| UniProt ID | CASPE_HUMAN | |
|---|---|---|
| UniProt AC | P31944 | |
| Protein Name | Caspase-14 | |
| Gene Name | CASP14 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 242 | |
| Subcellular Localization | Cytoplasm . Nucleus . | |
| Protein Description | Non-apoptotic caspase involved in epidermal differentiation. Is the predominant caspase in epidermal stratum corneum. [PubMed: 15556625 Seems to play a role in keratinocyte differentiation and is required for cornification. Regulates maturation of the epidermis by proteolytically processing filaggrin (By similarity In vitro has a preference for the substrate [WY]-X-X-D motif and is active on the synthetic caspase substrate WEHD-ACF] | |
| Protein Sequence | MSNPRSLEEEKYDMSGARLALILCVTKAREGSEEDLDALEHMFRQLRFESTMKRDPTAEQFQEELEKFQQAIDSREDPVSCAFVVLMAHGREGFLKGEDGEMVKLENLFEALNNKNCQALRAKPKVYIIQACRGEQRDPGETVGGDEIVMVIKDSPQTIPTYTDALHVYSTVEGYIAYRHDQKGSCFIQTLVDVFTKRKGHILELLTEVTRRMAEAELVQEGKARKTNPEIQSTLRKRLYLQ | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 5 | Dimethylation | ---MSNPRSLEEEKY ---CCCCCCHHHHHC | 59.11 | - | |
| 5 | Methylation | ---MSNPRSLEEEKY ---CCCCCCHHHHHC | 59.11 | - | |
| 6 | Phosphorylation | --MSNPRSLEEEKYD --CCCCCCHHHHHCC | 41.19 | 27251275 | |
| 12 | Phosphorylation | RSLEEEKYDMSGARL CCHHHHHCCCCHHHH | 21.84 | 28270605 | |
| 15 | Phosphorylation | EEEKYDMSGARLALI HHHHCCCCHHHHHHH | 26.80 | 28270605 | |
| 155 | Phosphorylation | IVMVIKDSPQTIPTY EEEEEECCCCCCCCC | 17.57 | 24043423 | |
| 158 | Phosphorylation | VIKDSPQTIPTYTDA EEECCCCCCCCCCCC | 32.10 | 24043423 | |
| 161 | Phosphorylation | DSPQTIPTYTDALHV CCCCCCCCCCCCCHH | 34.89 | 24043423 | |
| 162 | Phosphorylation | SPQTIPTYTDALHVY CCCCCCCCCCCCHHE | 9.40 | 24043423 | |
| 163 | Phosphorylation | PQTIPTYTDALHVYS CCCCCCCCCCCHHEE | 19.78 | 24043423 | |
| 169 | Phosphorylation | YTDALHVYSTVEGYI CCCCCHHEEEECEEE | 6.46 | 24043423 | |
| 170 | Phosphorylation | TDALHVYSTVEGYIA CCCCHHEEEECEEEC | 25.53 | 24043423 | |
| 171 | Phosphorylation | DALHVYSTVEGYIAY CCCHHEEEECEEECE | 12.61 | 24043423 | |
| 175 | Phosphorylation | VYSTVEGYIAYRHDQ HEEEECEEECEECCC | 2.94 | 24043423 | |
| 178 | Phosphorylation | TVEGYIAYRHDQKGS EECEEECEECCCCCC | 10.02 | 24043423 | |
| 185 | Phosphorylation | YRHDQKGSCFIQTLV EECCCCCCEEEHHHH | 16.94 | 20068231 | |
| 190 | Phosphorylation | KGSCFIQTLVDVFTK CCCEEEHHHHHHHHC | 24.75 | 20068231 | |
| 196 | Phosphorylation | QTLVDVFTKRKGHIL HHHHHHHHCCCCHHH | 29.77 | 20068231 |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
Oops, there are no upstream regulatory protein records of CASPE_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of CASPE_HUMAN !! | ||||||
* Distance = the distance between SAP position and PTM sites.
| Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
|---|---|---|---|---|---|---|
Oops, there are no SNP-PTM records of CASPE_HUMAN !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| CASP1_HUMAN | CASP1 | physical | 9792675 | |
| CASP2_HUMAN | CASP2 | physical | 9792675 | |
| CASP4_HUMAN | CASP4 | physical | 9792675 | |
| CASP8_HUMAN | CASP8 | physical | 9792675 | |
| CASPA_HUMAN | CASP10 | physical | 9792675 |
| Kegg Disease | ||||||
|---|---|---|---|---|---|---|
| There are no disease associations of PTM sites. | ||||||
| OMIM Disease | ||||||
| There are no disease associations of PTM sites. | ||||||
| Kegg Drug | ||||||
| There are no disease associations of PTM sites. | ||||||
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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