Efficiently　tunable　capture　of　the　glycosylated/phosphorylated　proteins　is　critical　to　meet　the　need　of　in-depth　glycoproteome　and　phosphoproteome　studies.　Reported　here　is　a　new　bifunctional　polymer　monolithic　column　by　introducing　benzeneboronic　acid　and　phosphonic　acid　onto　monolithic　column　(denoted　as　poly　(EDMA-co-VPBA-co-VPA)　monolith)　for　tunable　and　specific　enrichment　of　glycoproteins　and　phosphoproteins　via　switching　different　mobile　phases.　Based　on　boronate　affinity　and　immobilized　metal　affinity,　the　as-prepared　poly　(EDMA-co-VPBA-co-VPA)　monolith　exhibited　superior　performance　in　selective　separation　of　small　molecules　and　biomacromolecules　containing　cis-diol/phosphate　groups　or　not.　And　the　frontal　chromatography　analysis　showed　that　the　binding　capacity　of　the　poly　(EDMA-coVPBA-co-VPA)　monolith　towards　horseradish　peroxidase　(HRP,　glycoprotein)　or　beta-casein　(phosphoprotein)　is　four-fold　higher　than　that　of　bovine　serum　albumin　(BSA,　non-glycosylated/phosphorylated　protein).　Furthermore,　combined　with　mass　spectrometry　identification,　the　successful　application　in　specific　enrichment　of　glycopeptides/phosphopeptides　from　tryptic　digests　of　HRP/beta-casein　and　direct　capture　of　low　abundant　endogenous　phosphopeptides　from　human　serum　proved　great　practicability　in　complex　samples.　This　study　provides　a　novel　insight　for　fabricating　the　monolithic　columns　with　multifunctionalization　to　facilitate　further　post-translational　modification　(PTM)-proteomics　development.　(C)　2021　Elsevier　B.V.　All　rights　reserved.