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Intercellular adhesion molecule 1 (ICAM-1) (Major group rhinovirus receptor) (CD antigen CD54)

 ICAM1_HUMAN             Reviewed;         532 AA.
P05362; B2R6M3; Q5NKV7; Q96B50;
01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
21-JUN-2005, sequence version 2.
25-OCT-2017, entry version 218.
RecName: Full=Intercellular adhesion molecule 1;
Short=ICAM-1;
AltName: Full=Major group rhinovirus receptor;
AltName: CD_antigen=CD54;
Flags: Precursor;
Name=ICAM1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT GLU-469.
PubMed=3340213; DOI=10.1038/331624a0;
Simmons D., Makgoba M.W., Seed B.;
"ICAM, an adhesion ligand of LFA-1, is homologous to the neural cell
adhesion molecule NCAM.";
Nature 331:624-627(1988).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT GLU-469.
PubMed=3349522; DOI=10.1016/0092-8674(88)90434-5;
Staunton D.E., Marlin S.D., Stratowa C., Dustin M.L., Springer T.A.;
"Primary structure of ICAM-1 demonstrates interaction between members
of the immunoglobulin and integrin supergene families.";
Cell 52:925-933(1988).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2544880; DOI=10.1073/pnas.86.13.4907;
Tomassini J.E., Graham D., Dewitt C.M., Lineberger D.W., Rodkey J.A.,
Colonno R.J.;
"cDNA cloning reveals that the major group rhinovirus receptor on HeLa
cells is intercellular adhesion molecule 1.";
Proc. Natl. Acad. Sci. U.S.A. 86:4907-4911(1989).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT GLU-469.
PubMed=1680919;
Voraberger G.F., Schaefer R., Stratowa C.;
"Cloning of the human gene for intercellular adhesion molecule 1 and
analysis of its 5'-regulatory region. Induction by cytokines and
phorbol ester.";
J. Immunol. 147:2777-2786(1991).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT KILIFI MET-56, AND VARIANTS
ARG-241; LEU-352; GLN-397 AND TRP-478.
SeattleSNPs variation discovery resource;
Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lung;
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).
[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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Kidney;
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 1-22.
PubMed=1983003;
Stade B.G., Messer G., Riethmueller G., Johnson J.P.;
"Structural characteristics of the 5' region of the human ICAM-1
gene.";
Immunobiology 182:79-87(1990).
[11]
NUCLEOTIDE SEQUENCE [MRNA] OF 5-532, AND VARIANT GLU-469.
TISSUE=Blood;
PubMed=15572059; DOI=10.1016/j.jtbi.2004.08.024;
Walter N.A.R., Stebbing J., Messier W.;
"The potential significance of adaptive evolution and dimerization in
chimpanzee intercellular cell adhesion molecules (ICAMs).";
J. Theor. Biol. 232:339-346(2005).
[12]
PARTIAL PROTEIN SEQUENCE, FUNCTION (MICROBIAL INFECTION), AND
INTERACTION WITH RHINOVIRUS CAPSID PROTEINS.
PubMed=2538243; DOI=10.1016/0092-8674(89)90688-0;
Greve J.M., Davis G., Meyer A.M., Forte C.P., Yost S.C., Marlor C.W.,
Kamarck M.E., McClelland A.;
"The major human rhinovirus receptor is ICAM-1.";
Cell 56:839-847(1989).
[13]
FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH RHINOVIRUS CAPSID
PROTEINS.
PubMed=1968231; DOI=10.1038/344070a0;
Marlin S.D., Staunton D.E., Springer T.A., Stratowa C.,
Sommergruber W., Merluzzi V.J.;
"A soluble form of intercellular adhesion molecule-1 inhibits
rhinovirus infection.";
Nature 344:70-72(1990).
[14]
INTERACTION WITH MUC1, AND FUNCTION.
PubMed=11173916; DOI=10.1159/000051917;
Hayashi T., Takahashi T., Motoya S., Ishida T., Itoh F., Adachi M.,
Hinoda Y., Imai K.;
"MUC1 mucin core protein binds to the domain 1 of ICAM-1.";
Digestion 63 Suppl. 1:87-92(2001).
[15]
FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH COXSACKIEVIRUS
A21 CAPSID PROTEINS.
PubMed=11160747; DOI=10.1128/JVI.75.5.2444-2451.2001;
Xiao C., Bator C.M., Bowman V.D., Rieder E., He Y., Hebert B.,
Bella J., Baker T.S., Wimmer E., Kuhn R.J., Rossmann M.G.;
"Interaction of coxsackievirus A21 with its cellular receptor, ICAM-
1.";
J. Virol. 75:2444-2451(2001).
[16]
FUNCTION (MICROBIAL INFECTION).
