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P05362 (ICAM1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 185. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Intercellular adhesion molecule 1

Short name=ICAM-1
Alternative name(s):
Major group rhinovirus receptor
CD_antigen=CD54
Gene names
Name:ICAM1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length532 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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. In case of rhinovirus infection acts as a cellular receptor for the virus. Ref.12 Ref.13 Ref.14 Ref.18

Subunit structure

Homodimer Probable. Interacts with human herpesvirus 8 MIR2 protein Probable. Interacts with MUC1 and promotes cell aggregation in epithelial cells. Interacts with ARHGEF26/SGEF. Binds to coxsackievirus A21 capsid proteins and acts as a receptor for this virus. Ref.14 Ref.15 Ref.18 Ref.29 Ref.30

Subcellular location

Membrane; Single-pass type I membrane protein.

Post-translational modification

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].

Sequence similarities

Belongs to the immunoglobulin superfamily. ICAM family.

Contains 5 Ig-like C2-type (immunoglobulin-like) domains.

Ontologies

Keywords
   Biological processCell adhesion
Host-virus interaction
   Cellular componentMembrane
   Coding sequence diversityPolymorphism
   DomainImmunoglobulin domain
Repeat
Signal
Transmembrane
Transmembrane helix
   Molecular functionHost cell receptor for virus entry
Receptor
   PTMDisulfide bond
Glycoprotein
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processT cell activation via T cell receptor contact with antigen bound to MHC molecule on antigen presenting cell

Inferred from mutant phenotype PubMed 2477710. Source: BHF-UCL

T cell antigen processing and presentation

Inferred from electronic annotation. Source: Ensembl

adhesion of symbiont to host

Inferred from direct assay Ref.12. Source: BHF-UCL

cell adhesion

Inferred from direct assay PubMed 16809613. Source: BHF-UCL

cell adhesion mediated by integrin

Inferred from electronic annotation. Source: Ensembl

cell aging

Inferred from electronic annotation. Source: Ensembl

cellular response to alkaloid

Inferred from electronic annotation. Source: Ensembl

cellular response to glucose stimulus

Inferred from electronic annotation. Source: Ensembl

cellular response to hypoxia

Inferred from electronic annotation. Source: Ensembl

cellular response to interleukin-1

Inferred from electronic annotation. Source: Ensembl

cellular response to lipopolysaccharide

Inferred from electronic annotation. Source: Ensembl

cellular response to nutrient levels

Inferred from electronic annotation. Source: Ensembl

cellular response to tumor necrosis factor

Inferred from electronic annotation. Source: Ensembl

cytokine-mediated signaling pathway

Traceable author statement. Source: Reactome

establishment of endothelial barrier

Inferred from genetic interaction PubMed 23264465. Source: UniProt

extracellular matrix organization

Traceable author statement. Source: Reactome

heterophilic cell-cell adhesion

Traceable author statement PubMed 2477710. Source: BHF-UCL

interferon-gamma-mediated signaling pathway

Traceable author statement. Source: Reactome

leukocyte cell-cell adhesion

Inferred from mutant phenotype PubMed 2477710. Source: BHF-UCL

leukocyte migration

Inferred from expression pattern PubMed 12082081. Source: BHF-UCL

membrane to membrane docking

Inferred from expression pattern PubMed 12082081. Source: BHF-UCL

negative regulation of calcium ion transport

Inferred from electronic annotation. Source: Ensembl

negative regulation of endothelial cell apoptotic process

Inferred from direct assay PubMed 10903502. Source: BHF-UCL

negative regulation of extrinsic apoptotic signaling pathway via death domain receptors

