Most proteins that coat the surface of the extracellular forms of the human malaria parasite Plasmodium falciparum are attached to the plasma membrane via glycosyl-phosphatidylinositol (GPI) anchors. These proteins are exposed to neutralizing antibodies and several are advanced vaccine candidates. To identify the GPI-anchored proteome of P. falciparum we used a combination of proteomic and computational approaches. Focussing on the clinically relevant blood-stage of the life cycle, proteomic analysis of proteins labelled with radioactive glucosamine identified GPI-anchoring on 11 proteins (merozoite surface protein (MSP)-1, -2, -4, -5, -10, RAMA, ASP, Pf92, Pf38, Pf12 and Pf34). These proteins represent ~94% of the GPI-anchored schizont/merozoite proteome and constitute by far the largest validated set of GPI-anchored proteins in this organism. Moreover, MSP-1 and MSP-2 are present in similar copy number and we estimate that together these proteins comprise approximately two thirds of the total membrane-associated surface coat. This is the first time the stoichiometry of MSPs has been examined. We observed that available software performed poorly in predicting GPI-anchoring on P. falciparum proteins where such modification had been validated by proteomics, Therefore, we developed a hidden Markov model (GPI-HMM) trained on P. falciparum sequences and used this to rank all proteins encoded in the completed P. falciparum genome according to their likelihood of being GPI-anchored. GPI-HMM predicted GPI-modification on all validated proteins, on several known membrane proteins, and on a number of novel, presumably surface, proteins expressed in the blood, insect and/or pre-erythrocytic stages of the life cycle. Together, this work identifies 11 and predicts a further 19 GPI-anchored proteins in P. falciparum.