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Vascular cell adhesion protein 1 (V-CAM 1) (VCAM-1) (INCAM-100) (CD antigen CD106)

 VCAM1_HUMAN             Reviewed;         739 AA.
P19320; A8K6R7; B4DKS4; E9PDD1; Q6NUP8;
01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
01-NOV-1990, sequence version 1.
22-NOV-2017, entry version 219.
RecName: Full=Vascular cell adhesion protein 1;
Short=V-CAM 1;
Short=VCAM-1;
AltName: Full=INCAM-100;
AltName: CD_antigen=CD106;
Flags: Precursor;
Name=VCAM1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
PubMed=2688898; DOI=10.1016/0092-8674(89)90775-7;
Osborn L., Hession C., Tizard R., Vassallo C., Luhowskyj S.,
Chi-Rosso G., Lobb R.;
"Direct expression cloning of vascular cell adhesion molecule 1, a
cytokine-induced endothelial protein that binds to lymphocytes.";
Cell 59:1203-1211(1989).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Umbilical vein;
PubMed=1699207; DOI=10.1093/nar/18.19.5901;
Polte T., Newman W., Gopal T.V.;
"Full length vascular cell adhesion molecule 1 (VCAM-1).";
Nucleic Acids Res. 18:5901-5901(1990).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=1707873;
Hession C., Tizard R., Vassallo C., Schiffer S.B., Goff D., Moy P.,
Chi-Rosso G., Luhowskyj S., Lobb R., Osborn L.;
"Cloning of an alternate form of vascular cell adhesion molecule-1
(VCAM1).";
J. Biol. Chem. 266:6682-6685(1991).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), AND ALTERNATIVE
SPLICING.
PubMed=1715583; DOI=10.1073/pnas.88.17.7859;
Cybulsky M.I., Fries J.W.U., Williams A.J., Sultan P., Eddy R.,
Byers M., Shows T., Gimbrone M.A. Jr., Collins T.;
"Gene structure, chromosomal location, and basis for alternative mRNA
splicing of the human VCAM1 gene.";
Proc. Natl. Acad. Sci. U.S.A. 88:7859-7863(1991).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS PHE-318; ALA-384;
ALA-413 AND LEU-716.
SeattleSNPs variation discovery resource;
Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
TISSUE=Placenta, and Tongue;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Retinal pigment epithelium;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[10]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-21.
PubMed=1379595;
Iademarco M.F., McQuillan J.J., Rosen G.D., Dean D.C.;
"Characterization of the promoter for vascular cell adhesion molecule-
1 (VCAM-1).";
J. Biol. Chem. 267:16323-16329(1992).
[11]
NUCLEOTIDE SEQUENCE OF 25-686 (ISOFORMS 1 AND 2).
TISSUE=Umbilical vein endothelial cell;
PubMed=1707234;
Cybulsky M.I., Fries J.W., Williams A.J., Sultan P., Davis V.M.,
Gimbrone M.A. Jr., Collins T.;
"Alternative splicing of human VCAM-1 in activated vascular
endothelium.";
Am. J. Pathol. 138:815-820(1991).
[12]
NUCLEOTIDE SEQUENCE OF 25-402 (ISOFORMS 1 AND 2), AND CELL ADHESION
DOMAIN.
TISSUE=Endothelial cell;
PubMed=1377228; DOI=10.1084/jem.176.1.99;
Osborn L., Vassallo C., Benjamin C.D.;
"Activated endothelium binds lymphocytes through a novel binding site
in the alternately spliced domain of vascular cell adhesion molecule-
1.";
J. Exp. Med. 176:99-107(1992).
[13]
PROTEIN SEQUENCE OF 25-39.
PubMed=15340161; DOI=10.1110/ps.04682504;
Zhang Z., Henzel W.J.;
"Signal peptide prediction based on analysis of experimentally
verified cleavage sites.";
Protein Sci. 13:2819-2824(2004).
[14]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-561.
TISSUE=Plasma;
PubMed=16335952; DOI=10.1021/pr0502065;
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,
Moore R.J., Smith R.D.;
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
hydrazide chemistry, and mass spectrometry.";
J. Proteome Res. 4:2070-2080(2005).
[15]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 25-226.
PubMed=7531291; DOI=10.1038/373539a0;
Jones E.Y., Harlos K., Bottomley M.J., Robinson R.C., Driscoll P.C.,
Edwards R.M., Clements J.M., Dudgeon T.J., Stuart D.I.;
"Crystal structure of an integrin-binding fragment of vascular cell
adhesion molecule-1 at 1.8-A resolution.";
Nature 373:539-544(1995).
