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P43235

- CATK_HUMAN

UniProt

P43235 - CATK_HUMAN

Protein

Cathepsin K

Gene

CTSK

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 155 (01 Oct 2014)
      Sequence version 1 (01 Nov 1995)
      Previous versions | rss
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    Functioni

    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 activityi

    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.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei139 – 1391By similarity
    Active sitei276 – 2761By similarity
    Active sitei296 – 2961By similarity

    GO - Molecular functioni

    1. collagen binding Source: BHF-UCL
    2. cysteine-type endopeptidase activity Source: BHF-UCL
    3. cysteine-type peptidase activity Source: ProtInc
    4. fibronectin binding Source: BHF-UCL
    5. proteoglycan binding Source: BHF-UCL

    GO - Biological processi

    1. bone resorption Source: Ensembl
    2. collagen catabolic process Source: BHF-UCL
    3. extracellular matrix disassembly Source: Reactome
    4. extracellular matrix organization Source: Reactome
    5. innate immune response Source: Reactome
    6. intramembranous ossification Source: Ensembl
    7. proteolysis Source: ProtInc
    8. proteolysis involved in cellular protein catabolic process Source: BHF-UCL
    9. toll-like receptor signaling pathway Source: Reactome

    Keywords - Molecular functioni

    Hydrolase, Protease, Thiol protease

    Enzyme and pathway databases

    ReactomeiREACT_118572. Degradation of the extracellular matrix.
    REACT_118632. Trafficking and processing of endosomal TLR.
    REACT_118682. Activation of Matrix Metalloproteinases.
    REACT_121399. MHC class II antigen presentation.
    REACT_150401. Collagen degradation.

    Protein family/group databases

    MEROPSiC01.036.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cathepsin K (EC:3.4.22.38)
    Alternative name(s):
    Cathepsin O
    Cathepsin O2
    Cathepsin X
    Gene namesi
    Name:CTSK
    Synonyms:CTSO, CTSO2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:2536. CTSK.

    Subcellular locationi

    GO - Cellular componenti

    1. endolysosome lumen Source: Reactome
    2. extracellular region Source: Reactome
    3. extracellular space Source: BHF-UCL

    Keywords - Cellular componenti

    Lysosome

    Pathology & Biotechi

    Involvement in diseasei

    Pycnodysostosis (PKND) [MIM:265800]: A rare autosomal recessive bone disorder characterized by deformity of the skull, maxilla and phalanges, osteosclerosis, and fragility of bone.4 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti79 – 791G → E in PKND. 2 Publications
    VAR_015738
    Natural varianti146 – 1461G → R in PKND. 1 Publication
    VAR_006725
    Natural varianti277 – 2771A → V in PKND. 1 Publication
    VAR_015739
    Natural varianti309 – 3091L → P in PKND. 1 Publication
    Corresponds to variant rs29001685 [ dbSNP | Ensembl ].
    VAR_006726

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi265800. phenotype.
    Orphaneti763. Pycnodysostosis.
    PharmGKBiPA27034.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1515Sequence AnalysisAdd
    BLAST
    Propeptidei16 – 11499Activation peptidePRO_0000026295Add
    BLAST
    Chaini115 – 329215Cathepsin KPRO_0000026296Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi103 – 1031N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi136 ↔ 177
    Disulfide bondi170 ↔ 210
    Disulfide bondi269 ↔ 318

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Zymogen

    Proteomic databases

    PaxDbiP43235.
    PRIDEiP43235.

    PTM databases

    PhosphoSiteiP43235.

    Expressioni

    Tissue specificityi

    Predominantly expressed in osteoclasts (bones).

    Gene expression databases

    ArrayExpressiP43235.
    BgeeiP43235.
    CleanExiHS_CTSK.
    HS_CTSO.
    GenevestigatoriP43235.

    Interactioni

    Protein-protein interaction databases

    BioGridi107893. 3 interactions.
    DIPiDIP-39993N.
    IntActiP43235. 3 interactions.
    STRINGi9606.ENSP00000271651.