PubMed=11413168; DOI=10.1172/JCI12432;
Coscoy L., Ganem D.;
"A viral protein that selectively downregulates ICAM-1 and B7-2 and
modulates T cell costimulation.";
J. Clin. Invest. 107:1599-1606(2001).
[17]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-267.
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).
[18]
UBIQUITINATION.
PubMed=17174307; DOI=10.1016/j.febslet.2006.11.075;
Hoer S., Smith L., Lehner P.J.;
"MARCH-IX mediates ubiquitination and downregulation of ICAM-1.";
FEBS Lett. 581:45-51(2007).
[19]
INTERACTION WITH ARHGEF26, AND FUNCTION.
PubMed=17875742; DOI=10.1083/jcb.200612053;
van Buul J.D., Allingham M.J., Samson T., Meller J., Boulter E.,
Garcia-Mata R., Burridge K.;
"RhoG regulates endothelial apical cup assembly downstream from ICAM1
engagement and is involved in leukocyte trans-endothelial migration.";
J. Cell Biol. 178:1279-1293(2007).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-521 AND THR-530, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[21]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-202; ASN-260 AND ASN-267.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of
multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
[22]
GLYCOSYLATION AT ASN-145.
PubMed=19139490; DOI=10.1074/mcp.M800504-MCP200;
Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F.,
Zheng Z.B., Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y.,
Zhang Y.K., Deng Y.L., Ying W.T., He S.M., Qian X.H.;
"A strategy for precise and large scale identification of core
fucosylated glycoproteins.";
Mol. Cell. Proteomics 8:913-923(2009).
[23]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-145 AND ASN-267.
TISSUE=Leukemic T-cell;
PubMed=19349973; DOI=10.1038/nbt.1532;
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
Schiess R., Aebersold R., Watts J.D.;
"Mass-spectrometric identification and relative quantification of N-
linked cell surface glycoproteins.";
Nat. Biotechnol. 27:378-386(2009).
[24]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-521 AND THR-530, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[25]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[26]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-521, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[27]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-530, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[28]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[29]
X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 28-217, DISULFIDE BONDS, AND
GLYCOSYLATION AT ASN-130; ASN-145; ASN-183 AND ASN-202.
PubMed=9539702; DOI=10.1073/pnas.95.8.4134;
Casasnovas J.M., Stehle T., Liu J.H., Wang J.H., Springer T.A.;
"A dimeric crystal structure for the N-terminal two domains of
intercellular adhesion molecule-1.";
Proc. Natl. Acad. Sci. U.S.A. 95:4134-4139(1998).
[30]
X-RAY CRYSTALLOGRAPHY (3.25 ANGSTROMS) OF 28-212 IN COMPLEX WITH HUMAN
RHINOVIRUS 14, DISULFIDE BONDS, GLYCOSYLATION AT ASN-202, AND SUBUNIT.
PubMed=9539703; DOI=10.1073/pnas.95.8.4140;
Bella J., Kolatkar P.R., Marlor C.W., Greve J.M., Rossmann M.G.;
"The structure of the two amino-terminal domains of human ICAM-1
suggests how it functions as a rhinovirus receptor and as an LFA-1
integrin ligand.";
Proc. Natl. Acad. Sci. U.S.A. 95:4140-4145(1998).
[31]
X-RAY CRYSTALLOGRAPHY (3.25 ANGSTROMS) OF 28-212.
PubMed=10562537; DOI=10.1093/emboj/18.22.6249;
Kolatkar P.R., Bella J., Olson N.H., Bator C.M., Baker T.S.,
Rossmann M.G.;
"Structural studies of two rhinovirus serotypes complexed with
fragments of their cellular receptor.";
EMBO J. 18:6249-6259(1999).
[32]
X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF 28-318 IN COMPLEX WITH ITGAL
VWFA DOMAIN, DISULFIDE BONDS, GLYCOSYLATION AT ASN-130; ASN-145;
ASN-183 AND ASN-202, AND SUBUNIT.
PubMed=12526797; DOI=10.1016/S0092-8674(02)01257-6;
Shimaoka M., Xiao T., Liu J.H., Yang Y., Dong Y., Jun C.D.,
McCormack A., Zhang R., Joachimiak A., Takagi J., Wang J.H.,
Springer T.A.;
"Structures of the alpha L I domain and its complex with ICAM-1 reveal
a shape-shifting pathway for integrin regulation.";
Cell 112:99-111(2003).
