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Protein

Intercellular adhesion molecule 2

Gene

ICAM2

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). 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.

GO - Molecular functioni

  1. integrin binding Source: BHF-UCL

GO - Biological processi

  1. cell adhesion Source: GO_Central
  2. extracellular matrix organization Source: Reactome
  3. regulation of immune response Source: Reactome
  4. single organismal cell-cell adhesion Source: InterPro
Complete GO annotation...

Keywords - Biological processi

Cell adhesion

Enzyme and pathway databases

ReactomeiREACT_11152. Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
REACT_13552. Integrin cell surface interactions.

Names & Taxonomyi

Protein namesi
Recommended name:
Intercellular adhesion molecule 2
Short name:
ICAM-2
Alternative name(s):
CD_antigen: CD102
Gene namesi
Name:ICAM2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 17

Organism-specific databases

HGNCiHGNC:5345. ICAM2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini25 – 223199ExtracellularSequence AnalysisAdd
BLAST
Transmembranei224 – 24825HelicalSequence AnalysisAdd
BLAST
Topological domaini249 – 27527CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. extracellular vesicular exosome Source: UniProtKB
  2. integral component of plasma membrane Source: ProtInc
  3. membrane Source: UniProtKB
  4. plasma membrane Source: Reactome
  5. uropod Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA29593.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 24241 PublicationAdd
BLAST
Chaini25 – 275251Intercellular adhesion molecule 2PRO_0000014790Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi47 – 471N-linked (GlcNAc...)
Disulfide bondi48 ↔ 91
Disulfide bondi52 ↔ 95
Glycosylationi82 – 821N-linked (GlcNAc...)1 Publication
Glycosylationi105 – 1051N-linked (GlcNAc...)2 Publications
Disulfide bondi134 ↔ 190
Glycosylationi153 – 1531N-linked (GlcNAc...)1 Publication
Glycosylationi176 – 1761N-linked (GlcNAc...)2 Publications
Glycosylationi187 – 1871N-linked (GlcNAc...)

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiP13598.
PaxDbiP13598.
PRIDEiP13598.

PTM databases

PhosphoSiteiP13598.

Expressioni

Gene expression databases

BgeeiP13598.
CleanExiHS_ICAM2.
ExpressionAtlasiP13598. baseline and differential.
GenevestigatoriP13598.

Organism-specific databases

HPAiHPA002020.

Interactioni

Protein-protein interaction databases

BioGridi109611. 18 interactions.
DIPiDIP-629N.
IntActiP13598. 6 interactions.
STRINGi9606.ENSP00000225760.

Structurei

Secondary structure

1
275
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi29 – 3810Combined sources
Beta strandi42 – 5110Combined sources
Beta strandi56 – 616Combined sources
Beta strandi63 – 7210Combined sources
Beta strandi75 – 839Combined sources
Beta strandi87 – 959Combined sources
Beta strandi98 – 10811Combined sources
Beta strandi116 – 12510Combined sources
Beta strandi128 – 1369Combined sources
Helixi142 – 1443Combined sources
Beta strandi145 – 1517Combined sources
Beta strandi154 – 1607Combined sources
Beta strandi171 – 1788Combined sources
Helixi181 – 1855Combined sources
Beta strandi188 – 1958Combined sources
Helixi197 – 1993Combined sources
Beta strandi203 – 2075Combined sources
Beta strandi214 – 2163Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ZXQX-ray2.20A25-216[»]
ProteinModelPortaliP13598.
SMRiP13598. Positions 25-216.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP13598.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini41 – 9858Ig-like C2-type 1Add
BLAST
Domaini127 – 19771Ig-like C2-type 2Add
BLAST

Sequence similaritiesi

Belongs to the immunoglobulin superfamily. ICAM family.Curated

Keywords - Domaini

Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG41332.
HOVERGENiHBG052075.
InParanoidiP13598.
KOiK06523.
OMAiMLEIYEP.
PhylomeDBiP13598.
TreeFamiTF333745.

Family and domain databases

Gene3Di2.60.40.10. 2 hits.
InterProiIPR003988. ICAM.
IPR015653. ICAM2.
IPR013768. ICAM_N.
IPR003987. ICAM_VCAM_N.
IPR013783. Ig-like_fold.
[Graphical view]
PANTHERiPTHR13771:SF3. PTHR13771:SF3. 1 hit.
PfamiPF03921. ICAM_N. 1 hit.
[Graphical view]
PRINTSiPR01473. ICAM.
PR01472. ICAMVCAM1.

Sequencei

Sequence statusi: Complete.

