Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Vimentin

 VIME_MESAU              Reviewed;         465 AA.
P02544;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
25-OCT-2017, entry version 116.
RecName: Full=Vimentin;
Name=VIM;
Mesocricetus auratus (Golden hamster).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Cricetidae; Cricetinae; Mesocricetus.
NCBI_TaxID=10036;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Lens;
PubMed=6194898; DOI=10.1016/0092-8674(83)90224-6;
Quax W.J., Egberts W.V., Hendriks W., Quax-Jeuken Y.E.F.M.,
Bloemendal H.;
"The structure of the vimentin gene.";
Cell 35:215-223(1983).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Lens;
PubMed=6304716; DOI=10.1073/pnas.80.12.3548;
Quax-Jeuken Y.E.F.M., Quax W.J., Bloemendal H.;
"Primary and secondary structure of hamster vimentin predicted from
the nucleotide sequence.";
Proc. Natl. Acad. Sci. U.S.A. 80:3548-3552(1983).
[3]
PHOSPHORYLATION AT SER-55.
PubMed=2019567;
Chou Y.-H., Ngai K.-L., Goldman R.;
"The regulation of intermediate filament reorganization in mitosis.
p34cdc2 phosphorylates vimentin at a unique N-terminal site.";
J. Biol. Chem. 266:7325-7328(1991).
-!- 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 HCV core protein. 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.
{ECO:0000250|UniProtKB:P08670}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
-!- 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: Phosphorylation by PKN1 inhibits the formation of filaments.
Filament disassembly during mitosis is promoted by phosphorylation
at Ser-54 as well as by nestin (By similarity). One of the most
prominent phosphoproteins in various cells of mesenchymal origin.
Phosphorylation is enhanced during cell division, at which time
vimentin filaments are significantly reorganized. Phosphorylated
at Ser-55 by CDK5 during neutrophil secretion in the cytoplasm.
Phosphorylated by STK33 (By similarity). {ECO:0000250}.
-!- 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}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; K00927; AAA37104.1; -; Genomic_DNA.
EMBL; K00921; AAA37104.1; JOINED; Genomic_DNA.
EMBL; K00922; AAA37104.1; JOINED; Genomic_DNA.
EMBL; K00923; AAA37104.1; JOINED; Genomic_DNA.
EMBL; K00924; AAA37104.1; JOINED; Genomic_DNA.
EMBL; K00925; AAA37104.1; JOINED; Genomic_DNA.
EMBL; K00926; AAA37104.1; JOINED; Genomic_DNA.
PIR; A90842; VEHY.
ProteinModelPortal; P02544; -.
SMR; P02544; -.
iPTMnet; P02544; -.
PRIDE; P02544; -.
HOVERGEN; HBG013015; -.
Proteomes; UP000189706; Genome assembly.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005882; C:intermediate filament; ISS:UniProtKB.
GO; GO:0005200; F:structural constituent of cytoskeleton; ISS:UniProtKB.
GO; GO:0045107; P:intermediate filament polymerization; IDA:CAFA.
InterPro; IPR001664; IF.
InterPro; IPR006821; Intermed_filament_DNA-bd.
InterPro; IPR018039; Intermediate_filament_CS.
InterPro; IPR027699; Vimentin.
PANTHER; PTHR23239; PTHR23239; 1.
PANTHER; PTHR23239:SF27; PTHR23239:SF27; 1.
Pfam; PF00038; Filament; 1.
Pfam; PF04732; Filament_head; 1.
SMART; SM01391; Filament; 1.
PROSITE; PS00226; IF_ROD_1; 1.
PROSITE; PS51842; IF_ROD_2; 1.
1: Evidence at protein level;
Acetylation; Coiled coil; Complete proteome; Cytoplasm; Glycoprotein;
Intermediate filament; Isopeptide bond; Methylation; Nitration;
Phosphoprotein; Reference proteome; S-nitrosylation; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P08670}.
CHAIN 2 465 Vimentin.
/FTId=PRO_0000063755.
DOMAIN 102 410 IF rod. {ECO:0000255|PROSITE-
ProRule:PRU01188}.
REGION 2 94 Head.
REGION 95 130 Coil 1A.
REGION 131 152 Linker 1.
REGION 153 244 Coil 1B.
REGION 245 267 Linker 12.
REGION 268 406 Coil 2.
REGION 407 465 Tail.
COILED 95 130
COILED 153 244
COILED 302 406
MOTIF 325 328 [IL]-x-C-x-x-[DE] motif.
{ECO:0000250|UniProtKB:P08670}.
SITE 350 350 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; by PKA and PKC; alternate.
{ECO:0000250|UniProtKB:P08670}.
MOD_RES 8 8 Phosphoserine.
{ECO:0000250|UniProtKB:P08670}.
MOD_RES 9 9 Phosphoserine; by PKC.
{ECO:0000250|UniProtKB:P17661}.
MOD_RES 10 10 Phosphoserine; by PKC.
{ECO:0000250|UniProtKB:P08670}.
MOD_RES 11 11 Nitrated tyrosine.