[16]
X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 25-219, AND DISULFIDE BONDS.
PubMed=7539925; DOI=10.1073/pnas.92.12.5714;
Wang J.-H., Pepinsky R.B., Stehle T., Liu J.-H., Karpusas M.,
Browning B., Osborn L.;
"The crystal structure of an N-terminal two-domain fragment of
vascular cell adhesion molecule 1 (VCAM-1): a cyclic peptide based on
the domain 1 C-D loop can inhibit VCAM-1-alpha 4 integrin
interaction.";
Proc. Natl. Acad. Sci. U.S.A. 92:5714-5718(1995).
[17]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 25-220.
PubMed=15299708; DOI=10.1107/S0907444995012352;
Wang J.-H., Stehle T., Pepinsky R.B., Liu J.-H., Karpusas M.,
Osborn L.;
"Structure of a functional fragment of VCAM-1 refined at 1.9-A
resolution.";
Acta Crystallogr. D 52:369-379(1996).
-!- FUNCTION: Important in cell-cell recognition. Appears to function
in leukocyte-endothelial cell adhesion. Interacts with integrin
alpha-4/beta-1 (ITGA4/ITGB1) on leukocytes, and mediates both
adhesion and signal transduction. The VCAM1/ITGA4/ITGB1
interaction may play a pathophysiologic role both in immune
responses and in leukocyte emigration to sites of inflammation.
-!- SUBUNIT: Binds to ECMV-D capsid proteins and acts as a receptor
for this virus. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
protein.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Comment=Additional isoforms seem to exist.;
Name=1; Synonyms=Long, VCAM-7D;
IsoId=P19320-1; Sequence=Displayed;
Note=Major isoform.;
Name=2; Synonyms=Short, VCAM-6D;
IsoId=P19320-2; Sequence=VSP_002580;
Name=3;
IsoId=P19320-3; Sequence=VSP_044636;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Expressed on inflammed vascular endothelium,
as well as on macrophage-like and dendritic cell types in both
normal and inflammed tissue.
-!- INDUCTION: By cytokines (e.g. IL-1, TNF-alpha).
-!- DOMAIN: Either the first or the fourth Ig-like C2-type domain is
required for VLA4-dependent cell adhesion.
-!- PTM: Sialoglycoprotein.
-!- WEB RESOURCE: Name=Wikipedia; Note=VCAM1 entry;
URL="https://en.wikipedia.org/wiki/VCAM1";
-!- WEB RESOURCE: Name=SeattleSNPs;
URL="http://pga.gs.washington.edu/data/vcam1/";
-!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
Note=VCAM-1;
URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_hum_Itlect_266";
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EMBL; M30257; AAA51917.1; -; mRNA.
EMBL; X53051; CAA37218.1; -; mRNA.
EMBL; M60335; AAA61269.1; -; mRNA.
EMBL; M73255; AAA61270.1; -; Genomic_DNA.
EMBL; AF536818; AAM96190.1; -; Genomic_DNA.
EMBL; AK291732; BAF84421.1; -; mRNA.
EMBL; AK296692; BAG59286.1; -; mRNA.
EMBL; AC093428; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471097; EAW72950.1; -; Genomic_DNA.
EMBL; BC017276; AAH17276.3; -; mRNA.
EMBL; BC068490; AAH68490.2; -; mRNA.
EMBL; BC085003; AAH85003.1; -; mRNA.
EMBL; M92431; -; NOT_ANNOTATED_CDS; Genomic_DNA.
CCDS; CCDS55617.1; -. [P19320-3]
CCDS; CCDS773.1; -. [P19320-1]
CCDS; CCDS774.1; -. [P19320-2]
PIR; A41288; A41288.
PIR; B41288; B41288.
RefSeq; NP_001069.1; NM_001078.3. [P19320-1]
RefSeq; NP_001186763.1; NM_001199834.1. [P19320-3]
RefSeq; NP_542413.1; NM_080682.2. [P19320-2]
UniGene; Hs.109225; -.
PDB; 1IJ9; X-ray; 3.00 A; A=25-220.
PDB; 1VCA; X-ray; 1.80 A; A/B=25-226.
PDB; 1VSC; X-ray; 1.90 A; A/B=25-219.
PDBsum; 1IJ9; -.
PDBsum; 1VCA; -.
PDBsum; 1VSC; -.
