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Vimentin

 F6SFE6_MONDO            Unreviewed;       454 AA.
F6SFE6;
27-JUL-2011, integrated into UniProtKB/TrEMBL.
09-JAN-2013, sequence version 2.
05-JUN-2019, entry version 57.
SubName: Full=Vimentin {ECO:0000313|Ensembl:ENSMODP00000012279};
Name=VIM {ECO:0000313|Ensembl:ENSMODP00000012279};
Monodelphis domestica (Gray short-tailed opossum).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Metatheria; Didelphimorphia; Didelphidae; Monodelphis.
NCBI_TaxID=13616 {ECO:0000313|Ensembl:ENSMODP00000012279, ECO:0000313|Proteomes:UP000002280};
[1] {ECO:0000313|Ensembl:ENSMODP00000012279, ECO:0000313|Proteomes:UP000002280}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=17495919; DOI=10.1038/nature05805;
Mikkelsen T.S., Wakefield M.J., Aken B., Amemiya C.T., Chang J.L.,
Duke S., Garber M., Gentles A.J., Goodstadt L., Heger A., Jurka J.,
Kamal M., Mauceli E., Searle S.M., Sharpe T., Baker M.L., Batzer M.A.,
Benos P.V., Belov K., Clamp M., Cook A., Cuff J., Das R., Davidow L.,
Deakin J.E., Fazzari M.J., Glass J.L., Grabherr M., Greally J.M.,
Gu W., Hore T.A., Huttley G.A., Kleber M., Jirtle R.L., Koina E.,
Lee J.T., Mahony S., Marra M.A., Miller R.D., Nicholls R.D., Oda M.,
Papenfuss A.T., Parra Z.E., Pollock D.D., Ray D.A., Schein J.E.,
Speed T.P., Thompson K., VandeBerg J.L., Wade C.M., Walker J.A.,
Waters P.D., Webber C., Weidman J.R., Xie X., Zody M.C., Baldwin J.,
Abdouelleil A., Abdulkadir J., Abebe A., Abera B., Abreu J.,
Acer S.C., Aftuck L., Alexander A., An P., Anderson E., Anderson S.,
Arachi H., Azer M., Bachantsang P., Barry A., Bayul T., Berlin A.,
Bessette D., Bloom T., Bloom T., Boguslavskiy L., Bonnet C.,
Boukhgalter B., Bourzgui I., Brown A., Cahill P., Channer S.,
Cheshatsang Y., Chuda L., Citroen M., Collymore A., Cooke P.,
Costello M., D'Aco K., Daza R., De Haan G., DeGray S., DeMaso C.,
Dhargay N., Dooley K., Dooley E., Doricent M., Dorje P., Dorjee K.,
Dupes A., Elong R., Falk J., Farina A., Faro S., Ferguson D.,
Fisher S., Foley C.D., Franke A., Friedrich D., Gadbois L., Gearin G.,
Gearin C.R., Giannoukos G., Goode T., Graham J., Grandbois E.,
Grewal S., Gyaltsen K., Hafez N., Hagos B., Hall J., Henson C.,
Hollinger A., Honan T., Huard M.D., Hughes L., Hurhula B., Husby M.E.,
Kamat A., Kanga B., Kashin S., Khazanovich D., Kisner P., Lance K.,
Lara M., Lee W., Lennon N., Letendre F., LeVine R., Lipovsky A.,
Liu X., Liu J., Liu S., Lokyitsang T., Lokyitsang Y., Lubonja R.,
Lui A., MacDonald P., Magnisalis V., Maru K., Matthews C.,
McCusker W., McDonough S., Mehta T., Meldrim J., Meneus L., Mihai O.,
Mihalev A., Mihova T., Mittelman R., Mlenga V., Montmayeur A.,
Mulrain L., Navidi A., Naylor J., Negash T., Nguyen T., Nguyen N.,
Nicol R., Norbu C., Norbu N., Novod N., O'Neill B., Osman S.,
Markiewicz E., Oyono O.L., Patti C., Phunkhang P., Pierre F.,
Priest M., Raghuraman S., Rege F., Reyes R., Rise C., Rogov P.,
Ross K., Ryan E., Settipalli S., Shea T., Sherpa N., Shi L., Shih D.,
Sparrow T., Spaulding J., Stalker J., Stange-Thomann N.,
Stavropoulos S., Stone C., Strader C., Tesfaye S., Thomson T.,
Thoulutsang Y., Thoulutsang D., Topham K., Topping I., Tsamla T.,
Vassiliev H., Vo A., Wangchuk T., Wangdi T., Weiand M., Wilkinson J.,
Wilson A., Yadav S., Young G., Yu Q., Zembek L., Zhong D., Zimmer A.,
Zwirko Z., Jaffe D.B., Alvarez P., Brockman W., Butler J., Chin C.,
Gnerre S., MacCallum I., Graves J.A., Ponting C.P., Breen M.,
Samollow P.B., Lander E.S., Lindblad-Toh K.;
"Genome of the marsupial Monodelphis domestica reveals innovation in
non-coding sequences.";
Nature 447:167-177(2007).