{ECO:0000250|UniProtKB:P21807}.
MOD_RES 13 13 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:P31001}.
MOD_RES 20 20 Phosphothreonine.
{ECO:0000250|UniProtKB:P08670}.
MOD_RES 21 21 Phosphoserine; by PKC.
{ECO:0000250|UniProtKB:P20152}.
MOD_RES 25 25 Phosphoserine; by PKA and PKC.
{ECO:0000250|UniProtKB:P20152}.
MOD_RES 26 26 Phosphoserine; by PKC.
{ECO:0000250|UniProtKB:P20152}.
MOD_RES 28 28 Asymmetric dimethylarginine; alternate.
{ECO:0000250|UniProtKB:P31001}.
MOD_RES 28 28 Omega-N-methylarginine; alternate.
{ECO:0000250|UniProtKB:P31001}.
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; by PKC.
{ECO:0000250|UniProtKB:P08670}.
MOD_RES 46 46 Phosphoserine; by PKA.
{ECO:0000250|UniProtKB:P20152}.
MOD_RES 48 48 Phosphoserine.
{ECO:0000250|UniProtKB:P08670}.
MOD_RES 50 50 Phosphoserine; by PKA and PKC.
{ECO:0000250|UniProtKB:P20152}.
MOD_RES 52 52 Phosphotyrosine.
{ECO:0000250|UniProtKB:P20152}.
MOD_RES 54 54 Phosphoserine.
{ECO:0000250|UniProtKB:P31000}.
MOD_RES 55 55 Phosphoserine; by CDK5 and CDK1.
{ECO:0000269|PubMed:2019567}.
MOD_RES 60 60 Phosphotyrosine.
{ECO:0000250|UniProtKB:P08670}.
MOD_RES 65 65 Phosphoserine.
{ECO:0000250|UniProtKB:P20152}.
MOD_RES 71 71 Phosphoserine; by AURKB and ROCK2.
{ECO:0000250|UniProtKB:P08670}.
MOD_RES 72 72 Phosphoserine.
{ECO:0000250|UniProtKB:P08670}.
MOD_RES 82 82 Phosphoserine.
{ECO:0000250|UniProtKB:P20152}.
MOD_RES 86 86 Phosphoserine.
{ECO:0000250|UniProtKB:P08670}.
MOD_RES 116 116 Phosphotyrosine.
{ECO:0000250|UniProtKB:P08670}.
MOD_RES 119 119 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P08670}.
MOD_RES 119 119 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P20152}.
MOD_RES 128 128 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P20152}.
MOD_RES 128 128 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P20152}.
MOD_RES 138 138 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P08670}.
MOD_RES 143 143 Phosphoserine.
{ECO:0000250|UniProtKB:P08670}.
MOD_RES 167 167 N6-acetyllysine.
{ECO:0000250|UniProtKB:P20152}.
MOD_RES 187 187 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P20152}.
MOD_RES 187 187 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P20152}.
MOD_RES 213 213 Phosphoserine.
{ECO:0000250|UniProtKB:P08670}.
MOD_RES 222 222 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P20152}.
MOD_RES 225 225 Phosphoserine.
{ECO:0000250|UniProtKB:P08670}.
MOD_RES 234 234 N6-acetyllysine.
{ECO:0000250|UniProtKB:P20152}.
MOD_RES 293 293 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P20152}.
MOD_RES 293 293 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P20152}.
MOD_RES 298 298 Phosphoserine.
{ECO:0000250|UniProtKB:P08670}.
MOD_RES 324 324 Phosphoserine.
{ECO:0000250|UniProtKB:P20152}.
MOD_RES 372 372 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P08670}.
MOD_RES 382 382 Nitrated tyrosine.
{ECO:0000250|UniProtKB:P21807}.
MOD_RES 408 408 Phosphoserine.
{ECO:0000250|UniProtKB:P08670}.
MOD_RES 411 411 Phosphoserine.
{ECO:0000250|UniProtKB:P84198}.
MOD_RES 418 418 Phosphoserine.
{ECO:0000250|UniProtKB:P08670}.
MOD_RES 419 419 Phosphoserine.
{ECO:0000250|UniProtKB:P08670}.
MOD_RES 425 425 Phosphothreonine.
{ECO:0000250|UniProtKB:P08670}.
MOD_RES 429 429 Phosphoserine.
{ECO:0000250|UniProtKB:P08670}.
MOD_RES 435 435 Phosphothreonine.
{ECO:0000250|UniProtKB:P08670}.
MOD_RES 437 437 Phosphoserine.
{ECO:0000250|UniProtKB:P08670}.
MOD_RES 444 444 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P08670}.
MOD_RES 444 444 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P20152}.
MOD_RES 445 445 Phosphothreonine.
{ECO:0000250|UniProtKB:P08670}.
MOD_RES 457 457 Phosphothreonine.
{ECO:0000250|UniProtKB:P08670}.
MOD_RES 458 458 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 103 103 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P08670}.
CROSSLNK 119 119 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:P08670}.
CROSSLNK 128 128 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:P08670}.
CROSSLNK 138 138 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:P08670}.
