Abstract.The surface of the human red blood cell is dominated by a small number of abundant blood group active proteins. The major proteins are the anion transport protein (band 3) which has AB(H) activity, and Glycophorin A which has MN activity. Band 3 and Glycophorin A are of equal abundance in the normal red cell membrane (approximately 106copies of each) and the two proteins may associate together as a complex. The glucose transporter (band 4.5) has AB(H) activity and there are about 5 times 105copies/red cell. Several polypeptides associate together to form the Rh complex. The major components of this complex (abundance 1–2 times 105copies/red cell) are polypeptides of Mr30,000, polypeptides of Mr45,000–100,000 and Glycophorin B. The antigens of the Rh blood group system appear to be associated with the polypeptides of Mr30,000 and those of Mr45,000–100,000 (the latter also express AB(H) activity). Glycophorin B expresses the blood group ‘N’ antigen and the Ss antigens. Glycophorins C and D carry the Gerbich antigens and, together, these polypeptides comprise approximately 105copies/red cell. The complete protein sequence of all the above‐mentioned proteins is known, except for the Mr30,000 and Mr45,000–100,000 polypeptides of the Rh complex for which only partial sequences are available, and Glycophorin D, the sequence of which can be inferred from that of Glycophorin C. Several of the minor blood group active proteins at the red cell surface (abundance<1.2 times 104/red cell) have been the subject of recent studies. The polypeptide expressing Cromer‐related blood group antigens has been identified as decay‐accelerating factor and that carrying the Ina/Inbantigens as CD44. The protein sequence of both of these proteins has been deduced form nucleotide sequencing. The polypeptides expressing Kell antigens, Lutheran antigens, Fy antigens, and LW antigens have also been identified and partia