Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot Q15762 (CD226_HUMAN)

Last modified June 16, 2009. Version 68. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Hide | Top

Names and origin

Protein namesRecommended name:
    CD226 antigen
Alternative name(s):
    DNAX accessory molecule 1
      Short name=DNAM-1
    CD_antigen=CD226
Gene names
Name: CD226
Synonyms: DNAM1
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Hide | Top

Protein attributes

Sequence length336 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

Hide | Top

General annotation (Comments)

Function

Receptor involved in intercellular adhesion, lymphocyte signaling, cytotoxicity and lymphokine secretion mediated by cytotoxic T-lymphocyte (CTL) and NK cell. Ref.1

Subunit structure

Interacts with PVR and PVRL2. Ref.4 Ref.5

Subcellular location

Membrane; Single-pass type I membrane protein Potential.

Tissue specificity

Expressed by peripheral blood T-lymphocytes. Ref.1

Post-translational modification

Phosphorylated. Ref.1 Ref.6

Sequence similarities

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

Hide | Top

Ontologies

Keywords
   Biological processCell adhesion
   Cellular componentMembrane
   Coding sequence diversityPolymorphism
   DomainImmunoglobulin domain
Repeat
Signal
Transmembrane
   Molecular functionReceptor
   PTMDisulfide bond
Glycoprotein
Phosphoprotein
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological processcell adhesion Ref.1

Traceable author statement. Source: ProtInc

cell recognition

Traceable author statement. Source: UniProtKB

positive regulation of Fc receptor mediated stimulatory signaling pathway

Inferred from direct assay. Source: UniProtKB

positive regulation of immunoglobulin mediated immune response

Inferred from direct assay. Source: UniProtKB

positive regulation of mast cell activation

Inferred from direct assay. Source: UniProtKB

positive regulation of natural killer cell mediated cytotoxicity directed against tumor cell target

Inferred from mutant phenotype. Source: UniProtKB

signal transduction Ref.1

Traceable author statement. Source: ProtInc

   Cellular componentcell surface

Inferred from direct assay. Source: UniProtKB

integral to plasma membrane Ref.1

Traceable author statement. Source: ProtInc

membrane raft

Traceable author statement. Source: UniProtKB

   Molecular functioncell adhesion molecule binding

Inferred from physical interaction. Source: UniProtKB

integrin binding

Inferred from physical interaction. Source: UniProtKB

protein kinase binding

Inferred from physical interaction. Source: UniProtKB

receptor activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Hide | Top

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 Ref.1
Chain19 – 336318CD226 antigen
PRO_0000014665

Regions

Topological domain19 – 254236Extracellular Potential
Transmembrane255 – 27521 Potential
Topological domain276 – 33661Cytoplasmic Potential
Domain19 – 126108Ig-like C2-type 1
Domain135 – 239105Ig-like C2-type 2
Compositional bias277 – 2848Poly-Arg

Amino acid modifications

Modified residue2901Phosphoserine Ref.6
Modified residue3221Phosphotyrosine Ref.6
Glycosylation321N-linked (GlcNAc...) Potential
Glycosylation831N-linked (GlcNAc...) Potential
Glycosylation901N-linked (GlcNAc...) Potential
Glycosylation971N-linked (GlcNAc...) Potential
Glycosylation1471N-linked (GlcNAc...) Potential
Glycosylation1861N-linked (GlcNAc...) Potential
Glycosylation1981N-linked (GlcNAc...) Potential
Glycosylation2311N-linked (GlcNAc...) Potential
Disulfide bond37 ↔ 108 Potential
Disulfide bond152 ↔ 222 Potential

Natural variations

Natural variant3071G → S: dbSNP rs763361.
VAR_018632

Hide | Top

Sequences

Sequence LengthMass (Da)Tools
Q15762-1 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 5379182CC47C11C3

FASTA33638,584
        10         20         30         40         50         60 
MDYPTLLLAL LHVYRALCEE VLWHTSVPFA ENMSLECVYP SMGILTQVEW FKIGTQQDSI 

        70         80         90        100        110        120 
AIFSPTHGMV IRKPYAERVY FLNSTMASNN MTLFFRNASE DDVGYYSCSL YTYPQGTWQK 

       130        140        150        160        170        180 
VIQVVQSDSF EAAVPSNSHI VSEPGKNVTL TCQPQMTWPV QAVRWEKIQP RQIDLLTYCN 

       190        200        210        220        230        240 
LVHGRNFTSK FPRQIVSNCS HGRWSVIVIP DVTVSDSGLY RCYLQASAGE NETFVMRLTV 

