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P05362

- ICAM1_HUMAN

UniProt

P05362 - ICAM1_HUMAN

Protein

Intercellular adhesion molecule 1

Gene

ICAM1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 187 (01 Oct 2014)
      Sequence version 2 (21 Jun 2005)
      Previous versions | rss
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    Functioni

    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.4 Publications

    GO - Molecular functioni

    1. integrin binding Source: BHF-UCL
    2. protein binding Source: UniProtKB
    3. receptor activity Source: ProtInc
    4. transmembrane signaling receptor activity Source: ProtInc
    5. virus receptor activity Source: UniProtKB-KW

    GO - Biological processi

    1. adhesion of symbiont to host Source: BHF-UCL
    2. cell adhesion Source: BHF-UCL
    3. cell adhesion mediated by integrin Source: Ensembl
    4. cell aging Source: Ensembl
    5. cellular response to alkaloid Source: Ensembl
    6. cellular response to glucose stimulus Source: Ensembl
    7. cellular response to hypoxia Source: Ensembl
    8. cellular response to interleukin-1 Source: Ensembl
    9. cellular response to lipopolysaccharide Source: Ensembl
    10. cellular response to nutrient levels Source: Ensembl
    11. cellular response to tumor necrosis factor Source: Ensembl
    12. cytokine-mediated signaling pathway Source: Reactome
    13. establishment of endothelial barrier Source: UniProt
    14. extracellular matrix organization Source: Reactome
    15. heterophilic cell-cell adhesion Source: BHF-UCL
    16. interferon-gamma-mediated signaling pathway Source: Reactome
    17. leukocyte cell-cell adhesion Source: BHF-UCL
    18. leukocyte migration Source: BHF-UCL
    19. membrane to membrane docking Source: BHF-UCL
    20. negative regulation of calcium ion transport Source: Ensembl
    21. negative regulation of endothelial cell apoptotic process Source: BHF-UCL
    22. negative regulation of extrinsic apoptotic signaling pathway via death domain receptors Source: BHF-UCL
    23. ovarian follicle development Source: Ensembl
    24. positive regulation of actin filament polymerization Source: Ensembl
    25. positive regulation of cellular extravasation Source: BHF-UCL
    26. positive regulation of ERK1 and ERK2 cascade Source: BHF-UCL
    27. positive regulation of NF-kappaB transcription factor activity Source: Ensembl
    28. positive regulation of nitric oxide biosynthetic process Source: Ensembl
    29. positive regulation of peptidyl-tyrosine phosphorylation Source: Ensembl
    30. positive regulation of Rho GTPase activity Source: Ensembl
    31. positive regulation of vasoconstriction Source: Ensembl
    32. receptor-mediated virion attachment to host cell Source: BHF-UCL
    33. regulation of cell adhesion Source: Ensembl
    34. regulation of cell shape Source: Ensembl
    35. regulation of immune response Source: Reactome
    36. regulation of leukocyte mediated cytotoxicity Source: BHF-UCL
    37. response to amino acid Source: Ensembl
    38. response to amphetamine Source: Ensembl
    39. response to copper ion Source: Ensembl
    40. response to drug Source: Ensembl
    41. response to ethanol Source: Ensembl
    42. response to gonadotropin Source: Ensembl
    43. response to ionizing radiation Source: Ensembl
    44. response to organic cyclic compound Source: Ensembl
    45. response to sulfur dioxide Source: Ensembl
    46. T cell activation via T cell receptor contact with antigen bound to MHC molecule on antigen presenting cell Source: BHF-UCL
    47. T cell antigen processing and presentation Source: Ensembl

    Keywords - Molecular functioni

    Host cell receptor for virus entry, Receptor

    Keywords - Biological processi

    Cell adhesion, Host-virus interaction

    Enzyme and pathway databases

    ReactomeiREACT_11152. Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
    REACT_13552. Integrin cell surface interactions.
    REACT_25078. Interferon gamma signaling.
    SABIO-RKP05362.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Intercellular adhesion molecule 1
    Short name:
    ICAM-1
    Alternative name(s):
    Major group rhinovirus receptor
    CD_antigen: CD54
    Gene namesi
    Name:ICAM1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:5344. ICAM1.

