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Gene and Protein Information ![]() |
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Species | TM | AA | Chromosomal Location | Gene Symbol | Gene Name | Reference |
Human | - | 333 | 9q21.33 | CTSL | cathepsin L | |
Mouse | - | 334 | 13 33.26 cM | Ctsl | cathepsin L |
Previous and Unofficial Names ![]() |
MEP | nackt | nkt | cathepsin L1 | fs | furless | Cat L | p39 cysteine proteinase |
Database Links ![]() |
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Specialist databases | |
MEROPS | C01.032 (Hs) |
Other databases | |
BRENDA | 3.4.22.15 |
ChEMBL Target | CHEMBL3837 (Hs), CHEMBL5291 (Mm) |
Ensembl Gene | ENSG00000135047 (Hs), ENSMUSG00000021477 (Mm) |
Entrez Gene | 1514 (Hs), 13039 (Mm) |
Human Protein Atlas | ENSG00000135047 (Hs) |
KEGG Enzyme | 3.4.22.15 |
KEGG Gene | hsa:1514 (Hs), mmu:13039 (Mm) |
OMIM | 116880 (Hs) |
Pharos | P07711 (Hs) |
RefSeq Nucleotide | NM_001912 (Hs), NM_145918 (Hs), NM_001257971 (Hs), NM_001257972 (Hs), NM_009984 (Mm) |
RefSeq Protein | NP_666023 (Hs), NP_001903 (Hs), NP_001244901 (Hs), NP_001244900 (Hs), NP_034114 (Mm) |
UniProtKB | P07711 (Hs), P06797 (Mm) |
Wikipedia | CTSL (Hs) |
Enzyme Reaction ![]() |
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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 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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View species-specific inhibitor tables |
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 | ||||||||||||
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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. Kumar GD, Chavarria GE, Charlton-Sevcik AK, Yoo GK, Song J, Strecker TE, Siim BG, Chaplin DJ, Trawick ML, Pinney KG. (2010) Functionalized benzophenone, thiophene, pyridine, and fluorene thiosemicarbazone derivatives as inhibitors of cathepsin L. Bioorg. Med. Chem. Lett., 20 (22): 6610-5. [PMID:20933415]
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. Takahashi K, Ueno T, Tanida I, Minematsu-Ikeguchi N, Murata M, Kominami E. (2009) Characterization of CAA0225, a novel inhibitor specific for cathepsin L, as a probe for autophagic proteolysis. Biol. Pharm. Bull., 32 (3): 475-9. [PMID:19252298]
C1: Papain: cathepsin L. Last modified on 20/04/2020. Accessed on 03/03/2021. IUPHAR/BPS Guide to PHARMACOLOGY, http://www.guidetoimmunopharmacology.org/GRAC/ObjectDisplayForward?objectId=2351.