Target Information
| Target General Information | Top | |||||
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| Target ID |
T40785
(Former ID: TTDS00299)
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| Target Name |
Fungal Papulacandin B resistance protein 1 (Fung FKS1)
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| Synonyms |
UDP-glucose-1,3-beta-D-glucan glucosyltransferase; Papulacandin B sensitivity protein 1 of Saccharomyces cerevisiae; Glucan synthase; FKS1 protein of Saccharomyces cerevisiae; FKS1; CWN53 protein of Saccharomyces cerevisiae; CND1 protein of Saccharomyces cerevisiae; Beta-1,3-glucan synthetase; Beta-1,3-glucan synthase; 1,3-beta-D-glucan-UDP glucosyltransferase of Saccharomyces cerevisiae; (1,3)-beta-D-glucan synthase
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| Gene Name |
Fung FKS1
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| Target Type |
Clinical trial target
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[1] | ||||
| Disease | [+] 1 Target-related Diseases | + | ||||
| 1 | Fungal infection [ICD-11: 1F29-1F2F] | |||||
| Function |
Alternate catalytic subunit of the 1,3-beta-glucan synthase (GS). Synthesizes 1,3-beta-glucan, a major structural component of the yeast cell wall. Involved in cell wall synthesis, maintenance and cell wall remodeling.
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| BioChemical Class |
Hexosyltransferase
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| UniProt ID | ||||||
| EC Number |
EC 2.4.1.34
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| Sequence |
MNTDQQPYQGQTDYTQGPGNGQSQEQDYDQYGQPLYPSQADGYYDPNVAAGTEADMYGQQ
PPNESYDQDYTNGEYYGQPPNMAAQDGENFSDFSSYGPPGTPGYDSYGGQYTASQMSYGE PNSSGTSTPIYGNYDPNAIAMALPNEPYPAWTADSQSPVSIEQIEDIFIDLTNRLGFQRD SMRNMFDHFMVLLDSRSSRMSPDQALLSLHADYIGGDTANYKKWYFAAQLDMDDEIGFRN MSLGKLSRKARKAKKKNKKAMEEANPEDTEETLNKIEGDNSLEAADFRWKAKMNQLSPLE RVRHIALYLLCWGEANQVRFTAECLCFIYKCALDYLDSPLCQQRQEPMPEGDFLNRVITP IYHFIRNQVYEIVDGRFVKRERDHNKIVGYDDLNQLFWYPEGIAKIVLEDGTKLIELPLE ERYLRLGDVVWDDVFFKTYKETRTWLHLVTNFNRIWVMHISIFWMYFAYNSPTFYTHNYQ QLVDNQPLAAYKWASCALGGTVASLIQIVATLCEWSFVPRKWAGAQHLSRRFWFLCIIFG INLGPIIFVFAYDKDTVYSTAAHVVAAVMFFVAVATIIFFSIMPLGGLFTSYMKKSTRRY VASQTFTAAFAPLHGLDRWMSYLVWVTVFAAKYSESYYFLVLSLRDPIRILSTTAMRCTG EYWWGAVLCKVQPKIVLGLVIATDFILFFLDTYLWYIIVNTIFSVGKSFYLGISILTPWR NIFTRLPKRIYSKILATTDMEIKYKPKVLISQVWNAIIISMYREHLLAIDHVQKLLYHQV PSEIEGKRTLRAPTFFVSQDDNNFETEFFPRDSEAERRISFFAQSLSTPIPEPLPVDNMP TFTVLTPHYAERILLSLREIIREDDQFSRVTLLEYLKQLHPVEWECFVKDTKILAEETAA YEGNENEAEKEDALKSQIDDLPFYCIGFKSAAPEYTLRTRIWASLRSQTLYRTISGFMNY SRAIKLLYRVENPEIVQMFGGNAEGLERELEKMARRKFKFLVSMQRLAKFKPHELENAEF LLRAYPDLQIAYLDEEPPLTEGEEPRIYSALIDGHCEILDNGRRRPKFRVQLSGNPILGD GKSDNQNHALIFYRGEYIQLIDANQDNYLEECLKIRSVLAEFEELNVEQVNPYAPGLRYE EQTTNHPVAIVGAREYIFSENSGVLGDVAAGKEQTFGTLFARTLSQIGGKLHYGHPDFIN ATFMTTRGGVSKAQKGLHLNEDIYAGMNAMLRGGRIKHCEYYQCGKGRDLGFGTILNFTT KIGAGMGEQMLSREYYYLGTQLPVDRFLTFYYAHPGFHLNNLFIQLSLQMFMLTLVNLSS LAHESIMCIYDRNKPKTDVLVPIGCYNFQPAVDWVRRYTLSIFIVFWIAFVPIVVQELIE RGLWKATQRFFCHLLSLSPMFEVFAGQIYSSALLSDLAIGGARYISTGRGFATSRIPFSI LYSRFAGSAIYMGARSMLMLLFGTVAHWQAPLLWFWASLSSLIFAPFVFNPHQFAWEDFF LDYRDYIRWLSRGNNQYHRNSWIGYVRMSRARITGFKRKLVGDESEKAAGDASRAHRTNL IMAEIIPCAIYAAGCFIAFTFINAQTGVKTTDDDRVNSVLRIIICTLAPIAVNLGVLFFC MGMSCCSGPLFGMCCKKTGSVMAGIAHGVAVIVHIAFFIVMWVLESFNFVRMLIGVVTCI QCQRLIFHCMTALMLTREFKNDHANTAFWTGKWYGKGMGYMAWTQPSRELTAKVIELSEF AADFVLGHVILICQLPLIIIPKIDKFHSIMLFWLKPSRQIRPPIYSLKQTRLRKRMVKKY CSLYFLVLAIFAGCIIGPAVASAKIHKHIGDSLDGVVHNLFQPINTTNNDTGSQMSTYQS HYYTHTPSLKTWSTIK Click to Show/Hide
