Target Information
Target General Information | Top | |||||
---|---|---|---|---|---|---|
Target ID |
T12084
(Former ID: TTDI03514)
|
|||||
Target Name |
Retinoblastoma-binding protein 9 (RBBP9)
|
|||||
Synonyms |
Retinoblastoma-binding protein 10; RBBP10; RBBP-9; RBBP-10; Putative hydrolase RBBP9; Protein BOG; BOG; B5T-overexpressed gene protein
Click to Show/Hide
|
|||||
Gene Name |
RBBP9
|
|||||
Target Type |
Literature-reported target
|
[1] | ||||
Function |
May play a role in the transformation process due to its capacity to confer resistance to the growth-inhibitory effects of TGF-beta1 through interaction with retinoblastoma and the subsequent displacement of E2F-1.
Click to Show/Hide
|
|||||
UniProt ID | ||||||
EC Number |
EC 3.-.-.-
|
|||||
Sequence |
MASPSKAVIVPGNGGGDVTTHGWYGWVKKELEKIPGFQCLAKNMPDPITARESIWLPFME
TELHCDEKTIIIGHSSGAIAAMRYAETHRVYAIVLVSAYTSDLGDENERASGYFTRPWQW EKIKANCPYIVQFGSTDDPFLPWKEQQEVADRLETKLHKFTDCGHFQNTEFHELITVVKS LLKVPA Click to Show/Hide
|
|||||
3D Structure | Click to Show 3D Structure of This Target | PDB |
Cell-based Target Expression Variations | Top | |||||
---|---|---|---|---|---|---|
Cell-based Target Expression Variations |
Drug Binding Sites of Target | Top | |||||
---|---|---|---|---|---|---|
Ligand Name: L-phenylalanine | Ligand Info | |||||
Structure Description | Crystal structure of RBBP9 in complex with phenylalanine | PDB:7OEX | ||||
Method | X-ray diffraction | Resolution | 1.51 Å | Mutation | No | [2] |
PDB Sequence |
ASPSKAVIVP
11 GNGGGDVTTH21 GWYGWVKKEL31 EKIPGFQCLA41 KNMPDPITAR51 ESIWLPFMET 61 ELHCDEKTII71 IGHSSGAIAA81 MRYAETHRVY91 AIVLVSAYTS101 DLGDENERAS 111 GYFTRPWQWE121 KIKANCPYIV131 QFGSTDDPFL141 PWKEQQEVAD151 RLETKLHKFT 161 DCGHFQNTEF171 HELITVVKSL181 LKVPALEHHH191 HH
|
|||||
|
||||||
Click to View More Binding Site Information of This Target with Different Ligands |
Different Human System Profiles of Target | Top |
---|---|
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
|
There is no similarity protein (E value < 0.005) for this target
|
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.
|
Chemical Structure based Activity Landscape of Target | Top |
---|---|
References | Top | |||||
---|---|---|---|---|---|---|
REF 1 | A high-throughput, multiplexed assay for superfamily-wide profiling of enzyme activity. Nat Chem Biol. 2014 Aug;10(8):656-63. | |||||
REF 2 | Mechanism-based traps enable protease and hydrolase substrate discovery. Nature. 2022 Feb;602(7898):701-707. |
If You Find Any Error in Data or Bug in Web Service, Please Kindly Report It to Dr. Zhou and Dr. Zhang.