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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.
17-JUN-2020, entry version 240.
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; DOI=10.1016/s0171-2985(11)80585-1;
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 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]
INTERACTION WITH CD81, INTERACTION WITH CD9, AND INTERACTION WITH CD247.
PubMed=23858057; DOI=10.1128/mcb.00302-13;
Rocha-Perugini V., Zamai M., Gonzalez-Granado J.M., Barreiro O., Tejera E.,
Yanez-Mo M., Caiolfa V.R., Sanchez-Madrid F.;
"CD81 controls sustained T cell activation signaling and defines the
maturation stages of cognate immunological synapses.";
Mol. Cell. Biol. 33:3644-3658(2013).
[28]
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).
[29]
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).
[30]
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).
[31]
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).
[32]
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).
[33]
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).
[34]
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).
[35]
STRUCTURE BY ELECTRON MICROSCOPY (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).
[36]
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).
[37]
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).
[38]
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).
[39]
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. {ECO:0000269|PubMed:1968231,
ECO:0000269|PubMed:2538243}.
-!- FUNCTION: (Microbial infection) Acts as a receptor for Coxsackievirus
A21 capsid proteins. {ECO:0000269|PubMed:11160747,
ECO:0000269|PubMed:16004874, ECO:0000269|PubMed:9539703}.
-!- FUNCTION: (Microbial infection) 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. {ECO:0000269|PubMed:11413168}.
-!- SUBUNIT: Homodimer (Probable). Interacts with MUC1 and promotes cell
aggregation in epithelial cells. Interacts with ARHGEF26/SGEF.
Interacts (on T cell side) with CD81, CD247 and CD9 at immunological
synapses between antigen-presenting cells and T cells.
{ECO:0000269|PubMed:11173916, ECO:0000269|PubMed:12526797,
ECO:0000269|PubMed:15099525, ECO:0000269|PubMed:17875742,
ECO:0000269|PubMed:23858057, 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:
P05362; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-1035358, EBI-3867333;
P05362; P20701: ITGAL; NbExp=2; IntAct=EBI-1035358, EBI-961214;
P05362; Q14145: KEAP1; NbExp=3; IntAct=EBI-1035358, EBI-751001;
P05362; P60410: KRTAP10-8; NbExp=3; IntAct=EBI-1035358, EBI-10171774;
P05362; Q9UHD9: UBQLN2; NbExp=5; IntAct=EBI-1035358, EBI-947187;
-!- 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.
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.
PDB; 6EIT; EM; 3.90 A; 4=28-112.
PDB; 6S8U; X-ray; 3.67 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; -.
PDBsum; 6EIT; -.
PDBsum; 6S8U; -.
SMR; P05362; -.
BioGRID; 109610; 210.
DIP; DIP-36658N; -.
IntAct; P05362; 45.
MINT; P05362; -.
STRING; 9606.ENSP00000264832; -.
BindingDB; P05362; -.
ChEMBL; CHEMBL3070; -.
DrugBank; DB08818; Hyaluronic acid.
DrugBank; DB12598; Nafamostat.
DrugBank; DB00108; Natalizumab.
DrugCentral; P05362; -.
GlyConnect; 1423; -.
iPTMnet; P05362; -.
PhosphoSitePlus; P05362; -.
BioMuta; ICAM1; -.
DMDM; 68067956; -.
CPTAC; CPTAC-219; -.
CPTAC; CPTAC-220; -.
CPTAC; non-CPTAC-2679; -.
EPD; P05362; -.
jPOST; P05362; -.
MassIVE; P05362; -.
MaxQB; P05362; -.
PaxDb; P05362; -.
PeptideAtlas; P05362; -.
PRIDE; P05362; -.
ProteomicsDB; 51830; -.
ABCD; P05362; 3 sequenced antibodies.
Antibodypedia; 795; 2888 antibodies.
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; ENSG00000090339; Tissue enhanced (liver, lung).
MalaCards; ICAM1; -.
MIM; 147840; gene.
MIM; 611162; phenotype.
neXtProt; NX_P05362; -.
