ID ICAM1_HUMAN Reviewed; 532 AA. AC P05362; B2R6M3; Q5NKV7; Q96B50; DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot. DT 21-JUN-2005, sequence version 2. DT 01-MAY-2013, entry version 173. DE RecName: Full=Intercellular adhesion molecule 1; DE Short=ICAM-1; DE AltName: Full=Major group rhinovirus receptor; DE AltName: CD_antigen=CD54; DE Flags: Precursor; GN Name=ICAM1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT GLU-469. RX PubMed=3340213; DOI=10.1038/331624a0; RA Simmons D., Makgoba M.W., Seed B.; RT "ICAM, an adhesion ligand of LFA-1, is homologous to the neural cell RT adhesion molecule NCAM."; RL Nature 331:624-627(1988). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT GLU-469. RX PubMed=3349522; DOI=10.1016/0092-8674(88)90434-5; RA Staunton D.E., Marlin S.D., Stratowa C., Dustin M.L., Springer T.A.; RT "Primary structure of ICAM-1 demonstrates interaction between members RT of the immunoglobulin and integrin supergene families."; RL Cell 52:925-933(1988). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=2544880; DOI=10.1073/pnas.86.13.4907; RA Tomassini J.E., Graham D., Dewitt C.M., Lineberger D.W., Rodkey J.A., RA Colonno R.J.; RT "cDNA cloning reveals that the major group rhinovirus receptor on HeLa RT cells is intercellular adhesion molecule 1."; RL Proc. Natl. Acad. Sci. U.S.A. 86:4907-4911(1989). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT GLU-469. RX PubMed=1680919; RA Voraberger G.F., Schaefer R., Stratowa C.; RT "Cloning of the human gene for intercellular adhesion molecule 1 and RT analysis of its 5'-regulatory region. Induction by cytokines and RT phorbol ester."; RL J. Immunol. 147:2777-2786(1991). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor RT vector."; RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT KILIFI MET-56, AND VARIANTS RP ARG-241; LEU-352; GLN-397 AND TRP-478. RG SeattleSNPs variation discovery resource; RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Lung; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Kidney; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [10] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-22. RX PubMed=1983003; RA Stade B.G., Messer G., Riethmueller G., Johnson J.P.; RT "Structural characteristics of the 5' region of the human ICAM-1 RT gene."; RL Immunobiology 182:79-87(1990). RN [11] RP NUCLEOTIDE SEQUENCE [MRNA] OF 5-532, AND VARIANT GLU-469. RC TISSUE=Blood; RX PubMed=15572059; DOI=10.1016/j.jtbi.2004.08.024; RA Walter N.A.R., Stebbing J., Messier W.; RT "The potential significance of adaptive evolution and dimerization in RT chimpanzee intercellular cell adhesion molecules (ICAMs)."; RL J. Theor. Biol. 232:339-346(2005). RN [12] RP PARTIAL PROTEIN SEQUENCE, AND FUNCTION AS A RHINOVIRUS RECEPTOR. RX PubMed=2538243; DOI=10.1016/0092-8674(89)90688-0; RA Greve J.M., Davis G., Meyer A.M., Forte C.P., Yost S.C., Marlor C.W., RA Kamarck M.E., McClelland A.; RT "The major human rhinovirus receptor is ICAM-1."; RL Cell 56:839-847(1989). RN [13] RP FUNCTION AS A RHINOVIRUS RECEPTOR. RX PubMed=1968231; DOI=10.1038/344070a0; RA Marlin S.D., Staunton D.E., Springer T.A., Stratowa C., RA Sommergruber W., Merluzzi V.J.; RT "A soluble form of intercellular adhesion molecule-1 inhibits RT rhinovirus infection."; RL Nature 344:70-72(1990). RN [14] RP INTERACTION WITH MUC1, AND FUNCTION. RX PubMed=11173916; DOI=10.1159/000051917; RA Hayashi T., Takahashi T., Motoya S., Ishida T., Itoh F., Adachi M., RA Hinoda Y., Imai K.; RT "MUC1 mucin core protein binds to the domain 1 of ICAM-1."; RL Digestion 63 Suppl. 1:87-92(2001). RN [15] RP INTERACTION WITH COXSACKIEVIRUS A21 CAPSID PROTEINS. RX PubMed=11160747; DOI=10.1128/JVI.75.5.2444-2451.2001; RA Xiao C., Bator C.M., Bowman V.D., Rieder E., He Y., Hebert B., RA Bella J., Baker T.S., Wimmer E., Kuhn R.J., Rossmann M.G.; RT "Interaction of coxsackievirus A21 with its cellular receptor, ICAM- RT 1."; RL J. Virol. 75:2444-2451(2001). RN [16] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-267, AND MASS RP SPECTROMETRY. RC TISSUE=Plasma; RX PubMed=16335952; DOI=10.1021/pr0502065; RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., RA Moore R.J., Smith R.D.; RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, RT hydrazide chemistry, and mass spectrometry."; RL J. Proteome Res. 4:2070-2080(2005). RN [17] RP UBIQUITINATION. RX PubMed=17174307; DOI=10.1016/j.febslet.2006.11.075; RA Hoer S., Smith L., Lehner P.J.; RT "MARCH-IX mediates ubiquitination and downregulation of ICAM-1."; RL FEBS Lett. 581:45-51(2007). RN [18] RP INTERACTION WITH ARHGEF26, AND FUNCTION. RX PubMed=17875742; DOI=10.1083/jcb.200612053; RA van Buul J.D., Allingham M.J., Samson T., Meller J., Boulter E., RA Garcia-Mata R., Burridge K.; RT "RhoG regulates endothelial apical cup assembly downstream from ICAM1 RT engagement and is involved in leukocyte trans-endothelial migration."; RL J. Cell Biol. 178:1279-1293(2007). RN [19] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-521 AND THR-530, AND RP MASS SPECTROMETRY. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [20] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-202; ASN-260 AND ASN-267, RP AND MASS SPECTROMETRY. RC TISSUE=Liver; RX PubMed=19159218; DOI=10.1021/pr8008012; RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; RT "Glycoproteomics analysis of human liver tissue by combination of RT multiple enzyme digestion and hydrazide chemistry."; RL J. Proteome Res. 8:651-661(2009). RN [21] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-145 AND ASN-267, AND MASS RP SPECTROMETRY. RC TISSUE=Leukemic T-cell; RX PubMed=19349973; DOI=10.1038/nbt.1532; RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., RA Schiess R., Aebersold R., Watts J.D.; RT "Mass-spectrometric identification and relative quantification of N- RT linked cell surface glycoproteins."; RL Nat. Biotechnol. 27:378-386(2009). RN [22] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-521 AND THR-530, AND RP MASS SPECTROMETRY. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., RA Mann M.; RT "Quantitative phosphoproteomics reveals widespread full RT phosphorylation site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [23] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [24] RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 28-217. RX PubMed=9539702; DOI=10.1073/pnas.95.8.4134; RA Casasnovas J.M., Stehle T., Liu J.H., Wang J.H., Springer T.A.; RT "A dimeric crystal structure for the N-terminal two domains of RT intercellular adhesion molecule-1."; RL Proc. Natl. Acad. Sci. U.S.A. 95:4134-4139(1998). RN [25] RP X-RAY CRYSTALLOGRAPHY (3.25 ANGSTROMS) OF 28-212 IN COMPLEX WITH HUMAN RP RHINOVIRUS 14. RX PubMed=9539703; DOI=10.1073/pnas.95.8.4140; RA Bella J., Kolatkar P.R., Marlor C.W., Greve J.M., Rossmann M.G.; RT "The structure of the two amino-terminal domains of human ICAM-1 RT suggests how it functions as a rhinovirus receptor and as an LFA-1 RT integrin ligand."; RL Proc. Natl. Acad. Sci. U.S.A. 95:4140-4145(1998). RN [26] RP X-RAY CRYSTALLOGRAPHY (3.25 ANGSTROMS) OF 28-212. RX PubMed=10562537; DOI=10.1093/emboj/18.22.6249; RA Kolatkar P.R., Bella J., Olson N.H., Bator C.M., Baker T.S., RA Rossmann M.G.; RT "Structural studies of two rhinovirus serotypes complexed with RT fragments of their cellular receptor."; RL EMBO J. 18:6249-6259(1999). RN [27] RP X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF 28-318 IN COMPLEX WITH ITGAL RP VWFA DOMAIN, DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-130; ASN-145; RP ASN-183 AND ASN-202. RX PubMed=12526797; DOI=10.1016/S0092-8674(02)01257-6; RA Shimaoka M., Xiao T., Liu J.H., Yang Y., Dong Y., Jun C.D., RA McCormack A., Zhang R., Joachimiak A., Takagi J., Wang J.H., RA Springer T.A.; RT "Structures of the alpha L I domain and its complex with ICAM-1 reveal RT a shape-shifting pathway for integrin regulation."; RL Cell 112:99-111(2003). RN [28] RP X-RAY CRYSTALLOGRAPHY (3.06 ANGSTROMS) OF 212-477, SUBUNIT, DISULFIDE RP BONDS, AND GLYCOSYLATION AT ASN-267; ASN-296 AND ASN-385. RX PubMed=15099525; DOI=10.1016/S1097-2765(04)00204-7; RA Yang Y., Jun C.D., Liu J.H., Zhang R., Joachimiak A., Springer T.A., RA Wang J.H.; RT "Structural basis for dimerization of ICAM-1 on the cell surface."; RL Mol. Cell 14:269-276(2004). RN [29] RP STRUCTURE BY ELECTRON CRYOMICROSCOPY (8.0 ANGSTROMS) OF 24-473 IN RP COMPLEX WITH COXSACKIEVIRUS A21, AND SUBUNIT. RX PubMed=16004874; DOI=10.1016/j.str.2005.04.011; RA Xiao C., Bator-Kelly C.M., Rieder E., Chipman P.R., Craig A., RA Kuhn R.J., Wimmer E., Rossmann M.G.; RT "The crystal structure of coxsackievirus A21 and its interaction with RT ICAM-1."; RL Structure 13:1019-1033(2005). RN [30] RP VARIANTS ARG-241 AND GLU-469. RX PubMed=7525451; DOI=10.1006/geno.1994.1303; RA Vora D.K., Rosenbloom C.L., Beaudet A.L., Cottingham R.W.; RT "Polymorphisms and linkage analysis for ICAM-1 and the selectin gene RT cluster."; RL Genomics 21:473-477(1994). RN [31] RP VARIANT ARG-241. RX PubMed=8557254; DOI=10.1007/BF00218826; RA Wenzel K., Ernst M., Rohde K., Baumann G., Speer A.; RT "DNA polymorphisms in adhesion molecule genes -- a new risk factor for RT early atherosclerosis."; RL Hum. Genet. 