Reviewed, UniProtKB/Swiss-Prot P05362 (ICAM1_HUMAN)

Names and origin

Protein names

Recommended name:
    Intercellular adhesion molecule 1
      Short name=ICAM-1
Alternative name(s):
    Major group rhinovirus receptor
    CD_antigen=CD54

Gene names

Name:

ICAM1

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	532 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 SGEF and RHOG activation. In case of rhinovirus infection acts as a cellular receptor for the virus. Ref.10 Ref.11 Ref.12 Ref.16
Subunit structure	Homodimer Probable. Interacts with human herpesvirus 8 MIR2 protein Probable. Interacts with MUC1 and promotes cell aggregation in epithelial cells. Interacts with SGEF. Binds to coxsackievirus A21 capsid proteins and acts as a receptor for this virus.
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.
Sequence similarities	Belongs to the immunoglobulin superfamily. ICAM family. Contains 5 Ig-like C2-type (immunoglobulin-like) domains.

Ontologies

Keywords
Biological process	Cell adhesion Host-virus interaction
Cellular component	Membrane
Coding sequence diversity	Polymorphism
Domain	Immunoglobulin domain Repeat Signal Transmembrane
PTM	Disulfide bond Glycoprotein Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	T cell activation via T cell receptor contact with antigen bound to MHC molecule on antigen presenting cell Inferred from mutant phenotype. Source: UniProtKB adhesion to symbiont Ref.10 Inferred from direct assay. Source: UniProtKB heterophilic cell adhesion Traceable author statement. Source: UniProtKB leukocyte adhesion Inferred from mutant phenotype. Source: UniProtKB leukocyte migration Inferred from expression pattern. Source: UniProtKB membrane to membrane docking Inferred from expression pattern. Source: UniProtKB positive regulation of cellular extravasation Inferred from mutant phenotype. Source: UniProtKB regulation of leukocyte mediated cytotoxicity Traceable author statement. Source: UniProtKB virion attachment, binding of host cell surface receptor Ref.10 Inferred from direct assay. Source: UniProtKB
Cellular component	cytoplasm Inferred from direct assay. Source: HPA extracellular space Inferred from direct assay. Source: UniProtKB integral to plasma membrane Ref.10 Traceable author statement. Source: ProtInc
Molecular function	integrin binding Inferred from physical interaction. Source: UniProtKB transmembrane receptor activity Ref.10 Traceable author statement. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 27

27

Chain

28 – 532

505

Intercellular adhesion molecule 1

PRO_0000014783

Regions

Topological domain

28 – 480

453

Extracellular Potential

Transmembrane

481 – 503

23

Potential

Topological domain

504 – 532

29

Cytoplasmic Potential

Domain

41 – 103

63

Ig-like C2-type 1

Domain

128 – 193

66

Ig-like C2-type 2

Domain

230 – 297

68

Ig-like C2-type 3

Domain

325 – 378

54

Ig-like C2-type 4

Domain

412 – 464

53

Ig-like C2-type 5

Motif

152 – 154

3

Cell attachment site; atypical Potential

Amino acid modifications

Modified residue

521

1

Phosphothreonine Ref.17

Modified residue

530

1

Phosphothreonine Ref.17

Glycosylation

130

1

N-linked (GlcNAc...) Ref.24

Glycosylation

145

1

N-linked (GlcNAc...) Ref.24

Glycosylation

183

1

N-linked (GlcNAc...) Ref.24

Glycosylation

202

1

N-linked (GlcNAc...) Ref.24

Glycosylation

260

1

N-linked (GlcNAc...)

Glycosylation

267

1

N-linked (GlcNAc...) Ref.14 Ref.25

Glycosylation

296

1

N-linked (GlcNAc...) Ref.25

Glycosylation

385

1

N-linked (GlcNAc...) Ref.25

Glycosylation

406

1

N-linked (GlcNAc...) Potential

Disulfide bond

48 ↔ 92

Ref.24 Ref.25

Disulfide bond

52 ↔ 96

Ref.24 Ref.25

Disulfide bond

135 ↔ 186

Ref.24 Ref.25

Disulfide bond

237 ↔ 290

Ref.24 Ref.25

Disulfide bond

332 ↔ 371

Ref.24 Ref.25

Disulfide bond

403 ↔ 419

Ref.24 Ref.25

Disulfide bond

431 ↔ 457

Ref.24 Ref.25

Natural variations

Natural variant

34

1

S → C: dbSNP rs5491.