[33]
X-RAY CRYSTALLOGRAPHY (3.06 ANGSTROMS) OF 212-477, SUBUNIT, DISULFIDE
BONDS, AND GLYCOSYLATION AT ASN-267; ASN-296 AND ASN-385.
PubMed=15099525; DOI=10.1016/S1097-2765(04)00204-7;
Yang Y., Jun C.D., Liu J.H., Zhang R., Joachimiak A., Springer T.A.,
Wang J.H.;
"Structural basis for dimerization of ICAM-1 on the cell surface.";
Mol. Cell 14:269-276(2004).
[34]
STRUCTURE BY ELECTRON CRYOMICROSCOPY (8.0 ANGSTROMS) OF 24-473 IN
COMPLEX WITH COXSACKIEVIRUS A21, AND SUBUNIT.
PubMed=16004874; DOI=10.1016/j.str.2005.04.011;
Xiao C., Bator-Kelly C.M., Rieder E., Chipman P.R., Craig A.,
Kuhn R.J., Wimmer E., Rossmann M.G.;
"The crystal structure of coxsackievirus A21 and its interaction with
ICAM-1.";
Structure 13:1019-1033(2005).
[35]
VARIANTS ARG-241 AND GLU-469.
PubMed=7525451; DOI=10.1006/geno.1994.1303;
Vora D.K., Rosenbloom C.L., Beaudet A.L., Cottingham R.W.;
"Polymorphisms and linkage analysis for ICAM-1 and the selectin gene
cluster.";
Genomics 21:473-477(1994).
[36]
VARIANT ARG-241.
PubMed=8557254; DOI=10.1007/BF00218826;
Wenzel K., Ernst M., Rohde K., Baumann G., Speer A.;
"DNA polymorphisms in adhesion molecule genes -- a new risk factor for
early atherosclerosis.";
Hum. Genet. 97:15-20(1996).
[37]
VARIANT KILIFI MET-56, AND ASSOCIATION WITH SUSCEPTIBILITY TO MALARIA.
PubMed=9259284; DOI=10.1093/hmg/6.8.1357;
Fernandez-Reyes D., Craig A.G., Kyes S.A., Peshu N., Snow R.W.,
Berendt A.R., Marsh K., Newbold C.I.;
"A high frequency African coding polymorphism in the N-terminal domain
of ICAM-1 predisposing to cerebral malaria in Kenya.";
Hum. Mol. Genet. 6:1357-1360(1997).
[38]
VARIANT KILIFI MET-56, AND VARIANT GLU-469.
PubMed=10391210; DOI=10.1038/10297;
Halushka M.K., Fan J.-B., Bentley K., Hsie L., Shen N., Weder A.,
Cooper R., Lipshutz R., Chakravarti A.;
"Patterns of single-nucleotide polymorphisms in candidate genes for
blood-pressure homeostasis.";
Nat. Genet. 22:239-247(1999).
-!- FUNCTION: ICAM proteins are ligands for the leukocyte adhesion
protein LFA-1 (integrin alpha-L/beta-2). During leukocyte trans-
endothelial migration, ICAM1 engagement promotes the assembly of
endothelial apical cups through ARHGEF26/SGEF and RHOG activation.
{ECO:0000269|PubMed:11173916, ECO:0000269|PubMed:17875742}.
-!- FUNCTION: (Microbial infection) Acts as a receptor for major
receptor group rhinovirus A-B capsid proteins (PubMed:1968231,
PubMed:2538243). Acts as a receptor for Coxsackievirus A21 capsid
proteins (PubMed:11160747, PubMed:16004874, PubMed:9539703). Upon
Kaposi's sarcoma-associated herpesvirus/HHV-8 infection, is
degraded by viral E3 ubiquitin ligase MIR2, presumably to prevent
lysis of infected cells by cytotoxic T-lymphocytes and NK cell
(PubMed:11413168). {ECO:0000269|PubMed:11160747,
ECO:0000269|PubMed:11413168, ECO:0000269|PubMed:16004874,
ECO:0000269|PubMed:1968231, ECO:0000269|PubMed:2538243,
ECO:0000269|PubMed:9539703}.
-!- SUBUNIT: Homodimer (Probable). Interacts with MUC1 and promotes
cell aggregation in epithelial cells. Interacts with
ARHGEF26/SGEF. {ECO:0000269|PubMed:11173916,
ECO:0000269|PubMed:12526797, ECO:0000269|PubMed:15099525,
ECO:0000269|PubMed:17875742, ECO:0000305}.
-!- SUBUNIT: (Microbial infection) Interacts with major receptor group
rhinovirus A-B capsid proteins (PubMed:1968231, PubMed:2538243).