97:15-20(1996). RN [32] RP VARIANT KILIFI MET-56, AND ASSOCIATION WITH SUSCEPTIBILITY TO MALARIA. RX PubMed=9259284; DOI=10.1093/hmg/6.8.1357; RA Fernandez-Reyes D., Craig A.G., Kyes S.A., Peshu N., Snow R.W., RA Berendt A.R., Marsh K., Newbold C.I.; RT "A high frequency African coding polymorphism in the N-terminal domain RT of ICAM-1 predisposing to cerebral malaria in Kenya."; RL Hum. Mol. Genet. 6:1357-1360(1997). RN [33] RP VARIANT KILIFI MET-56, AND VARIANT GLU-469. RX PubMed=10391210; DOI=10.1038/10297; RA Halushka M.K., Fan J.-B., Bentley K., Hsie L., Shen N., Weder A., RA Cooper R., Lipshutz R., Chakravarti A.; RT "Patterns of single-nucleotide polymorphisms in candidate genes for RT blood-pressure homeostasis."; RL Nat. Genet. 22:239-247(1999). CC -!- FUNCTION: ICAM proteins are ligands for the leukocyte adhesion CC protein LFA-1 (integrin alpha-L/beta-2). During leukocyte trans- CC endothelial migration, ICAM1 engagement promotes the assembly of CC endothelial apical cups through ARHGEF26/SGEF and RHOG activation. CC In case of rhinovirus infection acts as a cellular receptor for CC the virus. CC -!- SUBUNIT: Homodimer (Probable). Interacts with human herpesvirus 8 CC MIR2 protein (Probable). Interacts with MUC1 and promotes cell CC aggregation in epithelial cells. Interacts with ARHGEF26/SGEF. CC Binds to coxsackievirus A21 capsid proteins and acts as a receptor CC for this virus. CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane CC protein. CC -!- PTM: Monoubiquitinated, which is promoted by MARCH9 and leads to CC endocytosis. CC -!- POLYMORPHISM: Homozygotes with ICAM1-Kalifi Met-56 seem to have an CC increased risk for cerebral malaria [MIM:611162]. CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. ICAM CC family. CC -!- SIMILARITY: Contains 5 Ig-like C2-type (immunoglobulin-like) CC domains. CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology CC and Haematology; CC URL="http://atlasgeneticsoncology.org//Genes/ICAM1ID40909ch19p13.html"; CC -!- WEB RESOURCE: Name=Wikipedia; Note=Intercellular adhesion molecule CC entry; CC URL="http://en.wikipedia.org/wiki/Intercellular_adhesion_molecule"; CC -!- WEB RESOURCE: Name=SeattleSNPs; CC URL="http://pga.gs.washington.edu/data/icam1/"; CC -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral CC capsid structure; CC URL="http://viperdb.scripps.edu/info_page.php?VDB=1z7z"; CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding; CC Note=ICAM-1; CC URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_hum_Itlect_261"; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X06990; CAA30051.1; -; mRNA. DR EMBL; J03132; AAA52709.1; -; mRNA. DR EMBL; M24283; AAA52708.1; -; mRNA. DR EMBL; X59286; CAA41977.1; -; Genomic_DNA. DR EMBL; X59287; CAA41977.1; JOINED; Genomic_DNA. DR EMBL; X59288; CAA41977.1; JOINED; Genomic_DNA. DR