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Hao Y, Li Z, Du X, Xie Q, Li D, Lei S, Guo Y. Characterization and chemoproteomic profiling of protein O-GlcNAcylation in SOD1-G93A mouse model. Molecular medicine (Cambridge, Mass.) 2025 31(1) 40021952
Abstract:
Amyotrophic lateral sclerosis (ALS) is a devastating motor neuron disease. Protein O-linked β-N-acetylglucosamine (O-GlcNAc) modification has been found to affect the processing of several important proteins implicated in ALS. However, the overall level and cellular localization of O-GlcNAc during ALS progression are incompletely understood, and large-scale profiling of O-GlcNAcylation sites in this context remains unexplored.
O-GlcNAc proteins:
TANC2, ZEP3, MA7D2, AMRA1, AJM1, CNTRL, SKT, TITIN, ARI1A, S14L1, KI16B, TM245, RHG42, CTTB2, SAFB1, CCDC6, SHAN1, CE350, SYGP1, TPR, DPYL2, EMD, SYPL1, M3K5, PPE2, VIAAT, CTND2, LIMK2, ACK1, SYUA, ATX2, PDLI1, ZN106, DC1I1, PLIN4, ZFR, HCN2, BSN, SYN1, CO4B, MBP, ARAF, ALDOA, GCR, CATL1, NFL, NFM, RC3H2, NCAM1, HSPB1, MAP1B, G3P, NFH, VIME, MTAP2, MOV10, CRYAB, KCC2B, PABP1, AIMP1, KIF4, FOXK1, STAT3, EAA2, AINX, SOX2, LMNA, INPP, RORG, APC1, ATX1, PCBP3, KCNN2, GCP3, TB182, KCNH8, NPHP4, YTHD1, PI5PA, MRTFB, DOCK4, RUVB1, ABI2, RS3, KCNA2, ZHX1, TRAF5, SURF6, NCOA1, RGRF2, LYAG, IRS2, GBX1, TNIK, WNK1, CSRP1, G3BP2, RLA2, CTNB1, PLAK, S30BP, ENAH, EMAL1, CNN2, CDK12, MA6D1, M3K13, PSD3, PLBL2, PRC2C, MILK2, YETS2, PBIP1, TPPC9, FUBP2, WNK2, LIMC1, TNR6C, ZEP2, AAK1, TNR6A, CAMKV, MINY4, GRM5, ARMX5, N42L1, PACS2, ABL2, OXR1, UN13A, HERC2, PHAR4, SRRM1, TR150, LIN54, TAB3, ZBTB4, UNKL, RBM27, TM1L2, MYO1G, ANR40, SYNRG, NACAD, A1CF, LAMA2, PMEL, NCOR1, LAMA5, BCAR1, HCFC1, MRE11, PACN1, MAFK, MCM7, PTN14, SPTB2, TAF6, SRBS1, DBNL, SH3G1, TLE4, IF4G2, MINT, ZYX, OMGP, HECAM, NR2E1, SF01, SYN2, GPDM, PLK4, SBNO1, SLAI1, PKP4, SYMC, SAM9L, SH3R1, HECD1, ABLM3, ARMX2, CE170, CDC5L, LAR4B, RHG20, F135A, SPKAP, SR140, KIF24, RPRD2, WWC2, REXO4, PTN23, IQCE, TRAK1, RN220, ERC2, NFRKB, MAGI1, TEX2, PF21A, CNOT1, NU188, TRPV1, SC6A5, SMAP2, CPEB3, PLPR3, MYCB2, PRC2B, TPPP, ATX2L, CCNT2, MAP6, SI1L2, ERBIN, R3HD2, AUXI, RERE, SNPH, RIMB2, NU214, INT2, SDA1, EPN1, AGFG2, C2C2L, NRAP, DDHD1, BCAS1, ZN598, CTIP, SHAN2, MACA1, ANR26, MAST4, RHG32, LPP, MYPT2, IF4B, ZN750, WDR48, TB10B, CSTP1, SP130, ZC21A, ZNT6, SUN2, RCC2, ABLM2, HSP13, CLAP2, CNOT4, SRRM2, IKZF5, TOX4, GEPH, DIP2A, LARP4, IFFO1, OSBL6, YTHD3, POGZ, ZHX2, TT21A, SI1L1, RBM14, UBP44, CNOT2, HYCC2, ANK2, DIDO1, PARP9, SYNPO, VCIP1, MB214, TAB1, RPB2, ASPP2, F193A, NAV1, SYNJ1, RPGF2, EP400, PHC3, VP37A, EPN2, PDLI5, CSR2B, FBP1L, SCAM1, ZBT20, HS12A, AGFG1, MATR3, FANCI, PO121, MRTFA, MTSS1, SPART, PPR42, NUP58, RFIP5, BRD8, PP6R2, CS047, LUZP1, RBM12, SC6A8, MAVS, MICA1, SIR2, AMOT, AGAP3, P66B, CCG8, TAF9, WDR13, UBAP2, NCOA5, PEX16, DCP1A, YTHD2, BMP2K, DYST, LRP1, SYUB, ALS2, BICD2, CLIP1, S12A6, NRBP, RP25L, TAB2, DDAH2, HGS, TM2D1, SNCAP, ASH1L, ANR17, RTN4, RRBP1, NUDC2, TPPP3, FLIP1, DDAH1, DLGP1, FIP1, TM263, CNN3, AL7A1, PLIN3, MYPT1, NDUBA, CRIP2, TSC1, NBEA, INP4A, RIMS2, SO1C1, RBP2, MKRN2, RTN3, NUDT3, LGI1, TULP4, ADRM1, FMN2, GIT2, BAG3, ZN207, ASAP1, SON, TBL1X, PLEC, MACF1, NPHP1, VAPB, ADDA, GOGA5, MAP1A, QKI, PCLO, GAB1, FBX6, FOXO1, ADA23, AKA12, NCOR2, C8AP2, TNIP1, DEMA, E41L3, SYUG, ITSN2, ZO2, ADNP, NEK4, APCL, MTMR1, MECP2, E41L1
Species: Mus musculus
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Hou C, Zhang H, Deng J, Wang X, Byers S, Levi M, Pak DTS, Moremen KW, Pei H, Hart GW, Ma J. Comprehensive Evaluation of Cleavable Bioorthogonal Probes for Site-Specific O-GlcNAc Proteomics. Molecular & cellular proteomics : MCP 2025 24(10) 40885482
Abstract:
O-linked β-N-acetylglucosamine (O-GlcNAc) modification (i.e., O-GlcNAcylation) on proteins is an essential modification in physiology and pathology. Although O-GlcNAcylation is functionally critical, its analysis has been challenging. Despite the existence of a number of methods developed in the past years, which one(s) might have the best performance is largely unclear. To that end, we conducted a rigorous comparison of several cleavable bioorthogonal biotin-alkyne probes which showed promise for sensitive O-GlcNAc proteomics. In brief, we developed chemoenzymatic labeling/click chemistry-based analytical workflows for O-GlcNAc proteomics by utilizing four cleavable bioorthogonal probes, including photocleavabe-biotin-alkyne (PC-biotin-alkyne), dialkoxydiphenylsilane-biotin-alkyne (DADPS-biotin-alkyne); 1-(4,4-dimethyl-2,6-dioxocyclohex-1-ylidene)ethyl-biotin-alkyne (Dde-biotin-alkyne), and diazobenzene-biotin-alkyne (Diazo-biotin-alkyne). The analytical performance of these probes was evaluated with synthetic O-GlcNAc peptides and then benchmarked by using mouse brain lysates for O-GlcNAc proteomics. Besides providing valuable technical insights into O-GlcNAc proteomics methods, our work yielded an unprecedented O-GlcNAc proteome depth in the mouse brain. In total, 2906 O-GlcNAc sites were unambiguously assigned on 878 proteins. Among them, 1611 sites were newly identified, including 138 O-GlcNAcylated tyrosine residues. Our work will help guide the selection/development of O-GlcNAc proteomics methods for future studies, provide an invaluable resource for functional elucidation of protein O-GlcNAcylation in brain biology, and yield critical insights into tyrosine O-GlcNAcylation.
