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Cathepsin K (EC 3.4.22.38) (Cathepsin O) (Cathepsin O2) (Cathepsin X)

 CATK_HUMAN              Reviewed;         329 AA.
P43235; Q6FHS6;
01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
01-NOV-1995, sequence version 1.
25-OCT-2017, entry version 182.
RecName: Full=Cathepsin K;
EC=3.4.22.38;
AltName: Full=Cathepsin O;
AltName: Full=Cathepsin O2;
AltName: Full=Cathepsin X;
Flags: Precursor;
Name=CTSK; Synonyms=CTSO, CTSO2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Blood;
PubMed=7805878; DOI=10.1016/0014-5793(94)01349-6;
Shi G.-P., Chapman H.A., Bhairi S.M., Deleeuw C., Reddy V.Y.,
Weiss S.J.;
"Molecular cloning of human cathepsin O, a novel endoproteinase and
homologue of rabbit OC2.";
FEBS Lett. 357:129-134(1995).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Bone;
PubMed=7818555; DOI=10.1006/bbrc.1995.1013;
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. 206:89-96(1995).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Osteoclastoma;
PubMed=8585423; DOI=10.1002/jbmr.5650100809;
Li Y., Alexander M., Wucherpfennig A.L., 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. 10:1197-1202(1995).
[4]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Spleen;
PubMed=7576232; DOI=10.1515/bchm3.1995.376.6.379;
Broemme 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 376:379-384(1995).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Skin;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
PubMed=9033587; DOI=10.1038/nsb0297-105;
McGrath M.E., Klaus J.L., Barnes M.G., Bromme D.;
"Crystal structure of human cathepsin K complexed with a potent
inhibitor.";
Nat. Struct. Biol. 4:105-109(1997).
[10]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
PubMed=9405598; DOI=10.1073/pnas.94.26.14249;
Thompson S.K., Halbert S.M., Bossard M.J., Tomaszek T.A., Levy M.A.,
Zhao B., Smith W.W., Abdel-Meguid S.S., Janson C.A., D'Alessio K.J.,
McQueney M.S., Amegadzie B.Y., Hanning C.R., Desjarlais R.L.,
Briand J., Sarkar S.K., Huddleston M.J., Ijames C.F., Carr S.A.,
Garnes K.T., Shu A., Heys J.R., Bradbeer J., Zembryki D., Veber D.F.;
"Design of potent and selective human cathepsin K inhibitors that span
the active site.";
Proc. Natl. Acad. Sci. U.S.A. 94:14249-14254(1997).
[11]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF ZYMOGEN FORM.
PubMed=9893980; DOI=10.1021/bi9822271;
LaLonde J.M., Zhao B., Janson C.A., D'Alessio K.J., McQueney M.S.,
Orsini M.J., Debouck C.M., Smith W.W.;
"The crystal structure of human procathepsin K.";
Biochemistry 38:862-869(1999).
[12]
X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS).
PubMed=10048321; DOI=10.1110/ps.8.2.283;
Sivaraman J., Lalumiere M., Menard R., Cygler M.;
"Crystal structure of wild-type human procathepsin K.";
Protein Sci. 8:283-290(1999).
[13]
VARIANT PKND ARG-146.
PubMed=8703060; DOI=10.1126/science.273.5279.1236;
Gelb B.D., Shi G.-P., Chapman H.A., Desnick R.J.;
"Pycnodysostosis, a lysosomal disease caused by cathepsin K
deficiency.";
Science 273:1236-1238(1996).
[14]
VARIANT PKND VAL-277.
PubMed=9529353; DOI=10.1086/301795;
Gelb B.D., Willner J.P., Dunn T.M., Kardon N.B., Verloes A.,
Poncin J., Desnick R.J.;
"Paternal uniparental disomy for chromosome 1 revealed by molecular
analysis of a patient with pycnodysostosis.";
Am. J. Hum. Genet. 62:848-854(1998).
[15]
VARIANT PKND GLU-79.
PubMed=10491211; DOI=10.1359/jbmr.1999.14.10.1649;
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. 14:1649-1653(1999).
[16]
VARIANTS PKND GLU-79 AND PRO-309.