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

P13598-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSFGYRTLT VALFTLICCP GSDEKVFEVH VRPKKLAVEP KGSLEVNCST
60 70 80 90 100
TCNQPEVGGL ETSLDKILLD EQAQWKHYLV SNISHDTVLQ CHFTCSGKQE
110 120 130 140 150
SMNSNVSVYQ PPRQVILTLQ PTLVAVGKSF TIECRVPTVE PLDSLTLFLF
160 170 180 190 200
RGNETLHYET FGKAAPAPQE ATATFNSTAD REDGHRNFSC LAVLDLMSRG
210 220 230 240 250
GNIFHKHSAP KMLEIYEPVS DSQMVIIVTV VSVLLSLFVT SVLLCFIFGQ
260 270
HLRQQRMGTY GVRAAWRRLP QAFRP
Length:275
Mass (Da):30,654
Last modified:October 3, 2006 - v2
Checksum:iC54FB34D92A6FC38
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti65 – 651D → N (PubMed:2497351).Curated
Sequence conflicti65 – 651D → N (PubMed:15489334).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti37 – 371A → T.
Corresponds to variant rs5503 [ dbSNP | Ensembl ].
VAR_014655
Natural varianti199 – 1991R → H.
Corresponds to variant rs5504 [ dbSNP | Ensembl ].
VAR_014656
Natural varianti256 – 2561R → Q.
Corresponds to variant rs3764867 [ dbSNP | Ensembl ].
VAR_021920

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X15606 mRNA. Translation: CAA33630.1.
M32334
, M32331, M32332, M32333 Genomic DNA. Translation: AAA36035.1.
BC003097 mRNA. Translation: AAH03097.1.
CCDSiCCDS11657.1.
PIRiS03967.
RefSeqiNP_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.
UniGeneiHs.431460.

Genome annotation databases

EnsembliENST00000412356; ENSP00000415283; ENSG00000108622.
ENST00000418105; ENSP00000388666; ENSG00000108622.
ENST00000449662; ENSP00000392634; ENSG00000108622.
ENST00000579687; ENSP00000462579; ENSG00000108622.
ENST00000579788; ENSP00000464665; ENSG00000108622.
GeneIDi3384.
KEGGihsa:3384.
UCSCiuc002jdu.4. human.

Polymorphism databases

DMDMi115502404.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Functional Glycomics Gateway - Glycan Binding

ICAM-2

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X15606 mRNA. Translation: CAA33630.1.
M32334
, M32331, M32332, M32333 Genomic DNA. Translation: AAA36035.1.
BC003097 mRNA. Translation: AAH03097.1.
CCDSiCCDS11657.1.
PIRiS03967.
RefSeqiNP_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.
UniGeneiHs.431460.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ZXQX-ray2.20A25-216[»]
ProteinModelPortaliP13598.
SMRiP13598. Positions 25-216.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109611. 18 interactions.
DIPiDIP-629N.
IntActiP13598. 6 interactions.
STRINGi9606.ENSP00000225760.

PTM databases

PhosphoSiteiP13598.

Polymorphism databases

DMDMi115502404.

Proteomic databases

MaxQBiP13598.
PaxDbiP13598.
PRIDEiP13598.

Protocols and materials databases

DNASUi3384.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000412356; ENSP00000415283; ENSG00000108622.
ENST00000418105; ENSP00000388666; ENSG00000108622.
ENST00000449662; ENSP00000392634; ENSG00000108622.
ENST00000579687; ENSP00000462579; ENSG00000108622.
ENST00000579788; ENSP00000464665; ENSG00000108622.
GeneIDi3384.
KEGGihsa:3384.
UCSCiuc002jdu.4. human.

Organism-specific databases

CTDi3384.
GeneCardsiGC17M062079.
H-InvDBHIX0014082.
HGNCiHGNC:5345. ICAM2.
HPAiHPA002020.
MIMi146630. gene.
neXtProtiNX_P13598.
PharmGKBiPA29593.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG41332.
HOVERGENiHBG052075.
InParanoidiP13598.
KOiK06523.
OMAiMLEIYEP.
PhylomeDBiP13598.
TreeFamiTF333745.

Enzyme and pathway databases

ReactomeiREACT_11152. Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
REACT_13552. Integrin cell surface interactions.

Miscellaneous databases

ChiTaRSiICAM2. human.
EvolutionaryTraceiP13598.
GeneWikiiICAM2.
GenomeRNAii3384.
NextBioi13380.
PROiP13598.
SOURCEiSearch...

Gene expression databases

BgeeiP13598.
CleanExiHS_ICAM2.
ExpressionAtlasiP13598. baseline and differential.
GenevestigatoriP13598.

Family and domain databases

Gene3Di2.60.40.10. 2 hits.
InterProiIPR003988. ICAM.
IPR015653. ICAM2.
IPR013768. ICAM_N.
IPR003987. ICAM_VCAM_N.
IPR013783. Ig-like_fold.
[Graphical view]
PANTHERiPTHR13771:SF3. PTHR13771:SF3. 1 hit.
PfamiPF03921. ICAM_N. 1 hit.
[Graphical view]
PRINTSiPR01473. ICAM.
PR01472. ICAMVCAM1.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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(1988) [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 (JAN-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(2003) [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(2008) [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(2004) [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(2008) [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(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 25-216.

Entry informationi

Entry nameiICAM2_HUMAN
AccessioniPrimary (citable) accession number: P13598
Secondary accession number(s): Q14600
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: October 3, 2006
Last modified: February 4, 2015
This is version 162 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 17
    Human chromosome 17: 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

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 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.