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Protein

Intercellular adhesion molecule 1

Gene

ICAM1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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.2 Publications
(Microbial infection) Acts as a receptor for major receptor group rhinovirus A-B capsid proteins (PubMed:1968231, PubMed:2538243). Acts as a receptor for Coxsackievirus A21 capsid proteins (PubMed:11160747, PubMed:16004874, PubMed:9539703). 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 (PubMed:11413168).6 Publications

GO - Molecular functioni

  • integrin binding Source: BHF-UCL
  • receptor activity Source: ProtInc
  • transmembrane signaling receptor activity Source: ProtInc
  • virus receptor activity Source: UniProtKB-KW

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Host cell receptor for virus entry, Receptor

Keywords - Biological processi

Cell adhesion, Host-virus interaction

Enzyme and pathway databases

BioCyciZFISH:ENSG00000090339-MONOMER.
ReactomeiR-HSA-198933. Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
R-HSA-216083. Integrin cell surface interactions.
R-HSA-877300. Interferon gamma signaling.
SABIO-RKP05362.
SIGNORiP05362.

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
Proteomesi
  • UP000005640 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:5344. ICAM1.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini28 – 480ExtracellularSequence analysisAdd BLAST453
Transmembranei481 – 503HelicalSequence analysisAdd BLAST23
Topological domaini504 – 532CytoplasmicSequence analysisAdd BLAST29

GO - Cellular componenti

  • cell surface Source: UniProtKB
  • external side of plasma membrane Source: Ensembl
  • extracellular exosome Source: UniProtKB
  • extracellular space Source: BHF-UCL
  • focal adhesion Source: UniProtKB
  • immunological synapse Source: Ensembl
  • integral component of plasma membrane Source: ProtInc
  • membrane Source: UniProtKB
  • membrane raft Source: Ensembl
  • plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Organism-specific databases

DisGeNETi3383.
MalaCardsiICAM1.
MIMi611162. phenotype.
OpenTargetsiENSG00000090339.
PharmGKBiPA29592.

Chemistry databases

ChEMBLiCHEMBL3070.
DrugBankiDB08818. Hyaluronic acid.
DB00108. Natalizumab.

Polymorphism and mutation databases

BioMutaiICAM1.
DMDMi68067956.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 27Add BLAST27
ChainiPRO_000001478328 – 532Intercellular adhesion molecule 1Add BLAST505

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi48 ↔ 92Combined sources3 Publications
Disulfide bondi52 ↔ 96Combined sources3 Publications
Glycosylationi130N-linked (GlcNAc...)2 Publications1
Disulfide bondi135 ↔ 186Combined sources3 Publications
Glycosylationi145N-linked (GlcNAc...) (complex)4 Publications1
Glycosylationi183N-linked (GlcNAc...)2 Publications1
Glycosylationi202N-linked (GlcNAc...)4 Publications1
Disulfide bondi237 ↔ 290Combined sources1 Publication
Glycosylationi260N-linked (GlcNAc...)1 Publication1
Glycosylationi267N-linked (GlcNAc...)4 Publications1
Glycosylationi296N-linked (GlcNAc...)1 Publication1
Disulfide bondi332 ↔ 371Combined sources1 Publication
Glycosylationi385N-linked (GlcNAc...)1 Publication1
Disulfide bondi403 ↔ 419Combined sources1 Publication
Glycosylationi406N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi431 ↔ 457Combined sources1 Publication
Modified residuei521PhosphothreonineCombined sources1
Modified residuei530PhosphothreonineCombined sources1

Post-translational modificationi

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

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP05362.
MaxQBiP05362.
PaxDbiP05362.
PeptideAtlasiP05362.
PRIDEiP05362.

PTM databases

iPTMnetiP05362.
PhosphoSitePlusiP05362.

Miscellaneous databases

PMAP-CutDBP05362.

Expressioni

Gene expression databases

BgeeiENSG00000090339.
CleanExiHS_ICAM1.
ExpressionAtlasiP05362. baseline and differential.
GenevisibleiP05362. HS.

Organism-specific databases

HPAiCAB002142.
HPA002126.
HPA004877.

Interactioni

Subunit structurei

Homodimer (Probable). Interacts with MUC1 and promotes cell aggregation in epithelial cells. Interacts with ARHGEF26/SGEF.Curated4 Publications
(Microbial infection) Interacts with major receptor group rhinovirus A-B capsid proteins (PubMed:1968231, PubMed:2538243).2 Publications
(Microbial infection) Interacts with Coxsackievirus A21 capsid proteins (PubMed:11160747, PubMed:16004874, PubMed:9539703).3 Publications

GO - Molecular functioni

  • integrin binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi109610. 170 interactors.
DIPiDIP-36658N.
IntActiP05362. 10 interactors.
MINTiMINT-4053071.
STRINGi9606.ENSP00000264832.

Chemistry databases

BindingDBiP05362.

