A lysosomal alpha-mannosidase that is encoded in the genome of human. [PRO:DNx, UniProtKB:O00754]
Laman;
EC 3.2.1.24;
Lysosomal acid alpha-mannosidase;
Mannosidase alpha class 2B member 1;
Mannosidase alpha-B
| Timeframe | Studies on this Protein(%) | All Drugs % |
|---|---|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 0 (0.00) | 18.2507 |
| 2000's | 1 (50.00) | 29.6817 |
| 2010's | 1 (50.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Drug | Taxonomy | Measurement | Average (mM) | Bioassay(s) | Publication(s) |
|---|---|---|---|---|---|
| swainsonine | Homo sapiens (human) | IC50 | 6.6867 | 3 | 3 |
| miglitol | Homo sapiens (human) | IC50 | 379.0000 | 1 | 1 |
This protein enables 3 target(s):
| Target | Category | Definition |
|---|---|---|
| carbohydrate binding | molecular function | Binding to a carbohydrate, which includes monosaccharides, oligosaccharides and polysaccharides as well as substances derived from monosaccharides by reduction of the carbonyl group (alditols), by oxidation of one or more hydroxy groups to afford the corresponding aldehydes, ketones, or carboxylic acids, or by replacement of one or more hydroxy group(s) by a hydrogen atom. Cyclitols are generally not regarded as carbohydrates. [GOC:mah] |
| metal ion binding | molecular function | Binding to a metal ion. [GOC:ai] |
| alpha-mannosidase activity | molecular function | Catalysis of the hydrolysis of terminal, non-reducing alpha-D-mannose residues in alpha-D-mannosides. [EC:3.2.1.24] |
This protein is located in 7 target(s):
| Target | Category | Definition |
|---|---|---|
| extracellular region | cellular component | The space external to the outermost structure of a cell. For cells without external protective or external encapsulating structures this refers to space outside of the plasma membrane. This term covers the host cell environment outside an intracellular parasite. [GOC:go_curators] |
| extracellular space | cellular component | That part of a multicellular organism outside the cells proper, usually taken to be outside the plasma membranes, and occupied by fluid. [ISBN:0198547684] |
| nucleoplasm | cellular component | That part of the nuclear content other than the chromosomes or the nucleolus. [GOC:ma, ISBN:0124325653] |
| azurophil granule lumen | cellular component | The volume enclosed by the membrane of an azurophil granule, a primary lysosomal granule found in neutrophil granulocytes that contains a wide range of hydrolytic enzymes and is released into the extracellular fluid. [GOC:bf, PMID:17152095] |
| lysosomal lumen | cellular component | The volume enclosed within the lysosomal membrane. [GOC:jl, PMID:15213228] |
| intracellular membrane-bounded organelle | cellular component | Organized structure of distinctive morphology and function, bounded by a single or double lipid bilayer membrane and occurring within the cell. Includes the nucleus, mitochondria, plastids, vacuoles, and vesicles. Excludes the plasma membrane. [GOC:go_curators] |
| extracellular exosome | cellular component | A vesicle that is released into the extracellular region by fusion of the limiting endosomal membrane of a multivesicular body with the plasma membrane. Extracellular exosomes, also simply called exosomes, have a diameter of about 40-100 nm. [GOC:BHF, GOC:mah, GOC:vesicles, PMID:15908444, PMID:17641064, PMID:19442504, PMID:19498381, PMID:22418571, PMID:24009894] |
This protein is active in 1 target(s):
| Target | Category | Definition |
|---|---|---|
| lysosome | cellular component | A small lytic vacuole that has cell cycle-independent morphology found in most animal cells and that contains a variety of hydrolases, most of which have their maximal activities in the pH range 5-6. The contained enzymes display latency if properly isolated. About 40 different lysosomal hydrolases are known and lysosomes have a great variety of morphologies and functions. [GOC:mah, ISBN:0198506732] |
This protein is involved in 5 target(s):
| Target | Category | Definition |
|---|---|---|
| mannose metabolic process | biological process | The chemical reactions and pathways involving mannose, the aldohexose manno-hexose, the C-2 epimer of glucose. The D-(+)-form is widely distributed in mannans and hemicelluloses and is of major importance in the core oligosaccharide of N-linked oligosaccharides of glycoproteins. [ISBN:0198506732] |
| protein deglycosylation | biological process | The removal of sugar residues from a glycosylated protein. [GOC:mah] |
| learning or memory | biological process | The acquisition and processing of information and/or the storage and retrieval of this information over time. [GOC:jid, PMID:8938125] |
| oligosaccharide catabolic process | biological process | The chemical reactions and pathways resulting in the breakdown of oligosaccharides, molecules with between two and (about) 20 monosaccharide residues connected by glycosidic linkages. [ISBN:0198506732] |
| protein modification process | biological process | The covalent alteration of one or more amino acids occurring in proteins, peptides and nascent polypeptides (co-translational, post-translational modifications). Includes the modification of charged tRNAs that are destined to occur in a protein (pre-translation modification). [GOC:bf, GOC:jl] |