O-galnac - OmicsDI

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Unknown (373)
Proteomics (87)
Transcriptomics (26)
Genomics (12)
Metabolomics (4)
Genomic (1)

Organisms

Aerococcus urinae NBRC 15544 = CCUG 36881 (59)
Andropogon gerardi (59)
Bacteria (59)
Bartonella quintana JK 31 (59)
Burkholderia ubonensis MSMB22 (59)
Canis lupus familiaris (59)
Cnidaria (59)
Ectopseudomonas oleovorans CECT 5344 (59)
Ensifer adhaerens (59)
Halictus scabiosae (59)
Human immunodeficiency virus 1 (59)
Mesocricetus auratus (59)
Miscanthus x giganteus (59)
Morchella importuna (59)
Mus musculus (59)
Panicum virgatum (59)
Pseudomonas aeruginosa PA103 (59)
Pseudomonas aeruginosa SJTD-1 (59)
Rabies virus Nishigahara RCEH (59)
Rattus norvegicus (59)
Rattus rattus (59)
Rhodococcus jostii RHA1 (59)
Rhodopseudomonas palustris (59)
Sorghastrum nutans (59)
Homo sapiens (38)
Mus musculus (6)
Rattus rattus (2)
Rattus norvegicus (1)
Arabidopsis thaliana (1)
Fusarium sinicum (1)

Organisms

Homo sapiens (8)
Mus musculus (2)

Repository

pride (59)
biostudies-arrayexpress (24)
ENA (12)
geo (11)
jPOST (7)
MassIVE (7)
iProX (5)
MetabolomicsWorkbench (3)
dbGaP (1)
MetaboLights (1)

Tissue

Cell culture (17)
Epithelial cell (5)
Blood serum (3)
Brain (3)
Heart (3)
Keratinocyte (3)
Kidney (3)
Skin (3)
Brain (2)
Blood plasma (2)
Cerebrospinal fluid (2)
HeLa cell (2)
Lung (2)
Spleen (2)
Sublingual gland (2)
T cell (2)
Urine (2)
Whole body (2)
Feces (1)
Bone (1)
Breast cancer cell (1)
Colon (1)
Dendritic cell (1)
Hepatocyte (1)
Intestinal epithelium (1)
Islet of Langerhans (1)
Liver (1)
Pancreatic islet cell (1)
Salivary gland (1)
Submandibular gland (1)

Disease

Hyperphosphatemic familial tumoral calcinosis (3)
Colon cancer (2)
Irritable bowel syndrome (1)
Cancer (1)
Breast cancer (1)
Cervix carcinoma (1)
Congenital disorder of glycosylation (1)
Disease free (1)
Type 1 diabetes mellitus (1)
Urinary bladder cancer (1)

Technology Type

Mass Spectrometry (62)
Shotgun proteomics (30)
Bottom-up proteomics (21)
Data-dependent acquisition (9)
Gel-based experiment (4)
ESI (3)
Affinity purification coupled with mass spectrometry proteomics (3)
Data-independent acquisition (2)
Top-down proteomics (2)
Mass spectrometry assay (1)
All-ion fragmentation (1)
Glycoproteomics (1)

Instrument Platform

Q Exactive (2)
Illumina Truseq RNA Sample Preparation Kit (1)
Illumina HiSeq 2000 (1)
6230A Time-of-Flight LC/MS (1)
6545 Q-TOF LC/MS (1)
LTQ Orbitrap Elite (1)
LTQ Orbitrap Velos Pro (1)
Orbitrap Exploris 480 (1)
Orbitrap Fusion Lumos (1)
Synapt G2 HDMS (1)
ZenoTOF 7600 (1)
Liquid Chromatography MS - positive - reverse-phase (1)
Liquid Chromatography MS - negative - reverse-phase (1)

Publication Date

2025 (29)
2013 (9)
2023 (9)
2019 (9)
2022 (9)
2015 (6)
2026 (6)
2021 (6)
2024 (6)
2011 (3)
2010 (3)
2008 (3)
2020 (3)
2018 (3)
2014 (2)
2012 (1)
2009 (1)
2007 (1)
2017 (1)