VAR_049879

Natural variant

56

1

K → M in Kilifi. dbSNP rs5491.

VAR_010204

Natural variant

155

1

K → N: dbSNP rs5492.

VAR_014651

Natural variant

241

1

G → R: dbSNP rs1799969. Ref.6 Ref.27 Ref.28

VAR_014186

Natural variant

315

1

V → M: dbSNP rs5495.

VAR_014652

Natural variant

352

1

P → L: dbSNP rs1801714. Ref.6

VAR_014653

Natural variant

397

1

R → Q: dbSNP rs5497. Ref.6

VAR_014654

Natural variant

469

1

K → E: dbSNP rs5498. Ref.27 Ref.1 Ref.2 Ref.4 Ref.9 Ref.30

VAR_014187

Natural variant

478

1

R → W: dbSNP rs5030400. Ref.6

VAR_016267

Experimental info

Sequence conflict

9 – 10

2

AL → PV in CAA40441. Ref.8

Sequence conflict

17

1

L → F in AAQ14902. Ref.9

Sequence conflict

27

1

A → V in AAQ14902. Ref.9

Secondary structure

1

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532

Helix Strand Turn

Details...

Beta strand

29 – 39

11

Beta strand

42 – 50

9

Beta strand

52 – 54

3

Beta strand

56 – 61

6

Beta strand

66 – 69

4

Beta strand

71 – 84

14

Beta strand

91 – 95

5

Beta strand

100 – 104

5

Beta strand

106 – 111

6

Beta strand

114 – 118

5

Beta strand

123 – 125

3

Beta strand

129 – 138

10

Helix

143 – 145

3

Beta strand

146 – 152

7

Beta strand

155 – 161

7

Turn

164 – 166

3

Beta strand

167 – 174

8

Beta strand

183 – 191

9

Helix

193 – 195

3

Beta strand

199 – 203

5

Beta strand

220 – 222

3

Beta strand

225 – 228

4

Beta strand

231 – 241

11

Helix

245 – 247

3

Beta strand

249 – 254

6

Beta strand

262 – 266

5

Beta strand

269 – 277

9

Helix

280 – 282

3

Beta strand

284 – 294

11

Beta strand

297 – 308

12

Beta strand

314 – 318

5

Beta strand

320 – 323

4

Beta strand

327 – 333

7

Beta strand

353 – 359

7

Helix

362 – 364

3

Beta strand

368 – 377

10

Beta strand

380 – 389

10

Beta strand

391 – 397

7

Beta strand

405 – 410

6

Beta strand

422 – 425

4

Beta strand

428 – 433

6

Turn

434 – 436

3

Helix

449 – 451

3

Beta strand

453 – 461

9

Beta strand

464 – 475

12

Sequences

	Sequence		Length	Mass (Da)
	P05362-1 [UniParc]. Last modified June 21, 2005. Version 2. Checksum: 550089365A733AFB	FASTA	532	57,825
	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

