Cathepsin B information

CTSB
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	3PBH, 1CSB, 1GMY, 1HUC, 1PBH, 2IPP, 2PBH, 3AI8, 3CBJ, 3CBK, 3K9M
Identifiers
Aliases	CTSB, APPS, CPSB, cathepsin B, RECEUP
External IDs	OMIM: 116810; MGI: 88561; HomoloGene: 37550; GeneCards: CTSB; OMA:CTSB - orthologs
Gene location (Human)
Chr.	Chromosome 8 (human)
End	11,869,448 bp
Gene location (Mouse)
Chr.	Chromosome 14 (mouse)
End	63,383,372 bp
RNA expression pattern
	Top expressed in
	stromal cell of endometrium; ; right lobe of thyroid gland; ; left lobe of thyroid gland; ; appendix; ; canal of the cervix; ; gallbladder; ; smooth muscle tissue; ; monocyte; ; upper lobe of left lung; ; right lung;
	Top expressed in
	calvaria; ; white adipose tissue; ; subcutaneous adipose tissue; ; epithelium of stomach; ; brown adipose tissue; ; carotid body; ; mucous cell of stomach; ; iris; ; uterus; ; spleen;
	More reference expression data
	; ; ; ;
	More reference expression data
Gene ontology
Molecular function	cysteine-type peptidase activity; collagen binding; peptidase activity; protein binding; cysteine-type endopeptidase activity; hydrolase activity; proteoglycan binding; serine-type endopeptidase activity; endopeptidase activity;
Cellular component	intracellular membrane-bounded organelle; melanosome; intracellular anatomical structure; extracellular region; endolysosome lumen; nucleolus; mitochondrion; lysosome; extracellular exosome; perinuclear region of cytoplasm; extracellular space; ficolin-1-rich granule lumen; collagen-containing extracellular matrix;
Biological process	regulation of apoptotic process; epithelial cell differentiation; proteolysis; toll-like receptor signaling pathway; decidualization; cellular response to thyroid hormone stimulus; collagen catabolic process; viral entry into host cell; regulation of catalytic activity; proteolysis involved in cellular protein catabolic process; neutrophil degranulation;
	Sources:Amigo / QuickGO
Orthologs
	1508
	13030
	ENSG00000164733; ENSG00000285132
	ENSMUSG00000021939
	P07858
	P10605
NM_001908; NM_147780; NM_147781; NM_147782; NM_147783;
	NM_001317237
	NM_007798
NP_001304166; NP_001899; NP_680090; NP_680091; NP_680092;
	NP_680093
	NP_031824
	Wikidata
View/Edit Human	View/Edit Mouse

Cathepsin B belongs to a family of lysosomal cysteine proteases known as the cysteine cathepsins and plays an important role in intracellular proteolysis.^[5] In humans, cathepsin B is encoded by the CTSB gene.^[6]^[7] Cathepsin B is upregulated in certain cancers, in pre-malignant lesions, and in various other pathological conditions.^[8]^[9]^[10]^[11]

