Top ▲
Gene and Protein Information  |
||||||
| Species | TM | AA | Chromosomal Location | Gene Symbol | Gene Name | Reference |
| Human | - | 335 | 15q25.1 | CTSH | cathepsin H | |
| Mouse | - | 333 | 9 47.4 cM | Ctsh | cathepsin H | |
| Rat | - | 333 | 8q31 | Ctsh | cathepsin H | |
| Previous and Unofficial Names |
| ACC-4 | ACC-5 | cathepsin B3 | cathepsin BA | CPSB |
| Database Links |
|
| Specialist databases | |
| MEROPS | C01.040 (Hs) |
| Other databases | |
| Alphafold | P09668 (Hs), P49935 (Mm), P00786 (Rn) |
| BRENDA | 3.4.22.16 |
| ChEMBL Target | CHEMBL2225 (Hs), CHEMBL1949491 (Mm), CHEMBL3308952 (Rn) |
| Ensembl Gene | ENSG00000103811 (Hs), ENSMUSG00000032359 (Mm), ENSRNOG00000014064 (Rn) |
| Entrez Gene | 1512 (Hs), 13036 (Mm), 25425 (Rn) |
| Human Protein Atlas | ENSG00000103811 (Hs) |
| KEGG Enzyme | 3.4.22.16 |
| KEGG Gene | hsa:1512 (Hs), mmu:13036 (Mm), rno:25425 (Rn) |
| OMIM | 116820 (Hs) |
| Orphanet | ORPHA371315 (Hs) |
| Pharos | P09668 (Hs) |
| RefSeq Nucleotide | NM_004390 (Hs), NM_007801 (Mm), NM_012939 (Rn) |
| RefSeq Protein | NP_004381 (Hs), NP_031827 (Mm), NP_037071 (Rn) |
| UniProtKB | P09668 (Hs), P49935 (Mm), P00786 (Rn) |
| Wikipedia | CTSH (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 |
| Cathepsin H may act as a pro-granzyme B convertase [2], granzyme B being the most potent proapoptotic cytotoxin of the granule exocytosis pathway of cytotoxic lymphocytes. It is similarly active in NK cells [4]. However, results from cathepsin H-null mice indicate a high degree of functional redundancy in granzyme B maturation, with enzymes other than cathepsin H active in this process. 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 | ||
|
||
|
||
|
||
|
||
|
||
|
| Clinically-Relevant Mutations and Pathophysiology
|
||||||||||||
|
||||||||||||
1. Adkison KK, Barrett DG, Deaton DN, Gampe RT, Hassell AM, Long ST, McFadyen RB, Miller AB, Miller LR, Payne JA et al.. (2006) Semicarbazone-based inhibitors of cathepsin K, are they prodrugs for aldehyde inhibitors?. Bioorg Med Chem Lett, 16 (4): 978-83. [PMID:16290936]
2. D'Angelo ME, Bird PI, Peters C, Reinheckel T, Trapani JA, Sutton VR. (2010) Cathepsin H is an additional convertase of pro-granzyme B. J Biol Chem, 285 (27): 20514-9. [PMID:20435891]
3. Garg S, Raghav N. (2016) 2,5-Diaryloxadiazoles and their precursors as novel inhibitors of cathepsins B, H and L. Bioorg Chem, 67: 64-74. [PMID:27285276]
4. Magister Š, Tseng HC, Bui VT, Kos J, Jewett A. (2015) Regulation of split anergy in natural killer cells by inhibition of cathepsins C and H and cystatin F. Oncotarget, 6 (26): 22310-27. [PMID:26247631]
C1: Papain: cathepsin H. Last modified on 21/04/2017. Accessed on 16/01/2025. IUPHAR/BPS Guide to PHARMACOLOGY, https://www.guidetopharmacology.org/GRAC/ObjectDisplayForward?objectId=2349.
target has curated data in GtoImmuPdb