OpenTargets; ENSG00000090339; -.
PharmGKB; PA29592; -.
eggNOG; ENOG410IPHM; Eukaryota.
eggNOG; ENOG410YQ1Q; LUCA.
GeneTree; ENSGT00940000162311; -.
HOGENOM; CLU_036160_1_1_1; -.
InParanoid; P05362; -.
KO; K06490; -.
OMA; TFLTVYW; -.
OrthoDB; 731140at2759; -.
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 Interleukin-13 signaling.
Reactome; R-HSA-877300; Interferon gamma signaling.
SABIO-RK; P05362; -.
SIGNOR; P05362; -.
BioGRID-ORCS; 3383; 6 hits in 787 CRISPR screens.
ChiTaRS; ICAM1; human.
EvolutionaryTrace; P05362; -.
GeneWiki; ICAM-1; -.
GenomeRNAi; 3383; -.
Pharos; P05362; Tchem.
PRO; PR:P05362; -.
Proteomes; UP000005640; Chromosome 19.
RNAct; P05362; protein.
Bgee; ENSG00000090339; Expressed in lung and 204 other tissues.
ExpressionAtlas; P05362; baseline and differential.
Genevisible; P05362; HS.
GO; GO:0005623; C:cell; IEA:GOC.
GO; GO:0009986; C:cell surface; HDA:UniProtKB.
GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
GO; GO:0001772; C:immunological synapse; IEA:Ensembl.
GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
GO; GO:0016020; C:membrane; HDA: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:0038023; F:signaling 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:1904646; P:cellular response to amyloid-beta; IDA:ARUK-UCL.
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:0019221; P:cytokine-mediated signaling pathway; TAS:Reactome.
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: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.
GO; GO:0072683; P:T cell extravasation; IEA:Ensembl.
Gene3D; 2.60.40.10; -; 5.
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; 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
/note="Intercellular adhesion molecule 1"
/id="PRO_0000014783"
TOPO_DOM 28..480
/note="Extracellular"
/evidence="ECO:0000255"
TRANSMEM 481..503
/note="Helical"
/evidence="ECO:0000255"
TOPO_DOM 504..532
/note="Cytoplasmic"
/evidence="ECO:0000255"
DOMAIN 41..103
/note="Ig-like C2-type 1"
DOMAIN 128..193
/note="Ig-like C2-type 2"
DOMAIN 230..297
/note="Ig-like C2-type 3"
DOMAIN 325..378
/note="Ig-like C2-type 4"
DOMAIN 412..464
/note="Ig-like C2-type 5"
MOTIF 152..154
/note="Cell attachment site; atypical"
/evidence="ECO:0000255"
MOD_RES 521
/note="Phosphothreonine"
/evidence="ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231, ECO:0000244|PubMed:23186163"
MOD_RES 530
/note="Phosphothreonine"
/evidence="ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231, ECO:0000244|PubMed:24275569"
CARBOHYD 130
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000269|PubMed:12526797,
ECO:0000269|PubMed:9539702"
CARBOHYD 145
/note="N-linked (GlcNAc...) (complex) asparagine"
/evidence="ECO:0000269|PubMed:12526797,
ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19349973,
ECO:0000269|PubMed:9539702"
CARBOHYD 183
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000269|PubMed:12526797,
ECO:0000269|PubMed:9539702"
CARBOHYD 202
