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Q07108

- CD69_HUMAN

UniProt

Q07108 - CD69_HUMAN

Protein

Early activation antigen CD69

Gene

CD69

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 139 (01 Oct 2014)
      Sequence version 1 (01 Oct 1994)
      Previous versions | rss
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    Functioni

    Involved in lymphocyte proliferation and functions as a signal transmitting receptor in lymphocytes, natural killer (NK) cells, and platelets.

    GO - Molecular functioni

    1. calcium ion binding Source: Ensembl
    2. carbohydrate binding Source: InterPro
    3. transmembrane signaling receptor activity Source: ProtInc

    GO - Biological processi

    1. cellular response to drug Source: Ensembl
    2. signal transduction Source: GOC

    Keywords - Ligandi

    Lectin

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Early activation antigen CD69
    Alternative name(s):
    Activation inducer molecule
    Short name:
    AIM
    BL-AC/P26
    C-type lectin domain family 2 member C
    EA1
    Early T-cell activation antigen p60
    GP32/28
    Leukocyte surface antigen Leu-23
    MLR-3
    CD_antigen: CD69
    Gene namesi
    Name:CD69
    Synonyms:CLEC2C
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:1694. CD69.

    Subcellular locationi

    GO - Cellular componenti

    1. external side of plasma membrane Source: Ensembl
    2. integral component of plasma membrane Source: ProtInc

    Keywords - Cellular componenti

    Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA26233.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 199199Early activation antigen CD69PRO_0000046583Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi68 – 68InterchainCurated
    Disulfide bondi85 ↔ 96
    Disulfide bondi113 ↔ 194
    Glycosylationi166 – 1661N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi173 ↔ 186

    Post-translational modificationi

    Constitutive Ser/Thr phosphorylation in both mature thymocytes and activated T-lymphocytes.

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein

    Proteomic databases

    MaxQBiQ07108.
    PaxDbiQ07108.
    PRIDEiQ07108.

    PTM databases

    PhosphoSiteiQ07108.

    Expressioni

    Tissue specificityi

    Expressed on the surface of activated T-cells, B-cells, natural killer cells, neutrophils, eosinophils, epidermal Langerhans cells and platelets.

    Developmental stagei

    Earliest inducible cell surface glycoprotein acquired during lymphoid activation.

    Inductioni

    By antigens, mitogens or activators of PKC on the surface of T and B-lymphocytes. By interaction of IL-2 with the p75 IL-2R on the surface of NK cells.

    Gene expression databases

    ArrayExpressiQ07108.
    BgeeiQ07108.
    CleanExiHS_CD69.
    GenevestigatoriQ07108.

    Organism-specific databases

    HPAiCAB002503.

    Interactioni

    Subunit structurei

    Homodimer; disulfide-linked.3 Publications

    Protein-protein interaction databases

    DIPiDIP-60426N.
    IntActiQ07108. 1 interaction.
    MINTiMINT-4656238.
    STRINGi9606.ENSP00000228434.

    Structurei

    Secondary structure

    1
    199
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi90 – 923
    Beta strandi95 – 995
    Helixi106 – 1149
    Turni115 – 1173
    Helixi126 – 13611
    Beta strandi141 – 1477
    Beta strandi153 – 1553
    Beta strandi168 – 1703
    Beta strandi172 – 1776
    Beta strandi180 – 1845
    Beta strandi190 – 1978

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1E87X-ray1.50A82-199[»]
    1E8IX-ray1.95A/B82-199[»]
    1FM5X-ray2.27A1-199[»]
    3CCKX-ray1.80A/B82-199[»]
    3HUPX-ray1.37A/B70-199[»]
    DisProtiDP00306.
    ProteinModelPortaliQ07108.
    SMRiQ07108. Positions 79-199.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ07108.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 4040CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini62 – 199138ExtracellularSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei41 – 6121Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini92 – 195104C-type lectinPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 C-type lectin domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal-anchor, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG276386.
    HOGENOMiHOG000111491.
    HOVERGENiHBG005288.
    InParanoidiQ07108.
    KOiK06502.
    OMAiVGQYNCP.
    OrthoDBiEOG793B96.
    PhylomeDBiQ07108.
    TreeFamiTF351467.