PubMed=10878663; DOI=10.1038/sj.ejhg.5200481;
Haagerup A., Hertz J.M., Christensen M.F., Binderup H., Kruse T.A.;
"Cathepsin K gene mutations and 1q21 haplotypes in at patients with
pycnodysostosis in an outbred population.";
Eur. J. Hum. Genet. 8:431-436(2000).
[17]
VARIANTS PKND PRO-122 AND VAL-277.
PubMed=22822386;
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. 2:254-258(2012).
[18]
VARIANT PKND CYS-283, AND CHARACTERIZATION OF VARIANT PKND CYS-283.
PubMed=25731711; DOI=10.1177/0022034515573964;
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. 94:674-681(2015).
-!- 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.
-!- CATALYTIC ACTIVITY: Broad proteolytic activity. With small-
molecule substrates and inhibitors, the major determinant of
specificity is P2, which is preferably Leu, Met > Phe, and not
Arg.
-!- SUBCELLULAR LOCATION: Lysosome.
-!- TISSUE SPECIFICITY: Predominantly expressed in osteoclasts
(bones).
-!- DISEASE: Pycnodysostosis (PKND) [MIM:265800]: A rare autosomal
recessive bone disorder characterized by deformity of the skull,
maxilla and phalanges, osteosclerosis, and fragility of bone.
{ECO:0000269|PubMed:10491211, ECO:0000269|PubMed:10878663,
ECO:0000269|PubMed:22822386, ECO:0000269|PubMed:25731711,
ECO:0000269|PubMed:8703060, ECO:0000269|PubMed:9529353}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- SIMILARITY: Belongs to the peptidase C1 family.
{ECO:0000255|PROSITE-ProRule:PRU10088, ECO:0000255|PROSITE-
ProRule:PRU10089, ECO:0000255|PROSITE-ProRule:PRU10090}.
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EMBL; U13665; AAA65233.1; -; mRNA.
EMBL; X82153; CAA57649.1; -; mRNA.
EMBL; U20280; AAA95998.1; -; mRNA.
EMBL; S79895; AAB35521.1; -; mRNA.
EMBL; CR541675; CAG46476.1; -; mRNA.
EMBL; AL355860; CAI12795.1; -; Genomic_DNA.
EMBL; AL356292; CAI12795.1; JOINED; Genomic_DNA.
EMBL; AL356292; CAI13649.1; -; Genomic_DNA.
EMBL; AL355860; CAI13649.1; JOINED; Genomic_DNA.
EMBL; CH471121; EAW53516.1; -; Genomic_DNA.
EMBL; BC016058; AAH16058.1; -; mRNA.
CCDS; CCDS969.1; -.
PIR; JC2476; JC2476.
RefSeq; NP_000387.1; NM_000396.3.
UniGene; Hs.632466; -.
PDB; 1ATK; X-ray; 2.20 A; A=115-329.
PDB; 1AU0; X-ray; 2.60 A; A=115-329.
PDB; 1AU2; X-ray; 2.60 A; A=115-329.
PDB; 1AU3; X-ray; 2.50 A; A=115-329.
PDB; 1AU4; X-ray; 2.30 A; A=115-329.
PDB; 1AYU; X-ray; 2.20 A; A=115-329.
PDB; 1AYV; X-ray; 2.30 A; A=115-329.
PDB; 1AYW; X-ray; 2.40 A; A=115-329.
PDB; 1BGO; X-ray; 2.30 A; A=115-329.
PDB; 1BY8; X-ray; 2.60 A; A=16-329.
PDB; 1MEM; X-ray; 1.80 A; A=115-329.
PDB; 1NL6; X-ray; 2.80 A; A/B=115-329.
PDB; 1NLJ; X-ray; 2.40 A; A/B=115-329.
PDB; 1Q6K; X-ray; 2.10 A; A=115-329.
PDB; 1SNK; X-ray; 2.40 A; A=116-329.
PDB; 1TU6; X-ray; 1.75 A; A/B=115-329.
PDB; 1U9V; X-ray; 2.20 A; A=113-329.
PDB; 1U9W; X-ray; 2.30 A; A=113-329.
PDB; 1U9X; X-ray; 2.10 A; A=113-329.
PDB; 1VSN; X-ray; 2.00 A; A=115-329.
PDB; 1YK7; X-ray; 2.50 A; A=115-329.
