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Vimentin

 VIME_PANTR              Reviewed;         466 AA.
Q5R1W8; A5A6N8;
01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
24-JUL-2007, sequence version 4.
05-JUN-2019, entry version 104.
RecName: Full=Vimentin;
Name=VIM;
Pan troglodytes (Chimpanzee).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Pan.
NCBI_TaxID=9598;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Skin;
Hirai M., Sakate R., Hida M., Sugano S., Hayasaka I., Suto Y.,
Osada N., Hashimoto K.;
Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Skin;
PubMed=17574350; DOI=10.1016/j.gene.2007.04.013;
Sakate R., Suto Y., Imanishi T., Tanoue T., Hida M., Hayasaka I.,
Kusuda J., Gojobori T., Hashimoto K., Hirai M.;
"Mapping of chimpanzee full-length cDNAs onto the human genome unveils
large potential divergence of the transcriptome.";
Gene 399:1-10(2007).
-!- FUNCTION: Vimentins are class-III intermediate filaments found in
various non-epithelial cells, especially mesenchymal cells.
Vimentin is attached to the nucleus, endoplasmic reticulum, and
mitochondria, either laterally or terminally.
-!- FUNCTION: Involved with LARP6 in the stabilization of type I
collagen mRNAs for CO1A1 and CO1A2. {ECO:0000250}.
-!- SUBUNIT: Homopolymer assembled from elementary dimers. Interacts
with BCAS3, LGSN and SYNM. Interacts (via rod region) with PLEC
(via CH 1 domain). Interacts with SLC6A4. Interacts with STK33.
Interacts with LARP6. Interacts with RAB8B. Interacts with TOR1A;
the interaction associates TOR1A with the cytoskeleton. Interacts
with TOR1AIP1. Interacts with DIAPH1. Interacts with EPPK1;
interaction is dependent of higher-order structure of intermediate
filament. Interacts with the non-receptor tyrosine kinase SRMS;
the interaction leads to phosphorylation of VIM. Interacts with
NOD2 (By similarity). Interacts (via head region) with CORO1C (By
similarity). {ECO:0000250|UniProtKB:P08670,
ECO:0000250|UniProtKB:P20152, ECO:0000250|UniProtKB:P31000}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P08670}.
Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P08670}. Nucleus
matrix {ECO:0000250|UniProtKB:P31000}.
-!- DOMAIN: The central alpha-helical coiled-coil IF rod domain
mediates elementary homodimerization. {ECO:0000250}.
-!- DOMAIN: The [IL]-x-C-x-x-[DE] motif is a proposed target motif for
cysteine S-nitrosylation mediated by the iNOS-S100A8/A9
transnitrosylase complex. {ECO:0000250|UniProtKB:P08670}.
-!- PTM: One of the most prominent phosphoproteins in various cells of
mesenchymal origin. Phosphorylation is enhanced during cell
division, at which time vimentin filaments are significantly
reorganized. Phosphorylation by PKN1 inhibits the formation of
filaments. Filament disassembly during mitosis is promoted by
phosphorylation at Ser-55 as well as by nestin. Phosphorylated at
Ser-56 by CDK5 during neutrophil secretion in the cytoplasm.
Phosphorylated by STK33. Phosphorylated on tyrosine residues by
SRMS. {ECO:0000250|UniProtKB:P08670,
ECO:0000250|UniProtKB:P31000}.
-!- PTM: S-nitrosylation is induced by interferon-gamma and
oxidatively-modified low-densitity lipoprotein (LDL(ox)) possibly
implicating the iNOS-S100A8/9 transnitrosylase complex.
{ECO:0000250|UniProtKB:P08670}.
-!- SIMILARITY: Belongs to the intermediate filament family.
{ECO:0000255|PROSITE-ProRule:PRU01188}.
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EMBL; AB188279; BAD74030.1; -; mRNA.
EMBL; AB222166; BAF62411.1; -; mRNA.
RefSeq; NP_001009148.1; NM_001009148.2.
SMR; Q5R1W8; -.
STRING; 9598.ENSPTRP00000003945; -.
PaxDb; Q5R1W8; -.
PRIDE; Q5R1W8; -.
GeneID; 493952; -.
KEGG; ptr:493952; -.
CTD; 7431; -.
eggNOG; ENOG410IFZ1; Eukaryota.
eggNOG; ENOG410XRBS; LUCA.
HOGENOM; HOG000230977; -.
InParanoid; Q5R1W8; -.
KO; K07606; -.
OrthoDB; 655109at2759; -.
Proteomes; UP000002277; Unplaced.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005882; C:intermediate filament; ISS:UniProtKB.
