P43235 · CATK_HUMAN
- ProteinCathepsin K
- GeneCTSK
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids329 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Thiol protease 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. Involved in the release of thyroid hormone thyroxine (T4) by limited proteolysis of TG/thyroglobulin in the thyroid follicle lumen (PubMed:11082042).
Catalytic activity
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 139 | |||||
Sequence: C | ||||||
Active site | 276 | |||||
Sequence: H | ||||||
Active site | 296 | |||||
Sequence: N |
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Keywords
- Molecular function
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameCathepsin K
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionP43235
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Apical cell membrane ; Peripheral membrane protein
Note: Localizes to the lumen of thyroid follicles and to the apical membrane of thyroid epithelial cells.
Keywords
- Cellular component
Disease & Variants
Involvement in disease
Pycnodysostosis (PKND)
- Note
- DescriptionA rare autosomal recessive bone disorder characterized by deformity of the skull, maxilla and phalanges, osteosclerosis, and fragility of bone.
- See alsoMIM:265800
Natural variants in PKND
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_015738 | 79 | G>E | in PKND; dbSNP:rs74315305 | |
VAR_074023 | 122 | R>P | in PKND | |
VAR_006725 | 146 | G>R | in PKND; dbSNP:rs74315302 | |
VAR_015739 | 277 | A>V | in PKND; dbSNP:rs74315304 | |
VAR_074024 | 283 | Y>C | in PKND; does not affect protein level; does not detect cysteine-type endopeptidase activity | |
VAR_006726 | 309 | L>P | in PKND; dbSNP:rs29001685 |
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_015738 | 79 | in PKND; dbSNP:rs74315305 | |||
Sequence: G → E | ||||||
Natural variant | VAR_074023 | 122 | in PKND | |||
Sequence: R → P | ||||||
Natural variant | VAR_006725 | 146 | in PKND; dbSNP:rs74315302 | |||
Sequence: G → R | ||||||
Natural variant | VAR_015739 | 277 | in PKND; dbSNP:rs74315304 | |||
Sequence: A → V | ||||||
Natural variant | VAR_074024 | 283 | in PKND; does not affect protein level; does not detect cysteine-type endopeptidase activity | |||
Sequence: Y → C | ||||||
Natural variant | VAR_006726 | 309 | in PKND; dbSNP:rs29001685 | |||
Sequence: L → P |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 367 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for signal, propeptide, glycosylation, chain, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-15 | |||||
Sequence: MWGLKVLLLPVVSFA | ||||||
Propeptide | PRO_0000026295 | 16-114 | Activation peptide | |||
Sequence: LYPEEILDTHWELWKKTHRKQYNNKVDEISRRLIWEKNLKYISIHNLEASLGVHTYELAMNHLGDMTSEEVVQKMTGLKVPLSHSRSNDTLYIPEWEGR | ||||||
Glycosylation | 103 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Chain | PRO_0000026296 | 115-329 | Cathepsin K | |||
Sequence: APDSVDYRKKGYVTPVKNQGQCGSCWAFSSVGALEGQLKKKTGKLLNLSPQNLVDCVSENDGCGGGYMTNAFQYVQKNRGIDSEDAYPYVGQEESCMYNPTGKAAKCRGYREIPEGNEKALKRAVARVGPVSVAIDASLTSFQFYSKGVYYDESCNSDNLNHAVLAVGYGIQKGNKHWIIKNSWGENWGNKGYILMARNKNNACGIANLASFPKM | ||||||
Disulfide bond | 136↔177 | |||||
Sequence: CGSCWAFSSVGALEGQLKKKTGKLLNLSPQNLVDCVSENDGC | ||||||
Disulfide bond | 170↔210 | |||||
Sequence: CVSENDGCGGGYMTNAFQYVQKNRGIDSEDAYPYVGQEESC | ||||||
Disulfide bond | 269↔318 | |||||
Sequence: CNSDNLNHAVLAVGYGIQKGNKHWIIKNSWGENWGNKGYILMARNKNNAC |
Keywords
- PTM
Proteomic databases
PTM databases
Structure
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length329
- Mass (Da)36,966
- Last updated1995-11-01 v1
- Checksum4677C3C89FF4CE85
Computationally mapped potential isoform sequences
There are 9 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A7I2YQX0 | A0A7I2YQX0_HUMAN | CTSK | 288 | ||
Q5QP40 | Q5QP40_HUMAN | CTSK | 388 | ||
A0A7I2V2M6 | A0A7I2V2M6_HUMAN | CTSK | 330 | ||
A0A7I2V354 | A0A7I2V354_HUMAN | CTSK | 233 | ||
A0A7I2V4B6 | A0A7I2V4B6_HUMAN | CTSK | 343 | ||
A0A7I2V4B1 | A0A7I2V4B1_HUMAN | CTSK | 333 | ||
A0A7I2V617 | A0A7I2V617_HUMAN | CTSK | 52 | ||
A0A7I2V5Y6 | A0A7I2V5Y6_HUMAN | CTSK | 341 | ||
A0A7I2V5Y9 | A0A7I2V5Y9_HUMAN | CTSK | 256 |
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 46 | in Ref. 3; AAA95998 | ||||
Sequence: R → P |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U13665 EMBL· GenBank· DDBJ | AAA65233.1 EMBL· GenBank· DDBJ | mRNA | ||
X82153 EMBL· GenBank· DDBJ | CAA57649.1 EMBL· GenBank· DDBJ | mRNA | ||
U20280 EMBL· GenBank· DDBJ | AAA95998.1 EMBL· GenBank· DDBJ | mRNA | ||
S79895 EMBL· GenBank· DDBJ | AAB35521.1 EMBL· GenBank· DDBJ | mRNA | ||
CR541675 EMBL· GenBank· DDBJ | CAG46476.1 EMBL· GenBank· DDBJ | mRNA | ||
AL355860 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AL356292 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471121 EMBL· GenBank· DDBJ | EAW53516.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC016058 EMBL· GenBank· DDBJ | AAH16058.1 EMBL· GenBank· DDBJ | mRNA |