O-GlcNAc proteins:
QSER1, TANC2, ZEP3, MA7D2, CKAP5, AMRA1, CAMP1, LZTS3, AJM1, MA7D1, FRPD1, RPGP1, UBR4, SKT, BCORL, AGRIN, TITIN, SVEP1, ARI1A, SPAS1, PHRF1, PTPRS, SCN2A, DLGP4, EP300, RBM25, ILDR2, CTTB2, PTPRZ, NLRC5, CCDC6, SHAN1, SET1A, PARP4, PRR12, TENS1, I2BP2, AKP13, C2CD2, ARI1B, ZC3HD, ARID2, NUMA1, PDZD7, SC16A, SYGP1, TPR, BICRA, SI1L3, PLGT3, DPYL2, EMD, STXB1, AKAP1, CLOCK, DCTN1, NUMBL, DBIL5, SYPL1, M3K5, SCRB2, ATN1, NOTC2, VIAAT, HAP1, CTND2, PITM1, OX2G, REPS1, AKAP2, ACK1, CNTP1, CAC1B, SYUA, PI51C, ATX2, E41L2, PDLI1, ULK1, UBR1, HCN4, KDM6A, ZN106, PDE8A, PPT1, ZFR, HCN2, HCN1, CTBP1, BSN, TOM1, AKA10, HIPK1, SYN1, LGMN, TPP1, THY1, LAMC1, MBP, ALDOA, GCR, CATL1, EGR1, HCK, ENPL, KCC4, NFL, NFM, ITB1, RC3H2, MAMD1, ATX1L, CATB, TAU, LAMP1, DMD, KCC2A, ITPR1, CNTN1, NCAM1, AT1B2, HSPB1, MAP1B, G3P, ATF2, PPIA, CATD, BASI, COF1, NFH, BIP, HEXB, MTAP2, MAG, CYTC, EMB, GRIA1, GRIA2, RS2, RGRF1, KCC2B, PABP1, C5AR1, AIMP1, DPOA2, RAB23, NMDE1, NMDZ1, FMR1, FOXK1, STAT3, EAA2, EGR3, RAD52, ITAV, CBP, AINX, NEDD4, STT3A, RP3A, EPB41, RFX1, SOX2, LMNA, MPIP1, INPP, DHI1, ARSB, VATA, DVL1, ADCY7, DBX1, E41LA, ARNT, SOX1, ATX1, RD23B, 3BP1, AMRP, CX6B1, CTBP2, MAZ, WFS1, PCBP3, PTPA, KCNN2, FOXP1, TB10A, TB182, GMEB2, KCNH8, CAPAM, RHG39, YTHD1, RPC2, PI5PA, MRTFB, DOCK4, IRPL1, MYPR, ABI2, GBB1, RAB3A, VAMP2, KCNA2, KCNJ3, ZHX1, DCC, NFIX, NCOA1, RGRF2, USP9X, TP53B, NACAM, LYAG, IRS2, TNIK, WNK1, G3BP2, ARG28, MPRIP, CAC1A, NPAS2, GRM1, XRN1, SHPS1, NEO1, G3BP1, NFIB, RLA2, GABPA, CBPE, NMDE2, NMDE3, NOTC1, CTNB1, PLAK, S30BP, ZEP1, ENAH, KCNB1, RCN1, PGBM, EMAL1, LG3BP, TLE3, MITF, SSRP1, CHD8, TRIO, TANC1, RELCH, CDK12, MA6D1, F171B, SHRM4, PHAR1, GSK3A, PSD3, MLXIP, NELL1, ESP1, PLBL2, PDLI7, PRC2C, MILK2, YETS2, SRSF6, FUBP2, SRBP2, GSE1, F117B, WDR62, FOXK2, CARL3, DIP2B, WNK2, LIMC1, TNR6C, DAB2P, AGAP2, ZEP2, ZSWM8, AAK1, TEN4, TNR6A, CAMKV, MTCL1, PKHA7, COBL1, GRIN1, PRRC1, MINY4, FCHO2, SNX21, LIGO2, MRCKA, KSR2, GRM5, ARMX5, ELAP2, GARL3, 5NTC, PACS2, STOX2, UBN1, ABL2, OXR1, DSCL1, CDV3, PHAR4, ANR28, LRC47, SRRM1, EME2, LIN54, TAB3, STB5L, NEXMI, JCAD, NYNRI, NUFP2, UNKL, PRSR1, OSBP2, SMG7, LRRK2, RBM27, PHF12, CYFP2, TM1L2, ANR40, CCD42, SYNRG, RPGP2, NACAD, LHPL4, EPAB2, LMTK3, SIN3A, SRC8, ICAM5, LAMA2, ITF2, CAPR1, NCOR1, FOXG1, LAMA5, NCOA2, LAMC2, IL18R, NAB1, ASTN1, SPIN1, PAPOA, HCFC1, SAP, NELL2, APC, PGCB, ZN638, AP180, FXR1, GRID2, GRID1, PACN1, HIRA, RAI1, MAFK, NPM, NOTC3, CSPG2, M3K7, DAG1, RO52, SN, SPTB2, TAF6, SPEG, ASPP1, SRBS1, DBNL, SH3G1, TLE4, SP4, IF4G2, MINT, ZYX, OMGP, MEF2D, TFE3, PAN3, HECAM, SF01, SYN2, TBR1, DHSO, CGT, CH058, SBNO1, CRTC1, BEGIN, K1549, GIT1, SLAI1, PKP4, SYMC, CDK13, GBA2, SH3R1, PREX1, JHD2C, HECD1, MOR2A, ABLM3, TBC12, ARMX2, CE170, LAR4B, RHG21, HELZ, MEG10, SCAF8, LIGO3, ZZZ3, F135A, FBX41, SPKAP, RPRD2, WWC2, ZN532, DPP10, TAF9B, S23IP, IF4G1, RBM26, NSD3, SNX19, FHOD1, FKB15, MTSS2, BCR, AHDC1, AAKB2, PTN23, LPPRC, PAPD7, MFF, PIGS, TRAK1, PHLB1, KMT2D, RN220, DLGP3, RA54B, GMIP, WASC2, ERC2, KCC2D, NFRKB, ALEX, MAGI1, CENPE, DNMBP, GGYF2, TEX2, PF21A, KDM3B, FNBP4, CNOT1, LARP1, NU188, SYNE1, IF2A, UB2R2, CMYA5, SEM6D, SOX11, ASAP2, HUWE1, SMAP2, PLPR3, PRC2B, C2CD5, TPPP, MACOI, AMPH, ATX2L, PRC2A, TMM94, PP6R1, MAP6, MCAF1, DAAF9, SI1L2, LRRC7, ERBIN, PHF24, R3HD2, NAV3, AGRL1, DEND, AUXI, RERE, SNPH, MADD, RIMB2, PUM1, NU214, SEPT9, SESD1, CBPM, SRA1, EPN1, AKNA, HYDIN, UBN2, AGFG2, CHST2, T106B, C2C2L, REPS2, WNK3, DDHD1, CNKR2, BCAS1, ZN598, SHAN2, PKHL1, S2611, ZFYV1, NRCAM, DLG1, MAST4, RHG32, GPHB5, RN214, LPP, MYPT2, TB10B, CSTP1, SP130, ZC3HE, DLGP2, ZC21A, ZNT6, SUN2, EME1, TNR6B, BAIP2, ABLM2, NCEH1, LRFN3, SHC2, SEN34, FAT3, DMXL2, GORAB, CLAP2, K1671, FAKD3, LIPA2, CNOT4, RALYL, SRRM2, TOX4, PAMR1, F163B, GEPH, CREST, KCC1D, GRIN3, LARP4, Z385B, IFFO1, OSBL6, CC169, TENR, YTHD3, STON2, TM266, POGZ, DOC10, ZHX2, EPC2, SWAHC, ZHX3, SI1L1, SH3R3, FRS2, RBM14, CNOT2, MOR2B, HYCC2, ANK2, ELFN1, TM163, DIDO1, SMAG1, SYNPO, BCAS3, VCIP1, BAKOR, TAB1, SCYL2, NED4L, MEF2C, ASPP2, TENS2, F193A, OGT1, CHERP, NAV1, SYNJ1, RPGF2, EP400, PHC3, DPYD, VP37A, EPN2, P66A, PDLI5, ANM5, DOCK3, PLXB1, DNER, SPAT2, SCAM1, SAM14, ZBT20, PHYIP, RTN1, HS12A, C2D1A, UNC5A, PACS1, TRI68, BRD3, LS14A, AGFG1, MATR3, DEN1A, I2BPL, PO121, ABLM1, MRTFA, RPTOR, PLCE1, SPNS1, CACL1, KCNC4, DC1L1, MTSS1, SPART, LRC42, ZN445, RFIP5, IGSF8, BRD8, WIPI1, CDK8, PP6R2, SHLB2, CS047, NTNG2, PP14C, STAB2, LUZP1, RBM12, STAB1, OTU7A, SC6A8, ULA1, CLPT1, MAVS, GRAP1, SGIP1, PI3R4, PHIP, SIR2, GOLI, AMOT, AGAP3, WASF3, P66B, CCG8, TAF9, ZCH14, MCR, SFPQ, WDR13, UBAP2, SMAP1, NCOA5, CXXC5, FRS3, SPS2L, FUBP1, SH319, ZFN2B, VPS36, DLG2, DYH8, DCP1A, YTHD2, PTBP2, SRGP2, SRGP1, BMP2K, DYST, LRP1, SYUB, ALS2, TRFE, GPS2, CLIP1, WAC, SPRE1, MED1, NRBP, NPTXR, GGT7, GORS2, NONO, TAB2, DPP3, EPN4, RNF34, GAK, DDAH2, ZN281, HGS, RB6I2, RIMS1, ANR17, RTN4, RRBP1, ZN318, TRI33, MZT2, PCYOX, NECP1, FLIP1, NRX1A, SNX2, DDAH1, YIF1B, NOPC1, CYGB, GFOD2, TPD54, CEP97