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UniProtKB/Swiss-Prot entry P05362


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name ICAM1_HUMAN
Primary accession number P05362
Secondary accession numbers Q5NKV7 Q96B50
Integrated into Swiss-Prot on November 1, 1988
Sequence was last modified on June 21, 2005 (Sequence version 2)
Annotations were last modified on    November 4, 2008 (Entry version 126)
Name and origin of the protein
Protein name Intercellular adhesion molecule 1 [Precursor]
Synonyms ICAM-1
Major group rhinovirus receptor
CD54 antigen
Gene name
Name: ICAM1
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT GLU-469.
DOI=10.1038/331624a0; PubMed=3340213 [NCBI, ExPASy, EBI, Israel, Japan]
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.
DOI=10.1016/0092-8674(88)90434-5; PubMed=3349522 [NCBI, ExPASy, EBI, Israel, Japan]
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 [NCBI, ExPASy, EBI, Israel, Japan]
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 [NCBI, ExPASy, EBI, Israel, Japan]
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 program for genomic applications;
Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Kidney;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-22.
PubMed=1983003 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[9]
NUCLEOTIDE SEQUENCE [MRNA] OF 5-532, AND VARIANT GLU-469.
TISSUE=Blood;
PubMed=15572059 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[10]
PARTIAL PROTEIN SEQUENCE, AND FUNCTION AS A RHINOVIRUS RECEPTOR.
DOI=10.1016/0092-8674(89)90688-0; PubMed=2538243 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[11]
FUNCTION AS A RHINOVIRUS RECEPTOR.
DOI=10.1038/344070a0; PubMed=1968231 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[12]
INTERACTION WITH MUC1, AND FUNCTION.
DOI=10.1159/000051917; PubMed=11173916 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[13]
INTERACTION WITH COXSACKIEVIRUS A21 CAPSID PROTEINS.
DOI=10.1128/JVI.75.5.2444-2451.2001; PubMed=11160747 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[14]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-267, AND MASS SPECTROMETRY.
TISSUE=Plasma;
DOI=10.1021/pr0502065; PubMed=16335952 [NCBI, ExPASy, EBI, Israel, Japan]
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]
UBIQUITINATION.
DOI=10.1016/j.febslet.2006.11.075; PubMed=17174307 [NCBI, ExPASy, EBI, Israel, Japan]
Hoer S., Smith L., Lehner P.J.;
"MARCH-IX mediates ubiquitination and downregulation of ICAM-1.";
FEBS Lett. 581:45-51(2007).
[16]
INTERACTION WITH SGEF, AND FUNCTION.
DOI=10.1083/jcb.200612053; PubMed=17875742 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[17]
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 28-217.
DOI=10.1073/pnas.95.8.4134; PubMed=9539702 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[18]
X-RAY CRYSTALLOGRAPHY (3.25 ANGSTROMS) OF 28-212 IN COMPLEX WITH HUMAN RHINOVIRUS 14.
DOI=10.1073/pnas.95.8.4140; PubMed=9539703 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[19]
X-RAY CRYSTALLOGRAPHY (3.25 ANGSTROMS) OF 28-212.
DOI=10.1093/emboj/18.22.6249; PubMed=10562537 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[20]
X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF 28-318 IN COMPLEX WITH ITGAL VWFA DOMAIN, DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-130; ASN-145; ASN-183 AND ASN-202.
DOI=10.1016/S0092-8674(02)01257-6; PubMed=12526797 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[21]
X-RAY CRYSTALLOGRAPHY (3.06 ANGSTROMS) OF 212-477, SUBUNIT, DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-267; ASN-296 AND ASN-385.
DOI=10.1016/S1097-2765(04)00204-7; PubMed=15099525 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[22]
STRUCTURE BY ELECTRON MICROSCOPY (8.0 ANGSTROMS) OF 24-473 IN COMPLEX WITH COXSACKIEVIRUS A21, AND SUBUNIT.
DOI=10.1016/j.str.2005.04.011; PubMed=16004874 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[23]
VARIANTS ARG-241 AND GLU-469.
DOI=10.1006/geno.1994.1303; PubMed=7525451 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[24]
VARIANT ARG-241.
