN; 1. DR Pfam; PF00038; Filament; 1. DR Pfam; PF04732; Filament_head; 1. DR SMART; SM01391; Filament; 1. DR SUPFAM; SSF64593; Intermediate filament protein, coiled coil region; 2. DR PROSITE; PS00226; IF_ROD_1; 1. DR PROSITE; PS51842; IF_ROD_2; 1. DR SWISS-2DPAGE; P08670; -. DR UCD-2DPAGE; P08670; -. DR Genevisible; P08670; HS. 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; uncertain significance; FT 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 //