, CD37L, SSBP3, SARNP, SP2, UB2V2, DLGP1, NDUV2, SH24A, FIP1, ST1C2, F135B, TM263, CNPY3, RM12, BTBDH, AL7A1, PLIN3, MYPT1, LNEBL, DCAF6, KC1D, CRIP2, TSC1, NBEA, TCF20, CPSF1, DPYL5, RIMS2, ZN704, RBP2, RTN3, SPN90, SP6, GILT, CLD12, ELF2, TSSC4, LRP1B, NUDT3, CATR, PPR3F, NUP50, TULP4, ORC3, ATR, HYOU1, ADRM1, FMN2, NCOA6, BAG3, MINK1, ZN207, PHC2, SRCN1, ASAP1, SON, SALL2, LIMD1, TBL1X, APBB1, PLEC, MACF1, ULK2, ADDB, ADDA, PCX1, GOGA5, NDRG2, MAGD1, MAP1A, QKI, PCLO, GAB1, MAGL2, FBX6, NPAS3, HIPK2, SH2D3, CATJ, YLPM1, CELR2, RHG07, GUAD, FOXO1, TAGL3, ADA22, AKA12, TEN1, TEN3, NCOR2, ATRN, COR1B, SR5A3, GANP, NFAT5, ASAH1, GSK3B, DEMA, E41L3, CARM1, JIP1, KCNH3, MAGI2, FXR2, SYUG, CLIP2, PALM, ITSN1, ITSN2, ZO2, DYR1B, APCL, BAG6, DPP6, MTMR1, MECP2, SE1L1, E41L1, GRIA3, HOME1
Species: Mus musculus
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Burt RA, Dejanovic B, Peckham HJ, Lee KA, Li X, Ounadjela JR, Rao A, Malaker SA, Carr SA, Myers SA. Novel Antibodies for the Simple and Efficient Enrichment of Native O-GlcNAc Modified Peptides. Molecular & cellular proteomics : MCP 2021 20 34678516
Abstract:
Antibodies against posttranslational modifications (PTMs) such as lysine acetylation, ubiquitin remnants, or phosphotyrosine have resulted in significant advances in our understanding of the fundamental roles of these PTMs in biology. However, the roles of a number of PTMs remain largely unexplored due to the lack of robust enrichment reagents. The addition of N-acetylglucosamine to serine and threonine residues (O-GlcNAc) by the O-GlcNAc transferase (OGT) is a PTM implicated in numerous biological processes and disease states but with limited techniques for its study. Here, we evaluate a new mixture of anti-O-GlcNAc monoclonal antibodies for the immunoprecipitation of native O-GlcNAcylated peptides from cells and tissues. The anti-O-GlcNAc antibodies display good sensitivity and high specificity toward O-GlcNAc-modified peptides and do not recognize O-GalNAc or GlcNAc in extended glycans. Applying this antibody-based enrichment strategy to synaptosomes from mouse brain tissue samples, we identified over 1300 unique O-GlcNAc-modified peptides and over 1000 sites using just a fraction of sample preparation and instrument time required in other landmark investigations of O-GlcNAcylation. Our rapid and robust method greatly simplifies the analysis of O-GlcNAc signaling and will help to elucidate the role of this challenging PTM in health and disease.
