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P13598 (ICAM2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 153. 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 2

Short name=ICAM-2
Alternative name(s):
CD_antigen=CD102
Gene names
Name:ICAM2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length275 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). ICAM2 may play a role in lymphocyte recirculation by blocking LFA-1-dependent cell adhesion. It mediates adhesive interactions important for antigen-specific immune response, NK-cell mediated clearance, lymphocyte recirculation, and other cellular interactions important for immune response and surveillance.

Subcellular location

Membrane; Single-pass type I membrane protein.

Sequence similarities

Belongs to the immunoglobulin superfamily. ICAM family.

Contains 2 Ig-like C2-type (immunoglobulin-like) domains.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424 Ref.4
Chain25 – 275251Intercellular adhesion molecule 2
PRO_0000014790

Regions

Topological domain25 – 223199Extracellular Potential
Transmembrane224 – 24825Helical; Potential
Topological domain249 – 27527Cytoplasmic Potential
Domain41 – 9858Ig-like C2-type 1
Domain127 – 19771Ig-like C2-type 2

Amino acid modifications

Glycosylation471N-linked (GlcNAc...)
Glycosylation821N-linked (GlcNAc...) Ref.6
Glycosylation1051N-linked (GlcNAc...) Ref.5 Ref.6
Glycosylation1531N-linked (GlcNAc...) Ref.6
Glycosylation1761N-linked (GlcNAc...) Ref.5 Ref.6
Glycosylation1871N-linked (GlcNAc...)
Disulfide bond48 ↔ 91
Disulfide bond52 ↔ 95
Disulfide bond134 ↔ 190

Natural variations

Natural variant371A → T.
Corresponds to variant rs5503 [ dbSNP | Ensembl ].
VAR_014655
Natural variant1991R → H.
Corresponds to variant rs5504 [ dbSNP | Ensembl ].
VAR_014656
Natural variant2561R → Q.
Corresponds to variant rs3764867 [ dbSNP | Ensembl ].
VAR_021920

Experimental info

Sequence conflict651D → N Ref.1
Sequence conflict651D → N Ref.3

Secondary structure

.................................... 275
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P13598 [UniParc].

Last modified October 3, 2006. Version 2.
Checksum: C54FB34D92A6FC38

FASTA27530,654
        10         20         30         40         50         60 
MSSFGYRTLT VALFTLICCP GSDEKVFEVH VRPKKLAVEP KGSLEVNCST TCNQPEVGGL 

        70         80         90        100        110        120 
ETSLDKILLD EQAQWKHYLV SNISHDTVLQ CHFTCSGKQE SMNSNVSVYQ PPRQVILTLQ 

       130        140        150        160        170        180 
PTLVAVGKSF TIECRVPTVE PLDSLTLFLF RGNETLHYET FGKAAPAPQE ATATFNSTAD 

       190        200        210        220        230        240 
REDGHRNFSC LAVLDLMSRG GNIFHKHSAP KMLEIYEPVS DSQMVIIVTV VSVLLSLFVT 

       250        260        270 
SVLLCFIFGQ HLRQQRMGTY GVRAAWRRLP QAFRP 

« Hide

References

« Hide 'large scale' references
[1]"Functional cloning of ICAM-2, a cell adhesion ligand for LFA-1 homologous to ICAM-1."
Staunton D.E., Dustin M.L., Springer T.A.
Nature 339:61-64(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Endothelial cell.
[2]"Structure of the gene for the human intercellular adhesion molecule 2 (ICAM-2)."
Garcia-Aguilar J., Staunton D., Springer T.A.
Submitted (FEB-1990) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"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: Brain.
[4]"Global profiling of protease cleavage sites by chemoselective labeling of protein N-termini."
Xu G., Shin S.B., Jaffrey S.R.
Proc. Natl. Acad. Sci. U.S.A. 106:19310-19315(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE [LARGE SCALE ANALYSIS] OF 25-33.
Tissue: Leukemic T-cell.
[5]"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-105 AND ASN-176.
Tissue: Plasma.
[6]"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-82; ASN-105; ASN-153 AND ASN-176.
Tissue: Leukemic T-cell.
[7]"Crystal structure of ICAM-2 reveals a distinctive integrin recognition surface."
Casasnovas J.M., Springer T.A., Liu J.-H., Harrison S.C., Wang J.-H.
Nature 387:312-315(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 25-216.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X15606 mRNA. Translation: CAA33630.1.
M32334 expand/collapse EMBL AC list , M32331, M32332, M32333 Genomic DNA. Translation: AAA36035.1.
BC003097 mRNA. Translation: AAH03097.1.
PIRS03967.
RefSeqNP_000864.2. NM_000873.3.
NP_001093256.1. NM_001099786.1.
NP_001093257.1. NM_001099787.1.
NP_001093258.1. NM_001099788.1.
NP_001093259.1. NM_001099789.1.
UniGeneHs.431460.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1ZXQX-ray2.20A25-216[»]
ProteinModelPortalP13598.
SMRP13598. Positions 25-251.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109611. 5 interactions.
DIPDIP-629N.
IntActP13598. 6 interactions.
STRING9606.ENSP00000225760.

PTM databases

PhosphoSiteP13598.

Polymorphism databases

DMDM115502404.

Proteomic databases

PaxDbP13598.
PRIDEP13598.

Protocols and materials databases

DNASU3384.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000412356; ENSP00000415283; ENSG00000108622.
ENST00000418105; ENSP00000388666; ENSG00000108622.
ENST00000449662; ENSP00000392634; ENSG00000108622.
ENST00000579687; ENSP00000462579; ENSG00000108622.
ENST00000579788; ENSP00000464665; ENSG00000108622.
GeneID3384.
KEGGhsa:3384.
UCSCuc002jdu.4. human.

Organism-specific databases

CTD3384.
GeneCardsGC17M062079.
H-InvDBHIX0014082.
HGNCHGNC:5345. ICAM2.
HPAHPA002020.
MIM146630. gene.
neXtProtNX_P13598.
PharmGKBPA29593.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG41332.
HOVERGENHBG052075.
InParanoidP13598.
KOK06523.
OMAFTIECRV.
PhylomeDBP13598.
TreeFamTF333745.

Enzyme and pathway databases

ReactomeREACT_118779. Extracellular matrix organization.
REACT_6900. Immune System.

Gene expression databases

ArrayExpressP13598.
BgeeP13598.
CleanExHS_ICAM2.
GenevestigatorP13598.

Family and domain databases

Gene3D2.60.40.10. 2 hits.
InterProIPR003988. ICAM.
IPR015653. ICAM2.
IPR013768. ICAM_N.
IPR003987. ICAM_VCAM_N.
IPR013783. Ig-like_fold.
[Graphical view]
PANTHERPTHR13771:SF3. PTHR13771:SF3. 1 hit.
PfamPF03921. ICAM_N. 1 hit.
[Graphical view]
PRINTSPR01473. ICAM.
PR01472. ICAMVCAM1.
ProtoNetSearch...

Other

ChiTaRSICAM2. human.
EvolutionaryTraceP13598.
GeneWikiICAM2.
GenomeRNAi3384.
NextBio13380.
PROP13598.
SOURCESearch...

Entry information

Entry nameICAM2_HUMAN
AccessionPrimary (citable) accession number: P13598
Secondary accession number(s): Q14600
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: October 3, 2006
Last modified: April 16, 2014
This is version 153 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 17

Human chromosome 17: entries, gene names and cross-references to MIM

Human cell differentiation molecules

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