References

	« Hide 'large scale' referencesShow '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: 3340213] [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: 3349522] [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: 2544880] [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: 1680919] [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]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Kidney.
[8]	"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: 1983003] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-22.
[9]	"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: 15572059] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 5-532, VARIANT GLU-469. Tissue: Blood.
[10]	"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: 2538243] [Abstract] Cited for: PARTIAL PROTEIN SEQUENCE, FUNCTION AS A RHINOVIRUS RECEPTOR.
[11]	"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: 1968231] [Abstract] Cited for: FUNCTION AS A RHINOVIRUS RECEPTOR.
[12]	"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: 11173916] [Abstract] Cited for: INTERACTION WITH MUC1, FUNCTION.
[13]	"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: 11160747] [Abstract] Cited for: INTERACTION WITH COXSACKIEVIRUS A21 CAPSID PROTEINS.
[14]	"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: 16335952] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-267, MASS SPECTROMETRY. Tissue: Plasma.
[15]	"MARCH-IX mediates ubiquitination and downregulation of ICAM-1." Hoer S., Smith L., Lehner P.J. FEBS Lett. 581:45-51(2007) [PubMed: 17174307] [Abstract] Cited for: UBIQUITINATION.
[16]	"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: 17875742] [Abstract] Cited for: INTERACTION WITH SGEF, FUNCTION.
[17]	"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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-521 AND THR-530, MASS SPECTROMETRY.
[18]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[19]	"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: 19159218] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-202; ASN-260 AND ASN-267, MASS SPECTROMETRY. Tissue: Liver.
[20]	"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: 19349973] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-145 AND ASN-267, MASS SPECTROMETRY.
[21]	"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: 9539702] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 28-217.
[22]	"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: 9539703] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.25 ANGSTROMS) OF 28-212 IN COMPLEX WITH HUMAN RHINOVIRUS 14.
[23]	"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: 10562537] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.25 ANGSTROMS) OF 28-212.
[24]	"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: 12526797] [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.
[25]	"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: 15099525] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.06 ANGSTROMS) OF 212-477, SUBUNIT, DISULFIDE BONDS, GLYCOSYLATION AT ASN-267; ASN-296 AND ASN-385.
[26]	"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: 16004874] [Abstract] Cited for: STRUCTURE BY ELECTRON MICROSCOPY (8.0 ANGSTROMS) OF 24-473 IN COMPLEX WITH COXSACKIEVIRUS A21, SUBUNIT.
[27]	"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: 7525451] [Abstract] Cited for: VARIANTS ARG-241 AND GLU-469.
[28]	"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: 8557254] [Abstract] Cited for: VARIANT ARG-241.
[29]	"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: 9259284] [Abstract] Cited for: VARIANT KILIFI MET-56.
[30]	"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: 10391210] [Abstract] Cited for: VARIANT KILIFI MET-56, VARIANT GLU-469.
+	Additional computationally mapped references.

Web resources

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

Cross-references

Sequence databases

EMBLGenBankDDBJ

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.
BC015969 mRNA. Translation: AAH15969.1.
X57151 Genomic DNA. Translation: CAA40441.1.
AF340039 mRNA. Translation: AAQ14902.1.

IPI

IPI00008494.

PIR

A29849.

RefSeq

NP_000192.2.

UniGene

Hs.706750
Hs.707983

3D structure databases

PDBPDBe

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	[»]

SMR

P05362. Positions 28-477.

ModBase

Search...

PTM databases

PhosphoSite

P05362.

Proteomic databases

PRIDE

P05362.

Genome annotation databases

Ensembl

ENSG00000090339. Homo sapiens. [Contig view]

GeneID

3383.

KEGG

hsa:3383.

UCSC

uc002mnq.2. human.

Organism-specific databases

GeneCards

GC19P010247.

H-InvDB

HIX0014738.

HGNC

HGNC:5344. ICAM1.

HPA

CAB002142.
HPA002126.
HPA004877.

MIM

147840. gene.

Orphanet

1334. Chronic mucocutaneous candidiasis.

PharmGKB

PA29592.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

P05362.

HOVERGEN

P05362.

OMA

P05362. YSFPAPN.

Enzyme and pathway databases

Pathway_Interaction_DB

amb2_neutrophils_pathway. amb2 Integrin signaling.
txa2pathway. Thromboxane A2 receptor signaling.

Reactome

REACT_13552. Integrin cell surface interactions.
REACT_6900. Signaling in Immune system.

Gene expression databases

ArrayExpress

P05362.

Bgee

P05362.

CleanEx

HS_ICAM1.

GermOnline

ENSG00000090339. Homo sapiens.

Family and domain databases

InterPro

IPR003988. ICAM.
IPR013768. ICAM_N.
IPR003987. ICAM_VCAM_N.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
[Graphical view]

Gene3D

G3DSA:2.60.40.10. Ig-like_fold. 3 hits.

Pfam

PF03921. ICAM_N. 1 hit.
[Graphical view]

PRINTS

PR01473. ICAM.
PR01472. ICAMVCAM1.

SMART

SM00409. IG. 1 hit.
[Graphical view]

PROSITE

PS50835. IG_LIKE. False negative.
[Graphical view]

ProtoNet

Search...

Other Resources

DrugBank

DB00108. Natalizumab.
DB00641. Simvastatin.

NextBio

13376.

PMAP-CutDB

P05362.

SOURCE

Search...

Entry information

Entry name

ICAM1_HUMAN

Accession

Primary (citable) accession number: P05362
Secondary accession number(s): Q5NKV7, Q96B50

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1988
Last sequence update:	June 21, 2005
Last modified:	July 7, 2009
This is version 135 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)