PDB; 1YK8; X-ray; 2.60 A; A=115-329.
PDB; 1YT7; X-ray; 2.30 A; A=115-329.
PDB; 2ATO; X-ray; 2.00 A; A=115-329.
PDB; 2AUX; X-ray; 2.40 A; A=115-329.
PDB; 2AUZ; X-ray; 2.30 A; A=115-329.
PDB; 2BDL; X-ray; 2.00 A; A=115-329.
PDB; 2R6N; X-ray; 1.95 A; A=113-329.
PDB; 3C9E; X-ray; 1.80 A; A=115-329.
PDB; 3H7D; X-ray; 2.24 A; A/E=115-329.
PDB; 3KW9; X-ray; 1.80 A; A=115-329.
PDB; 3KWB; X-ray; 2.02 A; X/Y=115-329.
PDB; 3KWZ; X-ray; 1.49 A; A=115-329.
PDB; 3KX1; X-ray; 1.51 A; A=115-329.
PDB; 3O0U; X-ray; 1.80 A; A=115-329.
PDB; 3O1G; X-ray; 1.65 A; A=115-329.
PDB; 3OVZ; X-ray; 2.02 A; A=121-329.
PDB; 4DMX; X-ray; 1.70 A; A=115-329.
PDB; 4DMY; X-ray; 1.63 A; A/B=115-329.
PDB; 4N79; X-ray; 2.62 A; A=115-329.
PDB; 4N8W; X-ray; 2.02 A; A=115-329.
PDB; 4X6H; X-ray; 1.00 A; A=115-329.
PDB; 4X6I; X-ray; 1.87 A; A=115-329.
PDB; 4X6J; X-ray; 1.59 A; A=115-329.
PDB; 4YV8; X-ray; 2.00 A; A=115-329.
PDB; 4YVA; X-ray; 1.80 A; A=115-329.
PDB; 5J94; X-ray; 2.60 A; A=107-329.
PDB; 5JA7; X-ray; 1.61 A; A/B=107-329.
PDB; 5JH3; X-ray; 1.75 A; A=107-329.
PDB; 5TDI; X-ray; 1.40 A; A=115-329.
PDB; 5TUN; X-ray; 1.62 A; A=115-329.
PDB; 7PCK; X-ray; 3.20 A; A/B/C/D=16-329.
PDBsum; 1ATK; -.
PDBsum; 1AU0; -.
PDBsum; 1AU2; -.
PDBsum; 1AU3; -.
PDBsum; 1AU4; -.
PDBsum; 1AYU; -.
PDBsum; 1AYV; -.
PDBsum; 1AYW; -.
PDBsum; 1BGO; -.
PDBsum; 1BY8; -.
PDBsum; 1MEM; -.
PDBsum; 1NL6; -.
PDBsum; 1NLJ; -.
PDBsum; 1Q6K; -.
PDBsum; 1SNK; -.
PDBsum; 1TU6; -.
PDBsum; 1U9V; -.
PDBsum; 1U9W; -.
PDBsum; 1U9X; -.
PDBsum; 1VSN; -.
PDBsum; 1YK7; -.
PDBsum; 1YK8; -.
PDBsum; 1YT7; -.
PDBsum; 2ATO; -.
PDBsum; 2AUX; -.
PDBsum; 2AUZ; -.
PDBsum; 2BDL; -.
PDBsum; 2R6N; -.
PDBsum; 3C9E; -.
PDBsum; 3H7D; -.
PDBsum; 3KW9; -.
PDBsum; 3KWB; -.
PDBsum; 3KWZ; -.
PDBsum; 3KX1; -.
PDBsum; 3O0U; -.
PDBsum; 3O1G; -.
PDBsum; 3OVZ; -.
PDBsum; 4DMX; -.
PDBsum; 4DMY; -.
PDBsum; 4N79; -.
PDBsum; 4N8W; -.
PDBsum; 4X6H; -.
PDBsum; 4X6I; -.
PDBsum; 4X6J; -.
PDBsum; 4YV8; -.
PDBsum; 4YVA; -.
PDBsum; 5J94; -.
PDBsum; 5JA7; -.
PDBsum; 5JH3; -.
PDBsum; 5TDI; -.
PDBsum; 5TUN; -.
PDBsum; 7PCK; -.
ProteinModelPortal; P43235; -.
SMR; P43235; -.
BioGrid; 107893; 8.
DIP; DIP-39993N; -.
IntAct; P43235; 4.
STRING; 9606.ENSP00000271651; -.
BindingDB; P43235; -.
ChEMBL; CHEMBL268; -.
DrugBank; DB07592; (1R)-2-METHYL-1-(PHENYLMETHYL)PROPYL[(1S)-1-FORMYLPENTYL]CARBAMATE.
DrugBank; DB07593; 1-(PHENYLMETHYL)CYCLOPENTYL[(1S)-1-FORMYLPENTYL]CARBAMATE.
DrugBank; DB04244; 1-[2-(3-Biphenyl)-4-Methylvaleryl)]Amino-3-(2-Pyridylsulfonyl)Amino-2-Propanone.
DrugBank; DB03405; 1-[N[(Phenylmethoxy)Carbonyl]-L-Leucyl-4-[[N/N-[(Phenylmethoxy)Carbonyl]-/Nl-Leucyl]Amino]-3-Pyrrolidinone/N.
DrugBank; DB02869; 3-amino-5-phenylpentane.
DrugBank; DB07965; 6-(cyclohexylamino)-9-[2-(4-methylpiperazin-1-yl)-ethyl]-9H-purine-2-carbonitrile.
DrugBank; DB07967; 9-CYCLOPENTYL-6-[2-(3-IMIDAZOL-1-YL-PROPOXY)-PHENYLAMINO]-9H-PURINE-2-CARBONITRILE.
DrugBank; DB01858; [1-(4-Fluorobenzyl)Cyclobutyl]Methyl (1s)-1-[Oxo(1h-Pyrazol-5-Ylamino)Acetyl]Pentylcarbamate.
DrugBank; DB03642; Benzofuran-2-Carboxylic Acid {(S)-3-Methyl-1-[3-Oxo-1-(Pyridin-2-Ylsulfonyl)Azepan-4-Ylcarbamoyl]Butyl}Amide.
DrugBank; DB05736; MIV-701.
DrugBank; DB04234; N2-({[(4-Bromophenyl)Methyl]Oxy}Carbonyl)-N1-[(1s)-1-Formylpentyl]-L-Leucinamide.
DrugBank; DB03456; N2-[(benzyloxy)carbonyl]-n1-[(3S)-1-cyanopyrrolidin-3-yl]-l-leucinamide.
DrugBank; DB08594; TERT-BUTYL 2-CYANO-2-METHYLHYDRAZINECARBOXYLATE.
DrugBank; DB04523; Tert-Butyl(1s)-1-Cyclohexyl-2-Oxoethylcarbamate.
GuidetoPHARMACOLOGY; 2350; -.
MEROPS; I29.007; -.
iPTMnet; P43235; -.
PhosphoSitePlus; P43235; -.
BioMuta; CTSK; -.
DMDM; 1168793; -.
EPD; P43235; -.
PaxDb; P43235; -.
PeptideAtlas; P43235; -.
PRIDE; P43235; -.
DNASU; 1513; -.
Ensembl; ENST00000271651; ENSP00000271651; ENSG00000143387.
GeneID; 1513; -.
KEGG; hsa:1513; -.
UCSC; uc001evp.3; human.
CTD; 1513; -.
DisGeNET; 1513; -.
EuPathDB; HostDB:ENSG00000143387.12; -.
GeneCards; CTSK; -.
HGNC; HGNC:2536; CTSK.
HPA; HPA050346; -.
MalaCards; CTSK; -.
MIM; 265800; phenotype.
MIM; 601105; gene.
neXtProt; NX_P43235; -.
OpenTargets; ENSG00000143387; -.
Orphanet; 763; Pycnodysostosis.
PharmGKB; PA27034; -.
eggNOG; KOG1543; Eukaryota.
eggNOG; COG4870; LUCA.
GeneTree; ENSGT00900000140823; -.
HOGENOM; HOG000230774; -.
HOVERGEN; HBG011513; -.
InParanoid; P43235; -.
KO; K01371; -.
OMA; KGNKHWI; -.
OrthoDB; EOG091G0AKT; -.
PhylomeDB; P43235; -.
TreeFam; TF313739; -.
BRENDA; 3.4.22.38; 2681.
Reactome; R-HSA-1442490; Collagen degradation.
Reactome; R-HSA-1474228; Degradation of the extracellular matrix.
Reactome; R-HSA-1592389; Activation of Matrix Metalloproteinases.
Reactome; R-HSA-1679131; Trafficking and processing of endosomal TLR.
Reactome; R-HSA-2132295; MHC class II antigen presentation.
Reactome; R-HSA-8939242; RUNX1 regulates transcription of genes involved in differentiation of keratinocytes.
SIGNOR; P43235; -.
ChiTaRS; CTSK; human.
EvolutionaryTrace; P43235; -.
GeneWiki; Cathepsin_K; -.
GenomeRNAi; 1513; -.
PRO; PR:P43235; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000143387; -.
CleanEx; HS_CTSK; -.
CleanEx; HS_CTSO; -.
ExpressionAtlas; P43235; baseline and differential.
Genevisible; P43235; HS.
GO; GO:0036021; C:endolysosome lumen; TAS:Reactome.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
GO; GO:0043202; C:lysosomal lumen; TAS:Reactome.
GO; GO:0005764; C:lysosome; IBA:GO_Central.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005518; F:collagen binding; IDA:BHF-UCL.
GO; GO:0004197; F:cysteine-type endopeptidase activity; IDA:BHF-UCL.
GO; GO:0008234; F:cysteine-type peptidase activity; TAS:ProtInc.
GO; GO:0001968; F:fibronectin binding; IPI:BHF-UCL.
GO; GO:0043394; F:proteoglycan binding; IPI:BHF-UCL.
GO; GO:0004252; F:serine-type endopeptidase activity; TAS:Reactome.
GO; GO:0045453; P:bone resorption; IEA:Ensembl.
GO; GO:0030574; P:collagen catabolic process; IDA:BHF-UCL.
GO; GO:0022617; P:extracellular matrix disassembly; TAS:Reactome.
GO; GO:0001957; P:intramembranous ossification; IEA:Ensembl.
GO; GO:1903955; P:positive regulation of protein targeting to mitochondrion; IMP:ParkinsonsUK-UCL.
GO; GO:0006508; P:proteolysis; TAS:ProtInc.
GO; GO:0051603; P:proteolysis involved in cellular protein catabolic process; IDA:BHF-UCL.
GO; GO:1903146; P:regulation of autophagy of mitochondrion; IMP:ParkinsonsUK-UCL.
GO; GO:0045616; P:regulation of keratinocyte differentiation; TAS:Reactome.
GO; GO:0002224; P:toll-like receptor signaling pathway; TAS:Reactome.
InterPro; IPR025661; Pept_asp_AS.
InterPro; IPR000169; Pept_cys_AS.
InterPro; IPR025660; Pept_his_AS.
InterPro; IPR013128; Peptidase_C1A.
InterPro; IPR000668; Peptidase_C1A_C.
InterPro; IPR015644; Peptidase_C1A_cathepsin-K.
InterPro; IPR013201; Prot_inhib_I29.
PANTHER; PTHR12411; PTHR12411; 1.
PANTHER; PTHR12411:SF55; PTHR12411:SF55; 1.
Pfam; PF08246; Inhibitor_I29; 1.
Pfam; PF00112; Peptidase_C1; 1.
PRINTS; PR00705; PAPAIN.
SMART; SM00848; Inhibitor_I29; 1.
SMART; SM00645; Pept_C1; 1.
PROSITE; PS00640; THIOL_PROTEASE_ASN; 1.
PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
PROSITE; PS00639; THIOL_PROTEASE_HIS; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Disease mutation; Disulfide bond;
Glycoprotein; Hydrolase; Lysosome; Protease; Reference proteome;
Signal; Thiol protease; Zymogen.
SIGNAL 1 15 {ECO:0000255}.
PROPEP 16 114 Activation peptide.
/FTId=PRO_0000026295.
CHAIN 115 329 Cathepsin K.
/FTId=PRO_0000026296.
ACT_SITE 139 139 {ECO:0000250}.
ACT_SITE 276 276 {ECO:0000250}.
ACT_SITE 296 296 {ECO:0000250}.
CARBOHYD 103 103 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 136 177
DISULFID 170 210
DISULFID 269 318
VARIANT 79 79 G -> E (in PKND; dbSNP:rs74315305).
{ECO:0000269|PubMed:10491211,
ECO:0000269|PubMed:10878663}.
/FTId=VAR_015738.
VARIANT 122 122 R -> P (in PKND).
{ECO:0000269|PubMed:22822386}.
/FTId=VAR_074023.
VARIANT 146 146 G -> R (in PKND; dbSNP:rs74315302).
{ECO:0000269|PubMed:8703060}.
/FTId=VAR_006725.
VARIANT 277 277 A -> V (in PKND; dbSNP:rs74315304).
{ECO:0000269|PubMed:22822386,
ECO:0000269|PubMed:9529353}.
/FTId=VAR_015739.
VARIANT 283 283 Y -> C (in PKND; does not affect protein
level; does not detect cysteine-type
endopeptidase activity).
{ECO:0000269|PubMed:25731711}.
/FTId=VAR_074024.
VARIANT 309 309 L -> P (in PKND; dbSNP:rs29001685).
{ECO:0000269|PubMed:10878663}.
/FTId=VAR_006726.
CONFLICT 46 46 R -> P (in Ref. 3; AAA95998).
{ECO:0000305}.
HELIX 22 32 {ECO:0000244|PDB:1BY8}.
HELIX 40 66 {ECO:0000244|PDB:1BY8}.
STRAND 70 73 {ECO:0000244|PDB:1BY8}.
STRAND 79 81 {ECO:0000244|PDB:1BY8}.
HELIX 83 89 {ECO:0000244|PDB:1BY8}.
STRAND 102 107 {ECO:0000244|PDB:1BY8}.
HELIX 121 124 {ECO:0000244|PDB:4X6H}.
STRAND 135 137 {ECO:0000244|PDB:3KX1}.
HELIX 139 156 {ECO:0000244|PDB:4X6H}.
HELIX 164 170 {ECO:0000244|PDB:4X6H}.
HELIX 176 178 {ECO:0000244|PDB:4X6H}.
HELIX 182 192 {ECO:0000244|PDB:4X6H}.
STRAND 195 197 {ECO:0000244|PDB:4X6H}.
TURN 198 200 {ECO:0000244|PDB:4X6H}.
HELIX 214 216 {ECO:0000244|PDB:4X6H}.
STRAND 217 219 {ECO:0000244|PDB:4X6H}.
STRAND 223 226 {ECO:0000244|PDB:4X6H}.
HELIX 232 242 {ECO:0000244|PDB:4X6H}.
STRAND 245 249 {ECO:0000244|PDB:4X6H}.
HELIX 254 257 {ECO:0000244|PDB:4X6H}.
STRAND 261 264 {ECO:0000244|PDB:4X6H}.
STRAND 276 286 {ECO:0000244|PDB:4X6H}.
STRAND 289 295 {ECO:0000244|PDB:4X6H}.
STRAND 300 302 {ECO:0000244|PDB:3H7D}.
TURN 303 305 {ECO:0000244|PDB:1AYV}.
STRAND 307 316 {ECO:0000244|PDB:4X6H}.
HELIX 317 319 {ECO:0000244|PDB:4X6H}.
TURN 320 322 {ECO:0000244|PDB:3KX1}.
STRAND 325 328 {ECO:0000244|PDB:4X6H}.
SEQUENCE 329 AA; 36966 MW; 4677C3C89FF4CE85 CRC64;
MWGLKVLLLP VVSFALYPEE ILDTHWELWK KTHRKQYNNK VDEISRRLIW EKNLKYISIH
NLEASLGVHT YELAMNHLGD MTSEEVVQKM TGLKVPLSHS RSNDTLYIPE WEGRAPDSVD
YRKKGYVTPV KNQGQCGSCW AFSSVGALEG QLKKKTGKLL NLSPQNLVDC VSENDGCGGG
YMTNAFQYVQ KNRGIDSEDA YPYVGQEESC MYNPTGKAAK CRGYREIPEG NEKALKRAVA
RVGPVSVAID ASLTSFQFYS KGVYYDESCN SDNLNHAVLA VGYGIQKGNK HWIIKNSWGE
NWGNKGYILM ARNKNNACGI ANLASFPKM


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