    Subcellular locationi

    GO - Cellular componenti

    1. external side of plasma membrane Source: Ensembl
    2. extracellular space Source: BHF-UCL
    3. extracellular vesicular exosome Source: UniProtKB
    4. immunological synapse Source: Ensembl
    5. integral component of plasma membrane Source: ProtInc
    6. membrane Source: UniProtKB
    7. plasma membrane Source: Reactome

    Keywords - Cellular componenti

    Membrane

    Pathology & Biotechi

    Organism-specific databases

    MIMi611162. phenotype.
    Orphaneti1334. Chronic mucocutaneous candidiasis.
    PharmGKBiPA29592.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2727Add
    BLAST
    Chaini28 – 532505Intercellular adhesion molecule 1PRO_0000014783Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi48 ↔ 92
    Disulfide bondi52 ↔ 96
    Glycosylationi130 – 1301N-linked (GlcNAc...)1 Publication
    Disulfide bondi135 ↔ 186
    Glycosylationi145 – 1451N-linked (GlcNAc...) (complex)3 Publications
    Glycosylationi183 – 1831N-linked (GlcNAc...)1 Publication
    Glycosylationi202 – 2021N-linked (GlcNAc...)2 Publications
    Disulfide bondi237 ↔ 290
    Glycosylationi260 – 2601N-linked (GlcNAc...)1 Publication
    Glycosylationi267 – 2671N-linked (GlcNAc...)4 Publications
    Glycosylationi296 – 2961N-linked (GlcNAc...)1 Publication
    Disulfide bondi332 ↔ 371
    Glycosylationi385 – 3851N-linked (GlcNAc...)1 Publication
    Disulfide bondi403 ↔ 419
    Glycosylationi406 – 4061N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi431 ↔ 457
    Modified residuei521 – 5211Phosphothreonine2 Publications
    Modified residuei530 – 5301Phosphothreonine2 Publications

    Post-translational modificationi

    Monoubiquitinated, which is promoted by MARCH9 and leads to endocytosis.

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiP05362.
    PaxDbiP05362.
    PRIDEiP05362.

    PTM databases

    PhosphoSiteiP05362.

    Miscellaneous databases

    PMAP-CutDBP05362.

    Expressioni

    Gene expression databases

    ArrayExpressiP05362.
    BgeeiP05362.
    CleanExiHS_ICAM1.
    GenevestigatoriP05362.

    Organism-specific databases

    HPAiCAB002142.
    HPA002126.
    HPA004877.

    Interactioni

    Subunit structurei

    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.7 PublicationsCurated

    Protein-protein interaction databases

    BioGridi109610. 138 interactions.
    IntActiP05362. 7 interactions.
    MINTiMINT-4053071.
    STRINGi9606.ENSP00000264832.

    Structurei

    Secondary structure

    1
    532
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi29 – 3911
    Beta strandi42 – 509
    Beta strandi52 – 543
    Beta strandi56 – 616
    Beta strandi66 – 694
    Beta strandi71 – 8414
    Beta strandi91 – 955
    Beta strandi97 – 993
    Beta strandi100 – 1045
    Beta strandi106 – 1116
    Beta strandi114 – 1185
    Beta strandi123 – 1253
    Beta strandi129 – 13810
    Helixi143 – 1453
    Beta strandi146 – 1527
    Beta strandi155 – 1617
    Turni164 – 1663
    Beta strandi167 – 1748
    Helixi177 – 1793
    Beta strandi183 – 1919
    Helixi193 – 1953
    Beta strandi199 – 2035
    Beta strandi210 – 2123
    Beta strandi220 – 2223
    Beta strandi225 – 2284
    Beta strandi231 – 24111
    Helixi245 – 2473
    Beta strandi249 – 2546
    Beta strandi262 – 2654
    Beta strandi267 – 27812
    Helixi280 – 2823
    Beta strandi284 – 29411
    Beta strandi297 – 30812
    Beta strandi314 – 3185
    Beta strandi320 – 3234
    Beta strandi327 – 3337
    Beta strandi338 – 3447
    Beta strandi346 – 3483
    Beta strandi351 – 3544
    Beta strandi357 – 3593
    Helixi362 – 3643
    Beta strandi367 – 37610
    Beta strandi378 – 39720
    Helixi400 – 4023
    Beta strandi405 – 4106
    Beta strandi422 – 4254
    Beta strandi428 – 4336
    Turni434 – 4363
    Helixi449 – 4513
    Beta strandi453 – 4619
    Beta strandi464 – 47512

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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[»]
    ProteinModelPortaliP05362.
    SMRiP05362. Positions 28-477.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP05362.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini28 – 480453ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini504 – 53229CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei481 – 50323HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini41 – 10363Ig-like C2-type 1Add
    BLAST
    Domaini128 – 19366Ig-like C2-type 2Add
    BLAST
    Domaini230 – 29768Ig-like C2-type 3Add
    BLAST
    Domaini325 – 37854Ig-like C2-type 4Add
    BLAST
    Domaini412 – 46453Ig-like C2-type 5Add
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi152 – 1543Cell attachment site; atypicalSequence Analysis

    Sequence similaritiesi

    Belongs to the immunoglobulin superfamily. ICAM family.Curated

    Keywords - Domaini

    Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG146347.
    HOGENOMiHOG000059554.
    HOVERGENiHBG052074.
    InParanoidiP05362.
    KOiK06490.
    OMAiRDCPGNW.
    OrthoDBiEOG7QG43X.
    PhylomeDBiP05362.
    TreeFamiTF333745.