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000269|PubMed:12526797,
ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:9539702,
ECO:0000269|PubMed:9539703"
CARBOHYD 267
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000269|PubMed:15099525,
ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218,
ECO:0000269|PubMed:19349973"
CARBOHYD 296
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000269|PubMed:15099525"
CARBOHYD 385
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000269|PubMed:15099525"
CARBOHYD 406
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
DISULFID 48..92
/evidence="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
/evidence="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
/evidence="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
/evidence="ECO:0000244|PDB:1P53,
ECO:0000269|PubMed:15099525"
DISULFID 332..371
/evidence="ECO:0000244|PDB:1P53,
ECO:0000269|PubMed:15099525"
DISULFID 403..419
/evidence="ECO:0000244|PDB:1P53,
ECO:0000269|PubMed:15099525"
DISULFID 431..457
/evidence="ECO:0000244|PDB:1P53,
ECO:0000269|PubMed:15099525"
VARIANT 34
/note="S -> C (in dbSNP:rs5491)"
/id="VAR_049879"
VARIANT 56
/note="K -> M (in Kilifi; at homozygosity it is associated
with increased susceptibility to cerebral malaria;
dbSNP:rs5491)"
/evidence="ECO:0000269|PubMed:10391210,
ECO:0000269|PubMed:9259284, ECO:0000269|Ref.6"
/id="VAR_010204"
VARIANT 155
/note="K -> N (in dbSNP:rs5492)"
/id="VAR_014651"
VARIANT 241
/note="G -> R (in dbSNP:rs1799969)"
/evidence="ECO:0000269|PubMed:7525451,
ECO:0000269|PubMed:8557254, ECO:0000269|Ref.6"
/id="VAR_014186"
VARIANT 315
/note="V -> M (in dbSNP:rs5495)"
/id="VAR_014652"
VARIANT 352
/note="P -> L (in dbSNP:rs1801714)"
/evidence="ECO:0000269|Ref.6"
/id="VAR_014653"
VARIANT 397
/note="R -> Q (in dbSNP:rs5497)"
/evidence="ECO:0000269|Ref.6"
/id="VAR_014654"
VARIANT 469
/note="K -> E (in dbSNP:rs5498)"
/evidence="ECO:0000269|PubMed:10391210,
ECO:0000269|PubMed:15572059, ECO:0000269|PubMed:1680919,
ECO:0000269|PubMed:3340213, ECO:0000269|PubMed:3349522,
ECO:0000269|PubMed:7525451"
/id="VAR_014187"
VARIANT 478
/note="R -> W (in dbSNP:rs5030400)"
/evidence="ECO:0000269|Ref.6"
/id="VAR_016267"
CONFLICT 9..10
/note="AL -> PV (in Ref. 10; CAA40441)"
/evidence="ECO:0000305"
CONFLICT 17
/note="L -> F (in Ref. 11; AAQ14902)"
/evidence="ECO:0000305"
CONFLICT 27
/note="A -> V (in Ref. 11; AAQ14902)"
/evidence="ECO:0000305"
STRAND 29..39
/evidence="ECO:0000244|PDB:1IAM"
STRAND 42..50
/evidence="ECO:0000244|PDB:1IAM"
STRAND 52..54
/evidence="ECO:0000244|PDB:1IAM"
STRAND 56..61
/evidence="ECO:0000244|PDB:1IAM"
STRAND 66..69
/evidence="ECO:0000244|PDB:1IAM"
STRAND 71..84
/evidence="ECO:0000244|PDB:1IAM"
STRAND 91..95
/evidence="ECO:0000244|PDB:1IAM"
STRAND 97..99
/evidence="ECO:0000244|PDB:1IC1"
STRAND 100..104
/evidence="ECO:0000244|PDB:1IAM"
STRAND 106..111
/evidence="ECO:0000244|PDB:1IAM"
STRAND 114..118
/evidence="ECO:0000244|PDB:1IAM"
STRAND 123..125