Metabolite Name

6-{[2-(2,4-dihydroxyphenyl)-3-(3,7-dimethylocta-2,6-dien-1-yl)-5-hydroxy-6-(4-hydroxy-3-methylbut-2-en-1-yl)-4-oxo-4H-chromen-7-yl]oxy}-3,4,5-trihydroxyoxane-2-carboxylic acid (1)
2-amino-4-({1-[(carboxymethyl)-C-hydroxycarbonimidoyl]-2-({5,9-dihydroxy-8,8-dimethyl-2-oxo-4-phenyl-2H,8H,9H,10H-pyrano[2,3-h]chromen-10-yl}sulfanyl)ethyl}-C-hydroxycarbonimidoyl)butanoic acid (1)
3-phenyl-1-(2,3,4,6-tetrahydroxyphenyl)prop-2-en-1-one (1)
13-(acetyloxy)-5-hydroxy-9-oxo-8,17-dioxatetracyclo[8.7.0.0,.0,]heptadeca-1(10),2(7),3,5,11,13,15-heptaen-14-yl 2-hydroxyacetate (1)
Nicotinate beta-D-ribonucleotide (1)
Cis-4-Decenoic acid (1)
3,4,5-trihydroxy-6-{[8-(2-hydroxypropan-2-yl)-4-(1-hydroxypropyl)-2-oxo-2H,8H,9H-furo[2,3-h]chromen-5-yl]oxy}oxane-2-carboxylic acid (1)
Cyclic 3-Hydroxymelatonin (1)
4-hydroxy-2H,8H-[1,3]dioxolo[4,5-h]chromen-8-one (1)
4-ACETOXYPHENOL (1)
Alpha-Acetolactate decarboxylase (enzyme preparation from bacillus subtilis recombinant) (1)
3,4,5-trihydroxy-6-[1-(3-phenyloxiran-2-yl)ethoxy]oxane-2-carboxylic acid (1)
3,4,5-trihydroxy-6-{[3-(4-hydroxy-3-methoxyphenyl)-2-oxopropanoyl]oxy}oxane-2-carboxylic acid (1)
[3-(3-{[3,4-dihydroxy-5-(hydroxymethyl)oxolan-2-yl]oxy}-5,7-dihydroxy-4-oxo-3,4-dihydro-2H-1-benzopyran-2-yl)phenyl]oxidanesulfonic acid (1)
[(6-{[5,7-dihydroxy-2-(4-oxocyclohexa-2,5-dien-1-ylidene)-2H-chromen-3-yl]oxy}-3,4-dihydroxy-5-{[3,4,5-trihydroxy-6-(hydroxymethyl)oxan-2-yl]oxy}oxan-2-yl)methyl][1-hydroxy-3-(4-hydroxyphenyl)prop-2-en-1-ylidene]oxidanium (1)
9,10-dihydroxy-8,8-dimethyl-2H,8H,9H,10H-pyrano[2,3-h]chromen-2-one (1)
3,4,5-trihydroxy-6-({3-[(7-methoxy-2-oxo-2H-chromen-8-yl)methyl]-2-methyloxiran-2-yl}methoxy)oxane-2-carboxylic acid (1)
Dimoracin (1)
6-{4-[3-(3,5-dihydroxyphenyl)oxiran-2-yl]phenoxy}-3,4,5-trihydroxyoxane-2-carboxylic acid (1)
2-amino-4-({1-[(carboxymethyl)-C-hydroxycarbonimidoyl]-2-{[2-hydroxy-3-(4-methoxyphenyl)-3-oxo-1-phenylpropyl]sulfanyl}ethyl}-C-hydroxycarbonimidoyl)butanoic acid (1)
3-{[3,4-dihydroxy-5-(hydroxymethyl)oxolan-2-yl]oxy}-5,7-dihydroxy-2-(3-hydroxyphenyl)-3,4-dihydro-2H-1-benzopyran-4-one (1)
(4-methyl-2-oxochromen-7-yl) acetate (1)
FRAXETIN (1)
[2-hydroxy-5-(2-hydroxy-3-methoxy-3-oxopropyl)phenyl]oxidanesulfonic acid (1)
2',3',4'-Trihydroxyacetophenone (1)
Nicotinamide Adenine Dinucleotide Phosphate (NADP+) (1)
7-[(6-carboxy-3,4,5-trihydroxyoxan-2-yl)oxy]-1-oxo-1H-isochromene-3-carboxylic acid (1)
5'-Adenylyl sulfate (APS) (1)
5-[(E)-2-[6-hydroxy-3-(3-hydroxyphenyl)-2-phenyl-2,3-dihydro-1-benzofuran-5-yl]ethenyl]benzene-1,3-diol (1)
5-hydroxy-3,6,7-trimethoxy-2-(4-methoxyphenyl)chromen-4-one (1)

First Public Date

2025 (5)
2014 (3)
2019 (2)
2023 (1)
2015 (1)

Study type

Transcription profiling by array (14)
Proteomic profiling by array (9)
RNA-seq of coding RNA (1)