{ECO:0000269|PubMed:1968231, ECO:0000269|PubMed:2538243}.
-!- SUBUNIT: (Microbial infection) Interacts with Coxsackievirus A21
capsid proteins (PubMed:11160747, PubMed:16004874,
PubMed:9539703). {ECO:0000269|PubMed:11160747,
ECO:0000269|PubMed:16004874, ECO:0000269|PubMed:9539703}.
-!- INTERACTION:
P20701:ITGAL; NbExp=2; IntAct=EBI-1035358, EBI-961214;
-!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
protein.
-!- PTM: Monoubiquitinated, which is promoted by MARCH9 and leads to
endocytosis.
-!- POLYMORPHISM: Homozygotes with ICAM1-Kalifi Met-56 seem to have an
increased risk for cerebral malaria [MIM:611162].
{ECO:0000269|PubMed:9259284}.
-!- SIMILARITY: Belongs to the immunoglobulin superfamily. ICAM
family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/ICAM1ID40909ch19p13.html";
-!- WEB RESOURCE: Name=Wikipedia; Note=Intercellular adhesion molecule
entry;
URL="https://en.wikipedia.org/wiki/Intercellular_adhesion_molecule";
-!- WEB RESOURCE: Name=SeattleSNPs;
URL="http://pga.gs.washington.edu/data/icam1/";
-!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral
capsid structure;
URL="http://viperdb.scripps.edu/info_page.php?VDB=1z7z";
-!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
Note=ICAM-1;
URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_hum_Itlect_261";
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EMBL; X06990; CAA30051.1; -; mRNA.
EMBL; J03132; AAA52709.1; -; mRNA.
EMBL; M24283; AAA52708.1; -; mRNA.
EMBL; X59286; CAA41977.1; -; Genomic_DNA.
EMBL; X59287; CAA41977.1; JOINED; Genomic_DNA.
EMBL; X59288; CAA41977.1; JOINED; Genomic_DNA.
EMBL; BT006854; AAP35500.1; -; mRNA.
EMBL; AY225514; AAO30128.1; -; Genomic_DNA.
EMBL; AK312636; BAG35520.1; -; mRNA.
EMBL; CH471106; EAW84086.1; -; Genomic_DNA.
EMBL; BC015969; AAH15969.1; -; mRNA.
EMBL; X57151; CAA40441.1; -; Genomic_DNA.
EMBL; AF340039; AAQ14902.1; -; mRNA.
CCDS; CCDS12231.1; -.
PIR; A29849; A29849.
RefSeq; NP_000192.2; NM_000201.2.
UniGene; Hs.643447; -.
PDB; 1D3E; EM; 28.00 A; I=28-212.
PDB; 1D3I; EM; 26.00 A; I=28-212.
PDB; 1D3L; X-ray; 3.25 A; A=28-212.
PDB; 1IAM; X-ray; 2.10 A; A=28-212.
PDB; 1IC1; X-ray; 3.00 A; A/B=28-217.
PDB; 1IJ4; Model; -; I=44-109.
PDB; 1MQ8; X-ray; 3.30 A; A/C=28-318.
PDB; 1P53; X-ray; 3.06 A; A/B=212-477.
PDB; 1Z7Z; EM; 8.00 A; I=28-477.
PDB; 2OZ4; X-ray; 2.70 A; A=213-477.
PDB; 3TCX; X-ray; 3.60 A; A/C/E/G/I/K/M/O/Q/S/U/W/Y/a=29-112.
PDB; 5MZA; X-ray; 2.78 A; B=28-212.
PDBsum; 1D3E; -.
PDBsum; 1D3I; -.
PDBsum; 1D3L; -.
PDBsum; 1IAM; -.
PDBsum; 1IC1; -.
PDBsum; 1IJ4; -.
PDBsum; 1MQ8; -.
PDBsum; 1P53; -.
PDBsum; 1Z7Z; -.
PDBsum; 2OZ4; -.
PDBsum; 3TCX; -.
PDBsum; 5MZA; -.
ProteinModelPortal; P05362; -.
SMR; P05362; -.
BioGrid; 109610; 175.
DIP; DIP-36658N; -.
IntAct; P05362; 12.
MINT; MINT-4053071; -.
STRING; 9606.ENSP00000264832; -.
BindingDB; P05362; -.
ChEMBL; CHEMBL3070; -.
DrugBank; DB08818; Hyaluronic acid.
DrugBank; DB00108; Natalizumab.
iPTMnet; P05362; -.
PhosphoSitePlus; P05362; -.
BioMuta; ICAM1; -.
DMDM; 68067956; -.
EPD; P05362; -.