ProteinModelPortal; P19320; -.
SMR; P19320; -.
BioGrid; 113255; 452.
CORUM; P19320; -.
IntAct; P19320; 629.
STRING; 9606.ENSP00000294728; -.
BindingDB; P19320; -.
ChEMBL; CHEMBL3735; -.
DrugBank; DB05399; AGI-1067.
DrugBank; DB01136; Carvedilol.
DrugBank; DB00898; Ethanol.
iPTMnet; P19320; -.
PhosphoSitePlus; P19320; -.
BioMuta; VCAM1; -.
DMDM; 137560; -.
EPD; P19320; -.
MaxQB; P19320; -.
PaxDb; P19320; -.
PeptideAtlas; P19320; -.
PRIDE; P19320; -.
DNASU; 7412; -.
Ensembl; ENST00000294728; ENSP00000294728; ENSG00000162692. [P19320-1]
Ensembl; ENST00000347652; ENSP00000304611; ENSG00000162692. [P19320-2]
Ensembl; ENST00000370119; ENSP00000359137; ENSG00000162692. [P19320-3]
GeneID; 7412; -.
KEGG; hsa:7412; -.
UCSC; uc001dti.5; human. [P19320-1]
CTD; 7412; -.
DisGeNET; 7412; -.
EuPathDB; HostDB:ENSG00000162692.10; -.
GeneCards; VCAM1; -.
HGNC; HGNC:12663; VCAM1.
HPA; CAB000154; -.
HPA; HPA034796; -.
HPA; HPA069867; -.
MIM; 192225; gene.
neXtProt; NX_P19320; -.
OpenTargets; ENSG00000162692; -.
PharmGKB; PA37286; -.
eggNOG; ENOG410IIKS; Eukaryota.
eggNOG; ENOG4111F4V; LUCA.
GeneTree; ENSGT00830000128299; -.
HOGENOM; HOG000004820; -.
HOVERGEN; HBG053965; -.
InParanoid; P19320; -.
KO; K06527; -.
OMA; GVYECES; -.
OrthoDB; EOG091G0590; -.
PhylomeDB; P19320; -.
TreeFam; TF333571; -.
Reactome; R-HSA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
Reactome; R-HSA-216083; Integrin cell surface interactions.
Reactome; R-HSA-6785807; Interleukin-4 and 13 signaling.
Reactome; R-HSA-877300; Interferon gamma signaling.
SIGNOR; P19320; -.
ChiTaRS; VCAM1; human.
EvolutionaryTrace; P19320; -.
GeneWiki; VCAM-1; -.
GenomeRNAi; 7412; -.
PMAP-CutDB; P19320; -.
PRO; PR:P19320; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000162692; -.
CleanEx; HS_L1CAM; -.
CleanEx; HS_VCAM1; -.
ExpressionAtlas; P19320; baseline and differential.
Genevisible; P19320; HS.
GO; GO:0071065; C:alpha9-beta1 integrin-vascular cell adhesion molecule-1 complex; IDA:BHF-UCL.
GO; GO:0045177; C:apical part of cell; IDA:BHF-UCL.
GO; GO:0009986; C:cell surface; IDA:UniProtKB.
GO; GO:0005769; C:early endosome; IDA:UniProtKB.
GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
GO; GO:0009897; C:external side of plasma membrane; IDA:BHF-UCL.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
GO; GO:0030175; C:filopodium; IDA:BHF-UCL.
GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005902; C:microvillus; IDA:BHF-UCL.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0002102; C:podosome; IDA:BHF-UCL.
GO; GO:0042383; C:sarcolemma; IEA:Ensembl.
GO; GO:0050839; F:cell adhesion molecule binding; IDA:BHF-UCL.
GO; GO:0005178; F:integrin binding; IDA:BHF-UCL.
GO; GO:0008131; F:primary amine oxidase activity; IDA:UniProtKB.
GO; GO:0002526; P:acute inflammatory response; IEA:Ensembl.
GO; GO:0007568; P:aging; IEA:Ensembl.
GO; GO:0009308; P:amine metabolic process; IDA:UniProtKB.
GO; GO:0030183; P:B cell differentiation; IC:BHF-UCL.
GO; GO:0035584; P:calcium-mediated signaling using intracellular calcium source; IGI:UniProtKB.
GO; GO:0007155; P:cell adhesion; IDA:BHF-UCL.
GO; GO:0060326; P:cell chemotaxis; IEA:Ensembl.