^ ^a ^b ^c ENSG00000285132 GRCh38: Ensembl release 89: ENSG00000164733, ENSG00000285132 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000021939 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ Sloane BF (April 1990). "Cathepsin B and cystatins: evidence for a role in cancer progression". Seminars in Cancer Biology. 1 (2): 137–52. PMID 2103490.
^ Chan SJ, San Segundo B, McCormick MB, Steiner DF (October 1986). "Nucleotide and predicted amino acid sequences of cloned human and mouse preprocathepsin B cDNAs". Proceedings of the National Academy of Sciences of the United States of America. 83 (20): 7721–5. Bibcode:1986PNAS...83.7721C. doi:10.1073/pnas.83.20.7721. PMC 386793. PMID 3463996.
^ Cao L, Taggart RT, Berquin IM, Moin K, Fong D, Sloane BF (February 1994). "Human gastric adenocarcinoma cathepsin B: isolation and sequencing of full-length cDNAs and polymorphisms of the gene". Gene. 139 (2): 163–9. doi:10.1016/0378-1119(94)90750-1. PMID 8112600.
^ Tong B, Wan B, Wei Z, Wang T, Zhao P, Dou Y, Lv Z, Xia Y, Dai Y (September 2014). "Role of cathepsin B in regulating migration and invasion of fibroblast-like synoviocytes into inflamed tissue from patients with rheumatoid arthritis". Clinical and Experimental Immunology. 177 (3): 586–97. doi:10.1111/cei.12357. PMC 4137842. PMID 24749816.
^ Lai WF, Chang CH, Tang Y, Bronson R, Tung CH (March 2004). "Early diagnosis of osteoarthritis using cathepsin B sensitive near-infrared fluorescent probes". Osteoarthritis and Cartilage. 12 (3): 239–44. doi:10.1016/j.joca.2003.11.005. PMID 14972341.
^ Ha SD, Ham B, Mogridge J, Saftig P, Lin S, Kim SO (January 2010). "Cathepsin B-mediated autophagy flux facilitates the anthrax toxin receptor 2-mediated delivery of anthrax lethal factor into the cytoplasm". The Journal of Biological Chemistry. 285 (3): 2120–9. doi:10.1074/jbc.M109.065813. PMC 2804368. PMID 19858192.
^ Yang WE, Ho CC, Yang SF, Lin SH, Yeh KT, Lin CW, Chen MK (2016). "Cathepsin B Expression and the Correlation with Clinical Aspects of Oral Squamous Cell Carcinoma". PLOS ONE. 11 (3): e0152165. Bibcode:2016PLoSO..1152165Y. doi:10.1371/journal.pone.0152165. PMC 4816521. PMID 27031837.

[refGRCh38Ensembl-1] ENSG00000285132 GRCh38: Ensembl release 89: ENSG00000164733, ENSG00000285132 – Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000021939 – Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid2103490-5] Sloane BF (April 1990). "Cathepsin B and cystatins: evidence for a role in cancer progression". Seminars in Cancer Biology. 1 (2): 137–52. PMID 2103490.

[pmid3463996-6] Chan SJ, San Segundo B, McCormick MB, Steiner DF (October 1986). "Nucleotide and predicted amino acid sequences of cloned human and mouse preprocathepsin B cDNAs". Proceedings of the National Academy of Sciences of the United States of America. 83 (20): 7721–5. Bibcode:1986PNAS...83.7721C. doi:10.1073/pnas.83.20.7721. PMC 386793. PMID 3463996.

[pmid8112600-7] Cao L, Taggart RT, Berquin IM, Moin K, Fong D, Sloane BF (February 1994). "Human gastric adenocarcinoma cathepsin B: isolation and sequencing of full-length cDNAs and polymorphisms of the gene". Gene. 139 (2): 163–9. doi:10.1016/0378-1119(94)90750-1. PMID 8112600.

[pmid24749816-8] Tong B, Wan B, Wei Z, Wang T, Zhao P, Dou Y, Lv Z, Xia Y, Dai Y (September 2014). "Role of cathepsin B in regulating migration and invasion of fibroblast-like synoviocytes into inflamed tissue from patients with rheumatoid arthritis". Clinical and Experimental Immunology. 177 (3): 586–97. doi:10.1111/cei.12357. PMC 4137842. PMID 24749816.

[pmid14972341-9] Lai WF, Chang CH, Tang Y, Bronson R, Tung CH (March 2004). "Early diagnosis of osteoarthritis using cathepsin B sensitive near-infrared fluorescent probes". Osteoarthritis and Cartilage. 12 (3): 239–44. doi:10.1016/j.joca.2003.11.005. PMID 14972341.

[pmid19858192-10] Ha SD, Ham B, Mogridge J, Saftig P, Lin S, Kim SO (January 2010). "Cathepsin B-mediated autophagy flux facilitates the anthrax toxin receptor 2-mediated delivery of anthrax lethal factor into the cytoplasm". The Journal of Biological Chemistry. 285 (3): 2120–9. doi:10.1074/jbc.M109.065813. PMC 2804368. PMID 19858192.

[pmid27031837-11] Yang WE, Ho CC, Yang SF, Lin SH, Yeh KT, Lin CW, Chen MK (2016). "Cathepsin B Expression and the Correlation with Clinical Aspects of Oral Squamous Cell Carcinoma". PLOS ONE. 11 (3): e0152165. Bibcode:2016PLoSO..1152165Y. doi:10.1371/journal.pone.0152165. PMC 4816521. PMID 27031837.

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