| UniProt ID | KLK5_HUMAN | |
|---|---|---|
| UniProt AC | Q9Y337 | |
| Protein Name | Kallikrein-5 {ECO:0000312|HGNC:HGNC:6366} | |
| Gene Name | KLK5 {ECO:0000312|HGNC:HGNC:6366} | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 293 | |
| Subcellular Localization | Secreted. | |
| Protein Description | May be involved in desquamation.. | |
| Protein Sequence | MATARPPWMWVLCALITALLLGVTEHVLANNDVSCDHPSNTVPSGSNQDLGAGAGEDARSDDSSSRIINGSDCDMHTQPWQAALLLRPNQLYCGAVLVHPQWLLTAAHCRKKVFRVRLGHYSLSPVYESGQQMFQGVKSIPHPGYSHPGHSNDLMLIKLNRRIRPTKDVRPINVSSHCPSAGTKCLVSGWGTTKSPQVHFPKVLQCLNISVLSQKRCEDAYPRQIDDTMFCAGDKAGRDSCQGDSGGPVVCNGSLQGLVSWGDYPCARPNRPGVYTNLCKFTKWIQETIQANS | |
| 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 |
|---|---|---|---|---|---|
| 46 | Phosphorylation | SNTVPSGSNQDLGAG CCCCCCCCCCCCCCC | 35.34 | 24505115 | |
| 69 | N-linked_Glycosylation | DSSSRIINGSDCDMH CCCCCEECCCCCCCC | 41.36 | UniProtKB CARBOHYD | |
| 173 | N-linked_Glycosylation | TKDVRPINVSSHCPS CCCCCCCCCCCCCCC | 30.24 | UniProtKB CARBOHYD | |
| 188 | Phosphorylation | AGTKCLVSGWGTTKS CCCEEEEECCCCCCC | 18.84 | 20639409 | |
| 192 | Phosphorylation | CLVSGWGTTKSPQVH EEEECCCCCCCCCCC | 25.25 | 20639409 | |
| 193 | Phosphorylation | LVSGWGTTKSPQVHF EEECCCCCCCCCCCH | 26.11 | 20639409 | |
| 195 | Phosphorylation | SGWGTTKSPQVHFPK ECCCCCCCCCCCHHH | 20.62 | 20639409 | |
| 208 | N-linked_Glycosylation | PKVLQCLNISVLSQK HHHHHHHCHHHHCCC | 31.92 | 17881000 | |
| 213 | Phosphorylation | CLNISVLSQKRCEDA HHCHHHHCCCCCCCC | 31.34 | - | |
| 252 | N-linked_Glycosylation | SGGPVVCNGSLQGLV CCCCEEECCCEECEE | 31.32 | UniProtKB CARBOHYD |
| 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 KLK5_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of KLK5_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 KLK5_HUMAN !! | ||||||
| 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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| N-linked Glycosylation | |
| Reference | PubMed |
| "Structural basis of the zinc inhibition of human tissue kallikrein5."; Debela M., Goettig P., Magdolen V., Huber R., Schechter N.M., Bode W.; J. Mol. Biol. 373:1017-1031(2007). Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 67-293 ALONE AND IN COMPLEXWITH ZINC, ENZYME REGULATION, ACTIVE SITE, GLYCOSYLATION AT ASN-208,AND DISULFIDE BONDS. | |