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Jaiswal R, Liu Y, Petriello M, Zhang X, Yi Z, Fehl C. A reference dataset of O-GlcNAc proteins in quadriceps skeletal muscle from mice. Glycobiology 2025 35(3) 39927985
Abstract:
A key nutrient sensing process in all animal tissues is the dynamic attachment of O-linked N-acetylglucosamine (O-GlcNAc). Determining the targets and roles of O-GlcNAc glycoproteins has the potential to reveal insights into healthy and diseased metabolic states. In cell studies, thousands of proteins are known to be O-GlcNAcylated, but reference datasets for most tissue types in animals are lacking. Here, we apply a chemoenzymatic labeling study to compile a high coverage dataset of quadriceps skeletal muscle O-GlcNAc glycoproteins from mice. Our dataset contains over 550 proteins, and > 80% of the dataset matched known O-GlcNAc proteins. This dataset was further annotated via bioinformatics, revealing the distribution, protein interactions, and gene ontology (GO) functions of these skeletal muscle proteins. We compared these quadriceps glycoproteins with a high-coverage O-GlcNAc enrichment profile from mouse hearts and describe the key overlap and differences between these tissue types. Quadriceps muscles can be used for biopsies, so we envision this dataset to have potential biomedical relevance in detecting aberrant glycoproteins in metabolic diseases and physiological studies. This new knowledge adds to the growing collection of tissues with high-coverage O-GlcNAc profiles, which we anticipate will further the systems biology of O-GlcNAc mechanisms, functions, and roles in disease.
O-GlcNAc proteins:
A0A087WS16, A0A0N4SUN5, A0A286YCS6, A0A5F8MPM4, A0A5F8MPQ4, A0A668KL51, A0A7N9VR94, A2A6J0, A2A6Q8, OBSCN, A2AEX6, A2AI87, A2AKD7, TITIN, KLH41, ARMT1, OSBL8, SHAN1, D3Z0V7, D3Z2B4, CD054, E0CZE0, E9PYG6, E9PYI8, E9PZD8, RYR1, E9Q1W3, NU153, E9Q3P4, RN213, E9Q616, TRDN, E9QL12, E9QN70, E9QND8, F6QYF8, F6VY18, F6YT88, F8VPN4, F8WGD9, MYH2, G3UYC5, RGS22, G3X972, AT2B1, G5E895, G5E8L1, G5E8R7, H7BWZ9, J3QN31, M0QW57, HXK2, CA2D1, PRDX6, DLDH, HCD2, MK12, SYPL1, CASQ1, PHB2, CAN1, CALU, CAVN1, IMPA1, NIPS2, AT2A2, PDLI3, PGAM2, PDLI1, RTN2, NTR1, WDR1, PLIN4, ZFR, SEM3F, ACTN3, SYPL2, CAH2, CO3, LAMC1, NU5M, ATP8, FABP4, MYG, ALDOA, KAPCA, AATC, AATM, TBA3, LDHA, MAOX, KCRM, ANXA2, A1AT1, SPA3K, HS90A, PHKG1, SODC, MDHM, ITB1, PDIA1, PGK1, MYL3, SODM, UBB, CALM3, ANXA1, EF1A1, CATB, TAU, GSTM1, H2B1F, H10, FINC, FABPH, DMD, COX5A, TNNI2, MYH3, MYH8, CAH1, GPDA, RL7, MDHC, HSPB1, ANXA6, GLNA, B4GT1, H12, CAH3, LEG1, LDHB, HS71L, G3P, ENOA, PPIA, TPIS, CATD, COF1, FAS, GSTP1, SERPH, COX5B, COX41, BIP, VIME, TNNC2, PLMN, ENOB, VTDB, CLK1, EST1C, RS2, TLN1, RADI, DHE3, FKB1A, MAP4, PLAP, PDIA3, ADHX, KCC2B, PGS2, MUG1, PABP1, DESM, AIMP1, PRVA, UBP4, ODPA, FAAA, PRDX1, RL12, HSPA9, CAP1, ACSL1, ECI1, STA5B, H14, H11, H15, H13, ALDR, COF2, ACADM, MYO1B, ALDH2, CAZA2, PFKAM, CACP, RL5, CBR1, ADT1, SAHH, CSRP3, ACADV, FMOD, ACADL, CAV3, ADT2, EAA3, AAAT, KPYM, CPT2, ODB2, MOT1, IDHP, STMN1, RD23B, PUR8, ADK, ACYP2, CX6B1, UBP5, ATPB, UCP3, EF2, TPM1, IRPL1, ACTB, CDC42, RAB5B, RAB10, UB2D1, 1433G, RS7, PP1B, 1433E, RS11, EF1A2, H4, RAB1A, RAN, RL23, CYC, RS3, YBOX1, RAC1, LIS1, HSP7C, CH60, 1433Z, HMGB1, IF5A1, ACTS, TBA4A, TBB4B, MP2K6, PEBP1, STIM1, HINT1, MYBPH, NACAM, TCPH, TCPB, TCPD, TCPE, TCPZ, SGCB, WNK1, ARF5, ISC2A, CSRP1, RS3A, SPSY, MYL11, FUMH, LYPA1, ARVC, PRDX5, XDH, NDKB, TERA, UBA1, CAC1S, ATPA, CO6A1, PGBM, PYC, ACADS, KCMA1, PADI2, CD36, Q14BI5, FAT4, CNNM3, Q3TCF3, PDLI7, PRC2C, SCRN3, DDB1, K0930, Q3UER8, LIMC1, PRRC1, EID3, AMPD1, Q561M1, MYPN, Q5F247, MLIP, Q5MJ56, CLU, MYH4, MYH1, UBR3, MYPC2, ODO1, LAMA2, COCA1, STIP1, REEP5, VDAC2, VDAC3, VDAC1, COQ8A, PRDX2, HCFC1, LAMB2, HSP74, HCDH, FBN1, GDIB, PZP, NNTM, DDX3X, MYOM1, SPEG, NDUA4, NUP62, AT2A3, GPDM, VINC, PUR2, CLH1, MYOF, HECD1, F120A, HELZ, Q6NVF7, IF4G1, Q6P1B9, Q6P6L5, KCRS, LPPRC, KMT2D, AT1A2, Q6S9I0, CAND1, CAND2, CMYA5, VWA2, TLN2, 