O-GlcNAc proteins:
IQIP1, A0A0A6YWG7, A0A0G2JF55, A0A0N4SW93, A0A0R4J060, A0A0U1RPL0, A0A140LIW3, A0A140T8K9, A0A1B0GS41, A0A1B0GS91, A0A1D5RMI8, A0A1L1M1J8, A0A1L1SR84, A0A1N9NPH8, A0A1Y7VNZ6, A0A286YDB3, A0JNY3, A2A482, A2A654, TANC2, LZTS3, AJM1, BCORL, A2AUD5, A2AWN8, B1ASA5, B1ATC3, B1AUX2, B2RQL0, CSPP1, B2RY58, B7ZNA5, CTTB2, D3YU22, D3YUV1, D3YWX2, D3YZ21, SHAN1, D3Z5K8, E0CXZ9, E9PUL3, PRRT2, E9PUR0, E9PV26, E9PVY8, SET1A, E9Q0N0, E9Q3E2, NU153, E9Q4K0, ARI1B, SETD2, E9Q6H8, E9Q6L9, E9Q828, E9Q9C0, E9Q9Y4, E9QAQ7, E9QAU4, E9QAU9, E9QKI2, E9QLZ9, E9QM77, F2Z3U3, F6RQA2, SYGP1, F7C376, BICRA, F8VQL9, F8WIS9, G3UZM1, G3X8R8, G3X928, RFIP2, H3BKF3, H3BKP8, H9KV00, J3QNT7, DPYL2, PRDX6, MNT, NUMBL, PEX5, BMPR2, CTND2, PITM1, ACK1, CAC1B, SYUA, DSG2, SPT5H, E41L2, SP3, KDM6A, CPNS1, ZFR, HCN1, CTBP1, BSN, STAM2, SYN1, MBP, EGR1, NFL, NFM, ITB1, RC3H2, ATX1L, RL7A, MAP1B, VIME, EIF3A, RGRF1, PABP1, FOXK1, EAA2, CBP, RFX1, SOX2, KPYM, CTBP2, GCP3, TB182, GMEB2, PI5PA, DOCK4, PCBP1, LIPA3, RS3, PAX6, KCNJ3, PP2BA, TBA4A, STAM1, NCOA1, CXB6, WNK1, PSME2, WBP2, SHPS1, NRSN1, CTNB1, PLAK, S30BP, ZEP1, YES, CAPR2, MITF, GRD2I, Q0VF59, HDX, MA6D1, F171B, ZFHX2, MLXIP, PDLI7, PRC2C, CIART, YETS2, SRBP2, Q3U2K8, GSE1, RREB1, WNK2, DAB2P, ZEP2, AAK1, TNR6A, GRIN1, SRBS2, GRM5, Q3UZG4, RBM44, Q3ZB57, PHAR4, RESF1, Q5EBP8, UNKL, VP13A, COBL, KDM6B, PRSR1, Q5RIM6, SMG7, RBM27, TM1L2, Q5SVJ0, Q5SXC4, SIN3A, GAS7, CAPR1, KLF3, SIX4, AP180, GRID2, PACN1, LASP1, RAI1, NOTC3, SALL3, SPTB2, ARI3A, NUP62, PHC1, TFE3, PAN3, TIF1A, SF01, SYN2, SBNO1, CRTC1, RIPR1, GIT1, PKP4, ABLM3, ARMX2, CE170, Q6AXD2, NIPBL, FBX41, RPRD2, WWC2, Q6P1J1, Q6P5E3, UGGG1, SPRE3, Q6P9N8, AHDC1, PTN23, TRAK1, DLGP3, NYAP1, DHX29, NFRKB, MAGI1, Q6XZL8, CNOT1, SYNE2, IF2A, PLPR4, PLPR3, CCNT2, PRC2A, MAP6, MCAF1, RERE, NU214, SESD1, C2C2L, CNKR2, SLIK5, RHG32, LPP, NELFA, C42S2, TB10B, TGO1, RFOX3, SP130, ANS1B, ZC3HE, ZC21A, BAIP2, KAT6B, RELL2, LIPA2, CNOT4, TOX4, GASP2, CREST, KDM4A, GRIN3, KAT6A, ZN609, PAK5, A16L1, SI1L1, SH3R3, SKA3, RBM14, Q8C5J0, CNOT2, WDR26, UBA6, ANK2, DIDO1, SYNPO, VCIP1, FHI2A, NUP88, NED4L, SET1B, TENS2, OGT1, NAV1, STAU2, AFG32, S4A8, ZBT20, HS12A, GLT18, UNC5A, AGFG1, FRRS1, KCNQ3, PO121, T2FB, MTSS1, Q8R2E1, NUP35, MAVS, SGIP1, HNRL1, PP16B, CCG8, SFPQ, UBAP2, NCOA5, AJUBA, DCP1A, TWF1, ALS2, ETFD, GRIP1, GORS2, NONO, ZN281, CT2NL, RN111, ANR17, PPP6, RBM7, CYGB, SARNP, DLGP1, SUN1, TM263, GON4L, PLIN3, MYPT1, NBEA, ZN704, RBP2, ARHG7, RTN3, NUDT3, TULP4, Q9JIZ5, PAR6G, SCAM5, PRG4, ZN207, SRCN1, ASAP1, DREB, ULK2, ADDA, PCLO, UBQL2, FBX6, PCM1, SYT7, CRY2, FOXO1, MAST1, LYPA2, TEN3, GANP, DEMA, E41L3, ZO2, BAG6, E41L1, RM40, GRIA3, S4R294, V9GWU7, V9GX40
Species: Mus musculus
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Alfaro JF, Gong CX, Monroe ME, Aldrich JT, Clauss TR, Purvine SO, Wang Z, Camp DG 2nd, Shabanowitz J, Stanley P, Hart GW, Hunt DF, Yang F, Smith RD. Tandem mass spectrometry identifies many mouse brain O-GlcNAcylated proteins including EGF domain-specific O-GlcNAc transferase targets. Proceedings of the National Academy of Sciences of the United States of America 2012 109(19) 22517741
