# N-acetylglucosamine-1-phosphate transferase subunits alpha and beta

> mammalian protein found in Homo sapiens

**Wikidata**: [Q21104958](https://www.wikidata.org/wiki/Q21104958)  
**Wikipedia**: [English](https://en.wikipedia.org/wiki/N-acetylglucosamine-1-phosphate_transferase)  
**Source**: https://4ort.xyz/entity/n-acetylglucosamine-1-phosphate-transferase-subunits-alpha-and-beta


## References

1. UniProt
2. [InterPro Release 71.0](http://www.ebi.ac.uk/interpro/protein/Q3T906)
3. Q20641742
4. [GOA](http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:Q3T906)
5. [A proteome-scale map of the human interactome network](http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:Q3T906)
6. [Analysis of Mucolipidosis II/III GNPTAB Missense Mutations Identifies Domains of UDP-GlcNAc:lysosomal Enzyme GlcNAc-1-phosphotransferase Involved in Catalytic Function and Lysosomal Enzyme Recognition](http://www.ebi.ac.uk/QuickGO/annotations?protein=Q3T906&geneProductId=UniProtKB:Q3T906)
7. [GOA](http://www.ebi.ac.uk/QuickGO/annotations?protein=Q3T906&geneProductId=UniProtKB:Q3T906)
8. [Functions of the alpha, beta, and gamma subunits of UDP-GlcNAc:lysosomal enzyme N-acetylglucosamine-1-phosphotransferase](http://www.ebi.ac.uk/QuickGO/annotations?protein=Q3T906&geneProductId=UniProtKB:Q3T906)
9. [Analyses of disease-related GNPTAB mutations define a novel GlcNAc-1-phosphotransferase interaction domain and an alternative site-1 protease cleavage site](http://www.ebi.ac.uk/QuickGO/annotations?protein=Q3T906&geneProductId=UniProtKB:Q3T906)
10. [The DMAP interaction domain of UDP-GlcNAc:lysosomal enzyme N -acetylglucosamine-1-phosphotransferase is a substrate recognition module](http://www.ebi.ac.uk/QuickGO/annotations?protein=Q3T906&geneProductId=UniProtKB:Q3T906)
11. [Analysis of Mucolipidosis II/III GNPTAB Missense Mutations Identifies Domains of UDP-GlcNAc:lysosomal Enzyme GlcNAc-1-phosphotransferase Involved in Catalytic Function and Lysosomal Enzyme Recognition](http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:Q3T906)
12. [Functions of the alpha, beta, and gamma subunits of UDP-GlcNAc:lysosomal enzyme N-acetylglucosamine-1-phosphotransferase](http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:Q3T906)
13. [The DMAP interaction domain of UDP-GlcNAc:lysosomal enzyme N -acetylglucosamine-1-phosphotransferase is a substrate recognition module](http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:Q3T906)
14. [Analyses of disease-related GNPTAB mutations define a novel GlcNAc-1-phosphotransferase interaction domain and an alternative site-1 protease cleavage site](http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:Q3T906)
15. [Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium](http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:Q3T906)
16. [Mucolipidosis II-related mutations inhibit the exit from the endoplasmic reticulum and proteolytic cleavage of GlcNAc-1-phosphotransferase precursor protein (GNPTAB)](http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:Q3T906)
17. [A key enzyme in the biogenesis of lysosomes is a protease that regulates cholesterol metabolism](http://www.ebi.ac.uk/QuickGO/annotations?protein=Q3T906&geneProductId=UniProtKB:Q3T906)
18. [A key enzyme in the biogenesis of lysosomes is a protease that regulates cholesterol metabolism](http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:Q3T906)
19. [Molecular analysis of cell lines from patients with mucolipidosis II and mucolipidosis III](http://www.ebi.ac.uk/QuickGO/annotations?protein=Q3T906&geneProductId=UniProtKB:Q3T906)
20. [Molecular analysis of cell lines from patients with mucolipidosis II and mucolipidosis III](http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:Q3T906)
21. Ensembl Release 99