| UniProt ID | PKDCC_HUMAN | |
|---|---|---|
| UniProt AC | Q504Y2 | |
| Protein Name | Extracellular tyrosine-protein kinase PKDCC {ECO:0000305} | |
| Gene Name | PKDCC {ECO:0000312|HGNC:HGNC:25123} | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 493 | |
| Subcellular Localization | Secreted . Golgi apparatus . | |
| Protein Description | Secreted tyrosine-protein kinase that mediates phosphorylation of extracellular proteins and endogenous proteins in the secretory pathway, which is essential for patterning at organogenesis stages. Mediates phosphorylation of MMP1, MMP13, MMP14, MMP19 and ERP29. [PubMed: 25171405 Probably plays a role in platelets: rapidly and quantitatively secreted from platelets in response to stimulation of platelet degranulation] | |
| Protein Sequence | MRRRRAAVAAGFCASFLLGSVLNVLFAPGSEPPRPGQSPEPSPAPGPGRRGGRGELARQIRARYEEVQRYSRGGPGPGAGRPERRRLMDLAPGGPGLPRPRPPWARPLSDGAPGWPPAPGPGSPGPGPRLGCAALRNVSGAQYMGSGYTKAVYRVRLPGGAAVALKAVDFSGHDLGSCVREFGVRRGCYRLAAHKLLKEMVLLERLRHPNVLQLYGYCYQDSEDIPDTLTTITELGAPVEMIQLLQTSWEDRFRICLSLGRLLHHLAHSPLGSVTLLDFRPRQFVLVDGELKVTDLDDARVEETPCAGSTDCILEFPARNFTLPCSAQGWCEGMNEKRNLYNAYRFFFTYLLPHSAPPSLRPLLDSIVNATGELAWGVDETLAQLEKVLHLYRSGQYLQNSTASSSTEYQCIPDSTIPQEDYRCWPSYHHGSCLLSVFNLAEAVDVCESHAQCRAFVVTNQTTWTGRQLVFFKTGWSQVVPDPNKTTYVKASG | |
| 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 |
|---|---|---|---|---|---|
| 64 | Phosphorylation | ARQIRARYEEVQRYS HHHHHHHHHHHHHHH | 18.56 | 24719451 | |
| 137 | N-linked_Glycosylation | LGCAALRNVSGAQYM CCCHHHCCCCCCCCC | 32.91 | UniProtKB CARBOHYD | |
| 148 | Phosphorylation | AQYMGSGYTKAVYRV CCCCCCCCCEEEEEE | 13.53 | - | |
| 177 | Phosphorylation | FSGHDLGSCVREFGV CCCCCHHHHHHHHCH | 19.41 | - | |
| 320 | N-linked_Glycosylation | ILEFPARNFTLPCSA EEEEECCCCCCCCCC | 36.04 | UniProtKB CARBOHYD | |
| 341 | Phosphorylation | MNEKRNLYNAYRFFF HHHHHCHHHHHHHHH | 10.99 | - | |
| 369 | N-linked_Glycosylation | PLLDSIVNATGELAW HHHHHHHHHHCHHCC | 30.07 | UniProtKB CARBOHYD | |
| 400 | N-linked_Glycosylation | RSGQYLQNSTASSST HCCCCCCCCCCCCCC | 38.44 | UniProtKB CARBOHYD | |
| 460 | N-linked_Glycosylation | CRAFVVTNQTTWTGR CEEEEEECCCCEEEC | 26.12 | UniProtKB CARBOHYD | |
| 474 | Phosphorylation | RQLVFFKTGWSQVVP CEEEEEECCCCCCCC | 38.43 | 18077418 | |
| 477 | Phosphorylation | VFFKTGWSQVVPDPN EEEECCCCCCCCCCC | 17.91 | 18077418 | |
| 484 | N-linked_Glycosylation | SQVVPDPNKTTYVKA CCCCCCCCCCCEEEE | 62.78 | UniProtKB CARBOHYD | |
| 487 | Phosphorylation | VPDPNKTTYVKASG- CCCCCCCCEEEECC- | 28.11 | 18077418 |
| 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 PKDCC_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of PKDCC_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 PKDCC_HUMAN !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
Oops, there are no PPI records of PKDCC_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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