Release Date

2022 (34)
2020 (32)
2021 (28)
2023 (27)
2015 (25)
2018 (25)
2019 (24)
2013 (23)
2025 (21)
2016 (21)
2024 (19)
2011 (18)
2010 (18)
2017 (17)
2012 (15)
2014 (14)
2009 (10)
2008 (7)
2004 (4)
2007 (3)
2005 (3)
2002 (3)
2026 (2)
1999 (2)
2003 (1)
1989 (1)

Lab affiliation

Department of Microbiology and Immunology, University of Melbourne at the Peter Doherty Institute for infection and immunity, Melbourne, 3000, Australia (10)
Biological Chemistry Section, National Institute of Dental and Craniofacial Research, National Institutes of Health, Bethesda, Maryland, United States (3)
Department of Cellular and Molecular Medicine, University of Copenhagen (3)
Center for Proteomics and Metabolomics, Leiden University Medical Center, Leiden, The Netherlands (2)
College of Chemistry and Molecular Engineering, Peking University, Beijing, China. (2)
Copenhagen Center for Glycomics, Department of Cellular and Molecular Medicine, University of Copenhagen (2)
Copenhagen Center for Glycomics, University of Copenhagen (2)
Department of Pathology, Johns Hopkins University School of Medicine, Baltimore, Maryland, USA. (2)
1. School of Natural Sciences, Macquarie University, Sydney, NSW 2109, Australia 2. Institute for Glyco-core Research (iGCORE), Nagoya University, Nagoya, Japan (1)
Associate Professor Glyco MS Group Copenhagen Center for Glycomics (CCG) Department of Cellular and Molecular Medicine (24.6.36) University of Copenahgen Blegdamsvej 3 2200 Copenhagen N Denmark (1)
Associate Professor Glyco MS Group Copenhagen Center for Glycomics (CCG) Department of Cellular and Molecular Medicine University of Copenahgen Blegdamsvej 3 2200 Copenhagen N Denmark (1)
Associate Professor of Chemistry and Chemical Biology, DEPARTMENT of CHEMISTRY & CHEMICAL BIOLOGY, HARVARD UNIVERSITY (1)
Center for Proteomics and Metabolomics, LUMC, The Netherlands (1)
Centro de Investigaciones en Química Biológica de Córdoba, CIQUIBIC, CONICET, and Departamento de Química Biológica Ranwel Caputto, Facultad de Ciencias Químicas, Universidad Nacional de Córdoba, Ciudad Universitaria, X5000HUA Córdoba, Argentina (1)
Copenhagen Center for Glycomics (CCG), Department of Cellular and Molecular Medicine, University of Copenhagen, Denmark (1)
Copenhagen Center for Glycomics, Department of Cellular and Molecular Medicine, University of Copenhagen, Copenhagen, Denmark. (1)
Copenhagen Center for Glycomics, University of Copenhagen, Denmark (1)
Department of Biochemistry and Molecular Biology, Drexel University College of Medicine. Translational Cellular Oncology Program, Sidney Kimmel Cancer Center, Thomas Jefferson University (1)
Department of Laboratory Medicine, Institute of Biomedicine, Sahlgrenska Academy, University of Gothenburg, Gothenburg, Sweden. (1)
Department of Laboratory Medicine, Sahlgrenska academy, University of Gothenburg, Gothenburg, Sweden (1)
Department of Medical Biochemistry and Cell Biology, University of Gothenburg, Gothenburg, Sweden (1)
Department of Microbiology and Immunology, University of Michigan, 1150 W Medical Center Dr, 1526 MSRB1, Ann Arbor, MI, 48109. (1)
Department of Psychiatry, Oregon Health & Science University, Portland, OR (1)
Experimental Pathology and Therapeutics Group, IPO Porto Research Center (CI-IPOP), Portuguese Oncology Institute (IPO Porto), 4200-072 Porto, Portugal (1)
Faculty of Health and Medical Sciences Department of Cellular and Molecular Medicine University of Copenhagen (1)
Glyco MS Group Copenhagen Center for Glycomics (CCG) Department of Cellular and Molecular Medicine University of Copenhagen (1)
LMU Munich, Department of Chemistry (1)
NIH/NIDCR (1)
PKU (1)
Professor, Department of Clinical Chemistry and Transfusion Medicine, Sahlgrenska Academy at the University of Gothenburg, Gothenburg, Sweden (1)

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O-GalNAc–glycosylated nuclear proteins

Biological functions of nuclear proteins are regulated by post-translational modifications (PTMs) that modulate gene expression and cellular physiology. However, the role of O-linked glycosylation (O-GalNAc) as a PTM of nuclear proteins in the human cell has not been previously reported. Here, we ex...

