P53954
Gene name |
ALG11 (YNL048W, N2510, YNL2510W) |
Protein name |
GDP-Man:Man(3)GlcNAc(2)-PP-Dol alpha-1,2-mannosyltransferase |
Names |
Alpha-1,2-mannosyltransferase ALG11, Asparagine-linked glycosylation protein 11, Glycolipid 2-alpha-mannosyltransferase |
Species |
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
KEGG Pathway |
sce:YNL048W |
EC number |
2.4.1.131: 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 P53954
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-P53954-F1 | Predicted | AlphaFoldDB |
8 variants for P53954
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| s14-538211 | 13 | V>G | No | SGRP | |
| s14-538250 | 26 | S>F | No | SGRP | |
| s14-538255 | 28 | V>L | No | SGRP | |
| s14-538316 | 48 | S>N | No | SGRP | |
| s14-538531 | 120 | V>I | No | SGRP | |
| s14-538565 | 131 | A>V | No | SGRP | |
| s14-539006 | 278 | T>M | No | SGRP | |
| s14-539026 | 285 | P>S | No | SGRP |
No associated diseases with P53954
Functions
| Description | ||
|---|---|---|
| EC Number | 2.4.1.131 | 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 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. |
| membrane | A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it. |
2 GO annotations of molecular function
| Name | Definition |
|---|---|
| alpha-1,2-mannosyltransferase activity | Catalysis of the transfer of a mannose residue to an oligosaccharide, forming an alpha-(1->2) linkage. |
| GDP-Man:Man3GlcNAc2-PP-Dol alpha-1,2-mannosyltransferase activity | Catalysis of the reaction: an alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-D-GlcNAc-diphosphodolichol + 2 GDP-alpha-D-mannose = an alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-D-GlcNAc-diphosphodolichol + 2 GDP + 2 H+. This reaction is the transfer of an alpha-D-mannosyl residue from GDP-mannose into lipid-linked oligosaccharide, forming an alpha-(1->2)-D-mannosyl-D-mannose linkage. |
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. |
3 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| Q9XEE9 | ALG11 | GDP-Man:Man(3)GlcNAc(2)-PP-Dol alpha-1,2-mannosyltransferase | Arabidopsis thaliana (Mouse-ear cress) | PR |
| Q6P312 | alg11 | GDP-Man:Man(3)GlcNAc(2)-PP-Dol alpha-1,2-mannosyltransferase | Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) | PR |
| Q7ZW24 | alg11 | GDP-Man:Man(3)GlcNAc(2)-PP-Dol alpha-1,2-mannosyltransferase | Danio rerio (Zebrafish) (Brachydanio rerio) | PR |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MGSAWTNYNF | EEVKSHFGFK | KYVVSSLVLV | YGLIKVLTWI | FRQWVYSSLN | PFSKKSSLLN |
| 70 | 80 | 90 | 100 | 110 | 120 |
| RAVASCGEKN | VKVFGFFHPY | CNAGGGGEKV | LWKAVDITLR | KDAKNVIVIY | SGDFVNGENV |
| 130 | 140 | 150 | 160 | 170 | 180 |
| TPENILNNVK | AKFDYDLDSD | RIFFISLKLR | YLVDSSTWKH | FTLIGQAIGS | MILAFESIIQ |
| 190 | 200 | 210 | 220 | 230 | 240 |
| CPPDIWIDTM | GYPFSYPIIA | RFLRRIPIVT | YTHYPIMSKD | MLNKLFKMPK | KGIKVYGKIL |
| 250 | 260 | 270 | 280 | 290 | 300 |
| YWKVFMLIYQ | SIGSKIDIVI | TNSTWTNNHI | KQIWQSNTCK | IIYPPCSTEK | LVDWKQKFGT |
| 310 | 320 | 330 | 340 | 350 | 360 |
| AKGERLNQAI | VLAQFRPEKR | HKLIIESFAT | FLKNLPDSVS | PIKLIMAGST | RSKQDENYVK |
| 370 | 380 | 390 | 400 | 410 | 420 |
| SLQDWSENVL | KIPKHLISFE | KNLPFDKIEI | LLNKSTFGVN | AMWNEHFGIA | VVEYMASGLI |
| 430 | 440 | 450 | 460 | 470 | 480 |
| PIVHASAGPL | LDIVTPWDAN | GNIGKAPPQW | ELQKKYFAKL | EDDGETTGFF | FKEPSDPDYN |
| 490 | 500 | 510 | 520 | 530 | 540 |
| TTKDPLRYPN | LSDLFLQITK | LDYDCLRVMG | ARNQQYSLYK | FSDLKFDKDW | ENFVLNPICK |
| LLEEEERG |