Protein　kinase　(CK2)　has　emerged　as　an　attractive　cancer　therapeutic　target　and　recent　efforts　have　been　made　to　develop　its　inhibitors.　However,　the　development　of　selective　inhibitors　remains　challenging　because　of　the　highly　conserved　ATP-binding　pocket　(orthosteric　site)　of　kinase　family.　As　an　alternative　strategy,　allosteric　inhibitors,　by　targeting　the　much　more　diversified　allosteric　site　relative　to　the　conserved　ATP-binding　site,　achieve　better　pharmacological　advantages　than　orthosteric　inhibitors.　Traditional　serendipitous　screening　and　structure-based　design　are　robust　tools　for　the　discovery　of　CK2　allosteric　inhibitors.　In　this　review,　we　summarize　the　recent　advances　in　the　identification　of　CK2　allosteric　inhibitors.　Firstly,　we　briefly　present　the　CK2　allosteric　sites.　Then,　the　allosteric　inhibitors　targeting　the　well-elucidated　allosteric　sites　(alpha/beta　interface,　alpha　D　pocket　and　interface　between　the　Glycine-rich　loop　and　alpha　C-helix)　are　highlighted　in　the　discovery　process　and　possible　binding　modes　with　the　allosteric　sites　are　described.　This　study　is　expected　to　provide　valuable　clues　for　the　design　of　CK2　allosteric　inhibitors.