    Structurei

    Secondary structure

    1
    329
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi22 – 3211
    Helixi40 – 6627
    Beta strandi70 – 734
    Beta strandi79 – 813
    Helixi83 – 897
    Beta strandi102 – 1076
    Turni121 – 1255
    Beta strandi135 – 1373
    Helixi139 – 15618
    Helixi164 – 1707
    Beta strandi172 – 1743
    Helixi176 – 1783
    Helixi182 – 19211
    Beta strandi195 – 1973
    Turni198 – 2003
    Helixi214 – 2163
    Beta strandi217 – 2193
    Beta strandi224 – 2263
    Helixi232 – 24110
    Beta strandi245 – 2495
    Helixi254 – 2574
    Beta strandi261 – 2644
    Beta strandi276 – 28611
    Beta strandi289 – 2957
    Beta strandi300 – 3023
    Turni303 – 3053
    Beta strandi307 – 31610
    Helixi317 – 3193
    Turni320 – 3223
    Beta strandi325 – 3273

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1ATKX-ray2.20A115-329[»]
    1AU0X-ray2.60A115-329[»]
    1AU2X-ray2.60A115-329[»]
    1AU3X-ray2.50A115-329[»]
    1AU4X-ray2.30A115-329[»]
    1AYUX-ray2.20A115-329[»]
    1AYVX-ray2.30A115-329[»]
    1AYWX-ray2.40A115-329[»]
    1BGOX-ray2.30A115-329[»]
    1BY8X-ray2.60A16-329[»]
    1MEMX-ray1.80A115-329[»]
    1NL6X-ray2.80A/B115-329[»]
    1NLJX-ray2.40A/B115-329[»]
    1Q6KX-ray2.10A115-329[»]
    1SNKX-ray2.40A116-329[»]
    1TU6X-ray1.75A/B115-329[»]
    1U9VX-ray2.20A113-329[»]
    1U9WX-ray2.30A113-329[»]
    1U9XX-ray2.10A113-329[»]
    1VSNX-ray2.00A115-329[»]
    1YK7X-ray2.50A115-329[»]
    1YK8X-ray2.60A115-329[»]
    1YT7X-ray2.30A115-329[»]
    2ATOX-ray2.00A115-329[»]
    2AUXX-ray2.40A115-329[»]
    2AUZX-ray2.30A115-329[»]
    2BDLX-ray2.00A115-329[»]
    2R6NX-ray1.95A113-329[»]
    3C9EX-ray1.80A115-329[»]
    3H7DX-ray2.24A/E115-329[»]
    3KW9X-ray1.80A115-329[»]
    3KWBX-ray2.02X/Y115-329[»]
    3KWZX-ray1.49A115-329[»]
    3KX1X-ray1.51A115-329[»]
    3O0UX-ray1.80A115-329[»]
    3O1GX-ray1.65A115-329[»]
    3OVZX-ray2.02A121-329[»]
    4DMXX-ray1.70A115-329[»]
    4DMYX-ray1.63A/B115-329[»]
    4LEGX-ray2.60A107-329[»]
    7PCKX-ray3.20A/B/C/D16-329[»]
    ProteinModelPortaliP43235.
    SMRiP43235. Positions 16-329.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP43235.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase C1 family.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG4870.
    HOGENOMiHOG000230774.
    HOVERGENiHBG011513.
    InParanoidiP43235.
    KOiK01371.
    OMAiILDTQWE.
    OrthoDBiEOG786H3P.
    PhylomeDBiP43235.
    TreeFamiTF313739.

    Family and domain databases

    InterProiIPR025661. Pept_asp_AS.
    IPR000169. Pept_cys_AS.
    IPR025660. Pept_his_AS.
    IPR013128. Peptidase_C1A.
    IPR000668. Peptidase_C1A_C.
    IPR015644. Peptidase_C1A_cathepsin-K.
    IPR013201. Prot_inhib_I29.
    [Graphical view]
    PANTHERiPTHR12411. PTHR12411. 1 hit.
    PTHR12411:SF55. PTHR12411:SF55. 1 hit.
    PfamiPF08246. Inhibitor_I29. 1 hit.
    PF00112. Peptidase_C1. 1 hit.
    [Graphical view]
    PRINTSiPR00705. PAPAIN.
    SMARTiSM00848. Inhibitor_I29. 1 hit.
    SM00645. Pept_C1. 1 hit.
    [Graphical view]
    PROSITEiPS00640. THIOL_PROTEASE_ASN. 1 hit.
    PS00139. THIOL_PROTEASE_CYS. 1 hit.
    PS00639. THIOL_PROTEASE_HIS. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P43235-1 [UniParc]FASTAAdd to Basket

