P16661
Gene name |
ALG1 (YBR110W, YBR0906) |
Protein name |
Chitobiosyldiphosphodolichol beta-mannosyltransferase |
Names |
Asparagine-linked glycosylation protein 1, Beta-1,4-mannosyltransferase, GDP-Man:GlcNAc2-PP-dolichol mannosyltransferase, GDP-mannose-dolichol diphosphochitobiose mannosyltransferase |
Species |
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
KEGG Pathway |
sce:YBR110W |
EC number |
2.4.1.142: Hexosyltransferases |
Protein Class |
|
Descriptions
The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.
Autoinhibitory domains (AIDs)
Target domain |
|
Relief mechanism |
|
Assay |
cis-regPred |
Accessory elements
No accessory elements
Autoinhibited structure
Activated structure
1 structures for P16661
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-P16661-F1 | Predicted | AlphaFoldDB |
6 variants for P16661
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| s02-459214 | 117 | V>F | No | SGRP | |
| s02-459530 | 222 | A>V | No | SGRP | |
| s02-459622 | 253 | N>D | No | SGRP | |
| s02-459656 | 264 | G>A | No | SGRP | |
| s02-459727 | 288 | K>E | No | SGRP | |
| s02-460196 | 444 | D>G | No | SGRP |
No associated diseases with P16661
1 regional properties for P16661
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Glycosyl transferase, family 1 | 257 - 427 | IPR001296 |
Functions
| Description | ||
|---|---|---|
| EC Number | 2.4.1.142 | Hexosyltransferases |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
3 GO annotations of cellular component
| Name | Definition |
|---|---|
| endoplasmic reticulum | The irregular network of unit membranes, visible only by electron microscopy, that occurs in the cytoplasm of many eukaryotic cells. The membranes form a complex meshwork of tubular channels, which are often expanded into slitlike cavities called cisternae. The ER takes two forms, rough (or granular), with ribosomes adhering to the outer surface, and smooth (with no ribosomes attached). |
| endoplasmic reticulum membrane | The lipid bilayer surrounding the endoplasmic reticulum. |
| integral component of membrane | The component of a membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane. |
3 GO annotations of molecular function
| Name | Definition |
|---|---|
| beta-1,4-mannosyltransferase activity | Catalysis of the transfer of a mannose residue to an oligosaccharide, forming a beta-(1->4) linkage. |
| chitobiosyldiphosphodolichol beta-mannosyltransferase activity | Catalysis of the reaction: GDP-mannose + chitobiosyldiphosphodolichol = GDP + beta-D-mannosylchitobiosyldiphosphodolichol. |
| mannosyltransferase activity | Catalysis of the transfer of a mannosyl group to an acceptor molecule, typically another carbohydrate or a lipid. |
3 GO annotations of biological process
| Name | Definition |
|---|---|
| oligosaccharide-lipid intermediate biosynthetic process | The chemical reactions and pathways resulting in the formation of an oligosaccharide-lipid intermediate, such as a molecule of dolichol-P-man or dolicol-P-Glc used in N-linked glycosylation. |
| protein glycosylation | A protein modification process that results in the addition of a carbohydrate or carbohydrate derivative unit to a protein amino acid, e.g. the addition of glycan chains to proteins. |
| protein N-linked glycosylation | A protein glycosylation process in which a carbohydrate or carbohydrate derivative unit is added to a protein via the N4 atom of peptidyl-asparagine, the omega-N of arginine, or the N1' atom peptidyl-tryptophan. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MFLEIPRWLL | ALIILYLSIP | LVVYYVIPYL | FYGNKSTKKR | IIIFVLGDVG | HSPRICYHAI |
| 70 | 80 | 90 | 100 | 110 | 120 |
| SFSKLGWQVE | LCGYVEDTLP | KIISSDPNIT | VHHMSNLKRK | GGGTSVIFMV | KKVLFQVLSI |
| 130 | 140 | 150 | 160 | 170 | 180 |
| FKLLWELRGS | DYILVQNPPS | IPILPIAVLY | KLTGCKLIID | WHNLAYSILQ | LKFKGNFYHP |
| 190 | 200 | 210 | 220 | 230 | 240 |
| LVLISYMVEM | IFSKFADYNL | TVTEAMRKYL | IQSFHLNPKR | CAVLYDRPAS | QFQPLAGDIS |
| 250 | 260 | 270 | 280 | 290 | 300 |
| RQKALTTKAF | IKNYIRDDFD | TEKGDKIIVT | STSFTPDEDI | GILLGALKIY | ENSYVKFDSS |
| 310 | 320 | 330 | 340 | 350 | 360 |
| LPKILCFITG | KGPLKEKYMK | QVEEYDWKRC | QIEFVWLSAE | DYPKLLQLCD | YGVSLHTSSS |
| 370 | 380 | 390 | 400 | 410 | 420 |
| GLDLPMKILD | MFGSGLPVIA | MNYPVLDELV | QHNVNGLKFV | DRRELHESLI | FAMKDADLYQ |
| 430 | 440 | ||||
| KLKKNVTQEA | ENRWQSNWER | TMRDLKLIH |