/evidence="ECO:0000244|PDB:1IAM"
STRAND 129..138
/evidence="ECO:0000244|PDB:1IAM"
HELIX 143..145
/evidence="ECO:0000244|PDB:1IAM"
STRAND 146..152
/evidence="ECO:0000244|PDB:1IAM"
STRAND 155..161
/evidence="ECO:0000244|PDB:1IAM"
TURN 164..166
/evidence="ECO:0000244|PDB:1IAM"
STRAND 167..174
/evidence="ECO:0000244|PDB:1IAM"
HELIX 177..179
/evidence="ECO:0000244|PDB:5MZA"
STRAND 183..191
/evidence="ECO:0000244|PDB:1IAM"
HELIX 193..195
/evidence="ECO:0000244|PDB:1IAM"
STRAND 199..203
/evidence="ECO:0000244|PDB:1IAM"
STRAND 210..212
/evidence="ECO:0000244|PDB:5MZA"
STRAND 220..222
/evidence="ECO:0000244|PDB:2OZ4"
STRAND 225..228
/evidence="ECO:0000244|PDB:2OZ4"
STRAND 231..241
/evidence="ECO:0000244|PDB:2OZ4"
HELIX 245..247
/evidence="ECO:0000244|PDB:2OZ4"
STRAND 249..254
/evidence="ECO:0000244|PDB:2OZ4"
STRAND 262..265
/evidence="ECO:0000244|PDB:2OZ4"
STRAND 267..278
/evidence="ECO:0000244|PDB:2OZ4"
HELIX 280..282
/evidence="ECO:0000244|PDB:2OZ4"
STRAND 284..294
/evidence="ECO:0000244|PDB:2OZ4"
STRAND 297..308
/evidence="ECO:0000244|PDB:2OZ4"
STRAND 314..318
/evidence="ECO:0000244|PDB:2OZ4"
STRAND 320..323
/evidence="ECO:0000244|PDB:2OZ4"
STRAND 327..333
/evidence="ECO:0000244|PDB:2OZ4"
STRAND 338..344
/evidence="ECO:0000244|PDB:2OZ4"
STRAND 346..348
/evidence="ECO:0000244|PDB:2OZ4"
STRAND 351..354
/evidence="ECO:0000244|PDB:2OZ4"
STRAND 357..359
/evidence="ECO:0000244|PDB:2OZ4"
HELIX 362..364
/evidence="ECO:0000244|PDB:2OZ4"
STRAND 367..376
/evidence="ECO:0000244|PDB:2OZ4"
STRAND 378..397
/evidence="ECO:0000244|PDB:2OZ4"
HELIX 400..402
/evidence="ECO:0000244|PDB:2OZ4"
STRAND 405..410
/evidence="ECO:0000244|PDB:2OZ4"
STRAND 422..425
/evidence="ECO:0000244|PDB:2OZ4"
STRAND 428..433
/evidence="ECO:0000244|PDB:2OZ4"
TURN 434..436
/evidence="ECO:0000244|PDB:2OZ4"
HELIX 449..451
/evidence="ECO:0000244|PDB:2OZ4"
STRAND 453..461
/evidence="ECO:0000244|PDB:2OZ4"
STRAND 464..475
/evidence="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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KN0117Rb Rabbit intercellular adhesion molecule 1,ICAM-1 per CD54 ELISA Kit 96 WELLS
SL0103Rb Rabbit intercellular adhesion molecule 1,ICAM-1 CD54 ELISA Kit 96T
228-10812-2 Recombinant Human Intercellular Adhesion Molecule-1 (ICAM-1) _ CD54 10
CSB-E06974Rb rabbit intercellular adhesion molecule 1,ICAM-1 per CD54 ELISA Kit 96T
UB-E70147 Canine intercellular adhesion molecule 1,ICAM-1 per CD54 ELISA Kit 96T
UB-E70049 Canine intercellular adhesion molecule 1,ICAM-1 per CD54 ELISA Kit 96T
228-10812-1 Recombinant Human Intercellular Adhesion Molecule-1 (ICAM-1) _ CD54 2
UB-E30194 rabbit intercellular adhesion molecule 1,ICAM-1 per CD54 ELISA Kit 96T
MD-11-0091 Mouse Anti-Human Intercellular Adhesion Molecule-1 (ICAM-1) _ CD54 200
E0534m ELISA Icam2,ICAM-2,Icam-2,Intercellular adhesion molecule 2,Lymphocyte function-associated AG-1 counter-receptor,Mouse,Mus musculus 96T