    « Hide

    MWGLKVLLLP VVSFALYPEE ILDTHWELWK KTHRKQYNNK VDEISRRLIW    50
    EKNLKYISIH NLEASLGVHT YELAMNHLGD MTSEEVVQKM TGLKVPLSHS 100
    RSNDTLYIPE WEGRAPDSVD YRKKGYVTPV KNQGQCGSCW AFSSVGALEG 150
    QLKKKTGKLL NLSPQNLVDC VSENDGCGGG YMTNAFQYVQ KNRGIDSEDA 200
    YPYVGQEESC MYNPTGKAAK CRGYREIPEG NEKALKRAVA RVGPVSVAID 250
    ASLTSFQFYS KGVYYDESCN SDNLNHAVLA VGYGIQKGNK HWIIKNSWGE 300
    NWGNKGYILM ARNKNNACGI ANLASFPKM 329
    Length:329
    Mass (Da):36,966
    Last modified:November 1, 1995 - v1
    Checksum:i4677C3C89FF4CE85
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti46 – 461R → P in AAA95998. (PubMed:8585423)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti79 – 791G → E in PKND. 2 Publications
    VAR_015738
    Natural varianti146 – 1461G → R in PKND. 1 Publication
    VAR_006725
    Natural varianti277 – 2771A → V in PKND. 1 Publication
    VAR_015739
    Natural varianti309 – 3091L → P in PKND. 1 Publication
    Corresponds to variant rs29001685 [ dbSNP | Ensembl ].
    VAR_006726

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U13665 mRNA. Translation: AAA65233.1.
    X82153 mRNA. Translation: CAA57649.1.
    U20280 mRNA. Translation: AAA95998.1.
    S79895 mRNA. Translation: AAB35521.1.
    CR541675 mRNA. Translation: CAG46476.1.
    AL355860, AL356292 Genomic DNA. Translation: CAI12795.1.
    AL356292, AL355860 Genomic DNA. Translation: CAI13649.1.
    CH471121 Genomic DNA. Translation: EAW53516.1.
    BC016058 mRNA. Translation: AAH16058.1.
    CCDSiCCDS969.1.
    PIRiJC2476.
    RefSeqiNP_000387.1. NM_000396.3.
    UniGeneiHs.632466.

    Genome annotation databases

    EnsembliENST00000271651; ENSP00000271651; ENSG00000143387.
    GeneIDi1513.
    KEGGihsa:1513.
    UCSCiuc001evp.2. human.

    Polymorphism databases

    DMDMi1168793.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U13665 mRNA. Translation: AAA65233.1 .
    X82153 mRNA. Translation: CAA57649.1 .
    U20280 mRNA. Translation: AAA95998.1 .
    S79895 mRNA. Translation: AAB35521.1 .
    CR541675 mRNA. Translation: CAG46476.1 .
    AL355860 , AL356292 Genomic DNA. Translation: CAI12795.1 .
    AL356292 , AL355860 Genomic DNA. Translation: CAI13649.1 .
    CH471121 Genomic DNA. Translation: EAW53516.1 .
    BC016058 mRNA. Translation: AAH16058.1 .
    CCDSi CCDS969.1.
    PIRi JC2476.
    RefSeqi NP_000387.1. NM_000396.3.
    UniGenei Hs.632466.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1ATK X-ray 2.20 A 115-329 [» ]
    1AU0 X-ray 2.60 A 115-329 [» ]
    1AU2 X-ray 2.60 A 115-329 [» ]
    1AU3 X-ray 2.50 A 115-329 [» ]
    1AU4 X-ray 2.30 A 115-329 [» ]
    1AYU X-ray 2.20 A 115-329 [» ]
    1AYV X-ray 2.30 A 115-329 [» ]
    1AYW X-ray 2.40 A 115-329 [» ]
    1BGO X-ray 2.30 A 115-329 [» ]
    1BY8 X-ray 2.60 A 16-329 [» ]
    1MEM X-ray 1.80 A 115-329 [» ]
    1NL6 X-ray 2.80 A/B 115-329 [» ]
    1NLJ X-ray 2.40 A/B 115-329 [» ]
    1Q6K X-ray 2.10 A 115-329 [» ]
    1SNK X-ray 2.40 A 116-329 [» ]
    1TU6 X-ray 1.75 A/B 115-329 [» ]
    1U9V X-ray 2.20 A 113-329 [» ]
    1U9W X-ray 2.30 A 113-329 [» ]
    1U9X X-ray 2.10 A 113-329 [» ]
    1VSN X-ray 2.00 A 115-329 [» ]
    1YK7 X-ray 2.50 A 115-329 [» ]
    1YK8 X-ray 2.60 A 115-329 [» ]
    1YT7 X-ray 2.30 A 115-329 [» ]
    2ATO X-ray 2.00 A 115-329 [» ]
    2AUX X-ray 2.40 A 115-329 [» ]
    2AUZ X-ray 2.30 A 115-329 [» ]
    2BDL X-ray 2.00 A 115-329 [» ]
    2R6N X-ray 1.95 A 113-329 [» ]
    3C9E X-ray 1.80 A 115-329 [» ]
    3H7D X-ray 2.24 A/E 115-329 [» ]
    3KW9 X-ray 1.80 A 115-329 [» ]
    3KWB X-ray 2.02 X/Y 115-329 [» ]
    3KWZ X-ray 1.49 A 115-329 [» ]
    3KX1 X-ray 1.51 A 115-329 [» ]
    3O0U X-ray 1.80 A 115-329 [» ]
    3O1G X-ray 1.65 A 115-329 [» ]
    3OVZ X-ray 2.02 A 121-329 [» ]
    4DMX X-ray 1.70 A 115-329 [» ]
    4DMY X-ray 1.63 A/B 115-329 [» ]
    4LEG X-ray 2.60 A 107-329 [» ]
    7PCK X-ray 3.20 A/B/C/D 16-329 [» ]
    ProteinModelPortali P43235.
    SMRi P43235. Positions 16-329.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107893. 3 interactions.
    DIPi DIP-39993N.
    IntActi P43235. 3 interactions.
    STRINGi 9606.ENSP00000271651.

    Chemistry

    BindingDBi P43235.
    ChEMBLi CHEMBL2111361.
    GuidetoPHARMACOLOGYi 2350.

    Protein family/group databases

    MEROPSi C01.036.

    PTM databases

    PhosphoSitei P43235.

    Polymorphism databases

    DMDMi 1168793.

    Proteomic databases

    PaxDbi P43235.
    PRIDEi P43235.

    Protocols and materials databases

    DNASUi 1513.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000271651 ; ENSP00000271651 ; ENSG00000143387 .
    GeneIDi 1513.
    KEGGi hsa:1513.
    UCSCi uc001evp.2. human.

    Organism-specific databases

    CTDi 1513.
    GeneCardsi GC01M150768.
    HGNCi HGNC:2536. CTSK.
    MIMi 265800. phenotype.
    601105. gene.
    neXtProti NX_P43235.
    Orphaneti 763. Pycnodysostosis.
    PharmGKBi PA27034.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG4870.
    HOGENOMi HOG000230774.
    HOVERGENi HBG011513.
    InParanoidi P43235.
    KOi K01371.
    OMAi ILDTQWE.
    OrthoDBi EOG786H3P.
    PhylomeDBi P43235.
    TreeFami TF313739.

    Enzyme and pathway databases

    Reactomei REACT_118572. Degradation of the extracellular matrix.
    REACT_118632. Trafficking and processing of endosomal TLR.
    REACT_118682. Activation of Matrix Metalloproteinases.
    REACT_121399. MHC class II antigen presentation.
    REACT_150401. Collagen degradation.

    Miscellaneous databases

    EvolutionaryTracei P43235.
    GeneWikii Cathepsin_K.
    GenomeRNAii 1513.
    NextBioi 6267.
    PROi P43235.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P43235.
    Bgeei P43235.
    CleanExi HS_CTSK.
    HS_CTSO.
    Genevestigatori P43235.

    Family and domain databases

    InterProi IPR025661. Pept_asp_AS.
    IPR000169. Pept_cys_AS.
    IPR025660. Pept_his_AS.
    IPR013128. Peptidase_C1A.
    IPR000668. Peptidase_C1A_C.
    IPR015644. Peptidase_C1A_cathepsin-K.
    IPR013201. Prot_inhib_I29.
    [Graphical view ]
    PANTHERi PTHR12411. PTHR12411. 1 hit.
    PTHR12411:SF55. PTHR12411:SF55. 1 hit.
    Pfami PF08246. Inhibitor_I29. 1 hit.
    PF00112. Peptidase_C1. 1 hit.
    [Graphical view ]
    PRINTSi PR00705. PAPAIN.
    SMARTi SM00848. Inhibitor_I29. 1 hit.
    SM00645. Pept_C1. 1 hit.
    [Graphical view ]
    PROSITEi PS00640. THIOL_PROTEASE_ASN. 1 hit.
    PS00139. THIOL_PROTEASE_CYS. 1 hit.
    PS00639. THIOL_PROTEASE_HIS. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning of human cathepsin O, a novel endoproteinase and homologue of rabbit OC2."
      Shi G.-P., Chapman H.A., Bhairi S.M., Deleeuw C., Reddy V.Y., Weiss S.J.
      FEBS Lett. 357:129-134(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Blood.
    2. "Molecular cloning of human cDNA for cathepsin K: novel cysteine proteinase predominantly expressed in bone."
      Inaoka T., Bilbe G., Ishibashi O., Tezuka K., Kumegawa M., Kokubo T.
      Biochem. Biophys. Res. Commun. 206:89-96(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Bone.
    3. "Cloning and complete coding sequence of a novel human cathepsin expressed in giant cells of osteoclastomas."
      Li Y., Alexander M., Wucherpfennig A.L., Yelick P., Chen W., Stashenko P.
      J. Bone Miner. Res. 10:1197-1202(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Osteoclastoma.
    4. "Human cathepsin O2, a novel cysteine protease highly expressed in osteoclastomas and ovary molecular cloning, sequencing and tissue distribution."
      Broemme D., Okamoto K.
      Biol. Chem. Hoppe-Seyler 376:379-384(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Spleen.
    5. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    6. "The DNA sequence and biological annotation of human chromosome 1."
      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.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Skin.
    9. "Crystal structure of human cathepsin K complexed with a potent inhibitor."
      McGrath M.E., Klaus J.L., Barnes M.G., Bromme D.
      Nat. Struct. Biol. 4:105-109(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
    10. Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
    11. Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF ZYMOGEN FORM.
    12. "Crystal structure of wild-type human procathepsin K."
      Sivaraman J., Lalumiere M., Menard R., Cygler M.
      Protein Sci. 8:283-290(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS).
    13. "Pycnodysostosis, a lysosomal disease caused by cathepsin K deficiency."
      Gelb B.D., Shi G.-P., Chapman H.A., Desnick R.J.
      Science 273:1236-1238(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT PKND ARG-146.
    14. "Paternal uniparental disomy for chromosome 1 revealed by molecular analysis of a patient with pycnodysostosis."
      Gelb B.D., Willner J.P., Dunn T.M., Kardon N.B., Verloes A., Poncin J., Desnick R.J.
      Am. J. Hum. Genet. 62:848-854(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT PKND VAL-277.
    15. "Mutations of CTSK result in pycnodysostosis via a reduction in cathepsin K protein."
      Ho N., Punturieri A., Wilkin D., Szabo J., Johnson M., Whaley J., Davis J., Clark A., Weiss S., Francomano C.
      J. Bone Miner. Res. 14:1649-1653(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT PKND GLU-79.
    16. "Cathepsin K gene mutations and 1q21 haplotypes in at patients with pycnodysostosis in an outbred population."
      Haagerup A., Hertz J.M., Christensen M.F., Binderup H., Kruse T.A.
      Eur. J. Hum. Genet. 8:431-436(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS PKND GLU-79 AND PRO-309.

    Entry informationi

    Entry nameiCATK_HUMAN
    AccessioniPrimary (citable) accession number: P43235
    Secondary accession number(s): Q6FHS6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: November 1, 1995
    Last modified: October 1, 2014
    This is version 155 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. Peptidase families
      Classification of peptidase families and list of entries
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3