ICAM2

Intercellular adhesion molecule 2
PDB rendering based on 1zxq.
Available structures PDB 1ZXQ
Identifiers
Symbols	ICAM2; CD102
External IDs	OMIM: 146630 MGI: 96394 HomoloGene: 675 GeneCards: ICAM2 Gene
Gene Ontology Molecular function • integrin binding Cellular component • uropod • plasma membrane • integral to plasma membrane Biological process • cell-cell adhesion • regulation of immune response Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	3384	15896
Ensembl	ENSG00000108622	ENSMUSG00000001029
UniProt	P13598	P35330
RefSeq (mRNA)	NM_000873.3	NM_010494.1
RefSeq (protein)	NP_000864.2	NP_034624.1
Location (UCSC)	Chr 17: 62.08 – 62.1 Mb	Chr 11: 106.24 – 106.25 Mb
PubMed search	[1]	[2]

Intercellular adhesion molecule 2 (ICAM2), also known as CD102 (Cluster of Differentiation 102), is a human gene.

The protein encoded by this gene is a member of the intercellular adhesion molecule (ICAM) family. All ICAM proteins are type I transmembrane glycoproteins, contain 2-9 immunoglobulin-like C2-type domains, and bind to the leukocyte adhesion LFA-1 protein. This protein may play a role in lymphocyte recirculation by blocking LFA-1-dependent cell adhesion. It mediates adhesive interactions important for antigen-specific immune response, NK-cell mediated clearance, lymphocyte recirculation, and other cellular interactions important for immune response and surveillance.

Interactions

ICAM2 has been shown to interact with EZR.

See also

• Cluster of differentiation

Further reading

• Simmons DL (1995). "The role of ICAM expression in immunity and disease.". Cancer Surv. 24: 141–55. PMID 7553659. 
• Hayflick JS, Kilgannon P, Gallatin WM (1998). "The intercellular adhesion molecule (ICAM) family of proteins. New members and novel functions.". Immunol. Res. 17 (3): 313–27. doi:10.1007/BF02786454. PMID 9638475. 
• Lalor PF, Shields P, Grant A, Adams DH (2002). "Recruitment of lymphocytes to the human liver.". Immunol. Cell Biol. 80 (1): 52–64. doi:10.1046/j.1440-1711.2002.01062.x. PMID 11869363. 
• Yonekawa K, Harlan JM (2005). "Targeting leukocyte integrins in human diseases.". J. Leukoc. Biol. 77 (2): 129–40. doi:10.1189/jlb.0804460. PMID 15548573. 
• de Fougerolles AR, Stacker SA, Schwarting R, Springer TA (1991). "Characterization of ICAM-2 and evidence for a third counter-receptor for LFA-1.". J. Exp. Med. 174 (1): 253–67. doi:10.1084/jem.174.1.253. PMC 2118873. PMID 1676048. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2118873. 
• Sansom D, Borrow J, Solomon E, Trowsdale J (1992). "The human ICAM2 gene maps to 17q23-25.". Genomics 11 (2): 462–4. doi:10.1016/0888-7543(91)90157-A. PMID 1769660. 
• Staunton DE, Dustin ML, Springer TA (1989). "Functional cloning of ICAM-2, a cell adhesion ligand for LFA-1 homologous to ICAM-1.". Nature 339 (6219): 61–4. doi:10.1038/339061a0. PMID 2497351. 
• Bujía J, Holly A, Kim C, et al. (1994). "Expression of human intercellular adhesion molecules in middle ear cholesteatoma.". Am J Otolaryngol 15 (4): 271–5. doi:10.1016/0196-0709(94)90094-9. PMID 7526720. 
• de Fougerolles AR, Qin X, Springer TA (1994). "Characterization of the function of intercellular adhesion molecule (ICAM)-3 and comparison with ICAM-1 and ICAM-2 in immune responses.". J. Exp. Med. 179 (2): 619–29. doi:10.1084/jem.179.2.619. PMC 2191386. PMID 7905020. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2191386. 
• Butini L, De Fougerolles AR, Vaccarezza M, et al. (1994). "Intercellular adhesion molecules (ICAM)-1 ICAM-2 and ICAM-3 function as counter-receptors for lymphocyte function-associated molecule 1 in human immunodeficiency virus-mediated syncytia formation.". Eur. J. Immunol. 24 (9): 2191–5. doi:10.1002/eji.1830240939. PMID 7916296. 
• Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides.". Gene 138 (1-2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298. 
• Hirao M, Sato N, Kondo T, et al. (1996). "Regulation mechanism of ERM (ezrin/radixin/moesin) protein/plasma membrane association: possible involvement of phosphatidylinositol turnover and Rho-dependent signaling pathway.". J. Cell Biol. 135 (1): 37–51. doi:10.1083/jcb.135.1.37. PMC 2121020. PMID 8858161. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2121020. 
• Bernstein CN, Sargent M, Gallatin WM, Wilkins J (1996). "Beta 2-integrin/intercellular adhesion molecule (ICAM) expression in the normal human intestine.". Clin. Exp. Immunol. 106 (1): 160–9. PMID 8870715. 
• Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery.". Genome Res. 6 (9): 791–806. doi:10.1101/gr.6.9.791. PMID 8889548. 
• Casasnovas JM, Springer TA, Liu JH, et al. (1997). "Crystal structure of ICAM-2 reveals a distinctive integrin recognition surface.". Nature 387 (6630): 312–5. doi:10.1038/387312a0. PMID 9153399. 
• Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library.". Gene 200 (1-2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149. 
• Sainio M, Zhao F, Heiska L, et al. (1997). "Neurofibromatosis 2 tumor suppressor protein colocalizes with ezrin and CD44 and associates with actin-containing cytoskeleton.". J. Cell. Sci.. 110 ( Pt 18): 2249–60. PMID 9378774. 
• Yonemura S, Hirao M, Doi Y, et al. (1998). "Ezrin/radixin/moesin (ERM) proteins bind to a positively charged amino acid cluster in the juxta-membrane cytoplasmic domain of CD44, CD43, and ICAM-2.". J. Cell Biol. 140 (4): 885–95. doi:10.1083/jcb.140.4.885. PMC 2141743. PMID 9472040. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2141743. 
• Bernstein CN, Sargent M, Gallatin WM (1998). "Beta2 integrin/ICAM expression in Crohn's disease.". Clin. Immunol. Immunopathol. 86 (2): 147–60. doi:10.1006/clin.1997.4462. PMID 9473377. 

External links

• MeSH ICAM2+protein,+human

This article incorporates text from the United States National Library of Medicine, which is in the public domain.