Inferred from direct assay PubMed 10903502. Source: BHF-UCL

ovarian follicle development

Inferred from electronic annotation. Source: Ensembl

positive regulation of ERK1 and ERK2 cascade

Inferred from mutant phenotype PubMed 10903502. Source: BHF-UCL

positive regulation of NF-kappaB transcription factor activity

Inferred from electronic annotation. Source: Ensembl

positive regulation of Rho GTPase activity

Inferred from electronic annotation. Source: Ensembl

positive regulation of actin filament polymerization

Inferred from electronic annotation. Source: Ensembl

positive regulation of cellular extravasation

Inferred from mutant phenotype PubMed 12902516. Source: BHF-UCL

positive regulation of nitric oxide biosynthetic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of peptidyl-tyrosine phosphorylation

Inferred from electronic annotation. Source: Ensembl

positive regulation of vasoconstriction

Inferred from electronic annotation. Source: Ensembl

receptor-mediated virion attachment to host cell

Inferred from direct assay Ref.12. Source: BHF-UCL

regulation of cell adhesion

Inferred from electronic annotation. Source: Ensembl

regulation of cell shape

Inferred from electronic annotation. Source: Ensembl

regulation of immune response

Traceable author statement. Source: Reactome

regulation of leukocyte mediated cytotoxicity

Traceable author statement PubMed 16038038. Source: BHF-UCL

response to amino acid

Inferred from electronic annotation. Source: Ensembl

response to amphetamine

Inferred from electronic annotation. Source: Ensembl

response to copper ion

Inferred from electronic annotation. Source: Ensembl

response to drug

Inferred from electronic annotation. Source: Ensembl

response to ethanol

Inferred from electronic annotation. Source: Ensembl

response to gonadotropin

Inferred from electronic annotation. Source: Ensembl

response to ionizing radiation

Inferred from electronic annotation. Source: Ensembl

response to organic cyclic compound

Inferred from electronic annotation. Source: Ensembl

response to sulfur dioxide

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentexternal side of plasma membrane

Inferred from electronic annotation. Source: Ensembl

extracellular space

Inferred from direct assay PubMed 9290466. Source: BHF-UCL

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867PubMed 20458337. Source: UniProt

immunological synapse

Inferred from electronic annotation. Source: Ensembl

integral component of plasma membrane

Traceable author statement Ref.12. Source: ProtInc

plasma membrane

Traceable author statement. Source: Reactome

   Molecular_functionintegrin binding

Inferred from physical interaction PubMed 1448173. Source: BHF-UCL

protein binding

Inferred from physical interaction PubMed 12716892. Source: UniProtKB

receptor activity

Traceable author statement Ref.12. Source: ProtInc

transmembrane signaling receptor activity

Traceable author statement Ref.12. Source: ProtInc

virus receptor activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2727
Chain28 – 532505Intercellular adhesion molecule 1
PRO_0000014783

Regions

Topological domain28 – 480453Extracellular Potential
Transmembrane481 – 50323Helical; Potential
Topological domain504 – 53229Cytoplasmic Potential
Domain41 – 10363Ig-like C2-type 1
Domain128 – 19366Ig-like C2-type 2
Domain230 – 29768Ig-like C2-type 3
Domain325 – 37854Ig-like C2-type 4
Domain412 – 46453Ig-like C2-type 5
Motif152 – 1543Cell attachment site; atypical Potential

Amino acid modifications

Modified residue5211Phosphothreonine Ref.19 Ref.23
Modified residue5301Phosphothreonine Ref.19 Ref.23
Glycosylation1301N-linked (GlcNAc...) Ref.28
Glycosylation1451N-linked (GlcNAc...) (complex) Ref.21 Ref.22 Ref.28
Glycosylation1831N-linked (GlcNAc...) Ref.28
Glycosylation2021N-linked (GlcNAc...) Ref.20 Ref.28
Glycosylation2601N-linked (GlcNAc...) Ref.20
Glycosylation2671N-linked (GlcNAc...) Ref.16 Ref.20 Ref.22 Ref.29
Glycosylation2961N-linked (GlcNAc...) Ref.29
Glycosylation3851N-linked (GlcNAc...) Ref.29
Glycosylation4061N-linked (GlcNAc...) Potential
Disulfide bond48 ↔ 92 Ref.28 Ref.29
Disulfide bond52 ↔ 96 Ref.28 Ref.29
Disulfide bond135 ↔ 186 Ref.28 Ref.29
Disulfide bond237 ↔ 290 Ref.28 Ref.29
Disulfide bond332 ↔ 371 Ref.28 Ref.29
Disulfide bond403 ↔ 419 Ref.28 Ref.29
Disulfide bond431 ↔ 457 Ref.28 Ref.29

