Cathepsin K
Details
- Name
- Cathepsin K
- Synonyms
- 3.4.22.38
- Cathepsin O
- Cathepsin O2
- Cathepsin X
- CTSO
- CTSO2
- Gene Name
- CTSK
- Organism
- Humans
- Amino acid sequence
>lcl|BSEQ0012392|Cathepsin K MWGLKVLLLPVVSFALYPEEILDTHWELWKKTHRKQYNNKVDEISRRLIWEKNLKYISIH NLEASLGVHTYELAMNHLGDMTSEEVVQKMTGLKVPLSHSRSNDTLYIPEWEGRAPDSVD YRKKGYVTPVKNQGQCGSCWAFSSVGALEGQLKKKTGKLLNLSPQNLVDCVSENDGCGGG YMTNAFQYVQKNRGIDSEDAYPYVGQEESCMYNPTGKAAKCRGYREIPEGNEKALKRAVA RVGPVSVAIDASLTSFQFYSKGVYYDESCNSDNLNHAVLAVGYGIQKGNKHWIIKNSWGE NWGNKGYILMARNKNNACGIANLASFPKM
- Number of residues
- 329
- Molecular Weight
- 36965.82
- Theoretical pI
- 8.65
- GO Classification
- Functionscollagen binding / cysteine-type endopeptidase activity / cysteine-type peptidase activity / fibronectin binding / proteoglycan bindingProcessesbone resorption / collagen catabolic process / extracellular matrix disassembly / extracellular matrix organization / innate immune response / intramembranous ossification / positive regulation of protein targeting to mitochondrion / proteolysis / proteolysis involved in cellular protein catabolic process / regulation of mitophagy / toll-like receptor signaling pathwayComponentsendolysosome lumen / extracellular region / extracellular space / lysosome
- General Function
- Proteoglycan binding
- Specific Function
- Closely involved in osteoclastic bone resorption and may participate partially in the disorder of bone remodeling. Displays potent endoprotease activity against fibrinogen at acid pH. May play an important role in extracellular matrix degradation.
- Pfam Domain Function
- Transmembrane Regions
- Not Available
- Cellular Location
- Lysosome
- Gene sequence
>lcl|BSEQ0012393|Cathepsin K (CTSK) ATGTGGGGGCTCAAGGTTCTGCTGCTACCTGTGGTGAGCTTTGCTCTGTACCCTGAGGAG ATACTGGACACCCACTGGGAGCTATGGAAGAAGACCCACAGGAAGCAATATAACAACAAG GTGGATGAAATCTCTCGGCGTTTAATTTGGGAAAAAAACCTGAAGTATATTTCCATCCAT AACCTTGAGGCTTCTCTTGGTGTCCATACATATGAACTGGCTATGAACCACCTGGGGGAC ATGACCAGTGAAGAGGTGGTTCAGAAGATGACTGGACTCAAAGTACCCCTGTCTCATTCC CGCAGTAATGACACCCTTTATATCCCAGAATGGGAAGGTAGAGCCCCAGACTCTGTCGAC TATCGAAAGAAAGGATATGTTACTCCTGTCAAAAATCAGGGTCAGTGTGGTTCCTGTTGG GCTTTTAGCTCTGTGGGTGCCCTGGAGGGCCAACTCAAGAAGAAAACTGGCAAACTCTTA AATCTGAGTCCCCAGAACCTAGTGGATTGTGTGTCTGAGAATGATGGCTGTGGAGGGGGC TACATGACCAATGCCTTCCAATATGTGCAGAAGAACCGGGGTATTGACTCTGAAGATGCC TACCCATATGTGGGACAGGAAGAGAGTTGTATGTACAACCCAACAGGCAAGGCAGCTAAA TGCAGAGGGTACAGAGAGATCCCCGAGGGGAATGAGAAAGCCCTGAAGAGGGCAGTGGCC CGAGTGGGACCTGTCTCTGTGGCCATTGATGCAAGCCTGACCTCCTTCCAGTTTTACAGC AAAGGTGTGTATTATGATGAAAGCTGCAATAGCGATAATCTGAACCATGCGGTTTTGGCA GTGGGATATGGAATCCAGAAGGGAAACAAGCACTGGATAATTAAAAACAGCTGGGGAGAA AACTGGGGAAACAAAGGATATATCCTCATGGCTCGAAATAAGAACAACGCCTGTGGCATT GCCAACCTGGCCAGCTTCCCCAAGATGTGA
- Chromosome Location
- 1
- Locus
- 1q21
- External Identifiers
Resource Link UniProtKB ID P43235 UniProtKB Entry Name CATK_HUMAN GenBank Gene ID U13665 GenAtlas ID CTSK HGNC ID HGNC:2536 - General References
- Shi GP, Chapman HA, Bhairi SM, DeLeeuw C, Reddy VY, Weiss SJ: Molecular cloning of human cathepsin O, a novel endoproteinase and homologue of rabbit OC2. FEBS Lett. 1995 Jan 3;357(2):129-34. [Article]
- Inaoka T, Bilbe G, Ishibashi O, Tezuka K, Kumegawa M, Kokubo T: Molecular cloning of human cDNA for cathepsin K: novel cysteine proteinase predominantly expressed in bone. Biochem Biophys Res Commun. 1995 Jan 5;206(1):89-96. [Article]
- Li YP, Alexander M, Wucherpfennig AL, Yelick P, Chen W, Stashenko P: Cloning and complete coding sequence of a novel human cathepsin expressed in giant cells of osteoclastomas. J Bone Miner Res. 1995 Aug;10(8):1197-202. [Article]
- Bromme D, Okamoto K: Human cathepsin O2, a novel cysteine protease highly expressed in osteoclastomas and ovary molecular cloning, sequencing and tissue distribution. Biol Chem Hoppe Seyler. 1995 Jun;376(6):379-84. [Article]
- Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [Article]
- 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. [Article]
- McGrath ME, Klaus JL, Barnes MG, Bromme D: Crystal structure of human cathepsin K complexed with a potent inhibitor. Nat Struct Biol. 1997 Feb;4(2):105-9. [Article]
- Thompson SK, Halbert SM, Bossard MJ, Tomaszek TA, Levy MA, Zhao B, Smith WW, Abdel-Meguid SS, Janson CA, D'Alessio KJ, McQueney MS, Amegadzie BY, Hanning CR, DesJarlais RL, Briand J, Sarkar SK, Huddleston MJ, Ijames CF, Carr SA, Garnes KT, Shu A, Heys JR, Bradbeer J, Zembryki D, Lee-Rykaczewski L, James IE, Lark MW, Drake FH, Gowen M, Gleason JG, Veber DF: Design of potent and selective human cathepsin K inhibitors that span the active site. Proc Natl Acad Sci U S A. 1997 Dec 23;94(26):14249-54. [Article]
- LaLonde JM, Zhao B, Janson CA, D'Alessio KJ, McQueney MS, Orsini MJ, Debouck CM, Smith WW: The crystal structure of human procathepsin K. Biochemistry. 1999 Jan 19;38(3):862-9. [Article]
- Sivaraman J, Lalumiere M, Menard R, Cygler M: Crystal structure of wild-type human procathepsin K. Protein Sci. 1999 Feb;8(2):283-90. [Article]
- Gelb BD, Shi GP, Chapman HA, Desnick RJ: Pycnodysostosis, a lysosomal disease caused by cathepsin K deficiency. Science. 1996 Aug 30;273(5279):1236-8. [Article]
- Gelb BD, Willner JP, Dunn TM, Kardon NB, Verloes A, Poncin J, Desnick RJ: Paternal uniparental disomy for chromosome 1 revealed by molecular analysis of a patient with pycnodysostosis. Am J Hum Genet. 1998 Apr;62(4):848-54. [Article]
- Ho N, Punturieri A, Wilkin D, Szabo J, Johnson M, Whaley J, Davis J, Clark A, Weiss S, Francomano C: Mutations of CTSK result in pycnodysostosis via a reduction in cathepsin K protein. J Bone Miner Res. 1999 Oct;14(10):1649-53. [Article]
- Haagerup A, Hertz JM, Christensen MF, Binderup H, Kruse TA: Cathepsin K gene mutations and 1q21 haplotypes in at patients with pycnodysostosis in an outbred population. Eur J Hum Genet. 2000 Jun;8(6):431-6. [Article]
- Matsushita M, Kitoh H, Kaneko H, Mishima K, Itoh Y, Hattori T, Ishiguro N: Novel Compound Heterozygous Mutations in the Cathepsin K Gene in Japanese Female Siblings with Pyknodysostosis. Mol Syndromol. 2012 Apr;2(6):254-258. Epub 2012 Mar 6. [Article]
- Xue Y, Wang L, Xia D, Li Q, Gao S, Dong M, Cai T, Shi S, He L, Hu K, Mao T, Duan X: Dental Abnormalities Caused by Novel Compound Heterozygous CTSK Mutations. J Dent Res. 2015 May;94(5):674-81. doi: 10.1177/0022034515573964. Epub 2015 Mar 2. [Article]
Drug Relations
- Drug Relations
DrugBank ID Name Drug group Pharmacological action? Actions Details DB03405 N2-[(Benzyloxy)carbonyl]-N-[(3R)-1-{N-[(benzyloxy)carbonyl]-L-leucyl}-4-oxo-3-pyrrolidinyl]-L-leucinamide experimental unknown Details DB03642 N-[(2S)-4-Methyl-1-oxo-1-{[(4S)-3-oxo-1-(2-pyridinylsulfonyl)-4-azepanyl]amino}-2-pentanyl]-1-benzofuran-2-carboxamide experimental unknown Details DB03891 Dibenzyl (carbonylbis{2,1-hydrazinediyl[(2S)-4-methyl-1-oxo-1,2-pentanediyl]})biscarbamate experimental unknown Details DB04244 (2R)-2-(3-Biphenylyl)-N-{(2R)-2-hydroxy-3-[(2-pyridinylsulfonyl)amino]propyl}-4-methylpentanamide experimental unknown Details DB05736 MIV-701 investigational unknown Details DB06367 Relacatib investigational unknown inhibitor Details DB07563 1-{7-cyclohexyl-6-[4-(4-methylpiperazin-1-yl)benzyl]-7H-pyrrolo[2,3-d]pyrimidin-2-yl}methanamine experimental unknown Details DB07592 (2R)-3-Methyl-1-phenyl-2-butanyl [(2S)-1-oxo-2-hexanyl]carbamate experimental unknown Details DB07593 1-(PHENYLMETHYL)CYCLOPENTYL[(1S)-1-FORMYLPENTYL]CARBAMATE experimental unknown Details DB01858 [1-(4-Fluorobenzyl)Cyclobutyl]Methyl (1s)-1-[Oxo(1h-Pyrazol-5-Ylamino)Acetyl]Pentylcarbamate experimental unknown Details DB07965 6-(cyclohexylamino)-9-[2-(4-methylpiperazin-1-yl)-ethyl]-9H-purine-2-carbonitrile experimental unknown Details DB07967 9-CYCLOPENTYL-6-[2-(3-IMIDAZOL-1-YL-PROPOXY)-PHENYLAMINO]-9H-PURINE-2-CARBONITRILE experimental unknown Details DB04234 N2-({[(4-Bromophenyl)Methyl]Oxy}Carbonyl)-N1-[(1s)-1-Formylpentyl]-L-Leucinamide experimental unknown Details DB03456 N2-[(benzyloxy)carbonyl]-n1-[(3S)-1-cyanopyrrolidin-3-yl]-l-leucinamide experimental unknown Details DB02869 3-amino-5-phenylpentane experimental unknown Details DB08270 N-(2-AMINOETHYL)-N~2~-{(1S)-1-[4'-(AMINOSULFONYL)BIPHENYL-4-YL]-2,2,2-TRIFLUOROETHYL}-L-LEUCINAMIDE experimental unknown Details DB08287 (1R,2R)-N-(2-Aminoethyl)-2-{[(4-methoxyphenyl)sulfonyl]methyl}cyclohexanecarboxamide experimental unknown Details DB08594 TERT-BUTYL 2-CYANO-2-METHYLHYDRAZINECARBOXYLATE experimental unknown Details DB04523 Tert-Butyl(1s)-1-Cyclohexyl-2-Oxoethylcarbamate experimental unknown Details DB06670 Odanacatib investigational unknown inhibitor Details DB02679 Cyanamide experimental unknown Details DB15599 MIV-711 investigational unknown inhibitor Details DB12239 Balicatib investigational unknown inhibitor Details