GO; GO:0016363; C:nuclear matrix; IEA:UniProtKB-SubCell.
GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
GO; GO:0071222; P:cellular response to lipopolysaccharide; ISS:UniProtKB.
GO; GO:0071225; P:cellular response to muramyl dipeptide; ISS:UniProtKB.
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.
2: Evidence at transcript level;
Acetylation; Coiled coil; Complete proteome; Cytoplasm; Cytoskeleton;
Glycoprotein; Intermediate filament; Isopeptide bond; Nucleus;
Phosphoprotein; Reference proteome; S-nitrosylation; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P08670}.
CHAIN 2 466 Vimentin.
/FTId=PRO_0000063757.
DOMAIN 103 411 IF rod. {ECO:0000255|PROSITE-
ProRule:PRU01188}.
REGION 2 95 Head.
REGION 96 131 Coil 1A.
REGION 132 153 Linker 1.
REGION 154 245 Coil 1B.
REGION 246 268 Linker 12.
REGION 269 407 Coil 2.
REGION 408 466 Tail.
COILED 96 131
COILED 154 245
COILED 303 407
MOTIF 326 329 [IL]-x-C-x-x-[DE] motif.
{ECO:0000250|UniProtKB:P08670}.
SITE 351 351 Stutter. {ECO:0000250}.
MOD_RES 2 2 N-acetylserine.
{ECO:0000250|UniProtKB:P08670}.
MOD_RES 5 5 Phosphoserine.
{ECO:0000250|UniProtKB:P08670}.
MOD_RES 7 7 Phosphoserine; alternate.
{ECO:0000250|UniProtKB:P08670}.
MOD_RES 8 8 Phosphoserine.
{ECO:0000250|UniProtKB:P08670}.
MOD_RES 9 9 Phosphoserine.
{ECO:0000250|UniProtKB:P08670}.
MOD_RES 10 10 Phosphoserine.
{ECO:0000250|UniProtKB:P08670}.
MOD_RES 20 20 Phosphothreonine.
{ECO:0000250|UniProtKB:P08670}.
MOD_RES 25 25 Phosphoserine.
{ECO:0000250|UniProtKB:P20152}.
MOD_RES 26 26 Phosphoserine.
{ECO:0000250|UniProtKB:P20152}.
MOD_RES 34 34 Phosphoserine; by PKC; alternate.
{ECO:0000250|UniProtKB:P08670}.
MOD_RES 39 39 Phosphoserine; by CaMK2, PKA, PKC and
ROCK2. {ECO:0000250|UniProtKB:P08670}.
MOD_RES 42 42 Phosphoserine.
{ECO:0000250|UniProtKB:P08670}.
MOD_RES 47 47 Phosphoserine.
{ECO:0000250|UniProtKB:P20152}.
MOD_RES 49 49 Phosphoserine.
{ECO:0000250|UniProtKB:P08670}.
MOD_RES 51 51 Phosphoserine.
{ECO:0000250|UniProtKB:P20152}.
MOD_RES 53 53 Phosphotyrosine.
{ECO:0000250|UniProtKB:P20152}.
MOD_RES 55 55 Phosphoserine.
{ECO:0000250|UniProtKB:P31000}.
MOD_RES 56 56 Phosphoserine; by CDK5 and CDK1.
{ECO:0000250|UniProtKB:P08670}.
MOD_RES 61 61 Phosphotyrosine.
{ECO:0000250|UniProtKB:P08670}.
MOD_RES 66 66 Phosphoserine.
{ECO:0000250|UniProtKB:P20152}.
MOD_RES 72 72 Phosphoserine; by AURKB and ROCK2.
{ECO:0000250|UniProtKB:P08670}.
MOD_RES 73 73 Phosphoserine.
{ECO:0000250|UniProtKB:P08670}.
MOD_RES 83 83 Phosphoserine.
{ECO:0000250|UniProtKB:P20152}.
MOD_RES 87 87 Phosphoserine.
{ECO:0000250|UniProtKB:P08670}.
MOD_RES 117 117 Phosphotyrosine.
{ECO:0000250|UniProtKB:P08670}.
MOD_RES 120 120 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P08670}.
MOD_RES 120 120 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P20152}.
MOD_RES 129 129 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P20152}.
MOD_RES 129 129 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P20152}.
MOD_RES 139 139 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P08670}.
MOD_RES 144 144 Phosphoserine.
{ECO:0000250|UniProtKB:P08670}.
MOD_RES 168 168 N6-acetyllysine.
{ECO:0000250|UniProtKB:P20152}.
MOD_RES 188 188 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P20152}.