    Family and domain databases

    Gene3Di2.60.40.10. 5 hits.
    InterProiIPR003988. ICAM.
    IPR013768. ICAM_N.
    IPR003987. ICAM_VCAM_N.
    IPR013783. Ig-like_fold.
    IPR003599. Ig_sub.
    [Graphical view]
    PfamiPF03921. ICAM_N. 1 hit.
    [Graphical view]
    PRINTSiPR01473. ICAM.
    PR01472. ICAMVCAM1.
    SMARTiSM00409. IG. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P05362-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAPSSPRPAL PALLVLLGAL FPGPGNAQTS VSPSKVILPR GGSVLVTCST    50
    SCDQPKLLGI ETPLPKKELL LPGNNRKVYE LSNVQEDSQP MCYSNCPDGQ 100
    STAKTFLTVY WTPERVELAP LPSWQPVGKN LTLRCQVEGG APRANLTVVL 150
    LRGEKELKRE PAVGEPAEVT TTVLVRRDHH GANFSCRTEL DLRPQGLELF 200
    ENTSAPYQLQ TFVLPATPPQ LVSPRVLEVD TQGTVVCSLD GLFPVSEAQV 250
    HLALGDQRLN PTVTYGNDSF SAKASVSVTA EDEGTQRLTC AVILGNQSQE 300
    TLQTVTIYSF PAPNVILTKP EVSEGTEVTV KCEAHPRAKV TLNGVPAQPL 350
    GPRAQLLLKA TPEDNGRSFS CSATLEVAGQ LIHKNQTREL RVLYGPRLDE 400
    RDCPGNWTWP ENSQQTPMCQ AWGNPLPELK CLKDGTFPLP IGESVTVTRD 450
    LEGTYLCRAR STQGEVTRKV TVNVLSPRYE IVIITVVAAA VIMGTAGLST 500
    YLYNRQRKIK KYRLQQAQKG TPMKPNTQAT PP 532
    Length:532
    Mass (Da):57,825
    Last modified:June 21, 2005 - v2
    Checksum:i550089365A733AFB
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti9 – 102AL → PV in CAA40441. (PubMed:1983003)Curated
    Sequence conflicti17 – 171L → F in AAQ14902. (PubMed:15572059)Curated
    Sequence conflicti27 – 271A → V in AAQ14902. (PubMed:15572059)Curated

    Polymorphismi

    Homozygotes with ICAM1-Kalifi Met-56 seem to have an increased risk for cerebral malaria [MIMi:611162].

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti34 – 341S → C.
    Corresponds to variant rs5491 [ dbSNP | Ensembl ].
    VAR_049879
    Natural varianti56 – 561K → M in Kilifi; at homozygosity it is associated with increased susceptibility to cerebral malaria. 3 Publications
    Corresponds to variant rs5491 [ dbSNP | Ensembl ].
    VAR_010204
    Natural varianti155 – 1551K → N.
    Corresponds to variant rs5492 [ dbSNP | Ensembl ].
    VAR_014651
    Natural varianti241 – 2411G → R.3 Publications
    Corresponds to variant rs1799969 [ dbSNP | Ensembl ].
    VAR_014186
    Natural varianti315 – 3151V → M.
    Corresponds to variant rs5495 [ dbSNP | Ensembl ].
    VAR_014652
    Natural varianti352 – 3521P → L.1 Publication
    Corresponds to variant rs1801714 [ dbSNP | Ensembl ].
    VAR_014653
    Natural varianti397 – 3971R → Q.1 Publication
    Corresponds to variant rs5497 [ dbSNP | Ensembl ].
    VAR_014654
    Natural varianti469 – 4691K → E.6 Publications
    Corresponds to variant rs5498 [ dbSNP | Ensembl ].
    VAR_014187
    Natural varianti478 – 4781R → W.1 Publication
    Corresponds to variant rs5030400 [ dbSNP | Ensembl ].
    VAR_016267

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS12231.1.
    PIRiA29849.
    RefSeqiNP_000192.2. NM_000201.2.
    UniGeneiHs.643447.

    Genome annotation databases

    EnsembliENST00000264832; ENSP00000264832; ENSG00000090339.
    GeneIDi3383.
    KEGGihsa:3383.
    UCSCiuc002mnq.2. human.

