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P43235

- CATK_HUMAN

UniProt

P43235 - CATK_HUMAN

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Protein

Cathepsin K

Gene

CTSK

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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
Complete GO annotation...

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
Complete GO annotation...

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

BgeeiP43235.
CleanExiHS_CTSK.
HS_CTSO.
ExpressionAtlasiP43235. baseline and differential.
GenevestigatoriP43235.

Interactioni

Protein-protein interaction databases

BioGridi107893. 7 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.
GeneTreeiENSGT00760000118871.
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

        10         20         30         40         50
MWGLKVLLLP VVSFALYPEE ILDTHWELWK KTHRKQYNNK VDEISRRLIW
60 70 80 90 100
EKNLKYISIH NLEASLGVHT YELAMNHLGD MTSEEVVQKM TGLKVPLSHS
110 120 130 140 150
RSNDTLYIPE WEGRAPDSVD YRKKGYVTPV KNQGQCGSCW AFSSVGALEG
160 170 180 190 200
QLKKKTGKLL NLSPQNLVDC VSENDGCGGG YMTNAFQYVQ KNRGIDSEDA
210 220 230 240 250
YPYVGQEESC MYNPTGKAAK CRGYREIPEG NEKALKRAVA RVGPVSVAID
260 270 280 290 300
ASLTSFQFYS KGVYYDESCN SDNLNHAVLA VGYGIQKGNK HWIIKNSWGE
310 320
NWGNKGYILM ARNKNNACGI ANLASFPKM
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. 7 interactions.
DIPi DIP-39993N.
IntActi P43235. 3 interactions.
STRINGi 9606.ENSP00000271651.

Chemistry

BindingDBi P43235.
ChEMBLi CHEMBL2111441.
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.
GeneTreei ENSGT00760000118871.
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

Bgeei P43235.
CleanExi HS_CTSK.
HS_CTSO.
ExpressionAtlasi P43235. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 156 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