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| Drugs and Modes of Action | Top | |||||
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| Clinical Trial Drug(s) | [+] 1 Clinical Trial Drugs | + | ||||
| 1 | Eraxis/Vfend | Drug Info | Phase 3 | Fungal infection | [2] | |
| Discontinued Drug(s) | [+] 1 Discontinued Drugs | + | ||||
| 1 | Cilofungin | Drug Info | Terminated | Candidiasis | [3] | |
| Mode of Action | [+] 1 Modes of Action | + | ||||
| Inhibitor | [+] 5 Inhibitor drugs | + | ||||
| 1 | Eraxis/Vfend | Drug Info | [1], [4] | |||
| 2 | Cilofungin | Drug Info | [5], [6], [7] | |||
| 3 | ACULEACIN A | Drug Info | [8] | |||
| 4 | L-692289 | Drug Info | [9] | |||
| 5 | Pyridobenzimidazole | Drug Info | [10] | |||
| 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 Similarity Proteins
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| Protein Name | Pfam ID | Percentage of Identity (%) | E value |
|---|---|---|---|
| TATA-binding protein-associated factor 2N (TAF15) | 30.769 (32/104) | 4.00E-03 |
| Target Profiles in Patients | Top | |||||
|---|---|---|---|---|---|---|
| Drug Resistance Mutation (DRM) | ||||||
| Target Affiliated Biological Pathways | Top | |||||
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| KEGG Pathway | [+] 2 KEGG Pathways | + | ||||
| 1 | Starch and sucrose metabolism | |||||
| 2 | MAPK signaling pathway - yeast | |||||
| Target-Related Models and Studies | Top | |||||
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| Target Validation | ||||||
| References | Top | |||||
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| REF 1 | Pfizer. Product Development Pipeline. March 31 2009. | |||||
| REF 2 | Clinical pipeline report, company report or official report of Pfizer. | |||||
| REF 3 | Fungi: Biology and Applications, Kevin Kavanagh. Page(211). | |||||
| REF 4 | Eraxis. News for Eraxis. 2008. eduDrugs. | |||||
| REF 5 | Cryptococcus neoformans resistance to echinocandins: (1,3)beta-glucan synthase activity is sensitive to echinocandins. Antimicrob Agents Chemother. 2005 Jul;49(7):2851-6. | |||||
| REF 6 | Correlation of cilofungin in vivo efficacy with its activity against Aspergillus fumigatus (1,3)-beta-D-glucan synthase. FEMS Microbiol Lett. 1993 Apr 1;108(2):133-7. | |||||
| REF 7 | Characterization and cilofungin inhibition of solubilized Aspergillus fumigatus (1,3)-beta-D-glucan synthase. Antimicrob Agents Chemother. 1994 May;38(5):937-44. | |||||
| REF 8 | Synthesis, anti-fungal and 1,3--D-glucan synthase inhibitory activities of caffeic and quinic acid derivatives. Bioorg Med Chem. 2010 Oct 1;18(19):7009-14. | |||||
| REF 9 | Antifungal lipopeptides: Structure-activity relationships of 3-hydroxyglutamine-modified pneumocandin B0 derivatives, Bioorg. Med. Chem. Lett. 5(20):2357-2362 (1995). | |||||
| REF 10 | Novel antifungal agents, targets or therapeutic strategies for the treatment of invasive fungal diseases: a review of the literature (2005-2009). Rev Iberoam Micol. 2009 Mar 31;26(1):15-22. | |||||
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