Target Information
| Target General Information | Top | |||||
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| Target ID |
T67812
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| Target Name |
Mannoside acetylglucosaminyltransferase 2 (MGAT2)
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| Synonyms |
N-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase II; GlcNAc-T II; GNT-II; Beta-1,2-N-acetylglucosaminyltransferase II; Alpha-1,6-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase
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| Gene Name |
MGAT2
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| Target Type |
Patented-recorded target
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[1] | ||||
| Function |
Catalyzes the transfer of N-acetylglucosamine (GlcNAc) onto the free terminal mannose moiety in the core structure of the nascent N-linked glycan chain, giving rise to the second branch in complex glycans. Plays an essential role in protein N-glycosylation.
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| BioChemical Class |
Glycosyltransferases
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| UniProt ID | ||||||
| EC Number |
EC 2.4.1.143
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| Sequence |
MRFRIYKRKVLILTLVVAACGFVLWSSNGRQRKNEALAPPLLDAEPARGAGGRGGDHPSV
AVGIRRVSNVSAASLVPAVPQPEADNLTLRYRSLVYQLNFDQTLRNVDKAGTWAPRELVL VVQVHNRPEYLRLLLDSLRKAQGIDNVLVIFSHDFWSTEINQLIAGVNFCPVLQVFFPFS IQLYPNEFPGSDPRDCPRDLPKNAALKLGCINAEYPDSFGHYREAKFSQTKHHWWWKLHF VWERVKILRDYAGLILFLEEDHYLAPDFYHVFKKMWKLKQQECPECDVLSLGTYSASRSF YGMADKVDVKTWKSTEHNMGLALTRNAYQKLIECTDTFCTYDDYNWDWTLQYLTVSCLPK FWKVLVPQIPRIFHAGDCGMHHKKTCRPSTQSAQIESLLNNNKQYMFPETLTISEKFTVV AISPPRKNGGWGDIRDHELCKSYRRLQ Click to Show/Hide
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| 3D Structure | Click to Show 3D Structure of This Target | PDB | ||||
| Cell-based Target Expression Variations | Top | |||||
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| Cell-based Target Expression Variations | ||||||
| Drug Binding Sites of Target | Top | |||||
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| Ligand Name: Uridine-5'-Diphosphate | Ligand Info | |||||
| Structure Description | Alpha-1,6-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase with bound UDP and Manganese | PDB:5VCM | ||||
| Method | X-ray diffraction | Resolution | 1.60 Å | Mutation | No | [2] |
| PDB Sequence |
NLTLRYRSLV
95 YQLNFDQTLR105 NVDWAPRELV119 LVVQVHNRPE129 YLRLLLDSLR139 KAQGIDNVLV 149 IFSHDFWSTE159 INQLIAGVNF169 CPVLQVFFPF179 SIQLYPNEFP189 GSDPRDCPRD 199 LPKNAALKLG209 CINAEYPDSF219 GHYREAKFSQ229 TKHHWWWKLH239 FVWERVKILR 249 DYAGLILFLE259 EDHYLAPDFY269 HVFKKMWKLK279 QQECPECDVL289 SLGTYSSRSF 300 YGMADKVDVK310 TWKSTEHNMG320 LALTRNAYQK330 LIECTDTFCT340 YDDYNWDWTL 350 QYLTVSCLPK360 FWKVLVPQIP370 RIFHAGDCGC386 RPSTQSAQIE396 SLLNNNKQYM 406 FPETLTISEK416 FTVVAISPPR426 KNGGWGDIRD436 HELCKSYRRL446 Q |
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| Click to View More Binding Site Information of This Target with Different Ligands | ||||||
| Different Human System Profiles of Target | Top |
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Human Similarity Proteins
of target is determined by comparing the sequence similarity of all human proteins with the target based on BLAST. The similarity proteins for a target are defined as the proteins with E-value < 0.005 and outside the protein families of the target.