ORGANISM(S): Homo sapiens (Human)

2019-04-17 | PXD013484 | Pride

Quantitative Mapping of the in vivo O-GalNAc Glycoproteome in Mouse Tissues

A large family of GalNAc transferases (GalNAc-Ts) catalyzes the covalent attachment of N-Acetylgalactosamine (GalNAc) to serine and threonine residues on proteins that pass through the secretory pathway in the first committed step of mucin-type O-glycosylation. Abnormalities in the activity of indi...

ORGANISM(S): Mus musculus (Mouse)

2024-05-24 | PXD040196 | Pride

O-galnac Site-specific Glycoproteome Mouse tissues

Deconstruction of O-glycosylation â€“ Polypeptide GalNAc-T Isoforms Direct Distinct Subsets of the O-Glycoproteome

GalNAc-transferase (GalNAc-T) isoforms modify distinct subsets of the O-glycoproteome and GalNAc-type O-glycosylation is found on most proteins trafficking through the secretory pathway in metazoan cells. The O-glycoproteome is regulated by up to 20 polypeptide GalNAc-Ts and the contributions and bi...

ORGANISM(S): Homo sapiens

2015-09-30 | E-MTAB-3844 | biostudies-arrayexpress

Deconstruction of O-glycosylation â€“ Polypeptide GalNAc-T Isoforms Direct Distinct Subsets of the O-Glycoproteome

PRJEB10772 | ENA

In vivo Mapping of the Mouse Galnt3-specific O-Glycoproteome

The polypeptide:N-acetylgalactosaminyltransferase (GalNAc-T) family of enzymes initiates O-linked glycosylation by catalyzing the addition of the first GalNAc sugar to serine or threonine on proteins destined to be membrane-bound or secreted. Defects in individual isoforms of the GalNAc-T family can...

ORGANISM(S): Mus musculus (Mouse)

2025-05-06 | PXD047517 | Pride

Galnac-t galnt glycopeptides glycosyltransferase hyperphosphatemic familial tumoral calcinosis (hftc) o-galnac o-glycosylation Mass spectrometry

Probing the contribution of individual polypeptide GalNAc-transferase isoforms to the O-glycoproteome by inducible expression in isogenic cell lines

The GalNAc-type O-glycoproteome is orchestrated by a large family of polypeptide GalNAc-transferase isoenzymes (GalNAc-Ts) with partially overlapping contributions to the O-glycoproteome as well as distinct non-redundant functions. Increasing evidence indicate that individual GalNAc-Ts co-regulate a...

ORGANISM(S): Homo sapiens (Human)

2018-10-16 | PXD010155 | Pride

Inducible expression Galnac-transferase O-glycosylation Glycoproteomics Mass spectrometry

Deconstruction of the GalNAc-Type O-Glycosylation Capacity of Human HEK293 Cells

Most proteins trafficking the secretory pathway of metazoan cells will acquire GalNAc-type O-glycosylation. GalNAc-type O-glycosylation is differentially regulated in cells by the expression of a repertoire of up to twenty genes encoding polypeptide GalNAc-transferase isoforms (GalNAc-Ts) that initi...

ORGANISM(S): Homo sapiens (Human)

2019-06-24 | PXD009955 | Pride

Simplecell Mass spectrometry Glycproteomics Etd Lc-ms

In vivo Mapping of the Mouse Galnt3-specific O-Glycoproteome

The UDP-N-acetylgalactosamine polypeptide:N-acetylgalactosaminyltransferase (GalNAc-T) family of enzymes initiates O-linked glycosylation by catalyzing the addition of the first GalNAc sugar to serine or threonine on proteins destined to be membrane-bound or secreted. Defects in individual isoforms ...

ORGANISM(S): Mus musculus (Mouse)

2025-05-07 | PXD053014 | Pride

Mass spectrometry Galnac-t galnt glycopeptides glycosyltransferase hyperphosphatemic familial tumoral calcinosis (hftc) o-galnac o-glycosylation

In vivo Mapping of the Mouse Galnt3-specific O-Glycoproteome

ORGANISM(S): Mus musculus (Mouse)

2025-05-07 | PXD052978 | Pride

Mass spectrometry Galnac-t galnt glycopeptides glycosyltransferase hyperphosphatemic familial tumoral calcinosis (hftc) o-galnac o-glycosylation

Deconstruction of protein O-glycosylation

ORGANISM(S): Homo sapiens (Human)

2015-08-21 | PXD002770 | Pride

Galnt/ dimethylation/ apolipoproteins/ mass spectrometry

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