Q11068
Gene name |
gly-13 (B0416.6) |
Protein name |
Putative alpha-1,3-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase |
Names |
N-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase I, GNT-I, GlcNAc-T I |
Species |
Caenorhabditis elegans |
KEGG Pathway |
cel:CELE_B0416.6 |
EC number |
2.4.1.101: 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 Q11068
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q11068-F1 | Predicted | AlphaFoldDB |
No variants for Q11068
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q11068 | |||||
No associated diseases with Q11068
No regional properties for Q11068
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| No domain, repeats, and functional sites for Q11068 | |||
Functions
| Description | ||
|---|---|---|
| EC Number | 2.4.1.101 | Hexosyltransferases |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
5 GO annotations of cellular component
| Name | Definition |
|---|---|
| Golgi apparatus | A membrane-bound cytoplasmic organelle of the endomembrane system that further processes the core oligosaccharides (e.g. N-glycans) added to proteins in the endoplasmic reticulum and packages them into membrane-bound vesicles. The Golgi apparatus operates at the intersection of the secretory, lysosomal, and endocytic pathways. |
| Golgi medial cisterna | The middle Golgi cisterna (or cisternae). |
| Golgi membrane | The lipid bilayer surrounding any of the compartments of the Golgi apparatus. |
| 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. |
| perinuclear region of cytoplasm | Cytoplasm situated near, or occurring around, the nucleus. |
2 GO annotations of molecular function
| Name | Definition |
|---|---|
| alpha-1,3-mannosylglycoprotein 2-beta-N-acetylglucosaminyltransferase activity | Catalysis of the reaction: 3-(alpha-D-mannosyl)-beta-D-mannosyl-R + UDP-N-acetyl-alpha-D-glucosamine = 3-(2--alpha-D-mannosyl)-beta-D-mannosyl-R + H(+) + UDP. |
| metal ion binding | Binding to a metal ion. |
2 GO annotations of biological process
| Name | Definition |
|---|---|
| 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 |
|---|---|---|---|---|
| P26572 | MGAT1 | Alpha-1,3-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase | Homo sapiens (Human) | PR |
| P27808 | Mgat1 | Alpha-1,3-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase | Mus musculus (Mouse) | PR |
| Q09325 | Mgat1 | Alpha-1,3-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase | Rattus norvegicus (Rat) | PR |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MHAVTKIFII | FIFVFILWTL | YVENDITNRT | RNTDNIDDLL | ESANRLERLL | KFEAKKIAAL |
| 70 | 80 | 90 | 100 | 110 | 120 |
| AEDVHKIRAN | RKGKHVIMEE | MVSQDLKQWK | DPIPVLVFSC | NRAMAVRDHV | EKLIRYRPSQ |
| 130 | 140 | 150 | 160 | 170 | 180 |
| EKFPIIVTQD | CDNENVKNEV | KKFGDKVEYI | KHLAGDKANI | TIPPSHRQYT | AYYRIARHYK |
| 190 | 200 | 210 | 220 | 230 | 240 |
| LALNHVFVDK | GYSSVIITED | DLDISPDFFS | YFSSTRYLLE | NDEKLWCVTA | WNDNGKQENI |
| 250 | 260 | 270 | 280 | 290 | 300 |
| DMTAASTLYR | SDFFAGLGWM | MSSKTWHELE | PIWPVGFWDD | WMRDPARRKD | RQCIRPEISR |
| 310 | 320 | 330 | 340 | 350 | 360 |
| TGMMSYGKEG | ASKGQFFSKH | LAKIKVNDKY | INFGKIDLDY | LLPANFAKKT | NLEVMKEAVE |
| 370 | 380 | 390 | 400 | 410 | 420 |
| LSIDNVASFV | LSSENKGKSV | RVMYDGNIDY | IRKADKLHIM | HDFKAGVPRT | AYDGIVTCFI |
| 430 | 440 | ||||
| NGIRIYLVPD | RTKVSAYNPD | WSVPPSFGE |