GO; GO:0007160; P:cell-matrix adhesion; IDA:UniProtKB.
GO; GO:0071356; P:cellular response to tumor necrosis factor; IEA:Ensembl.
GO; GO:0035924; P:cellular response to vascular endothelial growth factor stimulus; IEA:Ensembl.
GO; GO:0002544; P:chronic inflammatory response; IEA:Ensembl.
GO; GO:0030198; P:extracellular matrix organization; TAS:Reactome.
GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; IDA:BHF-UCL.
GO; GO:0060333; P:interferon-gamma-mediated signaling pathway; TAS:Reactome.
GO; GO:0007159; P:leukocyte cell-cell adhesion; IDA:BHF-UCL.
GO; GO:0050901; P:leukocyte tethering or rolling; IDA:UniProtKB.
GO; GO:0022614; P:membrane to membrane docking; IEP:BHF-UCL.
GO; GO:0042102; P:positive regulation of T cell proliferation; IDA:BHF-UCL.
GO; GO:0050776; P:regulation of immune response; TAS:Reactome.
GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
GO; GO:0010212; P:response to ionizing radiation; IEA:Ensembl.
GO; GO:0032496; P:response to lipopolysaccharide; IEA:Ensembl.
GO; GO:0035094; P:response to nicotine; IEA:Ensembl.
GO; GO:0007584; P:response to nutrient; IEA:Ensembl.
GO; GO:0010043; P:response to zinc ion; IEA:Ensembl.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
Gene3D; 2.60.40.10; -; 8.
InterPro; IPR003987; ICAM_VCAM_N.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR036179; Ig-like_dom_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR008424; Ig_C2-set.
InterPro; IPR013098; Ig_I-set.
InterPro; IPR003599; Ig_sub.
InterPro; IPR003598; Ig_sub2.
InterPro; IPR013106; Ig_V-set.
InterPro; IPR013151; Immunoglobulin.
InterPro; IPR003989; VCAM-1.
PANTHER; PTHR44644; PTHR44644; 3.
Pfam; PF05790; C2-set; 2.
Pfam; PF07679; I-set; 3.
Pfam; PF00047; ig; 1.
PRINTS; PR01472; ICAMVCAM1.
PRINTS; PR01474; VCAM1.
SMART; SM00409; IG; 5.
SMART; SM00408; IGc2; 5.
SMART; SM00406; IGv; 2.
SUPFAM; SSF48726; SSF48726; 7.
PROSITE; PS50835; IG_LIKE; 5.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell adhesion; Complete proteome;
Direct protein sequencing; Disulfide bond; Glycoprotein;
Host-virus interaction; Immunoglobulin domain; Membrane; Polymorphism;
Reference proteome; Repeat; Signal; Transmembrane;
Transmembrane helix.
SIGNAL 1 24 {ECO:0000269|PubMed:15340161}.
CHAIN 25 739 Vascular cell adhesion protein 1.
/FTId=PRO_0000014997.
TOPO_DOM 25 698 Extracellular. {ECO:0000255}.
TRANSMEM 699 720 Helical. {ECO:0000255}.
TOPO_DOM 721 739 Cytoplasmic. {ECO:0000255}.
DOMAIN 25 105 Ig-like C2-type 1.
DOMAIN 109 212 Ig-like C2-type 2.
DOMAIN 223 309 Ig-like C2-type 3.
DOMAIN 312 399 Ig-like C2-type 4.
DOMAIN 408 506 Ig-like C2-type 5.
DOMAIN 511 595 Ig-like C2-type 6.
DOMAIN 600 684 Ig-like C2-type 7.
CARBOHYD 273 273 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 365 365 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 417 417 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 463 463 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 531 531 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 561 561 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16335952}.
DISULFID 47 95 {ECO:0000269|PubMed:7539925}.
DISULFID 52 99 {ECO:0000269|PubMed:7539925}.
DISULFID 137 195 {ECO:0000269|PubMed:7539925}.
DISULFID 246 291 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 335 383 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 534 579 {ECO:0000255|PROSITE-ProRule:PRU00114}.
VAR_SEQ 52 113 Missing (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_044636.
VAR_SEQ 310 402 EKPFTVEISPGPRIAAQIGDSVMLTCSVMGCESPSFSWRTQ
IDSPLSGKVRSEGTNSTLTLSPVSFENEHSYLCTVTCGHKK
LEKGIQVELYS -> A (in isoform 2).
{ECO:0000303|PubMed:2688898}.