2AAA, MIC27, Q7TPG0, MBB1A, SRCA, ATX2L, Q7TQS8, KPBB, Q80T54, NU214, PANK4, Q810Q0, EFTU, H2A3, LPP, PSD11, S2512, ECHM, EIF2A, ODPX, MAON, ODP2, ECHA, Q8BPI2, Q8BUY2, DHPR, SYP2L, THIM, STAC3, ASGL1, TLK1, PRR33, STBD1, MIC60, SYNPO, CPLN1, SYEP, UN45B, PGP, DRS7C, EI2BE, PDLI5, AGO3, EFGM, FIBB, COQ9, SDHA, VRK3, NNRE, HIBCH, THIL, AIMP2, BLMH, CMBL, UBQL1, TSN8, SLF1, CACB1, AT2A1, CLYBL, PRAF3, LSM1, MAVS, MYLK2, EST1D, MYH9, PSMD2, HNRL1, LMCD1, HNRPU, S25A3, FLNC, NDUS1, RINI, ATPG, DDX1, UBAP2, NDUS2, CISD1, SH319, HEMO, SYNP2, NDUV1, MYH7, PCCA, UGPA, ETFD, MACD1, C1TC, CLIP1, MPI, CPT1B, TALDO, THTM, GORS2, ECHB, ACON, NAMPT, 3HIDH, DHRS4, NDUAA, ETFA, PARK7, ASPN, MCCA, PPR3A, GDIR1, LGUL, NDUC2, DECR, NDUA2, SDHB, TMED6, GLRX3, AT5F1, ACO13, RL14, NDUB7, M2OM, UCRI, CHSP1, SFT2C, PUR9, SGT1, CENPV, SERB1, SPCS2, QCR1, NSF1C, CISY, ODPB, PGM1, SCOT1, GAL3A, RAB1B, ODO2, NDUV2, FUND2, IDH3A, RL4, EF1G, CA074, ATPO, PXL2B, QCR2, ACDSB, MYPT1, Q9DBT6, DCAF6, OCTC, NDUA9, NDUA8, PUR6, NDUBA, NDUS3, ETFB, ATP5H, MIC26, MMSA, RB27A, JPH2, JPH1, IVD, DYHC1, NIT2, ACTN2, MYOTI, PROF2, MYOZ1, PRELP, YBOX3, MBNL1, LDB3, HIG1A, TRXR1, B4GT5, PPCE, PLEC, S2513, NDRG2, DNJA2, UBQL2, FHL3, GLYG, ESTD, KAD1, PDC6I, PYGM, SUCA, ECI2, SH3BG, ARC1B, ABEC2, VAPA, AIFM1, GYS1, STRAP, LETM1, SUCB1, S4R1W1
Species: Mus musculus
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Deracinois B, Camoin L, Lambert M, Boyer JB, Dupont E, Bastide B, Cieniewski-Bernard C. O-GlcNAcylation site mapping by (azide-alkyne) click chemistry and mass spectrometry following intensive fractionation of skeletal muscle cells proteins. Journal of proteomics 2018 186 30016717
Abstract:
The O-linked-N-acetyl-d-glucosaminylation (O-GlcNAcylation) modulates numerous aspects of cellular processes. Akin to phosphorylation, O-GlcNAcylation is highly dynamic, reversible, and responds rapidly to extracellular demand. Despite the absolute necessity to determine post-translational sites to fully understand the role of O-GlcNAcylation, it remains a high challenge for the major reason that unmodified proteins are in excess comparing to the O-GlcNAcylated ones. Based on a click chemistry approach, O-GlcNAcylated proteins were labelled with azido-GalNAc and coupled to agarose beads. The proteome extracted from C2C12 myotubes was submitted to an intensive fractionation prior to azide-alkyne click chemistry. This combination of fractionation and click chemistry is a powerful methodology to map O-GlcNAc sites; indeed, 342 proteins were identified through the identification of 620 peptides containing one or more O-GlcNAc sites. We localized O-GlcNAc sites on proteins involved in signalling pathways or in protein modification, as well as structural proteins. Considering the recent role of O-GlcNAcylation in the modulation of sarcomere morphometry and interaction between key structural protein, we focused on proteins involved in the cytoarchitecture of skeletal muscle cells. In particular, several O-GlcNAc sites were located into protein-protein interaction domains, suggesting that O-GlcNAcylation could be strongly involved in the organization and reorganization of sarcomere and myofibrils.
Species: Mus musculus
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