    Family and domain databases

    Gene3Di3.10.100.10. 1 hit.
    InterProiIPR001304. C-type_lectin.
    IPR016186. C-type_lectin-like.
    IPR016187. C-type_lectin_fold.
    [Graphical view]
    PfamiPF00059. Lectin_C. 1 hit.
    [Graphical view]
    SMARTiSM00034. CLECT. 1 hit.
    [Graphical view]
    SUPFAMiSSF56436. SSF56436. 1 hit.
    PROSITEiPS50041. C_TYPE_LECTIN_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q07108-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSSENCFVAE NSSLHPESGQ ENDATSPHFS TRHEGSFQVP VLCAVMNVVF    50
    ITILIIALIA LSVGQYNCPG QYTFSMPSDS HVSSCSEDWV GYQRKCYFIS 100
    TVKRSWTSAQ NACSEHGATL AVIDSEKDMN FLKRYAGREE HWVGLKKEPG 150
    HPWKWSNGKE FNNWFNVTGS DKCVFLKNTE VSSMECEKNL YWICNKPYK 199
    Length:199
    Mass (Da):22,559
    Last modified:October 1, 1994 - v1
    Checksum:i172E2699D2FB8DFB
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L07555 mRNA. Translation: AAB46359.1.
    Z22576 mRNA. Translation: CAA80298.1.
    Z30426
    , Z30430, Z30427, Z30429, Z30428 Genomic DNA. Translation: CAA83017.1.
    BC007037 mRNA. Translation: AAH07037.1.
    CCDSiCCDS8604.1.
    PIRiJH0822.
    RefSeqiNP_001772.1. NM_001781.2.
    UniGeneiHs.208854.

    Genome annotation databases

    EnsembliENST00000228434; ENSP00000228434; ENSG00000110848.
    GeneIDi969.
    KEGGihsa:969.
    UCSCiuc001qwk.3. human.

    Polymorphism databases

    DMDMi584906.

    Cross-referencesi

    Web resourcesi

    Functional Glycomics Gateway - Glycan Binding

    CD69

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L07555 mRNA. Translation: AAB46359.1 .
    Z22576 mRNA. Translation: CAA80298.1 .
    Z30426
    , Z30430 , Z30427 , Z30429 , Z30428 Genomic DNA. Translation: CAA83017.1 .
    BC007037 mRNA. Translation: AAH07037.1 .
    CCDSi CCDS8604.1.
    PIRi JH0822.
    RefSeqi NP_001772.1. NM_001781.2.
    UniGenei Hs.208854.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1E87 X-ray 1.50 A 82-199 [» ]
    1E8I X-ray 1.95 A/B 82-199 [» ]
    1FM5 X-ray 2.27 A 1-199 [» ]
    3CCK X-ray 1.80 A/B 82-199 [» ]
    3HUP X-ray 1.37 A/B 70-199 [» ]
    DisProti DP00306.
    ProteinModelPortali Q07108.
    SMRi Q07108. Positions 79-199.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-60426N.
    IntActi Q07108. 1 interaction.
    MINTi MINT-4656238.
    STRINGi 9606.ENSP00000228434.

    PTM databases

    PhosphoSitei Q07108.

    Polymorphism databases

    DMDMi 584906.

    Proteomic databases

    MaxQBi Q07108.
    PaxDbi Q07108.
    PRIDEi Q07108.

    Protocols and materials databases

    DNASUi 969.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000228434 ; ENSP00000228434 ; ENSG00000110848 .
    GeneIDi 969.
    KEGGi hsa:969.
    UCSCi uc001qwk.3. human.

    Organism-specific databases

    CTDi 969.
    GeneCardsi GC12M010256.
    HGNCi HGNC:1694. CD69.
    HPAi CAB002503.
    MIMi 107273. gene.
    neXtProti NX_Q07108.
    PharmGKBi PA26233.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG276386.
    HOGENOMi HOG000111491.
    HOVERGENi HBG005288.
    InParanoidi Q07108.
    KOi K06502.
    OMAi VGQYNCP.
    OrthoDBi EOG793B96.
    PhylomeDBi Q07108.
    TreeFami TF351467.