A target that has fewer human similarity proteins outside its family is commonly regarded to possess a greater capacity to avoid undesired interactions and thus increase the possibility of finding successful drugs
(Brief Bioinform, 21: 649-662, 2020).
Human Tissue Distribution
of target is determined from a proteomics study that quantified more than 12,000 genes across 32 normal human tissues. Tissue Specificity (TS) score was used to define the enrichment of target across tissues.
The distribution of targets among different tissues or organs need to be taken into consideration when assessing the target druggability, as it is generally accepted that the wider the target distribution, the greater the concern over potential adverse effects
(Nat Rev Drug Discov, 20: 64-81, 2021).
Human Pathway Affiliation
of target is determined by the life-essential pathways provided on KEGG database. The target-affiliated pathways were defined based on the following two criteria (a) the pathways of the studied target should be life-essential for both healthy individuals and patients, and (b) the studied target should occupy an upstream position in the pathways and therefore had the ability to regulate biological function.
Targets involved in a fewer pathways have greater likelihood to be successfully developed, while those associated with more human pathways increase the chance of undesirable interferences with other human processes
(Pharmacol Rev, 58: 259-279, 2006).
Biological Network Descriptors
of target is determined based on a human protein-protein interactions (PPI) network consisting of 9,309 proteins and 52,713 PPIs, which were with a high confidence score of ≥ 0.95 collected from STRING database.
The network properties of targets based on protein-protein interactions (PPIs) have been widely adopted for the assessment of target’s druggability. Proteins with high node degree tend to have a high impact on network function through multiple interactions, while proteins with high betweenness centrality are regarded to be central for communication in interaction networks and regulate the flow of signaling information
(Front Pharmacol, 9, 1245, 2018;
Curr Opin Struct Biol. 44:134-142, 2017).
Human Similarity Proteins
Human Tissue Distribution
Human Pathway Affiliation
Biological Network Descriptors
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There is no similarity protein (E value < 0.005) for this target
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Note:
If a protein has TS (tissue specficity) scores at least in one tissue >= 2.5, this protein is called tissue-enriched (including tissue-enriched-but-not-specific and tissue-specific). In the plots, the vertical lines are at thresholds 2.5 and 4.
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| KEGG Pathway | Pathway ID | Affiliated Target | Pathway Map |
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| N-Glycan biosynthesis | hsa00510 | Affiliated Target |
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| Class: Metabolism => Glycan biosynthesis and metabolism | Pathway Hierarchy | ||
| Various types of N-glycan biosynthesis | hsa00513 | Affiliated Target |
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| Class: Metabolism => Glycan biosynthesis and metabolism | Pathway Hierarchy | ||
| Degree | 8 | Degree centrality | 8.59E-04 | Betweenness centrality | 3.01E-04 |
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| Closeness centrality | 1.30E-01 | Radiality | 1.11E+01 | Clustering coefficient | 3.21E-01 |
| Neighborhood connectivity | 5.13E+00 | Topological coefficient | 3.33E-01 | Eccentricity | 15 |
| Download | Click to Download the Full PPI Network of This Target | ||||
| Chemical Structure based Activity Landscape of Target | Top |
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| Target Poor or Non Binders | Top | |||||
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| Target Poor or Non Binders | ||||||
| Target Affiliated Biological Pathways | Top | |||||
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| KEGG Pathway | [+] 2 KEGG Pathways | + | ||||
| 1 | N-Glycan biosynthesis | |||||
| 2 | Metabolic pathways | |||||
| References | Top | |||||
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| REF 1 | Acyltransferase inhibitors: a patent review (2010-present).Expert Opin Ther Pat. 2015 Feb;25(2):145-58. | |||||
| REF 2 | Human N-acetylglucosaminyltransferase II substrate recognition uses a modular architecture that includes a convergent exosite. Proc Natl Acad Sci U S A. 2018 May 1;115(18):4637-4642. | |||||
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