Target Information
| Target General Information | Top | |||||
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| Target ID |
T04303
(Former ID: TTDI03534)
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| Target Name |
TGF-beta-stimulated factor 1 (STK16)
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| Synonyms |
hPSK; Tyrosine-protein kinase STK16; TSF1; TSF-1; Serine/threonine-protein kinase 16; Protein kinase PKL12; PKL12; Myristoylated and palmitoylated serine/threonine-protein kinase; MPSK1; MPSK
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| Gene Name |
STK16
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| Target Type |
Literature-reported target
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[1] | ||||
| Function |
Membrane-associated protein kinase that phosphorylates on serine and threonine residues. In vitro substrates include DRG1, ENO1 and EIF4EBP1. Also autophosphorylates. May be involved in secretory vesicle trafficking or intracellular signaling. May have a role in regulating stromal-epithelial interactions that occur during ductal morphogenesis in the mammary gland. May be involved in TGF-beta signaling. Able to autophosphorylate on Tyr residue; it is however unclear whether it has tyrosine-protein kinase toward other proteins.
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| UniProt ID | ||||||
| EC Number |
EC 2.7.11.1
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| Sequence |
MGHALCVCSRGTVIIDNKRYLFIQKLGEGGFSYVDLVEGLHDGHFYALKRILCHEQQDRE
EAQREADMHRLFNHPNILRLVAYCLRERGAKHEAWLLLPFFKRGTLWNEIERLKDKGNFL TEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSMNQACIHVEGS RQALTLQDWAAQRCTISYRAPELFSVQSHCVIDERTDVWSLGCVLYAMMFGEGPYDMVFQ KGDSVALAVQNQLSIPQSPRHSSALRQLLNSMMTVDPHQRPHIPLLLSQLEALQPPAPGQ HTTQI 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: Staurosporine | Ligand Info | |||||
| Structure Description | Crystal structure of the human Serine-threonine Kinase 16 in complex with staurosporine | PDB:2BUJ | ||||
| Method | X-ray diffraction | Resolution | 2.60 Å | Mutation | Yes | [2] |
| PDB Sequence |
NLYFQGHMVI
14 IDNKHYLFIQ24 KLGEFSYVDL36 VEGLHDGHFY46 ALKRILCHEQ56 QDREEAQREA 66 DMHRLFNHPN76 ILRLVAYCLR86 ERGAKHEAWL96 LLPFFKRGTL106 WNEIERLKDK 116 GNFLTEDQIL126 WLLLGICRGL136 EAIHAKGYAH146 RDLKPTNILL156 GDEGQPVLMD 166 LGSMNQACIH176 VEGSRQALTL186 QDWAAQRCTI196 SYRAPELFSV206 QSHCVIDERT 216 DVWSLGCVLY226 AMMFGEGPYD236 MVFQKGDSVA246 LAVQNQIPQS258 PRHSSALWQL 268 LNSMMTVDPH278 QRPHIPLLLS288 QLEALQPPAP298 G
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LEU26
3.449
GLY27
3.856
GLU28
3.350
VAL34
3.622
ALA47
3.626
LYS49
3.966
CYS53
3.837
HIS54
3.867
GLU55
4.301
ARG59
3.869
LEU78
4.421
GLU87
3.120
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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 Similarity Proteins
Human Tissue Distribution
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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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| Chemical Structure based Activity Landscape of Target | Top |
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| References | Top | |||||
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| REF 1 | Fused bicyclic derivatives of 2,4-diaminopyrimidine as c-Met inhibitors. Bioorg Med Chem Lett. 2011 Jan 1;21(1):164-7. | |||||
| REF 2 | Crystal Structure of the Human Serine-Threonine Kinase 16 in Complex with Staurosporine | |||||
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