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Protein

Early activation antigen CD69

Gene

CD69

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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: UniProtKB-KW
  3. transmembrane signaling receptor activity Source: ProtInc

GO - Biological processi

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

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 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:1694. CD69.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 4040CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei41 – 6121Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST
Topological domaini62 – 199138ExtracellularSequence AnalysisAdd
BLAST

GO - Cellular componenti

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

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

BgeeiQ07108.
CleanExiHS_CD69.
ExpressionAtlasiQ07108. baseline and differential.
GenevestigatoriQ07108.

Organism-specific databases

HPAiCAB002503.
HPA050525.

Interactioni

Subunit structurei

Homodimer; disulfide-linked.3 Publications

Protein-protein interaction databases

BioGridi107407. 1 interaction.
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 – 923Combined sources
Beta strandi95 – 995Combined sources
Helixi106 – 1149Combined sources
Turni115 – 1173Combined sources
Helixi126 – 13611Combined sources
Beta strandi141 – 1477Combined sources
Beta strandi153 – 1553Combined sources
Beta strandi168 – 1703Combined sources
Beta strandi172 – 1776Combined sources
Beta strandi180 – 1845Combined sources
Beta strandi190 – 1978Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.

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

        10         20         30         40         50
MSSENCFVAE NSSLHPESGQ ENDATSPHFS TRHEGSFQVP VLCAVMNVVF
60 70 80 90 100
ITILIIALIA LSVGQYNCPG QYTFSMPSDS HVSSCSEDWV GYQRKCYFIS
110 120 130 140 150
TVKRSWTSAQ NACSEHGATL AVIDSEKDMN FLKRYAGREE HWVGLKKEPG
160 170 180 190
HPWKWSNGKE FNNWFNVTGS DKCVFLKNTE VSSMECEKNL YWICNKPYK
Length:199
Mass (Da):22,559
Last modified:October 1, 1994 - v1
Checksum:i172E2699D2FB8DFB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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...

Protein-protein interaction databases

BioGridi107407. 1 interaction.
DIPiDIP-60426N.
IntActiQ07108. 1 interaction.
MINTiMINT-4656238.
STRINGi9606.ENSP00000228434.

PTM databases

PhosphoSiteiQ07108.

Polymorphism databases

DMDMi584906.

Proteomic databases

MaxQBiQ07108.
PaxDbiQ07108.
PRIDEiQ07108.

Protocols and materials databases

DNASUi969.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi969.
GeneCardsiGC12M010498.
HGNCiHGNC:1694. CD69.
HPAiCAB002503.
HPA050525.
MIMi107273. gene.
neXtProtiNX_Q07108.
PharmGKBiPA26233.
GenAtlasiSearch...

Phylogenomic databases

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

Miscellaneous databases

ChiTaRSiCD69. human.
EvolutionaryTraceiQ07108.
GeneWikiiCD69.
GenomeRNAii969.
NextBioi4056.
PROiQ07108.
SOURCEiSearch...

Gene expression databases

BgeeiQ07108.
CleanExiHS_CD69.
ExpressionAtlasiQ07108. baseline and differential.
GenevestigatoriQ07108.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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(1992) [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(1992) [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(1992) [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(1993) [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(2003) [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(1999) [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(2000) [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(2007) [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: March 4, 2015
This is version 144 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

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.