E0534m ELISA kit Icam2,ICAM-2,Icam-2,Intercellular adhesion molecule 2,Lymphocyte function-associated AG-1 counter-receptor,Mouse,Mus musculus 96T
Pathways :
WP2328: Allograft rejection
WP1963: The effect of Glucocorticoids on target gene expression
WP2118: Arrhythmogenic right ventricular cardiomyopathy
WP74: Integrin-mediated cell adhesion
WP1004: Kit Receptor Signaling Pathway
WP1424: Globo Sphingolipid Metabolism
WP352: T Cell Receptor Signaling Pathway
WP897: Androgen receptor signaling pathway
WP1185: Integrin-mediated cell adhesion
WP444: Signaling of Hepatocyte Growth Factor Receptor
WP927: Signaling of Hepatocyte Growth Factor Receptor
WP1249: EPO Receptor Signaling
WP2272: Pathogenic Escherichia coli infection
WP774: Kit Receptor Signaling Pathway
WP1025: B Cell Receptor Signaling Pathway
WP1491: PI3K_AKT_NFKB pathway
WP794: B Cell Receptor Signaling Pathway
WP1067: Toll-like receptor signaling pathway
WP185: Integrin-mediated cell adhesion
WP566: canonical wnt - zebrafish
WP951: Integrin-mediated cell adhesion
WP1309: Toll-like receptor signaling pathway
WP1345: T Cell Receptor Signaling Pathway
WP258: TGF-beta Receptor Signaling Pathway
WP829: Toll-like receptor signaling pathway

Related Genes :
[Ceacam1 Bgp Bgp1] Carcinoembryonic antigen-related cell adhesion molecule 1 (Biliary glycoprotein 1) (BGP-1) (Biliary glycoprotein D) (MHVR1) (Murine hepatitis virus receptor) (MHV-R) (CD antigen CD66a)
[CD209 CLEC4L] CD209 antigen (C-type lectin domain family 4 member L) (Dendritic cell-specific ICAM-3-grabbing non-integrin 1) (DC-SIGN) (DC-SIGN1) (CD antigen CD209)
[CLEC4M CD209L CD209L1 CD299] C-type lectin domain family 4 member M (CD209 antigen-like protein 1) (DC-SIGN-related protein) (DC-SIGNR) (Dendritic cell-specific ICAM-3-grabbing non-integrin 2) (DC-SIGN2) (Liver/lymph node-specific ICAM-3-grabbing non-integrin) (L-SIGN) (CD antigen CD299)
[ITGAL CD11A] Integrin alpha-L (CD11 antigen-like family member A) (Leukocyte adhesion glycoprotein LFA-1 alpha chain) (LFA-1A) (Leukocyte function-associated molecule 1 alpha chain) (CD antigen CD11a)
[EPCAM GA733-2 M1S2 M4S1 MIC18 TACSTD1 TROP1] Epithelial cell adhesion molecule (Ep-CAM) (Adenocarcinoma-associated antigen) (Cell surface glycoprotein Trop-1) (Epithelial cell surface antigen) (Epithelial glycoprotein) (EGP) (Epithelial glycoprotein 314) (EGP314) (hEGP314) (KS 1/4 antigen) (KSA) (Major gastrointestinal tumor-associated protein GA733-2) (Tumor-associated calcium signal transducer 1) (CD antigen CD326)
[SELL LNHR LYAM1] L-selectin (CD62 antigen-like family member L) (Leukocyte adhesion molecule 1) (LAM-1) (Leukocyte surface antigen Leu-8) (Leukocyte-endothelial cell adhesion molecule 1) (LECAM1) (Lymph node homing receptor) (TQ1) (gp90-MEL) (CD antigen CD62L)
[Cd44 Ly-24] CD44 antigen (Extracellular matrix receptor III) (ECMR-III) (GP90 lymphocyte homing/adhesion receptor) (HUTCH-I) (Hermes antigen) (Hyaluronate receptor) (Lymphocyte antigen 24) (Ly-24) (Phagocytic glycoprotein 1) (PGP-1) (Phagocytic glycoprotein I) (PGP-I) (CD antigen CD44)
[Sell Lnhr Ly-22 Ly22] L-selectin (CD62 antigen-like family member L) (Leukocyte adhesion molecule 1) (LAM-1) (Leukocyte-endothelial cell adhesion molecule 1) (LECAM1) (Lymph node homing receptor) (Lymphocyte antigen 22) (Ly-22) (Lymphocyte surface MEL-14 antigen) (CD antigen CD62L)
[BCAM LU MSK19] Basal cell adhesion molecule (Auberger B antigen) (B-CAM cell surface glycoprotein) (F8/G253 antigen) (Lutheran antigen) (Lutheran blood group glycoprotein) (CD antigen CD239)
[Ceacam1] Carcinoembryonic antigen-related cell adhesion molecule 1 (ATP-dependent taurocolate-carrier protein) (Cell-CAM 105) (C-CAM 105) (Ecto-ATPase) (GP110) (pp120) (CD antigen CD66a)
[Sell Lnhr Ly-22] L-selectin (CD62 antigen-like family member L) (Leukocyte adhesion molecule 1) (LAM-1) (Leukocyte-endothelial cell adhesion molecule 1) (LECAM1) (Lymph node homing receptor) (Lymphocyte antigen 22) (Ly-22) (Lymphocyte surface MEL-14 antigen) (CD antigen CD62L)
[CD44 LHR MDU2 MDU3 MIC4] CD44 antigen (CDw44) (Epican) (Extracellular matrix receptor III) (ECMR-III) (GP90 lymphocyte homing/adhesion receptor) (HUTCH-I) (Heparan sulfate proteoglycan) (Hermes antigen) (Hyaluronate receptor) (Phagocytic glycoprotein 1) (PGP-1) (Phagocytic glycoprotein I) (PGP-I) (CD antigen CD44)
[CEACAM1 BGP BGP1] Carcinoembryonic antigen-related cell adhesion molecule 1 (Biliary glycoprotein 1) (BGP-1) (CD antigen CD66a)
[ITGAM CD11B CR3A] Integrin alpha-M (CD11 antigen-like family member B) (CR-3 alpha chain) (Cell surface glycoprotein MAC-1 subunit alpha) (Leukocyte adhesion receptor MO1) (Neutrophil adherence receptor) (CD antigen CD11b)
[PECAM1] Platelet endothelial cell adhesion molecule (PECAM-1) (EndoCAM) (GPIIA') (PECA1) (CD antigen CD31)
[Cd44] CD44 antigen (Extracellular matrix receptor III) (ECMR-III) (GP90 lymphocyte homing/adhesion receptor) (HUTCH-I) (Hermes antigen) (Hyaluronate receptor) (Phagocytic glycoprotein 1) (PGP-1) (Phagocytic glycoprotein I) (PGP-I) (CD antigen CD44)
[SELE ELAM1] E-selectin (CD62 antigen-like family member E) (Endothelial leukocyte adhesion molecule 1) (ELAM-1) (Leukocyte-endothelial cell adhesion molecule 2) (LECAM2) (CD antigen CD62E)
[CD44] CD44 antigen (Extracellular matrix receptor III) (ECMR-III) (GP90 lymphocyte homing/adhesion receptor) (HAM1 antigen) (HUTCH-I) (Heparan sulfate proteoglycan) (Hermes antigen) (Hyaluronate receptor) (Phagocytic glycoprotein 1) (PGP-1) (Phagocytic glycoprotein I) (PGP-I) (CD antigen CD44)
[Sirpa Bit Myd1 Ptpns1 Shps1 Sirp] Tyrosine-protein phosphatase non-receptor type substrate 1 (SHP substrate 1) (SHPS-1) (Brain Ig-like molecule with tyrosine-based activation motifs) (Bit) (CD172 antigen-like family member A) (Inhibitory receptor SHPS-1) (MyD-1 antigen) (Signal-regulatory protein alpha-1) (Sirp-alpha-1) (mSIRP-alpha1) (p84) (CD antigen CD172a)