Natural variations

Natural variant341S → C.
Corresponds to variant rs5491 [ dbSNP | Ensembl ].
VAR_049879
Natural variant561K → M in Kilifi; at homozygosity it is associated with increased susceptibility to cerebral malaria. Ref.6 Ref.33 Ref.34
Corresponds to variant rs5491 [ dbSNP | Ensembl ].
VAR_010204
Natural variant1551K → N.
Corresponds to variant rs5492 [ dbSNP | Ensembl ].
VAR_014651
Natural variant2411G → R. Ref.6 Ref.31 Ref.32
Corresponds to variant rs1799969 [ dbSNP | Ensembl ].
VAR_014186
Natural variant3151V → M.
Corresponds to variant rs5495 [ dbSNP | Ensembl ].
VAR_014652
Natural variant3521P → L. Ref.6
Corresponds to variant rs1801714 [ dbSNP | Ensembl ].
VAR_014653
Natural variant3971R → Q. Ref.6
Corresponds to variant rs5497 [ dbSNP | Ensembl ].
VAR_014654
Natural variant4691K → E. Ref.1 Ref.2 Ref.4 Ref.11 Ref.31 Ref.34
Corresponds to variant rs5498 [ dbSNP | Ensembl ].
VAR_014187
Natural variant4781R → W. Ref.6
Corresponds to variant rs5030400 [ dbSNP | Ensembl ].
VAR_016267

Experimental info

Sequence conflict9 – 102AL → PV in CAA40441. Ref.10
Sequence conflict171L → F in AAQ14902. Ref.11
Sequence conflict271A → V in AAQ14902. Ref.11

Secondary structure

................................................................................................... 532
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P05362 [UniParc].

Last modified June 21, 2005. Version 2.
Checksum: 550089365A733AFB

FASTA53257,825
        10         20         30         40         50         60 
MAPSSPRPAL PALLVLLGAL FPGPGNAQTS VSPSKVILPR GGSVLVTCST SCDQPKLLGI 

        70         80         90        100        110        120 
ETPLPKKELL LPGNNRKVYE LSNVQEDSQP MCYSNCPDGQ STAKTFLTVY WTPERVELAP 

       130        140        150        160        170        180 
LPSWQPVGKN LTLRCQVEGG APRANLTVVL LRGEKELKRE PAVGEPAEVT TTVLVRRDHH 

       190        200        210        220        230        240 
GANFSCRTEL DLRPQGLELF ENTSAPYQLQ TFVLPATPPQ LVSPRVLEVD TQGTVVCSLD 

       250        260        270        280        290        300 
GLFPVSEAQV HLALGDQRLN PTVTYGNDSF SAKASVSVTA EDEGTQRLTC AVILGNQSQE 

       310        320        330        340        350        360 
TLQTVTIYSF PAPNVILTKP EVSEGTEVTV KCEAHPRAKV TLNGVPAQPL GPRAQLLLKA 

       370        380        390        400        410        420 
TPEDNGRSFS CSATLEVAGQ LIHKNQTREL RVLYGPRLDE RDCPGNWTWP ENSQQTPMCQ 

       430        440        450        460        470        480 
AWGNPLPELK CLKDGTFPLP IGESVTVTRD LEGTYLCRAR STQGEVTRKV TVNVLSPRYE 