/FTId=VSP_002580.
VARIANT 18 18 M -> I (in dbSNP:rs34228330).
/FTId=VAR_049951.
VARIANT 318 318 S -> F (in dbSNP:rs3783611).
{ECO:0000269|Ref.5}.
/FTId=VAR_014309.
VARIANT 384 384 T -> A (in dbSNP:rs3783612).
{ECO:0000269|Ref.5}.
/FTId=VAR_014310.
VARIANT 413 413 G -> A (in dbSNP:rs3783613).
{ECO:0000269|Ref.5}.
/FTId=VAR_014311.
VARIANT 421 421 V -> I (in dbSNP:rs34100871).
/FTId=VAR_049952.
VARIANT 488 488 H -> R (in dbSNP:rs34199378).
/FTId=VAR_049953.
VARIANT 716 716 I -> L (in dbSNP:rs3783615).
{ECO:0000269|Ref.5}.
/FTId=VAR_014312.
CONFLICT 182 182 F -> G (in Ref. 12). {ECO:0000305}.
CONFLICT 402 402 S -> T (in Ref. 11). {ECO:0000305}.
CONFLICT 728 728 S -> P (in Ref. 6; BAG59286).
{ECO:0000305}.
STRAND 26 38 {ECO:0000244|PDB:1VCA}.
STRAND 43 51 {ECO:0000244|PDB:1VCA}.
STRAND 56 61 {ECO:0000244|PDB:1VCA}.
STRAND 68 74 {ECO:0000244|PDB:1VCA}.
STRAND 77 84 {ECO:0000244|PDB:1VCA}.
HELIX 87 89 {ECO:0000244|PDB:1VCA}.
STRAND 91 99 {ECO:0000244|PDB:1VCA}.
STRAND 102 114 {ECO:0000244|PDB:1VCA}.
STRAND 120 125 {ECO:0000244|PDB:1VCA}.
STRAND 133 144 {ECO:0000244|PDB:1VCA}.
HELIX 145 147 {ECO:0000244|PDB:1VCA}.
STRAND 148 154 {ECO:0000244|PDB:1VCA}.
STRAND 157 163 {ECO:0000244|PDB:1VCA}.
STRAND 169 171 {ECO:0000244|PDB:1IJ9}.
STRAND 174 182 {ECO:0000244|PDB:1VCA}.
HELIX 186 188 {ECO:0000244|PDB:1VCA}.
STRAND 192 199 {ECO:0000244|PDB:1VCA}.
STRAND 209 216 {ECO:0000244|PDB:1VCA}.
SEQUENCE 739 AA; 81276 MW; 050E2EBD39AC2FF4 CRC64;
MPGKMVVILG ASNILWIMFA ASQAFKIETT PESRYLAQIG DSVSLTCSTT GCESPFFSWR
TQIDSPLNGK VTNEGTTSTL TMNPVSFGNE HSYLCTATCE SRKLEKGIQV EIYSFPKDPE
IHLSGPLEAG KPITVKCSVA DVYPFDRLEI DLLKGDHLMK SQEFLEDADR KSLETKSLEV
TFTPVIEDIG KVLVCRAKLH IDEMDSVPTV RQAVKELQVY ISPKNTVISV NPSTKLQEGG
SVTMTCSSEG LPAPEIFWSK KLDNGNLQHL SGNATLTLIA MRMEDSGIYV CEGVNLIGKN
RKEVELIVQE KPFTVEISPG PRIAAQIGDS VMLTCSVMGC ESPSFSWRTQ IDSPLSGKVR
SEGTNSTLTL SPVSFENEHS YLCTVTCGHK KLEKGIQVEL YSFPRDPEIE MSGGLVNGSS
VTVSCKVPSV YPLDRLEIEL LKGETILENI EFLEDTDMKS LENKSLEMTF IPTIEDTGKA
LVCQAKLHID DMEFEPKQRQ STQTLYVNVA PRDTTVLVSP SSILEEGSSV NMTCLSQGFP
APKILWSRQL PNGELQPLSE NATLTLISTK MEDSGVYLCE GINQAGRSRK EVELIIQVTP
KDIKLTAFPS ESVKEGDTVI ISCTCGNVPE TWIILKKKAE TGDTVLKSID GAYTIRKAQL
KDAGVYECES KNKVGSQLRS LTLDVQGREN NKDYFSPELL VLYFASSLII PAIGMIIYFA
RKANMKGSYS LVEAQKSKV


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