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Subcellular localization database

JensenLab
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B4GAT1 localizations

B4GAT1 [ENSP00000309096]

Beta-1,4-glucuronyltransferase 1; Beta-1,4-glucuronyltransferase involved in O-mannosylation of alpha-dystroglycan (DAG1). Transfers a glucuronic acid (GlcA) residue onto a xylose (Xyl) acceptor to produce the glucuronyl-beta-1,4-xylose- beta disaccharide primer, which is further elongated by LARGE1, during synthesis of phosphorylated O-mannosyl glycan (PubMed:25279699, PubMed:25279697). Phosphorylated O-mannosyl glycan is a carbohydrate is a carbohydrate structure present in alpha-dystroglycan (DAG1), which is required for binding laminin G-like domain-containing extracellular proteins with high affinity . Required for axon guidance; via its function in O-mannosylation of alpha-dystroglycan (DAG1) (By similarity). ECO:0000269|PubMed:23359570, ECO:0000269|PubMed:25279697,

Synonyms:  B4GAT1,  B4GAT1p,  hB4GAT1,  A0A024R5F9,  B3GNT6 ...

Linkouts:  STRING  Pharos  UniProt

Extracellular space Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi Apparatus Nucleus Mitochondrion 0 1 2 3 4 5 Confidence

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The subcellular localizations are derived from database annotations, automatic text mining of the biomedical literature, and sequence-based predictions. The confidence of each association is signified by stars, where ★★★★★ is the highest confidence and ★☆☆☆☆ is the lowest.

Developed by Janos Binder, Sune Frankild, Kalliopi Tsafou, Christian Stolte, Sean O'Donoghue, Reinhard Schneider, and Lars Juhl Jensen from the Novo Nordisk Foundation Center for Protein Research (CPR), the Luxembourg Centre for Systems Biomedicine (LCSB), and the Commonwealth Scientific and Industrial Research Organisation (CSIRO).

Currently maintained by Qingyao Huang at Swiss Institute of Bioinformatics, University of Zurich. Licensed under CC BY 4.0.