Protein-polymer conjugates combine properties of biopolymers and synthetic polymers, such as specific bioactivity and increased stability, with great benefits for various applications from catalysis to biomedicine. Furthermore, polymer conjugation can mimic important posttranslational modifications of proteins such as glycosylation. There are typically two approaches to create protein-polymer conjugates: the protein is functionalized in advance with an initiator for a method or a previously produced polymer is conjugated to the protein a method. In this study, we present a new approach that uses native proteins and allows for direct using a thiol-induced, light-activated controlled radical polymerization (TIRP) that is initiated at thiols from specific cysteine residues of the protein. This straightforward method is employed to introduce polymers onto proteins and enzymes without any prior protein modifications, it works in aqueous buffer and maintains the protein's native structure and activity. The resulting protein-polymer conjugates exhibit high molar masses and low dispersities. We demonstrate the versatility of this approach by introducing different types of polymers such as hydrophilic poly(2-hydroxyethyl acrylate) (pHEAA), temperature-responsive poly(-isopropylacrylamide) (pNIPAM) as well as glycopolymers mimicking the natural protein glycosylation and enabling selective interactions. We present successful combinations of the protein and polymer functions , temperature-induced aggregation leading to an increase in enzyme activity and the introduction of artificial glycosylation inducing specific protein-protein cluster formation and giving straightforward access to glycosurfaces. Based on this straightforward, potentially scalable yet highly controlled synthesis of protein-polymer conjugates, various areas of applications are envisioned ranging from biomedicine to material sciences.