Structurei

Secondary structure

1532
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi29 – 39Combined sources11
Beta strandi42 – 50Combined sources9
Beta strandi52 – 54Combined sources3
Beta strandi56 – 61Combined sources6
Beta strandi66 – 69Combined sources4
Beta strandi71 – 84Combined sources14
Beta strandi91 – 95Combined sources5
Beta strandi97 – 99Combined sources3
Beta strandi100 – 104Combined sources5
Beta strandi106 – 111Combined sources6
Beta strandi114 – 118Combined sources5
Beta strandi123 – 125Combined sources3
Beta strandi129 – 138Combined sources10
Helixi143 – 145Combined sources3
Beta strandi146 – 152Combined sources7
Beta strandi155 – 161Combined sources7
Turni164 – 166Combined sources3
Beta strandi167 – 174Combined sources8
Helixi177 – 179Combined sources3
Beta strandi183 – 191Combined sources9
Helixi193 – 195Combined sources3
Beta strandi199 – 203Combined sources5
Beta strandi210 – 212Combined sources3
Beta strandi220 – 222Combined sources3
Beta strandi225 – 228Combined sources4
Beta strandi231 – 241Combined sources11
Helixi245 – 247Combined sources3
Beta strandi249 – 254Combined sources6
Beta strandi262 – 265Combined sources4
Beta strandi267 – 278Combined sources12
Helixi280 – 282Combined sources3
Beta strandi284 – 294Combined sources11
Beta strandi297 – 308Combined sources12
Beta strandi314 – 318Combined sources5
Beta strandi320 – 323Combined sources4
Beta strandi327 – 333Combined sources7
Beta strandi338 – 344Combined sources7
Beta strandi346 – 348Combined sources3
Beta strandi351 – 354Combined sources4
Beta strandi357 – 359Combined sources3
Helixi362 – 364Combined sources3
Beta strandi367 – 376Combined sources10
Beta strandi378 – 397Combined sources20
Helixi400 – 402Combined sources3
Beta strandi405 – 410Combined sources6
Beta strandi422 – 425Combined sources4
Beta strandi428 – 433Combined sources6
Turni434 – 436Combined sources3
Helixi449 – 451Combined sources3
Beta strandi453 – 461Combined sources9
Beta strandi464 – 475Combined sources12

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP05362.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini41 – 103Ig-like C2-type 1Add BLAST63
Domaini128 – 193Ig-like C2-type 2Add BLAST66
Domaini230 – 297Ig-like C2-type 3Add BLAST68
Domaini325 – 378Ig-like C2-type 4Add BLAST54
Domaini412 – 464Ig-like C2-type 5Add BLAST53

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi152 – 154Cell attachment site; atypicalSequence analysis3

Sequence similaritiesi

Belongs to the immunoglobulin superfamily. ICAM family.Curated

Keywords - Domaini

Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IPHM. Eukaryota.
ENOG410YQ1Q. LUCA.
GeneTreeiENSGT00530000063246.
HOGENOMiHOG000059554.
HOVERGENiHBG052074.
InParanoidiP05362.
KOiK06490.
OMAiGNWTWQE.
OrthoDBiEOG091G022Y.
PhylomeDBiP05362.
TreeFamiTF333745.

Family and domain databases

Gene3Di2.60.40.10. 5 hits.
InterProiIPR003988. ICAM.
IPR013768. ICAM_N.
IPR003987. ICAM_VCAM_N.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
[Graphical view]
PfamiPF03921. ICAM_N. 1 hit.
[Graphical view]
PRINTSiPR01473. ICAM.
PR01472. ICAMVCAM1.
SMARTiSM00409. IG. 3 hits.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 5 hits.

Sequencei

Sequence statusi: Complete.

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

P05362-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAPSSPRPAL PALLVLLGAL FPGPGNAQTS VSPSKVILPR GGSVLVTCST
60 70 80 90 100
SCDQPKLLGI ETPLPKKELL LPGNNRKVYE LSNVQEDSQP MCYSNCPDGQ
110 120 130 140 150
STAKTFLTVY WTPERVELAP LPSWQPVGKN LTLRCQVEGG APRANLTVVL
160 170 180 190 200
LRGEKELKRE PAVGEPAEVT TTVLVRRDHH GANFSCRTEL DLRPQGLELF
210 220 230 240 250
ENTSAPYQLQ TFVLPATPPQ LVSPRVLEVD TQGTVVCSLD GLFPVSEAQV
260 270 280 290 300
HLALGDQRLN PTVTYGNDSF SAKASVSVTA EDEGTQRLTC AVILGNQSQE
310 320 330 340 350
TLQTVTIYSF PAPNVILTKP EVSEGTEVTV KCEAHPRAKV TLNGVPAQPL
360 370 380 390 400
GPRAQLLLKA TPEDNGRSFS CSATLEVAGQ LIHKNQTREL RVLYGPRLDE
410 420 430 440 450
RDCPGNWTWP ENSQQTPMCQ AWGNPLPELK CLKDGTFPLP IGESVTVTRD
460 470 480 490 500
LEGTYLCRAR STQGEVTRKV TVNVLSPRYE IVIITVVAAA VIMGTAGLST
510 520 530
YLYNRQRKIK KYRLQQAQKG TPMKPNTQAT PP
Length:532
Mass (Da):57,825
Last modified:June 21, 2005 - v2
Checksum:i550089365A733AFB
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti9 – 10AL → PV in CAA40441 (PubMed:1983003).Curated2
Sequence conflicti17L → F in AAQ14902 (PubMed:15572059).Curated1
Sequence conflicti27A → V in AAQ14902 (PubMed:15572059).Curated1