EMBL; BT006854; AAP35500.1; -; mRNA. DR EMBL; AY225514; AAO30128.1; -; Genomic_DNA. DR EMBL; AK312636; BAG35520.1; -; mRNA. DR EMBL; CH471106; EAW84086.1; -; Genomic_DNA. DR EMBL; BC015969; AAH15969.1; -; mRNA. DR EMBL; X57151; CAA40441.1; -; Genomic_DNA. DR EMBL; AF340039; AAQ14902.1; -; mRNA. DR IPI; IPI00008494; -. DR PIR; A29849; A29849. DR RefSeq; NP_000192.2; NM_000201.2. DR UniGene; Hs.643447; -. DR PDB; 1D3E; EM; 28.00 A; I=28-212. DR PDB; 1D3I; EM; 26.00 A; I=28-212. DR PDB; 1D3L; X-ray; 3.25 A; A=28-212. DR PDB; 1IAM; X-ray; 2.10 A; A=28-212. DR PDB; 1IC1; X-ray; 3.00 A; A/B=28-217. DR PDB; 1IJ4; Model; -; I=44-109. DR PDB; 1MQ8; X-ray; 3.30 A; A/C=28-318. DR PDB; 1P53; X-ray; 3.06 A; A/B=212-477. DR PDB; 1Z7Z; EM; 8.00 A; I=28-477. DR PDB; 2OZ4; X-ray; 2.70 A; A=213-477. DR PDB; 3TCX; X-ray; 3.60 A; A/C/E/G/I/K/M/O/Q/S/U/W/Y/a=30-112. DR PDBsum; 1D3E; -. DR PDBsum; 1D3I; -. DR PDBsum; 1D3L; -. DR PDBsum; 1IAM; -. DR PDBsum; 1IC1; -. DR PDBsum; 1IJ4; -. DR PDBsum; 1MQ8; -. DR PDBsum; 1P53; -. DR PDBsum; 1Z7Z; -. DR PDBsum; 2OZ4; -. DR PDBsum; 3TCX; -. DR ProteinModelPortal; P05362; -. DR IntAct; P05362; 5. DR MINT; MINT-4053071; -. DR STRING; 9606.ENSP00000264832; -. DR PhosphoSite; P05362; -. DR DMDM; 68067956; -. DR PaxDb; P05362; -. DR PRIDE; P05362; -. DR DNASU; 3383; -. DR Ensembl; ENST00000264832; ENSP00000264832; ENSG00000090339. DR GeneID; 3383; -. DR KEGG; hsa:3383; -. DR UCSC; uc002mnq.2; human. DR CTD; 3383; -. DR GeneCards; GC19P010381; -. DR HGNC; HGNC:5344; ICAM1. DR HPA; CAB002142; -. DR HPA; HPA002126; -. DR HPA; HPA004877; -. DR MIM; 147840; gene. DR MIM; 611162; phenotype. DR neXtProt; NX_P05362; -. DR Orphanet; 1334; Chronic mucocutaneous candidiasis. DR PharmGKB; PA29592; -. DR eggNOG; NOG146347; -. DR HOGENOM; HOG000059554; -. DR HOVERGEN; HBG052074; -. DR InParanoid; P05362; -. DR KO; K06490; -. DR OMA; RDCPGNW; -. DR PhylomeDB; P05362; -. DR Pathway_Interaction_DB; amb2_neutrophils_pathway; amb2 Integrin signaling. DR Pathway_Interaction_DB; txa2pathway; Thromboxane A2 receptor signaling. DR Reactome; REACT_111102; Signal Transduction. DR Reactome; REACT_6900; Immune System. DR SABIO-RK; P05362; -. DR BindingDB; P05362; -. DR ChEMBL; CHEMBL3070; -. DR ChiTaRS; ICAM1; human. DR DrugBank; DB00108; Natalizumab. DR DrugBank; DB00641; Simvastatin. DR EvolutionaryTrace; P05362; -. DR GenomeRNAi; 3383; -. DR NextBio; 13376; -. DR PMAP-CutDB; P05362; -. DR ArrayExpress; P05362; -. DR Bgee; P05362; -. DR CleanEx; HS_ICAM1; -. DR Genevestigator; P05362; -. DR GermOnline; ENSG00000090339; Homo sapiens. DR GO; GO:0009897; C:external side of plasma membrane; IEA:Compara. DR GO; GO:0005615; C:extracellular space; IDA:BHF-UCL. DR GO; GO:0001772; C:immunological synapse; IEA:Compara. DR GO; GO:0005887; C:integral to plasma membrane; TAS:ProtInc. DR GO; GO:0043498; F:cell surface binding; IEA:Compara. DR GO; GO:0004888; F:transmembrane signaling receptor activity; TAS:ProtInc. DR GO; GO:0051856; P:adhesion to symbiont; IDA:BHF-UCL. DR