[2] {ECO:0000313|Ensembl:ENSMODP00000012279}
IDENTIFICATION.
Ensembl;
Submitted (JUL-2011) to UniProtKB.
-!- SIMILARITY: Belongs to the intermediate filament family.
{ECO:0000256|PROSITE-ProRule:PRU01188,
ECO:0000256|RuleBase:RU000685, ECO:0000256|SAAS:SAAS01036505}.
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STRING; 13616.ENSMODP00000012279; -.
Ensembl; ENSMODT00000012504; ENSMODP00000012279; ENSMODG00000009818.
eggNOG; ENOG410IFZ1; Eukaryota.
eggNOG; ENOG410XRBS; LUCA.
GeneTree; ENSGT00940000156146; -.
InParanoid; F6SFE6; -.
OMA; QVINEST; -.
TreeFam; TF330122; -.
Proteomes; UP000002280; Chromosome 8.
Bgee; ENSMODG00000009818; Expressed in 8 organ(s), highest expression level in female gonad.
GO; GO:0031252; C:cell leading edge; IEA:Ensembl.
GO; GO:0005829; C:cytosol; IEA:Ensembl.
GO; GO:0005882; C:intermediate filament; IEA:UniProtKB-KW.
GO; GO:0043005; C:neuron projection; IEA:Ensembl.
GO; GO:0005777; C:peroxisome; IEA:Ensembl.
GO; GO:0045335; C:phagocytic vesicle; IEA:Ensembl.
GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
GO; GO:0005844; C:polysome; IEA:Ensembl.
GO; GO:0003725; F:double-stranded RNA binding; IEA:Ensembl.
GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
GO; GO:1990254; F:keratin filament binding; IEA:Ensembl.
GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl.
GO; GO:0097110; F:scaffold protein binding; IEA:Ensembl.
GO; GO:0005200; F:structural constituent of cytoskeleton; IEA:Ensembl.
GO; GO:0005212; F:structural constituent of eye lens; IEA:Ensembl.
GO; GO:0014002; P:astrocyte development; IEA:Ensembl.
GO; GO:0060020; P:Bergmann glial cell differentiation; IEA:Ensembl.
GO; GO:0071346; P:cellular response to interferon-gamma; IEA:Ensembl.
GO; GO:0071222; P:cellular response to lipopolysaccharide; IEA:Ensembl.
GO; GO:0071225; P:cellular response to muramyl dipeptide; IEA:Ensembl.
GO; GO:0045109; P:intermediate filament organization; IEA:Ensembl.
GO; GO:0070307; P:lens fiber cell development; IEA:Ensembl.
GO; GO:0010977; P:negative regulation of neuron projection development; IEA:Ensembl.
GO; GO:0032967; P:positive regulation of collagen biosynthetic process; IEA:Ensembl.
GO; GO:0045727; P:positive regulation of translation; IEA:Ensembl.
GO; GO:0043488; P:regulation of mRNA stability; IEA:Ensembl.
GO; GO:0060395; P:SMAD protein signal transduction; IEA:Ensembl.
Gene3D; 1.20.5.1160; -; 1.
InterPro; IPR018039; IF_conserved.
InterPro; IPR039008; IF_rod_dom.
InterPro; IPR042180; IF_rod_dom_coil1B.
InterPro; IPR006821; Intermed_filament_DNA-bd.
InterPro; IPR027699; Vimentin.
PANTHER; PTHR45652:SF5; PTHR45652:SF5; 1.
Pfam; PF00038; Filament; 1.
Pfam; PF04732; Filament_head; 1.
SMART; SM01391; Filament; 1.
PROSITE; PS00226; IF_ROD_1; 1.
PROSITE; PS51842; IF_ROD_2; 1.
3: Inferred from homology;
Coiled coil {ECO:0000256|PROSITE-ProRule:PRU01188,
ECO:0000256|SAAS:SAAS01036532, ECO:0000256|SAM:Coils};
Complete proteome {ECO:0000313|Proteomes:UP000002280};
Intermediate filament {ECO:0000256|PROSITE-ProRule:PRU01188,
ECO:0000256|RuleBase:RU000685, ECO:0000256|SAAS:SAAS01036494};
Reference proteome {ECO:0000313|Proteomes:UP000002280}.