[Sele Elam-1] E-selectin (CD62 antigen-like family member E) (Endothelial leukocyte adhesion molecule 1) (ELAM-1) (Leukocyte-endothelial cell adhesion molecule 2) (LECAM2) (CD antigen CD62E)
[SIRPA BIT MFR MYD1 PTPNS1 SHPS1 SIRP] Tyrosine-protein phosphatase non-receptor type substrate 1 (SHP substrate 1) (SHPS-1) (Brain Ig-like molecule with tyrosine-based activation motifs) (Bit) (CD172 antigen-like family member A) (Inhibitory receptor SHPS-1) (Macrophage fusion receptor) (MyD-1 antigen) (Signal-regulatory protein alpha-1) (Sirp-alpha-1) (Signal-regulatory protein alpha-2) (Sirp-alpha-2) (Signal-regulatory protein alpha-3) (Sirp-alpha-3) (p84) (CD antigen CD172a)
[Sele Elam-1] E-selectin (CD62 antigen-like family member E) (Endothelial leukocyte adhesion molecule 1) (ELAM-1) (Leukocyte-endothelial cell adhesion molecule 2) (LECAM2) (CD antigen CD62E)
[CD44] CD44 antigen (Extracellular matrix receptor-III) (ECMR-III) (GP90 lymphocyte homing/adhesion receptor) (HUTCH-I) (Hermes antigen) (Hyaluronate receptor) (Phagocytic glycoprotein 1) (PGP-1) (Phagocytic glycoprotein I) (PGP-I) (CD antigen CD44) (Fragment)
[CD44] CD44 antigen (Extracellular matrix receptor III) (ECMR-III) (GP90 lymphocyte homing/adhesion receptor) (HUTCH-I) (Hermes antigen) (Hyaluronate receptor) (Phagocytic glycoprotein 1) (PGP-1) (Phagocytic glycoprotein I) (PGP-I) (CD antigen CD44)
[CD44] CD44 antigen (Extracellular matrix receptor III) (ECMR-III) (GP90 lymphocyte homing/adhesion receptor) (HUTCH-I) (Hermes antigen) (Hyaluronate receptor) (Phagocytic glycoprotein 1) (PGP-1) (Phagocytic glycoprotein I) (PGP-I) (CD antigen CD44)
[Sirpa Bit Mfr Ptpns1 Shps1 Sirp] Tyrosine-protein phosphatase non-receptor type substrate 1 (SHP substrate 1) (SHPS-1) (Brain Ig-like molecule with tyrosine-based activation motifs) (Bit) (CD172 antigen-like family member A) (Inhibitory receptor SHPS-1) (Macrophage fusion receptor) (Macrophage membrane protein MFP150) (Signal-regulatory protein alpha-1) (Sirp-alpha-1) (CD antigen CD172a)
[SIGLEC7 AIRM1] Sialic acid-binding Ig-like lectin 7 (Siglec-7) (Adhesion inhibitory receptor molecule 1) (AIRM-1) (CDw328) (D-siglec) (QA79 membrane protein) (p75) (CD antigen CD328)
[NECTIN1 HVEC PRR1 PVRL1] Nectin-1 (Herpes virus entry mediator C) (Herpesvirus entry mediator C) (HveC) (Herpesvirus Ig-like receptor) (HIgR) (Nectin cell adhesion molecule 1) (Poliovirus receptor-related protein 1) (CD antigen CD111)
[CD44] CD44 antigen (Extracellular matrix receptor III) (ECMR-III) (GP90 lymphocyte homing/adhesion receptor) (HUTCH-I) (Hermes antigen) (Hyaluronate receptor) (Phagocytic glycoprotein 1) (PGP-1) (Phagocytic glycoprotein I) (PGP-I) (CD antigen CD44)
[CD300A CMRF35H IGSF12 HSPC083] CMRF35-like molecule 8 (CLM-8) (CD300 antigen-like family member A) (CMRF-35-H9) (CMRF35-H9) (CMRF35-H) (IRC1/IRC2) (Immunoglobulin superfamily member 12) (IgSF12) (Inhibitory receptor protein 60) (IRp60) (NK inhibitory receptor) (CD antigen CD300a)

Bibliography :
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