       490        500        510        520        530 
IVIITVVAAA VIMGTAGLST YLYNRQRKIK KYRLQQAQKG TPMKPNTQAT PP 

« Hide

References

« Hide 'large scale' references
[1]"ICAM, an adhesion ligand of LFA-1, is homologous to the neural cell adhesion molecule NCAM."
Simmons D., Makgoba M.W., Seed B.
Nature 331:624-627(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT GLU-469.
[2]"Primary structure of ICAM-1 demonstrates interaction between members of the immunoglobulin and integrin supergene families."
Staunton D.E., Marlin S.D., Stratowa C., Dustin M.L., Springer T.A.
Cell 52:925-933(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT GLU-469.
[3]"cDNA cloning reveals that the major group rhinovirus receptor on HeLa cells is intercellular adhesion molecule 1."
Tomassini J.E., Graham D., Dewitt C.M., Lineberger D.W., Rodkey J.A., Colonno R.J.
Proc. Natl. Acad. Sci. U.S.A. 86:4907-4911(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]"Cloning of the human gene for intercellular adhesion molecule 1 and analysis of its 5'-regulatory region. Induction by cytokines and phorbol ester."
Voraberger G.F., Schaefer R., Stratowa C.
J. Immunol. 147:2777-2786(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT GLU-469.
[5]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
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.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[6]SeattleSNPs variation discovery resource
Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT KILIFI MET-56, VARIANTS ARG-241; LEU-352; GLN-397 AND TRP-478.
[7]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
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. expand/collapse author list , 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.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Lung.
[8]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. expand/collapse author list , 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
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Kidney.
[10]"Structural characteristics of the 5' region of the human ICAM-1 gene."
Stade B.G., Messer G., Riethmueller G., Johnson J.P.
Immunobiology 182:79-87(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-22.
[11]"The potential significance of adaptive evolution and dimerization in chimpanzee intercellular cell adhesion molecules (ICAMs)."
Walter N.A.R., Stebbing J., Messier W.
J. Theor. Biol. 232:339-346(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 5-532, VARIANT GLU-469.
Tissue: Blood.
[12]"The major human rhinovirus receptor is ICAM-1."
Greve J.M., Davis G., Meyer A.M., Forte C.P., Yost S.C., Marlor C.W., Kamarck M.E., McClelland A.
Cell 56:839-847(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL PROTEIN SEQUENCE, FUNCTION AS A RHINOVIRUS RECEPTOR.
[13]"A soluble form of intercellular adhesion molecule-1 inhibits rhinovirus infection."
Marlin S.D., Staunton D.E., Springer T.A., Stratowa C., Sommergruber W., Merluzzi V.J.
Nature 344:70-72(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS A RHINOVIRUS RECEPTOR.
[14]"MUC1 mucin core protein binds to the domain 1 of ICAM-1."
Hayashi T., Takahashi T., Motoya S., Ishida T., Itoh F., Adachi M., Hinoda Y., Imai K.
Digestion 63 Suppl. 1:87-92(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MUC1, FUNCTION.
[15]"Interaction of coxsackievirus A21 with its cellular receptor, ICAM-1."
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.
J. Virol. 75:2444-2451(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH COXSACKIEVIRUS A21 CAPSID PROTEINS.
[16]"Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-267.
Tissue: Plasma.
[17]"MARCH-IX mediates ubiquitination and downregulation of ICAM-1."
Hoer S., Smith L., Lehner P.J.
FEBS Lett. 581:45-51(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION.
[18]"RhoG regulates endothelial apical cup assembly downstream from ICAM1 engagement and is involved in leukocyte trans-endothelial migration."
van Buul J.D., Allingham M.J., Samson T., Meller J., Boulter E., Garcia-Mata R., Burridge K.
J. Cell Biol. 178:1279-1293(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ARHGEF26, FUNCTION.
[19]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-521 AND THR-530, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[20]"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-202; ASN-260 AND ASN-267.
Tissue: Liver.
[21]"A strategy for precise and large scale identification of core fucosylated glycoproteins."
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.
Mol. Cell. Proteomics 8:913-923(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT ASN-145.