MaxQB; P05362; -.
PaxDb; P05362; -.
PeptideAtlas; P05362; -.
PRIDE; P05362; -.
DNASU; 3383; -.
Ensembl; ENST00000264832; ENSP00000264832; ENSG00000090339.
GeneID; 3383; -.
KEGG; hsa:3383; -.
UCSC; uc002mnq.3; human.
CTD; 3383; -.
DisGeNET; 3383; -.
EuPathDB; HostDB:ENSG00000090339.8; -.
GeneCards; ICAM1; -.
HGNC; HGNC:5344; ICAM1.
HPA; CAB002142; -.
HPA; HPA002126; -.
HPA; HPA004877; -.
MalaCards; ICAM1; -.
MIM; 147840; gene.
MIM; 611162; phenotype.
neXtProt; NX_P05362; -.
OpenTargets; ENSG00000090339; -.
PharmGKB; PA29592; -.
eggNOG; ENOG410IPHM; Eukaryota.
eggNOG; ENOG410YQ1Q; LUCA.
GeneTree; ENSGT00530000063246; -.
HOGENOM; HOG000059554; -.
HOVERGEN; HBG052074; -.
InParanoid; P05362; -.
KO; K06490; -.
OMA; QTLRCQA; -.
OrthoDB; EOG091G022Y; -.
PhylomeDB; P05362; -.
TreeFam; TF333745; -.
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-6783783; Interleukin-10 signaling.
Reactome; R-HSA-6785807; Interleukin-4 and 13 signaling.
Reactome; R-HSA-877300; Interferon gamma signaling.
SABIO-RK; P05362; -.
SIGNOR; P05362; -.
ChiTaRS; ICAM1; human.
EvolutionaryTrace; P05362; -.
GeneWiki; ICAM-1; -.
GenomeRNAi; 3383; -.
PMAP-CutDB; P05362; -.
PRO; PR:P05362; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000090339; -.
CleanEx; HS_ICAM1; -.
ExpressionAtlas; P05362; baseline and differential.
Genevisible; P05362; HS.
GO; GO:0009986; C:cell surface; IDA:UniProtKB.
GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0031012; C:extracellular matrix; IDA:BHF-UCL.
GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
GO; GO:0005925; C:focal adhesion; IDA:UniProtKB.
GO; GO:0001772; C:immunological synapse; IEA:Ensembl.
GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0045121; C:membrane raft; IEA:Ensembl.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0005178; F:integrin binding; IDA:MGI.
GO; GO:0004872; F:receptor activity; TAS:ProtInc.
GO; GO:0004888; F:transmembrane signaling receptor activity; TAS:ProtInc.
GO; GO:0001618; F:virus receptor activity; IEA:UniProtKB-KW.
GO; GO:0002438; P:acute inflammatory response to antigenic stimulus; IEA:Ensembl.
GO; GO:0044406; P:adhesion of symbiont to host; IDA:BHF-UCL.
GO; GO:0007155; P:cell adhesion; IDA:BHF-UCL.
GO; GO:0033627; P:cell adhesion mediated by integrin; IEA:Ensembl.
GO; GO:0007569; P:cell aging; IEA:Ensembl.
GO; GO:0071312; P:cellular response to alkaloid; IEA:Ensembl.
GO; GO:0071549; P:cellular response to dexamethasone stimulus; IEA:Ensembl.
GO; GO:0071333; P:cellular response to glucose stimulus; IEA:Ensembl.
GO; GO:0071456; P:cellular response to hypoxia; IEA:Ensembl.
GO; GO:0071347; P:cellular response to interleukin-1; IEA:Ensembl.
GO; GO:0071354; P:cellular response to interleukin-6; IEA:Ensembl.
GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEA:Ensembl.
GO; GO:0071222; P:cellular response to lipopolysaccharide; IEA:Ensembl.
GO; GO:0031669; P:cellular response to nutrient levels; IEA:Ensembl.
GO; GO:0071356; P:cellular response to tumor necrosis factor; IEA:Ensembl.
GO; GO:0061028; P:establishment of endothelial barrier; IGI:UniProtKB.
GO; GO:0090557; P:establishment of endothelial intestinal barrier; IEA:Ensembl.
GO; GO:0097368; P:establishment of Sertoli cell barrier; 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; TAS:BHF-UCL.
GO; GO:0060333; P:interferon-gamma-mediated signaling pathway; TAS:Reactome.
GO; GO:0007159; P:leukocyte cell-cell adhesion; IMP:BHF-UCL.
GO; GO:0050900; P:leukocyte migration; IEP:BHF-UCL.
