Top ▲
Gene and Protein Information  |
||||||
| Species | TM | AA | Chromosomal Location | Gene Symbol | Gene Name | Reference |
| Human | - | 339 | 8p23.1 | CTSB | cathepsin B | |
| Mouse | - | 339 | 14 D1 | Ctsb | cathepsin B | |
| Rat | - | 339 | 15p12 | Ctsb | cathepsin B | |
| Previous and Unofficial Names |
| cathepsin B1 | CB | RSG-2 |
| Database Links |
|
| Specialist databases | |
| MEROPS | C01.060 (Hs) |
| Other databases | |
| Alphafold | P07858 (Hs), P10605 (Mm), P00787 (Rn) |
| BRENDA | 3.4.22.1 |
| ChEMBL Target | CHEMBL4072 (Hs), CHEMBL5187 (Mm), CHEMBL2602 (Rn) |
| Ensembl Gene | ENSG00000164733 (Hs), ENSMUSG00000021939 (Mm), ENSRNOG00000010331 (Rn) |
| Entrez Gene | 1508 (Hs), 13030 (Mm), 64529 (Rn) |
| Human Protein Atlas | ENSG00000164733 (Hs) |
| KEGG Enzyme | 3.4.22.1 |
| KEGG Gene | hsa:1508 (Hs), mmu:13030 (Mm), rno:64529 (Rn) |
| OMIM | 116810 (Hs) |
| Pharos | P07858 (Hs) |
| RefSeq Nucleotide | NM_147783 (Hs), NM_147781 (Hs), NM_147782 (Hs), NM_001908 (Hs), NM_147780 (Hs), NM_007798 (Mm), NM_022597 (Rn) |
| RefSeq Protein | NP_680093 (Hs), NP_680092 (Hs), NP_680091 (Hs), NP_680090 (Hs), NP_001899 (Hs), NP_031824 (Mm), NP_072119 (Rn) |
| UniProtKB | P07858 (Hs), P10605 (Mm), P00787 (Rn) |
| Wikipedia | CTSB (Hs) |
| Enzyme Reaction |
||||
|
||||
Download all structure-activity data for this target as a CSV file 
| Inhibitors | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Key to terms and symbols | View all chemical structures | Click column headers to sort | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
|
|||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Immunopharmacology Comments |
| Cathepsins B, H and L have become important therapeutic targets as their proteolytic activity has been implicated in several pathological inflammatory conditions, such as arthritis and periodontitis. Therefore, pharmacological inhibitors of these enzymes are in development as novel therapeutics. |
| Immuno Process Associations | ||
|
||
|
||
|
||
|
||
|
1. Elie BT, Gocheva V, Shree T, Dalrymple SA, Holsinger LJ, Joyce JA. (2010) Identification and pre-clinical testing of a reversible cathepsin protease inhibitor reveals anti-tumor efficacy in a pancreatic cancer model. Biochimie, 92 (11): 1618-24. [PMID:20447439]
2. Mellott DM, Tseng CT, Drelich A, Fajtová P, Chenna BC, Kostomiris DH, Hsu J, Zhu J, Taylor ZW, Kocurek KI et al.. (2021) A Clinical-Stage Cysteine Protease Inhibitor blocks SARS-CoV-2 Infection of Human and Monkey Cells. ACS Chem Biol, 16 (4): 642-650. [PMID:33787221]
3. Méthot N, Rubin J, Guay D, Beaulieu C, Ethier D, Reddy TJ, Riendeau D, Percival MD. (2007) Inhibition of the activation of multiple serine proteases with a cathepsin C inhibitor requires sustained exposure to prevent pro-enzyme processing. J Biol Chem, 282 (29): 20836-46. [PMID:17535802]
4. Tsuda M, Muraoka Y, Nagai M, Aoyagi T, Takeuchi T. (1996) Poststatin, a new inhibitor of prolyl endopeptidase. V. Endopeptidase inhibitory activity of poststatin analogues. J Antibiot, 49 (9): 890-9. [PMID:8931723]
5. Wieczerzak E, Drabik P, Łankiewicz L, Ołdziej S, Grzonka Z, Abrahamson M, Grubb A, Brömme D. (2002) Azapeptides structurally based upon inhibitory sites of cystatins as potent and selective inhibitors of cysteine proteases. J Med Chem, 45 (19): 4202-11. [PMID:12213061]
C1: Papain: cathepsin B. Last modified on 20/04/2021. Accessed on 19/04/2024. IUPHAR/BPS Guide to PHARMACOLOGY, https://www.guidetopharmacology.org/GRAC/ObjectDisplayForward?objectId=2343.
target has curated data in GtoImmuPdb