    Polymorphism databases

    DMDMi68067956.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology
    Wikipedia

    Intercellular adhesion molecule entry

    SeattleSNPs
    Virus Particle ExploreR db

    Icosahedral capsid structure

    Functional Glycomics Gateway - Glycan Binding

    ICAM-1

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS12231.1.
    PIRi A29849.
    RefSeqi NP_000192.2. NM_000201.2.
    UniGenei Hs.643447.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1D3E electron microscopy 28.00 I 28-212 [» ]
    1D3I electron microscopy 26.00 I 28-212 [» ]
    1D3L X-ray 3.25 A 28-212 [» ]
    1IAM X-ray 2.10 A 28-212 [» ]
    1IC1 X-ray 3.00 A/B 28-217 [» ]
    1IJ4 model - I 44-109 [» ]
    1MQ8 X-ray 3.30 A/C 28-318 [» ]
    1P53 X-ray 3.06 A/B 212-477 [» ]
    1Z7Z electron microscopy 8.00 I 28-477 [» ]
    2OZ4 X-ray 2.70 A 213-477 [» ]
    3TCX X-ray 3.60 A/C/E/G/I/K/M/O/Q/S/U/W/Y/a 29-112 [» ]
    ProteinModelPortali P05362.
    SMRi P05362. Positions 28-477.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109610. 138 interactions.
    IntActi P05362. 7 interactions.
    MINTi MINT-4053071.
    STRINGi 9606.ENSP00000264832.

    Chemistry

    BindingDBi P05362.
    ChEMBLi CHEMBL2096661.
    DrugBanki DB00108. Natalizumab.
    DB00641. Simvastatin.

    PTM databases

    PhosphoSitei P05362.

    Polymorphism databases

    DMDMi 68067956.

    Proteomic databases

    MaxQBi P05362.
    PaxDbi P05362.
    PRIDEi P05362.

    Protocols and materials databases

    DNASUi 3383.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000264832 ; ENSP00000264832 ; ENSG00000090339 .
    GeneIDi 3383.
    KEGGi hsa:3383.
    UCSCi uc002mnq.2. human.

    Organism-specific databases

    CTDi 3383.
    GeneCardsi GC19P010381.
    HGNCi HGNC:5344. ICAM1.
    HPAi CAB002142.
    HPA002126.
    HPA004877.
    MIMi 147840. gene.
    611162. phenotype.
    neXtProti NX_P05362.
    Orphaneti 1334. Chronic mucocutaneous candidiasis.
    PharmGKBi PA29592.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG146347.
    HOGENOMi HOG000059554.
    HOVERGENi HBG052074.
    InParanoidi P05362.
    KOi K06490.
    OMAi RDCPGNW.
    OrthoDBi EOG7QG43X.
    PhylomeDBi P05362.
    TreeFami TF333745.

    Enzyme and pathway databases

    Reactomei REACT_11152. Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
    REACT_13552. Integrin cell surface interactions.
    REACT_25078. Interferon gamma signaling.
    SABIO-RK P05362.

    Miscellaneous databases

    ChiTaRSi ICAM1. human.
    EvolutionaryTracei P05362.
    GeneWikii ICAM-1.
    GenomeRNAii 3383.
    NextBioi 13376.
    PMAP-CutDB P05362.
    PROi P05362.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P05362.
    Bgeei P05362.
    CleanExi HS_ICAM1.
    Genevestigatori P05362.

    Family and domain databases

    Gene3Di 2.60.40.10. 5 hits.
    InterProi IPR003988. ICAM.
    IPR013768. ICAM_N.
    IPR003987. ICAM_VCAM_N.
    IPR013783. Ig-like_fold.
    IPR003599. Ig_sub.
    [Graphical view ]
    Pfami PF03921. ICAM_N. 1 hit.
    [Graphical view ]
    PRINTSi PR01473. ICAM.
    PR01472. ICAMVCAM1.
    SMARTi SM00409. IG. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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. 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. 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. Cited for: INTERACTION WITH MUC1, FUNCTION.
    15. 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. 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. 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. 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.

    Entry informationi

    Entry nameiICAM1_HUMAN
    AccessioniPrimary (citable) accession number: P05362
    Secondary accession number(s): B2R6M3, Q5NKV7, Q96B50
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1988
    Last sequence update: June 21, 2005
    Last modified: October 1, 2014
    This is version 187 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human cell differentiation molecules
      CD nomenclature of surface proteins of human leucocytes and list of entries
    2. Human chromosome 19
      Human chromosome 19: entries, gene names and cross-references to MIM
    3. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    4. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    5. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    6. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3