MOD_RES 188 188 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P20152}.
MOD_RES 214 214 Phosphoserine.
{ECO:0000250|UniProtKB:P08670}.
MOD_RES 223 223 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P20152}.
MOD_RES 226 226 Phosphoserine.
{ECO:0000250|UniProtKB:P08670}.
MOD_RES 235 235 N6-acetyllysine.
{ECO:0000250|UniProtKB:P20152}.
MOD_RES 294 294 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P20152}.
MOD_RES 294 294 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P20152}.
MOD_RES 299 299 Phosphoserine.
{ECO:0000250|UniProtKB:P08670}.
MOD_RES 325 325 Phosphoserine.
{ECO:0000250|UniProtKB:P20152}.
MOD_RES 373 373 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P08670}.
MOD_RES 409 409 Phosphoserine.
{ECO:0000250|UniProtKB:P08670}.
MOD_RES 412 412 Phosphoserine.
{ECO:0000250|UniProtKB:P84198}.
MOD_RES 419 419 Phosphoserine.
{ECO:0000250|UniProtKB:P08670}.
MOD_RES 420 420 Phosphoserine.
{ECO:0000250|UniProtKB:P08670}.
MOD_RES 426 426 Phosphothreonine.
{ECO:0000250|UniProtKB:P08670}.
MOD_RES 430 430 Phosphoserine.
{ECO:0000250|UniProtKB:P08670}.
MOD_RES 436 436 Phosphothreonine.
{ECO:0000250|UniProtKB:P08670}.
MOD_RES 438 438 Phosphoserine.
{ECO:0000250|UniProtKB:P08670}.
MOD_RES 445 445 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P08670}.
MOD_RES 445 445 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P20152}.
MOD_RES 446 446 Phosphothreonine.
{ECO:0000250|UniProtKB:P08670}.
MOD_RES 458 458 Phosphothreonine.
{ECO:0000250|UniProtKB:P08670}.
MOD_RES 459 459 Phosphoserine.
{ECO:0000250|UniProtKB:P08670}.
CARBOHYD 7 7 O-linked (GlcNAc) serine; alternate.
{ECO:0000250}.
CARBOHYD 33 33 O-linked (GlcNAc) threonine.
{ECO:0000250}.
CARBOHYD 34 34 O-linked (GlcNAc) serine; alternate.
{ECO:0000250}.
CROSSLNK 104 104 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P08670}.
CROSSLNK 120 120 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:P08670}.
CROSSLNK 129 129 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:P08670}.
CROSSLNK 139 139 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:P08670}.
CROSSLNK 223 223 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:P08670}.
CROSSLNK 262 262 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P08670}.
CROSSLNK 294 294 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:P08670}.
CROSSLNK 313 313 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P08670}.
CROSSLNK 373 373 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:P08670}.
CROSSLNK 439 439 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P08670}.
CROSSLNK 445 445 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1);
alternate.
{ECO:0000250|UniProtKB:P08670}.
CROSSLNK 445 445 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:P08670}.
CONFLICT 3 3 T -> I (in Ref. 1; BAD74030).
{ECO:0000305}.
CONFLICT 326 326 L -> P (in Ref. 1; BAD74030).
{ECO:0000305}.
CONFLICT 371 371 D -> N (in Ref. 1; BAD74030).
{ECO:0000305}.
SEQUENCE 466 AA; 53653 MW; 5A5B4EC6885BE150 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 DMKEEMARHL REYQDLLNVK MALDIEIATY RKLLEGEESR ISLPLPNFSS
LNLRETNLDS LPLVDTHSKR TLLIKTVETR DGQVINETSQ HHDDLE


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Pathways :
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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
[vim1; vim2] Vimentin-1/2
[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
[VIM] Vimentin

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[31220448] The Expression of Yes-Associated Protein (YAP) Maintains Putative Cancer Stemness and Is Associated with Poor Prognosis in Intrahepatic Cholangiocarcinoma.
[31220419] LncRNA SNHG4 promotes proliferation, migration, invasion and epithelial-mesenchymal transition of lung cancer cells by regulating miR-98-5p.
[31219650] AEBP1, a prognostic indicator, promotes colon adenocarcinoma cell growth and metastasis through the NF-κB pathway.
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[31219186] MicroRNA-329 upregulation impairs the HMGB2/β-catenin pathway and regulates cell biological behaviors in melanoma.
[31217166] KRAS activation in gastric adenocarcinoma stimulates epithelial-to-mesenchymal transition to cancer stem-like cells and promotes metastasis.
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[31215499] FAM83H is involved in stabilization of β-catenin and progression of osteosarcomas.