[22]"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D.
Nat. Biotechnol. 27:378-386(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-145 AND ASN-267.
Tissue: Leukemic T-cell.
[23]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
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.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-521 AND THR-530, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[24]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[25]"A dimeric crystal structure for the N-terminal two domains of intercellular adhesion molecule-1."
Casasnovas J.M., Stehle T., Liu J.H., Wang J.H., Springer T.A.
Proc. Natl. Acad. Sci. U.S.A. 95:4134-4139(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 28-217.
[26]"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."
Bella J., Kolatkar P.R., Marlor C.W., Greve J.M., Rossmann M.G.
Proc. Natl. Acad. Sci. U.S.A. 95:4140-4145(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.25 ANGSTROMS) OF 28-212 IN COMPLEX WITH HUMAN RHINOVIRUS 14.
[27]"Structural studies of two rhinovirus serotypes complexed with fragments of their cellular receptor."
Kolatkar P.R., Bella J., Olson N.H., Bator C.M., Baker T.S., Rossmann M.G.
EMBO J. 18:6249-6259(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.25 ANGSTROMS) OF 28-212.
[28]"Structures of the alpha L I domain and its complex with ICAM-1 reveal a shape-shifting pathway for integrin regulation."
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.
Cell 112:99-111(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: 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.
[29]"Structural basis for dimerization of ICAM-1 on the cell surface."
Yang Y., Jun C.D., Liu J.H., Zhang R., Joachimiak A., Springer T.A., Wang J.H.
Mol. Cell 14:269-276(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.06 ANGSTROMS) OF 212-477, SUBUNIT, DISULFIDE BONDS, GLYCOSYLATION AT ASN-267; ASN-296 AND ASN-385.
[30]"The crystal structure of coxsackievirus A21 and its interaction with ICAM-1."
Xiao C., Bator-Kelly C.M., Rieder E., Chipman P.R., Craig A., Kuhn R.J., Wimmer E., Rossmann M.G.
Structure 13:1019-1033(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY ELECTRON CRYOMICROSCOPY (8.0 ANGSTROMS) OF 24-473 IN COMPLEX WITH COXSACKIEVIRUS A21, SUBUNIT.
[31]"Polymorphisms and linkage analysis for ICAM-1 and the selectin gene cluster."
Vora D.K., Rosenbloom C.L., Beaudet A.L., Cottingham R.W.
Genomics 21:473-477(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ARG-241 AND GLU-469.
[32]"DNA polymorphisms in adhesion molecule genes -- a new risk factor for early atherosclerosis."
Wenzel K., Ernst M., Rohde K., Baumann G., Speer A.
Hum. Genet. 97:15-20(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ARG-241.
[33]"A high frequency African coding polymorphism in the N-terminal domain of ICAM-1 predisposing to cerebral malaria in Kenya."
Fernandez-Reyes D., Craig A.G., Kyes S.A., Peshu N., Snow R.W., Berendt A.R., Marsh K., Newbold C.I.
Hum. Mol. Genet. 6:1357-1360(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT KILIFI MET-56, ASSOCIATION WITH SUSCEPTIBILITY TO MALARIA.
[34]"Patterns of single-nucleotide polymorphisms in candidate genes for blood-pressure homeostasis."
Halushka M.K., Fan J.-B., Bentley K., Hsie L., Shen N., Weder A., Cooper R., Lipshutz R., Chakravarti A.
Nat. Genet. 22:239-247(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT KILIFI MET-56, VARIANT GLU-469.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X06990 mRNA. Translation: CAA30051.1.
J03132 mRNA. Translation: AAA52709.1.
M24283 mRNA. Translation: AAA52708.1.
X59286, X59287, X59288 Genomic DNA. Translation: CAA41977.1.
BT006854 mRNA. Translation: AAP35500.1.
AY225514 Genomic DNA. Translation: AAO30128.1.
AK312636 mRNA. Translation: BAG35520.1.
CH471106 Genomic DNA. Translation: EAW84086.1.
BC015969 mRNA. Translation: AAH15969.1.
X57151 Genomic DNA. Translation: CAA40441.1.
AF340039 mRNA. Translation: AAQ14902.1.
CCDSCCDS12231.1.
PIRA29849.
RefSeqNP_000192.2. NM_000201.2.
UniGeneHs.643447.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1D3Eelectron microscopy28.00I28-212[»]
1D3Ielectron microscopy26.00I28-212[»]
1D3LX-ray3.25A28-212[»]
1IAMX-ray2.10A28-212[»]
1IC1X-ray3.00A/B28-217[»]
1IJ4model-I44-109[»]
1MQ8X-ray3.30A/C28-318[»]
1P53X-ray3.06A/B212-477[»]
1Z7Zelectron microscopy8.00I28-477[»]
2OZ4X-ray2.70A213-477[»]
3TCXX-ray3.60A/C/E/G/I/K/M/O/Q/S/U/W/Y/a29-112[»]
ProteinModelPortalP05362.
SMRP05362. Positions 28-477.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109610. 138 interactions.
IntActP05362. 6 interactions.
MINTMINT-4053071.
STRING9606.ENSP00000264832.