GO; GO:0022614; P:membrane to membrane docking; IEP:BHF-UCL.
GO; GO:0051926; P:negative regulation of calcium ion transport; IEA:Ensembl.
GO; GO:2000352; P:negative regulation of endothelial cell apoptotic process; IDA:BHF-UCL.
GO; GO:1902042; P:negative regulation of extrinsic apoptotic signaling pathway via death domain receptors; IDA:BHF-UCL.
GO; GO:0001541; P:ovarian follicle development; IEA:Ensembl.
GO; GO:0030838; P:positive regulation of actin filament polymerization; IEA:Ensembl.
GO; GO:0002693; P:positive regulation of cellular extravasation; IMP:BHF-UCL.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IMP:BHF-UCL.
GO; GO:0043547; P:positive regulation of GTPase activity; IEA:Ensembl.
GO; GO:1904996; P:positive regulation of leukocyte adhesion to vascular endothelial cell; IEA:Ensembl.
GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IEA:Ensembl.
GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; IEA:Ensembl.
GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IEA:Ensembl.
GO; GO:0045907; P:positive regulation of vasoconstriction; IEA:Ensembl.
GO; GO:0046813; P:receptor-mediated virion attachment to host cell; IDA:BHF-UCL.
GO; GO:0008360; P:regulation of cell shape; IEA:Ensembl.
GO; GO:0050776; P:regulation of immune response; TAS:Reactome.
GO; GO:0001910; P:regulation of leukocyte mediated cytotoxicity; TAS:BHF-UCL.
GO; GO:1900027; P:regulation of ruffle assembly; IEA:Ensembl.
GO; GO:0043200; P:response to amino acid; IEA:Ensembl.
GO; GO:0001975; P:response to amphetamine; IEA:Ensembl.
GO; GO:0046688; P:response to copper ion; IEA:Ensembl.
GO; GO:0042493; P:response to drug; IEA:Ensembl.
GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
GO; GO:0034698; P:response to gonadotropin; IEA:Ensembl.
GO; GO:0032868; P:response to insulin; IEA:Ensembl.
GO; GO:0010212; P:response to ionizing radiation; IEA:Ensembl.
GO; GO:0010477; P:response to sulfur dioxide; IEA:Ensembl.
GO; GO:0007605; P:sensory perception of sound; IEA:Ensembl.
GO; GO:0002291; P:T cell activation via T cell receptor contact with antigen bound to MHC molecule on antigen presenting cell; IMP:BHF-UCL.
GO; GO:0002457; P:T cell antigen processing and presentation; IEA:Ensembl.
Gene3D; 2.60.40.10; -; 6.
InterPro; IPR003988; ICAM.
InterPro; IPR013768; ICAM_N.
InterPro; IPR003987; ICAM_VCAM_N.
InterPro; IPR036179; Ig-like_dom_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR003599; Ig_sub.
Pfam; PF03921; ICAM_N; 1.
PRINTS; PR01473; ICAM.
PRINTS; PR01472; ICAMVCAM1.
SMART; SM00409; IG; 3.
SUPFAM; SSF48726; SSF48726; 5.
1: Evidence at protein level;
3D-structure; Cell adhesion; Complete proteome;
Direct protein sequencing; Disulfide bond; Glycoprotein;
Host cell receptor for virus entry; Host-virus interaction;
Immunoglobulin domain; Membrane; Phosphoprotein; Polymorphism;
Receptor; Reference proteome; Repeat; Signal; Transmembrane;
Transmembrane helix; Ubl conjugation.
SIGNAL 1 27
CHAIN 28 532 Intercellular adhesion molecule 1.
/FTId=PRO_0000014783.
TOPO_DOM 28 480 Extracellular. {ECO:0000255}.
TRANSMEM 481 503 Helical. {ECO:0000255}.
TOPO_DOM 504 532 Cytoplasmic. {ECO:0000255}.
DOMAIN 41 103 Ig-like C2-type 1.
DOMAIN 128 193 Ig-like C2-type 2.
DOMAIN 230 297 Ig-like C2-type 3.
DOMAIN 325 378 Ig-like C2-type 4.
DOMAIN 412 464 Ig-like C2-type 5.
MOTIF 152 154 Cell attachment site; atypical.
{ECO:0000255}.
MOD_RES 521 521 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 530 530 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:24275569}.
CARBOHYD 130 130 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:12526797,
ECO:0000269|PubMed:9539702}.
CARBOHYD 145 145 N-linked (GlcNAc...) (complex)
asparagine. {ECO:0000269|PubMed:12526797,
ECO:0000269|PubMed:19139490,
ECO:0000269|PubMed:19349973,
ECO:0000269|PubMed:9539702}.