       250        260        270        280        290        300 
AEGKTDNQYT LFVAGGTVLL LLFVISITTI IVIFLNRRRR RERRDLFTES WDTQKAPNNY 

       310        320        330 
RSPISTGQPT NQSMDDTRED IYVNYPTFSR RPKTRV

« Hide

Hide | Top

References

« Hide 'large scale' references
[1]"DNAM-1, a novel adhesion molecule involved in the cytolytic function of T lymphocytes."
Shibuya A., Campbell D., Hannum C., Yssel H., Franz-Bacon K., McClanahan T., Kitamura T., Nicholl J., Sutherland G.R., Lanier L.L., Phillips J.H.
Immunity 4:573-581(1996) [PubMed: 8673704] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 19-39; 54-72; 204-221 AND 285-294, FUNCTION, PHOSPHORYLATION, GLYCOSYLATION, TISSUE SPECIFICITY.
[2]"Receptor involved in the NK cell triggering."
Biassoni R.
Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Natural killer cell.
[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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[4]"Functional characterization of DNAM-1 (CD226) interaction with its ligands PVR (CD155) and nectin-2 (PRR-2/CD112)."
Tahara-Hanaoka S., Shibuya K., Onoda Y., Zhang H., Yamazaki S., Miyamoto A., Honda S., Lanier L.L., Shibuya A.
Int. Immunol. 16:533-538(2004) [PubMed: 15039383] [Abstract]
Cited for: INTERACTION WITH PVR AND PVRL2.
[5]"PVR (CD155) and Nectin-2 (CD112) as ligands of the human DNAM-1 (CD226) activating receptor: involvement in tumor cell lysis."
Pende D., Bottino C., Castriconi R., Cantoni C., Marcenaro S., Rivera P., Spaggiari G.M., Dondero A., Carnemolla B., Reymond N., Mingari M.C., Lopez M., Moretta L., Moretta A.
Mol. Immunol. 42:463-469(2005) [PubMed: 15607800] [Abstract]
Cited for: INTERACTION WITH PVR AND PVRL2.
[6]"Phosphoproteome of resting human platelets."
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A.
J. Proteome Res. 7:526-534(2008) [PubMed: 18088087] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-290 AND TYR-322, MASS SPECTROMETRY.
Tissue: Platelet.
+Additional computationally mapped references.

Hide | Top

Cross-references

Sequence databases

U56102 mRNA. Translation: AAC50560.1.
AJ537553 mRNA. Translation: CAD61184.1.
BC074787 mRNA. Translation: AAH74787.1.
IPIIPI00008578.
RefSeqNP_006557.2.
UniGeneHs.660130

3D structure databases

ModBaseSearch...

PTM databases

PhosphoSiteQ15762.

Proteomic databases

PRIDEQ15762.

Genome annotation databases

EnsemblENSG00000150637. Homo sapiens. [Contig view]
GeneID10666.
KEGGhsa:10666.

Organism-specific databases

GeneCardsGC18M065681.
H-InvDBHIX0039717.
HGNCHGNC:16961. CD226.
HPAHPA015715.
MIM605397. gene.
PharmGKBPA134911130.
GenAtlasSearch...

Phylogenomic databases

HOGENOMQ15762.
HOVERGENQ15762.

Enzyme and pathway databases

ReactomeREACT_6900. Signaling in Immune system.

Gene expression databases

ArrayExpressQ15762.
BgeeQ15762.
CleanExHS_CD226.
GermOnlineENSG00000150637. Homo sapiens.

Family and domain databases

InterProIPR007110. Ig-like.
IPR013783. Ig-like_fold.
IPR003598. Ig_sub2.
IPR013106. Ig_V-set.
[Graphical view]
Gene3DG3DSA:2.60.40.10. Ig-like_fold. 2 hits.
PfamPF07686. V-set. 2 hits.
[Graphical view]
SMARTSM00408. IGc2. 1 hit.
[Graphical view]
PROSITEPS50835. IG_LIKE. 2 hits.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio40559.
SOURCESearch...

Hide | Top

Entry information

Entry nameCD226_HUMAN
AccessionPrimary (citable) accession number: Q15762
Entry history
Integrated into UniProtKB/Swiss-Prot: May 24, 2004
Last sequence update: November 1, 1996
Last modified: June 16, 2009
This is version 68 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Hide | Top

Relevant documents

Human cell differentiation molecules

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

Human chromosome 18

Human chromosome 18: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents