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UniProtKB/Swiss-Prot entry P43235


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name CATK_HUMAN
Primary accession number P43235
Secondary accession numbers None
Integrated into Swiss-Prot on November 1, 1995
Sequence was last modified on November 1, 1995 (Sequence version 1)
Annotations were last modified on    June 10, 2008 (Entry version 93)
Name and origin of the protein
Protein name Cathepsin K [Precursor]
Synonyms EC 3.4.22.38
Cathepsin O
Cathepsin X
Cathepsin O2
Gene name
Name: CTSK
Synonyms: CTSO, CTSO2
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Blood;
DOI=10.1016/0014-5793(94)01349-6; PubMed=7805878 [NCBI, ExPASy, EBI, Israel, Japan]
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;
DOI=10.1006/bbrc.1995.1013; PubMed=7818555 [NCBI, ExPASy, EBI, Israel, Japan]
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 [NCBI, ExPASy, EBI, Israel, Japan]
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 [NCBI, ExPASy, EBI, Israel, Japan]
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].
TISSUE=Skin;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[6]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
DOI=10.1038/nsb0297-105; PubMed=9033587 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[7]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
DOI=10.1073/pnas.94.26.14249; PubMed=9405598 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[8]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF ZYMOGEN FORM.
DOI=10.1021/bi9822271; PubMed=9893980 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[9]
X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS).
PubMed=10048321 [NCBI, ExPASy, EBI, Israel, Japan]
Sivaraman J., Lalumiere M., Menard R., Cygler M.;
"Crystal structure of wild-type human procathepsin K.";
Protein Sci. 8:283-290(1999).
[10]
VARIANT PKND ARG-146.
PubMed=8703060 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[11]
VARIANT PKND VAL-277.
DOI=10.1086/301795; PubMed=9529353 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[12]
VARIANT PKND GLU-79.
PubMed=10491211 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[13]
VARIANTS PKND GLU-79 AND PRO-309.
DOI=10.1038/sj.ejhg.5200481; PubMed=10878663 [NCBI, ExPASy, EBI, Israel, Japan]
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).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
U13665; AAA65233.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X82153; CAA57649.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U20280; AAA95998.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
S79895; AAB35521.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC016058; AAH16058.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR JC2476; JC2476.
RefSeq NP_000387.1; -.
UniGene Hs.632466
3D structure databases
PDB
1ATK; X-ray; 2.20 A; A=115-329.[ExPASy / RCSB / EBI]
1AU0; X-ray; 2.60 A; A=115-329.[ExPASy / RCSB / EBI]
1AU2; X-ray; 2.60 A; A=115-329.[ExPASy / RCSB / EBI]
1AU3; X-ray; 2.50 A; A=115-329.[ExPASy / RCSB / EBI]
1AU4; X-ray; 2.30 A; A=115-329.[ExPASy / RCSB / EBI]
1AYU; X-ray; 2.20 A; A=115-329.[ExPASy / RCSB / EBI]
1AYV; X-ray; 2.30 A; A=115-329.[ExPASy / RCSB / EBI]
1AYW; X-ray; 2.40 A; A=115-329.[ExPASy / RCSB / EBI]
1BGO; X-ray; 2.30 A; A=115-329.[ExPASy / RCSB / EBI]
1BY8; X-ray; 2.60 A; A=16-329.[ExPASy / RCSB / EBI]
1MEM; X-ray; 1.80 A; A=115-329.[ExPASy / RCSB / EBI]
1NL6; X-ray; 2.80 A; A/B=115-329.[ExPASy / RCSB / EBI]
1NLJ; X-ray; 2.40 A; A/B=115-329.[ExPASy / RCSB / EBI]
1Q6K; X-ray; 2.10 A; A=115-329.[ExPASy / RCSB / EBI]
1SNK; X-ray; 2.40 A; A=116-329.[ExPASy / RCSB / EBI]
1TU6; X-ray; 1.75 A; A/B=115-329.[ExPASy / RCSB / EBI]
1U9V; X-ray; 2.20 A; A=113-329.[ExPASy / RCSB / EBI]
1U9W; X-ray; 2.30 A; A=113-329.[ExPASy / RCSB / EBI]
1U9X; X-ray; 2.10 A; A=113-329.[ExPASy / RCSB / EBI]
1VSN; X-ray; 2.00 A; A=115-329.[ExPASy / RCSB / EBI]
1YK7; X-ray; 2.50 A; A=115-329.[ExPASy / RCSB / EBI]
1YK8; X-ray; 2.60 A; A=115-329.[ExPASy / RCSB / EBI]
1YT7; X-ray; 2.30 A; A=115-329.[ExPASy / RCSB / EBI]
2ATO; X-ray; 2.00 A; A=115-329.[ExPASy / RCSB / EBI]
2AUX; X-ray; 2.40 A; A=115-329.[ExPASy / RCSB / EBI]
2AUZ; X-ray; 2.30 A; A=115-329.[ExPASy / RCSB / EBI]
2BDL; X-ray; 2.00 A; A=115-329.[ExPASy / RCSB / EBI]
2R6N; X-ray; 1.95 A; A=113-329.[ExPASy / RCSB / EBI]
7PCK; X-ray; 3.20 A; A/B/C/D=16-329.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1ATK; -.
1AU0; -.
1AU2; -.
1AU3; -.
1AU4; -.
1AYU; -.
1AYV; -.
1AYW; -.
1BGO; -.
1BY8; -.
1MEM; -.
1NL6; -.
1NLJ; -.
1Q6K; -.
1SNK; -.
1TU6; -.
1U9V; -.
1U9W; -.
1U9X; -.
1VSN; -.
1YK7; -.
1YK8; -.
1YT7; -.
2ATO; -.
2AUX; -.
2AUZ; -.
2BDL; -.
2R6N; -.
7PCK; -.
ModBase P43235.
Protein-protein interaction databases
IntAct P43235; -.
Protein family/group databases
MEROPS C01.036; -.
I29.007; -.
PTM databases
PhosphoSite P43235; -.
Organism-specific databases
H-InvDB HIX0001036; -.
HGNC HGNC:2536; CTSK.
GeneLynx CTSK; Homo sapiens.
GenAtlas CTSK.
MIM 265800; phenotype. [NCBI / EBI]
601105; gene. [NCBI / EBI]
Orphanet 763; Pycnodysostosis.
PharmGKB PA27034; -.
GeneCards P43235.
Gene expression databases
ArrayExpress P43235; -.
CleanEx HS_CTSK; -.
HS_CTSO; -.
GermOnline ENSG00000143387; Homo sapiens.
Ontologies
GO
GO:0004216; Molecular function: cathepsin K activity (traceable author statement from ProtInc).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0006508; Biological process: proteolysis (traceable author statement from ProtInc).
QuickGo view.
Family and domain databases
InterPro IPR000169; Pept_cys_AS.
IPR013128; Peptidase_C1A.
IPR000668; Peptidase_C1A_C.
IPR015644; Peptidase_C1A_cathepsin-K.
IPR013201; Prot_inhib_I29.
Graphical view of domain structure.
PANTHER PTHR12411:SF55; CathpsnK_like; 1.
PTHR12411; Peptidase_C1A; 1.
Pfam PF08246; Inhibitor_I29; 1.
PF00112; Peptidase_C1; 1.
Pfam graphical view of domain structure.
PRINTS PR00705; PAPAIN.
ProDom PD000158; Peptidase_C1; 1.
[Domain structure / List of seq. sharing at least 1 domain]
SMART SM00645; Pept_C1; 1.
SMART graphical view of domain structure.
PROSITE PS00640; THIOL_PROTEASE_ASN; 1.
PS00139; THIOL_PROTEASE_CYS; 1.
PS00639; THIOL_PROTEASE_HIS; 1.
BLOCKS P43235.
Genome annotation databases
Ensembl ENSG00000143387; Homo sapiens. [Contig view]
GeneID 1513; -.
KEGG hsa:1513; -.
Phylogenomic databases
HOVERGEN P43235; -.
Other
LinkHub P43235; -.
SOURCE CTSK; Homo sapiens.
ProtoNet P43235.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Disease mutation; Glycoprotein; Hydrolase; Lysosome; Protease; Signal; Thiol protease; Zymogen.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
SIGNAL   1    15  15     Potential. 
PROPEP   16   114  99     Activation peptide. PRO_0000026295
CHAIN   115   329  215     Cathepsin K. PRO_0000026296
ACT_SITE   139   139        By similarity. 
ACT_SITE   276   276        By similarity. 
ACT_SITE   296   296        By similarity. 
CARBOHYD   103   103        N-linked (GlcNAc...) (Potential). 
DISULFID   136   177         
DISULFID   170   210         
DISULFID   269   318         
VARIANT   79    79  1     G -> E (in PKND). VAR_015738 
VARIANT   146   146  1     G -> R (in PKND). VAR_006725 [3D]
VARIANT   277   277  1     A -> V (in PKND). VAR_015739 [3D]
VARIANT   309   309  1     L -> P (in PKND). VAR_006726 [3D]
CONFLICT   46    46        R -> P (in Ref. 3; AAA95998). 
HELIX   22    32  11      
HELIX   40    66  27      
STRAND   70    73  4      
STRAND   79    81  3      
HELIX   83    89  7      
STRAND   102   107  6      
TURN   121   125  5      
HELIX   139   156  18      
HELIX   164   170  7      
HELIX   182   192  11      
STRAND   195   197  3      
TURN   198   200  3      
HELIX   214   216  3      
STRAND   217   219  3      
STRAND   224   226  3      
HELIX   232   241  10      
STRAND   245   249  5      
HELIX   254   257  4      
STRAND   261   264  4      
STRAND   276   288  13      
STRAND   290   295  6      
STRAND   307   316  10      
HELIX   317   319  3      
TURN   320   322  3      
STRAND   325   327  3      
Sequence information
Length: 329 AA [This is the length of the unprocessed precursor] Molecular weight: 36966 Da [This is the MW of the unprocessed precursor] CRC64: 4677C3C89FF4CE85 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MWGLKVLLLP VVSFALYPEE ILDTHWELWK KTHRKQYNNK VDEISRRLIW EKNLKYISIH 

        70         80         90        100        110        120 
NLEASLGVHT YELAMNHLGD MTSEEVVQKM TGLKVPLSHS RSNDTLYIPE WEGRAPDSVD 

       130        140        150        160        170        180 
YRKKGYVTPV KNQGQCGSCW AFSSVGALEG QLKKKTGKLL NLSPQNLVDC VSENDGCGGG 

       190        200        210        220        230        240 
YMTNAFQYVQ KNRGIDSEDA YPYVGQEESC MYNPTGKAAK CRGYREIPEG NEKALKRAVA 

       250        260        270        280        290        300 
RVGPVSVAID ASLTSFQFYS KGVYYDESCN SDNLNHAVLA VGYGIQKGNK HWIIKNSWGE 

       310        320 
NWGNKGYILM ARNKNNACGI ANLASFPKM 

P43235 in FASTA format

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BLAST logo BLAST submission on ExPASy/SIB
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Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
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