GO; GO:0033627; P:cell adhesion mediated by integrin; IEA:Compara. DR GO; GO:0007569; P:cell aging; IEA:Compara. DR GO; GO:0071312; P:cellular response to alkaloid; IEA:Compara. DR GO; GO:0071333; P:cellular response to glucose stimulus; IEA:Compara. DR GO; GO:0071456; P:cellular response to hypoxia; IEA:Compara. DR GO; GO:0071347; P:cellular response to interleukin-1; IEA:Compara. DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IEA:Compara. DR GO; GO:0031669; P:cellular response to nutrient levels; IEA:Compara. DR GO; GO:0071356; P:cellular response to tumor necrosis factor; IEA:Compara. DR GO; GO:0007157; P:heterophilic cell-cell adhesion; TAS:BHF-UCL. DR GO; GO:0060333; P:interferon-gamma-mediated signaling pathway; TAS:Reactome. DR GO; GO:0007159; P:leukocyte cell-cell adhesion; IMP:BHF-UCL. DR GO; GO:0050900; P:leukocyte migration; IEP:BHF-UCL. DR GO; GO:0022614; P:membrane to membrane docking; IEP:BHF-UCL. DR GO; GO:0051926; P:negative regulation of calcium ion transport; IEA:Compara. DR GO; GO:0001541; P:ovarian follicle development; IEA:Compara. DR GO; GO:0002693; P:positive regulation of cellular extravasation; IMP:BHF-UCL. DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IEA:Compara. DR GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; IEA:Compara. DR GO; GO:0045907; P:positive regulation of vasoconstriction; IEA:Compara. DR GO; GO:0030155; P:regulation of cell adhesion; IEA:Compara. DR GO; GO:0008360; P:regulation of cell shape; IEA:Compara. DR GO; GO:0050776; P:regulation of immune response; TAS:Reactome. DR GO; GO:0001910; P:regulation of leukocyte mediated cytotoxicity; TAS:BHF-UCL. DR GO; GO:0043200; P:response to amino acid stimulus; IEA:Compara. DR GO; GO:0001975; P:response to amphetamine; IEA:Compara. DR GO; GO:0046688; P:response to copper ion; IEA:Compara. DR GO; GO:0042493; P:response to drug; IEA:Compara. DR GO; GO:0045471; P:response to ethanol; IEA:Compara. DR GO; GO:0034698; P:response to gonadotropin stimulus; IEA:Compara. DR GO; GO:0010212; P:response to ionizing radiation; IEA:Compara. DR GO; GO:0014070; P:response to organic cyclic compound; IEA:Compara. DR GO; GO:0010477; P:response to sulfur dioxide; IEA:Compara. DR 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. DR GO; GO:0002457; P:T cell antigen processing and presentation; IEA:Compara. DR GO; GO:0046813; P:virion attachment, binding of host cell surface receptor; IDA:BHF-UCL. DR Gene3D; 2.60.40.10; -; 5. DR InterPro; IPR003988; ICAM. DR InterPro; IPR013768; ICAM_N. DR InterPro; IPR003987; ICAM_VCAM_N. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003599; Ig_sub. DR Pfam; PF03921; ICAM_N; 1. DR PRINTS; PR01473; ICAM. DR PRINTS; PR01472; ICAMVCAM1. DR SMART; SM00409; IG; 1. DR PROSITE; PS50835; IG_LIKE; FALSE_NEG. PE 1: Evidence at protein level; KW 3D-structure; Cell adhesion; Complete proteome; KW Direct protein sequencing; Disulfide bond; Glycoprotein; KW Host cell receptor for virus entry; Host-virus interaction; KW Immunoglobulin domain; Membrane; Phosphoprotein; Polymorphism; KW Receptor; Reference proteome; Repeat; Signal; Transmembrane; KW Transmembrane helix; Ubl conjugation. FT SIGNAL 1 27 FT CHAIN 28 532 Intercellular adhesion molecule 1. FT /FTId=PRO_0000014783. FT TOPO_DOM 28 480 Extracellular (Potential). FT TRANSMEM 481 503 Helical; (Potential). FT TOPO_DOM 504 532 Cytoplasmic (Potential). FT DOMAIN 41 103 Ig-like C2-type 1. FT DOMAIN 128 193 Ig-like C2-type 2. FT DOMAIN 230 297 Ig-like C2-type 3. FT DOMAIN 325 378 Ig-like C2-type 4. FT DOMAIN 412 464 Ig-like C2-type 5. FT MOTIF 152 154 Cell attachment site; atypical FT (Potential). FT MOD_RES 521 521 Phosphothreonine. FT MOD_RES 530 530 Phosphothreonine. FT CARBOHYD 130 130 N-linked (GlcNAc...). FT CARBOHYD 145 145 N-linked (GlcNAc...). FT CARBOHYD 183 183 N-linked (GlcNAc...). FT CARBOHYD 202 202 N-linked (GlcNAc...). FT CARBOHYD 260 260 N-linked (GlcNAc...). FT CARBOHYD 267 267 N-linked (GlcNAc...). FT CARBOHYD 296 296 N-linked (GlcNAc...). FT CARBOHYD 385 385 N-linked (GlcNAc...). FT CARBOHYD 406 406 N-linked (GlcNAc...) (Potential). FT DISULFID 48 92 FT DISULFID 52 96 FT DISULFID 135 186 FT DISULFID 237 290 FT DISULFID 332 371 FT DISULFID 403 419 FT DISULFID 431 457 FT VARIANT 34 34 S -> C (in dbSNP:rs5491). FT /FTId=VAR_049879. FT VARIANT 56 56 K -> M (in Kilifi; at homozygosity it is FT associated with increased susceptibility FT to cerebral malaria; dbSNP:rs5491). FT /FTId=VAR_010204. FT VARIANT 155 155 K -> N (in dbSNP:rs5492). FT /FTId=VAR_014651. FT VARIANT 241 241 G -> R (in dbSNP:rs1799969). FT /FTId=VAR_014186. FT VARIANT 315 315 V -> M (in dbSNP:rs5495). FT /FTId=VAR_014652. FT VARIANT 352 352 P -> L (in dbSNP:rs1801714). FT /FTId=VAR_014653. FT VARIANT 397 397 R -> Q (in dbSNP:rs5497). FT /FTId=VAR_014654. FT VARIANT 469 469 K -> E (in dbSNP:rs5498). FT /FTId=VAR_014187. FT VARIANT 478 478 R -> W (in dbSNP:rs5030400). FT /FTId=VAR_016267. FT CONFLICT 9 10 AL -> PV (in Ref. 10; CAA40441). FT CONFLICT 17 17 L -> F (in Ref. 11; AAQ14902). FT CONFLICT 27 27 A -> V (in Ref. 11; AAQ14902). FT STRAND 29 39 FT STRAND 42 50 FT STRAND 52 54 FT STRAND 56 61 FT STRAND 66 69 FT STRAND 71 84 FT STRAND 91 95 FT STRAND 97 99 FT STRAND 100 104 FT STRAND 106 111 FT STRAND 114 118 FT STRAND 123 125 FT STRAND 129 138 FT HELIX 143 145 FT STRAND 146 152 FT STRAND 155 161 FT TURN 164 166 FT STRAND 167 174 FT HELIX 177 179 FT STRAND 183 191 FT HELIX 193 195 FT STRAND 199 203 FT STRAND 210 212 FT STRAND 220 222 FT STRAND 225 228 FT STRAND 231 241 FT HELIX 245 247 FT STRAND 249 254 FT STRAND 262 265 FT STRAND 267 278 FT HELIX 280 282 FT STRAND 284 294 FT STRAND 297 308 FT STRAND 314 318 FT STRAND 320 323 FT STRAND 327 333 FT STRAND 338 344 FT STRAND 346 348 FT STRAND 351 354 FT STRAND 357 359 FT HELIX 362 364 FT STRAND 367 376 FT STRAND 378 397 FT HELIX 400 402 FT STRAND 405 410 FT STRAND 422 425 FT STRAND 428 433 FT TURN 434 436 FT HELIX 449 451 FT STRAND 453 461 FT STRAND 464 475 SQ 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 //