ICAM1 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. (Microbial infection) Acts as a receptor for major receptor group rhinovirus A-B capsid proteins. (Microbial infection) Acts as a receptor for Coxsackievirus A21 capsid proteins. (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. Belongs to the immunoglobulin superfamily. ICAM family. Note: This description may include information from UniProtKB.
Protein type: Cell adhesion; Immunoglobulin superfamily; Membrane protein, integral
Chromosomal Location of human Ortholog: 19p13.2
Cellular Component:  external side of plasma membrane; extracellular exosome; extracellular space; immunological synapse; membrane raft; plasma membrane
Molecular Function:  integrin binding; protein binding; signaling receptor activity; transmembrane signaling receptor activity; virus receptor activity
Biological Process:  acute inflammatory response to antigenic stimulus; adhesion of symbiont to host; cell adhesion; cell adhesion mediated by integrin; cell aging; cellular response to alkaloid; cellular response to amyloid-beta; cellular response to dexamethasone stimulus; cellular response to glucose stimulus; cellular response to hypoxia; cellular response to interleukin-1; cellular response to interleukin-6; cellular response to leukemia inhibitory factor; cellular response to lipopolysaccharide; cellular response to nutrient levels; cellular response to tumor necrosis factor; cytokine-mediated signaling pathway; establishment of endothelial barrier; establishment of endothelial intestinal barrier; establishment of Sertoli cell barrier; extracellular matrix organization; heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; interferon-gamma-mediated signaling pathway; leukocyte cell-cell adhesion; leukocyte migration; membrane to membrane docking; negative regulation of calcium ion transport; negative regulation of endothelial cell apoptotic process; negative regulation of extrinsic apoptotic signaling pathway via death domain receptors; ovarian follicle development; positive regulation of actin filament polymerization; positive regulation of cellular extravasation; positive regulation of ERK1 and ERK2 cascade; positive regulation of GTPase activity; positive regulation of leukocyte adhesion to vascular endothelial cell; positive regulation of NF-kappaB transcription factor activity; positive regulation of nitric oxide biosynthetic process; positive regulation of peptidyl-tyrosine phosphorylation; positive regulation of vasoconstriction; receptor-mediated virion attachment to host cell; regulation of cell shape; regulation of immune response; regulation of leukocyte mediated cytotoxicity; regulation of ruffle assembly; response to amino acid; response to amphetamine; response to copper ion; response to ethanol; response to gonadotropin; response to insulin; response to ionizing radiation; response to sulfur dioxide; sensory perception of sound; T cell activation via T cell receptor contact with antigen bound to MHC molecule on antigen presenting cell; T cell antigen processing and presentation; T cell extravasation; viral entry into host cell
Disease: Malaria, Susceptibility To
Reference #:  P05362 (UniProtKB)
Alt. Names/Synonyms: BB2; CD54; cell surface glycoprotein P3.58; epididymis secretory sperm binding protein; human rhinovirus receptor; ICAM-1; ICAM1; Intercellular adhesion molecule 1; intercellular adhesion molecule 1 (CD54), human rhinovirus receptor; Major group rhinovirus receptor; P3.58
Gene Symbols: ICAM1
Molecular weight: 57,825 Da
Basal Isoelectric point: 8.31  Predict pI for various phosphorylation states
Protein-Specific Antibodies, siRNAs or Recombinant Proteins from Cell Signaling Technology® Total Proteins
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Protein Structure Not Found.

Cross-references to other databases:  AlphaFold  |  STRING  |  cBioPortal  |  Wikipedia  |  Reactome  |  neXtProt  |  Protein Atlas  |  BioGPS  |  Pfam  |  RCSB PDB  |  Phospho3D  |  Phospho.ELM  |  NetworKIN  |  GeneCards  |  UniProtKB  |  Entrez-Gene  |  GenPept  |  Ensembl Gene