CARBOHYD 183 183 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:12526797,
ECO:0000269|PubMed:9539702}.
CARBOHYD 202 202 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:12526797,
ECO:0000269|PubMed:19159218,
ECO:0000269|PubMed:9539702,
ECO:0000269|PubMed:9539703}.
CARBOHYD 260 260 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218}.
CARBOHYD 267 267 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:15099525,
ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:19159218,
ECO:0000269|PubMed:19349973}.
CARBOHYD 296 296 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:15099525}.
CARBOHYD 385 385 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:15099525}.
CARBOHYD 406 406 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 48 92 {ECO:0000244|PDB:1IAM,
ECO:0000244|PDB:1IC1,
ECO:0000244|PDB:1MQ8,
ECO:0000269|PubMed:12526797,
ECO:0000269|PubMed:9539702,
ECO:0000269|PubMed:9539703}.
DISULFID 52 96 {ECO:0000244|PDB:1IAM,
ECO:0000244|PDB:1IC1,
ECO:0000244|PDB:1MQ8,
ECO:0000269|PubMed:12526797,
ECO:0000269|PubMed:9539702,
ECO:0000269|PubMed:9539703}.
DISULFID 135 186 {ECO:0000244|PDB:1IAM,
ECO:0000244|PDB:1IC1,
ECO:0000244|PDB:1MQ8,
ECO:0000269|PubMed:12526797,
ECO:0000269|PubMed:9539702,
ECO:0000269|PubMed:9539703}.
DISULFID 237 290 {ECO:0000244|PDB:1P53,
ECO:0000269|PubMed:15099525}.
DISULFID 332 371 {ECO:0000244|PDB:1P53,
ECO:0000269|PubMed:15099525}.
DISULFID 403 419 {ECO:0000244|PDB:1P53,
ECO:0000269|PubMed:15099525}.
DISULFID 431 457 {ECO:0000244|PDB:1P53,
ECO:0000269|PubMed:15099525}.
VARIANT 34 34 S -> C (in dbSNP:rs5491).
/FTId=VAR_049879.
VARIANT 56 56 K -> M (in Kilifi; at homozygosity it is
associated with increased susceptibility
to cerebral malaria; dbSNP:rs5491).
{ECO:0000269|PubMed:10391210,
ECO:0000269|PubMed:9259284,
ECO:0000269|Ref.6}.
/FTId=VAR_010204.
VARIANT 155 155 K -> N (in dbSNP:rs5492).
/FTId=VAR_014651.
VARIANT 241 241 G -> R (in dbSNP:rs1799969).
{ECO:0000269|PubMed:7525451,
ECO:0000269|PubMed:8557254,
ECO:0000269|Ref.6}.
/FTId=VAR_014186.
VARIANT 315 315 V -> M (in dbSNP:rs5495).
/FTId=VAR_014652.
VARIANT 352 352 P -> L (in dbSNP:rs1801714).
{ECO:0000269|Ref.6}.
/FTId=VAR_014653.
VARIANT 397 397 R -> Q (in dbSNP:rs5497).
{ECO:0000269|Ref.6}.
/FTId=VAR_014654.
VARIANT 469 469 K -> E (in dbSNP:rs5498).
{ECO:0000269|PubMed:10391210,
ECO:0000269|PubMed:15572059,
ECO:0000269|PubMed:1680919,
ECO:0000269|PubMed:3340213,
ECO:0000269|PubMed:3349522,
ECO:0000269|PubMed:7525451}.
/FTId=VAR_014187.
VARIANT 478 478 R -> W (in dbSNP:rs5030400).
{ECO:0000269|Ref.6}.
/FTId=VAR_016267.
CONFLICT 9 10 AL -> PV (in Ref. 10; CAA40441).
{ECO:0000305}.
CONFLICT 17 17 L -> F (in Ref. 11; AAQ14902).
{ECO:0000305}.
CONFLICT 27 27 A -> V (in Ref. 11; AAQ14902).
{ECO:0000305}.
STRAND 29 39 {ECO:0000244|PDB:1IAM}.
STRAND 42 50 {ECO:0000244|PDB:1IAM}.
STRAND 52 54 {ECO:0000244|PDB:1IAM}.
STRAND 56 61 {ECO:0000244|PDB:1IAM}.
STRAND 66 69 {ECO:0000244|PDB:1IAM}.
STRAND 71 84 {ECO:0000244|PDB:1IAM}.
STRAND 91 95 {ECO:0000244|PDB:1IAM}.
STRAND 97 99 {ECO:0000244|PDB:1IC1}.