DOI=10.1007/BF00218826; PubMed=8557254 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[25]
VARIANT KILIFI MET-56.
DOI=10.1093/hmg/6.8.1357; PubMed=9259284 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[26]
VARIANT KILIFI MET-56, AND VARIANT GLU-469.
DOI=10.1038/10297; PubMed=10391210 [NCBI, ExPASy, EBI, Israel, Japan]
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).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X06990; CAA30051.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
J03132; AAA52709.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M24283; AAA52708.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X59286; CAA41977.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X59287; CAA41977.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X59288; CAA41977.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BT006854; AAP35500.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY225514; AAO30128.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC015969; AAH15969.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X57151; CAA40441.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF340039; AAQ14902.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A29849; A29849.
RefSeq NP_000192.2; -.
UniGene Hs.643447
3D structure databases
PDB
1D3E; EM; 28.00 A; I=28-212.[ExPASy / RCSB / EBI]
1D3I; EM; 26.00 A; I=28-212.[ExPASy / RCSB / EBI]
1D3L; X-ray; 3.25 A; A=28-212.[ExPASy / RCSB / EBI]
1IAM; X-ray; 2.10 A; A=28-212.[ExPASy / RCSB / EBI]
1IC1; X-ray; 3.00 A; A/B=28-217.[ExPASy / RCSB / EBI]
1IJ4; Model; -; I=44-109.[ExPASy / RCSB / EBI]
1MQ8; X-ray; 3.30 A; A/C=28-318.[ExPASy / RCSB / EBI]
1P53; X-ray; 3.06 A; A/B=212-477.[ExPASy / RCSB / EBI]
1Z7Z; EM; 8.00 A; I=24-473.[ExPASy / RCSB / EBI]
2OZ4; X-ray; 2.70 A; A=213-477.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1D3E; -.
1D3I; -.
1D3L; -.
1IAM; -.
1IC1; -.
1IJ4; -.
1MQ8; -.
1P53; -.
1Z7Z; -.
2OZ4; -.
SMR P05362; 28-477.
ModBase P05362.
PTM databases
PhosphoSite P05362; -.
Enzyme and pathway databases
Reactome REACT_6900; Signaling in Immune System.
Organism-specific databases
H-InvDB HIX0014738; -.
HGNC HGNC:5344; ICAM1.
GenAtlas ICAM1.
HPA CAB002142; -.
HPA002126; -.
HPA004877; -.
MIM 147840; gene. [NCBI / EBI]
Orphanet 1334; Candidiasis, chronic mucocutaneous.
PharmGKB PA29592; -.
GeneCards P05362.
Gene expression databases
ArrayExpress P05362; -.
CleanEx HS_ICAM1; -.
GermOnline ENSG00000090339; Homo sapiens.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from direct assay from HPA).
GO:0005615; Cellular component: extracellular space (inferred from direct assay from UniProtKB).
GO:0005887; Cellular component: integral to plasma membrane (traceable author statement from ProtInc).
GO:0004888; Molecular function: transmembrane receptor activity (traceable author statement from ProtInc).
GO:0007159; Biological process: leukocyte adhesion (inferred from expression pattern from UniProtKB).
GO:0050900; Biological process: leukocyte migration (inferred from expression pattern from UniProtKB).
GO:0022614; Biological process: membrane to membrane docking (inferred from expression pattern from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR003988; ICAM.
IPR013768; ICAM_N.
IPR003987; ICAM_VCAM_N.
IPR007110; Ig-like.
IPR013783; Ig-like_fold.
IPR003599; Ig_sub.
Graphical view of domain structure.
Gene3D G3DSA:2.60.40.10; Ig-like_fold; 3.
Pfam PF03921; ICAM_N; 1.
Pfam graphical view of domain structure.
PRINTS PR01473; ICAM.
PR01472; ICAMVCAM1.
SMART SM00409; IG; 1.
SMART graphical view of domain structure.
PROSITE PS50835; IG_LIKE; FALSE_NEG.
PROSITE graphical view of domain structure (profiles).
BLOCKS P05362.
ProtoNet P05362.