CROSSLNK 222 222 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:P08670}.
CROSSLNK 261 261 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P08670}.
CROSSLNK 293 293 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:P08670}.
CROSSLNK 312 312 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P08670}.
CROSSLNK 372 372 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:P08670}.
CROSSLNK 438 438 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P08670}.
CROSSLNK 444 444 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1);
alternate.
{ECO:0000250|UniProtKB:P08670}.
CROSSLNK 444 444 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:P08670}.
CONFLICT 43 43 L -> A (in Ref. 2). {ECO:0000305}.
CONFLICT 116 116 Y -> D (in Ref. 2). {ECO:0000305}.
CONFLICT 183 183 R -> I (in Ref. 2). {ECO:0000305}.
SEQUENCE 465 AA; 53730 MW; 81E6B65451E3EC54 CRC64;
MSTRSVSSSS YRRMFGGPGT SNRQSSNRSY VTTSTRTYSL GSLRPSTSRS LYSSSPGGAY
VTRSSAVRLR SSMPGVRLLQ DSVDFSLADA INTEFKNTRT NEKVELQELN DRFANYIDKV
RFLEQQNKIL LAELEQLKGQ GKSRLGDLYE EEMRELRRQV DQLTNDKARV EVERDNLAED
IMRLREKLQE EMLQREEAES TLQSFRQDVD NASLARLDLE RKVESLQEEI AFLKKLHDEE
IQELQAQIQE QHVQIDVDVS KPDLTAALRD VRQQYESVAA KNLQEAEEWY KSKFADLSEA
ANRNNDALRQ AKQESNEYRR QVQSLTCEVD ALKGTNESLE RQMREMEENF ALEAANYQDT
IGRLQDEIQN MKEEMARHLR EYQDLLNVKM ALDIEIATYR KLLEGEESRI SLPLPNFSSL
NLRETNLESL PLVDTHSKRT LLIKTVETRD GQVINETSQH HDDLE


Related products :

Catalog number Product name Quantity
orb22924 Vimentin antibody Monoclonal Mouse Anti Human Vimentin FITC 500
orb22923 Vimentin antibody Monoclonal Mouse Anti Human Vimentin Biotinylated 500
Mab-607041 Monoclonal Antibodies: Vimentin; Specificity: Vimentin ; Application: Elisa 0.1ml
orb22922 Vimentin antibody Monoclonal Mouse Anti Human Vimentin 500
ant-246 Mouse Anti Human Vimentin Biotinylated Vimentin Biotin 1mg
ant-246 Mouse Anti Human Vimentin Biotinylated Vimentin Biotin 500
ABP-FP-WVIM Alleleustrious pWasabi-Vimentin fusion vector Vimentin 5 ug
ABP-FP-TVIM Alleleustrious pmTFP1-Vimentin fusion vector Vimentin 5 ug
MA1102 Monoclonal Antibodies: Vimentin; reactive species: Human, rat.; Clone: VMT-24; Isotype: IgG1; Specificity: Vimentin 100?g
3634BP-50 Vimentin Blocking Peptide target: Vimentin 50 μg
18-271-81041 Vimentin - Chicken Anti Vimentin Polyclonal 0.1 mg
MAB - 606020118 Monoclonal Antibodies: Vimentin; reactive species: human; Clone: 9E7E7, 5G3F10,5G3F10E5; Isotype: IgG1; Specificity: Vimentin 0.1ml
L5-254-C025 Mouse Monoclonal to Vimentin Antigen Vimentin Isotype IgM Antigen Vimentin Isotype IgM 0.025 mg
A4-460-C100 Mouse Monoclonal to Vimentin Antigen Vimentin Isotype IgM Antigen Vimentin Isotype IgM 0.1 mg
A4-460-C025 Mouse Monoclonal to Vimentin Antigen Vimentin Isotype IgM Antigen Vimentin Isotype IgM 0.025 mg
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
1C-254-C100 Mouse Monoclonal to Vimentin Antigen Vimentin Isotype IgM Antigen Vimentin Isotype IgM 0.1 mg
1C-254-C025 Mouse Monoclonal to Vimentin Antigen Vimentin Isotype IgM Antigen Vimentin Isotype IgM 0.025 mg
11-254-C025 Mouse Monoclonal to Vimentin Antigen Vimentin Isotype IgM Antigen Vimentin Isotype IgM 0.025 mg
11-254-C100 Mouse Monoclonal to Vimentin Antigen Vimentin Isotype IgM Antigen Vimentin Isotype IgM 0.1 mg
L5-254-C100 Mouse Monoclonal to Vimentin Antigen Vimentin Isotype IgM Antigen Vimentin Isotype IgM 0.1 mg
11-460-C025 Mouse Monoclonal to Vimentin Antigen Vimentin Isotype IgM Antigen Vimentin Isotype IgM 0.025 mg
11-460-C100 Mouse Monoclonal to Vimentin Antigen Vimentin Isotype IgM Antigen Vimentin Isotype IgM 0.1 mg
ant-245 Mouse Anti Human Vimentin Vimentin 500


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur