Cathepsin B

Details

Name
Cathepsin B
Synonyms
  • 3.4.22.1
  • APP secretase
  • APPS
  • Cathepsin B1
  • CPSB
Gene Name
CTSB
Organism
Humans
Amino acid sequence
>lcl|BSEQ0019038|Cathepsin B
MWQLWASLCCLLVLANARSRPSFHPLSDELVNYVNKRNTTWQAGHNFYNVDMSYLKRLCG
TFLGGPKPPQRVMFTEDLKLPASFDAREQWPQCPTIKEIRDQGSCGSCWAFGAVEAISDR
ICIHTNAHVSVEVSAEDLLTCCGSMCGDGCNGGYPAEAWNFWTRKGLVSGGLYESHVGCR
PYSIPPCEHHVNGSRPPCTGEGDTPKCSKICEPGYSPTYKQDKHYGYNSYSVSNSEKDIM
AEIYKNGPVEGAFSVYSDFLLYKSGVYQHVTGEMMGGHAIRILGWGVENGTPYWLVANSW
NTDWGDNGFFKILRGQDHCGIESEVVAGIPRTDQYWEKI
Number of residues
339
Molecular Weight
37821.35
Theoretical pI
6.27
GO Classification
Functions
collagen binding / cysteine-type endopeptidase activity / cysteine-type peptidase activity / peptidase activity / peptide binding / proteoglycan binding
Processes
autophagy / cellular response to mechanical stimulus / cellular response to thyroid hormone stimulus / collagen catabolic process / decidualization / epithelial cell differentiation / extracellular matrix disassembly / extracellular matrix organization / innate immune response / negative regulation of cell death / proteolysis / proteolysis involved in cellular protein catabolic process / regulation of apoptotic process / regulation of catalytic activity / response to amine / response to ethanol / response to glucose / response to interleukin-4 / response to organic cyclic compound / response to peptide hormone / response to wounding / skeletal muscle tissue development / spermatogenesis / toll-like receptor signaling pathway / viral entry into host cell
Components
apical plasma membrane / caveola / endolysosome lumen / external side of plasma membrane / extracellular exosome / extracellular region / extracellular space / intracellular / intracellular membrane-bounded organelle / lysosome / melanosome / mitochondrion / nucleolus / perinuclear region of cytoplasm / sarcolemma
General Function
Proteoglycan binding
Specific Function
Thiol protease which is believed to participate in intracellular degradation and turnover of proteins. Has also been implicated in tumor invasion and metastasis.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Lysosome
Gene sequence
>lcl|BSEQ0019039|Cathepsin B (CTSB)
ATGTGGCAGCTCTGGGCCTCCCTCTGCTGCCTGCTGGTGTTGGCCAATGCCCGGAGCAGG
CCCTCTTTCCATCCCCTGTCGGATGAGCTGGTCAACTATGTCAACAAACGGAATACCACG
TGGCAGGCCGGGCACAACTTCTACAACGTGGACATGAGCTACTTGAAGAGGCTATGTGGT
ACCTTCCTGGGTGGGCCCAAGCCACCCCAGAGAGTTATGTTTACCGAGGACCTGAAGCTG
CCTGCAAGCTTCGATGCACGGGAACAATGGCCACAGTGTCCCACCATCAAAGAGATCAGA
GACCAGGGCTCCTGTGGCTCCTGCTGGGCCTTCGGGGCTGTGGAAGCCATCTCTGACCGG
ATCTGCATCCACACCAATGCGCACGTCAGCGTGGAGGTGTCGGCGGAGGACCTGCTCACA
TGCTGTGGCAGCATGTGTGGGGACGGCTGTAATGGTGGCTATCCTGCTGAAGCTTGGAAC
TTCTGGACAAGAAAAGGCCTGGTTTCTGGTGGCCTCTATGAATCCCATGTAGGGTGCAGA
CCGTACTCCATCCCTCCCTGTGAGCACCACGTCAACGGCTCCCGGCCCCCATGCACGGGG
GAGGGAGATACCCCCAAGTGTAGCAAGATCTGTGAGCCTGGCTACAGCCCGACCTACAAA
CAGGACAAGCACTACGGATACAATTCCTACAGCGTCTCCAATAGCGAGAAGGACATCATG
GCCGAGATCTACAAAAACGGCCCCGTGGAGGGAGCTTTCTCTGTGTATTCGGACTTCCTG
CTCTACAAGTCAGGAGTGTACCAACACGTCACCGGAGAGATGATGGGTGGCCATGCCATC
CGCATCCTGGGCTGGGGAGTGGAGAATGGCACACCCTACTGGCTGGTTGCCAACTCCTGG
AACACTGACTGGGGTGACAATGGCTTCTTTAAAATACTCAGAGGACAGGATCACTGTGGA
ATCGAATCAGAAGTGGTGGCTGGAATTCCACGCACCGATCAGTACTGGGAAAAGATCTAA
Chromosome Location
8
Locus
8p22
External Identifiers
ResourceLink
UniProtKB IDP07858
UniProtKB Entry NameCATB_HUMAN
GenBank Protein ID181192
GenBank Gene IDM14221
GenAtlas IDCTSB
HGNC IDHGNC:2527
General References
  1. Chan SJ, San Segundo B, McCormick MB, Steiner DF: Nucleotide and predicted amino acid sequences of cloned human and mouse preprocathepsin B cDNAs. Proc Natl Acad Sci U S A. 1986 Oct;83(20):7721-5. [PubMed:3463996]
  2. Cao L, Taggart RT, Berquin IM, Moin K, Fong D, Sloane BF: Human gastric adenocarcinoma cathepsin B: isolation and sequencing of full-length cDNAs and polymorphisms of the gene. Gene. 1994 Feb 25;139(2):163-9. [PubMed:8112600]
  3. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed:14702039]
  4. Otsuki T, Ota T, Nishikawa T, Hayashi K, Suzuki Y, Yamamoto J, Wakamatsu A, Kimura K, Sakamoto K, Hatano N, Kawai Y, Ishii S, Saito K, Kojima S, Sugiyama T, Ono T, Okano K, Yoshikawa Y, Aotsuka S, Sasaki N, Hattori A, Okumura K, Nagai K, Sugano S, Isogai T: Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries. DNA Res. 2005;12(2):117-26. [PubMed:16303743]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed:15489334]
  6. Ritonja A, Popovic T, Turk V, Wiedenmann K, Machleidt W: Amino acid sequence of human liver cathepsin B. FEBS Lett. 1985 Feb 11;181(1):169-72. [PubMed:3972105]
  7. Moin K, Day NA, Sameni M, Hasnain S, Hirama T, Sloane BF: Human tumour cathepsin B. Comparison with normal liver cathepsin B. Biochem J. 1992 Jul 15;285 ( Pt 2):427-34. [PubMed:1637335]
  8. Fong D, Calhoun DH, Hsieh WT, Lee B, Wells RD: Isolation of a cDNA clone for the human lysosomal proteinase cathepsin B. Proc Natl Acad Sci U S A. 1986 May;83(9):2909-13. [PubMed:3010323]
  9. Basrur V, Yang F, Kushimoto T, Higashimoto Y, Yasumoto K, Valencia J, Muller J, Vieira WD, Watabe H, Shabanowitz J, Hearing VJ, Hunt DF, Appella E: Proteomic analysis of early melanosomes: identification of novel melanosomal proteins. J Proteome Res. 2003 Jan-Feb;2(1):69-79. [PubMed:12643545]
  10. Chi A, Valencia JC, Hu ZZ, Watabe H, Yamaguchi H, Mangini NJ, Huang H, Canfield VA, Cheng KC, Yang F, Abe R, Yamagishi S, Shabanowitz J, Hearing VJ, Wu C, Appella E, Hunt DF: Proteomic and bioinformatic characterization of the biogenesis and function of melanosomes. J Proteome Res. 2006 Nov;5(11):3135-44. [PubMed:17081065]
  11. Royer-Zemmour B, Ponsole-Lenfant M, Gara H, Roll P, Leveque C, Massacrier A, Ferracci G, Cillario J, Robaglia-Schlupp A, Vincentelli R, Cau P, Szepetowski P: Epileptic and developmental disorders of the speech cortex: ligand/receptor interaction of wild-type and mutant SRPX2 with the plasminogen activator receptor uPAR. Hum Mol Genet. 2008 Dec 1;17(23):3617-30. doi: 10.1093/hmg/ddn256. Epub 2008 Aug 21. [PubMed:18718938]
