Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

EOGT and O-GlcNAc on secreted and membrane proteins.

Biochemical Society transactions - 15 Apr 2017

Varshney Shweta, Stanley Pamela

Abstract excerpt

Here, we describe a recently discovered O-GlcNAc transferase termed EOGT for EGF domain-specific O-GlcNAc transferase. EOGT transfers GlcNAc (N-acetylglucosamine) to Ser or Thr in secreted and membrane proteins that contain one or more epidermal growth factor-like repeats with a specific consensus sequence. Thus, EOGT is distinct from OGT, the O-GlcNAc transferase, that transfers GlcNAc to Ser/Thr in proteins of...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Acetylglucosamine
Share to Drosophila melanogaster
Share to Drosophila Proteins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Ectodermal Dysplasia

Share to Limb Deformities, Congenital

Share to N-Acetylglucosaminyltransferases

Share to Protein Domains

Share to Substrate Specificity

Source

Open in PubMed Open full text

Identifiers

PMID: 28408480
DOI: 10.1042/BST20160165
PMCID: PMC8837192

Genes

EOGT
OGT
EGF

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 3 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

EOGT and O-GlcNAc on secreted and membrane proteins.PMID 28408480Read ↗

N-acetylglucosamine modification in the lumen of the endoplasmic reticulum.Semantic proximity Read ↗

Impaired O-linked N-acetylglucosaminylation in the endoplasmic reticulum by mutated epidermal growth factor (EGF) domain-specific O-linked N-acetylglucosamine transferase found in Adams-Oliver syndrome.Semantic proximity Read ↗

Autosomal recessive Adams-Oliver syndrome caused by homozygous mutation in EOGT, encoding an EGF domain-specific O-GlcNAc transferase.Semantic proximity Read ↗

Drosophila O-GlcNAcase Mutants Reveal an Expanded Glycoproteome and Novel Growth and Longevity Phenotypes.Semantic proximity Read ↗

Mutations in EOGT confirm the genetic heterogeneity of autosomal-recessive Adams-Oliver syndrome.Semantic proximity Read ↗

O-GlcNAc transferase congenital disorder of glycosylation (OGT-CDG): Potential mechanistic targets revealed by evaluating the OGT interactome.Semantic proximity Read ↗

Global mapping of GalNAc-T isoform-specificities and O-glycosylation site-occupancy in a tissue-forming human cell lineSemantic proximity Read ↗

The EGF repeat-specific O-GlcNAc-transferase Eogt interacts with notch signaling and pyrimidine metabolism pathways in Drosophila.Semantic proximity Read ↗

Substrate-directed control of N-glycosylation in the endoplasmic reticulum calibrates signal reception at the cell-surfaceSemantic proximity Read ↗

Polypeptide N-acetylgalactosaminyltransferase-Associated Phenotypes in Mammals.Semantic proximity Read ↗

Human OGA binds substrates in a conserved peptide recognition groove.Semantic proximity Read ↗

A mutant O-GlcNAcase as a probe to reveal global dynamics of protein O-GlcNAcylation during Drosophila embryonic development.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.