Abstract:
O-linked N-acetylglucosamine (O-GlcNAc) is a reversible posttranslational modification of Ser and Thr residues on cytosolic and nuclear proteins of higher eukaryotes catalyzed by O-GlcNAc transferase (OGT). O-GlcNAc has recently been found on Notch1 extracellular domain catalyzed by EGF domain-specific OGT. Aberrant O-GlcNAc modification of brain proteins has been linked to Alzheimer's disease (AD). However, understanding specific functions of O-GlcNAcylation in AD has been impeded by the difficulty in characterization of O-GlcNAc sites on proteins. In this study, we modified a chemical/enzymatic photochemical cleavage approach for enriching O-GlcNAcylated peptides in samples containing ∼100 μg of tryptic peptides from mouse cerebrocortical brain tissue. A total of 274 O-GlcNAcylated proteins were identified. Of these, 168 were not previously known to be modified by O-GlcNAc. Overall, 458 O-GlcNAc sites in 195 proteins were identified. Many of the modified residues are either known phosphorylation sites or located proximal to known phosphorylation sites. These findings support the proposed regulatory cross-talk between O-GlcNAcylation and phosphorylation. This study produced the most comprehensive O-GlcNAc proteome of mammalian brain tissue with both protein identification and O-GlcNAc site assignment. Interestingly, we observed O-β-GlcNAc on EGF-like repeats in the extracellular domains of five membrane proteins, expanding the evidence for extracellular O-GlcNAcylation by the EGF domain-specific OGT. We also report a GlcNAc-β-1,3-Fuc-α-1-O-Thr modification on the EGF-like repeat of the versican core protein, a proposed substrate of Fringe β-1,3-N-acetylglucosaminyltransferases.
O-GlcNAc proteins:
ZEP3, CAMP1, FRPD1, SKT, DLGP4, DPYL2, STXB1, MAP2, NUMBL, M3K5, NOTC2, CTND2, CSK22, ACK1, SYUA, ATX2, ZFR, BSN, GCR, EGR1, NFL, NFM, RC3H2, MAMD1, ATX1L, DERPC, NCAM1, MAP1B, G3P, ATF2, MAP4, KCC2B, AIMP1, FOXK1, STAT3, AINX, NEDD4, RP3A, DVL1, GOGA3, FOXP1, TB182, GMEB2, PI5PA, MRTFB, DOCK4, ABI2, KCNJ3, NCOA1, RGRF2, TNIK, WNK1, G3BP2, MPRIP, XRN1, RLA2, S30BP, MARK3, ENAH, PGBM, CDK12, MA6D1, PHAR1, PSD3, NELL1, PRC2C, YETS2, FOXK2, WNK2, LIMC1, TNR6C, AGAP2, ZEP2, AAK1, TNR6A, CAMKV, PKHA7, GRIN1, FCHO2, GARL3, STOX2, UBN1, ABL2, CDV3, PHAR4, TAB3, NUFP2, UNKL, OSBP2, RBM27, CYFP2, TM1L2, ANR40, NACAD, SIN3A, NCOR1, LAMA5, NCOA2, AP180, RAI1, M3K7, TAF6, SRBS1, SH3G1, TLE4, MINT, ZYX, SF01, SYN2, TBR1, SBNO1, CRTC1, GIT1, SLAI1, PKP4, CDK13, RHG23, SH3R1, JHD2C, HECD1, ABLM3, ARMX2, LAR4B, RHG21, FBX41, RPRD2, WWC2, ZN532, BCR, DLGP3, NYAP1, GMIP, NFRKB, MAGI1, CNOT1, NU188, SMAP2, SPAG7, PRC2B, ATX2L, MAP6, MCAF1, PHF24, NAV3, AUXI, RERE, RIMB2, PUM1, NU214, KCMF1, EPN1, AGFG2, C2C2L, CNKR2, ZN598, SHAN2, MAST4, RHG32, MYPT2, TB10B, FRM4A, SP130, DLGP2, ZNT6, ABLM2, CLAP2, CNOT4, PAMR1, CREST, IFFO1, OSBL6, YTHD3, TM266, SI1L1, SH3R3, RBM14, CNOT2, ANK2, DIDO1, SYNPO, VCIP1, TAB1, SCYL2, ASPP2, F193A, OGT1, NAV1, SYNJ1, RPGF2, EP400, P66A, PDLI5, SCAM1, HS12A, AGFG1, I2BPL, PO121, ABLM1, SPART, RFIP5, CS047, SIR2, AMOT, CCG8, ZCH14, WDR13, UBAP2, NCOA5, FRS3, ZFN2B, BASP1, DCP1A, SRGP2, SRGP1, SYUB, CLIP1, UBXN1, GORS2, EPN4, RB6I2, ANR17, TXD12, NECP1, DLGP1, FIP1, F135B, TM263, PLIN3, MYPT1, CRIP2, TSC1, NBEA, RIMS2, ZN704, RBP2, RTN3, 4ET, ELF2, NUDT3, FMN2, NCOA6, SRCN1, ASAP1, RAD1, SON, PLEC, ULK2, ADDA, PCLO, HIPK2, SH2D3, YLPM1, RHG07, TEN1, NCOR2, COR1B, TNIP1, DEMA, E41L3, SYUG, APCL, MECP2, E41L1
Species: Mus musculus
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Hahne H, Kuster B. Discovery of O-GlcNAc-6-phosphate modified proteins in large-scale phosphoproteomics data. Molecular & cellular proteomics : MCP 2012 11(10) 22826440
Abstract:
Phosphorylated O-GlcNAc is a novel post-translational modification that has so far only been found on the neuronal protein AP180 from the rat (Graham et al., J. Proteome Res. 2011, 10, 2725-2733). Upon collision induced dissociation, the modification generates a highly mass deficient fragment ion (m/z 284.0530) that can be used as a reporter for the identification of phosphorylated O-GlcNAc. Using a publically available mouse brain phosphoproteome data set, we employed our recently developed Oscore software to re-evaluate high resolution/high accuracy tandem mass spectra and discovered the modification on 23 peptides corresponding to 11 mouse proteins. The systematic analysis of 220 candidate phosphoGlcNAc tandem mass spectra as well as a synthetic standard enabled the dissection of the major phosphoGlcNAc fragmentation pathways, suggesting that the modification is O-GlcNAc-6-phosphate. We find that the classical O-GlcNAc modification often exists on the same peptides indicating that O-GlcNAc-6-phosphate may biosynthetically arise in two steps involving the O-GlcNAc transferase and a currently unknown kinase. Many of the identified proteins are involved in synaptic transmission and for Ca(2+)/calmodulin kinase IV, the O-GlcNAc-6-phosphate modification was found in the vicinity of two autophosphorylation sites required for full activation of the kinase suggesting a potential regulatory role for O-GlcNAc-6-phosphate. By re-analyzing mass spectrometric data from human embryonic and induced pluripotent stem cells, our study also identified Zinc finger protein 462 (ZNF462) as the first human O-GlcNAc-6-phosphate modified protein. Collectively, the data suggests that O-GlcNAc-6-phosphate is a general post-translation modification of mammalian proteins with a variety of possible cellular functions.
O-GlcNAc proteins:
A0JNY3, SHAN1, CTND2, BSN, SYN1, KCC4, RC3H2, NCAM1, AIMP1, MRTFB, SPRL1, WNK1, WNK2, TAB3, TM1L2, SIN3A, PGCB, AP180, TBR1, PKP4, ATX2L, SHAN2, SGIP1, ZN462, RB6I2, DLGP1, MYPT1, SON, ULK2, PCLO
Species: Mus musculus, Homo sapiens
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