General Information of Drug Off-Target (DOT) (ID: OTONYLYO)

DOT Name Serine/threonine-protein kinase 32A (STK32A)
Synonyms EC 2.7.11.1; Yet another novel kinase 1
Gene Name STK32A
UniProt ID
ST32A_HUMAN
3D Structure
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2D Sequence (FASTA)
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3D Structure (PDB)
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PDB ID
4FR4
EC Number
2.7.11.1
Pfam ID
PF00069
Sequence
MGANTSRKPPVFDENEDVNFDHFEILRAIGKGSFGKVCIVQKNDTKKMYAMKYMNKQKCV
ERNEVRNVFKELQIMQGLEHPFLVNLWYSFQDEEDMFMVVDLLLGGDLRYHLQQNVHFKE
ETVKLFICELVMALDYLQNQRIIHRDMKPDNILLDEHGHVHITDFNIAAMLPRETQITTM
AGTKPYMAPEMFSSRKGAGYSFAVDWWSLGVTAYELLRGRRPYHIRSSTSSKEIVHTFET
TVVTYPSAWSQEMVSLLKKLLEPNPDQRFSQLSDVQNFPYMNDINWDAVFQKRLIPGFIP
NKGRLNCDPTFELEEMILESKPLHKKKKRLAKKEKDMRKCDSSQTCLLQEHLDSVQKEFI
IFNREKVNRDFNKRQPNLALEQTKDPQGEDGQNNNL

Molecular Interaction Atlas (MIA) of This DOT

Molecular Interaction Atlas (MIA) Jump to Detail Molecular Interaction Atlas of This DOT
11 Drug(s) Affected the Gene/Protein Processing of This DOT
Drug Name Drug ID Highest Status Interaction REF
Valproate DMCFE9I Approved Valproate decreases the expression of Serine/threonine-protein kinase 32A (STK32A). [1]
Ciclosporin DMAZJFX Approved Ciclosporin increases the expression of Serine/threonine-protein kinase 32A (STK32A). [2]
Acetaminophen DMUIE76 Approved Acetaminophen increases the expression of Serine/threonine-protein kinase 32A (STK32A). [3]
Vorinostat DMWMPD4 Approved Vorinostat decreases the expression of Serine/threonine-protein kinase 32A (STK32A). [4]
Zoledronate DMIXC7G Approved Zoledronate decreases the expression of Serine/threonine-protein kinase 32A (STK32A). [5]
Panobinostat DM58WKG Approved Panobinostat decreases the expression of Serine/threonine-protein kinase 32A (STK32A). [4]
Troglitazone DM3VFPD Approved Troglitazone increases the expression of Serine/threonine-protein kinase 32A (STK32A). [6]
SNDX-275 DMH7W9X Phase 3 SNDX-275 decreases the expression of Serine/threonine-protein kinase 32A (STK32A). [4]
Belinostat DM6OC53 Phase 2 Belinostat decreases the expression of Serine/threonine-protein kinase 32A (STK32A). [7]
THAPSIGARGIN DMDMQIE Preclinical THAPSIGARGIN decreases the expression of Serine/threonine-protein kinase 32A (STK32A). [9]
Trichostatin A DM9C8NX Investigative Trichostatin A decreases the expression of Serine/threonine-protein kinase 32A (STK32A). [10]
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⏷ Show the Full List of 11 Drug(s)
1 Drug(s) Affected the Post-Translational Modifications of This DOT
Drug Name Drug ID Highest Status Interaction REF
Benzo(a)pyrene DMN7J43 Phase 1 Benzo(a)pyrene increases the methylation of Serine/threonine-protein kinase 32A (STK32A). [8]
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References

1 Human embryonic stem cell-derived test systems for developmental neurotoxicity: a transcriptomics approach. Arch Toxicol. 2013 Jan;87(1):123-43.
2 Comparison of HepG2 and HepaRG by whole-genome gene expression analysis for the purpose of chemical hazard identification. Toxicol Sci. 2010 May;115(1):66-79.
3 Multiple microRNAs function as self-protective modules in acetaminophen-induced hepatotoxicity in humans. Arch Toxicol. 2018 Feb;92(2):845-858.
4 A transcriptome-based classifier to identify developmental toxicants by stem cell testing: design, validation and optimization for histone deacetylase inhibitors. Arch Toxicol. 2015 Sep;89(9):1599-618.
5 Interleukin-19 as a translational indicator of renal injury. Arch Toxicol. 2015 Jan;89(1):101-6.
6 Transcriptomic analysis of untreated and drug-treated differentiated HepaRG cells over a 2-week period. Toxicol In Vitro. 2015 Dec 25;30(1 Pt A):27-35.
7 Definition of transcriptome-based indices for quantitative characterization of chemically disturbed stem cell development: introduction of the STOP-Toxukn and STOP-Toxukk tests. Arch Toxicol. 2017 Feb;91(2):839-864.
8 Air pollution and DNA methylation alterations in lung cancer: A systematic and comparative study. Oncotarget. 2017 Jan 3;8(1):1369-1391. doi: 10.18632/oncotarget.13622.
9 The genome-wide expression profile of Scrophularia ningpoensis-treated thapsigargin-stimulated U-87MG cells. Neurotoxicology. 2009 May;30(3):368-76.
10 From transient transcriptome responses to disturbed neurodevelopment: role of histone acetylation and methylation as epigenetic switch between reversible and irreversible drug effects. Arch Toxicol. 2014 Jul;88(7):1451-68.