    Miscellaneous databases

    EvolutionaryTracei Q07108.
    GeneWikii CD69.
    GenomeRNAii 969.
    NextBioi 4056.
    PROi Q07108.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q07108.
    Bgeei Q07108.
    CleanExi HS_CD69.
    Genevestigatori Q07108.

    Family and domain databases

    Gene3Di 3.10.100.10. 1 hit.
    InterProi IPR001304. C-type_lectin.
    IPR016186. C-type_lectin-like.
    IPR016187. C-type_lectin_fold.
    [Graphical view ]
    Pfami PF00059. Lectin_C. 1 hit.
    [Graphical view ]
    SMARTi SM00034. CLECT. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56436. SSF56436. 1 hit.
    PROSITEi PS50041. C_TYPE_LECTIN_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Expression cloning of the early activation antigen CD69, a type II integral membrane protein with a C-type lectin domain."
      Hamann J., Fiebig H., Strauss M.
      J. Immunol. 150:4920-4927(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Blood.
    2. "Molecular cloning, expression, and chromosomal localization of the human earliest lymphocyte activation antigen AIM/CD69, a new member of the C-type animal lectin superfamily of signal-transmitting receptors."
      Lopez-Cabrera M., Santis A.G., Fernandez-Ruiz E., Blacher R., Esch F., Sanchez-Mateos P., Sanchez-Madrid F.
      J. Exp. Med. 178:537-547(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 96-103; 128-146 AND 189-199.
      Tissue: Blood.
    3. "Molecular characterization of the early activation antigen CD69: a type II membrane glycoprotein related to a family of natural killer cell activation antigens."
      Ziegler S.F., Ramsdell F., Hjerrild K.A., Armitage R.J., Grabstein K.H., Hennen K.B., Farrah T., Fanslow W.C., Shevach E.M., Alderson M.R.
      Eur. J. Immunol. 23:1643-1648(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    4. "Structure of the gene coding for the human early lymphocyte activation antigen CD69: a C-type lectin receptor evolutionarily related with the gene families of natural killer cell-specific receptors."
      Santis A., Lopez-Cabrera M., Hamann J., Strauss M., Sanchez-Madrid F.
      Eur. J. Immunol. 24:1692-1697(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Tissue: Placenta.
    5. "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: Pancreas.
    6. "Crystal structure of human CD69: a C-type lectin-like activation marker of hematopoietic cells."
      Natarajan K., Sawicki M.W., Margulies D.H., Mariuzza R.A.
      Biochemistry 39:14779-14786(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.27 ANGSTROMS), SUBUNIT, DISULFIDE BONDS.
    7. "Crystal structure of the C-type lectin-like domain from the human hematopoietic cell receptor CD69."
      Llera A.S., Viedma F., Sanchez-Madrid F., Tormo J.
      J. Biol. Chem. 276:7312-7319(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 82-199, SUBUNIT, DISULFIDE BONDS.
    8. "Soluble recombinant CD69 receptors optimized to have an exceptional physical and chemical stability display prolonged circulation and remain intact in the blood of mice."
      Vanek O., Nalezkova M., Kavan D., Borovickova I., Pompach P., Novak P., Kumar V., Vannucci L., Hudecek J., Hofbauerova K., Kopecky V. Jr., Brynda J., Kolenko P., Dohnalek J., Kaderavek P., Chmelik J., Gorcik L., Zidek L., Sklenar V., Bezouska K.
      FEBS J. 275:5589-5606(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 82-199, SUBUNIT, DISULFIDE BONDS.

    Entry informationi

    Entry nameiCD69_HUMAN
    AccessioniPrimary (citable) accession number: Q07108
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1994
    Last sequence update: October 1, 1994
    Last modified: October 1, 2014
    This is version 139 of the entry and version 1 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 12
      Human chromosome 12: entries, gene names and cross-references to MIM
    3. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    4. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3