STRAND 100 104 {ECO:0000244|PDB:1IAM}.
STRAND 106 111 {ECO:0000244|PDB:1IAM}.
STRAND 114 118 {ECO:0000244|PDB:1IAM}.
STRAND 123 125 {ECO:0000244|PDB:1IAM}.
STRAND 129 138 {ECO:0000244|PDB:1IAM}.
HELIX 143 145 {ECO:0000244|PDB:1IAM}.
STRAND 146 152 {ECO:0000244|PDB:1IAM}.
STRAND 155 161 {ECO:0000244|PDB:1IAM}.
TURN 164 166 {ECO:0000244|PDB:1IAM}.
STRAND 167 174 {ECO:0000244|PDB:1IAM}.
HELIX 177 179 {ECO:0000244|PDB:1IC1}.
STRAND 183 191 {ECO:0000244|PDB:1IAM}.
HELIX 193 195 {ECO:0000244|PDB:1IAM}.
STRAND 199 203 {ECO:0000244|PDB:1IAM}.
STRAND 210 212 {ECO:0000244|PDB:1IC1}.
STRAND 220 222 {ECO:0000244|PDB:2OZ4}.
STRAND 225 228 {ECO:0000244|PDB:2OZ4}.
STRAND 231 241 {ECO:0000244|PDB:2OZ4}.
HELIX 245 247 {ECO:0000244|PDB:2OZ4}.
STRAND 249 254 {ECO:0000244|PDB:2OZ4}.
STRAND 262 265 {ECO:0000244|PDB:2OZ4}.
STRAND 267 278 {ECO:0000244|PDB:2OZ4}.
HELIX 280 282 {ECO:0000244|PDB:2OZ4}.
STRAND 284 294 {ECO:0000244|PDB:2OZ4}.
STRAND 297 308 {ECO:0000244|PDB:2OZ4}.
STRAND 314 318 {ECO:0000244|PDB:2OZ4}.
STRAND 320 323 {ECO:0000244|PDB:2OZ4}.
STRAND 327 333 {ECO:0000244|PDB:2OZ4}.
STRAND 338 344 {ECO:0000244|PDB:2OZ4}.
STRAND 346 348 {ECO:0000244|PDB:2OZ4}.
STRAND 351 354 {ECO:0000244|PDB:2OZ4}.
STRAND 357 359 {ECO:0000244|PDB:2OZ4}.
HELIX 362 364 {ECO:0000244|PDB:2OZ4}.
STRAND 367 376 {ECO:0000244|PDB:2OZ4}.
STRAND 378 397 {ECO:0000244|PDB:2OZ4}.
HELIX 400 402 {ECO:0000244|PDB:2OZ4}.
STRAND 405 410 {ECO:0000244|PDB:2OZ4}.
STRAND 422 425 {ECO:0000244|PDB:2OZ4}.
STRAND 428 433 {ECO:0000244|PDB:2OZ4}.
TURN 434 436 {ECO:0000244|PDB:2OZ4}.
HELIX 449 451 {ECO:0000244|PDB:2OZ4}.
STRAND 453 461 {ECO:0000244|PDB:2OZ4}.
STRAND 464 475 {ECO:0000244|PDB:2OZ4}.
SEQUENCE 532 AA; 57825 MW; 550089365A733AFB CRC64;
MAPSSPRPAL PALLVLLGAL FPGPGNAQTS VSPSKVILPR GGSVLVTCST SCDQPKLLGI
ETPLPKKELL LPGNNRKVYE LSNVQEDSQP MCYSNCPDGQ STAKTFLTVY WTPERVELAP
LPSWQPVGKN LTLRCQVEGG APRANLTVVL LRGEKELKRE PAVGEPAEVT TTVLVRRDHH
GANFSCRTEL DLRPQGLELF ENTSAPYQLQ TFVLPATPPQ LVSPRVLEVD TQGTVVCSLD
GLFPVSEAQV HLALGDQRLN PTVTYGNDSF SAKASVSVTA EDEGTQRLTC AVILGNQSQE
TLQTVTIYSF PAPNVILTKP EVSEGTEVTV KCEAHPRAKV TLNGVPAQPL GPRAQLLLKA
TPEDNGRSFS CSATLEVAGQ LIHKNQTREL RVLYGPRLDE RDCPGNWTWP ENSQQTPMCQ
AWGNPLPELK CLKDGTFPLP IGESVTVTRD LEGTYLCRAR STQGEVTRKV TVNVLSPRYE
IVIITVVAAA VIMGTAGLST YLYNRQRKIK KYRLQQAQKG TPMKPNTQAT PP


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