DOMAIN 91 399 IF rod. {ECO:0000259|PROSITE:PS51842}.
COILED 81 129 {ECO:0000256|SAM:Coils}.
COILED 135 243 {ECO:0000256|SAM:Coils}.
COILED 283 377 {ECO:0000256|SAM:Coils}.
SEQUENCE 454 AA; 52163 MW; 3BF4C1E9760077F5 CRC64;
MFGGSSTGGR PSASRSYVTS TTRYSLGSAI RPSTTRSVYS SSPGAVYATR SSAARLRSSA
PIPGVRLLQD SVDFSLADAI NTEFKNTRTN EKVELQELND RFANYIDKVR FLEQQNKILL
AELEQLKGQG KSRLGDLYEE EMRELRRQVD QLTNDKARVE VERDNLAEDI MRLREKLQEE
MLQREEAEST LQSFRQDVDN ASLARLDLER KVESLQEEIA FLKKLHDEEI QELQAQIQEQ
HIQIDVDVAK PDLTAALRDV RQQYESVAAK NLQEAEEWYK SKFADLSEAA NRNNDALRQA
KQESNEYRRQ VQSLTCEVDA LKGTNESLER QMREMEENFA VEAANYQDTI GRLQDEIQNM
KEEMARHLRE YQDLLNVKMA LDIEIATYRK LLEGEESRIA LPLPNFSSLN LRETNLDSLP
LVDTHSKRTL LIKTVETRDG QVINETSQHH DDLE


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1C-460-C100 Mouse Monoclonal to Vimentin Antigen Vimentin Isotype IgM Antigen Vimentin Isotype IgM 0.1 mg
1C-460-C025 Mouse Monoclonal to Vimentin Antigen Vimentin Isotype IgM Antigen Vimentin Isotype IgM 0.025 mg
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Pathways :
No related Items

Related Genes :
[VIM] Vimentin
[Vim] Vimentin
[Vim] Vimentin
[VIM] Vimentin
[VIM] Vimentin
[VIM QtrA-12155] Vimentin
[Ctsg] Cathepsin G (EC 3.4.21.20) (Vimentin-specific protease) (VSP)
[NCKIPSD AF3P21 SPIN90] NCK-interacting protein with SH3 domain (54 kDa VacA-interacting protein) (54 kDa vimentin-interacting protein) (VIP54) (90 kDa SH3 protein interacting with Nck) (AF3p21) (Dia-interacting protein 1) (DIP-1) (Diaphanous protein-interacting protein) (SH3 adapter protein SPIN90) (WASP-interacting SH3-domain protein) (WISH) (Wiskott-Aldrich syndrome protein-interacting protein)
[VIM] Vimentin
[VIM] Vimentin
[VIM] Vimentin (Fragment)
[VIM] Vimentin
[VIM] Vimentin
[VIM] Vimentin
[VIM] Vimentin (Fragment)
[Vim rCG_55877] Vimentin (Vimentin, isoform CRA_b)
[vim] Vimentin
[VIM] Vimentin
[VIM] Vimentin
[VIM] Vimentin
[VIM] Vimentin
[VIM] Vimentin
[VIM] Vimentin
[VIM CK820_G0041162] VIM isoform 1 (VIM isoform 2) (VIM isoform 5) (Vimentin)
[VIM] Vimentin
[VIM] Vimentin
[VIM] vimentin
[Vim] vimentin
[VIM RLOC_00011576] Vimentin
[vim1; vim2] Vimentin-1/2

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[31298565] Adipose-Derived Stem/Stromal Cells Recapitulate Aging Biomarkers and Show Reduced Stem Cell Plasticity Affecting Their Adipogenic Differentiation Capacity.
[31298493] MicroRNA-539 functions as a tumour suppressor in prostate cancer via the TGF-β/Smad4 signalling pathway by down-regulating DLX1.
[31298392] LncRNA H19 promotes the development of hepatitis B related hepatocellular carcinoma through regulating microRNA-22 via EMT pathway.
[31298008] [Proliferation effect of ligamentum flavum cells induced by transforming growth factor β and its effect on connective tissue growth factor].
[31297980] miR-107 regulates growth and metastasis of gastric cancer cells via activation of the PI3K-AKT signaling pathway by down-regulating FAT4.
[31297730] Pleiotropic Effects of Epithelial Mesenchymal Crosstalk on Head and Neck Cancer: EMT and beyond.
[31297660] Transforming growth factor β1 promotes fibroblast-like synoviocytes migration and invasion via TGF-β1/Smad signaling in rheumatoid arthritis.
[31297345] Adult-type granulosa cell tumor of the testicle: case report.