Gene Ontology annotation through association of InterPro records with GO terms

Manual transfer of experimentally-verified manual GO annotation data to orthologs by curator judgment of sequence similarity

Annotation inferences using phylogenetic trees

Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt

Gene Ontology annotation based on curation of immunofluorescence data

Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara

Electronic Gene Ontology annotations created by ARBA machine learning models

Combined Automated Annotation using Multiple IEA Methods

Association of EXT1 and EXT2, hereditary multiple exostoses gene products, in Golgi apparatus.

In vitro polymerization of heparan sulfate backbone by the EXT proteins.

Contribution of EXT1, EXT2, and EXTL3 to heparan sulfate chain elongation.

Heparan sulfate biosynthesis enzymes EXT1 and EXT2 affect NDST1 expression and heparan sulfate sulfation.

Proteomic analysis of human parotid gland exosomes by multidimensional protein identification technology (MudPIT).

Defining the membrane proteome of NK cells.

Dual proteome-scale networks reveal cell-specific remodeling of the human interactome.

A dominant negative splice variant of the heparan sulfate biosynthesis enzyme NDST1 reduces heparan sulfate sulfation.

Structure of the human heparan sulfate polymerase complex EXT1-EXT2.

Structural basis for heparan sulfate co-polymerase action by the EXT1-2 complex.

Multimodal cell maps as a foundation for structural and functional genomics.

Mutation screening of the EXT1 and EXT2 genes in patients with hereditary multiple exostoses.

EXT1:EXT2 transfers GlcNAc to the heparan chain

EXT1:EXT2 transfers GlcA to heparan

EXT1:EXT2 transfers GlcA to heparan

Defective EXT2 (in EXT1:EXT2) does not transfer GlcNAc to the heparan chain

Defective EXT1 (in EXT1:EXT2) does not transfer GlcA to heparan

Defective EXT1 (in EXT1:EXT2) does not transfer GlcNAc to the heparan chain

Defective EXT2 (in EXT1:EXT2) does not transfer GlcA to heparan

Defective EXT1 (in EXT1:EXT2) does not transfer GlcA to heparan

Defective EXT2 (in EXT1:EXT2) does not transfer GlcA to heparan

The putative tumor suppressors EXT1 and EXT2 form a stable complex that accumulates in the Golgi apparatus and catalyzes the synthesis of heparan sulfate.

The putative tumor suppressors EXT1 and EXT2 are glycosyltransferases required for the biosynthesis of heparan sulfate.

The EXT1/EXT2 tumor suppressors: catalytic activities and role in heparan sulfate biosynthesis.

EXT1-EXT2 heparan sulfate biosynthesis complex