Genome annotation databases
Ensembl ENSG00000090339; Homo sapiens. [Contig view]
GeneID 3383; -.
KEGG hsa:3383; -.
Phylogenomic databases
HOGENOM P05362; -.
HOVERGEN P05362; -.
Other
DrugBank DB00108; Natalizumab.
DB00641; Simvastatin.
LinkHub P05362; -.
NextBio 13376; -.
SOURCE ICAM1; Homo sapiens.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Cell adhesion; Direct protein sequencing; Glycoprotein; Host-virus interaction; Immunoglobulin domain; Membrane; Polymorphism; Repeat; Signal; Transmembrane; Ubl conjugation.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
SIGNAL   1    27  27      
CHAIN   28   532  505     Intercellular adhesion molecule 1. PRO_0000014783
TOPO_DOM   28   480  453     Extracellular (Potential). 
TRANSMEM   481   503  23     Potential. 
TOPO_DOM   504   532  29     Cytoplasmic (Potential). 
DOMAIN   41   103  63     Ig-like C2-type 1. 
DOMAIN   128   193  66     Ig-like C2-type 2. 
DOMAIN   230   297  68     Ig-like C2-type 3. 
DOMAIN   325   378  54     Ig-like C2-type 4. 
DOMAIN   412   464  53     Ig-like C2-type 5. 
MOTIF   152   154  3     Cell attachment site; atypical (Potential). 
CARBOHYD   130   130        N-linked (GlcNAc...). 
CARBOHYD   145   145        N-linked (GlcNAc...). 
CARBOHYD   183   183        N-linked (GlcNAc...). 
CARBOHYD   202   202        N-linked (GlcNAc...). 
CARBOHYD   267   267        N-linked (GlcNAc...). 
CARBOHYD   296   296        N-linked (GlcNAc...). 
CARBOHYD   385   385        N-linked (GlcNAc...). 
CARBOHYD   406   406        N-linked (GlcNAc...) (Potential). 
DISULFID   48    92         
DISULFID   52    96         
DISULFID   135   186         
DISULFID   237   290         
DISULFID   332   371         
DISULFID   403   419         
DISULFID   431   457         
VARIANT   56    56  1     K -> M (in Kilifi; dbSNP:rs5491 [NCBI]). VAR_010204 [3D]
VARIANT   155   155  1     K -> N (in dbSNP:rs5492 [NCBI]). VAR_014651 [3D]
VARIANT   241   241  1     G -> R (in dbSNP:rs1799969 [NCBI]). VAR_014186 
VARIANT   315   315  1     V -> M (in dbSNP:rs5495 [NCBI]). VAR_014652 
VARIANT   352   352  1     P -> L (in dbSNP:rs1801714 [NCBI]). VAR_014653 
VARIANT   397   397  1     R -> Q (in dbSNP:rs5497 [NCBI]). VAR_014654 
VARIANT   469   469  1     K -> E (in dbSNP:rs5498 [NCBI]). VAR_014187 
VARIANT   478   478  1     R -> W (in dbSNP:rs5030400 [NCBI]). VAR_016267 
CONFLICT   9    10        AL -> PV (in Ref. 8; CAA40441). 
CONFLICT   17    17        L -> F (in Ref. 9; AAQ14902). 
CONFLICT   27    27        A -> V (in Ref. 9; AAQ14902). 
STRAND   29    39  11      
STRAND   42    50  9      
STRAND   52    54  3      
STRAND   56    61  6      
STRAND   66    69  4      
STRAND   71    84  14      
STRAND   91    95  5      
STRAND   100   104  5      
STRAND   106   111  6      
STRAND   114   118  5      
STRAND   123   125  3      
STRAND   129   138  10      
HELIX   143   145  3      
STRAND   146   152  7      
STRAND   155   161  7      
TURN   164   166  3      
STRAND   167   174  8      
STRAND   183   191  9      
HELIX   193   195  3      
STRAND   199   203  5      
STRAND   220   222  3      
STRAND   225   228  4      
STRAND   231   241  11      
HELIX   245   247  3      
STRAND   249   254  6      
STRAND   262   266  5      
STRAND   269   277  9      
HELIX   280   282  3      
STRAND   284   294  11