  12. Burkard TR, Planyavsky M, Kaupe I, Breitwieser FP, Burckstummer T, Bennett KL, Superti-Furga G, Colinge J: Initial characterization of the human central proteome. BMC Syst Biol. 2011 Jan 26;5:17. doi: 10.1186/1752-0509-5-17. [PubMed:21269460]
  13. Bian Y, Song C, Cheng K, Dong M, Wang F, Huang J, Sun D, Wang L, Ye M, Zou H: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. J Proteomics. 2014 Jan 16;96:253-62. doi: 10.1016/j.jprot.2013.11.014. Epub 2013 Nov 22. [PubMed:24275569]
  14. Vaca Jacome AS, Rabilloud T, Schaeffer-Reiss C, Rompais M, Ayoub D, Lane L, Bairoch A, Van Dorsselaer A, Carapito C: N-terminome analysis of the human mitochondrial proteome. Proteomics. 2015 Jul;15(14):2519-24. doi: 10.1002/pmic.201400617. Epub 2015 Jun 8. [PubMed:25944712]
  15. Musil D, Zucic D, Turk D, Engh RA, Mayr I, Huber R, Popovic T, Turk V, Towatari T, Katunuma N, et al.: The refined 2.15 A X-ray crystal structure of human liver cathepsin B: the structural basis for its specificity. EMBO J. 1991 Sep;10(9):2321-30. [PubMed:1868826]
  16. Turk D, Podobnik M, Kuhelj R, Dolinar M, Turk V: Crystal structures of human procathepsin B at 3.2 and 3.3 Angstroms resolution reveal an interaction motif between a papain-like cysteine protease and its propeptide. FEBS Lett. 1996 Apr 22;384(3):211-4. [PubMed:8617355]
  17. Podobnik M, Kuhelj R, Turk V, Turk D: Crystal structure of the wild-type human procathepsin B at 2.5 A resolution reveals the native active site of a papain-like cysteine protease zymogen. J Mol Biol. 1997 Sep 5;271(5):774-88. [PubMed:9299326]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB021082-Aminoethanimidic AcidexperimentalunknownDetails
DB021483-Amino-4-Oxybenzyl-2-ButanoneexperimentalunknownDetails
DB026853-MethylphenylalanineexperimentalunknownDetails
DB033292-PyridinethiolexperimentalunknownDetails
DB03588Diphenylacetic acidexperimentalunknownDetails
DB04579N-{[(2S,3S)-3-(Ethoxycarbonyl)-2-oxiranyl]carbonyl}-L-threonyl-L-isoleucineexperimentalunknownDetails
DB02855N-(3-Propylcarbamoyloxirane-2-Carbonyl)-Isoleucyl-ProlineexperimentalunknownDetails
DB07160N-{[(2S,3S)-3-(ETHOXYCARBONYL)OXIRAN-2-YL]CARBONYL}-L-ISOLEUCINEexperimentalunknownDetails
DB07219BENZYL N-({(2S,3S)-3-[(PROPYLAMINO)CARBONYL]OXIRAN-2-YL}CARBONYL)-L-ISOLEUCYL-L-PROLINATEexperimentalunknownDetails
DB07223METHYL N-({(2S,3S)-3-[(PROPYLAMINO)CARBONYL]OXIRAN-2-YL}CARBONYL)-L-ISOLEUCYL-L-PROLINATEexperimentalunknownDetails
DB07224N-{[(2S,3S)-3-(ETHOXYCARBONYL)OXIRAN-2-YL]CARBONYL}-L-ISOLEUCYL-L-ALANINEexperimentalunknownDetails
DB07225N-{[(2S,3S)-3-(ETHOXYCARBONYL)OXIRAN-2-YL]CARBONYL}-L-ISOLEUCYL-L-ISOLEUCINEexperimentalunknownDetails
DB07231N-({(2S,3S)-3-[(BENZYLAMINO)CARBONYL]OXIRAN-2-YL}CARBONYL)-L-ISOLEUCYL-L-PROLINEexperimentalunknownDetails
DB04126N-[1-Hydroxycarboxyethyl-Carbonyl]Leucylamino-2-Methyl-ButaneexperimentalunknownDetails
DB14962Trastuzumab deruxtecanapproved, investigationalunknownsubstrateDetails