Chemistry

BindingDBP05362.
ChEMBLCHEMBL2096661.
DrugBankDB00108. Natalizumab.
DB00641. Simvastatin.

PTM databases

PhosphoSiteP05362.

Polymorphism databases

DMDM68067956.

Proteomic databases

MaxQBP05362.
PaxDbP05362.
PRIDEP05362.

Protocols and materials databases

DNASU3383.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000264832; ENSP00000264832; ENSG00000090339.
GeneID3383.
KEGGhsa:3383.
UCSCuc002mnq.2. human.

Organism-specific databases

CTD3383.
GeneCardsGC19P010381.
HGNCHGNC:5344. ICAM1.
HPACAB002142.
HPA002126.
HPA004877.
MIM147840. gene.
611162. phenotype.
neXtProtNX_P05362.
Orphanet1334. Chronic mucocutaneous candidiasis.
PharmGKBPA29592.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG146347.
HOGENOMHOG000059554.
HOVERGENHBG052074.
InParanoidP05362.
KOK06490.
OMARDCPGNW.
OrthoDBEOG7QG43X.
PhylomeDBP05362.
TreeFamTF333745.

Enzyme and pathway databases

ReactomeREACT_118779. Extracellular matrix organization.
REACT_6900. Immune System.
SABIO-RKP05362.

Gene expression databases

ArrayExpressP05362.
BgeeP05362.
CleanExHS_ICAM1.
GenevestigatorP05362.

Family and domain databases

Gene3D2.60.40.10. 5 hits.
InterProIPR003988. ICAM.
IPR013768. ICAM_N.
IPR003987. ICAM_VCAM_N.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
[Graphical view]
PfamPF03921. ICAM_N. 1 hit.
[Graphical view]
PRINTSPR01473. ICAM.
PR01472. ICAMVCAM1.
SMARTSM00409. IG. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSICAM1. human.
EvolutionaryTraceP05362.
GeneWikiICAM-1.
GenomeRNAi3383.
NextBio13376.
PMAP-CutDBP05362.
PROP05362.
SOURCESearch...

Entry information

Entry nameICAM1_HUMAN
AccessionPrimary (citable) accession number: P05362
Secondary accession number(s): B2R6M3, Q5NKV7, Q96B50
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: June 21, 2005
Last modified: July 9, 2014
This is version 185 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM

Human cell differentiation molecules

CD nomenclature of surface proteins of human leucocytes and list of entries