Polymorphismi

Homozygotes with ICAM1-Kalifi Met-56 seem to have an increased risk for cerebral malaria [MIMi:611162].1 Publication

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_04987934S → C.Corresponds to variant rs5491dbSNPEnsembl.1
Natural variantiVAR_01020456K → M in Kilifi; at homozygosity it is associated with increased susceptibility to cerebral malaria. 3 PublicationsCorresponds to variant rs5491dbSNPEnsembl.1
Natural variantiVAR_014651155K → N.Corresponds to variant rs5492dbSNPEnsembl.1
Natural variantiVAR_014186241G → R.3 PublicationsCorresponds to variant rs1799969dbSNPEnsembl.1
Natural variantiVAR_014652315V → M.Corresponds to variant rs5495dbSNPEnsembl.1
Natural variantiVAR_014653352P → L.1 PublicationCorresponds to variant rs1801714dbSNPEnsembl.1
Natural variantiVAR_014654397R → Q.1 PublicationCorresponds to variant rs5497dbSNPEnsembl.1
Natural variantiVAR_014187469K → E.6 PublicationsCorresponds to variant rs5498dbSNPEnsembl.1
Natural variantiVAR_016267478R → W.1 PublicationCorresponds to variant rs5030400dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.3. human.

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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109610. 170 interactors.
DIPiDIP-36658N.
IntActiP05362. 10 interactors.
MINTiMINT-4053071.
STRINGi9606.ENSP00000264832.

Chemistry databases

BindingDBiP05362.
ChEMBLiCHEMBL3070.
DrugBankiDB08818. Hyaluronic acid.
DB00108. Natalizumab.

PTM databases

iPTMnetiP05362.
PhosphoSitePlusiP05362.

Polymorphism and mutation databases

BioMutaiICAM1.
DMDMi68067956.

Proteomic databases

EPDiP05362.
MaxQBiP05362.
PaxDbiP05362.
PeptideAtlasiP05362.
PRIDEiP05362.

Protocols and materials databases

DNASUi3383.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000264832; ENSP00000264832; ENSG00000090339.
GeneIDi3383.
KEGGihsa:3383.
UCSCiuc002mnq.3. human.

Organism-specific databases

CTDi3383.
DisGeNETi3383.
GeneCardsiICAM1.
HGNCiHGNC:5344. ICAM1.
HPAiCAB002142.
HPA002126.
HPA004877.
MalaCardsiICAM1.
MIMi147840. gene.
611162. phenotype.
neXtProtiNX_P05362.
OpenTargetsiENSG00000090339.
PharmGKBiPA29592.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IPHM. Eukaryota.
ENOG410YQ1Q. LUCA.
GeneTreeiENSGT00530000063246.
HOGENOMiHOG000059554.
HOVERGENiHBG052074.
InParanoidiP05362.
KOiK06490.
OMAiGNWTWQE.
OrthoDBiEOG091G022Y.
PhylomeDBiP05362.
TreeFamiTF333745.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000090339-MONOMER.
ReactomeiR-HSA-198933. Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
R-HSA-216083. Integrin cell surface interactions.
R-HSA-877300. Interferon gamma signaling.
SABIO-RKP05362.
SIGNORiP05362.

Miscellaneous databases

ChiTaRSiICAM1. human.
EvolutionaryTraceiP05362.
GeneWikiiICAM-1.
GenomeRNAii3383.
PMAP-CutDBP05362.
PROiP05362.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000090339.
CleanExiHS_ICAM1.
ExpressionAtlasiP05362. baseline and differential.
GenevisibleiP05362. HS.

Family and domain databases

Gene3Di2.60.40.10. 5 hits.
InterProiIPR003988. ICAM.
IPR013768. ICAM_N.
IPR003987. ICAM_VCAM_N.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
[Graphical view]
PfamiPF03921. ICAM_N. 1 hit.
[Graphical view]
PRINTSiPR01473. ICAM.
PR01472. ICAMVCAM1.
SMARTiSM00409. IG. 3 hits.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 5 hits.
ProtoNetiSearch...

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: November 30, 2016
This is version 210 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.