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EC Number Localization Commentary GeneOntology No. Reference
Show all pathways known for 2.4.1.142Display the word mapDisplay the reaction diagram Show all sequences 2.4.1.142endoplasmic reticulum - GO:0005783 AmiGO QuickGO 658848
Show all pathways known for 2.4.1.142Display the word mapDisplay the reaction diagram Show all sequences 2.4.1.142endoplasmic reticulum ER, the predicted transmembrane domain localizes the N-terminus of Alg1 into the ER lumen. The N-terminal transmembrane domain including the following positively charged amino acids and an N-terminal amphiphilic-like alpha-helix domain exposed on the protein surface strictly coordinate the Alg1 orientation on the ER membrane. The N- and C-termini of Alg1 are located to luminal and cytosolic side of the ER, respectively. The conserved proline 20 residue has no effect on its membrane-spanning property. The positively charged amino acids (K35, K38, K39 and R40) downstream of the N-terminal transmembrane region are important for ER membrane attachment GO:0005783 AmiGO QuickGO -, 759312
Show all pathways known for 2.4.1.142Display the word mapDisplay the reaction diagram Show all sequences 2.4.1.142membrane membrane topology of Alg1, overview. A conserved alpha-helix domain, Alg1 Nalpha3 domain, contributes to the membrane association of Alg1 protein GO:0016020 AmiGO QuickGO -, 759312
Show all pathways known for 2.4.1.142Display the word mapDisplay the reaction diagram Show all sequences 2.4.1.142microsome - - 636889, 636890, 722929
Show all pathways known for 2.4.1.142Display the word mapDisplay the reaction diagram Show all sequences 2.4.1.142rough endoplasmic reticulum membrane luminal side GO:0030867 AmiGO QuickGO 735995
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