The CD44 antigen is a cell-surface glycoprotein involved in cell-cell interactions, cell adhesion and migration.
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CHEMICAL STRUCTURE AND IMAGES
When relevant for the function
- Primary structure
- Secondary structure
- Tertiary structure
- Quaternary structure
Protein Aminoacids Percentage
The Protein Aminoacids Percentage gives useful information on the local environment and the metabolic status of the cell (starvation, lack of essential AA, hypoxia)
Model (Width 600 px)
SYNTHESIS AND TURNOVER
- Cell signaling and Ligand transport
- Structural proteins
In humans, HA is involved in several key processes, including cell signaling, wound repair and regeneration, morphogenesis, matrix organization and pathobiology.
Role, Metabolism, Chemical Modifications and Applications of Hyaluronan
CD44 and its role in inflammation and inflammatory diseases. 1999
1. FUNCTION: Possible transcription factor. Specifically binds to the CT/GC-rich region of the interleukin-3 promoter and mediates tax transactivation of IL-3.
2. SUBUNIT: Interacts with ARHGAP22 (By similarity).
3. SUBCELLULAR LOCATION: Nucleus.
4. TISSUE SPECIFICITY: Ubiquitously expressed. Highest levels in skeletal muscle and kidney.
5. SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein family.
6. SIMILARITY: Contains 6 C2H2-type zinc fingers.
The osteopontin-CD44 survival signal involves activation of the phosphatidylinositol 3-kinase/Akt signaling pathway.
J Biol Chem. 2001 Dec 7;276(49):46024-30. Epub 2001 Oct 5.
Lin YH, Yang-Yen HF.
We have recently demonstrated that the gene encoding the osteopontin (OPN) protein is activated both by interleukin-3 and granulocyte-macrophage colony-stimulating factor signaling pathways and that, through binding to the cell surface receptor CD44, OPN contributes to the survival activities of interleukin (IL)-3 and GM-CSF (Lin, Y.-H., Huang, C.-J., Chao, J.-R., Chen, S.-T., Lee, S.-F., Yen, J. J.-Y., and Yang-Yen, H.-F. (2000) Mol. Cell. Biol. 20, 2734-2742). In this report, we demonstrate that the CD44-binding domain of OPN involves a region containing amino acid residues from 121 to 140 and that both threonine and serine at positions 137 and 147, respectively, are essential for the survival stimulatory effect of OPN. Substitution of either residue with alanine results into a dominant negative mutant that overrides the survival effect of IL-3. Upon binding to the CD44 receptor, the wild-type OPN but not the inactive mutant induces activation of phosphatidylinositol 3-kinase and Akt. Last, we demonstrate that two waves of Akt activation are detected in IL-3-treated cells and that the survival promoting effect of OPN is mediated predominantly through the phosphatidylinositol 3-kinase/Akt signaling pathway. Together, our results suggest that a positive autoregulatory loop is involved in the survival pathway of IL-3.
1. FUNCTION: Regulator which is able to repress transcription, possibly via its interaction with a multiprotein chromatin remodeling complex that modifies the chromatin. Its interaction with BRCA2 suggests that it may play a central role in the DNA repair function of BRCA2.
2. SUBUNIT: Homodimer. Interacts with the transactivation domain of BRCA2. Interacts with the chromoshadow domain of CBX1 and with ZMYND11. Does not interact with CBX3 or CBX5.
3. SUBCELLULAR LOCATION: Nucleus. Note=Localizes to DNA damage markers in irradiated cells, suggesting that it participates in DNA repair process.
4. ALTERNATIVE PRODUCTS: Event=Alternative splicing; Named isoforms=3; Name=1; IsoId=Q7Z589-1; Sequence=Displayed; Name=2; IsoId=Q7Z589-2; Sequence=VSP_010431; Note=No experimental confirmation available; Name=3; IsoId=Q7Z589-3; Sequence=VSP_020774, VSP_020775; Note=No experimental confirmation available;
5. MISCELLANEOUS: Defects in EMSY may be a cause of sporadic breast cancer and higher-grade ovarian cancers. Overexpressed through amplification almost exclusively in sporadic breast cancer (13%) and higher-grade ovarian cancer (17%). Amplification is associated with worse survival, particularly in node-negative breast cancer, suggesting that it may be of prognostic value.
6. MISCELLANEOUS: Was named EMSY by PubMed:14651845 because the protein sequence contains the word 'SISTER', after the first author's sister, who is a breast cancer nurse.
7. SIMILARITY: Contains 1 ENT (EMSY N-terminal) domain.
8. SEQUENCE CAUTION: Sequence=AAF86947.1; Type=Erroneous initiation; Sequence=AAH29375.1; Type=Erroneous initiation; Sequence=AAL65260.1; Type=Erroneous initiation; Sequence=BAB14627.1; Type=Erroneous initiation;
9. WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL="http://atlasgeneticsoncology.org/Genes/C11ORF30ID173.html";
- FUNCTION: SRF is a transcription factor that binds to the serum response element (SRE), a short sequence of dyad symmetry located 300 bp to the 5' of the site of transcription initiation of some genes (such as FOS). Required for cardiac differentiation and maturation.
- SUBUNIT: Binds DNA as a multimer, probably a dimer. Interacts with MLLT7/FOXO4, NKX3A and SSRP1. Interacts with ARID2 and SRFBP1 (By similarity). Forms complexes with ARID2, MYOCD, NKX2-5 and SRFBP1 (By similarity). Forms a nuclear ternary complex with MKL1 and SCAI.
- INTERACTION: Q969V6:MKL1; NbExp=2; IntAct=EBI-493034, EBI-493122; Q9ULH7:MKL2; NbExp=2; IntAct=EBI-493034, EBI-493007; Q8IZQ8:MYOCD; NbExp=1; IntAct=EBI-493034, EBI-493384;
- SUBCELLULAR LOCATION: Nucleus.
- PTM: Phosphorylated by PRKDC.
- SIMILARITY: Contains 1 MADS-box domain