Human Gene CD36 (ENST00000435819.5) Description and Page Index
  Description: Seems to have numerous potential physiological functions. Binds to collagen, thrombospondin, anionic phospholipids and oxidized LDL. May function as a cell adhesion molecule. Directly mediates cytoadherence of Plasmodium falciparum parasitized erythrocytes. Binds long chain fatty acids and may function in the transport and/or as a regulator of fatty acid transport. Receptor for thombospondins, THBS1 AND THBS2, mediating their antiangiogenic effects. (from UniProt P16671)
Gencode Transcript: ENST00000435819.5
Gencode Gene: ENSG00000135218.19
Transcript (Including UTRs)
   Position: hg38 chr7:80,369,575-80,674,409 Size: 304,835 Total Exon Count: 17 Strand: +
Coding Region
   Position: hg38 chr7:80,646,741-80,674,147 Size: 27,407 Coding Exon Count: 12 

Page IndexSequence and LinksUniProtKB CommentsProtein StructureOther NamesMethods
Data last updated at UCSC: 2021-06-20 19:51:40

-  Sequence and Links to Tools and Databases
 
Genomic Sequence (chr7:80,369,575-80,674,409)mRNA (may differ from genome)Protein (472 aa)
Gene SorterGenome BrowserOther Species FASTATable SchemaExonPrimerGeneCards
HGNCMGIPubMedUniProtKB

+  Comments and Description Text from UniProtKB
  Press "+" in the title bar above to open this section.

-  Protein Domain and Structure Information
  InterPro Domains: Graphical view of domain structure
IPR002159 - CD36
IPR005428 - CD36_antigen

Pfam Domains:
PF01130 - CD36 family

ModBase Predicted Comparative 3D Structure on P16671
FrontTopSide
The pictures above may be empty if there is no ModBase structure for the protein. The ModBase structure frequently covers just a fragment of the protein. You may be asked to log onto ModBase the first time you click on the pictures. It is simplest after logging in to just click on the picture again to get to the specific info on that model.

+  Other Names for This Gene
  Press "+" in the title bar above to open this section.

+  Methods, Credits, and Use Restrictions
  Press "+" in the title bar above to open this section.