Target Information
| Target General Information | Top | |||||
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| Target ID |
T00088
(Former ID: TTDR01119)
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| Target Name |
GPI transamidase component PIG-U (PIGU)
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| Synonyms |
UNQ3055/PRO9875; Phosphatidylinositol-glycan biosynthesis, class U protein; PIGU; PIG-U; Cell division cycle protein 91-like 1; CDC91L1; CDC91-like 1 protein
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| Gene Name |
PIGU
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| Target Type |
Literature-reported target
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[1] | ||||
| Function |
Component of the GPI transamidase complex. May be involved in the recognition of either the GPI attachment signal or the lipid portion of GPI.
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| UniProt ID | ||||||
| Sequence |
MAAPLVLVLVVAVTVRAALFRSSLAEFISERVEVVSPLSSWKRVVEGLSLLDLGVSPYSG
AVFHETPLIIYLFHFLIDYAELVFMITDALTAIALYFAIQDFNKVVFKKQKLLLELDQYA PDVAELIRTPMEMRYIPLKVALFYLLNPYTILSCVAKSTCAINNTLIAFFILTTIKGSAF LSAIFLALATYQSLYPLTLFVPGLLYLLQRQYIPVKMKSKAFWIFSWEYAMMYVGSLVVI ICLSFFLLSSWDFIPAVYGFILSVPDLTPNIGLFWYFFAEMFEHFSLFFVCVFQINVFFY TIPLAIKLKEHPIFFMFIQIAVIAIFKSYPTVGDVALYMAFFPVWNHLYRFLRNIFVLTC IIIVCSLLFPVLWHLWIYAGSANSNFFYAITLTFNVGQILLISDYFYAFLRREYYLTHGL YLTAKDGTEAMLVLK Click to Show/Hide
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| 3D Structure | Click to Show 3D Structure of This Target | AlphaFold | ||||
| 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: [2-[[(2~{R})-2-hexanoyloxy-3-[(~{E})-hex-3-enoxy]propoxy]-oxidanyl-phosphoryl]oxy-3,4,5,6-tetrakis(oxidanyl)phenyl] (2~{E},4~{E})-hepta-2,4-dienoate | Ligand Info | |||||
| Structure Description | Structure of a human glycosylphosphatidylinositol (GPI) transamidase | PDB:7W72 | ||||
| Method | Electron microscopy | Resolution | 3.10 Å | Mutation | No | [2] |
| PDB Sequence |
MAAPLVLVLV
10 VAVTVRAALF20 RSSLAEFISE30 RVEVVSPLSS40 WKRVVEGLSL50 LDLGVSPYSG 60 AVFHETPLII70 YLFHFLIDYA80 ELVFMITDAL90 TAIALYFAIQ100 DFNKVVFKKQ 110 KLLLELDQYA120 PDVAELIRTP130 MEMRYIPLKV140 ALFYLLNPYT150 ILSCVAKSTC 160 AINNTLIAFF170 ILTTIKGSAF180 LSAIFLALAT190 YQSLYPLTLF200 VPGLLYLLQR 210 QYIPVKMKSK220 AFWIFSWEYA230 MMYVGSLVVI240 ICLSFFLLSS250 WDFIPAVYGF 260 ILSVPDLTPN270 IGLFWYFFAE280 MFEHFSLFFV290 CVFQINVFFY300 TIPLAIKLKE 310 HPIFFMFIQI320 AVIAIFKSYP330 TVGDVALYMA340 FFPVWNHLYR350 FLRNIFVLTC 360 IIIVCSLLFP370 VLWHLWIYAG380 SANSNFFYAI390 TLTFNVGQIL400 LISDYFYAFL 410 RREYYLTHGL420
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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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| Glycosylphosphatidylinositol (GPI)-anchor biosynthesis | hsa00563 | Affiliated Target |
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| Class: Metabolism => Glycan biosynthesis and metabolism | Pathway Hierarchy | ||
| Degree | 5 | Degree centrality | 5.37E-04 | Betweenness centrality | 0.00E+00 |
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| Closeness centrality | 8.82E-02 | Radiality | 7.84E+00 | Clustering coefficient | 1.00E+00 |
| Neighborhood connectivity | 5.20E+00 | Topological coefficient | 8.67E-01 | Eccentricity | 16 |
| Download | Click to Download the Full PPI Network of This Target | ||||
| References | Top | |||||
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| REF 1 | CDC91L1 (PIG-U) is a newly discovered oncogene in human bladder cancer. Nat Med. 2004 Apr;10(4):374-81. | |||||
| REF 2 | Structure of human glycosylphosphatidylinositol transamidase. Nat Struct Mol Biol. 2022 Mar;29(3):203-209. | |||||
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